data_7HD7
# 
_entry.id   7HD7 
# 
_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   7HD7         pdb_00007hd7 10.2210/pdb7hd7/pdb 
WWPDB D_1001407325 ?            ?                   
# 
_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                        7HD7 
_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 '[(6S)-5-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-5-azaspiro[2.4]heptan-6-yl]methanol' 244.292   2   ? ? ? ? 
4 water       nat water                                                                           18.015    425 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                          TFA   
3 '[(6S)-5-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-5-azaspiro[2.4]heptan-6-yl]methanol' A1A66 
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 
A1A66 non-polymer         . '[(6S)-5-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-5-azaspiro[2.4]heptan-6-yl]methanol' ? 'C13 H16 N4 O'   
244.292 
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 A1A66 1   202 201  A1A66 LA1 A . 
E 3 A1A66 1   203 301  A1A66 LA2 A . 
F 4 HOH   1   301 292  HOH   HOH A . 
F 4 HOH   2   302 1301 HOH   HOH A . 
F 4 HOH   3   303 625  HOH   HOH A . 
F 4 HOH   4   304 409  HOH   HOH A . 
F 4 HOH   5   305 15   HOH   HOH A . 
F 4 HOH   6   306 1283 HOH   HOH A . 
F 4 HOH   7   307 109  HOH   HOH A . 
F 4 HOH   8   308 153  HOH   HOH A . 
F 4 HOH   9   309 192  HOH   HOH A . 
F 4 HOH   10  310 196  HOH   HOH A . 
F 4 HOH   11  311 661  HOH   HOH A . 
F 4 HOH   12  312 132  HOH   HOH A . 
F 4 HOH   13  313 57   HOH   HOH A . 
F 4 HOH   14  314 136  HOH   HOH A . 
F 4 HOH   15  315 229  HOH   HOH A . 
F 4 HOH   16  316 209  HOH   HOH A . 
F 4 HOH   17  317 662  HOH   HOH A . 
F 4 HOH   18  318 461  HOH   HOH A . 
F 4 HOH   19  319 76   HOH   HOH A . 
F 4 HOH   20  320 1295 HOH   HOH A . 
F 4 HOH   21  321 247  HOH   HOH A . 
F 4 HOH   22  322 39   HOH   HOH A . 
F 4 HOH   23  323 4    HOH   HOH A . 
F 4 HOH   24  324 86   HOH   HOH A . 
F 4 HOH   25  325 124  HOH   HOH A . 
F 4 HOH   26  326 1309 HOH   HOH A . 
F 4 HOH   27  327 1300 HOH   HOH A . 
F 4 HOH   28  328 26   HOH   HOH A . 
F 4 HOH   29  329 236  HOH   HOH A . 
F 4 HOH   30  330 281  HOH   HOH A . 
F 4 HOH   31  331 493  HOH   HOH A . 
F 4 HOH   32  332 165  HOH   HOH A . 
F 4 HOH   33  333 140  HOH   HOH A . 
F 4 HOH   34  334 469  HOH   HOH A . 
F 4 HOH   35  335 105  HOH   HOH A . 
F 4 HOH   36  336 320  HOH   HOH A . 
F 4 HOH   37  337 15   HOH   HOH A . 
F 4 HOH   38  338 630  HOH   HOH A . 
F 4 HOH   39  339 164  HOH   HOH A . 
F 4 HOH   40  340 964  HOH   HOH A . 
F 4 HOH   41  341 151  HOH   HOH A . 
F 4 HOH   42  342 241  HOH   HOH A . 
F 4 HOH   43  343 169  HOH   HOH A . 
F 4 HOH   44  344 33   HOH   HOH A . 
F 4 HOH   45  345 337  HOH   HOH A . 
F 4 HOH   46  346 42   HOH   HOH A . 
F 4 HOH   47  347 225  HOH   HOH A . 
F 4 HOH   48  348 56   HOH   HOH A . 
F 4 HOH   49  349 6    HOH   HOH A . 
F 4 HOH   50  350 8    HOH   HOH A . 
F 4 HOH   51  351 354  HOH   HOH A . 
F 4 HOH   52  352 155  HOH   HOH A . 
F 4 HOH   53  353 93   HOH   HOH A . 
F 4 HOH   54  354 396  HOH   HOH A . 
F 4 HOH   55  355 218  HOH   HOH A . 
F 4 HOH   56  356 393  HOH   HOH A . 
F 4 HOH   57  357 92   HOH   HOH A . 
F 4 HOH   58  358 381  HOH   HOH A . 
F 4 HOH   59  359 17   HOH   HOH A . 
F 4 HOH   60  360 49   HOH   HOH A . 
F 4 HOH   61  361 66   HOH   HOH A . 
F 4 HOH   62  362 5    HOH   HOH A . 
F 4 HOH   63  363 102  HOH   HOH A . 
F 4 HOH   64  364 2    HOH   HOH A . 
F 4 HOH   65  365 1296 HOH   HOH A . 
F 4 HOH   66  366 8    HOH   HOH A . 
F 4 HOH   67  367 19   HOH   HOH A . 
F 4 HOH   68  368 139  HOH   HOH A . 
F 4 HOH   69  369 21   HOH   HOH A . 
F 4 HOH   70  370 138  HOH   HOH A . 
F 4 HOH   71  371 2    HOH   HOH A . 
F 4 HOH   72  372 36   HOH   HOH A . 
F 4 HOH   73  373 18   HOH   HOH A . 
F 4 HOH   74  374 45   HOH   HOH A . 
F 4 HOH   75  375 162  HOH   HOH A . 
F 4 HOH   76  376 1275 HOH   HOH A . 
F 4 HOH   77  377 939  HOH   HOH A . 
F 4 HOH   78  378 46   HOH   HOH A . 
F 4 HOH   79  379 186  HOH   HOH A . 
F 4 HOH   80  380 140  HOH   HOH A . 
F 4 HOH   81  381 4    HOH   HOH A . 
F 4 HOH   82  382 27   HOH   HOH A . 
F 4 HOH   83  383 1308 HOH   HOH A . 
F 4 HOH   84  384 159  HOH   HOH A . 
F 4 HOH   85  385 366  HOH   HOH A . 
F 4 HOH   86  386 154  HOH   HOH A . 
F 4 HOH   87  387 6    HOH   HOH A . 
F 4 HOH   88  388 134  HOH   HOH A . 
F 4 HOH   89  389 35   HOH   HOH A . 
F 4 HOH   90  390 83   HOH   HOH A . 
F 4 HOH   91  391 12   HOH   HOH A . 
F 4 HOH   92  392 148  HOH   HOH A . 
F 4 HOH   93  393 12   HOH   HOH A . 
F 4 HOH   94  394 67   HOH   HOH A . 
F 4 HOH   95  395 199  HOH   HOH A . 
F 4 HOH   96  396 34   HOH   HOH A . 
F 4 HOH   97  397 1310 HOH   HOH A . 
F 4 HOH   98  398 74   HOH   HOH A . 
F 4 HOH   99  399 70   HOH   HOH A . 
F 4 HOH   100 400 78   HOH   HOH A . 
F 4 HOH   101 401 116  HOH   HOH A . 
F 4 HOH   102 402 85   HOH   HOH A . 
F 4 HOH   103 403 278  HOH   HOH A . 
F 4 HOH   104 404 58   HOH   HOH A . 
F 4 HOH   105 405 303  HOH   HOH A . 
F 4 HOH   106 406 68   HOH   HOH A . 
F 4 HOH   107 407 195  HOH   HOH A . 
F 4 HOH   108 408 1068 HOH   HOH A . 
F 4 HOH   109 409 121  HOH   HOH A . 
F 4 HOH   110 410 1313 HOH   HOH A . 
F 4 HOH   111 411 212  HOH   HOH A . 
F 4 HOH   112 412 1315 HOH   HOH A . 
F 4 HOH   113 413 351  HOH   HOH A . 
F 4 HOH   114 414 115  HOH   HOH A . 
F 4 HOH   115 415 122  HOH   HOH A . 
F 4 HOH   116 416 53   HOH   HOH A . 
F 4 HOH   117 417 7    HOH   HOH A . 
F 4 HOH   118 418 3    HOH   HOH A . 
F 4 HOH   119 419 1290 HOH   HOH A . 
F 4 HOH   120 420 582  HOH   HOH A . 
F 4 HOH   121 421 123  HOH   HOH A . 
F 4 HOH   122 422 296  HOH   HOH A . 
F 4 HOH   123 423 96   HOH   HOH A . 
F 4 HOH   124 424 125  HOH   HOH A . 
F 4 HOH   125 425 25   HOH   HOH A . 
F 4 HOH   126 426 24   HOH   HOH A . 
F 4 HOH   127 427 51   HOH   HOH A . 
F 4 HOH   128 428 95   HOH   HOH A . 
F 4 HOH   129 429 156  HOH   HOH A . 
F 4 HOH   130 430 1289 HOH   HOH A . 
F 4 HOH   131 431 397  HOH   HOH A . 
F 4 HOH   132 432 333  HOH   HOH A . 
F 4 HOH   133 433 1279 HOH   HOH A . 
F 4 HOH   134 434 405  HOH   HOH A . 
F 4 HOH   135 435 80   HOH   HOH A . 
F 4 HOH   136 436 16   HOH   HOH A . 
F 4 HOH   137 437 73   HOH   HOH A . 
F 4 HOH   138 438 1238 HOH   HOH A . 
F 4 HOH   139 439 1222 HOH   HOH A . 
F 4 HOH   140 440 1134 HOH   HOH A . 
F 4 HOH   141 441 11   HOH   HOH A . 
F 4 HOH   142 442 71   HOH   HOH A . 
F 4 HOH   143 443 94   HOH   HOH A . 
F 4 HOH   144 444 14   HOH   HOH A . 
F 4 HOH   145 445 952  HOH   HOH A . 
F 4 HOH   146 446 576  HOH   HOH A . 
F 4 HOH   147 447 944  HOH   HOH A . 
F 4 HOH   148 448 97   HOH   HOH A . 
F 4 HOH   149 449 1189 HOH   HOH A . 
F 4 HOH   150 450 104  HOH   HOH A . 
F 4 HOH   151 451 1286 HOH   HOH A . 
F 4 HOH   152 452 40   HOH   HOH A . 
F 4 HOH   153 453 1094 HOH   HOH A . 
F 4 HOH   154 454 79   HOH   HOH A . 
F 4 HOH   155 455 188  HOH   HOH A . 
F 4 HOH   156 456 330  HOH   HOH A . 
F 4 HOH   157 457 1    HOH   HOH A . 
F 4 HOH   158 458 107  HOH   HOH A . 
F 4 HOH   159 459 163  HOH   HOH A . 
F 4 HOH   160 460 726  HOH   HOH A . 
F 4 HOH   161 461 509  HOH   HOH A . 
F 4 HOH   162 462 1119 HOH   HOH A . 
F 4 HOH   163 463 3    HOH   HOH A . 
F 4 HOH   164 464 280  HOH   HOH A . 
F 4 HOH   165 465 756  HOH   HOH A . 
F 4 HOH   166 466 408  HOH   HOH A . 
F 4 HOH   167 467 1276 HOH   HOH A . 
F 4 HOH   168 468 319  HOH   HOH A . 
F 4 HOH   169 469 801  HOH   HOH A . 
F 4 HOH   170 470 63   HOH   HOH A . 
F 4 HOH   171 471 556  HOH   HOH A . 
F 4 HOH   172 472 126  HOH   HOH A . 
F 4 HOH   173 473 361  HOH   HOH A . 
F 4 HOH   174 474 1307 HOH   HOH A . 
F 4 HOH   175 475 370  HOH   HOH A . 
F 4 HOH   176 476 342  HOH   HOH A . 
F 4 HOH   177 477 250  HOH   HOH A . 
F 4 HOH   178 478 1306 HOH   HOH A . 
F 4 HOH   179 479 521  HOH   HOH A . 
F 4 HOH   180 480 7    HOH   HOH A . 
F 4 HOH   181 481 267  HOH   HOH A . 
F 4 HOH   182 482 224  HOH   HOH A . 
F 4 HOH   183 483 695  HOH   HOH A . 
F 4 HOH   184 484 1287 HOH   HOH A . 
F 4 HOH   185 485 202  HOH   HOH A . 
F 4 HOH   186 486 674  HOH   HOH A . 
F 4 HOH   187 487 318  HOH   HOH A . 
F 4 HOH   188 488 919  HOH   HOH A . 
F 4 HOH   189 489 309  HOH   HOH A . 
F 4 HOH   190 490 331  HOH   HOH A . 
F 4 HOH   191 491 135  HOH   HOH A . 
F 4 HOH   192 492 1314 HOH   HOH A . 
F 4 HOH   193 493 315  HOH   HOH A . 
F 4 HOH   194 494 1299 HOH   HOH A . 
F 4 HOH   195 495 805  HOH   HOH A . 
F 4 HOH   196 496 941  HOH   HOH A . 
F 4 HOH   197 497 208  HOH   HOH A . 
F 4 HOH   198 498 263  HOH   HOH A . 
F 4 HOH   199 499 711  HOH   HOH A . 
F 4 HOH   200 500 356  HOH   HOH A . 
F 4 HOH   201 501 152  HOH   HOH A . 
F 4 HOH   202 502 981  HOH   HOH A . 
F 4 HOH   203 503 350  HOH   HOH A . 
F 4 HOH   204 504 5    HOH   HOH A . 
F 4 HOH   205 505 326  HOH   HOH A . 
F 4 HOH   206 506 1071 HOH   HOH A . 
F 4 HOH   207 507 180  HOH   HOH A . 
F 4 HOH   208 508 363  HOH   HOH A . 
F 4 HOH   209 509 313  HOH   HOH A . 
F 4 HOH   210 510 371  HOH   HOH A . 
F 4 HOH   211 511 16   HOH   HOH A . 
F 4 HOH   212 512 1284 HOH   HOH A . 
F 4 HOH   213 513 13   HOH   HOH A . 
F 4 HOH   214 514 9    HOH   HOH A . 
F 4 HOH   215 515 429  HOH   HOH A . 
F 4 HOH   216 516 185  HOH   HOH A . 
F 4 HOH   217 517 70   HOH   HOH A . 
F 4 HOH   218 518 772  HOH   HOH A . 
F 4 HOH   219 519 376  HOH   HOH A . 
F 4 HOH   220 520 1074 HOH   HOH A . 
F 4 HOH   221 521 346  HOH   HOH A . 
F 4 HOH   222 522 1292 HOH   HOH A . 
F 4 HOH   223 523 10   HOH   HOH A . 
F 4 HOH   224 524 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 549  HOH   HOH B . 
G 4 HOH   3   203 240  HOH   HOH B . 
G 4 HOH   4   204 531  HOH   HOH B . 
G 4 HOH   5   205 900  HOH   HOH B . 
G 4 HOH   6   206 364  HOH   HOH B . 
G 4 HOH   7   207 232  HOH   HOH B . 
G 4 HOH   8   208 1249 HOH   HOH B . 
G 4 HOH   9   209 120  HOH   HOH B . 
G 4 HOH   10  210 452  HOH   HOH B . 
G 4 HOH   11  211 398  HOH   HOH B . 
G 4 HOH   12  212 50   HOH   HOH B . 
G 4 HOH   13  213 332  HOH   HOH B . 
G 4 HOH   14  214 654  HOH   HOH B . 
G 4 HOH   15  215 205  HOH   HOH B . 
G 4 HOH   16  216 758  HOH   HOH B . 
G 4 HOH   17  217 444  HOH   HOH B . 
G 4 HOH   18  218 353  HOH   HOH B . 
G 4 HOH   19  219 264  HOH   HOH B . 
G 4 HOH   20  220 166  HOH   HOH B . 
G 4 HOH   21  221 1278 HOH   HOH B . 
G 4 HOH   22  222 743  HOH   HOH B . 
G 4 HOH   23  223 358  HOH   HOH B . 
G 4 HOH   24  224 172  HOH   HOH B . 
G 4 HOH   25  225 75   HOH   HOH B . 
G 4 HOH   26  226 54   HOH   HOH B . 
G 4 HOH   27  227 82   HOH   HOH B . 
G 4 HOH   28  228 276  HOH   HOH B . 
G 4 HOH   29  229 60   HOH   HOH B . 
G 4 HOH   30  230 110  HOH   HOH B . 
G 4 HOH   31  231 131  HOH   HOH B . 
G 4 HOH   32  232 41   HOH   HOH B . 
G 4 HOH   33  233 127  HOH   HOH B . 
G 4 HOH   34  234 181  HOH   HOH B . 
G 4 HOH   35  235 128  HOH   HOH B . 
G 4 HOH   36  236 282  HOH   HOH B . 
G 4 HOH   37  237 272  HOH   HOH B . 
G 4 HOH   38  238 325  HOH   HOH B . 
G 4 HOH   39  239 252  HOH   HOH B . 
G 4 HOH   40  240 1312 HOH   HOH B . 
G 4 HOH   41  241 133  HOH   HOH B . 
G 4 HOH   42  242 343  HOH   HOH B . 
G 4 HOH   43  243 14   HOH   HOH B . 
G 4 HOH   44  244 129  HOH   HOH B . 
G 4 HOH   45  245 391  HOH   HOH B . 
G 4 HOH   46  246 103  HOH   HOH B . 
G 4 HOH   47  247 1    HOH   HOH B . 
G 4 HOH   48  248 30   HOH   HOH B . 
G 4 HOH   49  249 1140 HOH   HOH B . 
G 4 HOH   50  250 52   HOH   HOH B . 
G 4 HOH   51  251 69   HOH   HOH B . 
G 4 HOH   52  252 72   HOH   HOH B . 
G 4 HOH   53  253 47   HOH   HOH B . 
G 4 HOH   54  254 300  HOH   HOH B . 
G 4 HOH   55  255 723  HOH   HOH B . 
G 4 HOH   56  256 81   HOH   HOH B . 
G 4 HOH   57  257 9    HOH   HOH B . 
G 4 HOH   58  258 62   HOH   HOH B . 
G 4 HOH   59  259 231  HOH   HOH B . 
G 4 HOH   60  260 31   HOH   HOH B . 
G 4 HOH   61  261 302  HOH   HOH B . 
G 4 HOH   62  262 144  HOH   HOH B . 
G 4 HOH   63  263 242  HOH   HOH B . 
G 4 HOH   64  264 114  HOH   HOH B . 
G 4 HOH   65  265 150  HOH   HOH B . 
G 4 HOH   66  266 271  HOH   HOH B . 
G 4 HOH   67  267 20   HOH   HOH B . 
G 4 HOH   68  268 10   HOH   HOH B . 
G 4 HOH   69  269 59   HOH   HOH B . 
G 4 HOH   70  270 61   HOH   HOH B . 
G 4 HOH   71  271 84   HOH   HOH B . 
G 4 HOH   72  272 287  HOH   HOH B . 
G 4 HOH   73  273 117  HOH   HOH B . 
G 4 HOH   74  274 143  HOH   HOH B . 
G 4 HOH   75  275 221  HOH   HOH B . 
G 4 HOH   76  276 347  HOH   HOH B . 
G 4 HOH   77  277 77   HOH   HOH B . 
G 4 HOH   78  278 243  HOH   HOH B . 
G 4 HOH   79  279 147  HOH   HOH B . 
G 4 HOH   80  280 1106 HOH   HOH B . 
G 4 HOH   81  281 175  HOH   HOH B . 
G 4 HOH   82  282 11   HOH   HOH B . 
G 4 HOH   83  283 22   HOH   HOH B . 
G 4 HOH   84  284 1277 HOH   HOH B . 
G 4 HOH   85  285 220  HOH   HOH B . 
G 4 HOH   86  286 43   HOH   HOH B . 
G 4 HOH   87  287 88   HOH   HOH B . 
G 4 HOH   88  288 235  HOH   HOH B . 
G 4 HOH   89  289 13   HOH   HOH B . 
G 4 HOH   90  290 1285 HOH   HOH B . 
G 4 HOH   91  291 207  HOH   HOH B . 
G 4 HOH   92  292 1305 HOH   HOH B . 
G 4 HOH   93  293 89   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 1066 HOH   HOH B . 
G 4 HOH   97  297 311  HOH   HOH B . 
G 4 HOH   98  298 137  HOH   HOH B . 
G 4 HOH   99  299 112  HOH   HOH B . 
G 4 HOH   100 300 416  HOH   HOH B . 
G 4 HOH   101 301 160  HOH   HOH B . 
G 4 HOH   102 302 99   HOH   HOH B . 
G 4 HOH   103 303 316  HOH   HOH B . 
G 4 HOH   104 304 215  HOH   HOH B . 
G 4 HOH   105 305 38   HOH   HOH B . 
G 4 HOH   106 306 297  HOH   HOH B . 
G 4 HOH   107 307 197  HOH   HOH B . 
G 4 HOH   108 308 142  HOH   HOH B . 
G 4 HOH   109 309 170  HOH   HOH B . 
G 4 HOH   110 310 32   HOH   HOH B . 
G 4 HOH   111 311 101  HOH   HOH B . 
G 4 HOH   112 312 37   HOH   HOH B . 
G 4 HOH   113 313 299  HOH   HOH B . 
G 4 HOH   114 314 23   HOH   HOH B . 
G 4 HOH   115 315 182  HOH   HOH B . 
G 4 HOH   116 316 48   HOH   HOH B . 
G 4 HOH   117 317 387  HOH   HOH B . 
G 4 HOH   118 318 118  HOH   HOH B . 
G 4 HOH   119 319 44   HOH   HOH B . 
G 4 HOH   120 320 91   HOH   HOH B . 
G 4 HOH   121 321 177  HOH   HOH B . 
G 4 HOH   122 322 1291 HOH   HOH B . 
G 4 HOH   123 323 445  HOH   HOH B . 
G 4 HOH   124 324 141  HOH   HOH B . 
G 4 HOH   125 325 28   HOH   HOH B . 
G 4 HOH   126 326 717  HOH   HOH B . 
G 4 HOH   127 327 704  HOH   HOH B . 
G 4 HOH   128 328 100  HOH   HOH B . 
G 4 HOH   129 329 1274 HOH   HOH B . 
G 4 HOH   130 330 29   HOH   HOH B . 
G 4 HOH   131 331 635  HOH   HOH B . 
G 4 HOH   132 332 55   HOH   HOH B . 
G 4 HOH   133 333 98   HOH   HOH B . 
G 4 HOH   134 334 1294 HOH   HOH B . 
G 4 HOH   135 335 161  HOH   HOH B . 
G 4 HOH   136 336 334  HOH   HOH B . 
G 4 HOH   137 337 339  HOH   HOH B . 
G 4 HOH   138 338 65   HOH   HOH B . 
G 4 HOH   139 339 1126 HOH   HOH B . 
G 4 HOH   140 340 234  HOH   HOH B . 
G 4 HOH   141 341 1293 HOH   HOH B . 
G 4 HOH   142 342 362  HOH   HOH B . 
G 4 HOH   143 343 341  HOH   HOH B . 
G 4 HOH   144 344 619  HOH   HOH B . 
G 4 HOH   145 345 178  HOH   HOH B . 
G 4 HOH   146 346 87   HOH   HOH B . 
G 4 HOH   147 347 90   HOH   HOH B . 
G 4 HOH   148 348 1304 HOH   HOH B . 
G 4 HOH   149 349 960  HOH   HOH B . 
G 4 HOH   150 350 191  HOH   HOH B . 
G 4 HOH   151 351 1046 HOH   HOH B . 
G 4 HOH   152 352 463  HOH   HOH B . 
G 4 HOH   153 353 203  HOH   HOH B . 
G 4 HOH   154 354 623  HOH   HOH B . 
G 4 HOH   155 355 1280 HOH   HOH B . 
G 4 HOH   156 356 335  HOH   HOH B . 
G 4 HOH   157 357 304  HOH   HOH B . 
G 4 HOH   158 358 1077 HOH   HOH B . 
G 4 HOH   159 359 290  HOH   HOH B . 
G 4 HOH   160 360 541  HOH   HOH B . 
G 4 HOH   161 361 389  HOH   HOH B . 
G 4 HOH   162 362 718  HOH   HOH B . 
G 4 HOH   163 363 1072 HOH   HOH B . 
G 4 HOH   164 364 283  HOH   HOH B . 
G 4 HOH   165 365 479  HOH   HOH B . 
G 4 HOH   166 366 291  HOH   HOH B . 
G 4 HOH   167 367 898  HOH   HOH B . 
G 4 HOH   168 368 615  HOH   HOH B . 
G 4 HOH   169 369 340  HOH   HOH B . 
G 4 HOH   170 370 1316 HOH   HOH B . 
G 4 HOH   171 371 667  HOH   HOH B . 
G 4 HOH   172 372 373  HOH   HOH B . 
G 4 HOH   173 373 190  HOH   HOH B . 
G 4 HOH   174 374 1303 HOH   HOH B . 
G 4 HOH   175 375 1173 HOH   HOH B . 
G 4 HOH   176 376 310  HOH   HOH B . 
G 4 HOH   177 377 431  HOH   HOH B . 
G 4 HOH   178 378 183  HOH   HOH B . 
G 4 HOH   179 379 418  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 1163 HOH   HOH B . 
G 4 HOH   183 383 1311 HOH   HOH B . 
G 4 HOH   184 384 424  HOH   HOH B . 
G 4 HOH   185 385 491  HOH   HOH B . 
G 4 HOH   186 386 176  HOH   HOH B . 
G 4 HOH   187 387 265  HOH   HOH B . 
G 4 HOH   188 388 248  HOH   HOH B . 
G 4 HOH   189 389 470  HOH   HOH B . 
G 4 HOH   190 390 1298 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   195 395 274  HOH   HOH B . 
G 4 HOH   196 396 314  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           7HD7 
_cell.length_a           88.805 
_cell.length_b           88.805 
_cell.length_c           39.451 
_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                         7HD7 
_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          7HD7 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.61 
_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                     7HD7 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156240 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.046 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.300 
_reflns.B_iso_Wilson_estimate        11.760 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.051 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1009425 
_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 1.020 1.040  ? 42663 7636 ? 0.873 ? ? ? 5.600 ? 1.300  ? ? ? ? ? ? 98.500 0.964 0.400 0.819 
1 2 5.590 44.400 ? 7114  1038 ? 0.030 ? ? ? 6.900 ? 50.200 ? ? ? ? ? ? 99.900 0.032 0.012 0.999 
# 
_refine.entry_id                                 7HD7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.8400 
_refine.ls_number_reflns_obs                     156179 
_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                          0.1436 
_refine.ls_R_factor_R_work                       0.1430 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1567 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7538 
_refine.ls_number_reflns_R_work                  148641 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.2076 
_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                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                78.800 
_refine.B_iso_min                                7.800 
_refine.pdbx_overall_phase_error                 16.1000 
_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                       1.0200 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         75 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               3042 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           11.30 
_refine_hist.pdbx_B_iso_mean_solvent          30.34 
_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 
1.0200 1.0300  30 98.0000  4877 . 0.3587 0.3890 . 200 0.0000 5077 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4952 . 0.2947 0.2977 . 281 0.0000 5233 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4866 . 0.2510 0.2344 . 279 0.0000 5145 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4927 . 0.2189 0.2639 . 282 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4911 . 0.2016 0.2078 . 235 0.0000 5146 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4962 . 0.1784 0.2043 . 232 0.0000 5194 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4885 . 0.1620 0.1794 . 271 0.0000 5156 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4994 . 0.1559 0.1673 . 215 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4933 . 0.1455 0.1592 . 240 0.0000 5173 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4927 . 0.1336 0.1650 . 265 0.0000 5192 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4951 . 0.1310 0.1647 . 245 0.0000 5196 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4857 . 0.1249 0.1567 . 266 0.0000 5123 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5058 . 0.1211 0.1476 . 224 0.0000 5282 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4905 . 0.1256 0.1540 . 244 0.0000 5149 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4912 . 0.1278 0.1392 . 251 0.0000 5163 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4949 . 0.1287 0.1499 . 268 0.0000 5217 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4959 . 0.1324 0.1490 . 252 0.0000 5211 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4960 . 0.1305 0.1497 . 254 0.0000 5214 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4961 . 0.1292 0.1570 . 239 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4960 . 0.1257 0.1420 . 250 0.0000 5210 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4967 . 0.1174 0.1281 . 235 0.0000 5202 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4962 . 0.1208 0.1350 . 265 0.0000 5227 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4930 . 0.1223 0.1372 . 266 0.0000 5196 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5031 . 0.1317 0.1507 . 200 0.0000 5231 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4946 . 0.1338 0.1426 . 292 0.0000 5238 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4976 . 0.1365 0.1324 . 246 0.0000 5222 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4941 . 0.1392 0.1434 . 289 0.0000 5230 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5002 . 0.1374 0.1426 . 252 0.0000 5254 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5019 . 0.1507 0.1643 . 248 0.0000 5267 . 'X-RAY DIFFRACTION' 
3.1700 44.4000 30 100.0000 5161 . 0.1483 0.1705 . 252 0.0000 5413 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HD7 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003710' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD7 
_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 7HD7 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD7 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 7HD7 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD7 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD7 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD7 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HD7 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    204 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    307 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
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 -69.92 98.84   
2 1 HIS A 86  ? ? 55.78  -132.48 
3 1 SER A 128 ? B 74.09  -5.51   
4 1 HIS B 86  ? ? 57.80  -127.41 
# 
_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 521 ? 5.85 . 
2 1 O ? A HOH 522 ? 5.96 . 
3 1 O B A HOH 523 ? 6.20 . 
4 1 O ? A HOH 524 ? 7.59 . 
5 1 O ? B HOH 401 ? 6.52 . 
# 
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 
A1A66 O1   O N N 1   
A1A66 C1   C N N 2   
A1A66 C2   C N S 3   
A1A66 C3   C N N 4   
A1A66 C4   C N N 5   
A1A66 C5   C N N 6   
A1A66 C6   C N N 7   
A1A66 C7   C N N 8   
A1A66 C8   C Y N 9   
A1A66 C10  C Y N 10  
A1A66 C11  C Y N 11  
A1A66 C12  C Y N 12  
A1A66 C13  C Y N 13  
A1A66 C9   C Y N 14  
A1A66 N1   N N N 15  
A1A66 N2   N Y N 16  
A1A66 N3   N Y N 17  
A1A66 N4   N Y N 18  
A1A66 H2   H N N 19  
A1A66 H4   H N N 20  
A1A66 H3   H N N 21  
A1A66 H1   H N N 22  
A1A66 H6   H N N 23  
A1A66 H5   H N N 24  
A1A66 H8   H N N 25  
A1A66 H7   H N N 26  
A1A66 H10  H N N 27  
A1A66 H9   H N N 28  
A1A66 H12  H N N 29  
A1A66 H11  H N N 30  
A1A66 H14  H N N 31  
A1A66 H15  H N N 32  
A1A66 H13  H N N 33  
A1A66 H16  H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
GLN   N    N N N 122 
GLN   CA   C N S 123 
GLN   C    C N N 124 
GLN   O    O N N 125 
GLN   CB   C N N 126 
GLN   CG   C N N 127 
GLN   CD   C N N 128 
GLN   OE1  O N N 129 
GLN   NE2  N N N 130 
GLN   OXT  O N N 131 
GLN   H    H N N 132 
GLN   H2   H N N 133 
GLN   HA   H N N 134 
GLN   HB2  H N N 135 
GLN   HB3  H N N 136 
GLN   HG2  H N N 137 
GLN   HG3  H N N 138 
GLN   HE21 H N N 139 
GLN   HE22 H N N 140 
GLN   HXT  H N N 141 
GLU   N    N N N 142 
GLU   CA   C N S 143 
GLU   C    C N N 144 
GLU   O    O N N 145 
GLU   CB   C N N 146 
GLU   CG   C N N 147 
GLU   CD   C N N 148 
GLU   OE1  O N N 149 
GLU   OE2  O N N 150 
GLU   OXT  O N N 151 
GLU   H    H N N 152 
GLU   H2   H N N 153 
GLU   HA   H N N 154 
GLU   HB2  H N N 155 
GLU   HB3  H N N 156 
GLU   HG2  H N N 157 
GLU   HG3  H N N 158 
GLU   HE2  H N N 159 
GLU   HXT  H N N 160 
GLY   N    N N N 161 
GLY   CA   C N N 162 
GLY   C    C N N 163 
GLY   O    O N N 164 
GLY   OXT  O N N 165 
GLY   H    H N N 166 
GLY   H2   H N N 167 
GLY   HA2  H N N 168 
GLY   HA3  H N N 169 
GLY   HXT  H N N 170 
HIS   N    N N N 171 
HIS   CA   C N S 172 
HIS   C    C N N 173 
HIS   O    O N N 174 
HIS   CB   C N N 175 
HIS   CG   C Y N 176 
HIS   ND1  N Y N 177 
HIS   CD2  C Y N 178 
HIS   CE1  C Y N 179 
HIS   NE2  N Y N 180 
HIS   OXT  O N N 181 
HIS   H    H N N 182 
HIS   H2   H N N 183 
HIS   HA   H N N 184 
HIS   HB2  H N N 185 
HIS   HB3  H N N 186 
HIS   HD1  H N N 187 
HIS   HD2  H N N 188 
HIS   HE1  H N N 189 
HIS   HE2  H N N 190 
HIS   HXT  H N N 191 
HOH   O    O N N 192 
HOH   H1   H N N 193 
HOH   H2   H N N 194 
ILE   N    N N N 195 
ILE   CA   C N S 196 
ILE   C    C N N 197 
ILE   O    O N N 198 
ILE   CB   C N S 199 
ILE   CG1  C N N 200 
ILE   CG2  C N N 201 
ILE   CD1  C N N 202 
ILE   OXT  O N N 203 
ILE   H    H N N 204 
ILE   H2   H N N 205 
ILE   HA   H N N 206 
ILE   HB   H N N 207 
ILE   HG12 H N N 208 
ILE   HG13 H N N 209 
ILE   HG21 H N N 210 
ILE   HG22 H N N 211 
ILE   HG23 H N N 212 
ILE   HD11 H N N 213 
ILE   HD12 H N N 214 
ILE   HD13 H N N 215 
ILE   HXT  H N N 216 
LEU   N    N N N 217 
LEU   CA   C N S 218 
LEU   C    C N N 219 
LEU   O    O N N 220 
LEU   CB   C N N 221 
LEU   CG   C N N 222 
LEU   CD1  C N N 223 
LEU   CD2  C N N 224 
LEU   OXT  O N N 225 
LEU   H    H N N 226 
LEU   H2   H N N 227 
LEU   HA   H N N 228 
LEU   HB2  H N N 229 
LEU   HB3  H N N 230 
LEU   HG   H N N 231 
LEU   HD11 H N N 232 
LEU   HD12 H N N 233 
LEU   HD13 H N N 234 
LEU   HD21 H N N 235 
LEU   HD22 H N N 236 
LEU   HD23 H N N 237 
LEU   HXT  H N N 238 
LYS   N    N N N 239 
LYS   CA   C N S 240 
LYS   C    C N N 241 
LYS   O    O N N 242 
LYS   CB   C N N 243 
LYS   CG   C N N 244 
LYS   CD   C N N 245 
LYS   CE   C N N 246 
LYS   NZ   N N N 247 
LYS   OXT  O N N 248 
LYS   H    H N N 249 
LYS   H2   H N N 250 
LYS   HA   H N N 251 
LYS   HB2  H N N 252 
LYS   HB3  H N N 253 
LYS   HG2  H N N 254 
LYS   HG3  H N N 255 
LYS   HD2  H N N 256 
LYS   HD3  H N N 257 
LYS   HE2  H N N 258 
LYS   HE3  H N N 259 
LYS   HZ1  H N N 260 
LYS   HZ2  H N N 261 
LYS   HZ3  H N N 262 
LYS   HXT  H N N 263 
MET   N    N N N 264 
MET   CA   C N S 265 
MET   C    C N N 266 
MET   O    O N N 267 
MET   CB   C N N 268 
MET   CG   C N N 269 
MET   SD   S N N 270 
MET   CE   C N N 271 
MET   OXT  O N N 272 
MET   H    H N N 273 
MET   H2   H N N 274 
MET   HA   H N N 275 
MET   HB2  H N N 276 
MET   HB3  H N N 277 
MET   HG2  H N N 278 
MET   HG3  H N N 279 
MET   HE1  H N N 280 
MET   HE2  H N N 281 
MET   HE3  H N N 282 
MET   HXT  H N N 283 
PHE   N    N N N 284 
PHE   CA   C N S 285 
PHE   C    C N N 286 
PHE   O    O N N 287 
PHE   CB   C N N 288 
PHE   CG   C Y N 289 
PHE   CD1  C Y N 290 
PHE   CD2  C Y N 291 
PHE   CE1  C Y N 292 
PHE   CE2  C Y N 293 
PHE   CZ   C Y N 294 
PHE   OXT  O N N 295 
PHE   H    H N N 296 
PHE   H2   H N N 297 
PHE   HA   H N N 298 
PHE   HB2  H N N 299 
PHE   HB3  H N N 300 
PHE   HD1  H N N 301 
PHE   HD2  H N N 302 
PHE   HE1  H N N 303 
PHE   HE2  H N N 304 
PHE   HZ   H N N 305 
PHE   HXT  H N N 306 
PRO   N    N N N 307 
PRO   CA   C N S 308 
PRO   C    C N N 309 
PRO   O    O N N 310 
PRO   CB   C N N 311 
PRO   CG   C N N 312 
PRO   CD   C N N 313 
PRO   OXT  O N N 314 
PRO   H    H N N 315 
PRO   HA   H N N 316 
PRO   HB2  H N N 317 
PRO   HB3  H N N 318 
PRO   HG2  H N N 319 
PRO   HG3  H N N 320 
PRO   HD2  H N N 321 
PRO   HD3  H N N 322 
PRO   HXT  H N N 323 
SER   N    N N N 324 
SER   CA   C N S 325 
SER   C    C N N 326 
SER   O    O N N 327 
SER   CB   C N N 328 
SER   OG   O N N 329 
SER   OXT  O N N 330 
SER   H    H N N 331 
SER   H2   H N N 332 
SER   HA   H N N 333 
SER   HB2  H N N 334 
SER   HB3  H N N 335 
SER   HG   H N N 336 
SER   HXT  H N N 337 
TFA   C1   C N N 338 
TFA   C2   C N N 339 
TFA   O    O N N 340 
TFA   F1   F N N 341 
TFA   F2   F N N 342 
TFA   F3   F N N 343 
TFA   OXT  O N N 344 
TFA   HXT  H N N 345 
THR   N    N N N 346 
THR   CA   C N S 347 
THR   C    C N N 348 
THR   O    O N N 349 
THR   CB   C N R 350 
THR   OG1  O N N 351 
THR   CG2  C N N 352 
THR   OXT  O N N 353 
THR   H    H N N 354 
THR   H2   H N N 355 
THR   HA   H N N 356 
THR   HB   H N N 357 
THR   HG1  H N N 358 
THR   HG21 H N N 359 
THR   HG22 H N N 360 
THR   HG23 H N N 361 
THR   HXT  H N N 362 
TYR   N    N N N 363 
TYR   CA   C N S 364 
TYR   C    C N N 365 
TYR   O    O N N 366 
TYR   CB   C N N 367 
TYR   CG   C Y N 368 
TYR   CD1  C Y N 369 
TYR   CD2  C Y N 370 
TYR   CE1  C Y N 371 
TYR   CE2  C Y N 372 
TYR   CZ   C Y N 373 
TYR   OH   O N N 374 
TYR   OXT  O N N 375 
TYR   H    H N N 376 
TYR   H2   H N N 377 
TYR   HA   H N N 378 
TYR   HB2  H N N 379 
TYR   HB3  H N N 380 
TYR   HD1  H N N 381 
TYR   HD2  H N N 382 
TYR   HE1  H N N 383 
TYR   HE2  H N N 384 
TYR   HH   H N N 385 
TYR   HXT  H N N 386 
VAL   N    N N N 387 
VAL   CA   C N S 388 
VAL   C    C N N 389 
VAL   O    O N N 390 
VAL   CB   C N N 391 
VAL   CG1  C N N 392 
VAL   CG2  C N N 393 
VAL   OXT  O N N 394 
VAL   H    H N N 395 
VAL   H2   H N N 396 
VAL   HA   H N N 397 
VAL   HB   H N N 398 
VAL   HG11 H N N 399 
VAL   HG12 H N N 400 
VAL   HG13 H N N 401 
VAL   HG21 H N N 402 
VAL   HG22 H N N 403 
VAL   HG23 H N N 404 
VAL   HXT  H N N 405 
# 
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 
A1A66 C5  C4   sing N N 1   
A1A66 C5  C6   sing N N 2   
A1A66 C3  C4   sing N N 3   
A1A66 C3  C2   sing N N 4   
A1A66 O1  C1   sing N N 5   
A1A66 C4  C6   sing N N 6   
A1A66 C4  C7   sing N N 7   
A1A66 C1  C2   sing N N 8   
A1A66 C7  N1   sing N N 9   
A1A66 C2  N1   sing N N 10  
A1A66 N1  C8   sing N N 11  
A1A66 C8  N2   doub Y N 12  
A1A66 C8  C11  sing Y N 13  
A1A66 C12 C11  sing Y N 14  
A1A66 C12 C13  doub Y N 15  
A1A66 N2  C9   sing Y N 16  
A1A66 C11 C10  doub Y N 17  
A1A66 C13 N4   sing Y N 18  
A1A66 C9  N3   doub Y N 19  
A1A66 C10 N4   sing Y N 20  
A1A66 C10 N3   sing Y N 21  
A1A66 O1  H2   sing N N 22  
A1A66 C1  H4   sing N N 23  
A1A66 C1  H3   sing N N 24  
A1A66 C2  H1   sing N N 25  
A1A66 C3  H6   sing N N 26  
A1A66 C3  H5   sing N N 27  
A1A66 C5  H8   sing N N 28  
A1A66 C5  H7   sing N N 29  
A1A66 C6  H10  sing N N 30  
A1A66 C6  H9   sing N N 31  
A1A66 C7  H12  sing N N 32  
A1A66 C7  H11  sing N N 33  
A1A66 C12 H14  sing N N 34  
A1A66 C13 H15  sing N N 35  
A1A66 C9  H13  sing N N 36  
A1A66 N4  H16  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
TFA   C1  C2   sing N N 327 
TFA   C1  O    doub N N 328 
TFA   C1  OXT  sing N N 329 
TFA   C2  F1   sing N N 330 
TFA   C2  F2   sing N N 331 
TFA   C2  F3   sing N N 332 
TFA   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TYR   N   CA   sing N N 350 
TYR   N   H    sing N N 351 
TYR   N   H2   sing N N 352 
TYR   CA  C    sing N N 353 
TYR   CA  CB   sing N N 354 
TYR   CA  HA   sing N N 355 
TYR   C   O    doub N N 356 
TYR   C   OXT  sing N N 357 
TYR   CB  CG   sing N N 358 
TYR   CB  HB2  sing N N 359 
TYR   CB  HB3  sing N N 360 
TYR   CG  CD1  doub Y N 361 
TYR   CG  CD2  sing Y N 362 
TYR   CD1 CE1  sing Y N 363 
TYR   CD1 HD1  sing N N 364 
TYR   CD2 CE2  doub Y N 365 
TYR   CD2 HD2  sing N N 366 
TYR   CE1 CZ   doub Y N 367 
TYR   CE1 HE1  sing N N 368 
TYR   CE2 CZ   sing Y N 369 
TYR   CE2 HE2  sing N N 370 
TYR   CZ  OH   sing N N 371 
TYR   OH  HH   sing N N 372 
TYR   OXT HXT  sing N N 373 
VAL   N   CA   sing N N 374 
VAL   N   H    sing N N 375 
VAL   N   H2   sing N N 376 
VAL   CA  C    sing N N 377 
VAL   CA  CB   sing N N 378 
VAL   CA  HA   sing N N 379 
VAL   C   O    doub N N 380 
VAL   C   OXT  sing N N 381 
VAL   CB  CG1  sing N N 382 
VAL   CB  CG2  sing N N 383 
VAL   CB  HB   sing N N 384 
VAL   CG1 HG11 sing N N 385 
VAL   CG1 HG12 sing N N 386 
VAL   CG1 HG13 sing N N 387 
VAL   CG2 HG21 sing N N 388 
VAL   CG2 HG22 sing N N 389 
VAL   CG2 HG23 sing N N 390 
VAL   OXT HXT  sing N N 391 
# 
_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                    7HD7 
_atom_sites.fract_transf_matrix[1][1]   0.011261 
_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]   0.011261 
_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]   0.025348 
_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   ? 19.672 -16.230 22.225  0.48 52.42 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.691 -15.938 22.361  0.52 52.42 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.696 -15.160 22.387  0.48 52.01 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.714 -14.871 22.539  0.52 51.95 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.344 -13.808 22.110  0.48 50.39 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.345 -13.524 22.208  0.52 50.29 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.444 -13.529 22.587  0.48 50.93 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.446 -13.217 22.666  0.52 50.87 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.053 -15.195 23.789  0.48 52.87 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.133 -14.876 23.966  0.52 52.74 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.025 -14.081 23.933  0.48 53.11 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.078 -13.790 24.114  0.52 52.97 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.413 -16.551 24.050  0.48 53.11 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.551 -16.242 24.300  0.52 52.97 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.987 -15.283 21.740  0.48 62.39 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.979 -15.013 21.926  0.52 62.31 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.741 -15.056 24.458  0.48 63.42 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.844 -14.692 24.600  0.52 63.27 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.512 -14.229 24.743  0.48 63.71 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.617 -13.912 24.958  0.52 63.54 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.485 -13.229 23.985  0.48 63.71 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.511 -12.922 24.098  0.52 63.54 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.436 -14.094 23.162  0.48 63.71 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.447 -13.861 23.380  0.52 63.54 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.957 -16.525 24.906  0.48 63.71 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.127 -16.200 25.172  0.52 63.54 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.778 -16.741 23.342  0.48 63.71 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.896 -16.478 23.625  0.52 63.54 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.105 -17.230 24.065  0.48 63.71 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.265 -16.897 24.311  0.52 63.54 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.660 -12.973 21.329  0.48 47.84 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.645 -12.721 21.408  0.52 47.60 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.103 -11.613 21.047  0.48 44.93 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.096 -11.382 21.049  0.52 44.54 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.947 -10.648 21.295  0.48 42.32 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.973 -10.383 21.315  0.52 41.88 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.840 -11.051 21.666  0.48 42.50 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.878 -10.747 21.757  0.52 42.04 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.676 -11.481 19.628  0.48 44.35 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.603 -11.316 19.601  0.52 43.87 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.692 -11.896 18.554  0.48 43.72 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.557 -11.734 18.591  0.52 43.15 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.542 -11.456 18.542  0.48 43.48 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.433 -11.232 18.597  0.52 42.86 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.141 -12.752 17.642  0.48 43.53 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.924 -12.662 17.713  0.52 42.94 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.918 -13.180 20.946  0.48 57.38 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.887 -12.938 21.060  0.52 57.10 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.814 -11.390 21.663  0.48 53.89 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.839 -11.150 21.621  0.52 53.42 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.920 -10.554 19.471  0.48 53.20 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.867 -10.402 19.401  0.52 52.62 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.460 -12.046 19.550  0.48 53.20 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.366 -11.907 19.506  0.52 52.62 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.625 -13.018 17.008  0.48 52.22 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.370 -12.933 17.115  0.52 51.50 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.952 -13.040 17.685  0.48 52.22 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.719 -12.991 17.743  0.52 51.50 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.209 -9.359  21.082  0.48 39.30 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.250 -9.110  21.037  0.52 38.82 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.282 -8.297  21.452  0.48 36.15 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.370 -8.014  21.420  0.52 35.65 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.430 -7.803  20.287  0.48 32.53 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.476 -7.530  20.283  0.52 31.79 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.777 -6.761  20.413  0.48 32.66 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.788 -6.516  20.443  0.52 31.88 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.042 -7.126  22.080  0.48 36.66 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.186 -6.846  21.979  0.52 36.34 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.044 -6.639  21.203  0.48 36.91 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 19.094 -6.350  21.012  0.52 36.67 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.930 -9.075  20.712  0.48 47.13 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.955 -8.857  20.615  0.52 46.56 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.683 -8.642  22.131  0.48 43.36 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.793 -8.324  22.134  0.52 42.75 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.415 -6.409  22.270  0.48 43.96 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.578 -6.134  22.238  0.52 43.58 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.460 -7.424  22.904  0.48 43.96 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.684 -7.152  22.753  0.52 43.58 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.452 -5.998  21.563  0.48 44.27 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.532 -5.709  21.334  0.52 43.98 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.418 -8.514  19.163  0.48 28.50 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.469 -8.216  19.143  0.52 27.56 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.530 -8.148  18.066  0.48 24.65 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.510 -7.889  18.097  0.52 23.57 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.091 -8.518  18.414  0.48 23.89 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.110 -8.268  18.560  0.52 23.51 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.823 -9.600  18.942  0.48 24.76 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.900 -9.344  19.124  0.52 24.44 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.959 -8.861  16.784  0.48 22.01 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.849 -8.637  16.810  0.52 20.52 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.241 -8.333  16.192  0.48 20.11 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.133 -8.187  16.167  0.52 18.40 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.245 -7.172  15.437  0.48 19.28 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.195 -6.985  15.482  0.52 17.58 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.437 -9.006  16.379  0.48 19.98 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.272 -8.970  16.237  0.52 18.36 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.420 -6.687  14.886  0.48 19.12 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.374 -6.569  14.887  0.52 17.34 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.614 -8.527  15.830  0.48 19.90 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.451 -8.562  15.641  0.52 18.24 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.605 -7.366  15.083  0.48 19.46 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.502 -7.359  14.967  0.52 17.72 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.912 -9.202  19.010  0.48 34.17 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 17.001 -8.865  18.953  0.52 33.05 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.576 -7.193  17.919  0.48 29.56 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.528 -6.939  17.923  0.52 28.26 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.089 -9.803  16.979  0.48 26.39 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.933 -9.583  17.008  0.52 24.60 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.262 -8.756  16.120  0.48 26.39 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.132 -8.498  16.170  0.52 24.60 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.450 -6.711  15.301  0.48 23.11 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.437 -6.447  15.426  0.52 21.07 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.450 -9.789  16.882  0.48 23.96 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.240 -9.782  16.693  0.52 22.01 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.412 -5.904  14.381  0.48 22.91 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.405 -5.757  14.431  0.52 20.78 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.412 -8.988  15.965  0.48 23.86 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.209 -9.098  15.701  0.52 21.87 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.395 -7.042  14.714  0.48 23.33 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.294 -7.082  14.568  0.52 21.23 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.158 -7.615  18.107  0.48 22.39 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.147 -7.379  18.327  0.52 22.71 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.778 -7.724  18.568  0.48 21.56 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.803 -7.549  18.862  0.52 23.13 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.799 -7.507  17.420  0.48 19.01 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.763 -7.352  17.770  0.52 21.34 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.006 -6.638  16.569  0.48 18.70 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.888 -6.459  16.928  0.52 21.43 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.510 -6.687  19.673  0.48 23.24 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.544 -6.555  20.002  0.52 25.04 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.139 -6.643  20.026  0.48 24.25 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.373 -6.900  20.719  0.52 26.52 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.305 -6.921  17.623  0.48 26.84 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.250 -6.667  17.855  0.52 27.22 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.628 -8.608  18.939  0.48 25.85 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.706 -8.447  19.216  0.52 27.73 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.036 -6.920  20.457  0.48 27.87 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.304 -6.566  20.608  0.52 30.03 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.775 -5.811  19.351  0.48 27.87 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.434 -5.668  19.627  0.52 30.03 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.021 -6.077  20.638  0.48 29.08 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.247 -6.352  21.341  0.52 31.80 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.729  -8.304  17.401  0.48 17.46 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.730  -8.191  17.793  0.52 19.75 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.627  -8.066  16.486  0.48 16.15 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.619  -8.035  16.882  0.52 18.63 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.815  -8.572  15.073  0.48 14.79 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.850  -8.537  15.479  0.52 17.01 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.087  -8.139  14.173  0.48 15.24 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.042  -8.233  14.594  0.52 17.34 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.624  -8.991  17.912  0.48 20.93 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.656  -8.858  18.330  0.52 23.68 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.826  -8.475  16.856  0.48 19.36 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.857  -8.515  17.233  0.52 22.33 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.470  -7.111  16.434  0.48 19.36 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.388  -7.096  16.829  0.52 22.33 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.761  -9.478  14.845  0.48 13.12 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.915  -9.297  15.240  0.52 15.52 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.029 -10.006 13.517  0.48 12.09 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.169 -9.817  13.906  0.52 13.80 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.182  -11.240 13.227  0.48 11.86 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.314  -11.048 13.627  0.52 12.58 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.831  -12.015 14.122  0.48 12.92 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.096  -11.892 14.504  0.52 13.85 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.507 -10.378 13.366  0.48 11.96 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.652 -10.160 13.728  0.52 14.19 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.437 -9.196  13.242  0.48 12.49 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.506 -8.939  13.458  0.52 14.13 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.782 -8.442  14.355  0.48 12.80 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.798 -8.041  14.472  0.52 14.61 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.969 -8.835  12.012  0.48 12.83 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 12.991 -8.672  12.183  0.52 13.68 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.626 -7.353  14.247  0.48 13.79 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.558 -6.914  14.230  0.52 14.73 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.813 -7.752  11.892  0.48 13.24 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.755 -7.549  11.931  0.52 13.87 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.136 -7.014  13.012  0.48 14.02 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.032 -6.674  12.957  0.52 14.37 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.975 -5.936  12.891  0.48 15.07 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.781 -5.552  12.705  0.52 14.76 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.258 -9.813  15.455  0.48 15.72 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.502 -9.526  15.831  0.52 18.60 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.813  -9.339  12.851  0.48 14.48 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.947  -9.131  13.256  0.52 16.53 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.784 -10.893 14.139  0.48 14.33 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.980 -10.591 14.533  0.52 17.01 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.601 -10.911 12.563  0.48 14.33 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.740 -10.765 12.972  0.52 17.01 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.426 -8.669  15.186  0.48 15.34 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.472 -8.204  15.330  0.52 17.51 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.749 -9.332  11.254  0.48 15.37 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.804 -9.263  11.489  0.52 16.39 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.845 -6.855  14.999  0.48 16.52 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.749 -6.324  14.920  0.52 17.65 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.165 -7.523  11.061  0.48 15.86 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.080 -7.385  11.073  0.52 16.62 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.096 -5.584  13.640  0.48 18.06 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.892 -5.113  13.410  0.52 17.69 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.873  -11.419 11.947  0.48 11.60 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.825  -11.131 12.393  0.52 11.87 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.284  -12.647 11.439  0.48 11.41 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.204  -12.339 11.879  0.52 11.93 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.411  -13.580 11.016  0.48 10.73 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.305  -13.290 11.428  0.52 11.21 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.379 -13.152 10.381  0.48 10.83 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.244 -12.883 10.738  0.52 10.83 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.416  -12.328 10.222  0.48 12.98 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.316  -11.976 10.691  0.52 13.04 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.685  -13.496 9.565   0.48 15.68 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.717  -13.136 9.898   0.52 15.24 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.616  -14.023 10.501  0.48 16.80 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.671  -13.857 10.720  0.52 16.60 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.085  -13.074 8.239   0.48 16.90 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.136  -12.628 8.592   0.52 16.24 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 9.009  -10.834 11.333  0.48 13.90 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.848  -10.479 11.825  0.52 14.22 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.747  -13.081 12.118  0.48 13.67 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.662  -12.756 12.570  0.52 14.29 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.743  -11.689 10.492  0.48 15.55 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.572  -11.438 11.016  0.52 15.62 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.983  -11.931 9.541   0.48 15.55 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.842  -11.444 10.073  0.52 15.62 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.315  -14.217 9.391   0.48 18.79 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.420  -13.768 9.683   0.52 18.27 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.189  -14.792 10.097  0.48 20.13 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.407  -14.667 10.253  0.52 19.90 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 6.027  -14.277 11.342  0.48 20.13 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.045  -14.082 11.586  0.52 19.90 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.962  -13.322 10.655  0.48 20.13 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 4.902  -13.276 10.834  0.52 19.90 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.625  -13.832 7.846   0.48 20.25 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.832  -13.389 8.072   0.52 19.47 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.458  -12.351 8.396   0.48 20.25 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.390  -12.041 8.788   0.52 19.47 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.796  -12.776 7.652   0.48 20.25 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.822  -12.147 8.107   0.52 19.47 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.278  -14.858 11.365  0.48 11.04 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.198  -14.551 11.826  0.52 11.53 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.287 -15.861 11.051  0.48 11.49 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.182 -15.553 11.443  0.52 11.55 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.950  -16.480 9.701   0.48 11.53 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.820  -16.097 10.066  0.52 11.10 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.901  -17.113 9.554   0.48 12.83 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.703  -16.581 9.862   0.52 11.65 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.320 -16.919 12.156  0.48 11.92 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.201 -16.668 12.485  0.52 12.17 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.386 -18.004 12.023  0.48 12.25 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.221 -17.764 12.228  0.52 12.65 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.483 -18.794 13.333  0.48 12.88 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.292 -18.715 13.417  0.52 13.30 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.488 -19.941 13.260  0.48 12.79 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.310 -19.838 13.214  0.52 13.40 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.854 -19.462 12.916  0.48 12.66 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.708 -19.328 13.089  0.52 13.75 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.590  -15.183 11.778  0.48 13.23 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.551  -14.846 12.311  0.52 13.81 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.157 -15.448 10.993  0.48 13.77 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.060 -15.140 11.399  0.52 13.83 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.477 -16.470 13.002  0.48 14.28 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.400 -16.273 13.350  0.52 14.58 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.462  -17.368 12.184  0.48 14.28 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.324  -17.077 12.509  0.52 14.58 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.146 -18.617 11.310  0.48 14.68 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.960 -18.268 11.442  0.52 15.16 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.250 -17.596 11.846  0.48 14.68 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.097 -17.365 12.098  0.52 15.16 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.761 -18.197 14.046  0.48 15.43 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.548 -18.216 14.208  0.52 15.94 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.613 -19.173 13.540  0.48 15.43 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.421 -19.122 13.548  0.52 15.94 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.531 -20.382 14.124  0.48 15.33 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.281 -20.439 13.974  0.52 16.05 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.206 -20.568 12.579  0.48 15.33 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.098 -20.320 12.400  0.52 16.05 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.416 -20.152 12.879  0.48 15.17 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.273 -20.009 12.975  0.52 16.48 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.843 -19.055 12.126  0.48 15.17 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.774 -18.781 12.390  0.52 16.48 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.141 -18.890 13.534  0.48 15.17 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.939 -18.885 13.826  0.52 16.48 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.828 -16.297 8.714   0.48 10.75 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.740 -15.994 9.110   0.52 11.23 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.592 -16.894 7.401   0.48 11.06 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.501 -16.540 7.777   0.52 11.57 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.190 -18.291 7.279   0.48 11.21 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.078 -17.937 7.597   0.52 11.48 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.565 -19.181 6.692   0.48 11.62 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.434 -18.796 6.988   0.52 11.44 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.154 -16.003 6.287   0.48 11.06 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.085 -15.621 6.699   0.52 12.81 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.510 -14.625 6.142   0.48 12.36 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.389 -14.288 6.433   0.52 14.13 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.291 -13.771 5.156   0.48 13.12 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 10.926 -13.678 5.148   0.52 14.99 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.044  -14.756 5.722   0.48 12.86 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.888  -14.481 6.351   0.52 14.56 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.559 -15.838 8.774   0.48 12.88 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.504 -15.603 9.206   0.52 13.45 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.637  -16.971 7.264   0.48 13.25 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.546  -16.604 7.636   0.52 13.86 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.099 -15.869 6.450   0.48 13.25 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.999 -15.413 6.947   0.52 15.34 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.038 -16.471 5.441   0.48 13.25 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.085 -16.108 5.863   0.52 15.34 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.531 -14.184 7.002   0.48 14.80 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.577 -13.674 7.162   0.52 16.93 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.855 -12.909 5.073   0.48 15.71 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.490 -12.826 4.992   0.52 17.96 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.195 -13.656 5.488   0.48 15.71 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.885 -13.547 5.236   0.52 17.96 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.309 -14.218 4.295   0.48 15.71 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.744 -14.283 4.410   0.52 17.96 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.688  -13.874 5.537   0.48 15.41 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.488  -13.693 5.956   0.52 17.45 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.990  -15.308 4.925   0.48 15.41 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.703  -15.260 5.802   0.52 17.45 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.541  -15.171 6.443   0.48 15.41 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.539  -14.619 7.246   0.52 17.45 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.397 -18.486 7.804   0.48 11.26 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.292 -18.171 8.086   0.52 11.59 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.113 -19.756 7.748   0.48 11.69 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.954 -19.463 7.980   0.52 11.95 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.872 -19.925 9.059   0.48 11.87 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.725 -19.710 9.269   0.52 12.18 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.742 -19.122 9.988   0.48 11.92 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.641 -18.944 10.234  0.52 12.51 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.097 -19.813 6.570   0.48 12.30 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.910 -19.523 6.780   0.52 12.41 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.185 -18.918 6.824   0.48 12.60 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.962 -18.574 6.972   0.52 12.38 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.439 -19.434 5.259   0.48 12.82 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.194 -19.243 5.460   0.52 13.50 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.838 -17.872 8.210   0.48 13.48 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.768 -17.572 8.484   0.52 13.89 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.476 -20.488 7.655   0.48 14.00 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.291 -20.159 7.880   0.52 14.32 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.440 -20.721 6.486   0.48 14.73 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.302 -20.406 6.727   0.52 14.86 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.738 -18.951 6.189   0.48 15.09 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.491 -18.586 6.314   0.52 14.83 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 14.058 -19.580 4.525   0.48 15.36 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.818 -19.337 4.719   0.52 16.18 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.649 -19.977 5.116   0.48 15.36 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.471 -19.880 5.339   0.52 16.18 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.184 -18.500 5.276   0.48 15.36 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 12.833 -18.347 5.457   0.52 16.18 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.710 -20.961 9.121   0.48 12.80 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.500 -20.791 9.264   0.52 12.92 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.499 -21.198 10.324  0.48 13.84 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.378 -21.089 10.384  0.52 13.93 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.330 -19.981 10.724  0.48 13.02 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.211 -19.870 10.759  0.52 13.38 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.630 -19.803 11.910  0.48 13.11 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.372 -19.561 11.945  0.52 14.15 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.428 -22.387 10.106  0.48 16.58 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.286 -22.261 10.008  0.52 16.44 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.389 -22.570 11.251  0.48 20.00 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.161 -22.708 11.161  0.52 19.39 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.942 -22.975 12.343  0.48 21.78 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.602 -23.050 12.226  0.52 20.65 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.589 -22.284 11.062  0.48 21.55 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.397 -22.736 10.997  0.52 21.19 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.839 -21.539 8.491   0.48 15.34 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.543 -21.350 8.623   0.52 15.48 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.906 -21.416 11.060  0.48 16.58 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.847 -21.348 11.155  0.52 16.69 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.891 -23.198 10.007  0.48 19.88 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.728 -23.017 9.739   0.52 19.71 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.954 -22.245 9.306   0.48 19.88 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.853 -21.999 9.265   0.52 19.71 ?  14  ASP   A HB3  1 
ATOM   371  N N    . ASN   A 1 15  ? 16.727 -19.144 9.762   1.00 12.53 ?  15  ASN   A N    1 
ATOM   372  C CA   . ASN   A 1 15  ? 17.707 -18.091 10.011  1.00 13.24 ?  15  ASN   A CA   1 
ATOM   373  C C    . ASN   A 1 15  ? 17.339 -16.706 9.493   1.00 13.19 ?  15  ASN   A C    1 
ATOM   374  O O    . ASN   A 1 15  ? 18.115 -15.775 9.719   1.00 14.72 ?  15  ASN   A O    1 
ATOM   375  C CB   . ASN   A 1 15  ? 19.080 -18.489 9.434   1.00 13.05 ?  15  ASN   A CB   1 
ATOM   376  C CG   . ASN   A 1 15  ? 19.073 -18.574 7.924   1.00 13.35 ?  15  ASN   A CG   1 
ATOM   377  O OD1  . ASN   A 1 15  ? 18.376 -19.407 7.341   1.00 14.10 ?  15  ASN   A OD1  1 
ATOM   378  N ND2  . ASN   A 1 15  ? 19.850 -17.709 7.276   1.00 13.25 ?  15  ASN   A ND2  1 
ATOM   379  H H    A ASN   A 1 15  ? 16.438 -19.169 8.958   0.48 15.01 ?  15  ASN   A H    1 
ATOM   380  H H    B ASN   A 1 15  ? 16.518 -19.244 8.938   0.52 15.01 ?  15  ASN   A H    1 
ATOM   381  H HA   . ASN   A 1 15  ? 17.827 -18.005 10.969  1.00 15.86 ?  15  ASN   A HA   1 
ATOM   382  H HB2  . ASN   A 1 15  ? 19.740 -17.822 9.698   1.00 15.64 ?  15  ASN   A HB2  1 
ATOM   383  H HB3  . ASN   A 1 15  ? 19.337 -19.358 9.784   1.00 15.64 ?  15  ASN   A HB3  1 
ATOM   384  H HD21 . ASN   A 1 15  ? 19.874 -17.714 6.415   1.00 15.88 ?  15  ASN   A HD21 1 
ATOM   385  H HD22 . ASN   A 1 15  ? 20.320 -17.132 7.712   1.00 15.88 ?  15  ASN   A HD22 1 
ATOM   386  N N    A VAL   A 1 16  ? 16.237 -16.562 8.755   0.48 12.42 ?  16  VAL   A N    1 
ATOM   387  N N    B VAL   A 1 16  ? 16.169 -16.514 8.886   0.52 13.05 ?  16  VAL   A N    1 
ATOM   388  C CA   A VAL   A 1 16  ? 15.835 -15.294 8.157   0.48 12.17 ?  16  VAL   A CA   1 
ATOM   389  C CA   B VAL   A 1 16  ? 15.777 -15.224 8.323   0.52 12.81 ?  16  VAL   A CA   1 
ATOM   390  C C    A VAL   A 1 16  ? 14.545 -14.811 8.805   0.48 11.54 ?  16  VAL   A C    1 
ATOM   391  C C    B VAL   A 1 16  ? 14.529 -14.713 9.040   0.52 12.51 ?  16  VAL   A C    1 
ATOM   392  O O    A VAL   A 1 16  ? 13.530 -15.523 8.826   0.48 11.14 ?  16  VAL   A O    1 
ATOM   393  O O    B VAL   A 1 16  ? 13.549 -15.453 9.211   0.52 12.13 ?  16  VAL   A O    1 
ATOM   394  C CB   A VAL   A 1 16  ? 15.681 -15.386 6.630   0.48 12.61 ?  16  VAL   A CB   1 
ATOM   395  C CB   B VAL   A 1 16  ? 15.568 -15.311 6.799   0.52 12.89 ?  16  VAL   A CB   1 
ATOM   396  C CG1  A VAL   A 1 16  ? 15.276 -14.025 6.069   0.48 13.15 ?  16  VAL   A CG1  1 
ATOM   397  C CG1  B VAL   A 1 16  ? 15.115 -13.972 6.226   0.52 13.34 ?  16  VAL   A CG1  1 
ATOM   398  C CG2  A VAL   A 1 16  ? 16.968 -15.869 5.988   0.48 13.08 ?  16  VAL   A CG2  1 
ATOM   399  C CG2  B VAL   A 1 16  ? 16.844 -15.793 6.105   0.52 13.39 ?  16  VAL   A CG2  1 
ATOM   400  H H    A VAL   A 1 16  ? 15.700 -17.215 8.582   0.48 14.88 ?  16  VAL   A H    1 
ATOM   401  H H    B VAL   A 1 16  ? 15.571 -17.128 8.796   0.52 15.63 ?  16  VAL   A H    1 
ATOM   402  H HA   A VAL   A 1 16  ? 16.526 -14.642 8.341   0.48 14.58 ?  16  VAL   A HA   1 
ATOM   403  H HA   B VAL   A 1 16  ? 16.488 -14.585 8.485   0.52 15.35 ?  16  VAL   A HA   1 
ATOM   404  H HB   A VAL   A 1 16  ? 14.983 -16.026 6.417   0.48 15.11 ?  16  VAL   A HB   1 
ATOM   405  H HB   B VAL   A 1 16  ? 14.876 -15.960 6.619   0.52 15.44 ?  16  VAL   A HB   1 
ATOM   406  H HG11 A VAL   A 1 16  ? 15.371 -14.039 5.106   0.48 15.76 ?  16  VAL   A HG11 1 
ATOM   407  H HG11 B VAL   A 1 16  ? 15.167 -14.015 5.256   0.52 15.99 ?  16  VAL   A HG11 1 
ATOM   408  H HG12 A VAL   A 1 16  ? 14.353 -13.845 6.308   0.48 15.76 ?  16  VAL   A HG12 1 
ATOM   409  H HG12 B VAL   A 1 16  ? 14.203 -13.803 6.499   0.52 15.99 ?  16  VAL   A HG12 1 
ATOM   410  H HG13 A VAL   A 1 16  ? 15.855 -13.343 6.449   0.48 15.76 ?  16  VAL   A HG13 1 
ATOM   411  H HG13 B VAL   A 1 16  ? 15.700 -13.272 6.555   0.52 15.99 ?  16  VAL   A HG13 1 
ATOM   412  H HG21 A VAL   A 1 16  ? 16.870 -15.837 5.025   0.48 15.67 ?  16  VAL   A HG21 1 
ATOM   413  H HG21 B VAL   A 1 16  ? 16.702 -15.798 5.145   0.52 16.05 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 A VAL   A 1 16  ? 17.695 -15.292 6.268   0.48 15.67 ?  16  VAL   A HG22 1 
ATOM   415  H HG22 B VAL   A 1 16  ? 17.577 -15.196 6.326   0.52 16.05 ?  16  VAL   A HG22 1 
ATOM   416  H HG23 A VAL   A 1 16  ? 17.142 -16.781 6.273   0.48 15.67 ?  16  VAL   A HG23 1 
ATOM   417  H HG23 B VAL   A 1 16  ? 17.053 -16.693 6.410   0.52 16.05 ?  16  VAL   A HG23 1 
ATOM   418  N N    A TYR   A 1 17  ? 14.590 -13.578 9.293   0.48 11.21 ?  17  TYR   A N    1 
ATOM   419  N N    B TYR   A 1 17  ? 14.569 -13.435 9.432   0.52 12.35 ?  17  TYR   A N    1 
ATOM   420  C CA   A TYR   A 1 17  ? 13.489 -12.881 9.931   0.48 11.18 ?  17  TYR   A CA   1 
ATOM   421  C CA   B TYR   A 1 17  ? 13.514 -12.761 10.179  0.52 11.89 ?  17  TYR   A CA   1 
ATOM   422  C C    A TYR   A 1 17  ? 13.220 -11.582 9.176   0.48 10.94 ?  17  TYR   A C    1 
ATOM   423  C C    B TYR   A 1 17  ? 13.232 -11.421 9.513   0.52 11.66 ?  17  TYR   A C    1 
ATOM   424  O O    A TYR   A 1 17  ? 14.108 -11.045 8.510   0.48 10.32 ?  17  TYR   A O    1 
ATOM   425  O O    B TYR   A 1 17  ? 14.143 -10.805 8.957   0.52 11.51 ?  17  TYR   A O    1 
ATOM   426  C CB   A TYR   A 1 17  ? 13.865 -12.565 11.382  0.48 11.80 ?  17  TYR   A CB   1 
ATOM   427  C CB   B TYR   A 1 17  ? 13.977 -12.519 11.619  0.52 12.30 ?  17  TYR   A CB   1 
ATOM   428  C CG   A TYR   A 1 17  ? 14.051 -13.808 12.227  0.48 13.04 ?  17  TYR   A CG   1 
ATOM   429  C CG   B TYR   A 1 17  ? 14.208 -13.790 12.403  0.52 13.09 ?  17  TYR   A CG   1 
ATOM   430  C CD1  A TYR   A 1 17  ? 15.238 -14.539 12.198  0.48 13.85 ?  17  TYR   A CD1  1 
ATOM   431  C CD1  B TYR   A 1 17  ? 15.404 -14.493 12.302  0.52 13.87 ?  17  TYR   A CD1  1 
ATOM   432  C CD2  A TYR   A 1 17  ? 13.025 -14.269 13.039  0.48 13.15 ?  17  TYR   A CD2  1 
ATOM   433  C CD2  B TYR   A 1 17  ? 13.223 -14.293 13.241  0.52 13.45 ?  17  TYR   A CD2  1 
ATOM   434  C CE1  A TYR   A 1 17  ? 15.390 -15.698 12.965  0.48 14.03 ?  17  TYR   A CE1  1 
ATOM   435  C CE1  B TYR   A 1 17  ? 15.609 -15.666 13.014  0.52 14.83 ?  17  TYR   A CE1  1 
ATOM   436  C CE2  A TYR   A 1 17  ? 13.168 -15.418 13.807  0.48 13.79 ?  17  TYR   A CE2  1 
ATOM   437  C CE2  B TYR   A 1 17  ? 13.420 -15.465 13.959  0.52 14.24 ?  17  TYR   A CE2  1 
ATOM   438  C CZ   A TYR   A 1 17  ? 14.348 -16.127 13.770  0.48 13.92 ?  17  TYR   A CZ   1 
ATOM   439  C CZ   B TYR   A 1 17  ? 14.615 -16.145 13.843  0.52 14.98 ?  17  TYR   A CZ   1 
ATOM   440  O OH   A TYR   A 1 17  ? 14.477 -17.267 14.537  0.48 14.16 ?  17  TYR   A OH   1 
ATOM   441  O OH   B TYR   A 1 17  ? 14.819 -17.307 14.557  0.52 15.96 ?  17  TYR   A OH   1 
ATOM   442  H H    A TYR   A 1 17  ? 15.305 -13.108 9.252   0.48 13.42 ?  17  TYR   A H    1 
ATOM   443  H H    B TYR   A 1 17  ? 15.231 -12.901 9.254   0.52 14.79 ?  17  TYR   A H    1 
ATOM   444  H HA   A TYR   A 1 17  ? 12.699 -13.451 9.913   0.48 13.40 ?  17  TYR   A HA   1 
ATOM   445  H HA   B TYR   A 1 17  ? 12.703 -13.291 10.184  0.52 14.24 ?  17  TYR   A HA   1 
ATOM   446  H HB2  A TYR   A 1 17  ? 14.696 -12.069 11.387  0.48 14.13 ?  17  TYR   A HB2  1 
ATOM   447  H HB2  B TYR   A 1 17  ? 14.813 -12.030 11.598  0.52 14.73 ?  17  TYR   A HB2  1 
ATOM   448  H HB3  A TYR   A 1 17  ? 13.158 -12.039 11.772  0.48 14.13 ?  17  TYR   A HB3  1 
ATOM   449  H HB3  B TYR   A 1 17  ? 13.304 -12.004 12.084  0.52 14.73 ?  17  TYR   A HB3  1 
ATOM   450  H HD1  A TYR   A 1 17  ? 15.941 -14.255 11.657  0.48 16.59 ?  17  TYR   A HD1  1 
ATOM   451  H HD1  B TYR   A 1 17  ? 16.076 -14.175 11.742  0.52 16.63 ?  17  TYR   A HD1  1 
ATOM   452  H HD2  A TYR   A 1 17  ? 12.222 -13.805 13.072  0.48 15.76 ?  17  TYR   A HD2  1 
ATOM   453  H HD2  B TYR   A 1 17  ? 12.414 -13.839 13.319  0.52 16.12 ?  17  TYR   A HD2  1 
ATOM   454  H HE1  A TYR   A 1 17  ? 16.195 -16.172 12.942  0.48 16.82 ?  17  TYR   A HE1  1 
ATOM   455  H HE1  B TYR   A 1 17  ? 16.415 -16.127 12.938  0.52 17.77 ?  17  TYR   A HE1  1 
ATOM   456  H HE2  A TYR   A 1 17  ? 12.472 -15.710 14.350  0.48 16.52 ?  17  TYR   A HE2  1 
ATOM   457  H HE2  B TYR   A 1 17  ? 12.748 -15.786 14.516  0.52 17.07 ?  17  TYR   A HE2  1 
ATOM   458  H HH   A TYR   A 1 17  ? 13.729 -17.493 14.835  0.48 16.97 ?  17  TYR   A HH   1 
ATOM   459  H HH   B TYR   A 1 17  ? 15.578 -17.620 14.388  0.52 19.12 ?  17  TYR   A HH   1 
ATOM   460  N N    A ILE   A 1 18  ? 12.000 -11.057 9.294   0.48 11.39 ?  18  ILE   A N    1 
ATOM   461  N N    B ILE   A 1 18  ? 11.977 -10.954 9.563   0.52 11.66 ?  18  ILE   A N    1 
ATOM   462  C CA   A ILE   A 1 18  ? 11.597 -9.891  8.502   0.48 11.49 ?  18  ILE   A CA   1 
ATOM   463  C CA   B ILE   A 1 18  ? 11.593 -9.755  8.819   0.52 11.19 ?  18  ILE   A CA   1 
ATOM   464  C C    A ILE   A 1 18  ? 10.607 -9.040  9.295   0.48 12.03 ?  18  ILE   A C    1 
ATOM   465  C C    B ILE   A 1 18  ? 10.643 -8.886  9.631   0.52 11.44 ?  18  ILE   A C    1 
ATOM   466  O O    A ILE   A 1 18  ? 9.764  -9.564  10.026  0.48 11.95 ?  18  ILE   A O    1 
ATOM   467  O O    B ILE   A 1 18  ? 9.860  -9.377  10.449  0.52 11.56 ?  18  ILE   A O    1 
ATOM   468  C CB   A ILE   A 1 18  ? 11.071 -10.332 7.117   0.48 11.22 ?  18  ILE   A CB   1 
ATOM   469  C CB   B ILE   A 1 18  ? 10.990 -10.137 7.450   0.52 10.86 ?  18  ILE   A CB   1 
ATOM   470  C CG1  A ILE   A 1 18  ? 10.985 -9.144  6.163   0.48 11.63 ?  18  ILE   A CG1  1 
ATOM   471  C CG1  B ILE   A 1 18  ? 10.929 -8.940  6.501   0.52 11.96 ?  18  ILE   A CG1  1 
ATOM   472  C CG2  A ILE   A 1 18  ? 9.736  -11.076 7.243   0.48 11.34 ?  18  ILE   A CG2  1 
ATOM   473  C CG2  B ILE   A 1 18  ? 9.625  -10.782 7.626   0.52 11.41 ?  18  ILE   A CG2  1 
ATOM   474  C CD1  A ILE   A 1 18  ? 10.837 -9.560  4.720   0.48 13.02 ?  18  ILE   A CD1  1 
ATOM   475  C CD1  B ILE   A 1 18  ? 10.591 -9.350  5.087   0.52 13.72 ?  18  ILE   A CD1  1 
ATOM   476  H H    A ILE   A 1 18  ? 11.402 -11.360 9.829   0.48 13.65 ?  18  ILE   A H    1 
ATOM   477  H H    B ILE   A 1 18  ? 11.330 -11.319 10.009  0.52 13.96 ?  18  ILE   A H    1 
ATOM   478  H HA   A ILE   A 1 18  ? 12.382 -9.354  8.346   0.48 13.76 ?  18  ILE   A HA   1 
ATOM   479  H HA   B ILE   A 1 18  ? 12.394 -9.234  8.651   0.52 13.40 ?  18  ILE   A HA   1 
ATOM   480  H HB   A ILE   A 1 18  ? 11.709 -10.964 6.740   0.48 13.44 ?  18  ILE   A HB   1 
ATOM   481  H HB   B ILE   A 1 18  ? 11.571 -10.793 7.050   0.52 13.00 ?  18  ILE   A HB   1 
ATOM   482  H HG12 A ILE   A 1 18  ? 10.218 -8.604  6.402   0.48 13.93 ?  18  ILE   A HG12 1 
ATOM   483  H HG12 B ILE   A 1 18  ? 10.246 -8.320  6.802   0.52 14.33 ?  18  ILE   A HG12 1 
ATOM   484  H HG13 A ILE   A 1 18  ? 11.799 -8.623  6.243   0.48 13.93 ?  18  ILE   A HG13 1 
ATOM   485  H HG13 B ILE   A 1 18  ? 11.794 -8.500  6.484   0.52 14.33 ?  18  ILE   A HG13 1 
ATOM   486  H HG21 A ILE   A 1 18  ? 9.503  -11.464 6.381   0.48 13.59 ?  18  ILE   A HG21 1 
ATOM   487  H HG21 B ILE   A 1 18  ? 9.363  -11.197 6.787   0.52 13.66 ?  18  ILE   A HG21 1 
ATOM   488  H HG22 A ILE   A 1 18  ? 9.825  -11.781 7.904   0.48 13.59 ?  18  ILE   A HG22 1 
ATOM   489  H HG22 B ILE   A 1 18  ? 9.680  -11.453 8.322   0.52 13.66 ?  18  ILE   A HG22 1 
ATOM   490  H HG23 A ILE   A 1 18  ? 9.048  -10.451 7.517   0.48 13.59 ?  18  ILE   A HG23 1 
ATOM   491  H HG23 B ILE   A 1 18  ? 8.977  -10.103 7.872   0.52 13.66 ?  18  ILE   A HG23 1 
ATOM   492  H HD11 A ILE   A 1 18  ? 10.830 -8.764  4.165   0.48 15.60 ?  18  ILE   A HD11 1 
ATOM   493  H HD11 B ILE   A 1 18  ? 10.685 -8.583  4.501   0.52 16.43 ?  18  ILE   A HD11 1 
ATOM   494  H HD12 A ILE   A 1 18  ? 11.582 -10.128 4.477   0.48 15.60 ?  18  ILE   A HD12 1 
ATOM   495  H HD12 B ILE   A 1 18  ? 11.202 -10.052 4.809   0.52 16.43 ?  18  ILE   A HD12 1 
ATOM   496  H HD13 A ILE   A 1 18  ? 10.002 -10.043 4.616   0.48 15.60 ?  18  ILE   A HD13 1 
ATOM   497  H HD13 B ILE   A 1 18  ? 9.679  -9.677  5.061   0.52 16.43 ?  18  ILE   A HD13 1 
ATOM   498  N N    A LYS   A 1 19  ? 10.706 -7.719  9.132   0.48 12.51 ?  19  LYS   A N    1 
ATOM   499  N N    B LYS   A 1 19  ? 10.693 -7.580  9.369   0.52 12.19 ?  19  LYS   A N    1 
ATOM   500  C CA   A LYS   A 1 19  ? 9.892  -6.760  9.875   0.48 13.28 ?  19  LYS   A CA   1 
ATOM   501  C CA   B LYS   A 1 19  ? 9.856  -6.622  10.080  0.52 13.89 ?  19  LYS   A CA   1 
ATOM   502  C C    A LYS   A 1 19  ? 9.706  -5.495  9.044   0.48 12.64 ?  19  LYS   A C    1 
ATOM   503  C C    B LYS   A 1 19  ? 9.679  -5.386  9.209   0.52 14.05 ?  19  LYS   A C    1 
ATOM   504  O O    A LYS   A 1 19  ? 10.554 -5.154  8.215   0.48 11.69 ?  19  LYS   A O    1 
ATOM   505  O O    B LYS   A 1 19  ? 10.638 -4.930  8.586   0.52 13.93 ?  19  LYS   A O    1 
ATOM   506  C CB   A LYS   A 1 19  ? 10.594 -6.390  11.192  0.48 14.01 ?  19  LYS   A CB   1 
ATOM   507  C CB   B LYS   A 1 19  ? 10.539 -6.231  11.394  0.52 14.75 ?  19  LYS   A CB   1 
ATOM   508  C CG   A LYS   A 1 19  ? 9.869  -5.412  12.125  0.48 15.23 ?  19  LYS   A CG   1 
ATOM   509  C CG   B LYS   A 1 19  ? 9.741  -5.302  12.274  0.52 16.01 ?  19  LYS   A CG   1 
ATOM   510  C CD   A LYS   A 1 19  ? 10.763 -5.124  13.340  0.48 16.23 ?  19  LYS   A CD   1 
ATOM   511  C CD   B LYS   A 1 19  ? 10.545 -4.964  13.506  0.52 17.31 ?  19  LYS   A CD   1 
ATOM   512  C CE   A LYS   A 1 19  ? 10.129 -4.192  14.362  0.48 16.94 ?  19  LYS   A CE   1 
ATOM   513  C CE   B LYS   A 1 19  ? 9.795  -4.037  14.432  0.52 18.13 ?  19  LYS   A CE   1 
ATOM   514  N NZ   A LYS   A 1 19  ? 11.031 -3.996  15.540  0.48 17.33 ?  19  LYS   A NZ   1 
ATOM   515  N NZ   B LYS   A 1 19  ? 10.664 -3.617  15.557  0.52 18.39 ?  19  LYS   A NZ   1 
ATOM   516  H H    A LYS   A 1 19  ? 11.258 -7.360  8.586   0.48 14.99 ?  19  LYS   A H    1 
ATOM   517  H H    B LYS   A 1 19  ? 11.209 -7.216  8.776   0.52 14.61 ?  19  LYS   A H    1 
ATOM   518  H HA   A LYS   A 1 19  ? 9.025  -7.153  10.069  0.48 15.91 ?  19  LYS   A HA   1 
ATOM   519  H HA   B LYS   A 1 19  ? 8.990  -7.010  10.272  0.52 16.64 ?  19  LYS   A HA   1 
ATOM   520  H HB2  A LYS   A 1 19  ? 10.731 -7.207  11.694  0.48 16.79 ?  19  LYS   A HB2  1 
ATOM   521  H HB2  B LYS   A 1 19  ? 10.710 -7.040  11.907  0.52 17.68 ?  19  LYS   A HB2  1 
ATOM   522  H HB3  A LYS   A 1 19  ? 11.449 -5.997  10.974  0.48 16.79 ?  19  LYS   A HB3  1 
ATOM   523  H HB3  B LYS   A 1 19  ? 11.379 -5.794  11.190  0.52 17.68 ?  19  LYS   A HB3  1 
ATOM   524  H HG2  A LYS   A 1 19  ? 9.699  -4.575  11.663  0.48 18.25 ?  19  LYS   A HG2  1 
ATOM   525  H HG2  B LYS   A 1 19  ? 9.551  -4.481  11.792  0.52 19.18 ?  19  LYS   A HG2  1 
ATOM   526  H HG3  A LYS   A 1 19  ? 9.038  -5.803  12.439  0.48 18.25 ?  19  LYS   A HG3  1 
ATOM   527  H HG3  B LYS   A 1 19  ? 8.919  -5.738  12.547  0.52 19.18 ?  19  LYS   A HG3  1 
ATOM   528  H HD2  A LYS   A 1 19  ? 10.962 -5.960  13.790  0.48 19.45 ?  19  LYS   A HD2  1 
ATOM   529  H HD2  B LYS   A 1 19  ? 10.746 -5.784  13.987  0.52 20.75 ?  19  LYS   A HD2  1 
ATOM   530  H HD3  A LYS   A 1 19  ? 11.585 -4.710  13.035  0.48 19.45 ?  19  LYS   A HD3  1 
ATOM   531  H HD3  B LYS   A 1 19  ? 11.370 -4.527  13.236  0.52 20.75 ?  19  LYS   A HD3  1 
ATOM   532  H HE2  A LYS   A 1 19  ? 9.969  -3.324  13.956  0.48 20.31 ?  19  LYS   A HE2  1 
ATOM   533  H HE2  B LYS   A 1 19  ? 9.520  -3.247  13.941  0.52 21.73 ?  19  LYS   A HE2  1 
ATOM   534  H HE3  A LYS   A 1 19  ? 9.296  -4.574  14.679  0.48 20.31 ?  19  LYS   A HE3  1 
ATOM   535  H HE3  B LYS   A 1 19  ? 9.023  -4.500  14.792  0.52 21.73 ?  19  LYS   A HE3  1 
ATOM   536  H HZ1  A LYS   A 1 19  ? 10.656 -3.438  16.125  0.48 20.77 ?  19  LYS   A HZ1  1 
ATOM   537  H HZ1  B LYS   A 1 19  ? 10.219 -3.073  16.099  0.52 22.04 ?  19  LYS   A HZ1  1 
ATOM   538  H HZ2  A LYS   A 1 19  ? 11.182 -4.776  15.941  0.48 20.77 ?  19  LYS   A HZ2  1 
ATOM   539  H HZ2  B LYS   A 1 19  ? 10.931 -4.332  16.017  0.52 22.04 ?  19  LYS   A HZ2  1 
ATOM   540  H HZ3  A LYS   A 1 19  ? 11.808 -3.653  15.275  0.48 20.77 ?  19  LYS   A HZ3  1 
ATOM   541  H HZ3  B LYS   A 1 19  ? 11.383 -3.194  15.244  0.52 22.04 ?  19  LYS   A HZ3  1 
ATOM   542  N N    A ASN   A 1 20  ? 8.592  -4.796  9.280   0.48 13.48 ?  20  ASN   A N    1 
ATOM   543  N N    B ASN   A 1 20  ? 8.453  -4.862  9.145   0.52 14.97 ?  20  ASN   A N    1 
ATOM   544  C CA   A ASN   A 1 20  ? 8.363  -3.472  8.708   0.48 14.37 ?  20  ASN   A CA   1 
ATOM   545  C CA   B ASN   A 1 20  ? 8.229  -3.557  8.521   0.52 16.16 ?  20  ASN   A CA   1 
ATOM   546  C C    A ASN   A 1 20  ? 8.973  -2.473  9.686   0.48 14.74 ?  20  ASN   A C    1 
ATOM   547  C C    B ASN   A 1 20  ? 8.834  -2.482  9.410   0.52 16.20 ?  20  ASN   A C    1 
ATOM   548  O O    A ASN   A 1 20  ? 8.483  -2.318  10.809  0.48 15.20 ?  20  ASN   A O    1 
ATOM   549  O O    B ASN   A 1 20  ? 8.214  -2.040  10.382  0.52 17.23 ?  20  ASN   A O    1 
ATOM   550  C CB   A ASN   A 1 20  ? 6.863  -3.239  8.500   0.48 15.53 ?  20  ASN   A CB   1 
ATOM   551  C CB   B ASN   A 1 20  ? 6.743  -3.291  8.320   0.52 17.72 ?  20  ASN   A CB   1 
ATOM   552  C CG   A ASN   A 1 20  ? 6.531  -1.854  7.936   0.48 16.95 ?  20  ASN   A CG   1 
ATOM   553  C CG   B ASN   A 1 20  ? 6.452  -1.829  8.025   0.52 19.59 ?  20  ASN   A CG   1 
ATOM   554  O OD1  A ASN   A 1 20  ? 5.490  -1.275  8.266   0.48 18.83 ?  20  ASN   A OD1  1 
ATOM   555  O OD1  B ASN   A 1 20  ? 5.601  -1.209  8.668   0.52 22.11 ?  20  ASN   A OD1  1 
ATOM   556  N ND2  A ASN   A 1 20  ? 7.398  -1.330  7.073   0.48 17.01 ?  20  ASN   A ND2  1 
ATOM   557  N ND2  B ASN   A 1 20  ? 7.179  -1.265  7.060   0.52 19.74 ?  20  ASN   A ND2  1 
ATOM   558  H H    A ASN   A 1 20  ? 7.959  -5.062  9.794   0.48 16.16 ?  20  ASN   A H    1 
ATOM   559  H H    B ASN   A 1 20  ? 7.743  -5.260  9.425   0.52 17.94 ?  20  ASN   A H    1 
ATOM   560  H HA   A ASN   A 1 20  ? 8.816  -3.402  7.854   0.48 17.22 ?  20  ASN   A HA   1 
ATOM   561  H HA   B ASN   A 1 20  ? 8.676  -3.532  7.660   0.52 19.37 ?  20  ASN   A HA   1 
ATOM   562  H HB2  A ASN   A 1 20  ? 6.532  -3.900  7.875   0.48 18.61 ?  20  ASN   A HB2  1 
ATOM   563  H HB2  B ASN   A 1 20  ? 6.427  -3.808  7.572   0.52 21.23 ?  20  ASN   A HB2  1 
ATOM   564  H HB3  A ASN   A 1 20  ? 6.414  -3.333  9.354   0.48 18.61 ?  20  ASN   A HB3  1 
ATOM   565  H HB3  B ASN   A 1 20  ? 6.269  -3.539  9.130   0.52 21.23 ?  20  ASN   A HB3  1 
ATOM   566  H HD21 A ASN   A 1 20  ? 7.246  -0.554  6.739   0.48 20.39 ?  20  ASN   A HD21 1 
ATOM   567  H HD21 B ASN   A 1 20  ? 7.064  -0.438  6.862   0.52 23.67 ?  20  ASN   A HD21 1 
ATOM   568  H HD22 A ASN   A 1 20  ? 8.106  -1.764  6.852   0.48 20.39 ?  20  ASN   A HD22 1 
ATOM   569  H HD22 B ASN   A 1 20  ? 7.764  -1.732  6.631   0.52 23.67 ?  20  ASN   A HD22 1 
ATOM   570  N N    A ALA   A 1 21  ? 10.077 -1.842  9.290   0.48 14.81 ?  21  ALA   A N    1 
ATOM   571  N N    B ALA   A 1 21  ? 10.038 -2.032  9.065   0.52 15.43 ?  21  ALA   A N    1 
ATOM   572  C CA   A ALA   A 1 21  ? 10.766 -0.938  10.199  0.48 15.31 ?  21  ALA   A CA   1 
ATOM   573  C CA   B ALA   A 1 21  ? 10.729 -1.055  9.890   0.52 15.10 ?  21  ALA   A CA   1 
ATOM   574  C C    A ALA   A 1 21  ? 11.739 -0.066  9.422   0.48 14.78 ?  21  ALA   A C    1 
ATOM   575  C C    B ALA   A 1 21  ? 11.763 -0.321  9.054   0.52 13.43 ?  21  ALA   A C    1 
ATOM   576  O O    A ALA   A 1 21  ? 12.203 -0.438  8.341   0.48 15.12 ?  21  ALA   A O    1 
ATOM   577  O O    B ALA   A 1 21  ? 12.249 -0.838  8.045   0.52 13.35 ?  21  ALA   A O    1 
ATOM   578  C CB   A ALA   A 1 21  ? 11.520 -1.713  11.284  0.48 16.32 ?  21  ALA   A CB   1 
ATOM   579  C CB   B ALA   A 1 21  ? 11.418 -1.718  11.088  0.52 16.41 ?  21  ALA   A CB   1 
ATOM   580  H H    A ALA   A 1 21  ? 10.448 -1.924  8.517   0.48 17.74 ?  21  ALA   A H    1 
ATOM   581  H H    B ALA   A 1 21  ? 10.460 -2.263  8.350   0.52 18.49 ?  21  ALA   A H    1 
ATOM   582  H HA   A ALA   A 1 21  ? 10.119 -0.357  10.630  0.48 18.35 ?  21  ALA   A HA   1 
ATOM   583  H HA   B ALA   A 1 21  ? 10.081 -0.413  10.224  0.52 18.09 ?  21  ALA   A HA   1 
ATOM   584  H HB1  A ALA   A 1 21  ? 11.920 -1.079  11.896  0.48 19.57 ?  21  ALA   A HB1  1 
ATOM   585  H HB1  B ALA   A 1 21  ? 11.845 -1.028  11.619  0.52 19.67 ?  21  ALA   A HB1  1 
ATOM   586  H HB2  A ALA   A 1 21  ? 10.887 -2.276  11.756  0.48 19.57 ?  21  ALA   A HB2  1 
ATOM   587  H HB2  B ALA   A 1 21  ? 10.750 -2.178  11.622  0.52 19.67 ?  21  ALA   A HB2  1 
ATOM   588  H HB3  A ALA   A 1 21  ? 12.202 -2.256  10.865  0.48 19.57 ?  21  ALA   A HB3  1 
ATOM   589  H HB3  B ALA   A 1 21  ? 12.076 -2.347  10.763  0.52 19.67 ?  21  ALA   A HB3  1 
ATOM   590  N N    A ASP   A 1 22  ? 12.029 1.102   9.995   0.48 14.65 ?  22  ASP   A N    1 
ATOM   591  N N    B ASP   A 1 22  ? 12.074 0.896   9.493   0.52 12.78 ?  22  ASP   A N    1 
ATOM   592  C CA   A ASP   A 1 22  ? 13.079 1.983   9.502   0.48 14.52 ?  22  ASP   A CA   1 
ATOM   593  C CA   B ASP   A 1 22  ? 13.193 1.667   8.969   0.52 12.13 ?  22  ASP   A CA   1 
ATOM   594  C C    A ASP   A 1 22  ? 14.407 1.511   10.078  0.48 13.29 ?  22  ASP   A C    1 
ATOM   595  C C    B ASP   A 1 22  ? 14.474 1.134   9.607   0.52 11.14 ?  22  ASP   A C    1 
ATOM   596  O O    A ASP   A 1 22  ? 14.602 1.536   11.297  0.48 13.35 ?  22  ASP   A O    1 
ATOM   597  O O    B ASP   A 1 22  ? 14.598 1.126   10.836  0.52 11.85 ?  22  ASP   A O    1 
ATOM   598  C CB   A ASP   A 1 22  ? 12.787 3.415   9.945   0.48 16.12 ?  22  ASP   A CB   1 
ATOM   599  C CB   B ASP   A 1 22  ? 12.976 3.132   9.347   0.52 13.52 ?  22  ASP   A CB   1 
ATOM   600  C CG   A ASP   A 1 22  ? 13.831 4.410   9.465   0.48 17.34 ?  22  ASP   A CG   1 
ATOM   601  C CG   B ASP   A 1 22  ? 13.972 4.071   8.703   0.52 14.25 ?  22  ASP   A CG   1 
ATOM   602  O OD1  A ASP   A 1 22  ? 14.864 3.995   8.902   0.48 17.67 ?  22  ASP   A OD1  1 
ATOM   603  O OD1  B ASP   A 1 22  ? 15.107 3.638   8.405   0.52 13.16 ?  22  ASP   A OD1  1 
ATOM   604  O OD2  A ASP   A 1 22  ? 13.608 5.625   9.650   0.48 18.15 -1 22  ASP   A OD2  1 
ATOM   605  O OD2  B ASP   A 1 22  ? 13.614 5.254   8.503   0.52 16.18 -1 22  ASP   A OD2  1 
ATOM   606  H H    A ASP   A 1 22  ? 11.616 1.413   10.683  0.48 17.56 ?  22  ASP   A H    1 
ATOM   607  H H    B ASP   A 1 22  ? 11.628 1.305   10.107  0.52 15.31 ?  22  ASP   A H    1 
ATOM   608  H HA   A ASP   A 1 22  ? 13.121 1.947   8.534   0.48 17.41 ?  22  ASP   A HA   1 
ATOM   609  H HA   B ASP   A 1 22  ? 13.241 1.575   8.004   0.52 14.54 ?  22  ASP   A HA   1 
ATOM   610  H HB2  A ASP   A 1 22  ? 11.932 3.688   9.586   0.48 19.32 ?  22  ASP   A HB2  1 
ATOM   611  H HB2  B ASP   A 1 22  ? 12.092 3.400   9.067   0.52 16.19 ?  22  ASP   A HB2  1 
ATOM   612  H HB3  A ASP   A 1 22  ? 12.763 3.441   10.917  0.48 19.32 ?  22  ASP   A HB3  1 
ATOM   613  H HB3  B ASP   A 1 22  ? 13.063 3.217   10.311  0.52 16.19 ?  22  ASP   A HB3  1 
ATOM   614  N N    A ILE   A 1 23  ? 15.316 1.076   9.202   0.48 12.68 ?  23  ILE   A N    1 
ATOM   615  N N    B ILE   A 1 23  ? 15.418 0.669   8.779   0.52 10.82 ?  23  ILE   A N    1 
ATOM   616  C CA   A ILE   A 1 23  ? 16.573 0.480   9.651   0.48 11.96 ?  23  ILE   A CA   1 
ATOM   617  C CA   B ILE   A 1 23  ? 16.661 0.100   9.301   0.52 10.70 ?  23  ILE   A CA   1 
ATOM   618  C C    A ILE   A 1 23  ? 17.364 1.445   10.522  0.48 11.97 ?  23  ILE   A C    1 
ATOM   619  C C    B ILE   A 1 23  ? 17.375 1.084   10.218  0.52 10.98 ?  23  ILE   A C    1 
ATOM   620  O O    A ILE   A 1 23  ? 18.099 1.020   11.423  0.48 12.59 ?  23  ILE   A O    1 
ATOM   621  O O    B ILE   A 1 23  ? 18.033 0.676   11.183  0.52 11.41 ?  23  ILE   A O    1 
ATOM   622  C CB   A ILE   A 1 23  ? 17.386 -0.031  8.443   0.48 11.81 ?  23  ILE   A CB   1 
ATOM   623  C CB   B ILE   A 1 23  ? 17.578 -0.412  8.164   0.52 10.92 ?  23  ILE   A CB   1 
ATOM   624  C CG1  A ILE   A 1 23  ? 18.540 -0.917  8.914   0.48 12.03 ?  23  ILE   A CG1  1 
ATOM   625  C CG1  B ILE   A 1 23  ? 18.624 -1.382  8.733   0.52 11.33 ?  23  ILE   A CG1  1 
ATOM   626  C CG2  A ILE   A 1 23  ? 17.876 1.133   7.580   0.48 12.18 ?  23  ILE   A CG2  1 
ATOM   627  C CG2  B ILE   A 1 23  ? 18.258 0.745   7.429   0.52 10.78 ?  23  ILE   A CG2  1 
ATOM   628  C CD1  A ILE   A 1 23  ? 19.199 -1.696  7.797   0.48 12.28 ?  23  ILE   A CD1  1 
ATOM   629  C CD1  B ILE   A 1 23  ? 19.561 -1.980  7.696   0.52 11.35 ?  23  ILE   A CD1  1 
ATOM   630  H H    A ILE   A 1 23  ? 15.226 1.112   8.351   0.48 15.19 ?  23  ILE   A H    1 
ATOM   631  H H    B ILE   A 1 23  ? 15.360 0.661   7.931   0.52 12.96 ?  23  ILE   A H    1 
ATOM   632  H HA   A ILE   A 1 23  ? 16.369 -0.291  10.199  0.48 14.32 ?  23  ILE   A HA   1 
ATOM   633  H HA   B ILE   A 1 23  ? 16.427 -0.678  9.832   0.52 12.81 ?  23  ILE   A HA   1 
ATOM   634  H HB   A ILE   A 1 23  ? 16.800 -0.575  7.898   0.48 14.14 ?  23  ILE   A HB   1 
ATOM   635  H HB   B ILE   A 1 23  ? 17.038 -0.903  7.523   0.52 13.08 ?  23  ILE   A HB   1 
ATOM   636  H HG12 A ILE   A 1 23  ? 19.219 -0.363  9.328   0.48 14.41 ?  23  ILE   A HG12 1 
ATOM   637  H HG12 B ILE   A 1 23  ? 19.170 -0.911  9.380   0.52 13.57 ?  23  ILE   A HG12 1 
ATOM   638  H HG13 A ILE   A 1 23  ? 18.200 -1.559  9.559   0.48 14.41 ?  23  ILE   A HG13 1 
ATOM   639  H HG13 B ILE   A 1 23  ? 18.165 -2.120  9.167   0.52 13.57 ?  23  ILE   A HG13 1 
ATOM   640  H HG21 A ILE   A 1 23  ? 18.251 0.782   6.756   0.48 14.59 ?  23  ILE   A HG21 1 
ATOM   641  H HG21 B ILE   A 1 23  ? 18.645 0.411   6.600   0.52 12.92 ?  23  ILE   A HG21 1 
ATOM   642  H HG22 A ILE   A 1 23  ? 17.122 1.712   7.376   0.48 14.59 ?  23  ILE   A HG22 1 
ATOM   643  H HG22 B ILE   A 1 23  ? 17.599 1.423   7.234   0.52 12.92 ?  23  ILE   A HG22 1 
ATOM   644  H HG23 A ILE   A 1 23  ? 18.551 1.630   8.065   0.48 14.59 ?  23  ILE   A HG23 1 
ATOM   645  H HG23 B ILE   A 1 23  ? 18.960 1.110   7.991   0.52 12.92 ?  23  ILE   A HG23 1 
ATOM   646  H HD11 A ILE   A 1 23  ? 19.887 -2.267  8.171   0.48 14.71 ?  23  ILE   A HD11 1 
ATOM   647  H HD11 B ILE   A 1 23  ? 20.111 -2.658  8.121   0.52 13.60 ?  23  ILE   A HD11 1 
ATOM   648  H HD12 A ILE   A 1 23  ? 18.527 -2.236  7.350   0.48 14.71 ?  23  ILE   A HD12 1 
ATOM   649  H HD12 B ILE   A 1 23  ? 19.033 -2.378  6.988   0.52 13.60 ?  23  ILE   A HD12 1 
ATOM   650  H HD13 A ILE   A 1 23  ? 19.592 -1.072  7.167   0.48 14.71 ?  23  ILE   A HD13 1 
ATOM   651  H HD13 B ILE   A 1 23  ? 20.123 -1.277  7.336   0.52 13.60 ?  23  ILE   A HD13 1 
ATOM   652  N N    A VAL   A 1 24  ? 17.226 2.749   10.282  0.48 12.53 ?  24  VAL   A N    1 
ATOM   653  N N    B VAL   A 1 24  ? 17.255 2.384   9.944   0.52 11.50 ?  24  VAL   A N    1 
ATOM   654  C CA   A VAL   A 1 24  ? 17.895 3.735   11.127  0.48 13.63 ?  24  VAL   A CA   1 
ATOM   655  C CA   B VAL   A 1 24  ? 17.903 3.384   10.786  0.52 12.71 ?  24  VAL   A CA   1 
ATOM   656  C C    A VAL   A 1 24  ? 17.369 3.656   12.552  0.48 14.16 ?  24  VAL   A C    1 
ATOM   657  C C    B VAL   A 1 24  ? 17.295 3.381   12.181  0.52 13.86 ?  24  VAL   A C    1 
ATOM   658  O O    A VAL   A 1 24  ? 18.139 3.586   13.519  0.48 14.59 ?  24  VAL   A O    1 
ATOM   659  O O    B VAL   A 1 24  ? 18.011 3.450   13.187  0.52 14.98 ?  24  VAL   A O    1 
ATOM   660  C CB   A VAL   A 1 24  ? 17.720 5.147   10.541  0.48 14.28 ?  24  VAL   A CB   1 
ATOM   661  C CB   B VAL   A 1 24  ? 17.829 4.770   10.120  0.52 13.36 ?  24  VAL   A CB   1 
ATOM   662  C CG1  A VAL   A 1 24  ? 18.199 6.200   11.536  0.48 14.65 ?  24  VAL   A CG1  1 
ATOM   663  C CG1  B VAL   A 1 24  ? 18.538 5.805   10.974  0.52 14.86 ?  24  VAL   A CG1  1 
ATOM   664  C CG2  A VAL   A 1 24  ? 18.462 5.265   9.223   0.48 14.67 ?  24  VAL   A CG2  1 
ATOM   665  C CG2  B VAL   A 1 24  ? 18.426 4.716   8.723   0.52 13.61 ?  24  VAL   A CG2  1 
ATOM   666  H H    A VAL   A 1 24  ? 16.753 3.086   9.645   0.48 15.01 ?  24  VAL   A H    1 
ATOM   667  H H    B VAL   A 1 24  ? 16.799 2.704   9.291   0.52 13.77 ?  24  VAL   A H    1 
ATOM   668  H HA   A VAL   A 1 24  ? 18.842 3.541   11.147  0.48 16.33 ?  24  VAL   A HA   1 
ATOM   669  H HA   B VAL   A 1 24  ? 18.836 3.151   10.878  0.52 15.23 ?  24  VAL   A HA   1 
ATOM   670  H HB   A VAL   A 1 24  ? 16.778 5.308   10.367  0.48 17.12 ?  24  VAL   A HB   1 
ATOM   671  H HB   B VAL   A 1 24  ? 16.899 5.033   10.038  0.52 16.01 ?  24  VAL   A HB   1 
ATOM   672  H HG11 A VAL   A 1 24  ? 18.350 7.033   11.063  0.48 17.56 ?  24  VAL   A HG11 1 
ATOM   673  H HG11 B VAL   A 1 24  ? 18.641 6.620   10.460  0.52 17.81 ?  24  VAL   A HG11 1 
ATOM   674  H HG12 A VAL   A 1 24  ? 17.521 6.325   12.217  0.48 17.56 ?  24  VAL   A HG12 1 
ATOM   675  H HG12 B VAL   A 1 24  ? 18.003 5.980   11.765  0.52 17.81 ?  24  VAL   A HG12 1 
ATOM   676  H HG13 A VAL   A 1 24  ? 19.027 5.896   11.939  0.48 17.56 ?  24  VAL   A HG13 1 
ATOM   677  H HG13 B VAL   A 1 24  ? 19.408 5.462   11.230  0.52 17.81 ?  24  VAL   A HG13 1 
ATOM   678  H HG21 A VAL   A 1 24  ? 18.240 6.113   8.808   0.48 17.58 ?  24  VAL   A HG21 1 
ATOM   679  H HG21 B VAL   A 1 24  ? 18.484 5.616   8.369   0.52 16.31 ?  24  VAL   A HG21 1 
ATOM   680  H HG22 A VAL   A 1 24  ? 19.417 5.223   9.393   0.48 17.58 ?  24  VAL   A HG22 1 
ATOM   681  H HG22 B VAL   A 1 24  ? 19.313 4.323   8.774   0.52 16.31 ?  24  VAL   A HG22 1 
ATOM   682  H HG23 A VAL   A 1 24  ? 18.198 4.535   8.641   0.48 17.58 ?  24  VAL   A HG23 1 
ATOM   683  H HG23 B VAL   A 1 24  ? 17.858 4.172   8.155   0.52 16.31 ?  24  VAL   A HG23 1 
ATOM   684  N N    A GLU   A 1 25  ? 16.044 3.695   12.704  0.48 14.41 ?  25  GLU   A N    1 
ATOM   685  N N    B GLU   A 1 25  ? 15.964 3.293   12.268  0.52 14.47 ?  25  GLU   A N    1 
ATOM   686  C CA   A GLU   A 1 25  ? 15.455 3.636   14.036  0.48 15.74 ?  25  GLU   A CA   1 
ATOM   687  C CA   B GLU   A 1 25  ? 15.309 3.242   13.572  0.52 15.63 ?  25  GLU   A CA   1 
ATOM   688  C C    A GLU   A 1 25  ? 15.686 2.277   14.680  0.48 14.70 ?  25  GLU   A C    1 
ATOM   689  C C    B GLU   A 1 25  ? 15.592 1.923   14.283  0.52 15.37 ?  25  GLU   A C    1 
ATOM   690  O O    A GLU   A 1 25  ? 15.909 2.191   15.894  0.48 15.06 ?  25  GLU   A O    1 
ATOM   691  O O    B GLU   A 1 25  ? 15.809 1.905   15.500  0.52 15.90 ?  25  GLU   A O    1 
ATOM   692  C CB   A GLU   A 1 25  ? 13.966 3.980   13.968  0.48 18.15 ?  25  GLU   A CB   1 
ATOM   693  C CB   B GLU   A 1 25  ? 13.806 3.484   13.422  0.52 17.61 ?  25  GLU   A CB   1 
ATOM   694  C CG   A GLU   A 1 25  ? 13.705 5.450   13.664  0.48 20.94 ?  25  GLU   A CG   1 
ATOM   695  C CG   B GLU   A 1 25  ? 13.463 4.880   12.921  0.52 20.77 ?  25  GLU   A CG   1 
ATOM   696  C CD   A GLU   A 1 25  ? 14.527 6.394   14.533  0.48 23.30 ?  25  GLU   A CD   1 
ATOM   697  C CD   B GLU   A 1 25  ? 14.042 5.967   13.799  0.52 23.73 ?  25  GLU   A CD   1 
ATOM   698  O OE1  A GLU   A 1 25  ? 14.616 6.158   15.757  0.48 23.99 ?  25  GLU   A OE1  1 
ATOM   699  O OE1  B GLU   A 1 25  ? 14.049 5.787   15.036  0.52 25.04 ?  25  GLU   A OE1  1 
ATOM   700  O OE2  A GLU   A 1 25  ? 15.100 7.359   13.985  0.48 24.47 -1 25  GLU   A OE2  1 
ATOM   701  O OE2  B GLU   A 1 25  ? 14.499 6.992   13.253  0.52 24.81 -1 25  GLU   A OE2  1 
ATOM   702  H H    A GLU   A 1 25  ? 15.475 3.769   12.060  0.48 17.26 ?  25  GLU   A H    1 
ATOM   703  H H    B GLU   A 1 25  ? 15.425 3.260   11.596  0.52 17.35 ?  25  GLU   A H    1 
ATOM   704  H HA   A GLU   A 1 25  ? 15.895 4.289   14.598  0.48 18.87 ?  25  GLU   A HA   1 
ATOM   705  H HA   B GLU   A 1 25  ? 15.670 3.948   14.126  0.52 18.73 ?  25  GLU   A HA   1 
ATOM   706  H HB2  A GLU   A 1 25  ? 13.547 3.455   13.262  0.48 21.75 ?  25  GLU   A HB2  1 
ATOM   707  H HB2  B GLU   A 1 25  ? 13.444 2.846   12.787  0.52 21.10 ?  25  GLU   A HB2  1 
ATOM   708  H HB3  A GLU   A 1 25  ? 13.548 3.774   14.819  0.48 21.75 ?  25  GLU   A HB3  1 
ATOM   709  H HB3  B GLU   A 1 25  ? 13.380 3.366   14.286  0.52 21.10 ?  25  GLU   A HB3  1 
ATOM   710  H HG2  A GLU   A 1 25  ? 13.939 5.625   12.742  0.48 25.11 ?  25  GLU   A HG2  1 
ATOM   711  H HG2  B GLU   A 1 25  ? 13.826 4.997   12.030  0.52 24.91 ?  25  GLU   A HG2  1 
ATOM   712  H HG3  A GLU   A 1 25  ? 12.768 5.641   13.818  0.48 25.11 ?  25  GLU   A HG3  1 
ATOM   713  H HG3  B GLU   A 1 25  ? 12.500 4.988   12.907  0.52 24.91 ?  25  GLU   A HG3  1 
ATOM   714  N N    A GLU   A 1 26  ? 15.649 1.205   13.885  0.48 14.03 ?  26  GLU   A N    1 
ATOM   715  N N    B GLU   A 1 26  ? 15.601 0.810   13.545  0.52 14.93 ?  26  GLU   A N    1 
ATOM   716  C CA   A GLU   A 1 26  ? 15.945 -0.120  14.419  0.48 14.35 ?  26  GLU   A CA   1 
ATOM   717  C CA   B GLU   A 1 26  ? 15.968 -0.467  14.152  0.52 15.32 ?  26  GLU   A CA   1 
ATOM   718  C C    A GLU   A 1 26  ? 17.362 -0.178  14.977  0.48 13.78 ?  26  GLU   A C    1 
ATOM   719  C C    B GLU   A 1 26  ? 17.381 -0.414  14.715  0.52 14.11 ?  26  GLU   A C    1 
ATOM   720  O O    A GLU   A 1 26  ? 17.581 -0.629  16.108  0.48 13.92 ?  26  GLU   A O    1 
ATOM   721  O O    B GLU   A 1 26  ? 17.650 -0.947  15.798  0.52 14.17 ?  26  GLU   A O    1 
ATOM   722  C CB   A GLU   A 1 26  ? 15.768 -1.179  13.329  0.48 15.66 ?  26  GLU   A CB   1 
ATOM   723  C CB   B GLU   A 1 26  ? 15.862 -1.595  13.123  0.52 16.95 ?  26  GLU   A CB   1 
ATOM   724  C CG   A GLU   A 1 26  ? 14.369 -1.732  13.185  0.48 18.84 ?  26  GLU   A CG   1 
ATOM   725  C CG   B GLU   A 1 26  ? 14.451 -2.039  12.816  0.52 18.37 ?  26  GLU   A CG   1 
ATOM   726  C CD   A GLU   A 1 26  ? 13.957 -2.579  14.378  0.48 20.86 ?  26  GLU   A CD   1 
ATOM   727  C CD   B GLU   A 1 26  ? 13.748 -2.620  14.024  0.52 19.24 ?  26  GLU   A CD   1 
ATOM   728  O OE1  A GLU   A 1 26  ? 14.372 -3.759  14.466  0.48 21.87 ?  26  GLU   A OE1  1 
ATOM   729  O OE1  B GLU   A 1 26  ? 14.271 -3.591  14.616  0.52 20.02 ?  26  GLU   A OE1  1 
ATOM   730  O OE2  A GLU   A 1 26  ? 13.228 -2.055  15.237  0.48 21.59 -1 26  GLU   A OE2  1 
ATOM   731  O OE2  B GLU   A 1 26  ? 12.678 -2.092  14.387  0.52 18.42 -1 26  GLU   A OE2  1 
ATOM   732  H H    A GLU   A 1 26  ? 15.467 1.229   13.045  0.48 16.81 ?  26  GLU   A H    1 
ATOM   733  H H    B GLU   A 1 26  ? 15.404 0.766   12.710  0.52 17.89 ?  26  GLU   A H    1 
ATOM   734  H HA   A GLU   A 1 26  ? 15.329 -0.312  15.138  0.48 17.20 ?  26  GLU   A HA   1 
ATOM   735  H HA   B GLU   A 1 26  ? 15.363 -0.665  14.881  0.52 18.37 ?  26  GLU   A HA   1 
ATOM   736  H HB2  A GLU   A 1 26  ? 16.019 -0.787  12.476  0.48 18.77 ?  26  GLU   A HB2  1 
ATOM   737  H HB2  B GLU   A 1 26  ? 16.262 -1.297  12.290  0.52 20.32 ?  26  GLU   A HB2  1 
ATOM   738  H HB3  A GLU   A 1 26  ? 16.357 -1.921  13.529  0.48 18.77 ?  26  GLU   A HB3  1 
ATOM   739  H HB3  B GLU   A 1 26  ? 16.347 -2.369  13.454  0.52 20.32 ?  26  GLU   A HB3  1 
ATOM   740  H HG2  A GLU   A 1 26  ? 13.753 -0.987  13.088  0.48 22.58 ?  26  GLU   A HG2  1 
ATOM   741  H HG2  B GLU   A 1 26  ? 13.940 -1.274  12.513  0.52 22.02 ?  26  GLU   A HG2  1 
ATOM   742  H HG3  A GLU   A 1 26  ? 14.333 -2.293  12.395  0.48 22.58 ?  26  GLU   A HG3  1 
ATOM   743  H HG3  B GLU   A 1 26  ? 14.474 -2.720  12.126  0.52 22.02 ?  26  GLU   A HG3  1 
ATOM   744  N N    A ALA   A 1 27  ? 18.343 0.274   14.191  0.48 13.74 ?  27  ALA   A N    1 
ATOM   745  N N    B ALA   A 1 27  ? 18.305 0.213   13.986  0.52 12.78 ?  27  ALA   A N    1 
ATOM   746  C CA   A ALA   A 1 27  ? 19.734 0.187   14.627  0.48 14.30 ?  27  ALA   A CA   1 
ATOM   747  C CA   B ALA   A 1 27  ? 19.681 0.297   14.465  0.52 12.70 ?  27  ALA   A CA   1 
ATOM   748  C C    A ALA   A 1 27  ? 19.963 0.970   15.914  0.48 15.50 ?  27  ALA   A C    1 
ATOM   749  C C    B ALA   A 1 27  ? 19.779 1.165   15.715  0.52 13.45 ?  27  ALA   A C    1 
ATOM   750  O O    A ALA   A 1 27  ? 20.655 0.496   16.823  0.48 15.77 ?  27  ALA   A O    1 
ATOM   751  O O    B ALA   A 1 27  ? 20.431 0.787   16.695  0.52 13.85 ?  27  ALA   A O    1 
ATOM   752  C CB   A ALA   A 1 27  ? 20.672 0.682   13.520  0.48 14.21 ?  27  ALA   A CB   1 
ATOM   753  C CB   B ALA   A 1 27  ? 20.592 0.829   13.356  0.52 12.33 ?  27  ALA   A CB   1 
ATOM   754  H H    A ALA   A 1 27  ? 18.232 0.636   13.418  0.48 16.46 ?  27  ALA   A H    1 
ATOM   755  H H    B ALA   A 1 27  ? 18.160 0.586   13.224  0.52 15.31 ?  27  ALA   A H    1 
ATOM   756  H HA   A ALA   A 1 27  ? 19.949 -0.739  14.799  0.48 17.14 ?  27  ALA   A HA   1 
ATOM   757  H HA   B ALA   A 1 27  ? 19.984 -0.590  14.697  0.52 15.22 ?  27  ALA   A HA   1 
ATOM   758  H HB1  A ALA   A 1 27  ? 21.592 0.614   13.827  0.48 17.03 ?  27  ALA   A HB1  1 
ATOM   759  H HB1  B ALA   A 1 27  ? 21.500 0.877   13.692  0.52 14.77 ?  27  ALA   A HB1  1 
ATOM   760  H HB2  A ALA   A 1 27  ? 20.550 0.130   12.730  0.48 17.03 ?  27  ALA   A HB2  1 
ATOM   761  H HB2  B ALA   A 1 27  ? 20.552 0.225   12.597  0.52 14.77 ?  27  ALA   A HB2  1 
ATOM   762  H HB3  A ALA   A 1 27  ? 20.463 1.606   13.311  0.48 17.03 ?  27  ALA   A HB3  1 
ATOM   763  H HB3  B ALA   A 1 27  ? 20.289 1.712   13.091  0.52 14.77 ?  27  ALA   A HB3  1 
ATOM   764  N N    A LYS   A 1 28  ? 19.389 2.171   16.015  0.48 17.47 ?  28  LYS   A N    1 
ATOM   765  N N    B LYS   A 1 28  ? 19.128 2.332   15.707  0.52 14.95 ?  28  LYS   A N    1 
ATOM   766  C CA   A LYS   A 1 28  ? 19.568 2.967   17.224  0.48 20.00 ?  28  LYS   A CA   1 
ATOM   767  C CA   B LYS   A 1 28  ? 19.215 3.227   16.858  0.52 17.56 ?  28  LYS   A CA   1 
ATOM   768  C C    A LYS   A 1 28  ? 19.007 2.257   18.450  0.48 21.15 ?  28  LYS   A C    1 
ATOM   769  C C    B LYS   A 1 28  ? 18.684 2.569   18.124  0.52 18.48 ?  28  LYS   A C    1 
ATOM   770  O O    A LYS   A 1 28  ? 19.565 2.382   19.547  0.48 21.88 ?  28  LYS   A O    1 
ATOM   771  O O    B LYS   A 1 28  ? 19.230 2.775   19.214  0.52 19.25 ?  28  LYS   A O    1 
ATOM   772  C CB   A LYS   A 1 28  ? 18.942 4.354   17.048  0.48 21.69 ?  28  LYS   A CB   1 
ATOM   773  C CB   B LYS   A 1 28  ? 18.460 4.526   16.579  0.52 19.97 ?  28  LYS   A CB   1 
ATOM   774  C CG   A LYS   A 1 28  ? 19.758 5.278   16.152  0.48 23.47 ?  28  LYS   A CG   1 
ATOM   775  C CG   B LYS   A 1 28  ? 19.195 5.466   15.650  0.52 22.70 ?  28  LYS   A CG   1 
ATOM   776  C CD   A LYS   A 1 28  ? 19.281 6.721   16.219  0.48 25.35 ?  28  LYS   A CD   1 
ATOM   777  C CD   B LYS   A 1 28  ? 18.586 6.857   15.670  0.52 25.53 ?  28  LYS   A CD   1 
ATOM   778  C CE   A LYS   A 1 28  ? 17.964 6.911   15.490  0.48 26.66 ?  28  LYS   A CE   1 
ATOM   779  C CE   B LYS   A 1 28  ? 17.667 7.080   14.484  0.52 27.58 ?  28  LYS   A CE   1 
ATOM   780  N NZ   A LYS   A 1 28  ? 17.591 8.351   15.408  0.48 27.48 ?  28  LYS   A NZ   1 
ATOM   781  N NZ   B LYS   A 1 28  ? 16.931 8.371   14.599  0.52 28.53 ?  28  LYS   A NZ   1 
ATOM   782  H H    A LYS   A 1 28  ? 18.905 2.536   15.411  0.48 20.94 ?  28  LYS   A H    1 
ATOM   783  H H    B LYS   A 1 28  ? 18.639 2.625   15.063  0.52 17.91 ?  28  LYS   A H    1 
ATOM   784  H HA   A LYS   A 1 28  ? 20.515 3.095   17.380  0.48 23.98 ?  28  LYS   A HA   1 
ATOM   785  H HA   B LYS   A 1 28  ? 20.141 3.454   17.014  0.52 21.04 ?  28  LYS   A HA   1 
ATOM   786  H HB2  A LYS   A 1 28  ? 18.065 4.259   16.648  0.48 26.01 ?  28  LYS   A HB2  1 
ATOM   787  H HB2  B LYS   A 1 28  ? 17.605 4.317   16.170  0.52 23.94 ?  28  LYS   A HB2  1 
ATOM   788  H HB3  A LYS   A 1 28  ? 18.865 4.782   17.915  0.48 26.01 ?  28  LYS   A HB3  1 
ATOM   789  H HB3  B LYS   A 1 28  ? 18.316 4.993   17.419  0.52 23.94 ?  28  LYS   A HB3  1 
ATOM   790  H HG2  A LYS   A 1 28  ? 20.686 5.256   16.432  0.48 28.14 ?  28  LYS   A HG2  1 
ATOM   791  H HG2  B LYS   A 1 28  ? 20.119 5.535   15.930  0.52 27.21 ?  28  LYS   A HG2  1 
ATOM   792  H HG3  A LYS   A 1 28  ? 19.680 4.980   15.232  0.48 28.14 ?  28  LYS   A HG3  1 
ATOM   793  H HG3  B LYS   A 1 28  ? 19.140 5.126   14.743  0.52 27.21 ?  28  LYS   A HG3  1 
ATOM   794  H HD2  A LYS   A 1 28  ? 19.153 6.974   17.147  0.48 30.39 ?  28  LYS   A HD2  1 
ATOM   795  H HD2  B LYS   A 1 28  ? 18.066 6.972   16.483  0.52 30.61 ?  28  LYS   A HD2  1 
ATOM   796  H HD3  A LYS   A 1 28  ? 19.943 7.298   15.804  0.48 30.39 ?  28  LYS   A HD3  1 
ATOM   797  H HD3  B LYS   A 1 28  ? 19.297 7.516   15.634  0.52 30.61 ?  28  LYS   A HD3  1 
ATOM   798  H HE2  A LYS   A 1 28  ? 18.045 6.566   14.587  0.48 31.97 ?  28  LYS   A HE2  1 
ATOM   799  H HE2  B LYS   A 1 28  ? 18.199 7.106   13.673  0.52 33.07 ?  28  LYS   A HE2  1 
ATOM   800  H HE3  A LYS   A 1 28  ? 17.263 6.442   15.968  0.48 31.97 ?  28  LYS   A HE3  1 
ATOM   801  H HE3  B LYS   A 1 28  ? 17.019 6.360   14.439  0.52 33.07 ?  28  LYS   A HE3  1 
ATOM   802  H HZ1  A LYS   A 1 28  ? 16.817 8.442   14.978  0.48 32.96 ?  28  LYS   A HZ1  1 
ATOM   803  H HZ1  B LYS   A 1 28  ? 16.400 8.482   13.894  0.52 34.21 ?  28  LYS   A HZ1  1 
ATOM   804  H HZ2  A LYS   A 1 28  ? 17.508 8.692   16.226  0.48 32.96 ?  28  LYS   A HZ2  1 
ATOM   805  H HZ2  B LYS   A 1 28  ? 16.435 8.373   15.338  0.52 34.21 ?  28  LYS   A HZ2  1 
ATOM   806  H HZ3  A LYS   A 1 28  ? 18.220 8.804   14.970  0.48 32.96 ?  28  LYS   A HZ3  1 
ATOM   807  H HZ3  B LYS   A 1 28  ? 17.508 9.048   14.636  0.52 34.21 ?  28  LYS   A HZ3  1 
ATOM   808  N N    A LYS   A 1 29  ? 17.926 1.493   18.285  0.48 21.96 ?  29  LYS   A N    1 
ATOM   809  N N    B LYS   A 1 29  ? 17.609 1.789   18.004  0.52 18.98 ?  29  LYS   A N    1 
ATOM   810  C CA   A LYS   A 1 29  ? 17.318 0.796   19.414  0.48 23.47 ?  29  LYS   A CA   1 
ATOM   811  C CA   B LYS   A 1 29  ? 17.011 1.147   19.169  0.52 20.39 ?  29  LYS   A CA   1 
ATOM   812  C C    A LYS   A 1 29  ? 18.118 -0.445  19.801  0.48 22.41 ?  29  LYS   A C    1 
ATOM   813  C C    B LYS   A 1 29  ? 17.817 -0.068  19.609  0.52 19.36 ?  29  LYS   A C    1 
ATOM   814  O O    A LYS   A 1 29  ? 18.412 -0.663  20.982  0.48 23.24 ?  29  LYS   A O    1 
ATOM   815  O O    B LYS   A 1 29  ? 18.114 -0.226  20.799  0.52 20.31 ?  29  LYS   A O    1 
ATOM   816  C CB   A LYS   A 1 29  ? 15.880 0.406   19.063  0.48 26.02 ?  29  LYS   A CB   1 
ATOM   817  C CB   B LYS   A 1 29  ? 15.573 0.732   18.848  0.52 23.00 ?  29  LYS   A CB   1 
ATOM   818  C CG   A LYS   A 1 29  ? 15.133 -0.314  20.176  0.48 28.76 ?  29  LYS   A CG   1 
ATOM   819  C CG   B LYS   A 1 29  ? 14.863 -0.005  19.976  0.52 26.17 ?  29  LYS   A CG   1 
ATOM   820  C CD   A LYS   A 1 29  ? 14.786 0.629   21.314  0.48 31.36 ?  29  LYS   A CD   1 
ATOM   821  C CD   B LYS   A 1 29  ? 14.571 0.920   21.143  0.52 29.19 ?  29  LYS   A CD   1 
ATOM   822  C CE   A LYS   A 1 29  ? 13.900 -0.051  22.345  0.48 33.12 ?  29  LYS   A CE   1 
ATOM   823  C CE   B LYS   A 1 29  ? 13.757 0.216   22.216  0.52 31.36 ?  29  LYS   A CE   1 
ATOM   824  N NZ   A LYS   A 1 29  ? 13.440 0.899   23.393  0.48 34.14 ?  29  LYS   A NZ   1 
ATOM   825  N NZ   B LYS   A 1 29  ? 13.427 1.133   23.339  0.52 32.61 ?  29  LYS   A NZ   1 
ATOM   826  H H    A LYS   A 1 29  ? 17.533 1.363   17.531  0.48 26.32 ?  29  LYS   A H    1 
ATOM   827  H H    B LYS   A 1 29  ? 17.204 1.622   17.263  0.52 22.75 ?  29  LYS   A H    1 
ATOM   828  H HA   A LYS   A 1 29  ? 17.288 1.395   20.177  0.48 28.14 ?  29  LYS   A HA   1 
ATOM   829  H HA   B LYS   A 1 29  ? 16.987 1.775   19.907  0.52 24.45 ?  29  LYS   A HA   1 
ATOM   830  H HB2  A LYS   A 1 29  ? 15.380 1.210   18.850  0.48 31.20 ?  29  LYS   A HB2  1 
ATOM   831  H HB2  B LYS   A 1 29  ? 15.056 1.528   18.651  0.52 27.58 ?  29  LYS   A HB2  1 
ATOM   832  H HB3  A LYS   A 1 29  ? 15.897 -0.182  18.293  0.48 31.20 ?  29  LYS   A HB3  1 
ATOM   833  H HB3  B LYS   A 1 29  ? 15.582 0.147   18.076  0.52 27.58 ?  29  LYS   A HB3  1 
ATOM   834  H HG2  A LYS   A 1 29  ? 14.307 -0.675  19.821  0.48 34.49 ?  29  LYS   A HG2  1 
ATOM   835  H HG2  B LYS   A 1 29  ? 14.020 -0.350  19.646  0.52 31.38 ?  29  LYS   A HG2  1 
ATOM   836  H HG3  A LYS   A 1 29  ? 15.683 -1.031  20.531  0.48 34.49 ?  29  LYS   A HG3  1 
ATOM   837  H HG3  B LYS   A 1 29  ? 15.417 -0.737  20.296  0.52 31.38 ?  29  LYS   A HG3  1 
ATOM   838  H HD2  A LYS   A 1 29  ? 15.602 0.916   21.755  0.48 37.61 ?  29  LYS   A HD2  1 
ATOM   839  H HD2  B LYS   A 1 29  ? 15.407 1.213   21.538  0.52 35.01 ?  29  LYS   A HD2  1 
ATOM   840  H HD3  A LYS   A 1 29  ? 14.309 1.396   20.960  0.48 37.61 ?  29  LYS   A HD3  1 
ATOM   841  H HD3  B LYS   A 1 29  ? 14.062 1.683   20.825  0.52 35.01 ?  29  LYS   A HD3  1 
ATOM   842  H HE2  A LYS   A 1 29  ? 13.118 -0.416  21.902  0.48 39.72 ?  29  LYS   A HE2  1 
ATOM   843  H HE2  B LYS   A 1 29  ? 12.926 -0.104  21.829  0.52 37.61 ?  29  LYS   A HE2  1 
ATOM   844  H HE3  A LYS   A 1 29  ? 14.401 -0.761  22.778  0.48 39.72 ?  29  LYS   A HE3  1 
ATOM   845  H HE3  B LYS   A 1 29  ? 14.270 -0.528  22.570  0.52 37.61 ?  29  LYS   A HE3  1 
ATOM   846  H HZ1  A LYS   A 1 29  ? 12.924 0.476   23.982  0.48 40.95 ?  29  LYS   A HZ1  1 
ATOM   847  H HZ1  B LYS   A 1 29  ? 12.951 0.701   23.954  0.52 39.11 ?  29  LYS   A HZ1  1 
ATOM   848  H HZ2  A LYS   A 1 29  ? 14.141 1.245   23.818  0.48 40.95 ?  29  LYS   A HZ2  1 
ATOM   849  H HZ2  B LYS   A 1 29  ? 14.175 1.438   23.712  0.52 39.11 ?  29  LYS   A HZ2  1 
ATOM   850  H HZ3  A LYS   A 1 29  ? 12.973 1.559   23.021  0.48 40.95 ?  29  LYS   A HZ3  1 
ATOM   851  H HZ3  B LYS   A 1 29  ? 12.952 1.823   23.037  0.52 39.11 ?  29  LYS   A HZ3  1 
ATOM   852  N N    A VAL   A 1 30  ? 18.465 -1.275  18.818  0.48 20.90 ?  30  VAL   A N    1 
ATOM   853  N N    B VAL   A 1 30  ? 18.168 -0.939  18.662  0.52 18.25 ?  30  VAL   A N    1 
ATOM   854  C CA   A VAL   A 1 30  ? 19.111 -2.552  19.103  0.48 19.66 ?  30  VAL   A CA   1 
ATOM   855  C CA   B VAL   A 1 30  ? 18.798 -2.208  19.012  0.52 17.56 ?  30  VAL   A CA   1 
ATOM   856  C C    A VAL   A 1 30  ? 20.613 -2.390  19.316  0.48 18.05 ?  30  VAL   A C    1 
ATOM   857  C C    B VAL   A 1 30  ? 20.295 -2.045  19.257  0.52 16.92 ?  30  VAL   A C    1 
ATOM   858  O O    A VAL   A 1 30  ? 21.211 -3.117  20.118  0.48 18.85 ?  30  VAL   A O    1 
ATOM   859  O O    B VAL   A 1 30  ? 20.863 -2.725  20.119  0.52 17.43 ?  30  VAL   A O    1 
ATOM   860  C CB   A VAL   A 1 30  ? 18.809 -3.548  17.969  0.48 20.47 ?  30  VAL   A CB   1 
ATOM   861  C CB   B VAL   A 1 30  ? 18.510 -3.253  17.917  0.52 18.20 ?  30  VAL   A CB   1 
ATOM   862  C CG1  A VAL   A 1 30  ? 19.592 -4.840  18.162  0.48 20.94 ?  30  VAL   A CG1  1 
ATOM   863  C CG1  B VAL   A 1 30  ? 19.257 -4.551  18.197  0.52 18.76 ?  30  VAL   A CG1  1 
ATOM   864  C CG2  A VAL   A 1 30  ? 17.316 -3.827  17.886  0.48 20.78 ?  30  VAL   A CG2  1 
ATOM   865  C CG2  B VAL   A 1 30  ? 17.012 -3.507  17.799  0.52 18.50 ?  30  VAL   A CG2  1 
ATOM   866  H H    A VAL   A 1 30  ? 18.331 -1.124  17.986  0.48 25.05 ?  30  VAL   A H    1 
ATOM   867  H H    B VAL   A 1 30  ? 18.045 -0.823  17.818  0.52 21.88 ?  30  VAL   A H    1 
ATOM   868  H HA   A VAL   A 1 30  ? 18.729 -2.914  19.918  0.48 23.56 ?  30  VAL   A HA   1 
ATOM   869  H HA   B VAL   A 1 30  ? 18.395 -2.534  19.830  0.52 21.04 ?  30  VAL   A HA   1 
ATOM   870  H HB   A VAL   A 1 30  ? 19.089 -3.156  17.126  0.48 24.54 ?  30  VAL   A HB   1 
ATOM   871  H HB   B VAL   A 1 30  ? 18.822 -2.913  17.063  0.52 21.82 ?  30  VAL   A HB   1 
ATOM   872  H HG11 A VAL   A 1 30  ? 19.220 -5.522  17.579  0.48 25.10 ?  30  VAL   A HG11 1 
ATOM   873  H HG11 B VAL   A 1 30  ? 18.889 -5.255  17.638  0.52 22.48 ?  30  VAL   A HG11 1 
ATOM   874  H HG12 A VAL   A 1 30  ? 20.523 -4.688  17.937  0.48 25.10 ?  30  VAL   A HG12 1 
ATOM   875  H HG12 B VAL   A 1 30  ? 20.198 -4.430  17.994  0.52 22.48 ?  30  VAL   A HG12 1 
ATOM   876  H HG13 A VAL   A 1 30  ? 19.514 -5.121  19.087  0.48 25.10 ?  30  VAL   A HG13 1 
ATOM   877  H HG13 B VAL   A 1 30  ? 19.145 -4.783  19.132  0.52 22.48 ?  30  VAL   A HG13 1 
ATOM   878  H HG21 A VAL   A 1 30  ? 17.158 -4.481  17.188  0.48 24.91 ?  30  VAL   A HG21 1 
ATOM   879  H HG21 B VAL   A 1 30  ? 16.859 -4.198  17.134  0.52 22.18 ?  30  VAL   A HG21 1 
ATOM   880  H HG22 A VAL   A 1 30  ? 17.014 -4.173  18.740  0.48 24.91 ?  30  VAL   A HG22 1 
ATOM   881  H HG22 B VAL   A 1 30  ? 16.674 -3.798  18.661  0.52 22.18 ?  30  VAL   A HG22 1 
ATOM   882  H HG23 A VAL   A 1 30  ? 16.853 -3.001  17.679  0.48 24.91 ?  30  VAL   A HG23 1 
ATOM   883  H HG23 B VAL   A 1 30  ? 16.573 -2.686  17.530  0.52 22.18 ?  30  VAL   A HG23 1 
ATOM   884  N N    A LYS   A 1 31  ? 21.243 -1.454  18.615  0.48 16.54 ?  31  LYS   A N    1 
ATOM   885  N N    B LYS   A 1 31  ? 20.947 -1.144  18.530  0.52 17.10 ?  31  LYS   A N    1 
ATOM   886  C CA   A LYS   A 1 31  ? 22.696 -1.342  18.566  0.48 16.93 ?  31  LYS   A CA   1 
ATOM   887  C CA   B LYS   A 1 31  ? 22.401 -1.042  18.505  0.52 17.82 ?  31  LYS   A CA   1 
ATOM   888  C C    A LYS   A 1 31  ? 23.314 -2.701  18.226  0.48 14.94 ?  31  LYS   A C    1 
ATOM   889  C C    B LYS   A 1 31  ? 23.026 -2.418  18.261  0.52 16.24 ?  31  LYS   A C    1 
ATOM   890  O O    A LYS   A 1 31  ? 24.088 -3.253  19.013  0.48 15.31 ?  31  LYS   A O    1 
ATOM   891  O O    B LYS   A 1 31  ? 23.765 -2.932  19.107  0.52 17.00 ?  31  LYS   A O    1 
ATOM   892  C CB   A LYS   A 1 31  ? 23.273 -0.787  19.861  0.48 20.71 ?  31  LYS   A CB   1 
ATOM   893  C CB   B LYS   A 1 31  ? 22.951 -0.409  19.775  0.52 21.04 ?  31  LYS   A CB   1 
ATOM   894  C CG   A LYS   A 1 31  ? 22.583 0.473   20.362  0.48 24.64 ?  31  LYS   A CG   1 
ATOM   895  C CG   B LYS   A 1 31  ? 22.276 0.893   20.157  0.52 24.96 ?  31  LYS   A CG   1 
ATOM   896  C CD   A LYS   A 1 31  ? 23.588 1.519   20.824  0.48 27.72 ?  31  LYS   A CD   1 
ATOM   897  C CD   B LYS   A 1 31  ? 23.289 1.902   20.663  0.52 28.06 ?  31  LYS   A CD   1 
ATOM   898  C CE   A LYS   A 1 31  ? 22.944 2.548   21.744  0.48 29.77 ?  31  LYS   A CE   1 
ATOM   899  C CE   B LYS   A 1 31  ? 22.627 2.980   21.499  0.52 30.36 ?  31  LYS   A CE   1 
ATOM   900  N NZ   A LYS   A 1 31  ? 21.762 3.215   21.130  0.48 30.79 ?  31  LYS   A NZ   1 
ATOM   901  N NZ   B LYS   A 1 31  ? 21.384 3.503   20.873  0.52 31.79 ?  31  LYS   A NZ   1 
ATOM   902  H H    A LYS   A 1 31  ? 20.838 -0.861  18.147  0.48 19.83 ?  31  LYS   A H    1 
ATOM   903  H H    B LYS   A 1 31  ? 20.550 -0.558  18.039  0.52 20.50 ?  31  LYS   A H    1 
ATOM   904  H HA   A LYS   A 1 31  ? 22.926 -0.726  17.859  0.48 20.29 ?  31  LYS   A HA   1 
ATOM   905  H HA   B LYS   A 1 31  ? 22.645 -0.468  17.767  0.52 21.36 ?  31  LYS   A HA   1 
ATOM   906  H HB2  A LYS   A 1 31  ? 23.198 -1.463  20.550  0.48 24.83 ?  31  LYS   A HB2  1 
ATOM   907  H HB2  B LYS   A 1 31  ? 22.838 -1.026  20.511  0.52 25.22 ?  31  LYS   A HB2  1 
ATOM   908  H HB3  A LYS   A 1 31  ? 24.210 -0.572  19.714  0.48 24.83 ?  31  LYS   A HB3  1 
ATOM   909  H HB3  B LYS   A 1 31  ? 23.895 -0.221  19.642  0.52 25.22 ?  31  LYS   A HB3  1 
ATOM   910  H HG2  A LYS   A 1 31  ? 22.055 0.856   19.645  0.48 29.55 ?  31  LYS   A HG2  1 
ATOM   911  H HG2  B LYS   A 1 31  ? 21.833 1.269   19.379  0.52 29.93 ?  31  LYS   A HG2  1 
ATOM   912  H HG3  A LYS   A 1 31  ? 22.014 0.247   21.115  0.48 29.55 ?  31  LYS   A HG3  1 
ATOM   913  H HG3  B LYS   A 1 31  ? 21.632 0.726   20.864  0.52 29.93 ?  31  LYS   A HG3  1 
ATOM   914  H HD2  A LYS   A 1 31  ? 24.305 1.084   21.312  0.48 33.24 ?  31  LYS   A HD2  1 
ATOM   915  H HD2  B LYS   A 1 31  ? 23.946 1.447   21.214  0.52 33.64 ?  31  LYS   A HD2  1 
ATOM   916  H HD3  A LYS   A 1 31  ? 23.944 1.985   20.050  0.48 33.24 ?  31  LYS   A HD3  1 
ATOM   917  H HD3  B LYS   A 1 31  ? 23.723 2.327   19.906  0.52 33.64 ?  31  LYS   A HD3  1 
ATOM   918  H HE2  A LYS   A 1 31  ? 22.649 2.105   22.555  0.48 35.70 ?  31  LYS   A HE2  1 
ATOM   919  H HE2  B LYS   A 1 31  ? 22.403 2.612   22.366  0.52 36.41 ?  31  LYS   A HE2  1 
ATOM   920  H HE3  A LYS   A 1 31  ? 23.596 3.233   21.959  0.48 35.70 ?  31  LYS   A HE3  1 
ATOM   921  H HE3  B LYS   A 1 31  ? 23.245 3.719   21.604  0.52 36.41 ?  31  LYS   A HE3  1 
ATOM   922  H HZ1  A LYS   A 1 31  ? 21.425 3.816   21.695  0.48 36.92 ?  31  LYS   A HZ1  1 
ATOM   923  H HZ1  B LYS   A 1 31  ? 21.073 4.190   21.345  0.52 38.13 ?  31  LYS   A HZ1  1 
ATOM   924  H HZ2  A LYS   A 1 31  ? 22.001 3.628   20.379  0.48 36.92 ?  31  LYS   A HZ2  1 
ATOM   925  H HZ2  B LYS   A 1 31  ? 21.554 3.774   20.043  0.52 38.13 ?  31  LYS   A HZ2  1 
ATOM   926  H HZ3  A LYS   A 1 31  ? 21.134 2.613   20.943  0.48 36.92 ?  31  LYS   A HZ3  1 
ATOM   927  H HZ3  B LYS   A 1 31  ? 20.763 2.865   20.847  0.52 38.13 ?  31  LYS   A HZ3  1 
ATOM   928  N N    A PRO   A 1 32  ? 22.989 -3.260  17.064  0.48 13.83 ?  32  PRO   A N    1 
ATOM   929  N N    B PRO   A 1 32  ? 22.752 -3.030  17.113  0.52 14.54 ?  32  PRO   A N    1 
ATOM   930  C CA   A PRO   A 1 32  ? 23.468 -4.602  16.728  0.48 13.87 ?  32  PRO   A CA   1 
ATOM   931  C CA   B PRO   A 1 32  ? 23.242 -4.385  16.856  0.52 14.21 ?  32  PRO   A CA   1 
ATOM   932  C C    A PRO   A 1 32  ? 24.970 -4.627  16.515  0.48 13.67 ?  32  PRO   A C    1 
ATOM   933  C C    B PRO   A 1 32  ? 24.750 -4.398  16.668  0.52 14.09 ?  32  PRO   A C    1 
ATOM   934  O O    A PRO   A 1 32  ? 25.611 -3.608  16.242  0.48 13.07 ?  32  PRO   A O    1 
ATOM   935  O O    B PRO   A 1 32  ? 25.414 -3.365  16.561  0.52 14.44 ?  32  PRO   A O    1 
ATOM   936  C CB   A PRO   A 1 32  ? 22.741 -4.910  15.416  0.48 14.28 ?  32  PRO   A CB   1 
ATOM   937  C CB   B PRO   A 1 32  ? 22.533 -4.757  15.553  0.52 14.52 ?  32  PRO   A CB   1 
ATOM   938  C CG   A PRO   A 1 32  ? 22.561 -3.566  14.787  0.48 13.84 ?  32  PRO   A CG   1 
ATOM   939  C CG   B PRO   A 1 32  ? 22.386 -3.447  14.846  0.52 14.28 ?  32  PRO   A CG   1 
ATOM   940  C CD   A PRO   A 1 32  ? 22.268 -2.642  15.939  0.48 13.34 ?  32  PRO   A CD   1 
ATOM   941  C CD   B PRO   A 1 32  ? 22.056 -2.470  15.941  0.52 14.11 ?  32  PRO   A CD   1 
ATOM   942  H HA   A PRO   A 1 32  ? 23.211 -5.245  17.413  0.48 16.62 ?  32  PRO   A HA   1 
ATOM   943  H HA   B PRO   A 1 32  ? 22.981 -4.994  17.566  0.52 17.02 ?  32  PRO   A HA   1 
ATOM   944  H HB2  A PRO   A 1 32  ? 23.295 -5.484  14.861  0.48 17.11 ?  32  PRO   A HB2  1 
ATOM   945  H HB2  B PRO   A 1 32  ? 23.081 -5.370  15.040  0.52 17.40 ?  32  PRO   A HB2  1 
ATOM   946  H HB3  A PRO   A 1 32  ? 21.886 -5.329  15.601  0.48 17.11 ?  32  PRO   A HB3  1 
ATOM   947  H HB3  B PRO   A 1 32  ? 21.662 -5.146  15.745  0.52 17.40 ?  32  PRO   A HB3  1 
ATOM   948  H HG2  A PRO   A 1 32  ? 23.377 -3.307  14.331  0.48 16.58 ?  32  PRO   A HG2  1 
ATOM   949  H HG2  B PRO   A 1 32  ? 23.221 -3.214  14.412  0.52 17.11 ?  32  PRO   A HG2  1 
ATOM   950  H HG3  A PRO   A 1 32  ? 21.815 -3.596  14.167  0.48 16.58 ?  32  PRO   A HG3  1 
ATOM   951  H HG3  B PRO   A 1 32  ? 21.664 -3.502  14.199  0.52 17.11 ?  32  PRO   A HG3  1 
ATOM   952  H HD2  A PRO   A 1 32  ? 22.619 -1.757  15.749  0.48 15.98 ?  32  PRO   A HD2  1 
ATOM   953  H HD2  B PRO   A 1 32  ? 22.406 -1.592  15.721  0.52 16.90 ?  32  PRO   A HD2  1 
ATOM   954  H HD3  A PRO   A 1 32  ? 21.317 -2.620  16.114  0.48 15.98 ?  32  PRO   A HD3  1 
ATOM   955  H HD3  B PRO   A 1 32  ? 21.096 -2.443  16.088  0.52 16.90 ?  32  PRO   A HD3  1 
ATOM   956  N N    A THR   A 1 33  ? 25.527 -5.834  16.618  0.48 13.83 ?  33  THR   A N    1 
ATOM   957  N N    B THR   A 1 33  ? 25.288 -5.614  16.602  0.52 13.93 ?  33  THR   A N    1 
ATOM   958  C CA   A THR   A 1 33  ? 26.931 -6.019  16.277  0.48 14.46 ?  33  THR   A CA   1 
ATOM   959  C CA   B THR   A 1 33  ? 26.711 -5.775  16.329  0.52 13.70 ?  33  THR   A CA   1 
ATOM   960  C C    A THR   A 1 33  ? 27.212 -5.560  14.849  0.48 13.40 ?  33  THR   A C    1 
ATOM   961  C C    B THR   A 1 33  ? 27.052 -5.328  14.911  0.52 12.64 ?  33  THR   A C    1 
ATOM   962  O O    A THR   A 1 33  ? 28.285 -5.007  14.572  0.48 13.22 ?  33  THR   A O    1 
ATOM   963  O O    B THR   A 1 33  ? 28.037 -4.610  14.694  0.52 12.47 ?  33  THR   A O    1 
ATOM   964  C CB   A THR   A 1 33  ? 27.326 -7.486  16.475  0.48 16.24 ?  33  THR   A CB   1 
ATOM   965  C CB   B THR   A 1 33  ? 27.105 -7.235  16.546  0.52 15.30 ?  33  THR   A CB   1 
ATOM   966  O OG1  A THR   A 1 33  ? 27.086 -7.876  17.833  0.48 17.66 ?  33  THR   A OG1  1 
ATOM   967  O OG1  B THR   A 1 33  ? 26.737 -7.629  17.874  0.52 16.68 ?  33  THR   A OG1  1 
ATOM   968  C CG2  A THR   A 1 33  ? 28.793 -7.702  16.163  0.48 16.83 ?  33  THR   A CG2  1 
ATOM   969  C CG2  B THR   A 1 33  ? 28.602 -7.427  16.347  0.52 16.12 ?  33  THR   A CG2  1 
ATOM   970  H H    A THR   A 1 33  ? 25.120 -6.547  16.878  0.48 16.57 ?  33  THR   A H    1 
ATOM   971  H H    B THR   A 1 33  ? 24.854 -6.349  16.719  0.52 16.70 ?  33  THR   A H    1 
ATOM   972  H HA   A THR   A 1 33  ? 27.473 -5.480  16.873  0.48 17.33 ?  33  THR   A HA   1 
ATOM   973  H HA   B THR   A 1 33  ? 27.216 -5.233  16.956  0.52 16.41 ?  33  THR   A HA   1 
ATOM   974  H HB   A THR   A 1 33  ? 26.794 -8.046  15.886  0.48 19.46 ?  33  THR   A HB   1 
ATOM   975  H HB   B THR   A 1 33  ? 26.636 -7.797  15.907  0.52 18.33 ?  33  THR   A HB   1 
ATOM   976  H HG1  A THR   A 1 33  ? 27.524 -7.385  18.357  0.48 21.17 ?  33  THR   A HG1  1 
ATOM   977  H HG1  B THR   A 1 33  ? 27.155 -7.166  18.439  0.52 19.99 ?  33  THR   A HG1  1 
ATOM   978  H HG21 A THR   A 1 33  ? 29.062 -8.588  16.452  0.48 20.17 ?  33  THR   A HG21 1 
ATOM   979  H HG21 B THR   A 1 33  ? 28.864 -8.313  16.642  0.52 19.32 ?  33  THR   A HG21 1 
ATOM   980  H HG22 A THR   A 1 33  ? 28.945 -7.621  15.211  0.48 20.17 ?  33  THR   A HG22 1 
ATOM   981  H HG22 B THR   A 1 33  ? 28.827 -7.330  15.408  0.52 19.32 ?  33  THR   A HG22 1 
ATOM   982  H HG23 A THR   A 1 33  ? 29.328 -7.042  16.630  0.48 20.17 ?  33  THR   A HG23 1 
ATOM   983  H HG23 B THR   A 1 33  ? 29.091 -6.767  16.860  0.52 19.32 ?  33  THR   A HG23 1 
ATOM   984  N N    . VAL   A 1 34  ? 26.258 -5.762  13.934  1.00 12.28 ?  34  VAL   A N    1 
ATOM   985  C CA   . VAL   A 1 34  ? 26.459 -5.430  12.525  1.00 11.44 ?  34  VAL   A CA   1 
ATOM   986  C C    . VAL   A 1 34  ? 25.165 -4.884  11.942  1.00 10.87 ?  34  VAL   A C    1 
ATOM   987  O O    . VAL   A 1 34  ? 24.132 -5.563  11.975  1.00 11.52 ?  34  VAL   A O    1 
ATOM   988  C CB   . VAL   A 1 34  ? 26.923 -6.641  11.694  1.00 12.11 ?  34  VAL   A CB   1 
ATOM   989  C CG1  . VAL   A 1 34  ? 27.107 -6.239  10.236  1.00 12.45 ?  34  VAL   A CG1  1 
ATOM   990  C CG2  . VAL   A 1 34  ? 28.200 -7.263  12.259  1.00 13.50 ?  34  VAL   A CG2  1 
ATOM   991  H H    A VAL   A 1 34  ? 25.483 -6.095  14.109  0.48 14.71 ?  34  VAL   A H    1 
ATOM   992  H H    B VAL   A 1 34  ? 25.576 -6.273  14.068  0.52 14.71 ?  34  VAL   A H    1 
ATOM   993  H HA   . VAL   A 1 34  ? 27.136 -4.737  12.458  1.00 13.71 ?  34  VAL   A HA   1 
ATOM   994  H HB   . VAL   A 1 34  ? 26.227 -7.317  11.732  1.00 14.50 ?  34  VAL   A HB   1 
ATOM   995  H HG11 . VAL   A 1 34  ? 27.615 -6.930  9.784   1.00 14.91 ?  34  VAL   A HG11 1 
ATOM   996  H HG12 . VAL   A 1 34  ? 26.239 -6.139  9.819   1.00 14.91 ?  34  VAL   A HG12 1 
ATOM   997  H HG13 . VAL   A 1 34  ? 27.594 -5.399  10.200  1.00 14.91 ?  34  VAL   A HG13 1 
ATOM   998  H HG21 . VAL   A 1 34  ? 28.498 -7.966  11.657  1.00 16.18 ?  34  VAL   A HG21 1 
ATOM   999  H HG22 . VAL   A 1 34  ? 28.883 -6.578  12.328  1.00 16.18 ?  34  VAL   A HG22 1 
ATOM   1000 H HG23 . VAL   A 1 34  ? 28.014 -7.637  13.134  1.00 16.18 ?  34  VAL   A HG23 1 
ATOM   1001 N N    . VAL   A 1 35  ? 25.233 -3.682  11.369  1.00 10.37 ?  35  VAL   A N    1 
ATOM   1002 C CA   . VAL   A 1 35  ? 24.205 -3.174  10.470  1.00 10.11 ?  35  VAL   A CA   1 
ATOM   1003 C C    . VAL   A 1 35  ? 24.766 -3.180  9.054   1.00 9.57  ?  35  VAL   A C    1 
ATOM   1004 O O    . VAL   A 1 35  ? 25.915 -2.781  8.832   1.00 10.33 ?  35  VAL   A O    1 
ATOM   1005 C CB   . VAL   A 1 35  ? 23.667 -1.781  10.877  1.00 10.80 ?  35  VAL   A CB   1 
ATOM   1006 C CG1  . VAL   A 1 35  ? 24.734 -0.683  10.759  1.00 11.47 ?  35  VAL   A CG1  1 
ATOM   1007 C CG2  . VAL   A 1 35  ? 22.436 -1.428  10.049  1.00 11.42 ?  35  VAL   A CG2  1 
ATOM   1008 H H    . VAL   A 1 35  ? 25.886 -3.133  11.482  1.00 12.41 ?  35  VAL   A H    1 
ATOM   1009 H HA   . VAL   A 1 35  ? 23.453 -3.787  10.488  1.00 12.11 ?  35  VAL   A HA   1 
ATOM   1010 H HB   . VAL   A 1 35  ? 23.387 -1.817  11.802  1.00 12.94 ?  35  VAL   A HB   1 
ATOM   1011 H HG11 . VAL   A 1 35  ? 24.375 0.147   11.114  1.00 13.74 ?  35  VAL   A HG11 1 
ATOM   1012 H HG12 . VAL   A 1 35  ? 25.516 -0.948  11.266  1.00 13.74 ?  35  VAL   A HG12 1 
ATOM   1013 H HG13 . VAL   A 1 35  ? 24.970 -0.564  9.824   1.00 13.74 ?  35  VAL   A HG13 1 
ATOM   1014 H HG21 . VAL   A 1 35  ? 22.078 -0.582  10.354  1.00 13.69 ?  35  VAL   A HG21 1 
ATOM   1015 H HG22 . VAL   A 1 35  ? 22.689 -1.361  9.112   1.00 13.69 ?  35  VAL   A HG22 1 
ATOM   1016 H HG23 . VAL   A 1 35  ? 21.770 -2.128  10.157  1.00 13.69 ?  35  VAL   A HG23 1 
ATOM   1017 N N    . VAL   A 1 36  ? 23.960 -3.647  8.099   1.00 9.11  ?  36  VAL   A N    1 
ATOM   1018 C CA   . VAL   A 1 36  ? 24.346 -3.658  6.695   1.00 8.83  ?  36  VAL   A CA   1 
ATOM   1019 C C    . VAL   A 1 36  ? 23.886 -2.371  6.026   1.00 9.08  ?  36  VAL   A C    1 
ATOM   1020 O O    . VAL   A 1 36  ? 22.720 -1.980  6.149   1.00 9.73  ?  36  VAL   A O    1 
ATOM   1021 C CB   . VAL   A 1 36  ? 23.751 -4.877  5.974   1.00 9.26  ?  36  VAL   A CB   1 
ATOM   1022 C CG1  . VAL   A 1 36  ? 24.026 -4.808  4.487   1.00 9.75  ?  36  VAL   A CG1  1 
ATOM   1023 C CG2  . VAL   A 1 36  ? 24.288 -6.165  6.566   1.00 9.96  ?  36  VAL   A CG2  1 
ATOM   1024 H H    . VAL   A 1 36  ? 23.169 -3.970  8.246   1.00 10.90 ?  36  VAL   A H    1 
ATOM   1025 H HA   . VAL   A 1 36  ? 25.316 -3.714  6.636   1.00 10.58 ?  36  VAL   A HA   1 
ATOM   1026 H HB   . VAL   A 1 36  ? 22.790 -4.870  6.098   1.00 11.09 ?  36  VAL   A HB   1 
ATOM   1027 H HG11 . VAL   A 1 36  ? 23.889 -5.686  4.101   1.00 11.68 ?  36  VAL   A HG11 1 
ATOM   1028 H HG12 . VAL   A 1 36  ? 23.420 -4.170  4.079   1.00 11.68 ?  36  VAL   A HG12 1 
ATOM   1029 H HG13 . VAL   A 1 36  ? 24.946 -4.528  4.349   1.00 11.68 ?  36  VAL   A HG13 1 
ATOM   1030 H HG21 . VAL   A 1 36  ? 23.907 -6.917  6.081   1.00 11.93 ?  36  VAL   A HG21 1 
ATOM   1031 H HG22 . VAL   A 1 36  ? 25.252 -6.175  6.484   1.00 11.93 ?  36  VAL   A HG22 1 
ATOM   1032 H HG23 . VAL   A 1 36  ? 24.033 -6.215  7.501   1.00 11.93 ?  36  VAL   A HG23 1 
ATOM   1033 N N    . ASN   A 1 37  ? 24.805 -1.732  5.300   1.00 8.70  ?  37  ASN   A N    1 
ATOM   1034 C CA   . ASN   A 1 37  ? 24.477 -0.621  4.425   1.00 8.64  ?  37  ASN   A CA   1 
ATOM   1035 C C    . ASN   A 1 37  ? 24.362 -1.099  2.988   1.00 8.64  ?  37  ASN   A C    1 
ATOM   1036 O O    . ASN   A 1 37  ? 25.159 -1.927  2.528   1.00 9.23  ?  37  ASN   A O    1 
ATOM   1037 C CB   . ASN   A 1 37  ? 25.551 0.463   4.512   1.00 9.06  ?  37  ASN   A CB   1 
ATOM   1038 C CG   . ASN   A 1 37  ? 25.231 1.656   3.653   1.00 9.21  ?  37  ASN   A CG   1 
ATOM   1039 O OD1  . ASN   A 1 37  ? 24.059 1.982   3.448   1.00 9.96  ?  37  ASN   A OD1  1 
ATOM   1040 N ND2  . ASN   A 1 37  ? 26.270 2.309   3.137   1.00 9.67  ?  37  ASN   A ND2  1 
ATOM   1041 H H    . ASN   A 1 37  ? 25.645 -1.935  5.304   1.00 10.41 ?  37  ASN   A H    1 
ATOM   1042 H HA   . ASN   A 1 37  ? 23.634 -0.235  4.698   1.00 10.34 ?  37  ASN   A HA   1 
ATOM   1043 H HB2  . ASN   A 1 37  ? 25.630 0.761   5.433   1.00 10.85 ?  37  ASN   A HB2  1 
ATOM   1044 H HB3  . ASN   A 1 37  ? 26.402 0.091   4.215   1.00 10.85 ?  37  ASN   A HB3  1 
ATOM   1045 H HD21 . ASN   A 1 37  ? 26.138 2.992   2.632   1.00 11.58 ?  37  ASN   A HD21 1 
ATOM   1046 H HD22 . ASN   A 1 37  ? 27.067 2.043   3.290   1.00 11.58 ?  37  ASN   A HD22 1 
ATOM   1047 N N    A ALA   A 1 38  ? 23.344 -0.569  2.305   0.48 8.94  ?  38  ALA   A N    1 
ATOM   1048 N N    B ALA   A 1 38  ? 23.349 -0.605  2.275   0.52 9.05  ?  38  ALA   A N    1 
ATOM   1049 C CA   A ALA   A 1 38  ? 23.157 -0.677  0.861   0.48 9.01  ?  38  ALA   A CA   1 
ATOM   1050 C CA   B ALA   A 1 38  ? 23.217 -0.891  0.846   0.52 9.58  ?  38  ALA   A CA   1 
ATOM   1051 C C    A ALA   A 1 38  ? 24.085 0.332   0.186   0.48 9.02  ?  38  ALA   A C    1 
ATOM   1052 C C    B ALA   A 1 38  ? 24.023 0.153   0.075   0.52 9.64  ?  38  ALA   A C    1 
ATOM   1053 O O    A ALA   A 1 38  ? 23.692 1.442   -0.184  0.48 8.63  ?  38  ALA   A O    1 
ATOM   1054 O O    B ALA   A 1 38  ? 23.511 1.177   -0.389  0.52 9.65  ?  38  ALA   A O    1 
ATOM   1055 C CB   A ALA   A 1 38  ? 21.697 -0.406  0.514   0.48 8.62  ?  38  ALA   A CB   1 
ATOM   1056 C CB   B ALA   A 1 38  ? 21.753 -0.908  0.430   0.52 10.03 ?  38  ALA   A CB   1 
ATOM   1057 H H    A ALA   A 1 38  ? 22.723 -0.110  2.685   0.48 10.70 ?  38  ALA   A H    1 
ATOM   1058 H H    B ALA   A 1 38  ? 22.733 -0.097  2.597   0.52 10.83 ?  38  ALA   A H    1 
ATOM   1059 H HA   A ALA   A 1 38  ? 23.393 -1.561  0.562   0.48 10.79 ?  38  ALA   A HA   1 
ATOM   1060 H HA   B ALA   A 1 38  ? 23.593 -1.767  0.664   0.52 11.48 ?  38  ALA   A HA   1 
ATOM   1061 H HB1  A ALA   A 1 38  ? 21.578 -0.480  -0.445  0.48 10.31 ?  38  ALA   A HB1  1 
ATOM   1062 H HB1  B ALA   A 1 38  ? 21.704 -1.056  -0.529  0.52 12.01 ?  38  ALA   A HB1  1 
ATOM   1063 H HB2  A ALA   A 1 38  ? 21.138 -1.054  0.970   0.48 10.31 ?  38  ALA   A HB2  1 
ATOM   1064 H HB2  B ALA   A 1 38  ? 21.295 -1.627  0.897   0.52 12.01 ?  38  ALA   A HB2  1 
ATOM   1065 H HB3  A ALA   A 1 38  ? 21.460 0.493   0.805   0.48 10.31 ?  38  ALA   A HB3  1 
ATOM   1066 H HB3  B ALA   A 1 38  ? 21.350 -0.057  0.652   0.52 12.01 ?  38  ALA   A HB3  1 
ATOM   1067 N N    A ALA   A 1 39  ? 25.344 -0.071  0.027   0.48 9.35  ?  39  ALA   A N    1 
ATOM   1068 N N    B ALA   A 1 39  ? 25.320 -0.116  -0.055  0.52 10.13 ?  39  ALA   A N    1 
ATOM   1069 C CA   A ALA   A 1 39  ? 26.422 0.798   -0.423  0.48 8.79  ?  39  ALA   A CA   1 
ATOM   1070 C CA   B ALA   A 1 39  ? 26.259 0.869   -0.564  0.52 9.86  ?  39  ALA   A CA   1 
ATOM   1071 C C    A ALA   A 1 39  ? 26.579 0.758   -1.939  0.48 9.17  ?  39  ALA   A C    1 
ATOM   1072 C C    B ALA   A 1 39  ? 26.403 0.772   -2.081  0.52 9.43  ?  39  ALA   A C    1 
ATOM   1073 O O    A ALA   A 1 39  ? 26.097 -0.152  -2.618  0.48 9.52  ?  39  ALA   A O    1 
ATOM   1074 O O    B ALA   A 1 39  ? 25.971 -0.190  -2.719  0.52 10.28 ?  39  ALA   A O    1 
ATOM   1075 C CB   A ALA   A 1 39  ? 27.740 0.359   0.224   0.48 8.54  ?  39  ALA   A CB   1 
ATOM   1076 C CB   B ALA   A 1 39  ? 27.621 0.685   0.106   0.52 10.66 ?  39  ALA   A CB   1 
ATOM   1077 H H    A ALA   A 1 39  ? 25.604 -0.873  0.184   0.48 11.20 ?  39  ALA   A H    1 
ATOM   1078 H H    B ALA   A 1 39  ? 25.684 -0.873  0.155   0.52 12.13 ?  39  ALA   A H    1 
ATOM   1079 H HA   A ALA   A 1 39  ? 26.243 1.713   -0.157  0.48 10.52 ?  39  ALA   A HA   1 
ATOM   1080 H HA   B ALA   A 1 39  ? 25.932 1.756   -0.338  0.52 11.81 ?  39  ALA   A HA   1 
ATOM   1081 H HB1  A ALA   A 1 39  ? 28.455 0.944   -0.082  0.48 10.23 ?  39  ALA   A HB1  1 
ATOM   1082 H HB1  B ALA   A 1 39  ? 28.234 1.352   -0.241  0.52 12.77 ?  39  ALA   A HB1  1 
ATOM   1083 H HB2  A ALA   A 1 39  ? 27.656 0.428   1.191   0.48 10.23 ?  39  ALA   A HB2  1 
ATOM   1084 H HB2  B ALA   A 1 39  ? 27.522 0.801   1.068   0.52 12.77 ?  39  ALA   A HB2  1 
ATOM   1085 H HB3  A ALA   A 1 39  ? 27.931 -0.555  -0.027  0.48 10.23 ?  39  ALA   A HB3  1 
ATOM   1086 H HB3  B ALA   A 1 39  ? 27.951 -0.204  -0.085  0.52 12.77 ?  39  ALA   A HB3  1 
ATOM   1087 N N    A ASN   A 1 40  ? 27.287 1.762   -2.465  0.48 9.52  ?  40  ASN   A N    1 
ATOM   1088 N N    B ASN   A 1 40  ? 27.012 1.806   -2.659  0.52 8.88  ?  40  ASN   A N    1 
ATOM   1089 C CA   A ASN   A 1 40  ? 27.848 1.719   -3.811  0.48 9.45  ?  40  ASN   A CA   1 
ATOM   1090 C CA   B ASN   A 1 40  ? 27.556 1.742   -4.008  0.52 9.01  ?  40  ASN   A CA   1 
ATOM   1091 C C    A ASN   A 1 40  ? 29.371 1.610   -3.729  0.48 8.80  ?  40  ASN   A C    1 
ATOM   1092 C C    B ASN   A 1 40  ? 29.079 1.607   -3.939  0.52 8.43  ?  40  ASN   A C    1 
ATOM   1093 O O    A ASN   A 1 40  ? 29.962 1.715   -2.650  0.48 9.23  ?  40  ASN   A O    1 
ATOM   1094 O O    B ASN   A 1 40  ? 29.685 1.689   -2.868  0.52 8.52  ?  40  ASN   A O    1 
ATOM   1095 C CB   A ASN   A 1 40  ? 27.385 2.907   -4.675  0.48 10.34 ?  40  ASN   A CB   1 
ATOM   1096 C CB   B ASN   A 1 40  ? 27.132 2.954   -4.851  0.52 9.49  ?  40  ASN   A CB   1 
ATOM   1097 C CG   A ASN   A 1 40  ? 27.734 4.251   -4.076  0.48 11.55 ?  40  ASN   A CG   1 
ATOM   1098 C CG   B ASN   A 1 40  ? 27.523 4.271   -4.228  0.52 9.79  ?  40  ASN   A CG   1 
ATOM   1099 O OD1  A ASN   A 1 40  ? 28.876 4.492   -3.683  0.48 11.01 ?  40  ASN   A OD1  1 
ATOM   1100 O OD1  B ASN   A 1 40  ? 28.706 4.543   -4.024  0.52 10.15 ?  40  ASN   A OD1  1 
ATOM   1101 N ND2  A ASN   A 1 40  ? 26.742 5.142   -4.006  0.48 12.99 ?  40  ASN   A ND2  1 
ATOM   1102 N ND2  B ASN   A 1 40  ? 26.528 5.102   -3.931  0.52 10.83 ?  40  ASN   A ND2  1 
ATOM   1103 H H    A ASN   A 1 40  ? 27.465 2.495   -2.049  0.48 11.41 ?  40  ASN   A H    1 
ATOM   1104 H H    B ASN   A 1 40  ? 27.120 2.567   -2.277  0.52 10.63 ?  40  ASN   A H    1 
ATOM   1105 H HA   A ASN   A 1 40  ? 27.529 0.918   -4.247  0.48 11.32 ?  40  ASN   A HA   1 
ATOM   1106 H HA   B ASN   A 1 40  ? 27.202 0.941   -4.441  0.52 10.79 ?  40  ASN   A HA   1 
ATOM   1107 H HB2  A ASN   A 1 40  ? 27.807 2.845   -5.554  0.48 12.39 ?  40  ASN   A HB2  1 
ATOM   1108 H HB2  B ASN   A 1 40  ? 27.557 2.890   -5.717  0.52 11.36 ?  40  ASN   A HB2  1 
ATOM   1109 H HB3  A ASN   A 1 40  ? 26.421 2.867   -4.779  0.48 12.39 ?  40  ASN   A HB3  1 
ATOM   1110 H HB3  B ASN   A 1 40  ? 26.166 2.939   -4.953  0.52 11.36 ?  40  ASN   A HB3  1 
ATOM   1111 H HD21 A ASN   A 1 40  ? 26.887 5.928   -3.685  0.48 15.57 ?  40  ASN   A HD21 1 
ATOM   1112 H HD21 B ASN   A 1 40  ? 26.700 5.868   -3.575  0.52 12.97 ?  40  ASN   A HD21 1 
ATOM   1113 H HD22 A ASN   A 1 40  ? 25.953 4.933   -4.282  0.48 15.57 ?  40  ASN   A HD22 1 
ATOM   1114 H HD22 B ASN   A 1 40  ? 25.716 4.878   -4.095  0.52 12.97 ?  40  ASN   A HD22 1 
ATOM   1115 N N    A VAL   A 1 41  ? 30.005 1.359   -4.882  0.48 8.93  ?  41  VAL   A N    1 
ATOM   1116 N N    B VAL   A 1 41  ? 29.696 1.372   -5.100  0.52 9.15  ?  41  VAL   A N    1 
ATOM   1117 C CA   A VAL   A 1 41  ? 31.433 1.030   -4.890  0.48 8.81  ?  41  VAL   A CA   1 
ATOM   1118 C CA   B VAL   A 1 41  ? 31.125 1.062   -5.132  0.52 9.74  ?  41  VAL   A CA   1 
ATOM   1119 C C    A VAL   A 1 41  ? 32.285 2.183   -4.394  0.48 8.82  ?  41  VAL   A C    1 
ATOM   1120 C C    B VAL   A 1 41  ? 31.990 2.204   -4.624  0.52 9.40  ?  41  VAL   A C    1 
ATOM   1121 O O    A VAL   A 1 41  ? 33.402 1.968   -3.904  0.48 9.38  ?  41  VAL   A O    1 
ATOM   1122 O O    B VAL   A 1 41  ? 33.147 1.978   -4.250  0.52 9.80  ?  41  VAL   A O    1 
ATOM   1123 C CB   A VAL   A 1 41  ? 31.927 0.526   -6.265  0.48 8.93  ?  41  VAL   A CB   1 
ATOM   1124 C CB   B VAL   A 1 41  ? 31.591 0.622   -6.540  0.52 10.92 ?  41  VAL   A CB   1 
ATOM   1125 C CG1  A VAL   A 1 41  ? 31.211 -0.752  -6.672  0.48 9.77  ?  41  VAL   A CG1  1 
ATOM   1126 C CG1  B VAL   A 1 41  ? 30.948 -0.701  -6.939  0.52 12.27 ?  41  VAL   A CG1  1 
ATOM   1127 C CG2  A VAL   A 1 41  ? 31.807 1.592   -7.351  0.48 8.40  ?  41  VAL   A CG2  1 
ATOM   1128 C CG2  B VAL   A 1 41  ? 31.316 1.700   -7.581  0.52 11.39 ?  41  VAL   A CG2  1 
ATOM   1129 H H    A VAL   A 1 41  ? 29.641 1.360   -5.659  0.48 10.69 ?  41  VAL   A H    1 
ATOM   1130 H H    B VAL   A 1 41  ? 29.306 1.369   -5.864  0.52 10.96 ?  41  VAL   A H    1 
ATOM   1131 H HA   A VAL   A 1 41  ? 31.579 0.307   -4.267  0.48 10.55 ?  41  VAL   A HA   1 
ATOM   1132 H HA   B VAL   A 1 41  ? 31.276 0.306   -4.540  0.52 11.66 ?  41  VAL   A HA   1 
ATOM   1133 H HB   A VAL   A 1 41  ? 32.875 0.309   -6.191  0.48 10.69 ?  41  VAL   A HB   1 
ATOM   1134 H HB   B VAL   A 1 41  ? 32.549 0.477   -6.511  0.52 13.08 ?  41  VAL   A HB   1 
ATOM   1135 H HG11 A VAL   A 1 41  ? 31.552 -1.058  -7.527  0.48 11.70 ?  41  VAL   A HG11 1 
ATOM   1136 H HG11 B VAL   A 1 41  ? 31.272 -0.959  -7.816  0.52 14.70 ?  41  VAL   A HG11 1 
ATOM   1137 H HG12 A VAL   A 1 41  ? 31.360 -1.431  -5.995  0.48 11.70 ?  41  VAL   A HG12 1 
ATOM   1138 H HG12 B VAL   A 1 41  ? 31.188 -1.381  -6.287  0.52 14.70 ?  41  VAL   A HG12 1 
ATOM   1139 H HG13 A VAL   A 1 41  ? 30.258 -0.569  -6.747  0.48 11.70 ?  41  VAL   A HG13 1 
ATOM   1140 H HG13 B VAL   A 1 41  ? 29.985 -0.593  -6.960  0.52 14.70 ?  41  VAL   A HG13 1 
ATOM   1141 H HG21 A VAL   A 1 41  ? 32.046 1.198   -8.209  0.48 10.06 ?  41  VAL   A HG21 1 
ATOM   1142 H HG21 B VAL   A 1 41  ? 31.626 1.385   -8.445  0.52 13.64 ?  41  VAL   A HG21 1 
ATOM   1143 H HG22 A VAL   A 1 41  ? 30.895 1.909   -7.377  0.48 10.06 ?  41  VAL   A HG22 1 
ATOM   1144 H HG22 B VAL   A 1 41  ? 30.361 1.869   -7.615  0.52 13.64 ?  41  VAL   A HG22 1 
ATOM   1145 H HG23 A VAL   A 1 41  ? 32.412 2.321   -7.147  0.48 10.06 ?  41  VAL   A HG23 1 
ATOM   1146 H HG23 B VAL   A 1 41  ? 31.789 2.506   -7.332  0.52 13.64 ?  41  VAL   A HG23 1 
ATOM   1147 N N    A TYR   A 1 42  ? 31.799 3.414   -4.527  0.48 9.30  ?  42  TYR   A N    1 
ATOM   1148 N N    B TYR   A 1 42  ? 31.473 3.434   -4.634  0.52 9.60  ?  42  TYR   A N    1 
ATOM   1149 C CA   A TYR   A 1 42  ? 32.531 4.598   -4.094  0.48 9.54  ?  42  TYR   A CA   1 
ATOM   1150 C CA   B TYR   A 1 42  ? 32.221 4.616   -4.216  0.52 9.62  ?  42  TYR   A CA   1 
ATOM   1151 C C    A TYR   A 1 42  ? 32.217 4.972   -2.656  0.48 9.16  ?  42  TYR   A C    1 
ATOM   1152 C C    B TYR   A 1 42  ? 31.993 4.990   -2.758  0.52 9.94  ?  42  TYR   A C    1 
ATOM   1153 O O    A TYR   A 1 42  ? 32.784 5.944   -2.143  0.48 9.57  ?  42  TYR   A O    1 
ATOM   1154 O O    B TYR   A 1 42  ? 32.561 5.986   -2.295  0.52 10.38 ?  42  TYR   A O    1 
ATOM   1155 C CB   A TYR   A 1 42  ? 32.220 5.786   -5.022  0.48 10.08 ?  42  TYR   A CB   1 
ATOM   1156 C CB   B TYR   A 1 42  ? 31.854 5.815   -5.104  0.52 9.91  ?  42  TYR   A CB   1 
ATOM   1157 C CG   A TYR   A 1 42  ? 32.395 5.457   -6.492  0.48 10.28 ?  42  TYR   A CG   1 
ATOM   1158 C CG   B TYR   A 1 42  ? 32.004 5.528   -6.575  0.52 10.44 ?  42  TYR   A CG   1 
ATOM   1159 C CD1  A TYR   A 1 42  ? 33.657 5.257   -7.028  0.48 10.62 ?  42  TYR   A CD1  1 
ATOM   1160 C CD1  B TYR   A 1 42  ? 33.257 5.331   -7.140  0.52 10.50 ?  42  TYR   A CD1  1 
ATOM   1161 C CD2  A TYR   A 1 42  ? 31.296 5.324   -7.338  0.48 10.94 ?  42  TYR   A CD2  1 
ATOM   1162 C CD2  B TYR   A 1 42  ? 30.891 5.444   -7.401  0.52 11.89 ?  42  TYR   A CD2  1 
ATOM   1163 C CE1  A TYR   A 1 42  ? 33.828 4.942   -8.362  0.48 11.11 ?  42  TYR   A CE1  1 
ATOM   1164 C CE1  B TYR   A 1 42  ? 33.394 5.058   -8.487  0.52 10.93 ?  42  TYR   A CE1  1 
ATOM   1165 C CE2  A TYR   A 1 42  ? 31.461 5.012   -8.680  0.48 11.22 ?  42  TYR   A CE2  1 
ATOM   1166 C CE2  B TYR   A 1 42  ? 31.019 5.183   -8.747  0.52 12.71 ?  42  TYR   A CE2  1 
ATOM   1167 C CZ   A TYR   A 1 42  ? 32.733 4.823   -9.184  0.48 11.23 ?  42  TYR   A CZ   1 
ATOM   1168 C CZ   B TYR   A 1 42  ? 32.270 4.987   -9.287  0.52 12.22 ?  42  TYR   A CZ   1 
ATOM   1169 O OH   A TYR   A 1 42  ? 32.917 4.505   -10.510 0.48 12.17 ?  42  TYR   A OH   1 
ATOM   1170 O OH   B TYR   A 1 42  ? 32.395 4.722   -10.630 0.52 13.41 ?  42  TYR   A OH   1 
ATOM   1171 H H    A TYR   A 1 42  ? 31.032 3.593   -4.862  0.48 11.14 ?  42  TYR   A H    1 
ATOM   1172 H H    B TYR   A 1 42  ? 30.671 3.610   -4.900  0.52 11.49 ?  42  TYR   A H    1 
ATOM   1173 H HA   A TYR   A 1 42  ? 33.484 4.423   -4.149  0.48 11.42 ?  42  TYR   A HA   1 
ATOM   1174 H HA   B TYR   A 1 42  ? 33.165 4.445   -4.338  0.52 11.52 ?  42  TYR   A HA   1 
ATOM   1175 H HB2  A TYR   A 1 42  ? 31.302 6.063   -4.881  0.48 12.07 ?  42  TYR   A HB2  1 
ATOM   1176 H HB2  B TYR   A 1 42  ? 30.928 6.060   -4.944  0.52 11.87 ?  42  TYR   A HB2  1 
ATOM   1177 H HB3  A TYR   A 1 42  ? 32.821 6.520   -4.805  0.48 12.07 ?  42  TYR   A HB3  1 
ATOM   1178 H HB3  B TYR   A 1 42  ? 32.435 6.561   -4.887  0.52 11.87 ?  42  TYR   A HB3  1 
ATOM   1179 H HD1  A TYR   A 1 42  ? 34.404 5.336   -6.479  0.48 12.72 ?  42  TYR   A HD1  1 
ATOM   1180 H HD1  B TYR   A 1 42  ? 34.016 5.379   -6.603  0.52 12.57 ?  42  TYR   A HD1  1 
ATOM   1181 H HD2  A TYR   A 1 42  ? 30.440 5.454   -6.996  0.48 13.11 ?  42  TYR   A HD2  1 
ATOM   1182 H HD2  B TYR   A 1 42  ? 30.043 5.578   -7.041  0.52 14.25 ?  42  TYR   A HD2  1 
ATOM   1183 H HE1  A TYR   A 1 42  ? 34.683 4.814   -8.705  0.48 13.31 ?  42  TYR   A HE1  1 
ATOM   1184 H HE1  B TYR   A 1 42  ? 34.240 4.928   -8.855  0.52 13.10 ?  42  TYR   A HE1  1 
ATOM   1185 H HE2  A TYR   A 1 42  ? 30.716 4.930   -9.236  0.48 13.44 ?  42  TYR   A HE2  1 
ATOM   1186 H HE2  B TYR   A 1 42  ? 30.262 5.129   -9.286  0.52 15.23 ?  42  TYR   A HE2  1 
ATOM   1187 H HH   A TYR   A 1 42  ? 33.719 4.304   -10.649 0.48 14.58 ?  42  TYR   A HH   1 
ATOM   1188 H HH   B TYR   A 1 42  ? 31.641 4.705   -10.992 0.52 16.07 ?  42  TYR   A HH   1 
ATOM   1189 N N    A LEU   A 1 43  ? 31.327 4.227   -2.004  0.48 8.92  ?  43  LEU   A N    1 
ATOM   1190 N N    B LEU   A 1 43  ? 31.177 4.226   -2.034  0.52 9.94  ?  43  LEU   A N    1 
ATOM   1191 C CA   A LEU   A 1 43  ? 30.861 4.548   -0.658  0.48 8.82  ?  43  LEU   A CA   1 
ATOM   1192 C CA   B LEU   A 1 43  ? 30.730 4.586   -0.687  0.52 9.82  ?  43  LEU   A CA   1 
ATOM   1193 C C    A LEU   A 1 43  ? 30.385 5.995   -0.563  0.48 9.33  ?  43  LEU   A C    1 
ATOM   1194 C C    B LEU   A 1 43  ? 30.247 6.033   -0.614  0.52 9.97  ?  43  LEU   A C    1 
ATOM   1195 O O    A LEU   A 1 43  ? 30.669 6.705   0.405   0.48 10.19 ?  43  LEU   A O    1 
ATOM   1196 O O    B LEU   A 1 43  ? 30.466 6.735   0.376   0.52 10.60 ?  43  LEU   A O    1 
ATOM   1197 C CB   A LEU   A 1 43  ? 31.906 4.234   0.409   0.48 9.75  ?  43  LEU   A CB   1 
ATOM   1198 C CB   B LEU   A 1 43  ? 31.771 4.289   0.390   0.52 9.60  ?  43  LEU   A CB   1 
ATOM   1199 C CG   A LEU   A 1 43  ? 32.409 2.791   0.481   0.48 10.25 ?  43  LEU   A CG   1 
ATOM   1200 C CG   B LEU   A 1 43  ? 32.272 2.846   0.497   0.52 9.86  ?  43  LEU   A CG   1 
ATOM   1201 C CD1  A LEU   A 1 43  ? 33.509 2.695   1.520   0.48 10.57 ?  43  LEU   A CD1  1 
ATOM   1202 C CD1  B LEU   A 1 43  ? 33.247 2.729   1.659   0.52 10.59 ?  43  LEU   A CD1  1 
ATOM   1203 C CD2  A LEU   A 1 43  ? 31.284 1.821   0.802   0.48 10.48 ?  43  LEU   A CD2  1 
ATOM   1204 C CD2  B LEU   A 1 43  ? 31.125 1.839   0.631   0.52 9.86  ?  43  LEU   A CD2  1 
ATOM   1205 H H    A LEU   A 1 43  ? 30.968 3.512   -2.328  0.48 10.68 ?  43  LEU   A H    1 
ATOM   1206 H H    B LEU   A 1 43  ? 30.861 3.476   -2.308  0.52 11.90 ?  43  LEU   A H    1 
ATOM   1207 H HA   A LEU   A 1 43  ? 30.091 3.981   -0.471  0.48 10.56 ?  43  LEU   A HA   1 
ATOM   1208 H HA   B LEU   A 1 43  ? 29.961 4.033   -0.483  0.52 11.76 ?  43  LEU   A HA   1 
ATOM   1209 H HB2  A LEU   A 1 43  ? 32.676 4.799   0.255   0.48 11.67 ?  43  LEU   A HB2  1 
ATOM   1210 H HB2  B LEU   A 1 43  ? 32.544 4.850   0.228   0.52 11.49 ?  43  LEU   A HB2  1 
ATOM   1211 H HB3  A LEU   A 1 43  ? 31.521 4.439   1.275   0.48 11.67 ?  43  LEU   A HB3  1 
ATOM   1212 H HB3  B LEU   A 1 43  ? 31.385 4.520   1.252   0.52 11.49 ?  43  LEU   A HB3  1 
ATOM   1213 H HG   A LEU   A 1 43  ? 32.789 2.539   -0.378  0.48 12.28 ?  43  LEU   A HG   1 
ATOM   1214 H HG   B LEU   A 1 43  ? 32.759 2.629   -0.312  0.52 11.80 ?  43  LEU   A HG   1 
ATOM   1215 H HD11 A LEU   A 1 43  ? 33.827 1.781   1.563   0.48 12.65 ?  43  LEU   A HD11 1 
ATOM   1216 H HD11 B LEU   A 1 43  ? 33.560 1.814   1.718   0.52 12.68 ?  43  LEU   A HD11 1 
ATOM   1217 H HD12 A LEU   A 1 43  ? 34.235 3.287   1.266   0.48 12.65 ?  43  LEU   A HD12 1 
ATOM   1218 H HD12 B LEU   A 1 43  ? 33.997 3.326   1.502   0.52 12.68 ?  43  LEU   A HD12 1 
ATOM   1219 H HD13 A LEU   A 1 43  ? 33.151 2.963   2.381   0.48 12.65 ?  43  LEU   A HD13 1 
ATOM   1220 H HD13 B LEU   A 1 43  ? 32.793 2.978   2.479   0.52 12.68 ?  43  LEU   A HD13 1 
ATOM   1221 H HD21 A LEU   A 1 43  ? 31.657 0.934   0.921   0.48 12.55 ?  43  LEU   A HD21 1 
ATOM   1222 H HD21 B LEU   A 1 43  ? 31.498 0.956   0.789   0.52 11.80 ?  43  LEU   A HD21 1 
ATOM   1223 H HD22 A LEU   A 1 43  ? 30.847 2.110   1.618   0.48 12.55 ?  43  LEU   A HD22 1 
ATOM   1224 H HD22 B LEU   A 1 43  ? 30.562 2.098   1.376   0.52 11.80 ?  43  LEU   A HD22 1 
ATOM   1225 H HD23 A LEU   A 1 43  ? 30.652 1.820   0.068   0.48 12.55 ?  43  LEU   A HD23 1 
ATOM   1226 H HD23 B LEU   A 1 43  ? 30.610 1.837   -0.190  0.52 11.80 ?  43  LEU   A HD23 1 
ATOM   1227 N N    A LYS   A 1 44  ? 29.650 6.437   -1.585  0.48 9.62  ?  44  LYS   A N    1 
ATOM   1228 N N    B LYS   A 1 44  ? 29.557 6.473   -1.667  0.52 9.66  ?  44  LYS   A N    1 
ATOM   1229 C CA   A LYS   A 1 44  ? 29.011 7.748   -1.587  0.48 10.21 ?  44  LYS   A CA   1 
ATOM   1230 C CA   B LYS   A 1 44  ? 28.909 7.784   -1.693  0.52 9.89  ?  44  LYS   A CA   1 
ATOM   1231 C C    A LYS   A 1 44  ? 27.572 7.554   -1.124  0.48 9.84  ?  44  LYS   A C    1 
ATOM   1232 C C    B LYS   A 1 44  ? 27.497 7.607   -1.156  0.52 9.33  ?  44  LYS   A C    1 
ATOM   1233 O O    A LYS   A 1 44  ? 26.741 7.001   -1.853  0.48 10.90 ?  44  LYS   A O    1 
ATOM   1234 O O    B LYS   A 1 44  ? 26.602 7.131   -1.861  0.52 9.97  ?  44  LYS   A O    1 
ATOM   1235 C CB   A LYS   A 1 44  ? 29.087 8.399   -2.966  0.48 12.13 ?  44  LYS   A CB   1 
ATOM   1236 C CB   B LYS   A 1 44  ? 28.908 8.359   -3.104  0.52 12.63 ?  44  LYS   A CB   1 
ATOM   1237 C CG   A LYS   A 1 44  ? 30.497 8.794   -3.388  0.48 14.79 ?  44  LYS   A CG   1 
ATOM   1238 C CG   B LYS   A 1 44  ? 30.245 8.933   -3.542  0.52 16.06 ?  44  LYS   A CG   1 
ATOM   1239 C CD   A LYS   A 1 44  ? 31.159 9.711   -2.373  0.48 19.22 ?  44  LYS   A CD   1 
ATOM   1240 C CD   B LYS   A 1 44  ? 30.848 9.830   -2.468  0.52 20.26 ?  44  LYS   A CD   1 
ATOM   1241 C CE   A LYS   A 1 44  ? 32.494 10.211  -2.879  0.48 21.78 ?  44  LYS   A CE   1 
ATOM   1242 C CE   B LYS   A 1 44  ? 32.081 10.548  -2.971  0.52 22.69 ?  44  LYS   A CE   1 
ATOM   1243 N NZ   A LYS   A 1 44  ? 33.274 10.863  -1.800  0.48 22.98 ?  44  LYS   A NZ   1 
ATOM   1244 N NZ   B LYS   A 1 44  ? 32.935 11.030  -1.852  0.52 24.30 ?  44  LYS   A NZ   1 
ATOM   1245 H H    A LYS   A 1 44  ? 29.505 5.982   -2.304  0.48 11.52 ?  44  LYS   A H    1 
ATOM   1246 H H    B LYS   A 1 44  ? 29.451 6.021   -2.392  0.52 11.57 ?  44  LYS   A H    1 
ATOM   1247 H HA   A LYS   A 1 44  ? 29.452 8.321   -0.942  0.48 12.23 ?  44  LYS   A HA   1 
ATOM   1248 H HA   B LYS   A 1 44  ? 29.368 8.382   -1.085  0.52 11.84 ?  44  LYS   A HA   1 
ATOM   1249 H HB2  A LYS   A 1 44  ? 28.744 7.778   -3.624  0.48 14.54 ?  44  LYS   A HB2  1 
ATOM   1250 H HB2  B LYS   A 1 44  ? 28.670 7.654   -3.729  0.52 15.13 ?  44  LYS   A HB2  1 
ATOM   1251 H HB3  A LYS   A 1 44  ? 28.546 9.205   -2.959  0.48 14.54 ?  44  LYS   A HB3  1 
ATOM   1252 H HB3  B LYS   A 1 44  ? 28.251 9.071   -3.151  0.52 15.13 ?  44  LYS   A HB3  1 
ATOM   1253 H HG2  A LYS   A 1 44  ? 31.042 7.996   -3.475  0.48 17.72 ?  44  LYS   A HG2  1 
ATOM   1254 H HG2  B LYS   A 1 44  ? 30.864 8.207   -3.719  0.52 19.25 ?  44  LYS   A HG2  1 
ATOM   1255 H HG3  A LYS   A 1 44  ? 30.457 9.264   -4.238  0.48 17.72 ?  44  LYS   A HG3  1 
ATOM   1256 H HG3  B LYS   A 1 44  ? 30.117 9.467   -4.345  0.52 19.25 ?  44  LYS   A HG3  1 
ATOM   1257 H HD2  A LYS   A 1 44  ? 30.579 10.474  -2.207  0.48 23.04 ?  44  LYS   A HD2  1 
ATOM   1258 H HD2  B LYS   A 1 44  ? 30.188 10.484  -2.189  0.52 24.29 ?  44  LYS   A HD2  1 
ATOM   1259 H HD3  A LYS   A 1 44  ? 31.312 9.221   -1.550  0.48 23.04 ?  44  LYS   A HD3  1 
ATOM   1260 H HD3  B LYS   A 1 44  ? 31.121 9.282   -1.712  0.52 24.29 ?  44  LYS   A HD3  1 
ATOM   1261 H HE2  A LYS   A 1 44  ? 33.006 9.460   -3.216  0.48 26.11 ?  44  LYS   A HE2  1 
ATOM   1262 H HE2  B LYS   A 1 44  ? 32.606 9.936   -3.512  0.52 27.20 ?  44  LYS   A HE2  1 
ATOM   1263 H HE3  A LYS   A 1 44  ? 32.342 10.859  -3.585  0.48 26.11 ?  44  LYS   A HE3  1 
ATOM   1264 H HE3  B LYS   A 1 44  ? 31.809 11.312  -3.498  0.52 27.20 ?  44  LYS   A HE3  1 
ATOM   1265 H HZ1  A LYS   A 1 44  ? 34.054 11.145  -2.119  0.48 27.56 ?  44  LYS   A HZ1  1 
ATOM   1266 H HZ1  B LYS   A 1 44  ? 33.652 11.446  -2.176  0.52 29.13 ?  44  LYS   A HZ1  1 
ATOM   1267 H HZ2  A LYS   A 1 44  ? 32.822 11.564  -1.482  0.48 27.56 ?  44  LYS   A HZ2  1 
ATOM   1268 H HZ2  B LYS   A 1 44  ? 32.477 11.595  -1.341  0.52 29.13 ?  44  LYS   A HZ2  1 
ATOM   1269 H HZ3  A LYS   A 1 44  ? 33.417 10.289  -1.139  0.48 27.56 ?  44  LYS   A HZ3  1 
ATOM   1270 H HZ3  B LYS   A 1 44  ? 33.203 10.341  -1.354  0.52 29.13 ?  44  LYS   A HZ3  1 
ATOM   1271 N N    . HIS   A 1 45  ? 27.295 7.980   0.106   1.00 9.38  ?  45  HIS   A N    1 
ATOM   1272 C CA   . HIS   A 1 45  ? 26.054 7.645   0.798   1.00 9.36  ?  45  HIS   A CA   1 
ATOM   1273 C C    . HIS   A 1 45  ? 25.028 8.761   0.613   1.00 9.96  ?  45  HIS   A C    1 
ATOM   1274 O O    . HIS   A 1 45  ? 24.741 9.539   1.518   1.00 11.71 ?  45  HIS   A O    1 
ATOM   1275 C CB   . HIS   A 1 45  ? 26.344 7.390   2.267   1.00 9.30  ?  45  HIS   A CB   1 
ATOM   1276 C CG   . HIS   A 1 45  ? 27.453 6.422   2.507   1.00 8.98  ?  45  HIS   A CG   1 
ATOM   1277 N ND1  . HIS   A 1 45  ? 27.455 5.135   2.001   1.00 9.69  ?  45  HIS   A ND1  1 
ATOM   1278 C CD2  . HIS   A 1 45  ? 28.607 6.572   3.198   1.00 9.28  ?  45  HIS   A CD2  1 
ATOM   1279 C CE1  . HIS   A 1 45  ? 28.564 4.535   2.393   1.00 9.46  ?  45  HIS   A CE1  1 
ATOM   1280 N NE2  . HIS   A 1 45  ? 29.283 5.386   3.110   1.00 9.49  ?  45  HIS   A NE2  1 
ATOM   1281 H H    A HIS   A 1 45  ? 27.824 8.476   0.571   0.48 11.23 ?  45  HIS   A H    1 
ATOM   1282 H H    B HIS   A 1 45  ? 27.856 8.429   0.580   0.52 11.23 ?  45  HIS   A H    1 
ATOM   1283 H HA   . HIS   A 1 45  ? 25.683 6.833   0.416   1.00 11.21 ?  45  HIS   A HA   1 
ATOM   1284 H HB2  . HIS   A 1 45  ? 26.571 8.228   2.691   1.00 11.14 ?  45  HIS   A HB2  1 
ATOM   1285 H HB3  . HIS   A 1 45  ? 25.535 7.026   2.680   1.00 11.14 ?  45  HIS   A HB3  1 
ATOM   1286 H HD2  . HIS   A 1 45  ? 28.891 7.339   3.643   1.00 11.11 ?  45  HIS   A HD2  1 
ATOM   1287 H HE1  . HIS   A 1 45  ? 28.807 3.660   2.193   1.00 11.33 ?  45  HIS   A HE1  1 
ATOM   1288 H HE2  . HIS   A 1 45  ? 30.051 5.219   3.466   1.00 11.36 ?  45  HIS   A HE2  1 
ATOM   1289 N N    . GLY   A 1 46  ? 24.441 8.810   -0.575  1.00 10.85 ?  46  GLY   A N    1 
ATOM   1290 C CA   . GLY   A 1 46  ? 23.616 9.949   -0.930  1.00 11.83 ?  46  GLY   A CA   1 
ATOM   1291 C C    . GLY   A 1 46  ? 22.135 9.825   -0.623  1.00 11.48 ?  46  GLY   A C    1 
ATOM   1292 O O    . GLY   A 1 46  ? 21.494 10.819  -0.269  1.00 13.02 ?  46  GLY   A O    1 
ATOM   1293 H H    . GLY   A 1 46  ? 24.498 8.204   -1.176  1.00 13.00 ?  46  GLY   A H    1 
ATOM   1294 H HA2  . GLY   A 1 46  ? 23.946 10.734  -0.460  1.00 14.17 ?  46  GLY   A HA2  1 
ATOM   1295 H HA3  . GLY   A 1 46  ? 23.704 10.112  -1.877  1.00 14.17 ?  46  GLY   A HA3  1 
ATOM   1296 N N    A GLY   A 1 47  ? 21.589 8.631   -0.808  0.48 11.35 ?  47  GLY   A N    1 
ATOM   1297 N N    B GLY   A 1 47  ? 21.574 8.619   -0.723  0.52 11.31 ?  47  GLY   A N    1 
ATOM   1298 C CA   A GLY   A 1 47  ? 20.157 8.428   -0.757  0.48 11.24 ?  47  GLY   A CA   1 
ATOM   1299 C CA   B GLY   A 1 47  ? 20.140 8.429   -0.579  0.52 11.10 ?  47  GLY   A CA   1 
ATOM   1300 C C    A GLY   A 1 47  ? 19.869 6.980   -0.436  0.48 10.74 ?  47  GLY   A C    1 
ATOM   1301 C C    B GLY   A 1 47  ? 19.791 7.023   -0.129  0.52 9.95  ?  47  GLY   A C    1 
ATOM   1302 O O    A GLY   A 1 47  ? 20.778 6.166   -0.257  0.48 10.82 ?  47  GLY   A O    1 
ATOM   1303 O O    B GLY   A 1 47  ? 20.666 6.180   0.084   0.52 9.55  ?  47  GLY   A O    1 
ATOM   1304 H H    A GLY   A 1 47  ? 22.040 7.916   -0.952  0.48 13.59 ?  47  GLY   A H    1 
ATOM   1305 H H    B GLY   A 1 47  ? 22.006 7.893   -0.860  0.52 13.55 ?  47  GLY   A H    1 
ATOM   1306 H HA2  A GLY   A 1 47  ? 19.762 8.995   -0.074  0.48 13.46 ?  47  GLY   A HA2  1 
ATOM   1307 H HA2  B GLY   A 1 47  ? 19.786 9.055   0.070   0.52 13.30 ?  47  GLY   A HA2  1 
ATOM   1308 H HA3  A GLY   A 1 47  ? 19.765 8.650   -1.617  0.48 13.46 ?  47  GLY   A HA3  1 
ATOM   1309 H HA3  B GLY   A 1 47  ? 19.707 8.593   -1.432  0.52 13.30 ?  47  GLY   A HA3  1 
ATOM   1310 N N    A GLY   A 1 48  ? 18.583 6.659   -0.380  0.48 10.15 ?  48  GLY   A N    1 
ATOM   1311 N N    B GLY   A 1 48  ? 18.485 6.773   0.012   0.52 10.10 ?  48  GLY   A N    1 
ATOM   1312 C CA   A GLY   A 1 48  ? 18.219 5.319   0.014   0.48 10.04 ?  48  GLY   A CA   1 
ATOM   1313 C CA   B GLY   A 1 48  ? 18.025 5.457   0.429   0.52 9.63  ?  48  GLY   A CA   1 
ATOM   1314 C C    A GLY   A 1 48  ? 18.680 5.027   1.429   0.48 9.59  ?  48  GLY   A C    1 
ATOM   1315 C C    B GLY   A 1 48  ? 18.603 5.055   1.770   0.52 9.60  ?  48  GLY   A C    1 
ATOM   1316 O O    A GLY   A 1 48  ? 18.849 5.929   2.256   0.48 9.79  ?  48  GLY   A O    1 
ATOM   1317 O O    B GLY   A 1 48  ? 18.755 5.874   2.685   0.52 10.03 ?  48  GLY   A O    1 
ATOM   1318 H H    A GLY   A 1 48  ? 17.931 7.186   -0.562  0.48 12.16 ?  48  GLY   A H    1 
ATOM   1319 H H    B GLY   A 1 48  ? 17.843 7.338   -0.125  0.52 12.09 ?  48  GLY   A H    1 
ATOM   1320 H HA2  A GLY   A 1 48  ? 17.261 5.215   -0.025  0.48 12.02 ?  48  GLY   A HA2  1 
ATOM   1321 H HA2  B GLY   A 1 48  ? 17.052 5.444   0.493   0.52 11.53 ?  48  GLY   A HA2  1 
ATOM   1322 H HA3  A GLY   A 1 48  ? 18.635 4.677   -0.581  0.48 12.02 ?  48  GLY   A HA3  1 
ATOM   1323 H HA3  B GLY   A 1 48  ? 18.292 4.790   -0.225  0.52 11.53 ?  48  GLY   A HA3  1 
ATOM   1324 N N    A VAL   A 1 49  ? 18.882 3.740   1.716   0.48 10.31 ?  49  VAL   A N    1 
ATOM   1325 N N    B VAL   A 1 49  ? 18.904 3.761   1.895   0.52 9.55  ?  49  VAL   A N    1 
ATOM   1326 C CA   A VAL   A 1 49  ? 19.387 3.342   3.030   0.48 10.50 ?  49  VAL   A CA   1 
ATOM   1327 C CA   B VAL   A 1 49  ? 19.499 3.225   3.118   0.52 9.38  ?  49  VAL   A CA   1 
ATOM   1328 C C    A VAL   A 1 49  ? 20.708 4.040   3.331   0.48 9.79  ?  49  VAL   A C    1 
ATOM   1329 C C    B VAL   A 1 49  ? 20.752 4.004   3.496   0.52 8.63  ?  49  VAL   A C    1 
ATOM   1330 O O    A VAL   A 1 49  ? 20.936 4.500   4.454   0.48 10.17 ?  49  VAL   A O    1 
ATOM   1331 O O    B VAL   A 1 49  ? 20.932 4.398   4.652   0.52 8.37  ?  49  VAL   A O    1 
ATOM   1332 C CB   A VAL   A 1 49  ? 19.524 1.810   3.119   0.48 11.07 ?  49  VAL   A CB   1 
ATOM   1333 C CB   B VAL   A 1 49  ? 19.813 1.728   2.940   0.52 9.42  ?  49  VAL   A CB   1 
ATOM   1334 C CG1  A VAL   A 1 49  ? 20.304 1.412   4.373   0.48 10.85 ?  49  VAL   A CG1  1 
ATOM   1335 C CG1  B VAL   A 1 49  ? 20.664 1.227   4.088   0.52 9.05  ?  49  VAL   A CG1  1 
ATOM   1336 C CG2  A VAL   A 1 49  ? 18.158 1.151   3.112   0.48 12.23 ?  49  VAL   A CG2  1 
ATOM   1337 C CG2  B VAL   A 1 49  ? 18.531 0.915   2.827   0.52 10.20 ?  49  VAL   A CG2  1 
ATOM   1338 H H    A VAL   A 1 49  ? 18.739 3.089   1.177   0.48 12.35 ?  49  VAL   A H    1 
ATOM   1339 H H    B VAL   A 1 49  ? 18.774 3.171   1.286   0.52 11.43 ?  49  VAL   A H    1 
ATOM   1340 H HA   A VAL   A 1 49  ? 18.745 3.615   3.706   0.48 12.58 ?  49  VAL   A HA   1 
ATOM   1341 H HA   B VAL   A 1 49  ? 18.864 3.310   3.848   0.52 11.23 ?  49  VAL   A HA   1 
ATOM   1342 H HB   A VAL   A 1 49  ? 20.020 1.490   2.348   0.48 13.27 ?  49  VAL   A HB   1 
ATOM   1343 H HB   B VAL   A 1 49  ? 20.315 1.606   2.120   0.52 11.28 ?  49  VAL   A HB   1 
ATOM   1344 H HG11 A VAL   A 1 49  ? 20.140 0.475   4.563   0.48 12.99 ?  49  VAL   A HG11 1 
ATOM   1345 H HG11 B VAL   A 1 49  ? 20.605 0.260   4.128   0.52 10.84 ?  49  VAL   A HG11 1 
ATOM   1346 H HG12 A VAL   A 1 49  ? 21.252 1.555   4.223   0.48 12.99 ?  49  VAL   A HG12 1 
ATOM   1347 H HG12 B VAL   A 1 49  ? 21.589 1.490   3.938   0.52 10.84 ?  49  VAL   A HG12 1 
ATOM   1348 H HG13 A VAL   A 1 49  ? 20.001 1.955   5.120   0.48 12.99 ?  49  VAL   A HG13 1 
ATOM   1349 H HG13 B VAL   A 1 49  ? 20.341 1.612   4.916   0.52 10.84 ?  49  VAL   A HG13 1 
ATOM   1350 H HG21 A VAL   A 1 49  ? 18.274 0.189   3.162   0.48 14.65 ?  49  VAL   A HG21 1 
ATOM   1351 H HG21 B VAL   A 1 49  ? 18.755 -0.021  2.711   0.52 12.22 ?  49  VAL   A HG21 1 
ATOM   1352 H HG22 A VAL   A 1 49  ? 17.655 1.465   3.879   0.48 14.65 ?  49  VAL   A HG22 1 
ATOM   1353 H HG22 B VAL   A 1 49  ? 18.010 1.031   3.640   0.52 12.22 ?  49  VAL   A HG22 1 
ATOM   1354 H HG23 A VAL   A 1 49  ? 17.701 1.389   2.293   0.48 14.65 ?  49  VAL   A HG23 1 
ATOM   1355 H HG23 B VAL   A 1 49  ? 18.022 1.231   2.064   0.52 12.22 ?  49  VAL   A HG23 1 
ATOM   1356 N N    A ALA   A 1 50  ? 21.610 4.094   2.348   0.48 9.00  ?  50  ALA   A N    1 
ATOM   1357 N N    B ALA   A 1 50  ? 21.663 4.183   2.536   0.52 8.27  ?  50  ALA   A N    1 
ATOM   1358 C CA   A ALA   A 1 50  ? 22.937 4.655   2.585   0.48 8.77  ?  50  ALA   A CA   1 
ATOM   1359 C CA   B ALA   A 1 50  ? 22.965 4.764   2.844   0.52 8.05  ?  50  ALA   A CA   1 
ATOM   1360 C C    A ALA   A 1 50  ? 22.851 6.108   3.027   0.48 8.86  ?  50  ALA   A C    1 
ATOM   1361 C C    B ALA   A 1 50  ? 22.832 6.221   3.255   0.52 8.32  ?  50  ALA   A C    1 
ATOM   1362 O O    A ALA   A 1 50  ? 23.509 6.517   3.988   0.48 8.85  ?  50  ALA   A O    1 
ATOM   1363 O O    B ALA   A 1 50  ? 23.422 6.653   4.252   0.52 8.27  ?  50  ALA   A O    1 
ATOM   1364 C CB   A ALA   A 1 50  ? 23.783 4.532   1.322   0.48 9.05  ?  50  ALA   A CB   1 
ATOM   1365 C CB   B ALA   A 1 50  ? 23.886 4.638   1.634   0.52 7.80  ?  50  ALA   A CB   1 
ATOM   1366 H H    A ALA   A 1 50  ? 21.478 3.816   1.552   0.48 10.77 ?  50  ALA   A H    1 
ATOM   1367 H H    B ALA   A 1 50  ? 21.547 3.982   1.710   0.52 9.91  ?  50  ALA   A H    1 
ATOM   1368 H HA   A ALA   A 1 50  ? 23.374 4.158   3.296   0.48 10.50 ?  50  ALA   A HA   1 
ATOM   1369 H HA   B ALA   A 1 50  ? 23.363 4.282   3.583   0.52 9.64  ?  50  ALA   A HA   1 
ATOM   1370 H HB1  A ALA   A 1 50  ? 24.658 4.914   1.493   0.48 10.84 ?  50  ALA   A HB1  1 
ATOM   1371 H HB1  B ALA   A 1 50  ? 24.749 5.020   1.854   0.52 9.33  ?  50  ALA   A HB1  1 
ATOM   1372 H HB2  A ALA   A 1 50  ? 23.867 3.597   1.090   0.48 10.84 ?  50  ALA   A HB2  1 
ATOM   1373 H HB2  B ALA   A 1 50  ? 23.983 3.701   1.410   0.52 9.33  ?  50  ALA   A HB2  1 
ATOM   1374 H HB3  A ALA   A 1 50  ? 23.345 5.017   0.606   0.48 10.84 ?  50  ALA   A HB3  1 
ATOM   1375 H HB3  B ALA   A 1 50  ? 23.491 5.119   0.887   0.52 9.33  ?  50  ALA   A HB3  1 
ATOM   1376 N N    A GLY   A 1 51  ? 22.052 6.914   2.330   0.48 9.09  ?  51  GLY   A N    1 
ATOM   1377 N N    B GLY   A 1 51  ? 22.061 6.999   2.495   0.52 9.05  ?  51  GLY   A N    1 
ATOM   1378 C CA   A GLY   A 1 51  ? 21.898 8.298   2.741   0.48 9.65  ?  51  GLY   A CA   1 
ATOM   1379 C CA   B GLY   A 1 51  ? 21.888 8.398   2.840   0.52 9.32  ?  51  GLY   A CA   1 
ATOM   1380 C C    A GLY   A 1 51  ? 21.284 8.421   4.123   0.48 9.53  ?  51  GLY   A C    1 
ATOM   1381 C C    B GLY   A 1 51  ? 21.262 8.573   4.208   0.52 8.95  ?  51  GLY   A C    1 
ATOM   1382 O O    A GLY   A 1 51  ? 21.655 9.304   4.901   0.48 10.14 ?  51  GLY   A O    1 
ATOM   1383 O O    B GLY   A 1 51  ? 21.648 9.465   4.970   0.52 9.36  ?  51  GLY   A O    1 
ATOM   1384 H H    A GLY   A 1 51  ? 21.609 6.689   1.633   0.48 10.89 ?  51  GLY   A H    1 
ATOM   1385 H H    B GLY   A 1 51  ? 21.636 6.745   1.793   0.52 10.83 ?  51  GLY   A H    1 
ATOM   1386 H HA2  A GLY   A 1 51  ? 22.764 8.736   2.751   0.48 11.56 ?  51  GLY   A HA2  1 
ATOM   1387 H HA2  B GLY   A 1 51  ? 22.748 8.846   2.835   0.52 11.16 ?  51  GLY   A HA2  1 
ATOM   1388 H HA3  A GLY   A 1 51  ? 21.326 8.762   2.112   0.48 11.56 ?  51  GLY   A HA3  1 
ATOM   1389 H HA3  B GLY   A 1 51  ? 21.315 8.828   2.182   0.52 11.16 ?  51  GLY   A HA3  1 
ATOM   1390 N N    A ALA   A 1 52  ? 20.340 7.531   4.447   0.48 9.82  ?  52  ALA   A N    1 
ATOM   1391 N N    B ALA   A 1 52  ? 20.283 7.723   4.539   0.52 8.77  ?  52  ALA   A N    1 
ATOM   1392 C CA   A ALA   A 1 52  ? 19.674 7.577   5.745   0.48 10.20 ?  52  ALA   A CA   1 
ATOM   1393 C CA   B ALA   A 1 52  ? 19.625 7.821   5.837   0.52 9.40  ?  52  ALA   A CA   1 
ATOM   1394 C C    A ALA   A 1 52  ? 20.625 7.194   6.875   0.48 10.04 ?  52  ALA   A C    1 
ATOM   1395 C C    B ALA   A 1 52  ? 20.543 7.364   6.970   0.52 9.03  ?  52  ALA   A C    1 
ATOM   1396 O O    A ALA   A 1 52  ? 20.685 7.873   7.906   0.48 10.54 ?  52  ALA   A O    1 
ATOM   1397 O O    B ALA   A 1 52  ? 20.588 7.996   8.032   0.52 9.88  ?  52  ALA   A O    1 
ATOM   1398 C CB   A ALA   A 1 52  ? 18.451 6.658   5.728   0.48 10.84 ?  52  ALA   A CB   1 
ATOM   1399 C CB   B ALA   A 1 52  ? 18.316 7.031   5.821   0.52 10.37 ?  52  ALA   A CB   1 
ATOM   1400 H H    A ALA   A 1 52  ? 20.079 6.891   3.941   0.48 11.76 ?  52  ALA   A H    1 
ATOM   1401 H H    B ALA   A 1 52  ? 19.991 7.090   4.030   0.52 10.50 ?  52  ALA   A H    1 
ATOM   1402 H HA   A ALA   A 1 52  ? 19.365 8.478   5.914   0.48 12.22 ?  52  ALA   A HA   1 
ATOM   1403 H HA   B ALA   A 1 52  ? 19.399 8.750   5.990   0.52 11.26 ?  52  ALA   A HA   1 
ATOM   1404 H HB1  A ALA   A 1 52  ? 18.004 6.703   6.590   0.48 12.98 ?  52  ALA   A HB1  1 
ATOM   1405 H HB1  B ALA   A 1 52  ? 17.886 7.115   6.688   0.52 12.43 ?  52  ALA   A HB1  1 
ATOM   1406 H HB2  A ALA   A 1 52  ? 17.845 6.953   5.030   0.48 12.98 ?  52  ALA   A HB2  1 
ATOM   1407 H HB2  B ALA   A 1 52  ? 17.734 7.387   5.130   0.52 12.43 ?  52  ALA   A HB2  1 
ATOM   1408 H HB3  A ALA   A 1 52  ? 18.737 5.748   5.553   0.48 12.98 ?  52  ALA   A HB3  1 
ATOM   1409 H HB3  B ALA   A 1 52  ? 18.509 6.097   5.639   0.52 12.43 ?  52  ALA   A HB3  1 
ATOM   1410 N N    A LEU   A 1 53  ? 21.366 6.096   6.714   0.48 9.66  ?  53  LEU   A N    1 
ATOM   1411 N N    B LEU   A 1 53  ? 21.271 6.260   6.779   0.52 8.63  ?  53  LEU   A N    1 
ATOM   1412 C CA   A LEU   A 1 53  ? 22.310 5.704   7.757   0.48 9.79  ?  53  LEU   A CA   1 
ATOM   1413 C CA   B LEU   A 1 53  ? 22.246 5.846   7.787   0.52 8.84  ?  53  LEU   A CA   1 
ATOM   1414 C C    A LEU   A 1 53  ? 23.365 6.779   7.961   0.48 9.35  ?  53  LEU   A C    1 
ATOM   1415 C C    B LEU   A 1 53  ? 23.292 6.931   7.991   0.52 8.34  ?  53  LEU   A C    1 
ATOM   1416 O O    A LEU   A 1 53  ? 23.754 7.070   9.097   0.48 9.78  ?  53  LEU   A O    1 
ATOM   1417 O O    B LEU   A 1 53  ? 23.556 7.350   9.122   0.52 8.72  ?  53  LEU   A O    1 
ATOM   1418 C CB   A LEU   A 1 53  ? 22.976 4.374   7.404   0.48 10.33 ?  53  LEU   A CB   1 
ATOM   1419 C CB   B LEU   A 1 53  ? 22.938 4.540   7.380   0.52 9.69  ?  53  LEU   A CB   1 
ATOM   1420 C CG   A LEU   A 1 53  ? 22.046 3.158   7.418   0.48 10.92 ?  53  LEU   A CG   1 
ATOM   1421 C CG   B LEU   A 1 53  ? 22.225 3.184   7.489   0.52 9.98  ?  53  LEU   A CG   1 
ATOM   1422 C CD1  A LEU   A 1 53  ? 22.770 1.943   6.880   0.48 10.93 ?  53  LEU   A CD1  1 
ATOM   1423 C CD1  B LEU   A 1 53  ? 23.080 2.097   6.843   0.52 10.49 ?  53  LEU   A CD1  1 
ATOM   1424 C CD2  A LEU   A 1 53  ? 21.518 2.889   8.819   0.48 11.53 ?  53  LEU   A CD2  1 
ATOM   1425 C CD2  B LEU   A 1 53  ? 21.911 2.811   8.929   0.52 10.16 ?  53  LEU   A CD2  1 
ATOM   1426 H H    A LEU   A 1 53  ? 21.342 5.576   6.030   0.48 11.57 ?  53  LEU   A H    1 
ATOM   1427 H H    B LEU   A 1 53  ? 21.216 5.747   6.094   0.52 10.34 ?  53  LEU   A H    1 
ATOM   1428 H HA   A LEU   A 1 53  ? 21.832 5.588   8.594   0.48 11.73 ?  53  LEU   A HA   1 
ATOM   1429 H HA   B LEU   A 1 53  ? 21.790 5.703   8.630   0.52 10.59 ?  53  LEU   A HA   1 
ATOM   1430 H HB2  A LEU   A 1 53  ? 23.352 4.443   6.510   0.48 12.37 ?  53  LEU   A HB2  1 
ATOM   1431 H HB2  B LEU   A 1 53  ? 23.196 4.634   6.450   0.52 11.61 ?  53  LEU   A HB2  1 
ATOM   1432 H HB3  A LEU   A 1 53  ? 23.687 4.202   8.040   0.48 12.37 ?  53  LEU   A HB3  1 
ATOM   1433 H HB3  B LEU   A 1 53  ? 23.739 4.465   7.917   0.52 11.61 ?  53  LEU   A HB3  1 
ATOM   1434 H HG   A LEU   A 1 53  ? 21.287 3.334   6.837   0.48 13.09 ?  53  LEU   A HG   1 
ATOM   1435 H HG   B LEU   A 1 53  ? 21.389 3.228   7.000   0.52 11.95 ?  53  LEU   A HG   1 
ATOM   1436 H HD11 A LEU   A 1 53  ? 22.168 1.186   6.896   0.48 13.10 ?  53  LEU   A HD11 1 
ATOM   1437 H HD11 B LEU   A 1 53  ? 22.620 1.246   6.922   0.52 12.57 ?  53  LEU   A HD11 1 
ATOM   1438 H HD12 A LEU   A 1 53  ? 23.056 2.125   5.971   0.48 13.10 ?  53  LEU   A HD12 1 
ATOM   1439 H HD12 B LEU   A 1 53  ? 23.215 2.315   5.908   0.52 12.57 ?  53  LEU   A HD12 1 
ATOM   1440 H HD13 A LEU   A 1 53  ? 23.543 1.768   7.441   0.48 13.10 ?  53  LEU   A HD13 1 
ATOM   1441 H HD13 B LEU   A 1 53  ? 23.934 2.055   7.300   0.52 12.57 ?  53  LEU   A HD13 1 
ATOM   1442 H HD21 A LEU   A 1 53  ? 21.016 2.060   8.813   0.48 13.82 ?  53  LEU   A HD21 1 
ATOM   1443 H HD21 B LEU   A 1 53  ? 21.412 1.979   8.939   0.52 12.17 ?  53  LEU   A HD21 1 
ATOM   1444 H HD22 A LEU   A 1 53  ? 22.269 2.817   9.428   0.48 13.82 ?  53  LEU   A HD22 1 
ATOM   1445 H HD22 B LEU   A 1 53  ? 22.740 2.708   9.418   0.52 12.17 ?  53  LEU   A HD22 1 
ATOM   1446 H HD23 A LEU   A 1 53  ? 20.942 3.621   9.088   0.48 13.82 ?  53  LEU   A HD23 1 
ATOM   1447 H HD23 B LEU   A 1 53  ? 21.377 3.519   9.327   0.52 12.17 ?  53  LEU   A HD23 1 
ATOM   1448 N N    A ASN   A 1 54  ? 23.828 7.391   6.876   0.48 9.31  ?  54  ASN   A N    1 
ATOM   1449 N N    B ASN   A 1 54  ? 23.893 7.403   6.900   0.52 8.74  ?  54  ASN   A N    1 
ATOM   1450 C CA   A ASN   A 1 54  ? 24.891 8.375   7.015   0.48 9.54  ?  54  ASN   A CA   1 
ATOM   1451 C CA   B ASN   A 1 54  ? 24.930 8.414   7.041   0.52 8.97  ?  54  ASN   A CA   1 
ATOM   1452 C C    A ASN   A 1 54  ? 24.393 9.632   7.728   0.48 9.84  ?  54  ASN   A C    1 
ATOM   1453 C C    B ASN   A 1 54  ? 24.394 9.652   7.751   0.52 9.57  ?  54  ASN   A C    1 
ATOM   1454 O O    A ASN   A 1 54  ? 25.094 10.188  8.583   0.48 10.22 ?  54  ASN   A O    1 
ATOM   1455 O O    B ASN   A 1 54  ? 25.066 10.217  8.624   0.52 9.84  ?  54  ASN   A O    1 
ATOM   1456 C CB   A ASN   A 1 54  ? 25.474 8.711   5.651   0.48 9.58  ?  54  ASN   A CB   1 
ATOM   1457 C CB   B ASN   A 1 54  ? 25.504 8.797   5.687   0.52 8.64  ?  54  ASN   A CB   1 
ATOM   1458 C CG   A ASN   A 1 54  ? 26.550 9.760   5.741   0.48 10.03 ?  54  ASN   A CG   1 
ATOM   1459 C CG   B ASN   A 1 54  ? 26.469 9.941   5.803   0.52 8.65  ?  54  ASN   A CG   1 
ATOM   1460 O OD1  A ASN   A 1 54  ? 27.549 9.577   6.438   0.48 10.35 ?  54  ASN   A OD1  1 
ATOM   1461 O OD1  B ASN   A 1 54  ? 27.482 9.825   6.498   0.52 8.38  ?  54  ASN   A OD1  1 
ATOM   1462 N ND2  A ASN   A 1 54  ? 26.355 10.872  5.055   0.48 10.41 ?  54  ASN   A ND2  1 
ATOM   1463 N ND2  B ASN   A 1 54  ? 26.157 11.064  5.168   0.52 9.23  ?  54  ASN   A ND2  1 
ATOM   1464 H H    A ASN   A 1 54  ? 23.546 7.255   6.073   0.48 11.15 ?  54  ASN   A H    1 
ATOM   1465 H H    B ASN   A 1 54  ? 23.716 7.165   6.094   0.52 10.47 ?  54  ASN   A H    1 
ATOM   1466 H HA   A ASN   A 1 54  ? 25.592 7.987   7.555   0.48 11.42 ?  54  ASN   A HA   1 
ATOM   1467 H HA   B ASN   A 1 54  ? 25.645 8.054   7.581   0.52 10.74 ?  54  ASN   A HA   1 
ATOM   1468 H HB2  A ASN   A 1 54  ? 25.859 7.904   5.270   0.48 11.47 ?  54  ASN   A HB2  1 
ATOM   1469 H HB2  B ASN   A 1 54  ? 25.979 8.034   5.321   0.52 10.34 ?  54  ASN   A HB2  1 
ATOM   1470 H HB3  A ASN   A 1 54  ? 24.767 9.044   5.079   0.48 11.47 ?  54  ASN   A HB3  1 
ATOM   1471 H HB3  B ASN   A 1 54  ? 24.783 9.060   5.097   0.52 10.34 ?  54  ASN   A HB3  1 
ATOM   1472 H HD21 A ASN   A 1 54  ? 26.943 11.495  5.080   0.48 12.46 ?  54  ASN   A HD21 1 
ATOM   1473 H HD21 B ASN   A 1 54  ? 26.678 11.747  5.214   0.52 11.05 ?  54  ASN   A HD21 1 
ATOM   1474 H HD22 A ASN   A 1 54  ? 25.643 10.964  4.583   0.48 12.46 ?  54  ASN   A HD22 1 
ATOM   1475 H HD22 B ASN   A 1 54  ? 25.436 11.106  4.699   0.52 11.05 ?  54  ASN   A HD22 1 
ATOM   1476 N N    . LYS   A 1 55  ? 23.185 10.094  7.390   1.00 9.77  ?  55  LYS   A N    1 
ATOM   1477 C CA   . LYS   A 1 55  ? 22.603 11.254  8.058   1.00 10.56 ?  55  LYS   A CA   1 
ATOM   1478 C C    . LYS   A 1 55  ? 22.501 11.018  9.558   1.00 10.45 ?  55  LYS   A C    1 
ATOM   1479 O O    . LYS   A 1 55  ? 22.782 11.916  10.361  1.00 11.27 ?  55  LYS   A O    1 
ATOM   1480 C CB   . LYS   A 1 55  ? 21.235 11.557  7.445   1.00 11.73 ?  55  LYS   A CB   1 
ATOM   1481 C CG   . LYS   A 1 55  ? 20.492 12.727  8.073   1.00 13.56 ?  55  LYS   A CG   1 
ATOM   1482 C CD   . LYS   A 1 55  ? 19.184 12.989  7.323   1.00 15.16 ?  55  LYS   A CD   1 
ATOM   1483 C CE   . LYS   A 1 55  ? 18.329 14.055  7.996   1.00 17.17 ?  55  LYS   A CE   1 
ATOM   1484 N NZ   . LYS   A 1 55  ? 16.996 14.202  7.341   1.00 18.34 ?  55  LYS   A NZ   1 
ATOM   1485 H H    A LYS   A 1 55  ? 22.681 9.752   6.783   0.48 11.70 ?  55  LYS   A H    1 
ATOM   1486 H H    B LYS   A 1 55  ? 22.683 9.737   6.790   0.52 11.70 ?  55  LYS   A H    1 
ATOM   1487 H HA   . LYS   A 1 55  ? 23.176 12.023  7.914   1.00 12.65 ?  55  LYS   A HA   1 
ATOM   1488 H HB2  . LYS   A 1 55  ? 21.356 11.761  6.506   1.00 14.06 ?  55  LYS   A HB2  1 
ATOM   1489 H HB3  . LYS   A 1 55  ? 20.673 10.772  7.540   1.00 14.06 ?  55  LYS   A HB3  1 
ATOM   1490 H HG2  . LYS   A 1 55  ? 20.278 12.515  8.995   1.00 16.24 ?  55  LYS   A HG2  1 
ATOM   1491 H HG3  . LYS   A 1 55  ? 21.044 13.521  8.024   1.00 16.24 ?  55  LYS   A HG3  1 
ATOM   1492 H HD2  . LYS   A 1 55  ? 19.399 13.287  6.422   1.00 18.16 ?  55  LYS   A HD2  1 
ATOM   1493 H HD3  . LYS   A 1 55  ? 18.676 12.163  7.283   1.00 18.16 ?  55  LYS   A HD3  1 
ATOM   1494 H HE2  . LYS   A 1 55  ? 18.187 13.805  8.920   1.00 20.58 ?  55  LYS   A HE2  1 
ATOM   1495 H HE3  . LYS   A 1 55  ? 18.789 14.906  7.943   1.00 20.58 ?  55  LYS   A HE3  1 
ATOM   1496 H HZ1  . LYS   A 1 55  ? 16.442 14.652  7.874   1.00 21.98 ?  55  LYS   A HZ1  1 
ATOM   1497 H HZ2  . LYS   A 1 55  ? 17.076 14.649  6.573   1.00 21.98 ?  55  LYS   A HZ2  1 
ATOM   1498 H HZ3  . LYS   A 1 55  ? 16.642 13.402  7.172   1.00 21.98 ?  55  LYS   A HZ3  1 
ATOM   1499 N N    . ALA   A 1 56  ? 22.112 9.807   9.960   1.00 10.83 ?  56  ALA   A N    1 
ATOM   1500 C CA   . ALA   A 1 56  ? 21.976 9.497   11.376  1.00 11.10 ?  56  ALA   A CA   1 
ATOM   1501 C C    . ALA   A 1 56  ? 23.311 9.519   12.110  1.00 11.29 ?  56  ALA   A C    1 
ATOM   1502 O O    . ALA   A 1 56  ? 23.324 9.699   13.329  1.00 12.71 ?  56  ALA   A O    1 
ATOM   1503 C CB   . ALA   A 1 56  ? 21.265 8.153   11.562  1.00 12.27 ?  56  ALA   A CB   1 
ATOM   1504 H H    . ALA   A 1 56  ? 21.926 9.161   9.434   1.00 12.97 ?  56  ALA   A H    1 
ATOM   1505 H HA   . ALA   A 1 56  ? 21.429 10.169  11.791  1.00 13.29 ?  56  ALA   A HA   1 
ATOM   1506 H HB1  . ALA   A 1 56  ? 21.192 7.961   12.512  1.00 14.70 ?  56  ALA   A HB1  1 
ATOM   1507 H HB2  . ALA   A 1 56  ? 20.377 8.216   11.172  1.00 14.70 ?  56  ALA   A HB2  1 
ATOM   1508 H HB3  . ALA   A 1 56  ? 21.771 7.456   11.122  1.00 14.70 ?  56  ALA   A HB3  1 
ATOM   1509 N N    . THR   A 1 57  ? 24.430 9.327   11.402  1.00 10.52 ?  57  THR   A N    1 
ATOM   1510 C CA   . THR   A 1 57  ? 25.769 9.454   11.982  1.00 10.80 ?  57  THR   A CA   1 
ATOM   1511 C C    . THR   A 1 57  ? 26.318 10.875  11.912  1.00 11.02 ?  57  THR   A C    1 
ATOM   1512 O O    . THR   A 1 57  ? 27.502 11.084  12.213  1.00 11.65 ?  57  THR   A O    1 
ATOM   1513 C CB   . THR   A 1 57  ? 26.782 8.504   11.311  1.00 10.71 ?  57  THR   A CB   1 
ATOM   1514 O OG1  . THR   A 1 57  ? 27.169 9.003   10.018  1.00 10.15 ?  57  THR   A OG1  1 
ATOM   1515 C CG2  . THR   A 1 57  ? 26.256 7.073   11.213  1.00 10.48 ?  57  THR   A CG2  1 
ATOM   1516 H H    . THR   A 1 57  ? 24.442 9.096   10.567  1.00 12.60 ?  57  THR   A H    1 
ATOM   1517 H HA   . THR   A 1 57  ? 25.723 9.197   12.919  1.00 12.94 ?  57  THR   A HA   1 
ATOM   1518 H HB   . THR   A 1 57  ? 27.581 8.469   11.871  1.00 12.83 ?  57  THR   A HB   1 
ATOM   1519 H HG1  . THR   A 1 57  ? 26.493 9.070   9.527   1.00 12.15 ?  57  THR   A HG1  1 
ATOM   1520 H HG21 . THR   A 1 57  ? 26.904 6.508   10.757  1.00 12.56 ?  57  THR   A HG21 1 
ATOM   1521 H HG22 . THR   A 1 57  ? 26.099 6.711   12.100  1.00 12.56 ?  57  THR   A HG22 1 
ATOM   1522 H HG23 . THR   A 1 57  ? 25.426 7.055   10.716  1.00 12.56 ?  57  THR   A HG23 1 
ATOM   1523 N N    . ASN   A 1 58  ? 25.505 11.846  11.497  1.00 11.43 ?  58  ASN   A N    1 
ATOM   1524 C CA   . ASN   A 1 58  ? 25.968 13.225  11.393  1.00 12.46 ?  58  ASN   A CA   1 
ATOM   1525 C C    . ASN   A 1 58  ? 27.124 13.348  10.398  1.00 10.94 ?  58  ASN   A C    1 
ATOM   1526 O O    . ASN   A 1 58  ? 28.016 14.186  10.560  1.00 12.02 ?  58  ASN   A O    1 
ATOM   1527 C CB   . ASN   A 1 58  ? 26.333 13.778  12.782  1.00 15.30 ?  58  ASN   A CB   1 
ATOM   1528 C CG   . ASN   A 1 58  ? 26.675 15.253  12.768  1.00 19.71 ?  58  ASN   A CG   1 
ATOM   1529 O OD1  . ASN   A 1 58  ? 26.039 16.040  12.075  1.00 21.51 ?  58  ASN   A OD1  1 
ATOM   1530 N ND2  . ASN   A 1 58  ? 27.677 15.640  13.552  1.00 21.46 ?  58  ASN   A ND2  1 
ATOM   1531 H H    . ASN   A 1 58  ? 24.685 11.720  11.258  1.00 13.69 ?  58  ASN   A H    1 
ATOM   1532 H HA   . ASN   A 1 58  ? 25.235 13.754  11.052  1.00 14.93 ?  58  ASN   A HA   1 
ATOM   1533 H HB2  . ASN   A 1 58  ? 25.573 13.646  13.380  1.00 18.34 ?  58  ASN   A HB2  1 
ATOM   1534 H HB3  . ASN   A 1 58  ? 27.102 13.303  13.124  1.00 18.34 ?  58  ASN   A HB3  1 
ATOM   1535 H HD21 . ASN   A 1 58  ? 27.896 16.474  13.580  1.00 25.73 ?  58  ASN   A HD21 1 
ATOM   1536 H HD22 . ASN   A 1 58  ? 28.089 15.066  14.029  1.00 25.73 ?  58  ASN   A HD22 1 
ATOM   1537 N N    . ASN   A 1 59  ? 27.110 12.528  9.344   1.00 10.42 ?  59  ASN   A N    1 
ATOM   1538 C CA   . ASN   A 1 59  ? 28.105 12.500  8.264   1.00 9.87  ?  59  ASN   A CA   1 
ATOM   1539 C C    . ASN   A 1 59  ? 29.417 11.822  8.664   1.00 9.84  ?  59  ASN   A C    1 
ATOM   1540 O O    . ASN   A 1 59  ? 30.338 11.774  7.844   1.00 10.16 ?  59  ASN   A O    1 
ATOM   1541 C CB   . ASN   A 1 59  ? 28.401 13.886  7.659   1.00 10.41 ?  59  ASN   A CB   1 
ATOM   1542 C CG   . ASN   A 1 59  ? 28.766 13.816  6.187   1.00 10.57 ?  59  ASN   A CG   1 
ATOM   1543 O OD1  . ASN   A 1 59  ? 28.060 13.196  5.389   1.00 11.18 ?  59  ASN   A OD1  1 
ATOM   1544 N ND2  . ASN   A 1 59  ? 29.854 14.478  5.810   1.00 11.23 ?  59  ASN   A ND2  1 
ATOM   1545 H H    . ASN   A 1 59  ? 26.493 11.937  9.223   1.00 12.48 ?  59  ASN   A H    1 
ATOM   1546 H HA   . ASN   A 1 59  ? 27.731 11.972  7.547   1.00 11.83 ?  59  ASN   A HA   1 
ATOM   1547 H HB2  . ASN   A 1 59  ? 27.617 14.451  7.743   1.00 12.47 ?  59  ASN   A HB2  1 
ATOM   1548 H HB3  . ASN   A 1 59  ? 29.151 14.289  8.126   1.00 12.47 ?  59  ASN   A HB3  1 
ATOM   1549 H HD21 . ASN   A 1 59  ? 30.102 14.478  4.983   1.00 13.45 ?  59  ASN   A HD21 1 
ATOM   1550 H HD22 . ASN   A 1 59  ? 30.328 14.909  6.391   1.00 13.45 ?  59  ASN   A HD22 1 
ATOM   1551 N N    . ALA   A 1 60  ? 29.531 11.277  9.874   1.00 10.05 ?  60  ALA   A N    1 
ATOM   1552 C CA   . ALA   A 1 60  ? 30.763 10.589  10.240  1.00 10.23 ?  60  ALA   A CA   1 
ATOM   1553 C C    . ALA   A 1 60  ? 30.993 9.353   9.376   1.00 10.22 ?  60  ALA   A C    1 
ATOM   1554 O O    . ALA   A 1 60  ? 32.141 9.035   9.044   1.00 10.57 ?  60  ALA   A O    1 
ATOM   1555 C CB   . ALA   A 1 60  ? 30.752 10.235  11.724  1.00 11.11 ?  60  ALA   A CB   1 
ATOM   1556 H H    . ALA   A 1 60  ? 28.924 11.289  10.485  1.00 12.04 ?  60  ALA   A H    1 
ATOM   1557 H HA   . ALA   A 1 60  ? 31.508 11.195  10.089  1.00 12.25 ?  60  ALA   A HA   1 
ATOM   1558 H HB1  . ALA   A 1 60  ? 31.576 9.784   11.949  1.00 13.30 ?  60  ALA   A HB1  1 
ATOM   1559 H HB2  . ALA   A 1 60  ? 30.668 11.054  12.243  1.00 13.30 ?  60  ALA   A HB2  1 
ATOM   1560 H HB3  . ALA   A 1 60  ? 29.993 9.657   11.903  1.00 13.30 ?  60  ALA   A HB3  1 
ATOM   1561 N N    . MET   A 1 61  ? 29.924 8.659   8.984   1.00 9.49  ?  61  MET   A N    1 
ATOM   1562 C CA   . MET   A 1 61  ? 30.065 7.518   8.083   1.00 9.36  ?  61  MET   A CA   1 
ATOM   1563 C C    . MET   A 1 61  ? 30.701 7.942   6.759   1.00 9.44  ?  61  MET   A C    1 
ATOM   1564 O O    . MET   A 1 61  ? 31.602 7.264   6.249   1.00 9.92  ?  61  MET   A O    1 
ATOM   1565 C CB   . MET   A 1 61  ? 28.703 6.855   7.869   1.00 9.67  ?  61  MET   A CB   1 
ATOM   1566 C CG   . MET   A 1 61  ? 28.719 5.687   6.899   1.00 10.12 ?  61  MET   A CG   1 
ATOM   1567 S SD   . MET   A 1 61  ? 27.104 4.937   6.673   1.00 10.91 ?  61  MET   A SD   1 
ATOM   1568 C CE   . MET   A 1 61  ? 26.973 4.053   8.237   1.00 12.04 ?  61  MET   A CE   1 
ATOM   1569 H H    . MET   A 1 61  ? 29.113 8.826   9.220   1.00 11.36 ?  61  MET   A H    1 
ATOM   1570 H HA   . MET   A 1 61  ? 30.645 6.863   8.506   1.00 11.20 ?  61  MET   A HA   1 
ATOM   1571 H HB2  . MET   A 1 61  ? 28.382 6.528   8.723   1.00 11.58 ?  61  MET   A HB2  1 
ATOM   1572 H HB3  . MET   A 1 61  ? 28.087 7.517   7.521   1.00 11.58 ?  61  MET   A HB3  1 
ATOM   1573 H HG2  . MET   A 1 61  ? 29.017 5.983   6.030   1.00 12.12 ?  61  MET   A HG2  1 
ATOM   1574 H HG3  . MET   A 1 61  ? 29.310 4.994   7.239   1.00 12.12 ?  61  MET   A HG3  1 
ATOM   1575 H HE1  . MET   A 1 61  ? 26.135 3.567   8.253   1.00 14.42 ?  61  MET   A HE1  1 
ATOM   1576 H HE2  . MET   A 1 61  ? 27.718 3.445   8.316   1.00 14.42 ?  61  MET   A HE2  1 
ATOM   1577 H HE3  . MET   A 1 61  ? 26.991 4.698   8.968   1.00 14.42 ?  61  MET   A HE3  1 
ATOM   1578 N N    . GLN   A 1 62  ? 30.266 9.073   6.199   1.00 9.46  ?  62  GLN   A N    1 
ATOM   1579 C CA   . GLN   A 1 62  ? 30.838 9.536   4.938   1.00 9.66  ?  62  GLN   A CA   1 
ATOM   1580 C C    . GLN   A 1 62  ? 32.305 9.918   5.095   1.00 9.72  ?  62  GLN   A C    1 
ATOM   1581 O O    . GLN   A 1 62  ? 33.122 9.596   4.228   1.00 10.01 ?  62  GLN   A O    1 
ATOM   1582 C CB   . GLN   A 1 62  ? 30.047 10.722  4.390   1.00 9.55  ?  62  GLN   A CB   1 
ATOM   1583 C CG   . GLN   A 1 62  ? 30.437 11.082  2.963   1.00 9.85  ?  62  GLN   A CG   1 
ATOM   1584 C CD   . GLN   A 1 62  ? 30.103 9.951   2.013   1.00 9.82  ?  62  GLN   A CD   1 
ATOM   1585 O OE1  . GLN   A 1 62  ? 28.925 9.649   1.799   1.00 10.52 ?  62  GLN   A OE1  1 
ATOM   1586 N NE2  . GLN   A 1 62  ? 31.121 9.277   1.487   1.00 10.36 ?  62  GLN   A NE2  1 
ATOM   1587 H H    . GLN   A 1 62  ? 29.645 9.572   6.521   1.00 11.33 ?  62  GLN   A H    1 
ATOM   1588 H HA   . GLN   A 1 62  ? 30.789 8.815   4.294   1.00 11.57 ?  62  GLN   A HA   1 
ATOM   1589 H HB2  . GLN   A 1 62  ? 29.105 10.509  4.404   1.00 11.44 ?  62  GLN   A HB2  1 
ATOM   1590 H HB3  . GLN   A 1 62  ? 30.222 11.501  4.946   1.00 11.44 ?  62  GLN   A HB3  1 
ATOM   1591 H HG2  . GLN   A 1 62  ? 29.935 11.859  2.681   1.00 11.79 ?  62  GLN   A HG2  1 
ATOM   1592 H HG3  . GLN   A 1 62  ? 31.386 11.247  2.914   1.00 11.79 ?  62  GLN   A HG3  1 
ATOM   1593 H HE21 . GLN   A 1 62  ? 31.930 9.504   1.676   1.00 12.41 ?  62  GLN   A HE21 1 
ATOM   1594 H HE22 . GLN   A 1 62  ? 30.976 8.619   0.951   1.00 12.41 ?  62  GLN   A HE22 1 
ATOM   1595 N N    . VAL   A 1 63  ? 32.659 10.605  6.185   1.00 10.13 ?  63  VAL   A N    1 
ATOM   1596 C CA   . VAL   A 1 63  ? 34.050 10.994  6.405   1.00 10.66 ?  63  VAL   A CA   1 
ATOM   1597 C C    . VAL   A 1 63  ? 34.945 9.757   6.475   1.00 10.23 ?  63  VAL   A C    1 
ATOM   1598 O O    . VAL   A 1 63  ? 36.006 9.687   5.836   1.00 10.79 ?  63  VAL   A O    1 
ATOM   1599 C CB   . VAL   A 1 63  ? 34.148 11.869  7.668   1.00 12.11 ?  63  VAL   A CB   1 
ATOM   1600 C CG1  . VAL   A 1 63  ? 35.590 12.093  8.059   1.00 14.14 ?  63  VAL   A CG1  1 
ATOM   1601 C CG2  . VAL   A 1 63  ? 33.439 13.208  7.435   1.00 12.64 ?  63  VAL   A CG2  1 
ATOM   1602 H H    . VAL   A 1 63  ? 32.110 10.853  6.806   1.00 12.14 ?  63  VAL   A H    1 
ATOM   1603 H HA   . VAL   A 1 63  ? 34.339 11.531  5.654   1.00 12.77 ?  63  VAL   A HA   1 
ATOM   1604 H HB   . VAL   A 1 63  ? 33.705 11.423  8.406   1.00 14.50 ?  63  VAL   A HB   1 
ATOM   1605 H HG11 . VAL   A 1 63  ? 35.634 12.832  8.687   1.00 16.94 ?  63  VAL   A HG11 1 
ATOM   1606 H HG12 . VAL   A 1 63  ? 35.937 11.289  8.468   1.00 16.94 ?  63  VAL   A HG12 1 
ATOM   1607 H HG13 . VAL   A 1 63  ? 36.100 12.312  7.261   1.00 16.94 ?  63  VAL   A HG13 1 
ATOM   1608 H HG21 . VAL   A 1 63  ? 33.521 13.754  8.236   1.00 15.14 ?  63  VAL   A HG21 1 
ATOM   1609 H HG22 . VAL   A 1 63  ? 33.860 13.662  6.686   1.00 15.14 ?  63  VAL   A HG22 1 
ATOM   1610 H HG23 . VAL   A 1 63  ? 32.506 13.044  7.241   1.00 15.14 ?  63  VAL   A HG23 1 
ATOM   1611 N N    . GLU   A 1 64  ? 34.517 8.751   7.243   1.00 10.19 ?  64  GLU   A N    1 
ATOM   1612 C CA   . GLU   A 1 64  ? 35.276 7.511   7.345   1.00 10.36 ?  64  GLU   A CA   1 
ATOM   1613 C C    . GLU   A 1 64  ? 35.374 6.823   5.990   1.00 10.15 ?  64  GLU   A C    1 
ATOM   1614 O O    . GLU   A 1 64  ? 36.426 6.278   5.624   1.00 10.48 ?  64  GLU   A O    1 
ATOM   1615 C CB   . GLU   A 1 64  ? 34.580 6.598   8.358   1.00 11.04 ?  64  GLU   A CB   1 
ATOM   1616 C CG   . GLU   A 1 64  ? 35.236 5.252   8.517   1.00 11.75 ?  64  GLU   A CG   1 
ATOM   1617 C CD   . GLU   A 1 64  ? 34.359 4.258   9.239   1.00 12.17 ?  64  GLU   A CD   1 
ATOM   1618 O OE1  . GLU   A 1 64  ? 33.122 4.355   9.098   1.00 12.73 ?  64  GLU   A OE1  1 
ATOM   1619 O OE2  . GLU   A 1 64  ? 34.906 3.368   9.929   1.00 12.60 -1 64  GLU   A OE2  1 
ATOM   1620 H H    . GLU   A 1 64  ? 33.784 8.760   7.696   1.00 12.21 ?  64  GLU   A H    1 
ATOM   1621 H HA   . GLU   A 1 64  ? 36.171 7.711   7.667   1.00 12.41 ?  64  GLU   A HA   1 
ATOM   1622 H HB2  . GLU   A 1 64  ? 34.588 7.038   9.228   1.00 13.22 ?  64  GLU   A HB2  1 
ATOM   1623 H HB3  . GLU   A 1 64  ? 33.665 6.464   8.071   1.00 13.22 ?  64  GLU   A HB3  1 
ATOM   1624 H HG2  . GLU   A 1 64  ? 35.438 4.883   7.641   1.00 14.07 ?  64  GLU   A HG2  1 
ATOM   1625 H HG3  . GLU   A 1 64  ? 36.048 5.356   9.028   1.00 14.07 ?  64  GLU   A HG3  1 
ATOM   1626 N N    . SER   A 1 65  ? 34.265 6.816   5.247   1.00 9.78  ?  65  SER   A N    1 
ATOM   1627 C CA   . SER   A 1 65  ? 34.220 6.154   3.949   1.00 9.89  ?  65  SER   A CA   1 
ATOM   1628 C C    . SER   A 1 65  ? 35.145 6.818   2.938   1.00 9.93  ?  65  SER   A C    1 
ATOM   1629 O O    . SER   A 1 65  ? 35.783 6.132   2.134   1.00 10.83 ?  65  SER   A O    1 
ATOM   1630 C CB   . SER   A 1 65  ? 32.785 6.156   3.412   1.00 9.86  ?  65  SER   A CB   1 
ATOM   1631 O OG   . SER   A 1 65  ? 31.932 5.340   4.207   1.00 10.17 ?  65  SER   A OG   1 
ATOM   1632 H H    . SER   A 1 65  ? 33.531 7.200   5.473   1.00 11.71 ?  65  SER   A H    1 
ATOM   1633 H HA   . SER   A 1 65  ? 34.504 5.237   4.056   1.00 11.84 ?  65  SER   A HA   1 
ATOM   1634 H HB2  . SER   A 1 65  ? 32.442 7.060   3.420   1.00 11.81 ?  65  SER   A HB2  1 
ATOM   1635 H HB3  . SER   A 1 65  ? 32.792 5.810   2.507   1.00 11.81 ?  65  SER   A HB3  1 
ATOM   1636 H HG   . SER   A 1 65  ? 31.922 5.623   5.001   1.00 12.19 ?  65  SER   A HG   1 
ATOM   1637 N N    . ASP   A 1 66  ? 35.219 8.153   2.948   1.00 9.96  ?  66  ASP   A N    1 
ATOM   1638 C CA   . ASP   A 1 66  ? 36.085 8.848   2.001   1.00 10.93 ?  66  ASP   A CA   1 
ATOM   1639 C C    . ASP   A 1 66  ? 37.546 8.498   2.256   1.00 11.06 ?  66  ASP   A C    1 
ATOM   1640 O O    . ASP   A 1 66  ? 38.324 8.325   1.313   1.00 11.96 ?  66  ASP   A O    1 
ATOM   1641 C CB   . ASP   A 1 66  ? 35.860 10.355  2.092   1.00 12.21 ?  66  ASP   A CB   1 
ATOM   1642 C CG   . ASP   A 1 66  ? 34.525 10.808  1.475   1.00 14.12 ?  66  ASP   A CG   1 
ATOM   1643 O OD1  . ASP   A 1 66  ? 33.828 10.007  0.813   1.00 14.31 ?  66  ASP   A OD1  1 
ATOM   1644 O OD2  . ASP   A 1 66  ? 34.219 12.010  1.626   1.00 17.02 -1 66  ASP   A OD2  1 
ATOM   1645 H H    . ASP   A 1 66  ? 34.775 8.672   3.478   1.00 11.92 ?  66  ASP   A H    1 
ATOM   1646 H HA   . ASP   A 1 66  ? 35.858 8.562   1.100   1.00 13.10 ?  66  ASP   A HA   1 
ATOM   1647 H HB2  . ASP   A 1 66  ? 35.860 10.617  3.024   1.00 14.63 ?  66  ASP   A HB2  1 
ATOM   1648 H HB3  . ASP   A 1 66  ? 36.585 10.805  1.623   1.00 14.63 ?  66  ASP   A HB3  1 
ATOM   1649 N N    . ASP   A 1 67  ? 37.931 8.373   3.525   1.00 11.14 ?  67  ASP   A N    1 
ATOM   1650 C CA   . ASP   A 1 67  ? 39.285 7.929   3.844   1.00 12.04 ?  67  ASP   A CA   1 
ATOM   1651 C C    . ASP   A 1 67  ? 39.515 6.493   3.382   1.00 12.04 ?  67  ASP   A C    1 
ATOM   1652 O O    . ASP   A 1 67  ? 40.582 6.170   2.845   1.00 12.69 ?  67  ASP   A O    1 
ATOM   1653 C CB   . ASP   A 1 67  ? 39.547 8.079   5.344   1.00 13.04 ?  67  ASP   A CB   1 
ATOM   1654 C CG   . ASP   A 1 67  ? 40.839 7.419   5.780   1.00 14.43 ?  67  ASP   A CG   1 
ATOM   1655 O OD1  . ASP   A 1 67  ? 41.909 8.057   5.664   1.00 17.25 ?  67  ASP   A OD1  1 
ATOM   1656 O OD2  . ASP   A 1 67  ? 40.789 6.254   6.232   1.00 14.49 -1 67  ASP   A OD2  1 
ATOM   1657 H H    . ASP   A 1 67  ? 37.440 8.541   4.207   1.00 13.34 ?  67  ASP   A H    1 
ATOM   1658 H HA   . ASP   A 1 67  ? 39.920 8.493   3.374   1.00 14.42 ?  67  ASP   A HA   1 
ATOM   1659 H HB2  . ASP   A 1 67  ? 39.603 9.021   5.559   1.00 15.63 ?  67  ASP   A HB2  1 
ATOM   1660 H HB3  . ASP   A 1 67  ? 38.819 7.666   5.833   1.00 15.63 ?  67  ASP   A HB3  1 
ATOM   1661 N N    . TYR   A 1 68  ? 38.522 5.616   3.566   1.00 11.58 ?  68  TYR   A N    1 
ATOM   1662 C CA   . TYR   A 1 68  ? 38.652 4.236   3.101   1.00 11.58 ?  68  TYR   A CA   1 
ATOM   1663 C C    . TYR   A 1 68  ? 38.896 4.184   1.594   1.00 11.55 ?  68  TYR   A C    1 
ATOM   1664 O O    . TYR   A 1 68  ? 39.783 3.458   1.123   1.00 12.14 ?  68  TYR   A O    1 
ATOM   1665 C CB   . TYR   A 1 68  ? 37.402 3.412   3.478   1.00 11.96 ?  68  TYR   A CB   1 
ATOM   1666 C CG   . TYR   A 1 68  ? 37.428 2.028   2.844   1.00 13.18 ?  68  TYR   A CG   1 
ATOM   1667 C CD1  . TYR   A 1 68  ? 36.976 1.841   1.542   1.00 14.02 ?  68  TYR   A CD1  1 
ATOM   1668 C CD2  . TYR   A 1 68  ? 37.957 0.939   3.514   1.00 14.73 ?  68  TYR   A CD2  1 
ATOM   1669 C CE1  . TYR   A 1 68  ? 37.047 0.626   0.921   1.00 15.74 ?  68  TYR   A CE1  1 
ATOM   1670 C CE2  . TYR   A 1 68  ? 38.016 -0.318  2.895   1.00 15.64 ?  68  TYR   A CE2  1 
ATOM   1671 C CZ   . TYR   A 1 68  ? 37.572 -0.445  1.597   1.00 16.13 ?  68  TYR   A CZ   1 
ATOM   1672 O OH   . TYR   A 1 68  ? 37.648 -1.656  0.962   1.00 17.54 ?  68  TYR   A OH   1 
ATOM   1673 H H    . TYR   A 1 68  ? 37.774 5.795   3.955   1.00 13.87 ?  68  TYR   A H    1 
ATOM   1674 H HA   . TYR   A 1 68  ? 39.413 3.830   3.539   1.00 13.87 ?  68  TYR   A HA   1 
ATOM   1675 H HB2  . TYR   A 1 68  ? 37.370 3.303   4.442   1.00 14.33 ?  68  TYR   A HB2  1 
ATOM   1676 H HB3  . TYR   A 1 68  ? 36.607 3.876   3.168   1.00 14.33 ?  68  TYR   A HB3  1 
ATOM   1677 H HD1  . TYR   A 1 68  ? 36.639 2.575   1.072   1.00 16.80 ?  68  TYR   A HD1  1 
ATOM   1678 H HD2  . TYR   A 1 68  ? 38.279 1.042   4.377   1.00 17.66 ?  68  TYR   A HD2  1 
ATOM   1679 H HE1  . TYR   A 1 68  ? 36.738 0.534   0.049   1.00 18.86 ?  68  TYR   A HE1  1 
ATOM   1680 H HE2  . TYR   A 1 68  ? 38.381 -1.049  3.334   1.00 18.75 ?  68  TYR   A HE2  1 
ATOM   1681 H HH   . TYR   A 1 68  ? 37.977 -2.231  1.479   1.00 21.02 ?  68  TYR   A HH   1 
ATOM   1682 N N    . ILE   A 1 69  ? 38.113 4.945   0.818   1.00 10.88 ?  69  ILE   A N    1 
ATOM   1683 C CA   . ILE   A 1 69  ? 38.253 4.929   -0.637  1.00 11.27 ?  69  ILE   A CA   1 
ATOM   1684 C C    . ILE   A 1 69  ? 39.590 5.531   -1.062  1.00 11.32 ?  69  ILE   A C    1 
ATOM   1685 O O    . ILE   A 1 69  ? 40.239 5.046   -1.997  1.00 11.83 ?  69  ILE   A O    1 
ATOM   1686 C CB   . ILE   A 1 69  ? 37.064 5.648   -1.304  1.00 11.93 ?  69  ILE   A CB   1 
ATOM   1687 C CG1  . ILE   A 1 69  ? 35.748 4.911   -1.034  1.00 12.12 ?  69  ILE   A CG1  1 
ATOM   1688 C CG2  . ILE   A 1 69  ? 37.308 5.826   -2.807  1.00 13.75 ?  69  ILE   A CG2  1 
ATOM   1689 C CD1  . ILE   A 1 69  ? 35.578 3.636   -1.827  1.00 12.91 ?  69  ILE   A CD1  1 
ATOM   1690 H H    . ILE   A 1 69  ? 37.505 5.477   1.111   1.00 13.03 ?  69  ILE   A H    1 
ATOM   1691 H HA   . ILE   A 1 69  ? 38.244 4.006   -0.935  1.00 13.50 ?  69  ILE   A HA   1 
ATOM   1692 H HB   . ILE   A 1 69  ? 36.994 6.529   -0.910  1.00 14.29 ?  69  ILE   A HB   1 
ATOM   1693 H HG12 . ILE   A 1 69  ? 35.711 4.683   -0.088  1.00 14.52 ?  69  ILE   A HG12 1 
ATOM   1694 H HG13 . ILE   A 1 69  ? 35.014 5.505   -1.251  1.00 14.52 ?  69  ILE   A HG13 1 
ATOM   1695 H HG21 . ILE   A 1 69  ? 36.460 6.031   -3.239  1.00 16.48 ?  69  ILE   A HG21 1 
ATOM   1696 H HG22 . ILE   A 1 69  ? 37.927 6.561   -2.944  1.00 16.48 ?  69  ILE   A HG22 1 
ATOM   1697 H HG23 . ILE   A 1 69  ? 37.672 5.008   -3.171  1.00 16.48 ?  69  ILE   A HG23 1 
ATOM   1698 H HD11 . ILE   A 1 69  ? 34.800 3.165   -1.494  1.00 15.47 ?  69  ILE   A HD11 1 
ATOM   1699 H HD12 . ILE   A 1 69  ? 35.451 3.864   -2.762  1.00 15.47 ?  69  ILE   A HD12 1 
ATOM   1700 H HD13 . ILE   A 1 69  ? 36.369 3.089   -1.722  1.00 15.47 ?  69  ILE   A HD13 1 
ATOM   1701 N N    . ALA   A 1 70  ? 40.007 6.614   -0.410  1.00 12.31 ?  70  ALA   A N    1 
ATOM   1702 C CA   . ALA   A 1 70  ? 41.284 7.227   -0.760  1.00 13.09 ?  70  ALA   A CA   1 
ATOM   1703 C C    . ALA   A 1 70  ? 42.433 6.244   -0.590  1.00 13.53 ?  70  ALA   A C    1 
ATOM   1704 O O    . ALA   A 1 70  ? 43.405 6.287   -1.350  1.00 15.63 ?  70  ALA   A O    1 
ATOM   1705 C CB   . ALA   A 1 70  ? 41.514 8.482   0.084   1.00 13.70 ?  70  ALA   A CB   1 
ATOM   1706 H H    . ALA   A 1 70  ? 39.574 7.010   0.215   1.00 14.75 ?  70  ALA   A H    1 
ATOM   1707 H HA   . ALA   A 1 70  ? 41.257 7.503   -1.693  1.00 15.68 ?  70  ALA   A HA   1 
ATOM   1708 H HB1  . ALA   A 1 70  ? 42.371 8.873   -0.160  1.00 16.42 ?  70  ALA   A HB1  1 
ATOM   1709 H HB2  . ALA   A 1 70  ? 40.803 9.118   -0.089  1.00 16.42 ?  70  ALA   A HB2  1 
ATOM   1710 H HB3  . ALA   A 1 70  ? 41.520 8.235   1.021   1.00 16.42 ?  70  ALA   A HB3  1 
ATOM   1711 N N    . THR   A 1 71  ? 42.326 5.330   0.366   1.00 13.10 ?  71  THR   A N    1 
ATOM   1712 C CA   . THR   A 1 71  ? 43.377 4.353   0.618   1.00 14.66 ?  71  THR   A CA   1 
ATOM   1713 C C    . THR   A 1 71  ? 43.261 3.120   -0.262  1.00 14.81 ?  71  THR   A C    1 
ATOM   1714 O O    . THR   A 1 71  ? 44.277 2.605   -0.749  1.00 17.26 ?  71  THR   A O    1 
ATOM   1715 C CB   . THR   A 1 71  ? 43.311 3.914   2.079   1.00 16.90 ?  71  THR   A CB   1 
ATOM   1716 O OG1  . THR   A 1 71  ? 43.547 5.047   2.919   1.00 18.26 ?  71  THR   A OG1  1 
ATOM   1717 C CG2  . THR   A 1 71  ? 44.328 2.814   2.374   1.00 18.56 ?  71  THR   A CG2  1 
ATOM   1718 H H    . THR   A 1 71  ? 41.638 5.241   0.872   1.00 15.69 ?  71  THR   A H    1 
ATOM   1719 H HA   . THR   A 1 71  ? 44.239 4.756   0.448   1.00 17.57 ?  71  THR   A HA   1 
ATOM   1720 H HB   . THR   A 1 71  ? 42.428 3.560   2.260   1.00 20.26 ?  71  THR   A HB   1 
ATOM   1721 H HG1  . THR   A 1 71  ? 42.961 5.631   2.776   1.00 21.88 ?  71  THR   A HG1  1 
ATOM   1722 H HG21 . THR   A 1 71  ? 44.467 2.745   3.331   1.00 22.25 ?  71  THR   A HG21 1 
ATOM   1723 H HG22 . THR   A 1 71  ? 44.011 1.961   2.040   1.00 22.25 ?  71  THR   A HG22 1 
ATOM   1724 H HG23 . THR   A 1 71  ? 45.177 3.023   1.950   1.00 22.25 ?  71  THR   A HG23 1 
ATOM   1725 N N    . ASN   A 1 72  ? 42.035 2.624   -0.459  1.00 13.52 ?  72  ASN   A N    1 
ATOM   1726 C CA   . ASN   A 1 72  ? 41.808 1.298   -1.021  1.00 13.62 ?  72  ASN   A CA   1 
ATOM   1727 C C    . ASN   A 1 72  ? 41.196 1.291   -2.409  1.00 13.58 ?  72  ASN   A C    1 
ATOM   1728 O O    . ASN   A 1 72  ? 41.199 0.238   -3.062  1.00 14.59 ?  72  ASN   A O    1 
ATOM   1729 C CB   . ASN   A 1 72  ? 40.908 0.486   -0.084  1.00 14.12 ?  72  ASN   A CB   1 
ATOM   1730 C CG   . ASN   A 1 72  ? 41.522 0.323   1.280   1.00 15.17 ?  72  ASN   A CG   1 
ATOM   1731 O OD1  . ASN   A 1 72  ? 41.075 0.926   2.252   1.00 16.92 ?  72  ASN   A OD1  1 
ATOM   1732 N ND2  . ASN   A 1 72  ? 42.571 -0.467  1.357   1.00 15.64 ?  72  ASN   A ND2  1 
ATOM   1733 H H    . ASN   A 1 72  ? 41.299 3.041   -0.263  1.00 16.20 ?  72  ASN   A H    1 
ATOM   1734 H HA   . ASN   A 1 72  ? 42.655 0.843   -1.081  1.00 16.32 ?  72  ASN   A HA   1 
ATOM   1735 H HB2  . ASN   A 1 72  ? 40.054 0.934   0.014   1.00 16.92 ?  72  ASN   A HB2  1 
ATOM   1736 H HB3  . ASN   A 1 72  ? 40.775 -0.402  -0.462  1.00 16.92 ?  72  ASN   A HB3  1 
ATOM   1737 H HD21 . ASN   A 1 72  ? 42.961 -0.586  2.115   1.00 18.74 ?  72  ASN   A HD21 1 
ATOM   1738 H HD22 . ASN   A 1 72  ? 42.860 -0.869  0.656   1.00 18.74 ?  72  ASN   A HD22 1 
ATOM   1739 N N    . GLY   A 1 73  ? 40.649 2.408   -2.867  1.00 13.03 ?  73  GLY   A N    1 
ATOM   1740 C CA   . GLY   A 1 73  ? 39.917 2.430   -4.106  1.00 13.07 ?  73  GLY   A CA   1 
ATOM   1741 C C    . GLY   A 1 73  ? 38.530 1.841   -3.939  1.00 12.37 ?  73  GLY   A C    1 
ATOM   1742 O O    . GLY   A 1 73  ? 38.142 1.393   -2.854  1.00 12.59 ?  73  GLY   A O    1 
ATOM   1743 H H    . GLY   A 1 73  ? 40.697 3.181   -2.475  1.00 15.62 ?  73  GLY   A H    1 
ATOM   1744 H HA2  . GLY   A 1 73  ? 39.835 3.349   -4.418  1.00 15.66 ?  73  GLY   A HA2  1 
ATOM   1745 H HA3  . GLY   A 1 73  ? 40.396 1.921   -4.777  1.00 15.66 ?  73  GLY   A HA3  1 
ATOM   1746 N N    . PRO   A 1 74  ? 37.754 1.850   -5.021  1.00 12.73 ?  74  PRO   A N    1 
ATOM   1747 C CA   . PRO   A 1 74  ? 36.356 1.420   -4.938  1.00 12.80 ?  74  PRO   A CA   1 
ATOM   1748 C C    . PRO   A 1 74  ? 36.207 -0.061  -4.626  1.00 11.72 ?  74  PRO   A C    1 
ATOM   1749 O O    . PRO   A 1 74  ? 37.080 -0.887  -4.910  1.00 12.72 ?  74  PRO   A O    1 
ATOM   1750 C CB   . PRO   A 1 74  ? 35.808 1.730   -6.337  1.00 14.43 ?  74  PRO   A CB   1 
ATOM   1751 C CG   . PRO   A 1 74  ? 36.758 2.716   -6.935  1.00 17.05 ?  74  PRO   A CG   1 
ATOM   1752 C CD   . PRO   A 1 74  ? 38.092 2.369   -6.357  1.00 14.73 ?  74  PRO   A CD   1 
ATOM   1753 H HA   . PRO   A 1 74  ? 35.877 1.940   -4.275  1.00 15.33 ?  74  PRO   A HA   1 
ATOM   1754 H HB2  . PRO   A 1 74  ? 35.777 0.917   -6.862  1.00 17.29 ?  74  PRO   A HB2  1 
ATOM   1755 H HB3  . PRO   A 1 74  ? 34.919 2.118   -6.256  1.00 17.29 ?  74  PRO   A HB3  1 
ATOM   1756 H HG2  . PRO   A 1 74  ? 36.768 2.618   -7.898  1.00 20.44 ?  74  PRO   A HG2  1 
ATOM   1757 H HG3  . PRO   A 1 74  ? 36.502 3.614   -6.681  1.00 20.44 ?  74  PRO   A HG3  1 
ATOM   1758 H HD2  . PRO   A 1 74  ? 38.528 1.680   -6.888  1.00 17.65 ?  74  PRO   A HD2  1 
ATOM   1759 H HD3  . PRO   A 1 74  ? 38.647 3.164   -6.293  1.00 17.65 ?  74  PRO   A HD3  1 
ATOM   1760 N N    . LEU   A 1 75  ? 35.061 -0.388  -4.040  1.00 11.15 ?  75  LEU   A N    1 
ATOM   1761 C CA   . LEU   A 1 75  ? 34.668 -1.775  -3.890  1.00 10.66 ?  75  LEU   A CA   1 
ATOM   1762 C C    . LEU   A 1 75  ? 34.304 -2.366  -5.251  1.00 10.89 ?  75  LEU   A C    1 
ATOM   1763 O O    . LEU   A 1 75  ? 34.144 -1.662  -6.249  1.00 12.45 ?  75  LEU   A O    1 
ATOM   1764 C CB   . LEU   A 1 75  ? 33.470 -1.896  -2.950  1.00 10.37 ?  75  LEU   A CB   1 
ATOM   1765 C CG   . LEU   A 1 75  ? 33.678 -1.484  -1.496  1.00 12.47 ?  75  LEU   A CG   1 
ATOM   1766 C CD1  . LEU   A 1 75  ? 32.383 -1.667  -0.719  1.00 14.19 ?  75  LEU   A CD1  1 
ATOM   1767 C CD2  . LEU   A 1 75  ? 34.796 -2.224  -0.826  1.00 15.59 ?  75  LEU   A CD2  1 
ATOM   1768 H H    . LEU   A 1 75  ? 34.497 0.178   -3.723  1.00 13.36 ?  75  LEU   A H    1 
ATOM   1769 H HA   . LEU   A 1 75  ? 35.404 -2.283  -3.518  1.00 12.77 ?  75  LEU   A HA   1 
ATOM   1770 H HB2  . LEU   A 1 75  ? 32.749 -1.350  -3.301  1.00 12.43 ?  75  LEU   A HB2  1 
ATOM   1771 H HB3  . LEU   A 1 75  ? 33.185 -2.827  -2.943  1.00 12.43 ?  75  LEU   A HB3  1 
ATOM   1772 H HG   . LEU   A 1 75  ? 33.904 -0.540  -1.477  1.00 14.94 ?  75  LEU   A HG   1 
ATOM   1773 H HD11 . LEU   A 1 75  ? 32.528 -1.396  0.201   1.00 17.00 ?  75  LEU   A HD11 1 
ATOM   1774 H HD12 . LEU   A 1 75  ? 31.696 -1.113  -1.123  1.00 17.00 ?  75  LEU   A HD12 1 
ATOM   1775 H HD13 . LEU   A 1 75  ? 32.123 -2.598  -0.756  1.00 17.00 ?  75  LEU   A HD13 1 
ATOM   1776 H HD21 . LEU   A 1 75  ? 34.838 -1.960  0.106   1.00 18.69 ?  75  LEU   A HD21 1 
ATOM   1777 H HD22 . LEU   A 1 75  ? 34.634 -3.177  -0.894  1.00 18.69 ?  75  LEU   A HD22 1 
ATOM   1778 H HD23 . LEU   A 1 75  ? 35.636 -2.001  -1.266  1.00 18.69 ?  75  LEU   A HD23 1 
ATOM   1779 N N    . LYS   A 1 76  ? 34.163 -3.689  -5.269  1.00 11.34 ?  76  LYS   A N    1 
ATOM   1780 C CA   . LYS   A 1 76  ? 33.583 -4.413  -6.394  1.00 11.78 ?  76  LYS   A CA   1 
ATOM   1781 C C    . LYS   A 1 76  ? 32.067 -4.488  -6.224  1.00 10.62 ?  76  LYS   A C    1 
ATOM   1782 O O    . LYS   A 1 76  ? 31.564 -4.590  -5.106  1.00 10.93 ?  76  LYS   A O    1 
ATOM   1783 C CB   . LYS   A 1 76  ? 34.126 -5.848  -6.431  1.00 12.87 ?  76  LYS   A CB   1 
ATOM   1784 C CG   . LYS   A 1 76  ? 35.632 -5.954  -6.634  1.00 14.25 ?  76  LYS   A CG   1 
ATOM   1785 C CD   . LYS   A 1 76  ? 36.146 -7.361  -6.433  1.00 15.57 ?  76  LYS   A CD   1 
ATOM   1786 C CE   . LYS   A 1 76  ? 37.642 -7.419  -6.659  1.00 18.08 ?  76  LYS   A CE   1 
ATOM   1787 N NZ   . LYS   A 1 76  ? 38.176 -8.783  -6.493  1.00 18.95 ?  76  LYS   A NZ   1 
ATOM   1788 H H    . LYS   A 1 76  ? 34.403 -4.205  -4.619  1.00 13.58 ?  76  LYS   A H    1 
ATOM   1789 H HA   . LYS   A 1 76  ? 33.797 -3.962  -7.228  1.00 14.11 ?  76  LYS   A HA   1 
ATOM   1790 H HB2  . LYS   A 1 76  ? 33.913 -6.279  -5.592  1.00 15.42 ?  76  LYS   A HB2  1 
ATOM   1791 H HB3  . LYS   A 1 76  ? 33.700 -6.318  -7.162  1.00 15.42 ?  76  LYS   A HB3  1 
ATOM   1792 H HG2  . LYS   A 1 76  ? 35.851 -5.678  -7.539  1.00 17.08 ?  76  LYS   A HG2  1 
ATOM   1793 H HG3  . LYS   A 1 76  ? 36.081 -5.375  -5.995  1.00 17.08 ?  76  LYS   A HG3  1 
ATOM   1794 H HD2  . LYS   A 1 76  ? 35.960 -7.645  -5.524  1.00 18.65 ?  76  LYS   A HD2  1 
ATOM   1795 H HD3  . LYS   A 1 76  ? 35.715 -7.955  -7.068  1.00 18.65 ?  76  LYS   A HD3  1 
ATOM   1796 H HE2  . LYS   A 1 76  ? 37.837 -7.125  -7.562  1.00 21.67 ?  76  LYS   A HE2  1 
ATOM   1797 H HE3  . LYS   A 1 76  ? 38.082 -6.844  -6.016  1.00 21.67 ?  76  LYS   A HE3  1 
ATOM   1798 H HZ1  . LYS   A 1 76  ? 39.055 -8.791  -6.633  1.00 22.72 ?  76  LYS   A HZ1  1 
ATOM   1799 H HZ2  . LYS   A 1 76  ? 38.013 -9.083  -5.670  1.00 22.72 ?  76  LYS   A HZ2  1 
ATOM   1800 H HZ3  . LYS   A 1 76  ? 37.790 -9.340  -7.078  1.00 22.72 ?  76  LYS   A HZ3  1 
ATOM   1801 N N    . VAL   A 1 77  ? 31.338 -4.462  -7.344  1.00 11.39 ?  77  VAL   A N    1 
ATOM   1802 C CA   . VAL   A 1 77  ? 29.928 -4.843  -7.279  1.00 11.49 ?  77  VAL   A CA   1 
ATOM   1803 C C    . VAL   A 1 77  ? 29.859 -6.293  -6.821  1.00 10.95 ?  77  VAL   A C    1 
ATOM   1804 O O    . VAL   A 1 77  ? 30.524 -7.166  -7.389  1.00 11.57 ?  77  VAL   A O    1 
ATOM   1805 C CB   . VAL   A 1 77  ? 29.231 -4.639  -8.632  1.00 12.26 ?  77  VAL   A CB   1 
ATOM   1806 C CG1  . VAL   A 1 77  ? 27.768 -5.054  -8.545  1.00 13.34 ?  77  VAL   A CG1  1 
ATOM   1807 C CG2  . VAL   A 1 77  ? 29.349 -3.191  -9.074  1.00 13.71 ?  77  VAL   A CG2  1 
ATOM   1808 H H    . VAL   A 1 77  ? 31.629 -4.237  -8.122  1.00 13.64 ?  77  VAL   A H    1 
ATOM   1809 H HA   . VAL   A 1 77  ? 29.483 -4.292  -6.618  1.00 13.77 ?  77  VAL   A HA   1 
ATOM   1810 H HB   . VAL   A 1 77  ? 29.667 -5.191  -9.299  1.00 14.69 ?  77  VAL   A HB   1 
ATOM   1811 H HG11 . VAL   A 1 77  ? 27.319 -4.782  -9.360  1.00 15.99 ?  77  VAL   A HG11 1 
ATOM   1812 H HG12 . VAL   A 1 77  ? 27.717 -6.015  -8.442  1.00 15.99 ?  77  VAL   A HG12 1 
ATOM   1813 H HG13 . VAL   A 1 77  ? 27.362 -4.613  -7.782  1.00 15.99 ?  77  VAL   A HG13 1 
ATOM   1814 H HG21 . VAL   A 1 77  ? 28.844 -3.068  -9.890  1.00 16.42 ?  77  VAL   A HG21 1 
ATOM   1815 H HG22 . VAL   A 1 77  ? 28.995 -2.618  -8.374  1.00 16.42 ?  77  VAL   A HG22 1 
ATOM   1816 H HG23 . VAL   A 1 77  ? 30.285 -2.980  -9.228  1.00 16.42 ?  77  VAL   A HG23 1 
ATOM   1817 N N    . GLY   A 1 78  ? 29.056 -6.559  -5.787  1.00 10.61 ?  78  GLY   A N    1 
ATOM   1818 C CA   . GLY   A 1 78  ? 29.027 -7.845  -5.127  1.00 10.83 ?  78  GLY   A CA   1 
ATOM   1819 C C    . GLY   A 1 78  ? 29.934 -7.938  -3.919  1.00 10.56 ?  78  GLY   A C    1 
ATOM   1820 O O    . GLY   A 1 78  ? 29.862 -8.941  -3.189  1.00 11.05 ?  78  GLY   A O    1 
ATOM   1821 H H    . GLY   A 1 78  ? 28.502 -5.987  -5.453  1.00 12.70 ?  78  GLY   A H    1 
ATOM   1822 H HA2  . GLY   A 1 78  ? 28.122 -8.035  -4.841  1.00 12.98 ?  78  GLY   A HA2  1 
ATOM   1823 H HA3  . GLY   A 1 78  ? 29.294 -8.531  -5.761  1.00 12.98 ?  78  GLY   A HA3  1 
ATOM   1824 N N    . GLY   A 1 79  ? 30.785 -6.932  -3.686  1.00 10.50 ?  79  GLY   A N    1 
ATOM   1825 C CA   . GLY   A 1 79  ? 31.733 -6.947  -2.595  1.00 10.70 ?  79  GLY   A CA   1 
ATOM   1826 C C    . GLY   A 1 79  ? 31.274 -6.142  -1.391  1.00 9.85  ?  79  GLY   A C    1 
ATOM   1827 O O    . GLY   A 1 79  ? 30.152 -5.632  -1.325  1.00 10.84 ?  79  GLY   A O    1 
ATOM   1828 H H    . GLY   A 1 79  ? 30.835 -6.220  -4.171  1.00 12.58 ?  79  GLY   A H    1 
ATOM   1829 H HA2  . GLY   A 1 79  ? 31.881 -7.871  -2.317  1.00 12.82 ?  79  GLY   A HA2  1 
ATOM   1830 H HA3  . GLY   A 1 79  ? 32.581 -6.590  -2.900  1.00 12.82 ?  79  GLY   A HA3  1 
ATOM   1831 N N    . SER   A 1 80  ? 32.172 -6.044  -0.412  1.00 10.65 ?  80  SER   A N    1 
ATOM   1832 C CA   . SER   A 1 80  ? 31.841 -5.415  0.855   1.00 10.14 ?  80  SER   A CA   1 
ATOM   1833 C C    . SER   A 1 80  ? 33.104 -4.958  1.569   1.00 10.18 ?  80  SER   A C    1 
ATOM   1834 O O    . SER   A 1 80  ? 34.220 -5.390  1.256   1.00 11.62 ?  80  SER   A O    1 
ATOM   1835 C CB   . SER   A 1 80  ? 31.077 -6.370  1.777   1.00 11.15 ?  80  SER   A CB   1 
ATOM   1836 O OG   . SER   A 1 80  ? 31.898 -7.420  2.258   1.00 12.84 ?  80  SER   A OG   1 
ATOM   1837 H H    . SER   A 1 80  ? 32.987 -6.320  -0.466  1.00 12.76 ?  80  SER   A H    1 
ATOM   1838 H HA   . SER   A 1 80  ? 31.289 -4.639  0.675   1.00 12.15 ?  80  SER   A HA   1 
ATOM   1839 H HB2  . SER   A 1 80  ? 30.739 -5.866  2.533   1.00 13.36 ?  80  SER   A HB2  1 
ATOM   1840 H HB3  . SER   A 1 80  ? 30.336 -6.752  1.281   1.00 13.36 ?  80  SER   A HB3  1 
ATOM   1841 H HG   . SER   A 1 80  ? 32.196 -7.868  1.611   1.00 15.39 ?  80  SER   A HG   1 
ATOM   1842 N N    . CYS   A 1 81  ? 32.901 -4.103  2.570   1.00 10.01 ?  81  CYS   A N    1 
ATOM   1843 C CA   . CYS   A 1 81  ? 33.944 -3.819  3.540   1.00 10.22 ?  81  CYS   A CA   1 
ATOM   1844 C C    . CYS   A 1 81  ? 33.294 -3.581  4.896   1.00 9.90  ?  81  CYS   A C    1 
ATOM   1845 O O    . CYS   A 1 81  ? 32.125 -3.183  4.981   1.00 11.09 ?  81  CYS   A O    1 
ATOM   1846 C CB   . CYS   A 1 81  ? 34.812 -2.623  3.124   1.00 10.87 ?  81  CYS   A CB   1 
ATOM   1847 S SG   . CYS   A 1 81  ? 33.916 -1.053  3.133   1.00 10.70 ?  81  CYS   A SG   1 
ATOM   1848 H H    . CYS   A 1 81  ? 32.164 -3.682  2.710   1.00 11.99 ?  81  CYS   A H    1 
ATOM   1849 H HA   . CYS   A 1 81  ? 34.526 -4.594  3.615   1.00 12.24 ?  81  CYS   A HA   1 
ATOM   1850 H HB2  . CYS   A 1 81  ? 35.562 -2.551  3.740   1.00 13.02 ?  81  CYS   A HB2  1 
ATOM   1851 H HB3  . CYS   A 1 81  ? 35.147 -2.775  2.223   1.00 13.02 ?  81  CYS   A HB3  1 
ATOM   1852 H HG   . CYS   A 1 81  ? 34.662 -0.174  2.804   1.00 12.82 ?  81  CYS   A HG   1 
ATOM   1853 N N    . VAL   A 1 82  ? 34.059 -3.841  5.954   1.00 10.23 ?  82  VAL   A N    1 
ATOM   1854 C CA   . VAL   A 1 82  ? 33.628 -3.600  7.324   1.00 10.77 ?  82  VAL   A CA   1 
ATOM   1855 C C    . VAL   A 1 82  ? 34.221 -2.285  7.798   1.00 10.90 ?  82  VAL   A C    1 
ATOM   1856 O O    . VAL   A 1 82  ? 35.442 -2.109  7.793   1.00 11.38 ?  82  VAL   A O    1 
ATOM   1857 C CB   . VAL   A 1 82  ? 34.048 -4.743  8.258   1.00 12.11 ?  82  VAL   A CB   1 
ATOM   1858 C CG1  . VAL   A 1 82  ? 33.590 -4.454  9.677   1.00 13.71 ?  82  VAL   A CG1  1 
ATOM   1859 C CG2  . VAL   A 1 82  ? 33.491 -6.073  7.781   1.00 12.96 ?  82  VAL   A CG2  1 
ATOM   1860 H H    . VAL   A 1 82  ? 34.855 -4.174  5.898   1.00 12.26 ?  82  VAL   A H    1 
ATOM   1861 H HA   . VAL   A 1 82  ? 32.662 -3.521  7.345   1.00 12.91 ?  82  VAL   A HA   1 
ATOM   1862 H HB   . VAL   A 1 82  ? 35.014 -4.805  8.264   1.00 14.51 ?  82  VAL   A HB   1 
ATOM   1863 H HG11 . VAL   A 1 82  ? 33.676 -5.262  10.208  1.00 16.43 ?  82  VAL   A HG11 1 
ATOM   1864 H HG12 . VAL   A 1 82  ? 34.139 -3.751  10.058  1.00 16.43 ?  82  VAL   A HG12 1 
ATOM   1865 H HG13 . VAL   A 1 82  ? 32.659 -4.172  9.661   1.00 16.43 ?  82  VAL   A HG13 1 
ATOM   1866 H HG21 . VAL   A 1 82  ? 33.739 -6.763  8.413   1.00 15.53 ?  82  VAL   A HG21 1 
ATOM   1867 H HG22 . VAL   A 1 82  ? 32.524 -6.008  7.723   1.00 15.53 ?  82  VAL   A HG22 1 
ATOM   1868 H HG23 . VAL   A 1 82  ? 33.860 -6.274  6.907   1.00 15.53 ?  82  VAL   A HG23 1 
ATOM   1869 N N    . LEU   A 1 83  ? 33.362 -1.363  8.208   1.00 10.34 ?  83  LEU   A N    1 
ATOM   1870 C CA   . LEU   A 1 83  ? 33.771 -0.092  8.786   1.00 10.16 ?  83  LEU   A CA   1 
ATOM   1871 C C    . LEU   A 1 83  ? 33.041 0.087   10.112  1.00 10.47 ?  83  LEU   A C    1 
ATOM   1872 O O    . LEU   A 1 83  ? 32.320 -0.807  10.568  1.00 11.02 ?  83  LEU   A O    1 
ATOM   1873 C CB   . LEU   A 1 83  ? 33.521 1.063   7.806   1.00 10.83 ?  83  LEU   A CB   1 
ATOM   1874 C CG   . LEU   A 1 83  ? 34.427 1.053   6.570   1.00 11.58 ?  83  LEU   A CG   1 
ATOM   1875 C CD1  . LEU   A 1 83  ? 33.993 2.112   5.574   1.00 12.15 ?  83  LEU   A CD1  1 
ATOM   1876 C CD2  . LEU   A 1 83  ? 35.897 1.273   6.959   1.00 12.38 ?  83  LEU   A CD2  1 
ATOM   1877 H H    . LEU   A 1 83  ? 32.512 -1.448  8.153   1.00 12.38 ?  83  LEU   A H    1 
ATOM   1878 H HA   . LEU   A 1 83  ? 34.723 -0.108  8.974   1.00 12.17 ?  83  LEU   A HA   1 
ATOM   1879 H HB2  . LEU   A 1 83  ? 32.600 1.015   7.490   1.00 12.98 ?  83  LEU   A HB2  1 
ATOM   1880 H HB3  . LEU   A 1 83  ? 33.656 1.910   8.263   1.00 12.98 ?  83  LEU   A HB3  1 
ATOM   1881 H HG   . LEU   A 1 83  ? 34.362 0.188   6.139   1.00 13.88 ?  83  LEU   A HG   1 
ATOM   1882 H HD11 . LEU   A 1 83  ? 34.580 2.080   4.804   1.00 14.56 ?  83  LEU   A HD11 1 
ATOM   1883 H HD12 . LEU   A 1 83  ? 33.079 1.929   5.303   1.00 14.56 ?  83  LEU   A HD12 1 
ATOM   1884 H HD13 . LEU   A 1 83  ? 34.044 2.983   5.997   1.00 14.56 ?  83  LEU   A HD13 1 
ATOM   1885 H HD21 . LEU   A 1 83  ? 36.421 1.429   6.155   1.00 14.83 ?  83  LEU   A HD21 1 
ATOM   1886 H HD22 . LEU   A 1 83  ? 35.960 2.051   7.542   1.00 14.83 ?  83  LEU   A HD22 1 
ATOM   1887 H HD23 . LEU   A 1 83  ? 36.231 0.490   7.422   1.00 14.83 ?  83  LEU   A HD23 1 
ATOM   1888 N N    . SER   A 1 84  ? 33.244 1.236   10.750  1.00 11.37 ?  84  SER   A N    1 
ATOM   1889 C CA   . SER   A 1 84  ? 32.586 1.492   12.021  1.00 11.20 ?  84  SER   A CA   1 
ATOM   1890 C C    . SER   A 1 84  ? 31.070 1.585   11.854  1.00 11.33 ?  84  SER   A C    1 
ATOM   1891 O O    . SER   A 1 84  ? 30.559 2.046   10.833  1.00 11.20 ?  84  SER   A O    1 
ATOM   1892 C CB   . SER   A 1 84  ? 33.077 2.816   12.597  1.00 12.20 ?  84  SER   A CB   1 
ATOM   1893 O OG   . SER   A 1 84  ? 32.449 3.093   13.830  1.00 13.30 ?  84  SER   A OG   1 
ATOM   1894 H H    . SER   A 1 84  ? 33.745 1.882   10.467  1.00 13.62 ?  84  SER   A H    1 
ATOM   1895 H HA   . SER   A 1 84  ? 32.796 0.778   12.642  1.00 13.42 ?  84  SER   A HA   1 
ATOM   1896 H HB2  . SER   A 1 84  ? 34.039 2.763   12.726  1.00 14.62 ?  84  SER   A HB2  1 
ATOM   1897 H HB3  . SER   A 1 84  ? 32.868 3.526   11.971  1.00 14.62 ?  84  SER   A HB3  1 
ATOM   1898 H HG   . SER   A 1 84  ? 32.738 3.818   14.138  1.00 15.94 ?  84  SER   A HG   1 
ATOM   1899 N N    . GLY   A 1 85  ? 30.348 1.181   12.894  1.00 12.14 ?  85  GLY   A N    1 
ATOM   1900 C CA   . GLY   A 1 85  ? 28.925 1.425   12.971  1.00 12.48 ?  85  GLY   A CA   1 
ATOM   1901 C C    . GLY   A 1 85  ? 28.555 2.735   13.624  1.00 12.29 ?  85  GLY   A C    1 
ATOM   1902 O O    . GLY   A 1 85  ? 27.367 3.055   13.724  1.00 12.91 ?  85  GLY   A O    1 
ATOM   1903 H H    . GLY   A 1 85  ? 30.666 0.751   13.569  1.00 14.54 ?  85  GLY   A H    1 
ATOM   1904 H HA2  . GLY   A 1 85  ? 28.555 1.423   12.073  1.00 14.95 ?  85  GLY   A HA2  1 
ATOM   1905 H HA3  . GLY   A 1 85  ? 28.505 0.714   13.471  1.00 14.95 ?  85  GLY   A HA3  1 
ATOM   1906 N N    . HIS   A 1 86  ? 29.542 3.505   14.074  1.00 12.35 ?  86  HIS   A N    1 
ATOM   1907 C CA   . HIS   A 1 86  ? 29.323 4.846   14.636  1.00 12.48 ?  86  HIS   A CA   1 
ATOM   1908 C C    . HIS   A 1 86  ? 28.327 4.731   15.784  1.00 13.30 ?  86  HIS   A C    1 
ATOM   1909 O O    . HIS   A 1 86  ? 28.499 3.854   16.646  1.00 14.60 ?  86  HIS   A O    1 
ATOM   1910 C CB   . HIS   A 1 86  ? 28.959 5.824   13.525  1.00 12.39 ?  86  HIS   A CB   1 
ATOM   1911 C CG   . HIS   A 1 86  ? 30.024 5.920   12.493  1.00 12.27 ?  86  HIS   A CG   1 
ATOM   1912 N ND1  . HIS   A 1 86  ? 31.113 6.754   12.632  1.00 13.44 ?  86  HIS   A ND1  1 
ATOM   1913 C CD2  . HIS   A 1 86  ? 30.217 5.226   11.349  1.00 12.11 ?  86  HIS   A CD2  1 
ATOM   1914 C CE1  . HIS   A 1 86  ? 31.918 6.585   11.599  1.00 13.19 ?  86  HIS   A CE1  1 
ATOM   1915 N NE2  . HIS   A 1 86  ? 31.404 5.658   10.812  1.00 12.36 ?  86  HIS   A NE2  1 
ATOM   1916 H H    . HIS   A 1 86  ? 30.368 3.281   14.073  1.00 14.80 ?  86  HIS   A H    1 
ATOM   1917 H HA   . HIS   A 1 86  ? 30.156 5.161   15.015  1.00 14.95 ?  86  HIS   A HA   1 
ATOM   1918 H HB2  . HIS   A 1 86  ? 28.141 5.534   13.091  1.00 14.85 ?  86  HIS   A HB2  1 
ATOM   1919 H HB3  . HIS   A 1 86  ? 28.833 6.714   13.902  1.00 14.85 ?  86  HIS   A HB3  1 
ATOM   1920 H HD2  . HIS   A 1 86  ? 29.657 4.568   10.991  1.00 14.51 ?  86  HIS   A HD2  1 
ATOM   1921 H HE1  . HIS   A 1 86  ? 32.713 7.038   11.439  1.00 15.80 ?  86  HIS   A HE1  1 
ATOM   1922 H HE2  . HIS   A 1 86  ? 31.744 5.381   10.062  1.00 14.81 ?  86  HIS   A HE2  1 
ATOM   1923 N N    . ASN   A 1 87  ? 27.307 5.579   15.842  1.00 14.37 ?  87  ASN   A N    1 
ATOM   1924 C CA   . ASN   A 1 87  ? 26.312 5.570   16.900  1.00 15.01 ?  87  ASN   A CA   1 
ATOM   1925 C C    . ASN   A 1 87  ? 25.186 4.579   16.648  1.00 15.90 ?  87  ASN   A C    1 
ATOM   1926 O O    . ASN   A 1 87  ? 24.247 4.525   17.445  1.00 18.40 ?  87  ASN   A O    1 
ATOM   1927 C CB   . ASN   A 1 87  ? 25.719 6.979   17.059  1.00 16.25 ?  87  ASN   A CB   1 
ATOM   1928 C CG   . ASN   A 1 87  ? 25.215 7.562   15.738  1.00 16.98 ?  87  ASN   A CG   1 
ATOM   1929 O OD1  . ASN   A 1 87  ? 25.847 7.411   14.696  1.00 17.59 ?  87  ASN   A OD1  1 
ATOM   1930 N ND2  . ASN   A 1 87  ? 24.074 8.230   15.784  1.00 18.32 ?  87  ASN   A ND2  1 
ATOM   1931 H H    . ASN   A 1 87  ? 27.162 6.187   15.256  1.00 17.22 ?  87  ASN   A H    1 
ATOM   1932 H HA   . ASN   A 1 87  ? 26.733 5.325   17.741  1.00 17.99 ?  87  ASN   A HA   1 
ATOM   1933 H HB2  . ASN   A 1 87  ? 24.969 6.939   17.679  1.00 19.47 ?  87  ASN   A HB2  1 
ATOM   1934 H HB3  . ASN   A 1 87  ? 26.404 7.569   17.408  1.00 19.47 ?  87  ASN   A HB3  1 
ATOM   1935 H HD21 . ASN   A 1 87  ? 23.753 8.571   15.064  1.00 21.96 ?  87  ASN   A HD21 1 
ATOM   1936 H HD22 . ASN   A 1 87  ? 23.660 8.325   16.531  1.00 21.96 ?  87  ASN   A HD22 1 
ATOM   1937 N N    A LEU   A 1 88  ? 25.259 3.795   15.574  0.48 14.68 ?  88  LEU   A N    1 
ATOM   1938 N N    B LEU   A 1 88  ? 25.260 3.782   15.581  0.52 14.75 ?  88  LEU   A N    1 
ATOM   1939 C CA   A LEU   A 1 88  ? 24.162 2.924   15.170  0.48 14.58 ?  88  LEU   A CA   1 
ATOM   1940 C CA   B LEU   A 1 88  ? 24.150 2.926   15.182  0.52 14.66 ?  88  LEU   A CA   1 
ATOM   1941 C C    A LEU   A 1 88  ? 24.382 1.456   15.514  0.48 14.14 ?  88  LEU   A C    1 
ATOM   1942 C C    B LEU   A 1 88  ? 24.379 1.439   15.415  0.52 14.05 ?  88  LEU   A C    1 
ATOM   1943 O O    A LEU   A 1 88  ? 23.410 0.744   15.787  0.48 14.84 ?  88  LEU   A O    1 
ATOM   1944 O O    B LEU   A 1 88  ? 23.402 0.687   15.479  0.52 14.35 ?  88  LEU   A O    1 
ATOM   1945 C CB   A LEU   A 1 88  ? 23.934 3.045   13.659  0.48 14.81 ?  88  LEU   A CB   1 
ATOM   1946 C CB   B LEU   A 1 88  ? 23.839 3.137   13.695  0.52 15.11 ?  88  LEU   A CB   1 
ATOM   1947 C CG   A LEU   A 1 88  ? 23.676 4.451   13.118  0.48 15.68 ?  88  LEU   A CG   1 
ATOM   1948 C CG   B LEU   A 1 88  ? 23.549 4.582   13.285  0.52 15.90 ?  88  LEU   A CG   1 
ATOM   1949 C CD1  A LEU   A 1 88  ? 23.576 4.408   11.605  0.48 15.85 ?  88  LEU   A CD1  1 
ATOM   1950 C CD1  B LEU   A 1 88  ? 23.325 4.688   11.784  0.52 15.91 ?  88  LEU   A CD1  1 
ATOM   1951 C CD2  A LEU   A 1 88  ? 22.412 5.048   13.724  0.48 17.24 ?  88  LEU   A CD2  1 
ATOM   1952 C CD2  B LEU   A 1 88  ? 22.347 5.126   14.043  0.52 17.06 ?  88  LEU   A CD2  1 
ATOM   1953 H H    A LEU   A 1 88  ? 25.948 3.751   15.060  0.48 17.60 ?  88  LEU   A H    1 
ATOM   1954 H H    B LEU   A 1 88  ? 25.949 3.722   15.072  0.52 17.68 ?  88  LEU   A H    1 
ATOM   1955 H HA   A LEU   A 1 88  ? 23.352 3.212   15.612  0.48 17.47 ?  88  LEU   A HA   1 
ATOM   1956 H HA   B LEU   A 1 88  ? 23.362 3.185   15.686  0.52 17.57 ?  88  LEU   A HA   1 
ATOM   1957 H HB2  A LEU   A 1 88  ? 24.713 2.705   13.199  0.48 17.74 ?  88  LEU   A HB2  1 
ATOM   1958 H HB2  B LEU   A 1 88  ? 24.597 2.832   13.176  0.52 18.11 ?  88  LEU   A HB2  1 
ATOM   1959 H HB3  A LEU   A 1 88  ? 23.160 2.508   13.423  0.48 17.74 ?  88  LEU   A HB3  1 
ATOM   1960 H HB3  B LEU   A 1 88  ? 23.057 2.608   13.468  0.52 18.11 ?  88  LEU   A HB3  1 
ATOM   1961 H HG   A LEU   A 1 88  ? 24.421 5.026   13.351  0.48 18.79 ?  88  LEU   A HG   1 
ATOM   1962 H HG   B LEU   A 1 88  ? 24.315 5.131   13.507  0.52 19.05 ?  88  LEU   A HG   1 
ATOM   1963 H HD11 A LEU   A 1 88  ? 23.454 5.310   11.268  0.48 19.00 ?  88  LEU   A HD11 1 
ATOM   1964 H HD11 B LEU   A 1 88  ? 23.159 5.617   11.553  0.52 19.07 ?  88  LEU   A HD11 1 
ATOM   1965 H HD12 A LEU   A 1 88  ? 24.392 4.027   11.245  0.48 19.00 ?  88  LEU   A HD12 1 
ATOM   1966 H HD12 B LEU   A 1 88  ? 24.118 4.371   11.322  0.52 19.07 ?  88  LEU   A HD12 1 
ATOM   1967 H HD13 A LEU   A 1 88  ? 22.816 3.857   11.356  0.48 19.00 ?  88  LEU   A HD13 1 
ATOM   1968 H HD13 B LEU   A 1 88  ? 22.560 4.145   11.537  0.52 19.07 ?  88  LEU   A HD13 1 
ATOM   1969 H HD21 A LEU   A 1 88  ? 22.234 5.905   13.306  0.48 20.66 ?  88  LEU   A HD21 1 
ATOM   1970 H HD21 B LEU   A 1 88  ? 22.106 5.987   13.670  0.52 20.45 ?  88  LEU   A HD21 1 
ATOM   1971 H HD22 A LEU   A 1 88  ? 21.671 4.442   13.566  0.48 20.66 ?  88  LEU   A HD22 1 
ATOM   1972 H HD22 B LEU   A 1 88  ? 21.611 4.503   13.948  0.52 20.45 ?  88  LEU   A HD22 1 
ATOM   1973 H HD23 A LEU   A 1 88  ? 22.546 5.166   14.677  0.48 20.66 ?  88  LEU   A HD23 1 
ATOM   1974 H HD23 B LEU   A 1 88  ? 22.585 5.221   14.977  0.52 20.45 ?  88  LEU   A HD23 1 
ATOM   1975 N N    . ALA   A 1 89  ? 25.629 0.998   15.515  1.00 13.68 ?  89  ALA   A N    1 
ATOM   1976 C CA   . ALA   A 1 89  ? 25.962 -0.414  15.639  1.00 13.14 ?  89  ALA   A CA   1 
ATOM   1977 C C    . ALA   A 1 89  ? 27.446 -0.468  15.956  1.00 13.50 ?  89  ALA   A C    1 
ATOM   1978 O O    . ALA   A 1 89  ? 28.152 0.535   15.849  1.00 14.43 ?  89  ALA   A O    1 
ATOM   1979 C CB   . ALA   A 1 89  ? 25.704 -1.136  14.318  1.00 13.02 ?  89  ALA   A CB   1 
ATOM   1980 H H    A ALA   A 1 89  ? 26.321 1.507   15.446  0.48 16.39 ?  89  ALA   A H    1 
ATOM   1981 H H    B ALA   A 1 89  ? 26.318 1.513   15.487  0.52 16.39 ?  89  ALA   A H    1 
ATOM   1982 H HA   . ALA   A 1 89  ? 25.452 -0.825  16.354  1.00 15.75 ?  89  ALA   A HA   1 
ATOM   1983 H HB1  . ALA   A 1 89  ? 25.954 -2.068  14.414  1.00 15.60 ?  89  ALA   A HB1  1 
ATOM   1984 H HB2  . ALA   A 1 89  ? 24.760 -1.069  14.098  1.00 15.60 ?  89  ALA   A HB2  1 
ATOM   1985 H HB3  . ALA   A 1 89  ? 26.235 -0.722  13.621  1.00 15.60 ?  89  ALA   A HB3  1 
ATOM   1986 N N    A LYS   A 1 90  ? 27.930 -1.657  16.309  0.48 14.13 ?  90  LYS   A N    1 
ATOM   1987 N N    B LYS   A 1 90  ? 27.918 -1.638  16.378  0.52 13.46 ?  90  LYS   A N    1 
ATOM   1988 C CA   A LYS   A 1 90  ? 29.373 -1.814  16.460  0.48 15.32 ?  90  LYS   A CA   1 
ATOM   1989 C CA   B LYS   A 1 90  ? 29.359 -1.787  16.545  0.52 14.12 ?  90  LYS   A CA   1 
ATOM   1990 C C    A LYS   A 1 90  ? 30.078 -1.658  15.115  0.48 14.72 ?  90  LYS   A C    1 
ATOM   1991 C C    B LYS   A 1 90  ? 30.069 -1.599  15.211  0.52 13.08 ?  90  LYS   A C    1 
ATOM   1992 O O    A LYS   A 1 90  ? 30.995 -0.837  14.971  0.48 15.87 ?  90  LYS   A O    1 
ATOM   1993 O O    B LYS   A 1 90  ? 31.028 -0.819  15.099  0.52 14.35 ?  90  LYS   A O    1 
ATOM   1994 C CB   A LYS   A 1 90  ? 29.706 -3.159  17.111  0.48 17.71 ?  90  LYS   A CB   1 
ATOM   1995 C CB   B LYS   A 1 90  ? 29.694 -3.148  17.155  0.52 16.47 ?  90  LYS   A CB   1 
ATOM   1996 C CG   A LYS   A 1 90  ? 31.189 -3.335  17.418  0.48 21.32 ?  90  LYS   A CG   1 
ATOM   1997 C CG   B LYS   A 1 90  ? 31.166 -3.298  17.509  0.52 20.41 ?  90  LYS   A CG   1 
ATOM   1998 C CD   A LYS   A 1 90  ? 31.432 -4.548  18.304  0.48 24.46 ?  90  LYS   A CD   1 
ATOM   1999 C CD   B LYS   A 1 90  ? 31.424 -4.580  18.280  0.52 23.77 ?  90  LYS   A CD   1 
ATOM   2000 C CE   A LYS   A 1 90  ? 32.854 -4.581  18.851  0.48 26.96 ?  90  LYS   A CE   1 
ATOM   2001 C CE   B LYS   A 1 90  ? 32.793 -4.566  18.940  0.52 26.37 ?  90  LYS   A CE   1 
ATOM   2002 N NZ   A LYS   A 1 90  ? 33.862 -4.981  17.831  0.48 28.67 ?  90  LYS   A NZ   1 
ATOM   2003 N NZ   B LYS   A 1 90  ? 33.899 -4.489  17.948  0.52 28.05 ?  90  LYS   A NZ   1 
ATOM   2004 H H    A LYS   A 1 90  ? 27.460 -2.357  16.466  0.48 16.93 ?  90  LYS   A H    1 
ATOM   2005 H H    B LYS   A 1 90  ? 27.442 -2.325  16.576  0.52 16.13 ?  90  LYS   A H    1 
ATOM   2006 H HA   A LYS   A 1 90  ? 29.702 -1.117  17.043  0.48 18.36 ?  90  LYS   A HA   1 
ATOM   2007 H HA   B LYS   A 1 90  ? 29.678 -1.101  17.148  0.52 16.92 ?  90  LYS   A HA   1 
ATOM   2008 H HB2  A LYS   A 1 90  ? 29.217 -3.229  17.949  0.48 21.22 ?  90  LYS   A HB2  1 
ATOM   2009 H HB2  B LYS   A 1 90  ? 29.175 -3.262  17.967  0.52 19.73 ?  90  LYS   A HB2  1 
ATOM   2010 H HB3  A LYS   A 1 90  ? 29.435 -3.874  16.515  0.48 21.22 ?  90  LYS   A HB3  1 
ATOM   2011 H HB3  B LYS   A 1 90  ? 29.465 -3.843  16.518  0.52 19.73 ?  90  LYS   A HB3  1 
ATOM   2012 H HG2  A LYS   A 1 90  ? 31.675 -3.462  16.588  0.48 25.56 ?  90  LYS   A HG2  1 
ATOM   2013 H HG2  B LYS   A 1 90  ? 31.692 -3.323  16.693  0.52 24.47 ?  90  LYS   A HG2  1 
ATOM   2014 H HG3  A LYS   A 1 90  ? 31.516 -2.549  17.882  0.48 25.56 ?  90  LYS   A HG3  1 
ATOM   2015 H HG3  B LYS   A 1 90  ? 31.441 -2.550  18.062  0.52 24.47 ?  90  LYS   A HG3  1 
ATOM   2016 H HD2  A LYS   A 1 90  ? 30.819 -4.522  19.056  0.48 29.33 ?  90  LYS   A HD2  1 
ATOM   2017 H HD2  B LYS   A 1 90  ? 30.752 -4.679  18.974  0.52 28.50 ?  90  LYS   A HD2  1 
ATOM   2018 H HD3  A LYS   A 1 90  ? 31.289 -5.356  17.785  0.48 29.33 ?  90  LYS   A HD3  1 
ATOM   2019 H HD3  B LYS   A 1 90  ? 31.388 -5.335  17.670  0.52 28.50 ?  90  LYS   A HD3  1 
ATOM   2020 H HE2  A LYS   A 1 90  ? 33.089 -3.695  19.171  0.48 32.32 ?  90  LYS   A HE2  1 
ATOM   2021 H HE2  B LYS   A 1 90  ? 32.857 -3.792  19.522  0.52 31.62 ?  90  LYS   A HE2  1 
ATOM   2022 H HE3  A LYS   A 1 90  ? 32.898 -5.218  19.581  0.48 32.32 ?  90  LYS   A HE3  1 
ATOM   2023 H HE3  B LYS   A 1 90  ? 32.907 -5.380  19.456  0.52 31.62 ?  90  LYS   A HE3  1 
ATOM   2024 H HZ1  A LYS   A 1 90  ? 34.670 -5.031  18.204  0.48 34.38 ?  90  LYS   A HZ1  1 
ATOM   2025 H HZ1  B LYS   A 1 90  ? 34.683 -4.469  18.369  0.52 33.64 ?  90  LYS   A HZ1  1 
ATOM   2026 H HZ2  A LYS   A 1 90  ? 33.653 -5.776  17.491  0.48 34.38 ?  90  LYS   A HZ2  1 
ATOM   2027 H HZ2  B LYS   A 1 90  ? 33.877 -5.201  17.414  0.52 33.64 ?  90  LYS   A HZ2  1 
ATOM   2028 H HZ3  A LYS   A 1 90  ? 33.886 -4.382  17.174  0.48 34.38 ?  90  LYS   A HZ3  1 
ATOM   2029 H HZ3  B LYS   A 1 90  ? 33.815 -3.754  17.456  0.52 33.64 ?  90  LYS   A HZ3  1 
ATOM   2030 N N    A HIS   A 1 91  ? 29.635 -2.414  14.111  0.48 13.48 ?  91  HIS   A N    1 
ATOM   2031 N N    B HIS   A 1 91  ? 29.577 -2.281  14.178  0.52 11.38 ?  91  HIS   A N    1 
ATOM   2032 C CA   A HIS   A 1 91  ? 30.226 -2.401  12.785  0.48 12.89 ?  91  HIS   A CA   1 
ATOM   2033 C CA   B HIS   A 1 91  ? 30.167 -2.260  12.854  0.52 10.80 ?  91  HIS   A CA   1 
ATOM   2034 C C    A HIS   A 1 91  ? 29.146 -2.147  11.750  0.48 11.11 ?  91  HIS   A C    1 
ATOM   2035 C C    B HIS   A 1 91  ? 29.092 -1.989  11.818  0.52 10.36 ?  91  HIS   A C    1 
ATOM   2036 O O    A HIS   A 1 91  ? 27.998 -2.572  11.908  0.48 10.50 ?  91  HIS   A O    1 
ATOM   2037 O O    B HIS   A 1 91  ? 27.908 -2.267  12.028  0.52 10.76 ?  91  HIS   A O    1 
ATOM   2038 C CB   A HIS   A 1 91  ? 30.852 -3.755  12.435  0.48 15.12 ?  91  HIS   A CB   1 
ATOM   2039 C CB   B HIS   A 1 91  ? 30.787 -3.614  12.505  0.52 12.95 ?  91  HIS   A CB   1 
ATOM   2040 C CG   A HIS   A 1 91  ? 31.850 -4.241  13.435  0.48 18.28 ?  91  HIS   A CG   1 
ATOM   2041 C CG   B HIS   A 1 91  ? 31.740 -4.126  13.534  0.52 16.52 ?  91  HIS   A CG   1 
ATOM   2042 N ND1  A HIS   A 1 91  ? 33.114 -3.706  13.544  0.48 19.91 ?  91  HIS   A ND1  1 
ATOM   2043 N ND1  B HIS   A 1 91  ? 33.014 -3.623  13.679  0.52 18.47 ?  91  HIS   A ND1  1 
ATOM   2044 C CD2  A HIS   A 1 91  ? 31.777 -5.227  14.360  0.48 19.68 ?  91  HIS   A CD2  1 
ATOM   2045 C CD2  B HIS   A 1 91  ? 31.610 -5.099  14.465  0.52 18.20 ?  91  HIS   A CD2  1 
ATOM   2046 C CE1  A HIS   A 1 91  ? 33.775 -4.334  14.501  0.48 20.60 ?  91  HIS   A CE1  1 
ATOM   2047 C CE1  B HIS   A 1 91  ? 33.629 -4.264  14.658  0.52 19.23 ?  91  HIS   A CE1  1 
ATOM   2048 N NE2  A HIS   A 1 91  ? 32.986 -5.262  15.012  0.48 20.68 ?  91  HIS   A NE2  1 
ATOM   2049 N NE2  B HIS   A 1 91  ? 32.797 -5.165  15.152  0.52 19.31 ?  91  HIS   A NE2  1 
ATOM   2050 H H    A HIS   A 1 91  ? 28.963 -2.957  14.177  0.48 16.15 ?  91  HIS   A H    1 
ATOM   2051 H H    B HIS   A 1 91  ? 28.869 -2.786  14.230  0.52 13.63 ?  91  HIS   A H    1 
ATOM   2052 H HA   A HIS   A 1 91  ? 30.896 -1.710  12.714  0.48 15.44 ?  91  HIS   A HA   1 
ATOM   2053 H HA   B HIS   A 1 91  ? 30.838 -1.568  12.805  0.52 12.94 ?  91  HIS   A HA   1 
ATOM   2054 H HB2  A HIS   A 1 91  ? 30.148 -4.420  12.372  0.48 18.12 ?  91  HIS   A HB2  1 
ATOM   2055 H HB2  B HIS   A 1 91  ? 30.075 -4.267  12.407  0.52 15.51 ?  91  HIS   A HB2  1 
ATOM   2056 H HB3  A HIS   A 1 91  ? 31.304 -3.676  11.579  0.48 18.12 ?  91  HIS   A HB3  1 
ATOM   2057 H HB3  B HIS   A 1 91  ? 31.266 -3.524  11.667  0.52 15.51 ?  91  HIS   A HB3  1 
ATOM   2058 H HD1  A HIS   A 1 91  ? 33.423 -3.060  13.065  0.48 23.87 ?  91  HIS   A HD1  1 
ATOM   2059 H HD1  B HIS   A 1 91  ? 33.357 -2.988  13.204  0.52 22.14 ?  91  HIS   A HD1  1 
ATOM   2060 H HD2  A HIS   A 1 91  ? 31.042 -5.770  14.526  0.48 23.59 ?  91  HIS   A HD2  1 
ATOM   2061 H HD2  B HIS   A 1 91  ? 30.861 -5.625  14.612  0.52 21.82 ?  91  HIS   A HD2  1 
ATOM   2062 H HE1  A HIS   A 1 91  ? 34.646 -4.152  14.768  0.48 24.70 ?  91  HIS   A HE1  1 
ATOM   2063 H HE1  B HIS   A 1 91  ? 34.500 -4.104  14.945  0.52 23.06 ?  91  HIS   A HE1  1 
ATOM   2064 N N    . CYS   A 1 92  ? 29.529 -1.466  10.676  1.00 10.43 ?  92  CYS   A N    1 
ATOM   2065 C CA   . CYS   A 1 92  ? 28.706 -1.380  9.479   1.00 10.30 ?  92  CYS   A CA   1 
ATOM   2066 C C    . CYS   A 1 92  ? 29.364 -2.199  8.378   1.00 9.73  ?  92  CYS   A C    1 
ATOM   2067 O O    . CYS   A 1 92  ? 30.527 -1.960  8.024   1.00 10.76 ?  92  CYS   A O    1 
ATOM   2068 C CB   . CYS   A 1 92  ? 28.492 0.060   9.016   1.00 10.60 ?  92  CYS   A CB   1 
ATOM   2069 S SG   . CYS   A 1 92  ? 27.491 0.159   7.498   1.00 10.07 ?  92  CYS   A SG   1 
ATOM   2070 H H    A CYS   A 1 92  ? 30.267 -1.033  10.621  0.48 12.49 ?  92  CYS   A H    1 
ATOM   2071 H H    B CYS   A 1 92  ? 30.324 -1.165  10.563  0.52 12.49 ?  92  CYS   A H    1 
ATOM   2072 H HA   . CYS   A 1 92  ? 27.836 -1.764  9.661   1.00 12.33 ?  92  CYS   A HA   1 
ATOM   2073 H HB2  . CYS   A 1 92  ? 28.025 0.556   9.711   1.00 12.69 ?  92  CYS   A HB2  1 
ATOM   2074 H HB3  . CYS   A 1 92  ? 29.348 0.472   8.832   1.00 12.69 ?  92  CYS   A HB3  1 
ATOM   2075 H HG   . CYS   A 1 92  ? 27.345 1.308   7.203   1.00 12.06 ?  92  CYS   A HG   1 
ATOM   2076 N N    . LEU   A 1 93  ? 28.635 -3.188  7.872   1.00 9.49  ?  93  LEU   A N    1 
ATOM   2077 C CA   . LEU   A 1 93  ? 29.051 -3.950  6.702   1.00 9.40  ?  93  LEU   A CA   1 
ATOM   2078 C C    . LEU   A 1 93  ? 28.464 -3.266  5.470   1.00 8.98  ?  93  LEU   A C    1 
ATOM   2079 O O    . LEU   A 1 93  ? 27.251 -3.326  5.233   1.00 8.99  ?  93  LEU   A O    1 
ATOM   2080 C CB   . LEU   A 1 93  ? 28.576 -5.398  6.819   1.00 9.53  ?  93  LEU   A CB   1 
ATOM   2081 C CG   . LEU   A 1 93  ? 28.970 -6.300  5.647   1.00 10.41 ?  93  LEU   A CG   1 
ATOM   2082 C CD1  . LEU   A 1 93  ? 30.475 -6.553  5.618   1.00 11.11 ?  93  LEU   A CD1  1 
ATOM   2083 C CD2  . LEU   A 1 93  ? 28.199 -7.626  5.688   1.00 11.20 ?  93  LEU   A CD2  1 
ATOM   2084 H H    . LEU   A 1 93  ? 27.878 -3.439  8.204   1.00 11.36 ?  93  LEU   A H    1 
ATOM   2085 H HA   . LEU   A 1 93  ? 30.015 -3.934  6.638   1.00 11.25 ?  93  LEU   A HA   1 
ATOM   2086 H HB2  . LEU   A 1 93  ? 28.961 -5.779  7.627   1.00 11.42 ?  93  LEU   A HB2  1 
ATOM   2087 H HB3  . LEU   A 1 93  ? 27.612 -5.403  6.886   1.00 11.42 ?  93  LEU   A HB3  1 
ATOM   2088 H HG   . LEU   A 1 93  ? 28.735 -5.858  4.823   1.00 12.47 ?  93  LEU   A HG   1 
ATOM   2089 H HD11 . LEU   A 1 93  ? 30.681 -7.161  4.893   1.00 13.31 ?  93  LEU   A HD11 1 
ATOM   2090 H HD12 . LEU   A 1 93  ? 30.935 -5.710  5.486   1.00 13.31 ?  93  LEU   A HD12 1 
ATOM   2091 H HD13 . LEU   A 1 93  ? 30.748 -6.947  6.465   1.00 13.31 ?  93  LEU   A HD13 1 
ATOM   2092 H HD21 . LEU   A 1 93  ? 28.474 -8.175  4.934   1.00 13.42 ?  93  LEU   A HD21 1 
ATOM   2093 H HD22 . LEU   A 1 93  ? 28.402 -8.089  6.519   1.00 13.42 ?  93  LEU   A HD22 1 
ATOM   2094 H HD23 . LEU   A 1 93  ? 27.249 -7.444  5.634   1.00 13.42 ?  93  LEU   A HD23 1 
ATOM   2095 N N    . HIS   A 1 94  ? 29.316 -2.575  4.713   1.00 8.88  ?  94  HIS   A N    1 
ATOM   2096 C CA   . HIS   A 1 94  ? 28.901 -1.908  3.482   1.00 9.31  ?  94  HIS   A CA   1 
ATOM   2097 C C    . HIS   A 1 94  ? 28.924 -2.941  2.370   1.00 9.10  ?  94  HIS   A C    1 
ATOM   2098 O O    . HIS   A 1 94  ? 29.996 -3.459  2.036   1.00 10.42 ?  94  HIS   A O    1 
ATOM   2099 C CB   . HIS   A 1 94  ? 29.848 -0.751  3.157   1.00 9.17  ?  94  HIS   A CB   1 
ATOM   2100 C CG   . HIS   A 1 94  ? 29.827 0.337   4.176   1.00 9.04  ?  94  HIS   A CG   1 
ATOM   2101 N ND1  . HIS   A 1 94  ? 28.951 1.404   4.118   1.00 9.34  ?  94  HIS   A ND1  1 
ATOM   2102 C CD2  . HIS   A 1 94  ? 30.562 0.503   5.299   1.00 9.75  ?  94  HIS   A CD2  1 
ATOM   2103 C CE1  . HIS   A 1 94  ? 29.164 2.180   5.165   1.00 9.49  ?  94  HIS   A CE1  1 
ATOM   2104 N NE2  . HIS   A 1 94  ? 30.136 1.660   5.893   1.00 9.63  ?  94  HIS   A NE2  1 
ATOM   2105 H H    . HIS   A 1 94  ? 30.150 -2.473  4.896   1.00 10.64 ?  94  HIS   A H    1 
ATOM   2106 H HA   . HIS   A 1 94  ? 27.998 -1.563  3.576   1.00 11.15 ?  94  HIS   A HA   1 
ATOM   2107 H HB2  . HIS   A 1 94  ? 30.749 -1.087  3.102   1.00 10.98 ?  94  HIS   A HB2  1 
ATOM   2108 H HB3  . HIS   A 1 94  ? 29.582 -0.359  2.308   1.00 10.98 ?  94  HIS   A HB3  1 
ATOM   2109 H HD2  . HIS   A 1 94  ? 31.240 -0.047  5.608   1.00 11.68 ?  94  HIS   A HD2  1 
ATOM   2110 H HE1  . HIS   A 1 94  ? 28.693 2.965   5.350   1.00 11.36 ?  94  HIS   A HE1  1 
ATOM   2111 H HE2  . HIS   A 1 94  ? 30.442 2.009   6.616   1.00 11.53 ?  94  HIS   A HE2  1 
ATOM   2112 N N    . VAL   A 1 95  ? 27.755 -3.259  1.809   1.00 8.54  ?  95  VAL   A N    1 
ATOM   2113 C CA   . VAL   A 1 95  ? 27.624 -4.297  0.791   1.00 8.79  ?  95  VAL   A CA   1 
ATOM   2114 C C    . VAL   A 1 95  ? 27.088 -3.666  -0.482  1.00 8.69  ?  95  VAL   A C    1 
ATOM   2115 O O    . VAL   A 1 95  ? 26.079 -2.948  -0.440  1.00 9.62  ?  95  VAL   A O    1 
ATOM   2116 C CB   . VAL   A 1 95  ? 26.690 -5.439  1.238   1.00 9.39  ?  95  VAL   A CB   1 
ATOM   2117 C CG1  . VAL   A 1 95  ? 26.593 -6.486  0.133   1.00 10.38 ?  95  VAL   A CG1  1 
ATOM   2118 C CG2  . VAL   A 1 95  ? 27.176 -6.053  2.535   1.00 9.83  ?  95  VAL   A CG2  1 
ATOM   2119 H H    . VAL   A 1 95  ? 27.005 -2.882  2.010   1.00 10.22 ?  95  VAL   A H    1 
ATOM   2120 H HA   . VAL   A 1 95  ? 28.496 -4.676  0.602   1.00 10.52 ?  95  VAL   A HA   1 
ATOM   2121 H HB   . VAL   A 1 95  ? 25.804 -5.083  1.388   1.00 11.25 ?  95  VAL   A HB   1 
ATOM   2122 H HG11 . VAL   A 1 95  ? 26.203 -7.299  0.496   1.00 12.44 ?  95  VAL   A HG11 1 
ATOM   2123 H HG12 . VAL   A 1 95  ? 26.029 -6.149  -0.584  1.00 12.44 ?  95  VAL   A HG12 1 
ATOM   2124 H HG13 . VAL   A 1 95  ? 27.482 -6.677  -0.210  1.00 12.44 ?  95  VAL   A HG13 1 
ATOM   2125 H HG21 . VAL   A 1 95  ? 26.607 -6.809  2.756   1.00 11.77 ?  95  VAL   A HG21 1 
ATOM   2126 H HG22 . VAL   A 1 95  ? 28.091 -6.351  2.420   1.00 11.77 ?  95  VAL   A HG22 1 
ATOM   2127 H HG23 . VAL   A 1 95  ? 27.126 -5.385  3.234   1.00 11.77 ?  95  VAL   A HG23 1 
ATOM   2128 N N    . VAL   A 1 96  ? 27.729 -3.964  -1.611  1.00 8.68  ?  96  VAL   A N    1 
ATOM   2129 C CA   . VAL   A 1 96  ? 27.325 -3.421  -2.902  1.00 9.64  ?  96  VAL   A CA   1 
ATOM   2130 C C    . VAL   A 1 96  ? 26.536 -4.472  -3.676  1.00 9.80  ?  96  VAL   A C    1 
ATOM   2131 O O    . VAL   A 1 96  ? 27.107 -5.418  -4.222  1.00 10.73 ?  96  VAL   A O    1 
ATOM   2132 C CB   . VAL   A 1 96  ? 28.523 -2.941  -3.723  1.00 10.04 ?  96  VAL   A CB   1 
ATOM   2133 C CG1  . VAL   A 1 96  ? 28.030 -2.324  -5.016  1.00 10.31 ?  96  VAL   A CG1  1 
ATOM   2134 C CG2  . VAL   A 1 96  ? 29.366 -1.951  -2.928  1.00 10.68 ?  96  VAL   A CG2  1 
ATOM   2135 H H    . VAL   A 1 96  ? 28.423 -4.479  -1.653  1.00 10.39 ?  96  VAL   A H    1 
ATOM   2136 H HA   . VAL   A 1 96  ? 26.745 -2.662  -2.754  1.00 11.55 ?  96  VAL   A HA   1 
ATOM   2137 H HB   . VAL   A 1 96  ? 29.083 -3.695  -3.946  1.00 12.03 ?  96  VAL   A HB   1 
ATOM   2138 H HG11 . VAL   A 1 96  ? 28.761 -1.833  -5.429  1.00 12.35 ?  96  VAL   A HG11 1 
ATOM   2139 H HG12 . VAL   A 1 96  ? 27.731 -3.027  -5.611  1.00 12.35 ?  96  VAL   A HG12 1 
ATOM   2140 H HG13 . VAL   A 1 96  ? 27.298 -1.717  -4.821  1.00 12.35 ?  96  VAL   A HG13 1 
ATOM   2141 H HG21 . VAL   A 1 96  ? 30.069 -1.605  -3.496  1.00 12.79 ?  96  VAL   A HG21 1 
ATOM   2142 H HG22 . VAL   A 1 96  ? 28.795 -1.220  -2.628  1.00 12.79 ?  96  VAL   A HG22 1 
ATOM   2143 H HG23 . VAL   A 1 96  ? 29.747 -2.404  -2.162  1.00 12.79 ?  96  VAL   A HG23 1 
ATOM   2144 N N    A GLY   A 1 97  ? 25.215 -4.326  -3.683  0.48 10.03 ?  97  GLY   A N    1 
ATOM   2145 N N    B GLY   A 1 97  ? 25.220 -4.304  -3.772  0.52 9.73  ?  97  GLY   A N    1 
ATOM   2146 C CA   A GLY   A 1 97  ? 24.379 -5.067  -4.589  0.48 10.66 ?  97  GLY   A CA   1 
ATOM   2147 C CA   B GLY   A 1 97  ? 24.440 -5.092  -4.696  0.52 10.21 ?  97  GLY   A CA   1 
ATOM   2148 C C    A GLY   A 1 97  ? 24.345 -4.372  -5.933  0.48 10.72 ?  97  GLY   A C    1 
ATOM   2149 C C    B GLY   A 1 97  ? 24.515 -4.516  -6.099  0.52 10.48 ?  97  GLY   A C    1 
ATOM   2150 O O    A GLY   A 1 97  ? 24.596 -3.166  -6.036  0.48 10.95 ?  97  GLY   A O    1 
ATOM   2151 O O    B GLY   A 1 97  ? 24.831 -3.335  -6.289  0.52 11.05 ?  97  GLY   A O    1 
ATOM   2152 H H    A GLY   A 1 97  ? 24.782 -3.787  -3.166  0.48 12.01 ?  97  GLY   A H    1 
ATOM   2153 H H    B GLY   A 1 97  ? 24.761 -3.737  -3.311  0.52 11.65 ?  97  GLY   A H    1 
ATOM   2154 H HA2  A GLY   A 1 97  ? 24.736 -5.958  -4.701  0.48 12.77 ?  97  GLY   A HA2  1 
ATOM   2155 H HA2  B GLY   A 1 97  ? 24.777 -6.003  -4.700  0.52 12.23 ?  97  GLY   A HA2  1 
ATOM   2156 H HA3  A GLY   A 1 97  ? 23.477 -5.127  -4.233  0.48 12.77 ?  97  GLY   A HA3  1 
ATOM   2157 H HA3  B GLY   A 1 97  ? 23.512 -5.105  -4.414  0.52 12.23 ?  97  GLY   A HA3  1 
ATOM   2158 N N    A PRO   A 1 98  ? 24.042 -5.114  -6.993  0.48 10.41 ?  98  PRO   A N    1 
ATOM   2159 N N    B PRO   A 1 98  ? 24.220 -5.330  -7.113  0.52 11.01 ?  98  PRO   A N    1 
ATOM   2160 C CA   A PRO   A 1 98  ? 23.947 -4.490  -8.317  0.48 10.65 ?  98  PRO   A CA   1 
ATOM   2161 C CA   B PRO   A 1 98  ? 24.196 -4.810  -8.486  0.52 11.68 ?  98  PRO   A CA   1 
ATOM   2162 C C    A PRO   A 1 98  ? 22.836 -3.452  -8.355  0.48 10.85 ?  98  PRO   A C    1 
ATOM   2163 C C    B PRO   A 1 98  ? 23.081 -3.793  -8.686  0.52 11.99 ?  98  PRO   A C    1 
ATOM   2164 O O    A PRO   A 1 98  ? 21.769 -3.632  -7.763  0.48 10.36 ?  98  PRO   A O    1 
ATOM   2165 O O    B PRO   A 1 98  ? 21.973 -3.937  -8.163  0.52 12.35 ?  98  PRO   A O    1 
ATOM   2166 C CB   A PRO   A 1 98  ? 23.637 -5.672  -9.244  0.48 10.82 ?  98  PRO   A CB   1 
ATOM   2167 C CB   B PRO   A 1 98  ? 23.955 -6.064  -9.337  0.52 11.79 ?  98  PRO   A CB   1 
ATOM   2168 C CG   A PRO   A 1 98  ? 23.016 -6.702  -8.354  0.48 10.53 ?  98  PRO   A CG   1 
ATOM   2169 C CG   B PRO   A 1 98  ? 23.312 -7.043  -8.403  0.52 12.34 ?  98  PRO   A CG   1 
ATOM   2170 C CD   A PRO   A 1 98  ? 23.714 -6.550  -7.030  0.48 10.42 ?  98  PRO   A CD   1 
ATOM   2171 C CD   B PRO   A 1 98  ? 23.944 -6.777  -7.064  0.52 11.54 ?  98  PRO   A CD   1 
ATOM   2172 H HA   A PRO   A 1 98  ? 24.790 -4.084  -8.564  0.48 12.76 ?  98  PRO   A HA   1 
ATOM   2173 H HA   B PRO   A 1 98  ? 25.055 -4.417  -8.718  0.52 13.99 ?  98  PRO   A HA   1 
ATOM   2174 H HB2  A PRO   A 1 98  ? 23.012 -5.392  -9.930  0.48 12.96 ?  98  PRO   A HB2  1 
ATOM   2175 H HB2  B PRO   A 1 98  ? 23.361 -5.848  -10.071 0.52 14.13 ?  98  PRO   A HB2  1 
ATOM   2176 H HB3  A PRO   A 1 98  ? 24.458 -6.004  -9.634  0.48 12.96 ?  98  PRO   A HB3  1 
ATOM   2177 H HB3  B PRO   A 1 98  ? 24.801 -6.408  -9.666  0.52 14.13 ?  98  PRO   A HB3  1 
ATOM   2178 H HG2  A PRO   A 1 98  ? 22.068 -6.528  -8.260  0.48 12.61 ?  98  PRO   A HG2  1 
ATOM   2179 H HG2  B PRO   A 1 98  ? 22.356 -6.884  -8.367  0.52 14.79 ?  98  PRO   A HG2  1 
ATOM   2180 H HG3  A PRO   A 1 98  ? 23.172 -7.586  -8.720  0.48 12.61 ?  98  PRO   A HG3  1 
ATOM   2181 H HG3  B PRO   A 1 98  ? 23.498 -7.950  -8.698  0.52 14.79 ?  98  PRO   A HG3  1 
ATOM   2182 H HD2  A PRO   A 1 98  ? 23.117 -6.786  -6.298  0.48 12.48 ?  98  PRO   A HD2  1 
ATOM   2183 H HD2  B PRO   A 1 98  ? 23.322 -6.982  -6.346  0.52 13.82 ?  98  PRO   A HD2  1 
ATOM   2184 H HD3  A PRO   A 1 98  ? 24.528 -7.080  -7.004  0.48 12.48 ?  98  PRO   A HD3  1 
ATOM   2185 H HD3  B PRO   A 1 98  ? 24.769 -7.286  -6.969  0.52 13.82 ?  98  PRO   A HD3  1 
ATOM   2186 N N    A ASN   A 1 99  ? 23.107 -2.350  -9.051  0.48 11.48 ?  99  ASN   A N    1 
ATOM   2187 N N    B ASN   A 1 99  ? 23.386 -2.758  -9.461  0.52 12.66 ?  99  ASN   A N    1 
ATOM   2188 C CA   A ASN   A 1 99  ? 22.128 -1.289  -9.278  0.48 12.69 ?  99  ASN   A CA   1 
ATOM   2189 C CA   B ASN   A 1 99  ? 22.426 -1.722  -9.839  0.52 14.09 ?  99  ASN   A CA   1 
ATOM   2190 C C    A ASN   A 1 99  ? 21.578 -1.465  -10.690 0.48 13.55 ?  99  ASN   A C    1 
ATOM   2191 C C    B ASN   A 1 99  ? 21.977 -2.029  -11.264 0.52 14.23 ?  99  ASN   A C    1 
ATOM   2192 O O    A ASN   A 1 99  ? 22.243 -1.128  -11.675 0.48 14.72 ?  99  ASN   A O    1 
ATOM   2193 O O    B ASN   A 1 99  ? 22.714 -1.792  -12.222 0.52 14.08 ?  99  ASN   A O    1 
ATOM   2194 C CB   A ASN   A 1 99  ? 22.772 0.083   -9.106  0.48 13.42 ?  99  ASN   A CB   1 
ATOM   2195 C CB   B ASN   A 1 99  ? 23.095 -0.354  -9.763  0.52 15.86 ?  99  ASN   A CB   1 
ATOM   2196 C CG   A ASN   A 1 99  ? 21.750 1.221   -9.059  0.48 14.22 ?  99  ASN   A CG   1 
ATOM   2197 C CG   B ASN   A 1 99  ? 22.140 0.785   -10.055 0.52 17.31 ?  99  ASN   A CG   1 
ATOM   2198 O OD1  A ASN   A 1 99  ? 20.735 1.196   -9.755  0.48 14.54 ?  99  ASN   A OD1  1 
ATOM   2199 O OD1  B ASN   A 1 99  ? 21.103 0.598   -10.683 0.52 17.36 ?  99  ASN   A OD1  1 
ATOM   2200 N ND2  A ASN   A 1 99  ? 22.026 2.225   -8.238  0.48 14.60 ?  99  ASN   A ND2  1 
ATOM   2201 N ND2  B ASN   A 1 99  ? 22.498 1.979   -9.606  0.52 18.71 ?  99  ASN   A ND2  1 
ATOM   2202 H H    A ASN   A 1 99  ? 23.875 -2.188  -9.398  0.48 13.75 ?  99  ASN   A H    1 
ATOM   2203 H H    B ASN   A 1 99  ? 24.174 -2.631  -9.782  0.52 15.16 ?  99  ASN   A H    1 
ATOM   2204 H HA   A ASN   A 1 99  ? 21.399 -1.381  -8.642  0.48 15.20 ?  99  ASN   A HA   1 
ATOM   2205 H HA   B ASN   A 1 99  ? 21.659 -1.748  -9.244  0.52 16.89 ?  99  ASN   A HA   1 
ATOM   2206 H HB2  A ASN   A 1 99  ? 23.277 0.092   -8.281  0.48 16.08 ?  99  ASN   A HB2  1 
ATOM   2207 H HB2  B ASN   A 1 99  ? 23.461 -0.230  -8.874  0.52 19.01 ?  99  ASN   A HB2  1 
ATOM   2208 H HB3  A ASN   A 1 99  ? 23.365 0.242   -9.860  0.48 16.08 ?  99  ASN   A HB3  1 
ATOM   2209 H HB3  B ASN   A 1 99  ? 23.800 -0.330  -10.423 0.52 19.01 ?  99  ASN   A HB3  1 
ATOM   2210 H HD21 A ASN   A 1 99  ? 21.483 2.884   -8.174  0.48 17.49 ?  99  ASN   A HD21 1 
ATOM   2211 H HD21 B ASN   A 1 99  ? 21.990 2.657   -9.742  0.52 22.43 ?  99  ASN   A HD21 1 
ATOM   2212 H HD22 A ASN   A 1 99  ? 22.748 2.209   -7.769  0.48 17.49 ?  99  ASN   A HD22 1 
ATOM   2213 H HD22 B ASN   A 1 99  ? 23.236 2.073   -9.180  0.52 22.43 ?  99  ASN   A HD22 1 
ATOM   2214 N N    A VAL   A 1 100 ? 20.355 -1.998  -10.780 0.48 14.39 ?  100 VAL   A N    1 
ATOM   2215 N N    B VAL   A 1 100 ? 20.766 -2.573  -11.409 0.52 16.09 ?  100 VAL   A N    1 
ATOM   2216 C CA   A VAL   A 1 100 ? 19.722 -2.232  -12.077 0.48 16.36 ?  100 VAL   A CA   1 
ATOM   2217 C CA   B VAL   A 1 100 ? 20.305 -2.955  -12.741 0.52 18.21 ?  100 VAL   A CA   1 
ATOM   2218 C C    A VAL   A 1 100 ? 19.628 -0.938  -12.875 0.48 17.21 ?  100 VAL   A C    1 
ATOM   2219 C C    B VAL   A 1 100 ? 19.978 -1.742  -13.602 0.52 19.07 ?  100 VAL   A C    1 
ATOM   2220 O O    A VAL   A 1 100 ? 19.746 -0.947  -14.106 0.48 17.96 ?  100 VAL   A O    1 
ATOM   2221 O O    B VAL   A 1 100 ? 19.865 -1.876  -14.825 0.52 19.53 ?  100 VAL   A O    1 
ATOM   2222 C CB   A VAL   A 1 100 ? 18.345 -2.908  -11.886 0.48 17.98 ?  100 VAL   A CB   1 
ATOM   2223 C CB   B VAL   A 1 100 ? 19.150 -3.975  -12.697 0.52 19.63 ?  100 VAL   A CB   1 
ATOM   2224 C CG1  A VAL   A 1 100 ? 17.631 -3.089  -13.222 0.48 18.63 ?  100 VAL   A CG1  1 
ATOM   2225 C CG1  B VAL   A 1 100 ? 19.554 -5.187  -11.873 0.52 20.12 ?  100 VAL   A CG1  1 
ATOM   2226 C CG2  A VAL   A 1 100 ? 18.507 -4.254  -11.189 0.48 18.38 ?  100 VAL   A CG2  1 
ATOM   2227 C CG2  B VAL   A 1 100 ? 17.881 -3.336  -12.162 0.52 20.20 ?  100 VAL   A CG2  1 
ATOM   2228 H H    A VAL   A 1 100 ? 19.868 -2.230  -10.104 0.48 17.25 ?  100 VAL   A H    1 
ATOM   2229 H H    B VAL   A 1 100 ? 20.218 -2.735  -10.773 0.52 19.29 ?  100 VAL   A H    1 
ATOM   2230 H HA   A VAL   A 1 100 ? 20.269 -2.850  -12.583 0.48 19.61 ?  100 VAL   A HA   1 
ATOM   2231 H HA   B VAL   A 1 100 ? 21.038 -3.402  -13.184 0.52 21.83 ?  100 VAL   A HA   1 
ATOM   2232 H HB   A VAL   A 1 100 ? 17.785 -2.351  -11.323 0.48 21.56 ?  100 VAL   A HB   1 
ATOM   2233 H HB   B VAL   A 1 100 ? 18.968 -4.277  -13.604 0.52 23.53 ?  100 VAL   A HB   1 
ATOM   2234 H HG11 A VAL   A 1 100 ? 16.872 -3.685  -13.099 0.48 22.33 ?  100 VAL   A HG11 1 
ATOM   2235 H HG11 B VAL   A 1 100 ? 18.848 -5.849  -11.921 0.52 24.12 ?  100 VAL   A HG11 1 
ATOM   2236 H HG12 A VAL   A 1 100 ? 17.321 -2.226  -13.536 0.48 22.33 ?  100 VAL   A HG12 1 
ATOM   2237 H HG12 B VAL   A 1 100 ? 20.377 -5.552  -12.234 0.52 24.12 ?  100 VAL   A HG12 1 
ATOM   2238 H HG13 A VAL   A 1 100 ? 18.250 -3.475  -13.861 0.48 22.33 ?  100 VAL   A HG13 1 
ATOM   2239 H HG13 B VAL   A 1 100 ? 19.689 -4.911  -10.954 0.52 24.12 ?  100 VAL   A HG13 1 
ATOM   2240 H HG21 A VAL   A 1 100 ? 17.641 -4.692  -11.133 0.48 22.03 ?  100 VAL   A HG21 1 
ATOM   2241 H HG21 B VAL   A 1 100 ? 17.213 -4.027  -12.032 0.52 24.21 ?  100 VAL   A HG21 1 
ATOM   2242 H HG22 A VAL   A 1 100 ? 19.121 -4.804  -11.701 0.48 22.03 ?  100 VAL   A HG22 1 
ATOM   2243 H HG22 B VAL   A 1 100 ? 18.080 -2.902  -11.320 0.52 24.21 ?  100 VAL   A HG22 1 
ATOM   2244 H HG23 A VAL   A 1 100 ? 18.859 -4.109  -10.297 0.48 22.03 ?  100 VAL   A HG23 1 
ATOM   2245 H HG23 B VAL   A 1 100 ? 17.558 -2.683  -12.804 0.52 24.21 ?  100 VAL   A HG23 1 
ATOM   2246 N N    A ASN   A 1 101 ? 19.420 0.192   -12.200 0.48 18.14 ?  101 ASN   A N    1 
ATOM   2247 N N    B ASN   A 1 101 ? 19.823 -0.558  -13.001 0.52 19.51 ?  101 ASN   A N    1 
ATOM   2248 C CA   A ASN   A 1 101 ? 19.336 1.473   -12.892 0.48 19.15 ?  101 ASN   A CA   1 
ATOM   2249 C CA   B ASN   A 1 101 ? 19.741 0.669   -13.788 0.52 20.59 ?  101 ASN   A CA   1 
ATOM   2250 C C    A ASN   A 1 101 ? 20.681 1.936   -13.443 0.48 20.67 ?  101 ASN   A C    1 
ATOM   2251 C C    B ASN   A 1 101 ? 21.079 1.027   -14.420 0.52 21.47 ?  101 ASN   A C    1 
ATOM   2252 O O    A ASN   A 1 101 ? 20.730 2.974   -14.117 0.48 21.68 ?  101 ASN   A O    1 
ATOM   2253 O O    B ASN   A 1 101 ? 21.102 1.773   -15.405 0.52 21.77 ?  101 ASN   A O    1 
ATOM   2254 C CB   A ASN   A 1 101 ? 18.730 2.526   -11.964 0.48 18.36 ?  101 ASN   A CB   1 
ATOM   2255 C CB   B ASN   A 1 101 ? 19.246 1.831   -12.920 0.52 21.12 ?  101 ASN   A CB   1 
ATOM   2256 C CG   A ASN   A 1 101 ? 17.363 2.121   -11.446 0.48 18.44 ?  101 ASN   A CG   1 
ATOM   2257 C CG   B ASN   A 1 101 ? 17.906 1.544   -12.273 0.52 22.06 ?  101 ASN   A CG   1 
ATOM   2258 O OD1  A ASN   A 1 101 ? 16.534 1.598   -12.192 0.48 18.31 ?  101 ASN   A OD1  1 
ATOM   2259 O OD1  B ASN   A 1 101 ? 17.067 0.841   -12.837 0.52 22.94 ?  101 ASN   A OD1  1 
ATOM   2260 N ND2  A ASN   A 1 101 ? 17.127 2.343   -10.157 0.48 19.01 ?  101 ASN   A ND2  1 
ATOM   2261 N ND2  B ASN   A 1 101 ? 17.703 2.081   -11.077 0.52 22.28 ?  101 ASN   A ND2  1 
ATOM   2262 H H    A ASN   A 1 101 ? 19.321 0.237   -11.349 0.48 21.75 ?  101 ASN   A H    1 
ATOM   2263 H H    B ASN   A 1 101 ? 19.754 -0.441  -12.154 0.52 23.39 ?  101 ASN   A H    1 
ATOM   2264 H HA   A ASN   A 1 101 ? 18.734 1.369   -13.644 0.48 22.96 ?  101 ASN   A HA   1 
ATOM   2265 H HA   B ASN   A 1 101 ? 19.103 0.544   -14.505 0.52 24.68 ?  101 ASN   A HA   1 
ATOM   2266 H HB2  A ASN   A 1 101 ? 19.315 2.655   -11.204 0.48 22.01 ?  101 ASN   A HB2  1 
ATOM   2267 H HB2  B ASN   A 1 101 ? 19.891 2.004   -12.216 0.52 25.33 ?  101 ASN   A HB2  1 
ATOM   2268 H HB3  A ASN   A 1 101 ? 18.630 3.356   -12.456 0.48 22.01 ?  101 ASN   A HB3  1 
ATOM   2269 H HB3  B ASN   A 1 101 ? 19.144 2.620   -13.475 0.52 25.33 ?  101 ASN   A HB3  1 
ATOM   2270 H HD21 A ASN   A 1 101 ? 16.367 2.129   -9.815  0.48 22.79 ?  101 ASN   A HD21 1 
ATOM   2271 H HD21 B ASN   A 1 101 ? 16.960 1.945   -10.667 0.52 26.71 ?  101 ASN   A HD21 1 
ATOM   2272 H HD22 A ASN   A 1 101 ? 17.732 2.707   -9.667  0.48 22.79 ?  101 ASN   A HD22 1 
ATOM   2273 H HD22 B ASN   A 1 101 ? 18.315 2.564   -10.713 0.52 26.71 ?  101 ASN   A HD22 1 
ATOM   2274 N N    A LYS   A 1 102 ? 21.762 1.202   -13.175 0.48 21.96 ?  102 LYS   A N    1 
ATOM   2275 N N    B LYS   A 1 102 ? 22.185 0.520   -13.873 0.52 22.46 ?  102 LYS   A N    1 
ATOM   2276 C CA   A LYS   A 1 102 ? 23.040 1.404   -13.844 0.48 23.42 ?  102 LYS   A CA   1 
ATOM   2277 C CA   B LYS   A 1 102 ? 23.518 0.693   -14.441 0.52 23.18 ?  102 LYS   A CA   1 
ATOM   2278 C C    A LYS   A 1 102 ? 23.352 0.306   -14.850 0.48 23.81 ?  102 LYS   A C    1 
ATOM   2279 C C    B LYS   A 1 102 ? 23.905 -0.437  -15.391 0.52 22.11 ?  102 LYS   A C    1 
ATOM   2280 O O    A LYS   A 1 102 ? 24.421 0.341   -15.470 0.48 24.38 ?  102 LYS   A O    1 
ATOM   2281 O O    B LYS   A 1 102 ? 25.051 -0.481  -15.848 0.52 22.77 ?  102 LYS   A O    1 
ATOM   2282 C CB   A LYS   A 1 102 ? 24.179 1.488   -12.821 0.48 24.71 ?  102 LYS   A CB   1 
ATOM   2283 C CB   B LYS   A 1 102 ? 24.574 0.751   -13.329 0.52 25.19 ?  102 LYS   A CB   1 
ATOM   2284 C CG   A LYS   A 1 102 ? 24.035 2.603   -11.803 0.48 25.82 ?  102 LYS   A CG   1 
ATOM   2285 C CG   B LYS   A 1 102 ? 24.493 1.936   -12.378 0.52 27.22 ?  102 LYS   A CG   1 
ATOM   2286 C CD   A LYS   A 1 102 ? 25.208 2.598   -10.836 0.48 27.08 ?  102 LYS   A CD   1 
ATOM   2287 C CD   B LYS   A 1 102 ? 25.549 1.799   -11.277 0.52 29.05 ?  102 LYS   A CD   1 
ATOM   2288 C CE   A LYS   A 1 102 ? 25.079 3.687   -9.784  0.48 28.05 ?  102 LYS   A CE   1 
ATOM   2289 C CE   B LYS   A 1 102 ? 25.493 2.943   -10.276 0.52 30.50 ?  102 LYS   A CE   1 
ATOM   2290 N NZ   A LYS   A 1 102 ? 26.188 3.620   -8.789  0.48 28.59 ?  102 LYS   A NZ   1 
ATOM   2291 N NZ   B LYS   A 1 102 ? 25.531 2.455   -8.863  0.52 31.35 ?  102 LYS   A NZ   1 
ATOM   2292 H H    A LYS   A 1 102 ? 21.779 0.568   -12.593 0.48 26.33 ?  102 LYS   A H    1 
ATOM   2293 H H    B LYS   A 1 102 ? 22.187 0.060   -13.144 0.52 26.93 ?  102 LYS   A H    1 
ATOM   2294 H HA   A LYS   A 1 102 ? 23.013 2.239   -14.327 0.48 28.08 ?  102 LYS   A HA   1 
ATOM   2295 H HA   B LYS   A 1 102 ? 23.547 1.536   -14.923 0.52 27.79 ?  102 LYS   A HA   1 
ATOM   2296 H HB2  A LYS   A 1 102 ? 24.223 0.649   -12.336 0.48 29.63 ?  102 LYS   A HB2  1 
ATOM   2297 H HB2  B LYS   A 1 102 ? 24.498 -0.053  -12.792 0.52 30.20 ?  102 LYS   A HB2  1 
ATOM   2298 H HB3  A LYS   A 1 102 ? 25.012 1.631   -13.299 0.48 29.63 ?  102 LYS   A HB3  1 
ATOM   2299 H HB3  B LYS   A 1 102 ? 25.453 0.777   -13.742 0.52 30.20 ?  102 LYS   A HB3  1 
ATOM   2300 H HG2  A LYS   A 1 102 ? 24.017 3.458   -12.261 0.48 30.96 ?  102 LYS   A HG2  1 
ATOM   2301 H HG2  B LYS   A 1 102 ? 24.666 2.757   -12.865 0.52 32.63 ?  102 LYS   A HG2  1 
ATOM   2302 H HG3  A LYS   A 1 102 ? 23.217 2.474   -11.297 0.48 30.96 ?  102 LYS   A HG3  1 
ATOM   2303 H HG3  B LYS   A 1 102 ? 23.617 1.964   -11.965 0.52 32.63 ?  102 LYS   A HG3  1 
ATOM   2304 H HD2  A LYS   A 1 102 ? 25.244 1.741   -10.382 0.48 32.48 ?  102 LYS   A HD2  1 
ATOM   2305 H HD2  B LYS   A 1 102 ? 25.413 0.968   -10.796 0.52 34.84 ?  102 LYS   A HD2  1 
ATOM   2306 H HD3  A LYS   A 1 102 ? 26.030 2.748   -11.330 0.48 32.48 ?  102 LYS   A HD3  1 
ATOM   2307 H HD3  B LYS   A 1 102 ? 26.429 1.800   -11.685 0.52 34.84 ?  102 LYS   A HD3  1 
ATOM   2308 H HE2  A LYS   A 1 102 ? 25.111 4.555   -10.218 0.48 33.63 ?  102 LYS   A HE2  1 
ATOM   2309 H HE2  B LYS   A 1 102 ? 26.260 3.523   -10.416 0.52 36.57 ?  102 LYS   A HE2  1 
ATOM   2310 H HE3  A LYS   A 1 102 ? 24.239 3.578   -9.312  0.48 33.63 ?  102 LYS   A HE3  1 
ATOM   2311 H HE3  B LYS   A 1 102 ? 24.672 3.439   -10.405 0.52 36.57 ?  102 LYS   A HE3  1 
ATOM   2312 H HZ1  A LYS   A 1 102 ? 26.093 4.266   -8.185  0.48 34.28 ?  102 LYS   A HZ1  1 
ATOM   2313 H HZ1  B LYS   A 1 102 ? 25.214 3.082   -8.316  0.52 37.60 ?  102 LYS   A HZ1  1 
ATOM   2314 H HZ2  A LYS   A 1 102 ? 26.178 2.832   -8.376  0.48 34.28 ?  102 LYS   A HZ2  1 
ATOM   2315 H HZ2  B LYS   A 1 102 ? 25.033 1.721   -8.781  0.52 37.60 ?  102 LYS   A HZ2  1 
ATOM   2316 H HZ3  A LYS   A 1 102 ? 26.971 3.721   -9.200  0.48 34.28 ?  102 LYS   A HZ3  1 
ATOM   2317 H HZ3  B LYS   A 1 102 ? 26.367 2.261   -8.630  0.52 37.60 ?  102 LYS   A HZ3  1 
ATOM   2318 N N    A GLY   A 1 103 ? 22.460 -0.668  -15.024 0.48 24.30 ?  103 GLY   A N    1 
ATOM   2319 N N    B GLY   A 1 103 ? 22.994 -1.363  -15.679 0.52 20.44 ?  103 GLY   A N    1 
ATOM   2320 C CA   A GLY   A 1 103 ? 22.695 -1.752  -15.955 0.48 24.58 ?  103 GLY   A CA   1 
ATOM   2321 C CA   B GLY   A 1 103 ? 23.341 -2.510  -16.496 0.52 19.86 ?  103 GLY   A CA   1 
ATOM   2322 C C    A GLY   A 1 103 ? 23.536 -2.881  -15.410 0.48 25.12 ?  103 GLY   A C    1 
ATOM   2323 C C    B GLY   A 1 103 ? 24.113 -3.595  -15.774 0.52 19.15 ?  103 GLY   A C    1 
ATOM   2324 O O    A GLY   A 1 103 ? 24.062 -3.679  -16.192 0.48 26.08 ?  103 GLY   A O    1 
ATOM   2325 O O    B GLY   A 1 103 ? 24.705 -4.461  -16.428 0.52 19.92 ?  103 GLY   A O    1 
ATOM   2326 H H    A GLY   A 1 103 ? 21.709 -0.724  -14.609 0.48 29.13 ?  103 GLY   A H    1 
ATOM   2327 H H    B GLY   A 1 103 ? 22.176 -1.337  -15.419 0.52 24.50 ?  103 GLY   A H    1 
ATOM   2328 H HA2  A GLY   A 1 103 ? 21.840 -2.109  -16.252 0.48 29.48 ?  103 GLY   A HA2  1 
ATOM   2329 H HA2  B GLY   A 1 103 ? 22.523 -2.900  -16.838 0.52 23.80 ?  103 GLY   A HA2  1 
ATOM   2330 H HA3  A GLY   A 1 103 ? 23.158 -1.405  -16.731 0.48 29.48 ?  103 GLY   A HA3  1 
ATOM   2331 H HA3  B GLY   A 1 103 ? 23.862 -2.198  -17.259 0.52 23.80 ?  103 GLY   A HA3  1 
ATOM   2332 N N    A GLU   A 1 104 ? 23.687 -2.974  -14.093 0.48 24.27 ?  104 GLU   A N    1 
ATOM   2333 N N    B GLU   A 1 104 ? 24.117 -3.588  -14.445 0.52 17.30 ?  104 GLU   A N    1 
ATOM   2334 C CA   A GLU   A 1 104 ? 24.553 -3.978  -13.495 0.48 23.53 ?  104 GLU   A CA   1 
ATOM   2335 C CA   B GLU   A 1 104 ? 24.926 -4.534  -13.690 0.52 15.53 ?  104 GLU   A CA   1 
ATOM   2336 C C    A GLU   A 1 104 ? 23.856 -5.333  -13.407 0.48 23.69 ?  104 GLU   A C    1 
ATOM   2337 C C    B GLU   A 1 104 ? 24.191 -5.860  -13.518 0.52 15.76 ?  104 GLU   A C    1 
ATOM   2338 O O    A GLU   A 1 104 ? 22.629 -5.426  -13.313 0.48 23.84 ?  104 GLU   A O    1 
ATOM   2339 O O    B GLU   A 1 104 ? 22.968 -5.898  -13.344 0.52 16.70 ?  104 GLU   A O    1 
ATOM   2340 C CB   A GLU   A 1 104 ? 25.037 -3.499  -12.124 0.48 22.61 ?  104 GLU   A CB   1 
ATOM   2341 C CB   B GLU   A 1 104 ? 25.333 -3.927  -12.345 0.52 14.54 ?  104 GLU   A CB   1 
ATOM   2342 C CG   A GLU   A 1 104 ? 25.968 -2.289  -12.254 0.48 22.11 ?  104 GLU   A CG   1 
ATOM   2343 C CG   B GLU   A 1 104 ? 26.194 -2.675  -12.531 0.52 14.56 ?  104 GLU   A CG   1 
ATOM   2344 C CD   A GLU   A 1 104 ? 26.256 -1.557  -10.953 0.48 21.50 ?  104 GLU   A CD   1 
ATOM   2345 C CD   B GLU   A 1 104 ? 26.556 -1.929  -11.251 0.52 14.69 ?  104 GLU   A CD   1 
ATOM   2346 O OE1  A GLU   A 1 104 ? 25.688 -1.919  -9.903  0.48 20.69 ?  104 GLU   A OE1  1 
ATOM   2347 O OE1  B GLU   A 1 104 ? 26.011 -2.229  -10.172 0.52 14.77 ?  104 GLU   A OE1  1 
ATOM   2348 O OE2  A GLU   A 1 104 ? 27.051 -0.591  -10.996 0.48 21.84 -1 104 GLU   A OE2  1 
ATOM   2349 O OE2  B GLU   A 1 104 ? 27.396 -1.007  -11.341 0.52 15.41 -1 104 GLU   A OE2  1 
ATOM   2350 H H    A GLU   A 1 104 ? 23.306 -2.456  -13.525 0.48 29.10 ?  104 GLU   A H    1 
ATOM   2351 H H    B GLU   A 1 104 ? 23.657 -3.041  -13.966 0.52 20.74 ?  104 GLU   A H    1 
ATOM   2352 H HA   A GLU   A 1 104 ? 25.330 -4.089  -14.060 0.48 28.21 ?  104 GLU   A HA   1 
ATOM   2353 H HA   B GLU   A 1 104 ? 25.737 -4.706  -14.194 0.52 18.61 ?  104 GLU   A HA   1 
ATOM   2354 H HB2  A GLU   A 1 104 ? 24.270 -3.243  -11.588 0.48 27.11 ?  104 GLU   A HB2  1 
ATOM   2355 H HB2  B GLU   A 1 104 ? 24.540 -3.680  -11.852 0.52 17.42 ?  104 GLU   A HB2  1 
ATOM   2356 H HB3  A GLU   A 1 104 ? 25.523 -4.219  -11.691 0.48 27.11 ?  104 GLU   A HB3  1 
ATOM   2357 H HB3  B GLU   A 1 104 ? 25.853 -4.580  -11.852 0.52 17.42 ?  104 GLU   A HB3  1 
ATOM   2358 H HG2  A GLU   A 1 104 ? 26.810 -2.591  -12.626 0.48 26.51 ?  104 GLU   A HG2  1 
ATOM   2359 H HG2  B GLU   A 1 104 ? 27.019 -2.930  -12.971 0.52 17.44 ?  104 GLU   A HG2  1 
ATOM   2360 H HG3  A GLU   A 1 104 ? 25.555 -1.647  -12.849 0.48 26.51 ?  104 GLU   A HG3  1 
ATOM   2361 H HG3  B GLU   A 1 104 ? 25.707 -2.046  -13.085 0.52 17.44 ?  104 GLU   A HG3  1 
ATOM   2362 N N    A ASP   A 1 105 ? 24.668 -6.390  -13.442 0.48 24.09 ?  105 ASP   A N    1 
ATOM   2363 N N    B ASP   A 1 105 ? 24.956 -6.949  -13.582 0.52 16.40 ?  105 ASP   A N    1 
ATOM   2364 C CA   A ASP   A 1 105 ? 24.171 -7.755  -13.571 0.48 24.72 ?  105 ASP   A CA   1 
ATOM   2365 C CA   B ASP   A 1 105 ? 24.405 -8.299  -13.657 0.52 17.63 ?  105 ASP   A CA   1 
ATOM   2366 C C    A ASP   A 1 105 ? 23.488 -8.195  -12.279 0.48 23.23 ?  105 ASP   A C    1 
ATOM   2367 C C    B ASP   A 1 105 ? 23.693 -8.666  -12.357 0.52 16.15 ?  105 ASP   A C    1 
ATOM   2368 O O    A ASP   A 1 105 ? 24.118 -8.231  -11.217 0.48 22.46 ?  105 ASP   A O    1 
ATOM   2369 O O    B ASP   A 1 105 ? 24.306 -8.689  -11.286 0.52 14.34 ?  105 ASP   A O    1 
ATOM   2370 C CB   A ASP   A 1 105 ? 25.345 -8.677  -13.897 0.48 26.93 ?  105 ASP   A CB   1 
ATOM   2371 C CB   B ASP   A 1 105 ? 25.553 -9.267  -13.938 0.52 20.68 ?  105 ASP   A CB   1 
ATOM   2372 C CG   A ASP   A 1 105 ? 24.910 -10.095 -14.188 0.48 28.80 ?  105 ASP   A CG   1 
ATOM   2373 C CG   B ASP   A 1 105 ? 25.114 -10.716 -13.996 0.52 23.08 ?  105 ASP   A CG   1 
ATOM   2374 O OD1  A ASP   A 1 105 ? 23.689 -10.331 -14.304 0.48 29.31 ?  105 ASP   A OD1  1 
ATOM   2375 O OD1  B ASP   A 1 105 ? 23.896 -10.981 -14.061 0.52 23.35 ?  105 ASP   A OD1  1 
ATOM   2376 O OD2  A ASP   A 1 105 ? 25.793 -10.971 -14.305 0.48 29.85 -1 105 ASP   A OD2  1 
ATOM   2377 O OD2  B ASP   A 1 105 ? 26.005 -11.596 -13.969 0.52 24.79 -1 105 ASP   A OD2  1 
ATOM   2378 H H    A ASP   A 1 105 ? 25.524 -6.342  -13.390 0.48 28.89 ?  105 ASP   A H    1 
ATOM   2379 H H    B ASP   A 1 105 ? 25.815 -6.924  -13.596 0.52 19.65 ?  105 ASP   A H    1 
ATOM   2380 H HA   A ASP   A 1 105 ? 23.529 -7.812  -14.297 0.48 29.64 ?  105 ASP   A HA   1 
ATOM   2381 H HA   B ASP   A 1 105 ? 23.766 -8.348  -14.389 0.52 21.14 ?  105 ASP   A HA   1 
ATOM   2382 H HB2  A ASP   A 1 105 ? 25.803 -8.347  -14.689 0.48 32.29 ?  105 ASP   A HB2  1 
ATOM   2383 H HB2  B ASP   A 1 105 ? 25.966 -9.024  -14.787 0.52 24.79 ?  105 ASP   A HB2  1 
ATOM   2384 H HB3  A ASP   A 1 105 ? 25.961 -8.691  -13.145 0.48 32.29 ?  105 ASP   A HB3  1 
ATOM   2385 H HB3  B ASP   A 1 105 ? 26.202 -9.199  -13.226 0.52 24.79 ?  105 ASP   A HB3  1 
ATOM   2386 N N    A ILE   A 1 106 ? 22.200 -8.538  -12.373 0.48 22.58 ?  106 ILE   A N    1 
ATOM   2387 N N    B ILE   A 1 106 ? 22.395 -8.963  -12.450 0.52 17.09 ?  106 ILE   A N    1 
ATOM   2388 C CA   A ILE   A 1 106 ? 21.448 -8.973  -11.200 0.48 21.79 ?  106 ILE   A CA   1 
ATOM   2389 C CA   B ILE   A 1 106 ? 21.626 -9.313  -11.261 0.52 17.82 ?  106 ILE   A CA   1 
ATOM   2390 C C    A ILE   A 1 106 ? 22.000 -10.269 -10.625 0.48 21.06 ?  106 ILE   A C    1 
ATOM   2391 C C    B ILE   A 1 106 ? 22.146 -10.581 -10.601 0.52 17.70 ?  106 ILE   A C    1 
ATOM   2392 O O    A ILE   A 1 106 ? 21.804 -10.549 -9.438  0.48 20.27 ?  106 ILE   A O    1 
ATOM   2393 O O    B ILE   A 1 106 ? 21.911 -10.792 -9.406  0.52 17.31 ?  106 ILE   A O    1 
ATOM   2394 C CB   A ILE   A 1 106 ? 19.941 -9.079  -11.531 0.48 22.62 ?  106 ILE   A CB   1 
ATOM   2395 C CB   B ILE   A 1 106 ? 20.118 -9.395  -11.589 0.52 19.95 ?  106 ILE   A CB   1 
ATOM   2396 C CG1  A ILE   A 1 106 ? 19.107 -9.205  -10.252 0.48 22.96 ?  106 ILE   A CG1  1 
ATOM   2397 C CG1  B ILE   A 1 106 ? 19.282 -9.269  -10.313 0.52 21.36 ?  106 ILE   A CG1  1 
ATOM   2398 C CG2  A ILE   A 1 106 ? 19.671 -10.273 -12.422 0.48 23.01 ?  106 ILE   A CG2  1 
ATOM   2399 C CG2  B ILE   A 1 106 ? 19.788 -10.693 -12.299 0.52 20.49 ?  106 ILE   A CG2  1 
ATOM   2400 C CD1  A ILE   A 1 106 ? 19.201 -8.006  -9.339  0.48 23.14 ?  106 ILE   A CD1  1 
ATOM   2401 C CD1  B ILE   A 1 106 ? 19.512 -7.978  -9.557  0.52 22.13 ?  106 ILE   A CD1  1 
ATOM   2402 H H    A ILE   A 1 106 ? 21.745 -8.521  -13.099 0.48 27.07 ?  106 ILE   A H    1 
ATOM   2403 H H    B ILE   A 1 106 ? 21.945 -8.955  -13.177 0.52 20.49 ?  106 ILE   A H    1 
ATOM   2404 H HA   A ILE   A 1 106 ? 21.550 -8.298  -10.516 0.48 26.13 ?  106 ILE   A HA   1 
ATOM   2405 H HA   B ILE   A 1 106 ? 21.753 -8.605  -10.616 0.52 21.36 ?  106 ILE   A HA   1 
ATOM   2406 H HB   A ILE   A 1 106 ? 19.668 -8.274  -11.999 0.48 27.11 ?  106 ILE   A HB   1 
ATOM   2407 H HB   B ILE   A 1 106 ? 19.896 -8.657  -12.175 0.52 23.91 ?  106 ILE   A HB   1 
ATOM   2408 H HG12 A ILE   A 1 106 ? 18.175 -9.314  -10.498 0.48 27.53 ?  106 ILE   A HG12 1 
ATOM   2409 H HG12 B ILE   A 1 106 ? 18.343 -9.304  -10.550 0.52 25.61 ?  106 ILE   A HG12 1 
ATOM   2410 H HG13 A ILE   A 1 106 ? 19.407 -9.980  -9.755  0.48 27.53 ?  106 ILE   A HG13 1 
ATOM   2411 H HG13 B ILE   A 1 106 ? 19.501 -10.000 -9.718  0.52 25.61 ?  106 ILE   A HG13 1 
ATOM   2412 H HG21 A ILE   A 1 106 ? 18.779 -10.192 -12.792 0.48 27.58 ?  106 ILE   A HG21 1 
ATOM   2413 H HG21 B ILE   A 1 106 ? 18.908 -10.613 -12.697 0.52 24.57 ?  106 ILE   A HG21 1 
ATOM   2414 H HG22 A ILE   A 1 106 ? 20.327 -10.285 -13.133 0.48 27.58 ?  106 ILE   A HG22 1 
ATOM   2415 H HG22 B ILE   A 1 106 ? 20.452 -10.849 -12.986 0.52 24.57 ?  106 ILE   A HG22 1 
ATOM   2416 H HG23 A ILE   A 1 106 ? 19.738 -11.082 -11.892 0.48 27.58 ?  106 ILE   A HG23 1 
ATOM   2417 H HG23 B ILE   A 1 106 ? 19.797 -11.417 -11.655 0.52 24.57 ?  106 ILE   A HG23 1 
ATOM   2418 H HD11 A ILE   A 1 106 ? 18.480 -8.046  -8.693  0.48 27.74 ?  106 ILE   A HD11 1 
ATOM   2419 H HD11 B ILE   A 1 106 ? 18.734 -7.788  -9.014  0.52 26.53 ?  106 ILE   A HD11 1 
ATOM   2420 H HD12 A ILE   A 1 106 ? 20.056 -8.022  -8.882  0.48 27.74 ?  106 ILE   A HD12 1 
ATOM   2421 H HD12 B ILE   A 1 106 ? 20.295 -8.078  -8.991  0.52 26.53 ?  106 ILE   A HD12 1 
ATOM   2422 H HD13 A ILE   A 1 106 ? 19.124 -7.198  -9.871  0.48 27.74 ?  106 ILE   A HD13 1 
ATOM   2423 H HD13 B ILE   A 1 106 ? 19.654 -7.261  -10.194 0.52 26.53 ?  106 ILE   A HD13 1 
ATOM   2424 N N    A GLN   A 1 107 ? 22.705 -11.064 -11.436 0.48 21.89 ?  107 GLN   A N    1 
ATOM   2425 N N    B GLN   A 1 107 ? 22.868 -11.429 -11.346 0.52 18.47 ?  107 GLN   A N    1 
ATOM   2426 C CA   A GLN   A 1 107 ? 23.307 -12.298 -10.940 0.48 23.43 ?  107 GLN   A CA   1 
ATOM   2427 C CA   B GLN   A 1 107 ? 23.501 -12.595 -10.735 0.52 20.44 ?  107 GLN   A CA   1 
ATOM   2428 C C    A GLN   A 1 107 ? 24.306 -12.036 -9.819  0.48 21.10 ?  107 GLN   A C    1 
ATOM   2429 C C    B GLN   A 1 107 ? 24.436 -12.184 -9.604  0.52 18.05 ?  107 GLN   A C    1 
ATOM   2430 O O    A GLN   A 1 107 ? 24.576 -12.937 -9.018  0.48 22.49 ?  107 GLN   A O    1 
ATOM   2431 O O    B GLN   A 1 107 ? 24.662 -12.958 -8.664  0.52 18.42 ?  107 GLN   A O    1 
ATOM   2432 C CB   A GLN   A 1 107 ? 23.985 -13.050 -12.093 0.48 27.36 ?  107 GLN   A CB   1 
ATOM   2433 C CB   B GLN   A 1 107 ? 24.255 -13.398 -11.801 0.52 24.87 ?  107 GLN   A CB   1 
ATOM   2434 C CG   A GLN   A 1 107 ? 23.077 -13.305 -13.289 0.48 31.26 ?  107 GLN   A CG   1 
ATOM   2435 C CG   B GLN   A 1 107 ? 23.373 -13.877 -12.947 0.52 29.21 ?  107 GLN   A CG   1 
ATOM   2436 C CD   A GLN   A 1 107 ? 21.815 -14.055 -12.914 0.48 34.43 ?  107 GLN   A CD   1 
ATOM   2437 C CD   B GLN   A 1 107 ? 22.313 -14.861 -12.493 0.52 32.90 ?  107 GLN   A CD   1 
ATOM   2438 O OE1  A GLN   A 1 107 ? 21.865 -15.084 -12.241 0.48 35.70 ?  107 GLN   A OE1  1 
ATOM   2439 O OE1  B GLN   A 1 107 ? 22.572 -15.729 -11.659 0.52 34.13 ?  107 GLN   A OE1  1 
ATOM   2440 N NE2  A GLN   A 1 107 ? 20.671 -13.536 -13.342 0.48 35.46 ?  107 GLN   A NE2  1 
ATOM   2441 N NE2  B GLN   A 1 107 ? 21.108 -14.726 -13.037 0.52 34.03 ?  107 GLN   A NE2  1 
ATOM   2442 H H    A GLN   A 1 107 ? 22.853 -10.907 -12.267 0.48 26.24 ?  107 GLN   A H    1 
ATOM   2443 H H    B GLN   A 1 107 ? 23.008 -11.349 -12.193 0.52 22.14 ?  107 GLN   A H    1 
ATOM   2444 H HA   A GLN   A 1 107 ? 22.612 -12.871 -10.586 0.48 28.09 ?  107 GLN   A HA   1 
ATOM   2445 H HA   B GLN   A 1 107 ? 22.818 -13.170 -10.367 0.52 24.50 ?  107 GLN   A HA   1 
ATOM   2446 H HB2  A GLN   A 1 107 ? 24.741 -12.531 -12.408 0.48 32.81 ?  107 GLN   A HB2  1 
ATOM   2447 H HB2  B GLN   A 1 107 ? 24.956 -12.846 -12.182 0.52 29.82 ?  107 GLN   A HB2  1 
ATOM   2448 H HB3  A GLN   A 1 107 ? 24.290 -13.913 -11.772 0.48 32.81 ?  107 GLN   A HB3  1 
ATOM   2449 H HB3  B GLN   A 1 107 ? 24.647 -14.185 -11.389 0.52 29.82 ?  107 GLN   A HB3  1 
ATOM   2450 H HG2  A GLN   A 1 107 ? 22.815 -12.457 -13.679 0.48 37.49 ?  107 GLN   A HG2  1 
ATOM   2451 H HG2  B GLN   A 1 107 ? 22.924 -13.113 -13.344 0.52 35.03 ?  107 GLN   A HG2  1 
ATOM   2452 H HG3  A GLN   A 1 107 ? 23.559 -13.835 -13.946 0.48 37.49 ?  107 GLN   A HG3  1 
ATOM   2453 H HG3  B GLN   A 1 107 ? 23.926 -14.316 -13.613 0.52 35.03 ?  107 GLN   A HG3  1 
ATOM   2454 H HE21 A GLN   A 1 107 ? 20.674 -12.815 -13.809 0.48 42.52 ?  107 GLN   A HE21 1 
ATOM   2455 H HE21 B GLN   A 1 107 ? 20.962 -14.106 -13.616 0.52 40.82 ?  107 GLN   A HE21 1 
ATOM   2456 H HE22 A GLN   A 1 107 ? 19.928 -13.925 -13.155 0.48 42.52 ?  107 GLN   A HE22 1 
ATOM   2457 H HE22 B GLN   A 1 107 ? 20.473 -15.260 -12.811 0.52 40.82 ?  107 GLN   A HE22 1 
ATOM   2458 N N    A LEU   A 1 108 ? 24.850 -10.819 -9.736  0.48 17.58 ?  108 LEU   A N    1 
ATOM   2459 N N    B LEU   A 1 108 ? 24.971 -10.962 -9.664  0.52 15.79 ?  108 LEU   A N    1 
ATOM   2460 C CA   A LEU   A 1 108 ? 25.791 -10.468 -8.678  0.48 15.22 ?  108 LEU   A CA   1 
ATOM   2461 C CA   B LEU   A 1 108 ? 25.846 -10.465 -8.612  0.52 14.31 ?  108 LEU   A CA   1 
ATOM   2462 C C    A LEU   A 1 108 ? 25.110 -10.285 -7.327  0.48 13.20 ?  108 LEU   A C    1 
ATOM   2463 C C    B LEU   A 1 108 ? 25.112 -10.247 -7.296  0.52 12.72 ?  108 LEU   A C    1 
ATOM   2464 O O    A LEU   A 1 108 ? 25.807 -10.140 -6.317  0.48 13.31 ?  108 LEU   A O    1 
ATOM   2465 O O    B LEU   A 1 108 ? 25.773 -10.041 -6.272  0.52 12.98 ?  108 LEU   A O    1 
ATOM   2466 C CB   A LEU   A 1 108 ? 26.564 -9.203  -9.061  0.48 15.22 ?  108 LEU   A CB   1 
ATOM   2467 C CB   B LEU   A 1 108 ? 26.538 -9.175  -9.064  0.52 14.83 ?  108 LEU   A CB   1 
ATOM   2468 C CG   A LEU   A 1 108 ? 27.514 -9.381  -10.248 0.48 16.24 ?  108 LEU   A CG   1 
ATOM   2469 C CG   B LEU   A 1 108 ? 27.615 -9.373  -10.135 0.52 16.27 ?  108 LEU   A CG   1 
ATOM   2470 C CD1  A LEU   A 1 108 ? 28.018 -8.040  -10.764 0.48 16.70 ?  108 LEU   A CD1  1 
ATOM   2471 C CD1  B LEU   A 1 108 ? 28.047 -8.046  -10.737 0.52 16.78 ?  108 LEU   A CD1  1 
ATOM   2472 C CD2  A LEU   A 1 108 ? 28.688 -10.272 -9.865  0.48 17.03 ?  108 LEU   A CD2  1 
ATOM   2473 C CD2  B LEU   A 1 108 ? 28.817 -10.096 -9.549  0.52 17.17 ?  108 LEU   A CD2  1 
ATOM   2474 H H    A LEU   A 1 108 ? 24.685 -10.185 -10.285 0.48 21.07 ?  108 LEU   A H    1 
ATOM   2475 H H    B LEU   A 1 108 ? 24.838 -10.408 -10.304 0.52 18.93 ?  108 LEU   A H    1 
ATOM   2476 H HA   A LEU   A 1 108 ? 26.430 -11.190 -8.584  0.48 18.24 ?  108 LEU   A HA   1 
ATOM   2477 H HA   B LEU   A 1 108 ? 26.535 -11.128 -8.450  0.52 17.15 ?  108 LEU   A HA   1 
ATOM   2478 H HB2  A LEU   A 1 108 ? 25.927 -8.509  -9.296  0.48 18.24 ?  108 LEU   A HB2  1 
ATOM   2479 H HB2  B LEU   A 1 108 ? 25.869 -8.575  -9.429  0.52 17.77 ?  108 LEU   A HB2  1 
ATOM   2480 H HB3  A LEU   A 1 108 ? 27.091 -8.921  -8.300  0.48 18.24 ?  108 LEU   A HB3  1 
ATOM   2481 H HB3  B LEU   A 1 108 ? 26.961 -8.767  -8.296  0.52 17.77 ?  108 LEU   A HB3  1 
ATOM   2482 H HG   A LEU   A 1 108 ? 27.037 -9.815  -10.972 0.48 19.47 ?  108 LEU   A HG   1 
ATOM   2483 H HG   B LEU   A 1 108 ? 27.254 -9.922  -10.850 0.52 19.50 ?  108 LEU   A HG   1 
ATOM   2484 H HD11 A LEU   A 1 108 ? 28.611 -8.194  -11.518 0.48 20.01 ?  108 LEU   A HD11 1 
ATOM   2485 H HD11 B LEU   A 1 108 ? 28.691 -8.213  -11.444 0.52 20.11 ?  108 LEU   A HD11 1 
ATOM   2486 H HD12 A LEU   A 1 108 ? 27.260 -7.504  -11.045 0.48 20.01 ?  108 LEU   A HD12 1 
ATOM   2487 H HD12 B LEU   A 1 108 ? 27.269 -7.594  -11.098 0.52 20.11 ?  108 LEU   A HD12 1 
ATOM   2488 H HD13 A LEU   A 1 108 ? 28.499 -7.588  -10.053 0.48 20.01 ?  108 LEU   A HD13 1 
ATOM   2489 H HD13 B LEU   A 1 108 ? 28.453 -7.502  -10.043 0.52 20.11 ?  108 LEU   A HD13 1 
ATOM   2490 H HD21 A LEU   A 1 108 ? 29.341 -10.257 -10.581 0.48 20.41 ?  108 LEU   A HD21 1 
ATOM   2491 H HD21 B LEU   A 1 108 ? 29.543 -10.069 -10.191 0.52 20.57 ?  108 LEU   A HD21 1 
ATOM   2492 H HD22 A LEU   A 1 108 ? 29.086 -9.931  -9.047  0.48 20.41 ?  108 LEU   A HD22 1 
ATOM   2493 H HD22 B LEU   A 1 108 ? 29.082 -9.652  -8.730  0.52 20.57 ?  108 LEU   A HD22 1 
ATOM   2494 H HD23 A LEU   A 1 108 ? 28.367 -11.175 -9.725  0.48 20.41 ?  108 LEU   A HD23 1 
ATOM   2495 H HD23 B LEU   A 1 108 ? 28.573 -11.016 -9.364  0.52 20.57 ?  108 LEU   A HD23 1 
ATOM   2496 N N    . LEU   A 1 109 ? 23.776 -10.313 -7.283  1.00 12.39 ?  109 LEU   A N    1 
ATOM   2497 C CA   . LEU   A 1 109 ? 23.066 -10.176 -6.017  1.00 11.73 ?  109 LEU   A CA   1 
ATOM   2498 C C    . LEU   A 1 109 ? 23.393 -11.332 -5.076  1.00 11.30 ?  109 LEU   A C    1 
ATOM   2499 O O    . LEU   A 1 109 ? 23.514 -11.139 -3.863  1.00 11.45 ?  109 LEU   A O    1 
ATOM   2500 C CB   . LEU   A 1 109 ? 21.563 -10.076 -6.277  1.00 12.60 ?  109 LEU   A CB   1 
ATOM   2501 C CG   . LEU   A 1 109 ? 20.668 -9.807  -5.071  1.00 13.06 ?  109 LEU   A CG   1 
ATOM   2502 C CD1  . LEU   A 1 109 ? 21.123 -8.554  -4.346  1.00 13.35 ?  109 LEU   A CD1  1 
ATOM   2503 C CD2  . LEU   A 1 109 ? 19.210 -9.671  -5.505  1.00 14.11 ?  109 LEU   A CD2  1 
ATOM   2504 H H    A LEU   A 1 109 ? 23.263 -10.416 -7.969  0.48 14.85 ?  109 LEU   A H    1 
ATOM   2505 H H    B LEU   A 1 109 ? 23.274 -10.439 -7.973  0.52 14.85 ?  109 LEU   A H    1 
ATOM   2506 H HA   . LEU   A 1 109 ? 23.354 -9.351  -5.596  1.00 14.06 ?  109 LEU   A HA   1 
ATOM   2507 H HB2  . LEU   A 1 109 ? 21.410 -9.358  -6.911  1.00 15.09 ?  109 LEU   A HB2  1 
ATOM   2508 H HB3  . LEU   A 1 109 ? 21.267 -10.914 -6.666  1.00 15.09 ?  109 LEU   A HB3  1 
ATOM   2509 H HG   . LEU   A 1 109 ? 20.731 -10.548 -4.452  1.00 15.64 ?  109 LEU   A HG   1 
ATOM   2510 H HD11 . LEU   A 1 109 ? 20.437 -8.280  -3.721  1.00 15.99 ?  109 LEU   A HD11 1 
ATOM   2511 H HD12 . LEU   A 1 109 ? 21.949 -8.738  -3.877  1.00 15.99 ?  109 LEU   A HD12 1 
ATOM   2512 H HD13 . LEU   A 1 109 ? 21.268 -7.846  -5.002  1.00 15.99 ?  109 LEU   A HD13 1 
ATOM   2513 H HD21 . LEU   A 1 109 ? 18.674 -9.395  -4.741  1.00 16.91 ?  109 LEU   A HD21 1 
ATOM   2514 H HD22 . LEU   A 1 109 ? 19.144 -9.006  -6.207  1.00 16.91 ?  109 LEU   A HD22 1 
ATOM   2515 H HD23 . LEU   A 1 109 ? 18.894 -10.529 -5.832  1.00 16.91 ?  109 LEU   A HD23 1 
ATOM   2516 N N    . LYS   A 1 110 ? 23.548 -12.544 -5.611  1.00 11.20 ?  110 LYS   A N    1 
ATOM   2517 C CA   . LYS   A 1 110 ? 23.912 -13.664 -4.749  1.00 11.26 ?  110 LYS   A CA   1 
ATOM   2518 C C    . LYS   A 1 110 ? 25.289 -13.443 -4.133  1.00 10.72 ?  110 LYS   A C    1 
ATOM   2519 O O    . LYS   A 1 110 ? 25.474 -13.647 -2.931  1.00 10.87 ?  110 LYS   A O    1 
ATOM   2520 C CB   . LYS   A 1 110 ? 23.846 -14.991 -5.511  1.00 12.41 ?  110 LYS   A CB   1 
ATOM   2521 C CG   . LYS   A 1 110 ? 24.030 -16.201 -4.603  1.00 12.42 ?  110 LYS   A CG   1 
ATOM   2522 C CD   . LYS   A 1 110 ? 23.793 -17.520 -5.321  1.00 13.01 ?  110 LYS   A CD   1 
ATOM   2523 C CE   . LYS   A 1 110 ? 23.887 -18.709 -4.373  1.00 13.80 ?  110 LYS   A CE   1 
ATOM   2524 N NZ   . LYS   A 1 110 ? 22.693 -18.821 -3.503  1.00 13.97 ?  110 LYS   A NZ   1 
ATOM   2525 H H    . LYS   A 1 110 ? 23.462 -12.737 -6.442  1.00 13.41 ?  110 LYS   A H    1 
ATOM   2526 H HA   . LYS   A 1 110 ? 23.263 -13.709 -4.022  1.00 13.49 ?  110 LYS   A HA   1 
ATOM   2527 H HB2  . LYS   A 1 110 ? 22.982 -15.066 -5.938  1.00 14.87 ?  110 LYS   A HB2  1 
ATOM   2528 H HB3  . LYS   A 1 110 ? 24.552 -15.003 -6.173  1.00 14.87 ?  110 LYS   A HB3  1 
ATOM   2529 H HG2  . LYS   A 1 110 ? 24.938 -16.197 -4.258  1.00 14.88 ?  110 LYS   A HG2  1 
ATOM   2530 H HG3  . LYS   A 1 110 ? 23.400 -16.136 -3.867  1.00 14.88 ?  110 LYS   A HG3  1 
ATOM   2531 H HD2  . LYS   A 1 110 ? 22.910 -17.509 -5.710  1.00 15.59 ?  110 LYS   A HD2  1 
ATOM   2532 H HD3  . LYS   A 1 110 ? 24.468 -17.622 -6.010  1.00 15.59 ?  110 LYS   A HD3  1 
ATOM   2533 H HE2  . LYS   A 1 110 ? 23.969 -19.522 -4.891  1.00 16.54 ?  110 LYS   A HE2  1 
ATOM   2534 H HE3  . LYS   A 1 110 ? 24.670 -18.600 -3.800  1.00 16.54 ?  110 LYS   A HE3  1 
ATOM   2535 H HZ1  . LYS   A 1 110 ? 22.770 -19.521 -2.963  1.00 16.74 ?  110 LYS   A HZ1  1 
ATOM   2536 H HZ2  . LYS   A 1 110 ? 22.600 -18.083 -3.012  1.00 16.74 ?  110 LYS   A HZ2  1 
ATOM   2537 H HZ3  . LYS   A 1 110 ? 21.962 -18.922 -4.006  1.00 16.74 ?  110 LYS   A HZ3  1 
ATOM   2538 N N    . SER   A 1 111 ? 26.255 -12.996 -4.939  1.00 10.65 ?  111 SER   A N    1 
ATOM   2539 C CA   . SER   A 1 111 ? 27.580 -12.687 -4.411  1.00 10.98 ?  111 SER   A CA   1 
ATOM   2540 C C    . SER   A 1 111 ? 27.502 -11.642 -3.304  1.00 10.40 ?  111 SER   A C    1 
ATOM   2541 O O    . SER   A 1 111 ? 28.200 -11.744 -2.287  1.00 10.96 ?  111 SER   A O    1 
ATOM   2542 C CB   . SER   A 1 111 ? 28.477 -12.199 -5.547  1.00 12.25 ?  111 SER   A CB   1 
ATOM   2543 O OG   . SER   A 1 111 ? 28.551 -13.172 -6.579  1.00 14.10 ?  111 SER   A OG   1 
ATOM   2544 H H    . SER   A 1 111 ? 26.156 -12.871 -5.781  1.00 12.75 ?  111 SER   A H    1 
ATOM   2545 H HA   . SER   A 1 111 ? 27.966 -13.499 -4.044  1.00 13.15 ?  111 SER   A HA   1 
ATOM   2546 H HB2  . SER   A 1 111 ? 28.100 -11.388 -5.920  1.00 14.67 ?  111 SER   A HB2  1 
ATOM   2547 H HB3  . SER   A 1 111 ? 29.361 -12.028 -5.195  1.00 14.67 ?  111 SER   A HB3  1 
ATOM   2548 H HG   . SER   A 1 111 ? 29.067 -12.898 -7.194  1.00 16.90 ?  111 SER   A HG   1 
ATOM   2549 N N    . ALA   A 1 112 ? 26.658 -10.620 -3.493  1.00 10.37 ?  112 ALA   A N    1 
ATOM   2550 C CA   . ALA   A 1 112 ? 26.498 -9.586  -2.475  1.00 10.26 ?  112 ALA   A CA   1 
ATOM   2551 C C    . ALA   A 1 112 ? 26.017 -10.192 -1.159  1.00 10.00 ?  112 ALA   A C    1 
ATOM   2552 O O    . ALA   A 1 112 ? 26.561 -9.901  -0.090  1.00 10.34 ?  112 ALA   A O    1 
ATOM   2553 C CB   . ALA   A 1 112 ? 25.526 -8.510  -2.970  1.00 11.03 ?  112 ALA   A CB   1 
ATOM   2554 H H    . ALA   A 1 112 ? 26.175 -10.506 -4.196  1.00 12.42 ?  112 ALA   A H    1 
ATOM   2555 H HA   . ALA   A 1 112 ? 27.355 -9.162  -2.316  1.00 12.29 ?  112 ALA   A HA   1 
ATOM   2556 H HB1  . ALA   A 1 112 ? 25.445 -7.818  -2.290  1.00 13.21 ?  112 ALA   A HB1  1 
ATOM   2557 H HB2  . ALA   A 1 112 ? 25.870 -8.122  -3.790  1.00 13.21 ?  112 ALA   A HB2  1 
ATOM   2558 H HB3  . ALA   A 1 112 ? 24.658 -8.912  -3.132  1.00 13.21 ?  112 ALA   A HB3  1 
ATOM   2559 N N    . TYR   A 1 113 ? 24.972 -11.026 -1.214  1.00 9.94  ?  113 TYR   A N    1 
ATOM   2560 C CA   . TYR   A 1 113 ? 24.456 -11.633 0.010   1.00 9.89  ?  113 TYR   A CA   1 
ATOM   2561 C C    . TYR   A 1 113 ? 25.457 -12.593 0.654   1.00 9.67  ?  113 TYR   A C    1 
ATOM   2562 O O    . TYR   A 1 113 ? 25.416 -12.786 1.873   1.00 10.11 ?  113 TYR   A O    1 
ATOM   2563 C CB   . TYR   A 1 113 ? 23.128 -12.348 -0.258  1.00 10.20 ?  113 TYR   A CB   1 
ATOM   2564 C CG   . TYR   A 1 113 ? 21.924 -11.435 -0.223  1.00 10.16 ?  113 TYR   A CG   1 
ATOM   2565 C CD1  . TYR   A 1 113 ? 21.555 -10.793 0.953   1.00 10.78 ?  113 TYR   A CD1  1 
ATOM   2566 C CD2  . TYR   A 1 113 ? 21.132 -11.243 -1.349  1.00 10.71 ?  113 TYR   A CD2  1 
ATOM   2567 C CE1  . TYR   A 1 113 ? 20.433 -9.983  1.004   1.00 11.42 ?  113 TYR   A CE1  1 
ATOM   2568 C CE2  . TYR   A 1 113 ? 19.989 -10.434 -1.304  1.00 11.27 ?  113 TYR   A CE2  1 
ATOM   2569 C CZ   . TYR   A 1 113 ? 19.656 -9.808  -0.125  1.00 11.37 ?  113 TYR   A CZ   1 
ATOM   2570 O OH   . TYR   A 1 113 ? 18.540 -8.997  -0.056  1.00 12.50 ?  113 TYR   A OH   1 
ATOM   2571 H H    . TYR   A 1 113 ? 24.561 -11.251 -1.935  1.00 11.91 ?  113 TYR   A H    1 
ATOM   2572 H HA   . TYR   A 1 113 ? 24.285 -10.933 0.649   1.00 11.85 ?  113 TYR   A HA   1 
ATOM   2573 H HB2  . TYR   A 1 113 ? 23.162 -12.756 -1.138  1.00 12.22 ?  113 TYR   A HB2  1 
ATOM   2574 H HB3  . TYR   A 1 113 ? 23.002 -13.035 0.416   1.00 12.22 ?  113 TYR   A HB3  1 
ATOM   2575 H HD1  . TYR   A 1 113 ? 22.071 -10.923 1.721   1.00 12.91 ?  113 TYR   A HD1  1 
ATOM   2576 H HD2  . TYR   A 1 113 ? 21.353 -11.676 -2.141  1.00 12.82 ?  113 TYR   A HD2  1 
ATOM   2577 H HE1  . TYR   A 1 113 ? 20.207 -9.567  1.801   1.00 13.68 ?  113 TYR   A HE1  1 
ATOM   2578 H HE2  . TYR   A 1 113 ? 19.468 -10.307 -2.065  1.00 13.50 ?  113 TYR   A HE2  1 
ATOM   2579 H HH   . TYR   A 1 113 ? 18.160 -8.973  -0.810  1.00 14.98 ?  113 TYR   A HH   1 
ATOM   2580 N N    . GLU   A 1 114 ? 26.361 -13.206 -0.127  1.00 9.93  ?  114 GLU   A N    1 
ATOM   2581 C CA   . GLU   A 1 114 ? 27.347 -14.103 0.474   1.00 10.42 ?  114 GLU   A CA   1 
ATOM   2582 C C    . GLU   A 1 114 ? 28.193 -13.394 1.528   1.00 10.25 ?  114 GLU   A C    1 
ATOM   2583 O O    . GLU   A 1 114 ? 28.671 -14.034 2.473   1.00 10.45 ?  114 GLU   A O    1 
ATOM   2584 C CB   . GLU   A 1 114 ? 28.218 -14.740 -0.612  1.00 10.74 ?  114 GLU   A CB   1 
ATOM   2585 C CG   . GLU   A 1 114 ? 27.462 -15.786 -1.409  1.00 11.01 ?  114 GLU   A CG   1 
ATOM   2586 C CD   . GLU   A 1 114 ? 28.182 -16.317 -2.642  1.00 11.34 ?  114 GLU   A CD   1 
ATOM   2587 O OE1  . GLU   A 1 114 ? 29.144 -15.691 -3.140  1.00 11.74 ?  114 GLU   A OE1  1 
ATOM   2588 O OE2  . GLU   A 1 114 ? 27.749 -17.385 -3.134  1.00 12.61 -1 114 GLU   A OE2  1 
ATOM   2589 H H    . GLU   A 1 114 ? 26.419 -13.111 -0.984  1.00 11.89 ?  114 GLU   A H    1 
ATOM   2590 H HA   . GLU   A 1 114 ? 26.870 -14.819 0.915   1.00 12.48 ?  114 GLU   A HA   1 
ATOM   2591 H HB2  . GLU   A 1 114 ? 28.519 -14.054 -1.232  1.00 12.86 ?  114 GLU   A HB2  1 
ATOM   2592 H HB3  . GLU   A 1 114 ? 28.979 -15.174 -0.200  1.00 12.86 ?  114 GLU   A HB3  1 
ATOM   2593 H HG2  . GLU   A 1 114 ? 27.282 -16.544 -0.835  1.00 13.19 ?  114 GLU   A HG2  1 
ATOM   2594 H HG3  . GLU   A 1 114 ? 26.621 -15.400 -1.709  1.00 13.19 ?  114 GLU   A HG3  1 
ATOM   2595 N N    . ASN   A 1 115 ? 28.382 -12.076 1.395   1.00 10.13 ?  115 ASN   A N    1 
ATOM   2596 C CA   . ASN   A 1 115 ? 29.147 -11.348 2.401   1.00 10.19 ?  115 ASN   A CA   1 
ATOM   2597 C C    . ASN   A 1 115 ? 28.523 -11.476 3.786   1.00 10.03 ?  115 ASN   A C    1 
ATOM   2598 O O    . ASN   A 1 115 ? 29.234 -11.399 4.795   1.00 10.46 ?  115 ASN   A O    1 
ATOM   2599 C CB   . ASN   A 1 115 ? 29.263 -9.872  2.023   1.00 10.69 ?  115 ASN   A CB   1 
ATOM   2600 C CG   . ASN   A 1 115 ? 30.064 -9.660  0.765   1.00 11.37 ?  115 ASN   A CG   1 
ATOM   2601 O OD1  . ASN   A 1 115 ? 31.279 -9.773  0.781   1.00 14.60 ?  115 ASN   A OD1  1 
ATOM   2602 N ND2  . ASN   A 1 115 ? 29.392 -9.347  -0.327  1.00 10.91 ?  115 ASN   A ND2  1 
ATOM   2603 H H    . ASN   A 1 115 ? 28.072 -11.591 0.752   1.00 12.13 ?  115 ASN   A H    1 
ATOM   2604 H HA   . ASN   A 1 115 ? 30.036 -11.721 2.443   1.00 12.20 ?  115 ASN   A HA   1 
ATOM   2605 H HB2  . ASN   A 1 115 ? 28.373 -9.513  1.887   1.00 12.81 ?  115 ASN   A HB2  1 
ATOM   2606 H HB3  . ASN   A 1 115 ? 29.703 -9.402  2.750   1.00 12.81 ?  115 ASN   A HB3  1 
ATOM   2607 H HD21 . ASN   A 1 115 ? 29.809 -9.213  -1.066  1.00 13.07 ?  115 ASN   A HD21 1 
ATOM   2608 H HD22 . ASN   A 1 115 ? 28.534 -9.287  -0.301  1.00 13.07 ?  115 ASN   A HD22 1 
ATOM   2609 N N    . PHE   A 1 116 ? 27.195 -11.641 3.861   1.00 10.06 ?  116 PHE   A N    1 
ATOM   2610 C CA   . PHE   A 1 116 ? 26.538 -11.731 5.164   1.00 10.11 ?  116 PHE   A CA   1 
ATOM   2611 C C    . PHE   A 1 116 ? 27.004 -12.964 5.940   1.00 10.52 ?  116 PHE   A C    1 
ATOM   2612 O O    . PHE   A 1 116 ? 26.930 -12.981 7.170   1.00 10.87 ?  116 PHE   A O    1 
ATOM   2613 C CB   . PHE   A 1 116 ? 25.009 -11.861 5.023   1.00 10.44 ?  116 PHE   A CB   1 
ATOM   2614 C CG   . PHE   A 1 116 ? 24.252 -10.618 4.530   1.00 9.85  ?  116 PHE   A CG   1 
ATOM   2615 C CD1  . PHE   A 1 116 ? 24.826 -9.618  3.756   1.00 10.28 ?  116 PHE   A CD1  1 
ATOM   2616 C CD2  . PHE   A 1 116 ? 22.900 -10.507 4.848   1.00 10.82 ?  116 PHE   A CD2  1 
ATOM   2617 C CE1  . PHE   A 1 116 ? 24.062 -8.547  3.317   1.00 10.57 ?  116 PHE   A CE1  1 
ATOM   2618 C CE2  . PHE   A 1 116 ? 22.137 -9.436  4.415   1.00 10.62 ?  116 PHE   A CE2  1 
ATOM   2619 C CZ   . PHE   A 1 116 ? 22.714 -8.459  3.647   1.00 10.26 ?  116 PHE   A CZ   1 
ATOM   2620 H H    . PHE   A 1 116 ? 26.662 -11.701 3.186   1.00 12.05 ?  116 PHE   A H    1 
ATOM   2621 H HA   . PHE   A 1 116 ? 26.734 -10.939 5.686   1.00 12.10 ?  116 PHE   A HA   1 
ATOM   2622 H HB2  . PHE   A 1 116 ? 24.826 -12.584 4.400   1.00 12.51 ?  116 PHE   A HB2  1 
ATOM   2623 H HB3  . PHE   A 1 116 ? 24.648 -12.100 5.895   1.00 12.51 ?  116 PHE   A HB3  1 
ATOM   2624 H HD1  . PHE   A 1 116 ? 25.721 -9.689  3.524   1.00 12.32 ?  116 PHE   A HD1  1 
ATOM   2625 H HD2  . PHE   A 1 116 ? 22.493 -11.177 5.361   1.00 12.96 ?  116 PHE   A HD2  1 
ATOM   2626 H HE1  . PHE   A 1 116 ? 24.459 -7.888  2.803   1.00 12.65 ?  116 PHE   A HE1  1 
ATOM   2627 H HE2  . PHE   A 1 116 ? 21.235 -9.386  4.645   1.00 12.72 ?  116 PHE   A HE2  1 
ATOM   2628 H HZ   . PHE   A 1 116 ? 22.212 -7.735  3.363   1.00 12.28 ?  116 PHE   A HZ   1 
ATOM   2629 N N    . ASN   A 1 117 ? 27.446 -14.016 5.243   1.00 10.57 ?  117 ASN   A N    1 
ATOM   2630 C CA   . ASN   A 1 117 ? 27.817 -15.259 5.915   1.00 10.80 ?  117 ASN   A CA   1 
ATOM   2631 C C    . ASN   A 1 117 ? 29.075 -15.138 6.757   1.00 11.24 ?  117 ASN   A C    1 
ATOM   2632 O O    . ASN   A 1 117 ? 29.368 -16.052 7.537   1.00 12.01 ?  117 ASN   A O    1 
ATOM   2633 C CB   . ASN   A 1 117 ? 27.946 -16.379 4.892   1.00 10.91 ?  117 ASN   A CB   1 
ATOM   2634 C CG   . ASN   A 1 117 ? 26.597 -16.773 4.351   1.00 11.09 ?  117 ASN   A CG   1 
ATOM   2635 O OD1  . ASN   A 1 117 ? 25.615 -16.794 5.093   1.00 11.88 ?  117 ASN   A OD1  1 
ATOM   2636 N ND2  . ASN   A 1 117 ? 26.520 -17.029 3.061   1.00 10.95 ?  117 ASN   A ND2  1 
ATOM   2637 H H    . ASN   A 1 117 ? 27.524 -14.035 4.386   1.00 12.66 ?  117 ASN   A H    1 
ATOM   2638 H HA   . ASN   A 1 117 ? 27.094 -15.497 6.516   1.00 12.93 ?  117 ASN   A HA   1 
ATOM   2639 H HB2  . ASN   A 1 117 ? 28.494 -16.071 4.151   1.00 13.06 ?  117 ASN   A HB2  1 
ATOM   2640 H HB3  . ASN   A 1 117 ? 28.345 -17.149 5.313   1.00 13.06 ?  117 ASN   A HB3  1 
ATOM   2641 H HD21 . ASN   A 1 117 ? 25.767 -17.247 2.717   1.00 13.11 ?  117 ASN   A HD21 1 
ATOM   2642 H HD22 . ASN   A 1 117 ? 27.225 -16.979 2.575   1.00 13.11 ?  117 ASN   A HD22 1 
ATOM   2643 N N    . GLN   A 1 118 ? 29.803 -14.030 6.642   1.00 11.25 ?  118 GLN   A N    1 
ATOM   2644 C CA   . GLN   A 1 118 ? 30.976 -13.792 7.472   1.00 12.03 ?  118 GLN   A CA   1 
ATOM   2645 C C    . GLN   A 1 118 ? 30.623 -13.212 8.835   1.00 11.96 ?  118 GLN   A C    1 
ATOM   2646 O O    . GLN   A 1 118 ? 31.532 -12.917 9.617   1.00 13.07 ?  118 GLN   A O    1 
ATOM   2647 C CB   . GLN   A 1 118 ? 31.978 -12.887 6.739   1.00 12.31 ?  118 GLN   A CB   1 
ATOM   2648 C CG   . GLN   A 1 118 ? 32.441 -13.473 5.408   1.00 12.16 ?  118 GLN   A CG   1 
ATOM   2649 C CD   . GLN   A 1 118 ? 33.282 -14.723 5.584   1.00 12.44 ?  118 GLN   A CD   1 
ATOM   2650 O OE1  . GLN   A 1 118 ? 34.142 -14.783 6.475   1.00 13.31 ?  118 GLN   A OE1  1 
ATOM   2651 N NE2  . GLN   A 1 118 ? 33.042 -15.729 4.735   1.00 12.43 ?  118 GLN   A NE2  1 
ATOM   2652 H H    . GLN   A 1 118 ? 29.631 -13.383 6.089   1.00 13.48 ?  118 GLN   A H    1 
ATOM   2653 H HA   . GLN   A 1 118 ? 31.405 -14.643 7.629   1.00 14.41 ?  118 GLN   A HA   1 
ATOM   2654 H HB2  . GLN   A 1 118 ? 31.565 -12.032 6.570   1.00 14.75 ?  118 GLN   A HB2  1 
ATOM   2655 H HB3  . GLN   A 1 118 ? 32.761 -12.775 7.306   1.00 14.75 ?  118 GLN   A HB3  1 
ATOM   2656 H HG2  . GLN   A 1 118 ? 31.663 -13.702 4.872   1.00 14.57 ?  118 GLN   A HG2  1 
ATOM   2657 H HG3  . GLN   A 1 118 ? 32.978 -12.813 4.943   1.00 14.57 ?  118 GLN   A HG3  1 
ATOM   2658 H HE21 . GLN   A 1 118 ? 32.427 -15.648 4.129   1.00 14.89 ?  118 GLN   A HE21 1 
ATOM   2659 H HE22 . GLN   A 1 118 ? 33.485 -16.462 4.789   1.00 14.89 ?  118 GLN   A HE22 1 
ATOM   2660 N N    . HIS   A 1 119 ? 29.333 -13.055 9.138   1.00 11.70 ?  119 HIS   A N    1 
ATOM   2661 C CA   . HIS   A 1 119 ? 28.873 -12.446 10.381  1.00 11.73 ?  119 HIS   A CA   1 
ATOM   2662 C C    . HIS   A 1 119 ? 27.732 -13.271 10.951  1.00 12.17 ?  119 HIS   A C    1 
ATOM   2663 O O    . HIS   A 1 119 ? 26.789 -13.609 10.231  1.00 12.51 ?  119 HIS   A O    1 
ATOM   2664 C CB   . HIS   A 1 119 ? 28.414 -11.012 10.113  1.00 12.25 ?  119 HIS   A CB   1 
ATOM   2665 C CG   . HIS   A 1 119 ? 29.493 -10.202 9.498   1.00 13.59 ?  119 HIS   A CG   1 
ATOM   2666 N ND1  . HIS   A 1 119 ? 30.457 -9.584  10.257  1.00 16.03 ?  119 HIS   A ND1  1 
ATOM   2667 C CD2  . HIS   A 1 119 ? 29.841 -10.014 8.206   1.00 14.77 ?  119 HIS   A CD2  1 
ATOM   2668 C CE1  . HIS   A 1 119 ? 31.330 -9.002  9.454   1.00 16.39 ?  119 HIS   A CE1  1 
ATOM   2669 N NE2  . HIS   A 1 119 ? 30.986 -9.257  8.204   1.00 16.19 ?  119 HIS   A NE2  1 
ATOM   2670 H H    . HIS   A 1 119 ? 28.681 -13.318 8.632   1.00 14.02 ?  119 HIS   A H    1 
ATOM   2671 H HA   . HIS   A 1 119 ? 29.593 -12.434 11.027  1.00 14.06 ?  119 HIS   A HA   1 
ATOM   2672 H HB2  . HIS   A 1 119 ? 27.658 -11.029 9.508   1.00 14.67 ?  119 HIS   A HB2  1 
ATOM   2673 H HB3  . HIS   A 1 119 ? 28.164 -10.600 10.955  1.00 14.67 ?  119 HIS   A HB3  1 
ATOM   2674 H HD2  . HIS   A 1 119 ? 29.391 -10.339 7.457   1.00 17.70 ?  119 HIS   A HD2  1 
ATOM   2675 H HE1  . HIS   A 1 119 ? 32.065 -8.494  9.717   1.00 19.65 ?  119 HIS   A HE1  1 
ATOM   2676 H HE2  . HIS   A 1 119 ? 31.396 -8.971  7.500   1.00 19.40 ?  119 HIS   A HE2  1 
ATOM   2677 N N    . GLU   A 1 120 ? 27.813 -13.579 12.246  1.00 12.81 ?  120 GLU   A N    1 
ATOM   2678 C CA   . GLU   A 1 120 ? 26.855 -14.511 12.841  1.00 14.88 ?  120 GLU   A CA   1 
ATOM   2679 C C    . GLU   A 1 120 ? 25.441 -13.947 12.899  1.00 13.50 ?  120 GLU   A C    1 
ATOM   2680 O O    . GLU   A 1 120 ? 24.471 -14.713 12.789  1.00 13.64 ?  120 GLU   A O    1 
ATOM   2681 C CB   . GLU   A 1 120 ? 27.320 -14.918 14.240  1.00 19.26 ?  120 GLU   A CB   1 
ATOM   2682 C CG   . GLU   A 1 120 ? 28.529 -15.834 14.251  1.00 25.45 ?  120 GLU   A CG   1 
ATOM   2683 C CD   . GLU   A 1 120 ? 28.652 -16.614 15.542  1.00 31.39 ?  120 GLU   A CD   1 
ATOM   2684 O OE1  . GLU   A 1 120 ? 28.385 -16.034 16.617  1.00 33.40 ?  120 GLU   A OE1  1 
ATOM   2685 O OE2  . GLU   A 1 120 ? 29.006 -17.811 15.479  1.00 33.69 -1 120 GLU   A OE2  1 
ATOM   2686 H H    . GLU   A 1 120 ? 28.411 -13.281 12.791  1.00 15.34 ?  120 GLU   A H    1 
ATOM   2687 H HA   . GLU   A 1 120 ? 26.831 -15.316 12.306  1.00 17.83 ?  120 GLU   A HA   1 
ATOM   2688 H HB2  . GLU   A 1 120 ? 27.555 -14.126 14.746  1.00 23.09 ?  120 GLU   A HB2  1 
ATOM   2689 H HB3  . GLU   A 1 120 ? 26.599 -15.390 14.691  1.00 23.09 ?  120 GLU   A HB3  1 
ATOM   2690 H HG2  . GLU   A 1 120 ? 28.460 -16.472 13.527  1.00 30.51 ?  120 GLU   A HG2  1 
ATOM   2691 H HG3  . GLU   A 1 120 ? 29.337 -15.305 14.157  1.00 30.51 ?  120 GLU   A HG3  1 
ATOM   2692 N N    . VAL   A 1 121 ? 25.303 -12.634 13.101  1.00 12.88 ?  121 VAL   A N    1 
ATOM   2693 C CA   . VAL   A 1 121 ? 24.007 -11.975 13.222  1.00 12.98 ?  121 VAL   A CA   1 
ATOM   2694 C C    . VAL   A 1 121 ? 24.112 -10.597 12.583  1.00 11.68 ?  121 VAL   A C    1 
ATOM   2695 O O    . VAL   A 1 121 ? 25.068 -9.859  12.842  1.00 12.52 ?  121 VAL   A O    1 
ATOM   2696 C CB   . VAL   A 1 121 ? 23.567 -11.829 14.698  1.00 16.24 ?  121 VAL   A CB   1 
ATOM   2697 C CG1  . VAL   A 1 121 ? 22.161 -11.242 14.781  1.00 16.74 ?  121 VAL   A CG1  1 
ATOM   2698 C CG2  . VAL   A 1 121 ? 23.631 -13.149 15.445  1.00 18.56 ?  121 VAL   A CG2  1 
ATOM   2699 H H    . VAL   A 1 121 ? 25.968 -12.090 13.171  1.00 15.43 ?  121 VAL   A H    1 
ATOM   2700 H HA   . VAL   A 1 121 ? 23.337 -12.490 12.750  1.00 15.55 ?  121 VAL   A HA   1 
ATOM   2701 H HB   . VAL   A 1 121 ? 24.170 -11.211 15.141  1.00 19.46 ?  121 VAL   A HB   1 
ATOM   2702 H HG11 . VAL   A 1 121 ? 21.857 -11.283 15.703  1.00 20.06 ?  121 VAL   A HG11 1 
ATOM   2703 H HG12 . VAL   A 1 121 ? 22.181 -10.321 14.482  1.00 20.06 ?  121 VAL   A HG12 1 
ATOM   2704 H HG13 . VAL   A 1 121 ? 21.568 -11.763 14.217  1.00 20.06 ?  121 VAL   A HG13 1 
ATOM   2705 H HG21 . VAL   A 1 121 ? 23.273 -13.024 16.343  1.00 22.25 ?  121 VAL   A HG21 1 
ATOM   2706 H HG22 . VAL   A 1 121 ? 23.097 -13.809 14.973  1.00 22.25 ?  121 VAL   A HG22 1 
ATOM   2707 H HG23 . VAL   A 1 121 ? 24.551 -13.445 15.498  1.00 22.25 ?  121 VAL   A HG23 1 
ATOM   2708 N N    . LEU   A 1 122 ? 23.110 -10.225 11.782  1.00 11.14 ?  122 LEU   A N    1 
ATOM   2709 C CA   . LEU   A 1 122 ? 23.110 -8.932  11.103  1.00 11.13 ?  122 LEU   A CA   1 
ATOM   2710 C C    . LEU   A 1 122 ? 21.709 -8.347  11.065  1.00 10.72 ?  122 LEU   A C    1 
ATOM   2711 O O    . LEU   A 1 122 ? 20.727 -9.075  10.922  1.00 11.90 ?  122 LEU   A O    1 
ATOM   2712 C CB   . LEU   A 1 122 ? 23.537 -9.030  9.633   1.00 12.57 ?  122 LEU   A CB   1 
ATOM   2713 C CG   . LEU   A 1 122 ? 24.749 -9.874  9.286   1.00 12.53 ?  122 LEU   A CG   1 
ATOM   2714 C CD1  . LEU   A 1 122 ? 24.338 -11.323 9.073   1.00 13.34 ?  122 LEU   A CD1  1 
ATOM   2715 C CD2  . LEU   A 1 122 ? 25.422 -9.319  8.043   1.00 12.06 ?  122 LEU   A CD2  1 
ATOM   2716 H H    . LEU   A 1 122 ? 22.409 -10.703 11.622  1.00 13.34 ?  122 LEU   A H    1 
ATOM   2717 H HA   . LEU   A 1 122 ? 23.700 -8.314  11.562  1.00 13.33 ?  122 LEU   A HA   1 
ATOM   2718 H HB2  . LEU   A 1 122 ? 22.797 -9.398  9.130   1.00 15.06 ?  122 LEU   A HB2  1 
ATOM   2719 H HB3  . LEU   A 1 122 ? 23.727 -8.137  9.316   1.00 15.06 ?  122 LEU   A HB3  1 
ATOM   2720 H HG   . LEU   A 1 122 ? 25.396 -9.848  10.011  1.00 15.01 ?  122 LEU   A HG   1 
ATOM   2721 H HD11 . LEU   A 1 122 ? 25.109 -11.846 8.808   1.00 15.98 ?  122 LEU   A HD11 1 
ATOM   2722 H HD12 . LEU   A 1 122 ? 23.972 -11.675 9.902   1.00 15.98 ?  122 LEU   A HD12 1 
ATOM   2723 H HD13 . LEU   A 1 122 ? 23.660 -11.362 8.376   1.00 15.98 ?  122 LEU   A HD13 1 
ATOM   2724 H HD21 . LEU   A 1 122 ? 26.174 -9.891  7.798   1.00 14.45 ?  122 LEU   A HD21 1 
ATOM   2725 H HD22 . LEU   A 1 122 ? 24.782 -9.298  7.315   1.00 14.45 ?  122 LEU   A HD22 1 
ATOM   2726 H HD23 . LEU   A 1 122 ? 25.745 -8.423  8.227   1.00 14.45 ?  122 LEU   A HD23 1 
ATOM   2727 N N    . LEU   A 1 123 ? 21.639 -7.018  11.157  1.00 10.52 ?  123 LEU   A N    1 
ATOM   2728 C CA   . LEU   A 1 123 ? 20.467 -6.230  10.778  1.00 10.30 ?  123 LEU   A CA   1 
ATOM   2729 C C    . LEU   A 1 123 ? 20.716 -5.705  9.369   1.00 9.85  ?  123 LEU   A C    1 
ATOM   2730 O O    . LEU   A 1 123 ? 21.765 -5.101  9.122   1.00 10.66 ?  123 LEU   A O    1 
ATOM   2731 C CB   . LEU   A 1 123 ? 20.326 -5.046  11.738  1.00 10.77 ?  123 LEU   A CB   1 
ATOM   2732 C CG   . LEU   A 1 123 ? 19.280 -3.988  11.389  1.00 11.67 ?  123 LEU   A CG   1 
ATOM   2733 C CD1  . LEU   A 1 123 ? 17.872 -4.587  11.380  1.00 12.35 ?  123 LEU   A CD1  1 
ATOM   2734 C CD2  . LEU   A 1 123 ? 19.381 -2.815  12.360  1.00 12.27 ?  123 LEU   A CD2  1 
ATOM   2735 H H    . LEU   A 1 123 ? 22.288 -6.531  11.449  1.00 12.60 ?  123 LEU   A H    1 
ATOM   2736 H HA   . LEU   A 1 123 ? 19.664 -6.771  10.798  1.00 12.34 ?  123 LEU   A HA   1 
ATOM   2737 H HB2  . LEU   A 1 123 ? 20.089 -5.390  12.617  1.00 12.90 ?  123 LEU   A HB2  1 
ATOM   2738 H HB3  . LEU   A 1 123 ? 21.176 -4.589  11.795  1.00 12.90 ?  123 LEU   A HB3  1 
ATOM   2739 H HG   . LEU   A 1 123 ? 19.451 -3.641  10.498  1.00 13.99 ?  123 LEU   A HG   1 
ATOM   2740 H HD11 . LEU   A 1 123 ? 17.227 -3.892  11.190  1.00 14.80 ?  123 LEU   A HD11 1 
ATOM   2741 H HD12 . LEU   A 1 123 ? 17.830 -5.278  10.700  1.00 14.80 ?  123 LEU   A HD12 1 
ATOM   2742 H HD13 . LEU   A 1 123 ? 17.694 -4.976  12.254  1.00 14.80 ?  123 LEU   A HD13 1 
ATOM   2743 H HD21 . LEU   A 1 123 ? 18.713 -2.152  12.133  1.00 14.70 ?  123 LEU   A HD21 1 
ATOM   2744 H HD22 . LEU   A 1 123 ? 19.227 -3.145  13.262  1.00 14.70 ?  123 LEU   A HD22 1 
ATOM   2745 H HD23 . LEU   A 1 123 ? 20.268 -2.433  12.296  1.00 14.70 ?  123 LEU   A HD23 1 
ATOM   2746 N N    A ALA   A 1 124 ? 19.760 -5.899  8.457   0.48 9.77  ?  124 ALA   A N    1 
ATOM   2747 N N    B ALA   A 1 124 ? 19.773 -5.930  8.455   0.52 9.68  ?  124 ALA   A N    1 
ATOM   2748 C CA   A ALA   A 1 124 ? 20.053 -5.619  7.057   0.48 9.80  ?  124 ALA   A CA   1 
ATOM   2749 C CA   B ALA   A 1 124 ? 20.057 -5.659  7.055   0.52 9.73  ?  124 ALA   A CA   1 
ATOM   2750 C C    A ALA   A 1 124 ? 18.818 -5.194  6.275   0.48 9.65  ?  124 ALA   A C    1 
ATOM   2751 C C    B ALA   A 1 124 ? 18.822 -5.151  6.331   0.52 9.33  ?  124 ALA   A C    1 
ATOM   2752 O O    A ALA   A 1 124 ? 17.692 -5.588  6.610   0.48 10.16 ?  124 ALA   A O    1 
ATOM   2753 O O    B ALA   A 1 124 ? 17.685 -5.422  6.744   0.52 10.12 ?  124 ALA   A O    1 
ATOM   2754 C CB   A ALA   A 1 124 ? 20.653 -6.851  6.371   0.48 10.19 ?  124 ALA   A CB   1 
ATOM   2755 C CB   B ALA   A 1 124 ? 20.596 -6.902  6.339   0.52 10.11 ?  124 ALA   A CB   1 
ATOM   2756 H H    A ALA   A 1 124 ? 18.957 -6.164  8.617   0.48 11.70 ?  124 ALA   A H    1 
ATOM   2757 H H    B ALA   A 1 124 ? 18.980 -6.233  8.614   0.52 11.59 ?  124 ALA   A H    1 
ATOM   2758 H HA   A ALA   A 1 124 ? 20.722 -4.911  7.025   0.48 11.74 ?  124 ALA   A HA   1 
ATOM   2759 H HA   B ALA   A 1 124 ? 20.731 -4.971  7.005   0.52 11.65 ?  124 ALA   A HA   1 
ATOM   2760 H HB1  A ALA   A 1 124 ? 20.845 -6.636  5.444   0.48 12.21 ?  124 ALA   A HB1  1 
ATOM   2761 H HB1  B ALA   A 1 124 ? 20.774 -6.689  5.409   0.52 12.11 ?  124 ALA   A HB1  1 
ATOM   2762 H HB2  A ALA   A 1 124 ? 21.473 -7.106  6.826   0.48 12.21 ?  124 ALA   A HB2  1 
ATOM   2763 H HB2  B ALA   A 1 124 ? 21.423 -7.179  6.773   0.52 12.11 ?  124 ALA   A HB2  1 
ATOM   2764 H HB3  A ALA   A 1 124 ? 20.013 -7.579  6.415   0.48 12.21 ?  124 ALA   A HB3  1 
ATOM   2765 H HB3  B ALA   A 1 124 ? 19.943 -7.615  6.395   0.52 12.11 ?  124 ALA   A HB3  1 
ATOM   2766 N N    A PRO   A 1 125 ? 19.009 -4.425  5.208   0.48 9.92  ?  125 PRO   A N    1 
ATOM   2767 N N    B PRO   A 1 125 ? 19.021 -4.429  5.225   0.52 9.03  ?  125 PRO   A N    1 
ATOM   2768 C CA   A PRO   A 1 125 ? 17.958 -4.200  4.216   0.48 9.83  ?  125 PRO   A CA   1 
ATOM   2769 C CA   B PRO   A 1 125 ? 17.933 -4.093  4.311   0.52 9.70  ?  125 PRO   A CA   1 
ATOM   2770 C C    A PRO   A 1 125 ? 18.016 -5.260  3.120   0.48 9.49  ?  125 PRO   A C    1 
ATOM   2771 C C    B PRO   A 1 125 ? 17.903 -5.109  3.185   0.52 10.38 ?  125 PRO   A C    1 
ATOM   2772 O O    A PRO   A 1 125 ? 18.981 -6.019  3.001   0.48 9.89  ?  125 PRO   A O    1 
ATOM   2773 O O    B PRO   A 1 125 ? 18.809 -5.944  3.083   0.52 11.06 ?  125 PRO   A O    1 
ATOM   2774 C CB   A PRO   A 1 125 ? 18.382 -2.854  3.618   0.48 10.34 ?  125 PRO   A CB   1 
ATOM   2775 C CB   B PRO   A 1 125 ? 18.398 -2.738  3.769   0.52 9.64  ?  125 PRO   A CB   1 
ATOM   2776 C CG   A PRO   A 1 125 ? 19.888 -2.963  3.590   0.48 10.74 ?  125 PRO   A CG   1 
ATOM   2777 C CG   B PRO   A 1 125 ? 19.908 -2.958  3.598   0.52 9.63  ?  125 PRO   A CG   1 
ATOM   2778 C CD   A PRO   A 1 125 ? 20.226 -3.646  4.900   0.48 10.49 ?  125 PRO   A CD   1 
ATOM   2779 C CD   B PRO   A 1 125 ? 20.311 -3.914  4.722   0.52 8.61  ?  125 PRO   A CD   1 
ATOM   2780 H HA   A PRO   A 1 125 ? 17.075 -4.152  4.620   0.48 11.77 ?  125 PRO   A HA   1 
ATOM   2781 H HA   B PRO   A 1 125 ? 17.067 -4.023  4.751   0.52 11.62 ?  125 PRO   A HA   1 
ATOM   2782 H HB2  A PRO   A 1 125 ? 18.015 -2.761  2.723   0.48 12.38 ?  125 PRO   A HB2  1 
ATOM   2783 H HB2  B PRO   A 1 125 ? 17.972 -2.545  2.917   0.52 11.54 ?  125 PRO   A HB2  1 
ATOM   2784 H HB3  A PRO   A 1 125 ? 18.088 -2.130  4.193   0.48 12.38 ?  125 PRO   A HB3  1 
ATOM   2785 H HB3  B PRO   A 1 125 ? 18.215 -2.034  4.415   0.52 11.54 ?  125 PRO   A HB3  1 
ATOM   2786 H HG2  A PRO   A 1 125 ? 20.168 -3.505  2.834   0.48 12.87 ?  125 PRO   A HG2  1 
ATOM   2787 H HG2  B PRO   A 1 125 ? 20.084 -3.352  2.729   0.52 11.53 ?  125 PRO   A HG2  1 
ATOM   2788 H HG3  A PRO   A 1 125 ? 20.281 -2.076  3.544   0.48 12.87 ?  125 PRO   A HG3  1 
ATOM   2789 H HG3  B PRO   A 1 125 ? 20.374 -2.107  3.684   0.52 11.53 ?  125 PRO   A HG3  1 
ATOM   2790 H HD2  A PRO   A 1 125 ? 20.989 -4.231  4.792   0.48 12.57 ?  125 PRO   A HD2  1 
ATOM   2791 H HD2  B PRO   A 1 125 ? 20.853 -4.634  4.368   0.52 10.30 ?  125 PRO   A HD2  1 
ATOM   2792 H HD3  A PRO   A 1 125 ? 20.386 -2.981  5.596   0.48 12.57 ?  125 PRO   A HD3  1 
ATOM   2793 H HD3  B PRO   A 1 125 ? 20.777 -3.424  5.419   0.52 10.30 ?  125 PRO   A HD3  1 
ATOM   2794 N N    A LEU   A 1 126 ? 16.972 -5.272  2.293   0.48 9.72  ?  126 LEU   A N    1 
ATOM   2795 N N    B LEU   A 1 126 ? 16.899 -5.037  2.319   0.52 11.31 ?  126 LEU   A N    1 
ATOM   2796 C CA   A LEU   A 1 126 ? 16.981 -6.072  1.075   0.48 10.40 ?  126 LEU   A CA   1 
ATOM   2797 C CA   B LEU   A 1 126 ? 16.932 -5.814  1.088   0.52 11.61 ?  126 LEU   A CA   1 
ATOM   2798 C C    A LEU   A 1 126 ? 17.901 -5.438  0.044   0.48 11.21 ?  126 LEU   A C    1 
ATOM   2799 C C    B LEU   A 1 126 ? 17.891 -5.165  0.096   0.52 11.19 ?  126 LEU   A C    1 
ATOM   2800 O O    A LEU   A 1 126 ? 17.621 -4.354  -0.479  0.48 11.82 ?  126 LEU   A O    1 
ATOM   2801 O O    B LEU   A 1 126 ? 17.799 -3.966  -0.176  0.52 12.41 ?  126 LEU   A O    1 
ATOM   2802 C CB   A LEU   A 1 126 ? 15.570 -6.214  0.523   0.48 10.95 ?  126 LEU   A CB   1 
ATOM   2803 C CB   B LEU   A 1 126 ? 15.537 -5.903  0.475   0.52 12.91 ?  126 LEU   A CB   1 
ATOM   2804 C CG   A LEU   A 1 126 ? 14.703 -7.159  1.348   0.48 11.71 ?  126 LEU   A CG   1 
ATOM   2805 C CG   B LEU   A 1 126 ? 14.562 -6.905  1.087   0.52 13.64 ?  126 LEU   A CG   1 
ATOM   2806 C CD1  A LEU   A 1 126 ? 13.250 -7.026  0.947   0.48 12.33 ?  126 LEU   A CD1  1 
ATOM   2807 C CD1  B LEU   A 1 126 ? 13.244 -6.828  0.350   0.52 14.18 ?  126 LEU   A CD1  1 
ATOM   2808 C CD2  A LEU   A 1 126 ? 15.180 -8.598  1.183   0.48 11.65 ?  126 LEU   A CD2  1 
ATOM   2809 C CD2  B LEU   A 1 126 ? 15.104 -8.329  1.032   0.52 14.25 ?  126 LEU   A CD2  1 
ATOM   2810 H H    A LEU   A 1 126 ? 16.253 -4.817  2.408   0.48 11.64 ?  126 LEU   A H    1 
ATOM   2811 H H    B LEU   A 1 126 ? 16.200 -4.540  2.429   0.52 13.55 ?  126 LEU   A H    1 
ATOM   2812 H HA   A LEU   A 1 126 ? 17.324 -6.949  1.269   0.48 12.45 ?  126 LEU   A HA   1 
ATOM   2813 H HA   B LEU   A 1 126 ? 17.241 -6.707  1.287   0.52 13.90 ?  126 LEU   A HA   1 
ATOM   2814 H HB2  A LEU   A 1 126 ? 15.138 -5.342  0.518   0.48 13.11 ?  126 LEU   A HB2  1 
ATOM   2815 H HB2  B LEU   A 1 126 ? 15.116 -5.029  0.542   0.52 15.46 ?  126 LEU   A HB2  1 
ATOM   2816 H HB3  A LEU   A 1 126 ? 15.613 -6.560  -0.384  0.48 13.11 ?  126 LEU   A HB3  1 
ATOM   2817 H HB3  B LEU   A 1 126 ? 15.633 -6.138  -0.459  0.52 15.46 ?  126 LEU   A HB3  1 
ATOM   2818 H HG   A LEU   A 1 126 ? 14.780 -6.924  2.285   0.48 14.03 ?  126 LEU   A HG   1 
ATOM   2819 H HG   B LEU   A 1 126 ? 14.403 -6.677  2.017   0.52 16.34 ?  126 LEU   A HG   1 
ATOM   2820 H HD11 A LEU   A 1 126 ? 12.718 -7.636  1.482   0.48 14.77 ?  126 LEU   A HD11 1 
ATOM   2821 H HD11 B LEU   A 1 126 ? 12.625 -7.465  0.742   0.52 16.99 ?  126 LEU   A HD11 1 
ATOM   2822 H HD12 A LEU   A 1 126 ? 12.963 -6.113  1.101   0.48 14.77 ?  126 LEU   A HD12 1 
ATOM   2823 H HD12 B LEU   A 1 126 ? 12.890 -5.930  0.429   0.52 16.99 ?  126 LEU   A HD12 1 
ATOM   2824 H HD13 A LEU   A 1 126 ? 13.161 -7.248  0.007   0.48 14.77 ?  126 LEU   A HD13 1 
ATOM   2825 H HD13 B LEU   A 1 126 ? 13.393 -7.046  -0.584  0.52 16.99 ?  126 LEU   A HD13 1 
ATOM   2826 H HD21 A LEU   A 1 126 ? 14.513 -9.196  1.549   0.48 13.96 ?  126 LEU   A HD21 1 
ATOM   2827 H HD21 B LEU   A 1 126 ? 14.395 -8.949  1.258   0.52 17.08 ?  126 LEU   A HD21 1 
ATOM   2828 H HD22 A LEU   A 1 126 ? 15.308 -8.780  0.238   0.48 13.96 ?  126 LEU   A HD22 1 
ATOM   2829 H HD22 B LEU   A 1 126 ? 15.426 -8.508  0.133   0.52 17.08 ?  126 LEU   A HD22 1 
ATOM   2830 H HD23 A LEU   A 1 126 ? 16.021 -8.709  1.655   0.48 13.96 ?  126 LEU   A HD23 1 
ATOM   2831 H HD23 B LEU   A 1 126 ? 15.835 -8.414  1.665   0.52 17.08 ?  126 LEU   A HD23 1 
ATOM   2832 N N    A LEU   A 1 127 ? 18.977 -6.147  -0.278  0.48 11.66 ?  127 LEU   A N    1 
ATOM   2833 N N    B LEU   A 1 127 ? 18.812 -5.950  -0.446  0.52 10.37 ?  127 LEU   A N    1 
ATOM   2834 C CA   A LEU   A 1 127 ? 19.961 -5.646  -1.220  0.48 11.44 ?  127 LEU   A CA   1 
ATOM   2835 C CA   B LEU   A 1 127 ? 19.812 -5.410  -1.354  0.52 10.86 ?  127 LEU   A CA   1 
ATOM   2836 C C    A LEU   A 1 127 ? 19.328 -5.438  -2.583  0.48 10.73 ?  127 LEU   A C    1 
ATOM   2837 C C    B LEU   A 1 127 ? 19.311 -5.393  -2.797  0.52 11.36 ?  127 LEU   A C    1 
ATOM   2838 O O    A LEU   A 1 127 ? 18.457 -6.203  -3.015  0.48 10.98 ?  127 LEU   A O    1 
ATOM   2839 O O    B LEU   A 1 127 ? 18.533 -6.251  -3.232  0.52 11.73 ?  127 LEU   A O    1 
ATOM   2840 C CB   A LEU   A 1 127 ? 21.117 -6.635  -1.339  0.48 11.52 ?  127 LEU   A CB   1 
ATOM   2841 C CB   B LEU   A 1 127 ? 21.115 -6.209  -1.274  0.52 11.04 ?  127 LEU   A CB   1 
ATOM   2842 C CG   A LEU   A 1 127 ? 21.899 -6.853  -0.048  0.48 11.75 ?  127 LEU   A CG   1 
ATOM   2843 C CG   B LEU   A 1 127 ? 21.884 -6.178  0.053   0.52 12.00 ?  127 LEU   A CG   1 
ATOM   2844 C CD1  A LEU   A 1 127 ? 23.001 -7.855  -0.299  0.48 11.96 ?  127 LEU   A CD1  1 
ATOM   2845 C CD1  B LEU   A 1 127 ? 23.070 -7.126  0.011   0.52 12.66 ?  127 LEU   A CD1  1 
ATOM   2846 C CD2  A LEU   A 1 127 ? 22.472 -5.545  0.469   0.48 12.51 ?  127 LEU   A CD2  1 
ATOM   2847 C CD2  B LEU   A 1 127 ? 22.347 -4.765  0.389   0.52 12.93 ?  127 LEU   A CD2  1 
ATOM   2848 H H    A LEU   A 1 127 ? 19.147 -6.931  0.026   0.48 13.97 ?  127 LEU   A H    1 
ATOM   2849 H H    B LEU   A 1 127 ? 18.884 -6.798  -0.290  0.52 12.42 ?  127 LEU   A H    1 
ATOM   2850 H HA   A LEU   A 1 127 ? 20.307 -4.799  -0.913  0.48 13.71 ?  127 LEU   A HA   1 
ATOM   2851 H HA   B LEU   A 1 127 ? 20.010 -4.496  -1.078  0.52 13.01 ?  127 LEU   A HA   1 
ATOM   2852 H HB2  A LEU   A 1 127 ? 20.764 -7.498  -1.618  0.48 13.80 ?  127 LEU   A HB2  1 
ATOM   2853 H HB2  B LEU   A 1 127 ? 20.911 -7.136  -1.462  0.52 13.23 ?  127 LEU   A HB2  1 
ATOM   2854 H HB3  A LEU   A 1 127 ? 21.741 -6.311  -2.010  0.48 13.80 ?  127 LEU   A HB3  1 
ATOM   2855 H HB3  B LEU   A 1 127 ? 21.714 -5.866  -1.955  0.52 13.23 ?  127 LEU   A HB3  1 
ATOM   2856 H HG   A LEU   A 1 127 ? 21.304 -7.217  0.628   0.48 14.08 ?  127 LEU   A HG   1 
ATOM   2857 H HG   B LEU   A 1 127 ? 21.295 -6.474  0.764   0.52 14.37 ?  127 LEU   A HG   1 
ATOM   2858 H HD11 A LEU   A 1 127 ? 23.463 -8.026  0.535   0.48 14.32 ?  127 LEU   A HD11 1 
ATOM   2859 H HD11 B LEU   A 1 127 ? 23.538 -7.085  0.862   0.52 15.17 ?  127 LEU   A HD11 1 
ATOM   2860 H HD12 A LEU   A 1 127 ? 22.610 -8.674  -0.638  0.48 14.32 ?  127 LEU   A HD12 1 
ATOM   2861 H HD12 B LEU   A 1 127 ? 22.748 -8.028  -0.144  0.52 15.17 ?  127 LEU   A HD12 1 
ATOM   2862 H HD13 A LEU   A 1 127 ? 23.615 -7.485  -0.951  0.48 14.32 ?  127 LEU   A HD13 1 
ATOM   2863 H HD13 B LEU   A 1 127 ? 23.665 -6.858  -0.705  0.52 15.17 ?  127 LEU   A HD13 1 
ATOM   2864 H HD21 A LEU   A 1 127 ? 23.113 -5.736  1.169   0.48 14.99 ?  127 LEU   A HD21 1 
ATOM   2865 H HD21 B LEU   A 1 127 ? 22.911 -4.797  1.178   0.52 15.49 ?  127 LEU   A HD21 1 
ATOM   2866 H HD22 A LEU   A 1 127 ? 22.911 -5.083  -0.265  0.48 14.99 ?  127 LEU   A HD22 1 
ATOM   2867 H HD22 B LEU   A 1 127 ? 22.850 -4.412  -0.362  0.52 15.49 ?  127 LEU   A HD22 1 
ATOM   2868 H HD23 A LEU   A 1 127 ? 21.751 -4.998  0.818   0.48 14.99 ?  127 LEU   A HD23 1 
ATOM   2869 H HD23 B LEU   A 1 127 ? 21.571 -4.211  0.558   0.52 15.49 ?  127 LEU   A HD23 1 
ATOM   2870 N N    A SER   A 1 128 ? 19.774 -4.381  -3.255  0.48 10.98 ?  128 SER   A N    1 
ATOM   2871 N N    B SER   A 1 128 ? 19.783 -4.385  -3.530  0.52 12.06 ?  128 SER   A N    1 
ATOM   2872 C CA   A SER   A 1 128 ? 19.388 -4.004  -4.604  0.48 11.00 ?  128 SER   A CA   1 
ATOM   2873 C CA   B SER   A 1 128 ? 19.542 -4.157  -4.952  0.52 13.04 ?  128 SER   A CA   1 
ATOM   2874 C C    A SER   A 1 128 ? 17.934 -3.578  -4.713  0.48 10.62 ?  128 SER   A C    1 
ATOM   2875 C C    B SER   A 1 128 ? 18.142 -3.649  -5.277  0.52 14.17 ?  128 SER   A C    1 
ATOM   2876 O O    A SER   A 1 128 ? 17.483 -3.275  -5.820  0.48 11.14 ?  128 SER   A O    1 
ATOM   2877 O O    B SER   A 1 128 ? 17.873 -3.303  -6.430  0.52 14.34 ?  128 SER   A O    1 
ATOM   2878 C CB   A SER   A 1 128 ? 19.725 -5.070  -5.655  0.48 11.02 ?  128 SER   A CB   1 
ATOM   2879 C CB   B SER   A 1 128 ? 19.928 -5.359  -5.825  0.52 12.50 ?  128 SER   A CB   1 
ATOM   2880 O OG   A SER   A 1 128 ? 21.131 -5.254  -5.738  0.48 10.79 ?  128 SER   A OG   1 
ATOM   2881 O OG   B SER   A 1 128 ? 21.335 -5.531  -5.828  0.52 11.95 ?  128 SER   A OG   1 
ATOM   2882 H H    A SER   A 1 128 ? 20.344 -3.819  -2.919  0.48 13.15 ?  128 SER   A H    1 
ATOM   2883 H H    B SER   A 1 128 ? 20.296 -3.785  -3.190  0.52 14.44 ?  128 SER   A H    1 
ATOM   2884 H HA   A SER   A 1 128 ? 19.903 -3.223  -4.838  0.48 13.18 ?  128 SER   A HA   1 
ATOM   2885 H HA   B SER   A 1 128 ? 20.143 -3.448  -5.202  0.52 15.62 ?  128 SER   A HA   1 
ATOM   2886 H HB2  A SER   A 1 128 ? 19.303 -5.903  -5.403  0.48 13.20 ?  128 SER   A HB2  1 
ATOM   2887 H HB2  B SER   A 1 128 ? 19.504 -6.159  -5.492  0.52 14.98 ?  128 SER   A HB2  1 
ATOM   2888 H HB3  A SER   A 1 128 ? 19.399 -4.772  -6.519  0.48 13.20 ?  128 SER   A HB3  1 
ATOM   2889 H HB3  B SER   A 1 128 ? 19.638 -5.180  -6.741  0.52 14.98 ?  128 SER   A HB3  1 
ATOM   2890 H HG   A SER   A 1 128 ? 21.500 -4.514  -5.918  0.48 12.92 ?  128 SER   A HG   1 
ATOM   2891 H HG   B SER   A 1 128 ? 21.707 -4.822  -6.095  0.52 14.32 ?  128 SER   A HG   1 
ATOM   2892 N N    A ALA   A 1 129 ? 17.193 -3.523  -3.607  0.48 10.68 ?  129 ALA   A N    1 
ATOM   2893 N N    B ALA   A 1 129 ? 17.254 -3.569  -4.289  0.52 15.30 ?  129 ALA   A N    1 
ATOM   2894 C CA   A ALA   A 1 129 ? 15.822 -3.038  -3.625  0.48 11.09 ?  129 ALA   A CA   1 
ATOM   2895 C CA   B ALA   A 1 129 ? 15.925 -3.043  -4.546  0.52 17.01 ?  129 ALA   A CA   1 
ATOM   2896 C C    A ALA   A 1 129 ? 15.810 -1.509  -3.594  0.48 10.99 ?  129 ALA   A C    1 
ATOM   2897 C C    B ALA   A 1 129 ? 15.906 -1.521  -4.400  0.52 19.20 ?  129 ALA   A C    1 
ATOM   2898 O O    A ALA   A 1 129 ? 16.851 -0.847  -3.620  0.48 12.22 ?  129 ALA   A O    1 
ATOM   2899 O O    B ALA   A 1 129 ? 16.909 -0.884  -4.071  0.52 19.34 ?  129 ALA   A O    1 
ATOM   2900 C CB   A ALA   A 1 129 ? 15.025 -3.659  -2.474  0.48 12.53 ?  129 ALA   A CB   1 
ATOM   2901 C CB   B ALA   A 1 129 ? 14.892 -3.725  -3.652  0.52 17.72 ?  129 ALA   A CB   1 
ATOM   2902 H H    A ALA   A 1 129 ? 17.462 -3.761  -2.822  0.48 12.79 ?  129 ALA   A H    1 
ATOM   2903 H H    B ALA   A 1 129 ? 17.388 -3.806  -3.469  0.52 18.33 ?  129 ALA   A H    1 
ATOM   2904 H HA   A ALA   A 1 129 ? 15.397 -3.303  -4.446  0.48 13.28 ?  129 ALA   A HA   1 
ATOM   2905 H HA   B ALA   A 1 129 ? 15.692 -3.239  -5.463  0.52 20.39 ?  129 ALA   A HA   1 
ATOM   2906 H HB1  A ALA   A 1 129 ? 14.111 -3.331  -2.498  0.48 15.01 ?  129 ALA   A HB1  1 
ATOM   2907 H HB1  B ALA   A 1 129 ? 14.018 -3.344  -3.840  0.52 21.24 ?  129 ALA   A HB1  1 
ATOM   2908 H HB2  A ALA   A 1 129 ? 15.027 -4.627  -2.568  0.48 15.01 ?  129 ALA   A HB2  1 
ATOM   2909 H HB2  B ALA   A 1 129 ? 14.889 -4.673  -3.852  0.52 21.24 ?  129 ALA   A HB2  1 
ATOM   2910 H HB3  A ALA   A 1 129 ? 15.436 -3.415  -1.625  0.48 15.01 ?  129 ALA   A HB3  1 
ATOM   2911 H HB3  B ALA   A 1 129 ? 15.128 -3.577  -2.728  0.52 21.24 ?  129 ALA   A HB3  1 
ATOM   2912 N N    A GLY   A 1 130 ? 14.613 -0.939  -3.567  0.48 11.03 ?  130 GLY   A N    1 
ATOM   2913 N N    B GLY   A 1 130 ? 14.750 -0.929  -4.678  0.52 21.36 ?  130 GLY   A N    1 
ATOM   2914 C CA   A GLY   A 1 130 ? 14.504 0.508   -3.514  0.48 12.01 ?  130 GLY   A CA   1 
ATOM   2915 C CA   B GLY   A 1 130 ? 14.605 0.511   -4.560  0.52 22.61 ?  130 GLY   A CA   1 
ATOM   2916 C C    A GLY   A 1 130 ? 15.124 1.149   -4.743  0.48 12.21 ?  130 GLY   A C    1 
ATOM   2917 C C    B GLY   A 1 130 ? 15.454 1.239   -5.583  0.52 23.50 ?  130 GLY   A C    1 
ATOM   2918 O O    A GLY   A 1 130 ? 14.904 0.719   -5.881  0.48 11.76 ?  130 GLY   A O    1 
ATOM   2919 O O    B GLY   A 1 130 ? 15.441 0.902   -6.773  0.52 23.78 ?  130 GLY   A O    1 
ATOM   2920 H H    A GLY   A 1 130 ? 13.857 -1.362  -3.587  0.48 13.21 ?  130 GLY   A H    1 
ATOM   2921 H H    B GLY   A 1 130 ? 14.043 -1.325  -4.941  0.52 25.60 ?  130 GLY   A H    1 
ATOM   2922 H HA2  A GLY   A 1 130 ? 13.564 0.760   -3.460  0.48 14.39 ?  130 GLY   A HA2  1 
ATOM   2923 H HA2  B GLY   A 1 130 ? 13.686 0.753   -4.706  0.52 27.11 ?  130 GLY   A HA2  1 
ATOM   2924 H HA3  A GLY   A 1 130 ? 14.955 0.842   -2.723  0.48 14.39 ?  130 GLY   A HA3  1 
ATOM   2925 H HA3  B GLY   A 1 130 ? 14.823 0.786   -3.673  0.52 27.11 ?  130 GLY   A HA3  1 
ATOM   2926 N N    A ILE   A 1 131 ? 15.926 2.189   -4.513  0.48 12.63 ?  131 ILE   A N    1 
ATOM   2927 N N    B ILE   A 1 131 ? 16.205 2.250   -5.134  0.52 24.15 ?  131 ILE   A N    1 
ATOM   2928 C CA   A ILE   A 1 131 ? 16.494 2.964   -5.614  0.48 12.29 ?  131 ILE   A CA   1 
ATOM   2929 C CA   B ILE   A 1 131 ? 16.977 3.075   -6.057  0.52 24.20 ?  131 ILE   A CA   1 
ATOM   2930 C C    A ILE   A 1 131 ? 17.535 2.202   -6.420  0.48 11.88 ?  131 ILE   A C    1 
ATOM   2931 C C    B ILE   A 1 131 ? 18.008 2.272   -6.835  0.52 23.82 ?  131 ILE   A C    1 
ATOM   2932 O O    A ILE   A 1 131 ? 17.964 2.701   -7.471  0.48 11.99 ?  131 ILE   A O    1 
ATOM   2933 O O    B ILE   A 1 131 ? 18.568 2.785   -7.808  0.52 24.31 ?  131 ILE   A O    1 
ATOM   2934 C CB   A ILE   A 1 131 ? 17.038 4.322   -5.124  0.48 13.59 ?  131 ILE   A CB   1 
ATOM   2935 C CB   B ILE   A 1 131 ? 17.599 4.327   -5.381  0.52 24.79 ?  131 ILE   A CB   1 
ATOM   2936 C CG1  A ILE   A 1 131 ? 18.251 4.133   -4.210  0.48 15.49 ?  131 ILE   A CG1  1 
ATOM   2937 C CG1  B ILE   A 1 131 ? 18.800 3.965   -4.504  0.52 25.20 ?  131 ILE   A CG1  1 
ATOM   2938 C CG2  A ILE   A 1 131 ? 15.937 5.100   -4.415  0.48 14.12 ?  131 ILE   A CG2  1 
ATOM   2939 C CG2  B ILE   A 1 131 ? 16.554 5.070   -4.556  0.52 25.02 ?  131 ILE   A CG2  1 
ATOM   2940 C CD1  A ILE   A 1 131 ? 18.884 5.441   -3.773  0.48 16.56 ?  131 ILE   A CD1  1 
ATOM   2941 C CD1  B ILE   A 1 131 ? 19.493 5.180   -3.894  0.52 25.53 ?  131 ILE   A CD1  1 
ATOM   2942 H H    A ILE   A 1 131 ? 16.130 2.470   -3.731  0.48 15.14 ?  131 ILE   A H    1 
ATOM   2943 H H    B ILE   A 1 131 ? 16.284 2.475   -4.308  0.52 28.96 ?  131 ILE   A H    1 
ATOM   2944 H HA   A ILE   A 1 131 ? 15.768 3.156   -6.226  0.48 14.72 ?  131 ILE   A HA   1 
ATOM   2945 H HA   B ILE   A 1 131 ? 16.368 3.412   -6.721  0.52 29.02 ?  131 ILE   A HA   1 
ATOM   2946 H HB   A ILE   A 1 131 ? 17.308 4.825   -5.902  0.48 16.29 ?  131 ILE   A HB   1 
ATOM   2947 H HB   B ILE   A 1 131 ? 17.908 4.926   -6.080  0.52 29.72 ?  131 ILE   A HB   1 
ATOM   2948 H HG12 A ILE   A 1 131 ? 17.970 3.653   -3.415  0.48 18.56 ?  131 ILE   A HG12 1 
ATOM   2949 H HG12 B ILE   A 1 131 ? 18.501 3.401   -3.778  0.52 30.22 ?  131 ILE   A HG12 1 
ATOM   2950 H HG13 A ILE   A 1 131 ? 18.923 3.621   -4.685  0.48 18.56 ?  131 ILE   A HG13 1 
ATOM   2951 H HG13 B ILE   A 1 131 ? 19.460 3.500   -5.038  0.52 30.22 ?  131 ILE   A HG13 1 
ATOM   2952 H HG21 A ILE   A 1 131 ? 16.260 5.987   -4.208  0.48 16.92 ?  131 ILE   A HG21 1 
ATOM   2953 H HG21 B ILE   A 1 131 ? 16.898 5.948   -4.323  0.52 30.00 ?  131 ILE   A HG21 1 
ATOM   2954 H HG22 A ILE   A 1 131 ? 15.164 5.158   -5.001  0.48 16.92 ?  131 ILE   A HG22 1 
ATOM   2955 H HG22 B ILE   A 1 131 ? 15.747 5.162   -5.084  0.52 30.00 ?  131 ILE   A HG22 1 
ATOM   2956 H HG23 A ILE   A 1 131 ? 15.693 4.634   -3.598  0.48 16.92 ?  131 ILE   A HG23 1 
ATOM   2957 H HG23 B ILE   A 1 131 ? 16.369 4.563   -3.751  0.52 30.00 ?  131 ILE   A HG23 1 
ATOM   2958 H HD11 A ILE   A 1 131 ? 19.725 5.251   -3.333  0.48 19.84 ?  131 ILE   A HD11 1 
ATOM   2959 H HD11 B ILE   A 1 131 ? 20.320 4.895   -3.476  0.52 30.61 ?  131 ILE   A HD11 1 
ATOM   2960 H HD12 A ILE   A 1 131 ? 19.036 5.995   -4.556  0.48 19.84 ?  131 ILE   A HD12 1 
ATOM   2961 H HD12 B ILE   A 1 131 ? 19.683 5.823   -4.597  0.52 30.61 ?  131 ILE   A HD12 1 
ATOM   2962 H HD13 A ILE   A 1 131 ? 18.283 5.895   -3.161  0.48 19.84 ?  131 ILE   A HD13 1 
ATOM   2963 H HD13 B ILE   A 1 131 ? 18.908 5.581   -3.231  0.52 30.61 ?  131 ILE   A HD13 1 
ATOM   2964 N N    A PHE   A 1 132 ? 17.946 1.010   -5.963  0.48 11.80 ?  132 PHE   A N    1 
ATOM   2965 N N    B PHE   A 1 132 ? 18.262 1.021   -6.444  0.52 22.51 ?  132 PHE   A N    1 
ATOM   2966 C CA   A PHE   A 1 132 ? 18.820 0.148   -6.751  0.48 12.32 ?  132 PHE   A CA   1 
ATOM   2967 C CA   B PHE   A 1 132 ? 19.131 0.145   -7.218  0.52 21.64 ?  132 PHE   A CA   1 
ATOM   2968 C C    A PHE   A 1 132 ? 18.067 -0.614  -7.841  0.48 13.14 ?  132 PHE   A C    1 
ATOM   2969 C C    B PHE   A 1 132 ? 18.389 -0.607  -8.318  0.52 20.66 ?  132 PHE   A C    1 
ATOM   2970 O O    A PHE   A 1 132 ? 18.707 -1.234  -8.698  0.48 14.18 ?  132 PHE   A O    1 
ATOM   2971 O O    B PHE   A 1 132 ? 19.038 -1.202  -9.186  0.52 21.01 ?  132 PHE   A O    1 
ATOM   2972 C CB   A PHE   A 1 132 ? 19.591 -0.816  -5.840  0.48 11.41 ?  132 PHE   A CB   1 
ATOM   2973 C CB   B PHE   A 1 132 ? 19.868 -0.835  -6.297  0.52 21.44 ?  132 PHE   A CB   1 
ATOM   2974 C CG   A PHE   A 1 132 ? 20.813 -0.210  -5.172  0.48 10.38 ?  132 PHE   A CG   1 
ATOM   2975 C CG   B PHE   A 1 132 ? 21.157 -0.292  -5.741  0.52 22.08 ?  132 PHE   A CG   1 
ATOM   2976 C CD1  A PHE   A 1 132 ? 20.682 0.813   -4.248  0.48 10.48 ?  132 PHE   A CD1  1 
ATOM   2977 C CD1  B PHE   A 1 132 ? 21.165 0.829   -4.925  0.52 22.80 ?  132 PHE   A CD1  1 
ATOM   2978 C CD2  A PHE   A 1 132 ? 22.086 -0.706  -5.436  0.48 10.90 ?  132 PHE   A CD2  1 
ATOM   2979 C CD2  B PHE   A 1 132 ? 22.360 -0.912  -6.031  0.52 22.65 ?  132 PHE   A CD2  1 
ATOM   2980 C CE1  A PHE   A 1 132 ? 21.804 1.348   -3.625  0.48 10.65 ?  132 PHE   A CE1  1 
ATOM   2981 C CE1  B PHE   A 1 132 ? 22.356 1.321   -4.417  0.52 23.15 ?  132 PHE   A CE1  1 
ATOM   2982 C CE2  A PHE   A 1 132 ? 23.203 -0.179  -4.812  0.48 10.62 ?  132 PHE   A CE2  1 
ATOM   2983 C CE2  B PHE   A 1 132 ? 23.547 -0.427  -5.527  0.52 23.28 ?  132 PHE   A CE2  1 
ATOM   2984 C CZ   A PHE   A 1 132 ? 23.061 0.850   -3.906  0.48 10.21 ?  132 PHE   A CZ   1 
ATOM   2985 C CZ   B PHE   A 1 132 ? 23.548 0.688   -4.720  0.52 23.41 ?  132 PHE   A CZ   1 
ATOM   2986 H H    A PHE   A 1 132 ? 17.727 0.679   -5.190  0.48 14.13 ?  132 PHE   A H    1 
ATOM   2987 H H    B PHE   A 1 132 ? 17.938 0.657   -5.731  0.52 26.99 ?  132 PHE   A H    1 
ATOM   2988 H HA   A PHE   A 1 132 ? 19.467 0.704   -7.193  0.48 14.76 ?  132 PHE   A HA   1 
ATOM   2989 H HA   B PHE   A 1 132 ? 19.805 0.696   -7.642  0.52 25.95 ?  132 PHE   A HA   1 
ATOM   2990 H HB2  A PHE   A 1 132 ? 18.989 -1.124  -5.135  0.48 13.66 ?  132 PHE   A HB2  1 
ATOM   2991 H HB2  B PHE   A 1 132 ? 19.297 -1.058  -5.549  0.52 25.71 ?  132 PHE   A HB2  1 
ATOM   2992 H HB3  A PHE   A 1 132 ? 19.884 -1.573  -6.367  0.48 13.66 ?  132 PHE   A HB3  1 
ATOM   2993 H HB3  B PHE   A 1 132 ? 20.083 -1.634  -6.802  0.52 25.71 ?  132 PHE   A HB3  1 
ATOM   2994 H HD1  A PHE   A 1 132 ? 19.836 1.154   -4.045  0.48 12.55 ?  132 PHE   A HD1  1 
ATOM   2995 H HD1  B PHE   A 1 132 ? 20.367 1.260   -4.720  0.52 27.34 ?  132 PHE   A HD1  1 
ATOM   2996 H HD2  A PHE   A 1 132 ? 22.181 -1.404  -6.046  0.48 13.05 ?  132 PHE   A HD2  1 
ATOM   2997 H HD2  B PHE   A 1 132 ? 22.365 -1.664  -6.576  0.52 27.16 ?  132 PHE   A HD2  1 
ATOM   2998 H HE1  A PHE   A 1 132 ? 21.707 2.041   -3.009  0.48 12.75 ?  132 PHE   A HE1  1 
ATOM   2999 H HE1  B PHE   A 1 132 ? 22.358 2.075   -3.872  0.52 27.76 ?  132 PHE   A HE1  1 
ATOM   3000 H HE2  A PHE   A 1 132 ? 24.043 -0.518  -5.011  0.48 12.72 ?  132 PHE   A HE2  1 
ATOM   3001 H HE2  B PHE   A 1 132 ? 24.347 -0.855  -5.733  0.52 27.91 ?  132 PHE   A HE2  1 
ATOM   3002 H HZ   A PHE   A 1 132 ? 23.810 1.208   -3.491  0.48 12.22 ?  132 PHE   A HZ   1 
ATOM   3003 H HZ   B PHE   A 1 132 ? 24.352 1.013   -4.382  0.52 28.07 ?  132 PHE   A HZ   1 
ATOM   3004 N N    A GLY   A 1 133 ? 16.733 -0.592  -7.825  0.48 13.47 ?  133 GLY   A N    1 
ATOM   3005 N N    B GLY   A 1 133 ? 17.054 -0.609  -8.298  0.52 19.48 ?  133 GLY   A N    1 
ATOM   3006 C CA   A GLY   A 1 133 ? 15.941 -0.969  -8.983  0.48 14.29 ?  133 GLY   A CA   1 
ATOM   3007 C CA   B GLY   A 1 133 ? 16.260 -0.978  -9.449  0.52 18.75 ?  133 GLY   A CA   1 
ATOM   3008 C C    A GLY   A 1 133 ? 15.674 -2.443  -9.201  0.48 14.85 ?  133 GLY   A C    1 
ATOM   3009 C C    B GLY   A 1 133 ? 15.679 -2.379  -9.441  0.52 18.32 ?  133 GLY   A C    1 
ATOM   3010 O O    A GLY   A 1 133 ? 15.150 -2.797  -10.264 0.48 15.87 ?  133 GLY   A O    1 
ATOM   3011 O O    B GLY   A 1 133 ? 14.750 -2.642  -10.216 0.52 18.60 ?  133 GLY   A O    1 
ATOM   3012 H H    A GLY   A 1 133 ? 16.252 -0.356  -7.147  0.48 16.14 ?  133 GLY   A H    1 
ATOM   3013 H H    B GLY   A 1 133 ? 16.586 -0.391  -7.609  0.52 23.35 ?  133 GLY   A H    1 
ATOM   3014 H HA2  A GLY   A 1 133 ? 15.075 -0.533  -8.923  0.48 17.12 ?  133 GLY   A HA2  1 
ATOM   3015 H HA2  B GLY   A 1 133 ? 15.522 -0.357  -9.530  0.52 22.47 ?  133 GLY   A HA2  1 
ATOM   3016 H HA3  A GLY   A 1 133 ? 16.381 -0.641  -9.777  0.48 17.12 ?  133 GLY   A HA3  1 
ATOM   3017 H HA3  B GLY   A 1 133 ? 16.808 -0.892  -10.243 0.52 22.47 ?  133 GLY   A HA3  1 
ATOM   3018 N N    A ALA   A 1 134 ? 15.995 -3.315  -8.249  0.48 14.70 ?  134 ALA   A N    1 
ATOM   3019 N N    B ALA   A 1 134 ? 16.185 -3.285  -8.605  0.52 17.80 ?  134 ALA   A N    1 
ATOM   3020 C CA   A ALA   A 1 134 ? 15.699 -4.731  -8.418  0.48 15.36 ?  134 ALA   A CA   1 
ATOM   3021 C CA   B ALA   A 1 134 ? 15.749 -4.671  -8.701  0.52 17.51 ?  134 ALA   A CA   1 
ATOM   3022 C C    A ALA   A 1 134 ? 14.345 -5.080  -7.805  0.48 16.04 ?  134 ALA   A C    1 
ATOM   3023 C C    B ALA   A 1 134 ? 14.434 -4.895  -7.951  0.52 17.22 ?  134 ALA   A C    1 
ATOM   3024 O O    A ALA   A 1 134 ? 13.770 -4.317  -7.024  0.48 17.06 ?  134 ALA   A O    1 
ATOM   3025 O O    B ALA   A 1 134 ? 13.984 -4.068  -7.151  0.52 17.64 ?  134 ALA   A O    1 
ATOM   3026 C CB   A ALA   A 1 134 ? 16.789 -5.604  -7.798  0.48 15.62 ?  134 ALA   A CB   1 
ATOM   3027 C CB   B ALA   A 1 134 ? 16.831 -5.621  -8.192  0.52 17.77 ?  134 ALA   A CB   1 
ATOM   3028 H H    A ALA   A 1 134 ? 16.372 -3.113  -7.500  0.48 17.62 ?  134 ALA   A H    1 
ATOM   3029 H H    B ALA   A 1 134 ? 16.768 -3.125  -7.989  0.52 21.33 ?  134 ALA   A H    1 
ATOM   3030 H HA   A ALA   A 1 134 ? 15.656 -4.933  -9.364  0.48 18.40 ?  134 ALA   A HA   1 
ATOM   3031 H HA   B ALA   A 1 134 ? 15.593 -4.876  -9.634  0.52 20.98 ?  134 ALA   A HA   1 
ATOM   3032 H HB1  A ALA   A 1 134 ? 16.566 -6.537  -7.951  0.48 18.72 ?  134 ALA   A HB1  1 
ATOM   3033 H HB1  B ALA   A 1 134 ? 16.517 -6.534  -8.292  0.52 21.30 ?  134 ALA   A HB1  1 
ATOM   3034 H HB2  A ALA   A 1 134 ? 17.635 -5.393  -8.218  0.48 18.72 ?  134 ALA   A HB2  1 
ATOM   3035 H HB2  B ALA   A 1 134 ? 17.635 -5.489  -8.718  0.52 21.30 ?  134 ALA   A HB2  1 
ATOM   3036 H HB3  A ALA   A 1 134 ? 16.833 -5.427  -6.847  0.48 18.72 ?  134 ALA   A HB3  1 
ATOM   3037 H HB3  B ALA   A 1 134 ? 17.008 -5.430  -7.260  0.52 21.30 ?  134 ALA   A HB3  1 
ATOM   3038 N N    A ASP   A 1 135 ? 13.842 -6.252  -8.184  0.48 16.14 ?  135 ASP   A N    1 
ATOM   3039 N N    B ASP   A 1 135 ? 13.824 -6.047  -8.224  0.52 17.17 ?  135 ASP   A N    1 
ATOM   3040 C CA   A ASP   A 1 135 ? 12.590 -6.775  -7.642  0.48 16.26 ?  135 ASP   A CA   1 
ATOM   3041 C CA   B ASP   A 1 135 ? 12.547 -6.410  -7.622  0.52 17.57 ?  135 ASP   A CA   1 
ATOM   3042 C C    A ASP   A 1 135 ? 12.801 -7.202  -6.194  0.48 15.30 ?  135 ASP   A C    1 
ATOM   3043 C C    B ASP   A 1 135 ? 12.776 -6.931  -6.207  0.52 16.54 ?  135 ASP   A C    1 
ATOM   3044 O O    A ASP   A 1 135 ? 13.627 -8.087  -5.932  0.48 14.69 ?  135 ASP   A O    1 
ATOM   3045 O O    B ASP   A 1 135 ? 13.491 -7.925  -6.032  0.52 16.28 ?  135 ASP   A O    1 
ATOM   3046 C CB   A ASP   A 1 135 ? 12.143 -7.971  -8.483  0.48 17.41 ?  135 ASP   A CB   1 
ATOM   3047 C CB   B ASP   A 1 135 ? 11.875 -7.492  -8.463  0.52 19.21 ?  135 ASP   A CB   1 
ATOM   3048 C CG   A ASP   A 1 135 ? 10.873 -8.621  -7.967  0.48 18.64 ?  135 ASP   A CG   1 
ATOM   3049 C CG   B ASP   A 1 135 ? 10.471 -7.837  -7.977  0.52 21.17 ?  135 ASP   A CG   1 
ATOM   3050 O OD1  A ASP   A 1 135 ? 10.259 -8.098  -7.015  0.48 18.53 ?  135 ASP   A OD1  1 
ATOM   3051 O OD1  B ASP   A 1 135 ? 10.070 -7.354  -6.896  0.52 22.01 ?  135 ASP   A OD1  1 
ATOM   3052 O OD2  A ASP   A 1 135 ? 10.499 -9.677  -8.517  0.48 20.57 -1 135 ASP   A OD2  1 
ATOM   3053 O OD2  B ASP   A 1 135 ? 9.767  -8.595  -8.680  0.52 22.28 -1 135 ASP   A OD2  1 
ATOM   3054 H H    A ASP   A 1 135 ? 14.208 -6.772  -8.763  0.48 19.34 ?  135 ASP   A H    1 
ATOM   3055 H H    B ASP   A 1 135 ? 14.134 -6.644  -8.759  0.52 20.58 ?  135 ASP   A H    1 
ATOM   3056 H HA   A ASP   A 1 135 ? 11.905 -6.091  -7.692  0.48 19.48 ?  135 ASP   A HA   1 
ATOM   3057 H HA   B ASP   A 1 135 ? 11.968 -5.634  -7.605  0.52 21.06 ?  135 ASP   A HA   1 
ATOM   3058 H HB2  A ASP   A 1 135 ? 11.993 -7.679  -9.396  0.48 20.87 ?  135 ASP   A HB2  1 
ATOM   3059 H HB2  B ASP   A 1 135 ? 11.838 -7.190  -9.386  0.52 23.03 ?  135 ASP   A HB2  1 
ATOM   3060 H HB3  A ASP   A 1 135 ? 12.826 -8.653  -8.457  0.48 20.87 ?  135 ASP   A HB3  1 
ATOM   3061 H HB3  B ASP   A 1 135 ? 12.396 -8.306  -8.403  0.52 23.03 ?  135 ASP   A HB3  1 
ATOM   3062 N N    A PRO   A 1 136 ? 12.092 -6.611  -5.229  0.48 15.27 ?  136 PRO   A N    1 
ATOM   3063 N N    B PRO   A 1 136 ? 12.196 -6.304  -5.182  0.52 16.12 ?  136 PRO   A N    1 
ATOM   3064 C CA   A PRO   A 1 136 ? 12.310 -6.999  -3.826  0.48 15.02 ?  136 PRO   A CA   1 
ATOM   3065 C CA   B PRO   A 1 136 ? 12.428 -6.774  -3.805  0.52 15.91 ?  136 PRO   A CA   1 
ATOM   3066 C C    A PRO   A 1 136 ? 11.918 -8.431  -3.517  0.48 14.03 ?  136 PRO   A C    1 
ATOM   3067 C C    B PRO   A 1 136 ? 11.956 -8.193  -3.538  0.52 15.28 ?  136 PRO   A C    1 
ATOM   3068 O O    A PRO   A 1 136 ? 12.549 -9.055  -2.655  0.48 13.56 ?  136 PRO   A O    1 
ATOM   3069 O O    B PRO   A 1 136 ? 12.480 -8.843  -2.626  0.52 14.49 ?  136 PRO   A O    1 
ATOM   3070 C CB   A PRO   A 1 136 ? 11.460 -5.990  -3.040  0.48 15.87 ?  136 PRO   A CB   1 
ATOM   3071 C CB   B PRO   A 1 136 ? 11.677 -5.742  -2.950  0.52 16.22 ?  136 PRO   A CB   1 
ATOM   3072 C CG   A PRO   A 1 136 ? 10.443 -5.507  -4.015  0.48 16.40 ?  136 PRO   A CG   1 
ATOM   3073 C CG   B PRO   A 1 136 ? 10.713 -5.088  -3.893  0.52 16.71 ?  136 PRO   A CG   1 
ATOM   3074 C CD   A PRO   A 1 136 ? 11.096 -5.534  -5.360  0.48 15.91 ?  136 PRO   A CD   1 
ATOM   3075 C CD   B PRO   A 1 136 ? 11.376 -5.083  -5.218  0.52 16.36 ?  136 PRO   A CD   1 
ATOM   3076 H HA   A PRO   A 1 136 ? 13.246 -6.877  -3.589  0.48 17.99 ?  136 PRO   A HA   1 
ATOM   3077 H HA   B PRO   A 1 136 ? 13.374 -6.721  -3.594  0.52 19.07 ?  136 PRO   A HA   1 
ATOM   3078 H HB2  A PRO   A 1 136 ? 11.039 -6.439  -2.289  0.48 19.02 ?  136 PRO   A HB2  1 
ATOM   3079 H HB2  B PRO   A 1 136 ? 11.202 -6.193  -2.233  0.52 19.44 ?  136 PRO   A HB2  1 
ATOM   3080 H HB3  A PRO   A 1 136 ? 12.024 -5.264  -2.734  0.48 19.02 ?  136 PRO   A HB3  1 
ATOM   3081 H HB3  B PRO   A 1 136 ? 12.304 -5.094  -2.593  0.52 19.44 ?  136 PRO   A HB3  1 
ATOM   3082 H HG2  A PRO   A 1 136 ? 9.676  -6.100  -4.000  0.48 19.65 ?  136 PRO   A HG2  1 
ATOM   3083 H HG2  B PRO   A 1 136 ? 9.894  -5.605  -3.935  0.52 20.03 ?  136 PRO   A HG2  1 
ATOM   3084 H HG3  A PRO   A 1 136 ? 10.182 -4.604  -3.785  0.48 19.65 ?  136 PRO   A HG3  1 
ATOM   3085 H HG3  B PRO   A 1 136 ? 10.534 -4.182  -3.603  0.52 20.03 ?  136 PRO   A HG3  1 
ATOM   3086 H HD2  A PRO   A 1 136 ? 10.450 -5.762  -6.048  0.48 19.07 ?  136 PRO   A HD2  1 
ATOM   3087 H HD2  B PRO   A 1 136 ? 10.713 -5.136  -5.926  0.52 19.61 ?  136 PRO   A HD2  1 
ATOM   3088 H HD3  A PRO   A 1 136 ? 11.534 -4.689  -5.549  0.48 19.07 ?  136 PRO   A HD3  1 
ATOM   3089 H HD3  B PRO   A 1 136 ? 11.942 -4.301  -5.318  0.52 19.61 ?  136 PRO   A HD3  1 
ATOM   3090 N N    A ILE   A 1 137 ? 10.885 -8.969  -4.167  0.48 14.17 ?  137 ILE   A N    1 
ATOM   3091 N N    B ILE   A 1 137 ? 10.970 -8.690  -4.286  0.52 15.73 ?  137 ILE   A N    1 
ATOM   3092 C CA   A ILE   A 1 137 ? 10.551 -10.378 -3.977  0.48 14.13 ?  137 ILE   A CA   1 
ATOM   3093 C CA   B ILE   A 1 137 ? 10.545 -10.080 -4.124  0.52 16.47 ?  137 ILE   A CA   1 
ATOM   3094 C C    A ILE   A 1 137 ? 11.732 -11.253 -4.371  0.48 13.38 ?  137 ILE   A C    1 
ATOM   3095 C C    B ILE   A 1 137 ? 11.699 -11.020 -4.453  0.52 16.28 ?  137 ILE   A C    1 
ATOM   3096 O O    A ILE   A 1 137 ? 12.079 -12.214 -3.671  0.48 13.15 ?  137 ILE   A O    1 
ATOM   3097 O O    B ILE   A 1 137 ? 11.967 -11.989 -3.732  0.52 16.38 ?  137 ILE   A O    1 
ATOM   3098 C CB   A ILE   A 1 137 ? 9.272  -10.738 -4.757  0.48 15.06 ?  137 ILE   A CB   1 
ATOM   3099 C CB   B ILE   A 1 137 ? 9.314  -10.367 -5.001  0.52 17.56 ?  137 ILE   A CB   1 
ATOM   3100 C CG1  A ILE   A 1 137 ? 8.081  -9.927  -4.230  0.48 16.16 ?  137 ILE   A CG1  1 
ATOM   3101 C CG1  B ILE   A 1 137 ? 8.187  -9.379  -4.681  0.52 18.53 ?  137 ILE   A CG1  1 
ATOM   3102 C CG2  A ILE   A 1 137 ? 8.993  -12.235 -4.664  0.48 15.65 ?  137 ILE   A CG2  1 
ATOM   3103 C CG2  B ILE   A 1 137 ? 8.852  -11.804 -4.808  0.52 17.99 ?  137 ILE   A CG2  1 
ATOM   3104 C CD1  A ILE   A 1 137 ? 6.794  -10.133 -5.004  0.48 17.04 ?  137 ILE   A CD1  1 
ATOM   3105 C CD1  B ILE   A 1 137 ? 6.984  -9.509  -5.589  0.52 19.27 ?  137 ILE   A CD1  1 
ATOM   3106 H H    A ILE   A 1 137 ? 10.372 -8.552  -4.713  0.48 16.98 ?  137 ILE   A H    1 
ATOM   3107 H H    B ILE   A 1 137 ? 10.535 -8.247  -4.879  0.52 18.85 ?  137 ILE   A H    1 
ATOM   3108 H HA   A ILE   A 1 137 ? 10.377 -10.542 -3.041  0.48 16.93 ?  137 ILE   A HA   1 
ATOM   3109 H HA   B ILE   A 1 137 ? 10.292 -10.232 -3.202  0.52 19.74 ?  137 ILE   A HA   1 
ATOM   3110 H HB   A ILE   A 1 137 ? 9.400  -10.512 -5.689  0.48 18.04 ?  137 ILE   A HB   1 
ATOM   3111 H HB   B ILE   A 1 137 ? 9.565  -10.250 -5.930  0.52 21.04 ?  137 ILE   A HB   1 
ATOM   3112 H HG12 A ILE   A 1 137 ? 7.916  -10.174 -3.307  0.48 19.37 ?  137 ILE   A HG12 1 
ATOM   3113 H HG12 B ILE   A 1 137 ? 7.890  -9.528  -3.770  0.52 22.21 ?  137 ILE   A HG12 1 
ATOM   3114 H HG13 A ILE   A 1 137 ? 8.304  -8.980  -4.278  0.48 19.37 ?  137 ILE   A HG13 1 
ATOM   3115 H HG13 B ILE   A 1 137 ? 8.521  -8.472  -4.772  0.52 22.21 ?  137 ILE   A HG13 1 
ATOM   3116 H HG21 A ILE   A 1 137 ? 8.180  -12.443 -5.156  0.48 18.76 ?  137 ILE   A HG21 1 
ATOM   3117 H HG21 B ILE   A 1 137 ? 8.024  -11.942 -5.294  0.52 21.56 ?  137 ILE   A HG21 1 
ATOM   3118 H HG22 A ILE   A 1 137 ? 9.728  -12.725 -5.053  0.48 18.76 ?  137 ILE   A HG22 1 
ATOM   3119 H HG22 B ILE   A 1 137 ? 9.533  -12.405 -5.145  0.52 21.56 ?  137 ILE   A HG22 1 
ATOM   3120 H HG23 A ILE   A 1 137 ? 8.881  -12.477 -3.733  0.48 18.76 ?  137 ILE   A HG23 1 
ATOM   3121 H HG23 B ILE   A 1 137 ? 8.708  -11.963 -3.862  0.52 21.56 ?  137 ILE   A HG23 1 
ATOM   3122 H HD11 A ILE   A 1 137 ? 6.084  -9.679  -4.532  0.48 20.42 ?  137 ILE   A HD11 1 
ATOM   3123 H HD11 B ILE   A 1 137 ? 6.736  -8.629  -5.910  0.52 23.10 ?  137 ILE   A HD11 1 
ATOM   3124 H HD12 A ILE   A 1 137 ? 6.896  -9.761  -5.895  0.48 20.42 ?  137 ILE   A HD12 1 
ATOM   3125 H HD12 B ILE   A 1 137 ? 7.216  -10.080 -6.338  0.52 23.10 ?  137 ILE   A HD12 1 
ATOM   3126 H HD13 A ILE   A 1 137 ? 6.592  -11.078 -5.058  0.48 20.42 ?  137 ILE   A HD13 1 
ATOM   3127 H HD13 B ILE   A 1 137 ? 6.253  -9.901  -5.087  0.52 23.10 ?  137 ILE   A HD13 1 
ATOM   3128 N N    A HIS   A 1 138 ? 12.365 -10.936 -5.502  0.48 13.94 ?  138 HIS   A N    1 
ATOM   3129 N N    B HIS   A 1 138 ? 12.388 -10.749 -5.560  0.52 16.50 ?  138 HIS   A N    1 
ATOM   3130 C CA   A HIS   A 1 138 ? 13.569 -11.656 -5.901  0.48 14.35 ?  138 HIS   A CA   1 
ATOM   3131 C CA   B HIS   A 1 138 ? 13.538 -11.557 -5.947  0.52 15.93 ?  138 HIS   A CA   1 
ATOM   3132 C C    A HIS   A 1 138 ? 14.691 -11.466 -4.887  0.48 13.91 ?  138 HIS   A C    1 
ATOM   3133 C C    B HIS   A 1 138 ? 14.669 -11.441 -4.929  0.52 14.80 ?  138 HIS   A C    1 
ATOM   3134 O O    A HIS   A 1 138 ? 15.366 -12.433 -4.511  0.48 13.93 ?  138 HIS   A O    1 
ATOM   3135 O O    B HIS   A 1 138 ? 15.321 -12.437 -4.591  0.52 14.97 ?  138 HIS   A O    1 
ATOM   3136 C CB   A HIS   A 1 138 ? 14.012 -11.217 -7.296  0.48 15.16 ?  138 HIS   A CB   1 
ATOM   3137 C CB   B HIS   A 1 138 ? 14.003 -11.121 -7.334  0.52 16.46 ?  138 HIS   A CB   1 
ATOM   3138 C CG   A HIS   A 1 138 ? 15.274 -11.876 -7.756  0.48 16.19 ?  138 HIS   A CG   1 
ATOM   3139 C CG   B HIS   A 1 138 ? 15.280 -11.762 -7.773  0.52 17.17 ?  138 HIS   A CG   1 
ATOM   3140 N ND1  A HIS   A 1 138 ? 15.366 -13.234 -7.979  0.48 17.02 ?  138 HIS   A ND1  1 
ATOM   3141 N ND1  B HIS   A 1 138 ? 15.376 -13.104 -8.071  0.52 17.86 ?  138 HIS   A ND1  1 
ATOM   3142 C CD2  A HIS   A 1 138 ? 16.501 -11.367 -8.021  0.48 16.68 ?  138 HIS   A CD2  1 
ATOM   3143 C CD2  B HIS   A 1 138 ? 16.516 -11.244 -7.964  0.52 17.40 ?  138 HIS   A CD2  1 
ATOM   3144 C CE1  A HIS   A 1 138 ? 16.593 -13.530 -8.370  0.48 17.42 ?  138 HIS   A CE1  1 
ATOM   3145 C CE1  B HIS   A 1 138 ? 16.616 -13.384 -8.429  0.52 18.02 ?  138 HIS   A CE1  1 
ATOM   3146 N NE2  A HIS   A 1 138 ? 17.302 -12.416 -8.401  0.48 17.00 ?  138 HIS   A NE2  1 
ATOM   3147 N NE2  B HIS   A 1 138 ? 17.329 -12.274 -8.370  0.52 17.58 ?  138 HIS   A NE2  1 
ATOM   3148 H H    A HIS   A 1 138 ? 12.120 -10.315 -6.051  0.48 16.71 ?  138 HIS   A H    1 
ATOM   3149 H H    B HIS   A 1 138 ? 12.204 -10.107 -6.105  0.52 19.78 ?  138 HIS   A H    1 
ATOM   3150 H HA   A HIS   A 1 138 ? 13.364 -12.602 -5.946  0.48 17.20 ?  138 HIS   A HA   1 
ATOM   3151 H HA   B HIS   A 1 138 ? 13.269 -12.486 -5.998  0.52 19.09 ?  138 HIS   A HA   1 
ATOM   3152 H HB2  A HIS   A 1 138 ? 13.313 -11.437 -7.935  0.48 18.16 ?  138 HIS   A HB2  1 
ATOM   3153 H HB2  B HIS   A 1 138 ? 13.314 -11.352 -7.981  0.52 19.73 ?  138 HIS   A HB2  1 
ATOM   3154 H HB3  A HIS   A 1 138 ? 14.163 -10.259 -7.294  0.48 18.16 ?  138 HIS   A HB3  1 
ATOM   3155 H HB3  B HIS   A 1 138 ? 14.137 -10.160 -7.333  0.52 19.73 ?  138 HIS   A HB3  1 
ATOM   3156 H HD1  A HIS   A 1 138 ? 14.723 -13.799 -7.885  0.48 20.41 ?  138 HIS   A HD1  1 
ATOM   3157 H HD2  A HIS   A 1 138 ? 16.751 -10.476 -7.960  0.48 19.99 ?  138 HIS   A HD2  1 
ATOM   3158 H HD2  B HIS   A 1 138 ? 16.764 -10.358 -7.843  0.52 20.86 ?  138 HIS   A HD2  1 
ATOM   3159 H HE1  A HIS   A 1 138 ? 16.904 -14.381 -8.584  0.48 20.88 ?  138 HIS   A HE1  1 
ATOM   3160 H HE1  B HIS   A 1 138 ? 16.930 -14.224 -8.678  0.52 21.60 ?  138 HIS   A HE1  1 
ATOM   3161 H HE2  B HIS   A 1 138 ? 18.162 -12.208 -8.559  0.52 21.08 ?  138 HIS   A HE2  1 
ATOM   3162 N N    . SER   A 1 139 ? 14.906 -10.232 -4.422  1.00 13.68 ?  139 SER   A N    1 
ATOM   3163 C CA   . SER   A 1 139 ? 15.973 -10.017 -3.453  1.00 13.33 ?  139 SER   A CA   1 
ATOM   3164 C C    . SER   A 1 139 ? 15.754 -10.844 -2.191  1.00 12.46 ?  139 SER   A C    1 
ATOM   3165 O O    . SER   A 1 139 ? 16.707 -11.418 -1.644  1.00 12.33 ?  139 SER   A O    1 
ATOM   3166 C CB   . SER   A 1 139 ? 16.085 -8.530  -3.120  1.00 13.22 ?  139 SER   A CB   1 
ATOM   3167 O OG   . SER   A 1 139 ? 17.164 -8.322  -2.230  1.00 13.20 ?  139 SER   A OG   1 
ATOM   3168 H H    A SER   A 1 139 ? 14.463 -9.530  -4.641  0.48 16.39 ?  139 SER   A H    1 
ATOM   3169 H H    B SER   A 1 139 ? 14.461 -9.525  -4.618  0.52 16.39 ?  139 SER   A H    1 
ATOM   3170 H HA   . SER   A 1 139 ? 16.817 -10.293 -3.842  1.00 15.97 ?  139 SER   A HA   1 
ATOM   3171 H HB2  . SER   A 1 139 ? 16.246 -8.025  -3.933  1.00 15.84 ?  139 SER   A HB2  1 
ATOM   3172 H HB3  . SER   A 1 139 ? 15.265 -8.228  -2.696  1.00 15.84 ?  139 SER   A HB3  1 
ATOM   3173 H HG   . SER   A 1 139 ? 17.235 -7.497  -2.037  1.00 15.82 ?  139 SER   A HG   1 
ATOM   3174 N N    . LEU   A 1 140 ? 14.510 -10.916 -1.713  1.00 12.32 ?  140 LEU   A N    1 
ATOM   3175 C CA   . LEU   A 1 140 ? 14.237 -11.726 -0.531  1.00 12.14 ?  140 LEU   A CA   1 
ATOM   3176 C C    . LEU   A 1 140 ? 14.514 -13.199 -0.801  1.00 12.00 ?  140 LEU   A C    1 
ATOM   3177 O O    . LEU   A 1 140 ? 15.078 -13.900 0.049   1.00 12.47 ?  140 LEU   A O    1 
ATOM   3178 C CB   . LEU   A 1 140 ? 12.792 -11.520 -0.084  1.00 12.33 ?  140 LEU   A CB   1 
ATOM   3179 C CG   . LEU   A 1 140 ? 12.333 -12.373 1.096   1.00 12.77 ?  140 LEU   A CG   1 
ATOM   3180 C CD1  . LEU   A 1 140 ? 13.215 -12.159 2.311   1.00 13.32 ?  140 LEU   A CD1  1 
ATOM   3181 C CD2  . LEU   A 1 140 ? 10.871 -12.074 1.435   1.00 13.72 ?  140 LEU   A CD2  1 
ATOM   3182 H H    . LEU   A 1 140 ? 13.827 -10.513 -2.044  1.00 14.76 ?  140 LEU   A H    1 
ATOM   3183 H HA   . LEU   A 1 140 ? 14.813 -11.440 0.192   1.00 14.54 ?  140 LEU   A HA   1 
ATOM   3184 H HB2  . LEU   A 1 140 ? 12.675 -10.596 0.171   1.00 14.78 ?  140 LEU   A HB2  1 
ATOM   3185 H HB3  . LEU   A 1 140 ? 12.206 -11.728 -0.830  1.00 14.78 ?  140 LEU   A HB3  1 
ATOM   3186 H HG   . LEU   A 1 140 ? 12.385 -13.314 0.852   1.00 15.30 ?  140 LEU   A HG   1 
ATOM   3187 H HD11 . LEU   A 1 140 ? 12.831 -12.632 3.068   1.00 15.96 ?  140 LEU   A HD11 1 
ATOM   3188 H HD12 . LEU   A 1 140 ? 14.100 -12.511 2.122   1.00 15.96 ?  140 LEU   A HD12 1 
ATOM   3189 H HD13 . LEU   A 1 140 ? 13.265 -11.213 2.501   1.00 15.96 ?  140 LEU   A HD13 1 
ATOM   3190 H HD21 . LEU   A 1 140 ? 10.597 -12.631 2.188   1.00 16.44 ?  140 LEU   A HD21 1 
ATOM   3191 H HD22 . LEU   A 1 140 ? 10.783 -11.140 1.671   1.00 16.44 ?  140 LEU   A HD22 1 
ATOM   3192 H HD23 . LEU   A 1 140 ? 10.315 -12.277 0.665   1.00 16.44 ?  140 LEU   A HD23 1 
ATOM   3193 N N    . ARG   A 1 141 ? 14.125 -13.687 -1.983  1.00 12.46 ?  141 ARG   A N    1 
ATOM   3194 C CA   . ARG   A 1 141 ? 14.375 -15.081 -2.335  1.00 13.67 ?  141 ARG   A CA   1 
ATOM   3195 C C    . ARG   A 1 141 ? 15.869 -15.380 -2.335  1.00 12.99 ?  141 ARG   A C    1 
ATOM   3196 O O    . ARG   A 1 141 ? 16.312 -16.392 -1.775  1.00 13.22 ?  141 ARG   A O    1 
ATOM   3197 C CB   . ARG   A 1 141 ? 13.760 -15.371 -3.707  1.00 15.88 ?  141 ARG   A CB   1 
ATOM   3198 C CG   . ARG   A 1 141 ? 13.780 -16.827 -4.141  1.00 18.85 ?  141 ARG   A CG   1 
ATOM   3199 C CD   . ARG   A 1 141 ? 12.755 -17.612 -3.380  1.00 21.44 ?  141 ARG   A CD   1 
ATOM   3200 N NE   . ARG   A 1 141 ? 13.364 -18.397 -2.320  1.00 22.47 ?  141 ARG   A NE   1 
ATOM   3201 C CZ   . ARG   A 1 141 ? 12.680 -18.974 -1.340  1.00 23.34 ?  141 ARG   A CZ   1 
ATOM   3202 N NH1  . ARG   A 1 141 ? 11.383 -18.762 -1.182  1.00 22.91 ?  141 ARG   A NH1  1 
ATOM   3203 N NH2  . ARG   A 1 141 ? 13.317 -19.773 -0.489  1.00 24.36 ?  141 ARG   A NH2  1 
ATOM   3204 H H    . ARG   A 1 141 ? 13.720 -13.236 -2.591  1.00 14.93 ?  141 ARG   A H    1 
ATOM   3205 H HA   . ARG   A 1 141 ? 13.954 -15.660 -1.684  1.00 16.38 ?  141 ARG   A HA   1 
ATOM   3206 H HB2  . ARG   A 1 141 ? 12.835 -15.082 -3.700  1.00 19.03 ?  141 ARG   A HB2  1 
ATOM   3207 H HB3  . ARG   A 1 141 ? 14.249 -14.871 -4.376  1.00 19.03 ?  141 ARG   A HB3  1 
ATOM   3208 H HG2  . ARG   A 1 141 ? 13.571 -16.891 -5.089  1.00 22.60 ?  141 ARG   A HG2  1 
ATOM   3209 H HG3  . ARG   A 1 141 ? 14.653 -17.215 -3.965  1.00 22.60 ?  141 ARG   A HG3  1 
ATOM   3210 H HD2  . ARG   A 1 141 ? 12.119 -17.003 -2.970  1.00 25.71 ?  141 ARG   A HD2  1 
ATOM   3211 H HD3  . ARG   A 1 141 ? 12.289 -18.213 -3.988  1.00 25.71 ?  141 ARG   A HD3  1 
ATOM   3212 H HE   . ARG   A 1 141 ? 14.194 -18.599 -2.398  1.00 26.94 ?  141 ARG   A HE   1 
ATOM   3213 H HH11 . ARG   A 1 141 ? 10.955 -18.258 -1.730  1.00 27.47 ?  141 ARG   A HH11 1 
ATOM   3214 H HH12 . ARG   A 1 141 ? 10.960 -19.144 -0.535  1.00 27.47 ?  141 ARG   A HH12 1 
ATOM   3215 H HH21 . ARG   A 1 141 ? 14.158 -19.918 -0.582  1.00 29.21 ?  141 ARG   A HH21 1 
ATOM   3216 H HH22 . ARG   A 1 141 ? 12.886 -20.144 0.158   1.00 29.21 ?  141 ARG   A HH22 1 
ATOM   3217 N N    . VAL   A 1 142 ? 16.664 -14.513 -2.965  1.00 12.38 ?  142 VAL   A N    1 
ATOM   3218 C CA   . VAL   A 1 142 ? 18.108 -14.726 -2.990  1.00 12.27 ?  142 VAL   A CA   1 
ATOM   3219 C C    . VAL   A 1 142 ? 18.674 -14.698 -1.579  1.00 11.67 ?  142 VAL   A C    1 
ATOM   3220 O O    . VAL   A 1 142 ? 19.538 -15.508 -1.225  1.00 12.20 ?  142 VAL   A O    1 
ATOM   3221 C CB   . VAL   A 1 142 ? 18.801 -13.708 -3.913  1.00 13.05 ?  142 VAL   A CB   1 
ATOM   3222 C CG1  . VAL   A 1 142 ? 20.312 -13.920 -3.887  1.00 12.81 ?  142 VAL   A CG1  1 
ATOM   3223 C CG2  . VAL   A 1 142 ? 18.290 -13.834 -5.335  1.00 14.27 ?  142 VAL   A CG2  1 
ATOM   3224 H H    . VAL   A 1 142 ? 16.402 -13.804 -3.377  1.00 14.84 ?  142 VAL   A H    1 
ATOM   3225 H HA   . VAL   A 1 142 ? 18.287 -15.603 -3.355  1.00 14.70 ?  142 VAL   A HA   1 
ATOM   3226 H HB   . VAL   A 1 142 ? 18.621 -12.803 -3.601  1.00 15.64 ?  142 VAL   A HB   1 
ATOM   3227 H HG11 . VAL   A 1 142 ? 20.716 -13.427 -4.621  1.00 15.35 ?  142 VAL   A HG11 1 
ATOM   3228 H HG12 . VAL   A 1 142 ? 20.668 -13.595 -3.043  1.00 15.35 ?  142 VAL   A HG12 1 
ATOM   3229 H HG13 . VAL   A 1 142 ? 20.500 -14.865 -3.985  1.00 15.35 ?  142 VAL   A HG13 1 
ATOM   3230 H HG21 . VAL   A 1 142 ? 18.748 -13.185 -5.894  1.00 17.10 ?  142 VAL   A HG21 1 
ATOM   3231 H HG22 . VAL   A 1 142 ? 18.470 -14.731 -5.652  1.00 17.10 ?  142 VAL   A HG22 1 
ATOM   3232 H HG23 . VAL   A 1 142 ? 17.338 -13.662 -5.341  1.00 17.10 ?  142 VAL   A HG23 1 
ATOM   3233 N N    . CYS   A 1 143 ? 18.205 -13.761 -0.755  1.00 11.59 ?  143 CYS   A N    1 
ATOM   3234 C CA   . CYS   A 1 143 ? 18.664 -13.701 0.627   1.00 11.92 ?  143 CYS   A CA   1 
ATOM   3235 C C    . CYS   A 1 143 ? 18.430 -15.035 1.329   1.00 11.71 ?  143 CYS   A C    1 
ATOM   3236 O O    . CYS   A 1 143 ? 19.344 -15.618 1.920   1.00 11.71 ?  143 CYS   A O    1 
ATOM   3237 C CB   . CYS   A 1 143 ? 17.932 -12.575 1.354   1.00 12.32 ?  143 CYS   A CB   1 
ATOM   3238 S SG   . CYS   A 1 143 ? 18.429 -12.372 3.076   1.00 12.59 ?  143 CYS   A SG   1 
ATOM   3239 H H    . CYS   A 1 143 ? 17.622 -13.168 -0.965  1.00 13.88 ?  143 CYS   A H    1 
ATOM   3240 H HA   . CYS   A 1 143 ? 19.613 -13.517 0.644   1.00 14.29 ?  143 CYS   A HA   1 
ATOM   3241 H HB2  . CYS   A 1 143 ? 18.106 -11.745 0.892   1.00 14.76 ?  143 CYS   A HB2  1 
ATOM   3242 H HB3  . CYS   A 1 143 ? 16.982 -12.766 1.342   1.00 14.76 ?  143 CYS   A HB3  1 
ATOM   3243 H HG   . CYS   A 1 143 ? 17.830 -11.440 3.540   1.00 15.09 ?  143 CYS   A HG   1 
ATOM   3244 N N    . VAL   A 1 144 ? 17.196 -15.536 1.267   1.00 12.21 ?  144 VAL   A N    1 
ATOM   3245 C CA   . VAL   A 1 144 ? 16.843 -16.768 1.965   1.00 13.21 ?  144 VAL   A CA   1 
ATOM   3246 C C    . VAL   A 1 144 ? 17.672 -17.937 1.462   1.00 12.95 ?  144 VAL   A C    1 
ATOM   3247 O O    . VAL   A 1 144 ? 18.039 -18.833 2.233   1.00 13.97 ?  144 VAL   A O    1 
ATOM   3248 C CB   . VAL   A 1 144 ? 15.332 -17.016 1.801   1.00 15.30 ?  144 VAL   A CB   1 
ATOM   3249 C CG1  . VAL   A 1 144 ? 14.969 -18.460 2.107   1.00 16.63 ?  144 VAL   A CG1  1 
ATOM   3250 C CG2  . VAL   A 1 144 ? 14.547 -16.033 2.672   1.00 15.46 ?  144 VAL   A CG2  1 
ATOM   3251 H H    . VAL   A 1 144 ? 16.545 -15.181 0.826   1.00 14.62 ?  144 VAL   A H    1 
ATOM   3252 H HA   . VAL   A 1 144 ? 17.020 -16.660 2.908   1.00 15.83 ?  144 VAL   A HA   1 
ATOM   3253 H HB   . VAL   A 1 144 ? 15.081 -16.844 0.877   1.00 18.34 ?  144 VAL   A HB   1 
ATOM   3254 H HG11 . VAL   A 1 144 ? 14.010 -18.518 2.266   1.00 19.93 ?  144 VAL   A HG11 1 
ATOM   3255 H HG12 . VAL   A 1 144 ? 15.206 -19.015 1.348   1.00 19.93 ?  144 VAL   A HG12 1 
ATOM   3256 H HG13 . VAL   A 1 144 ? 15.449 -18.744 2.897   1.00 19.93 ?  144 VAL   A HG13 1 
ATOM   3257 H HG21 . VAL   A 1 144 ? 13.603 -16.270 2.662   1.00 18.53 ?  144 VAL   A HG21 1 
ATOM   3258 H HG22 . VAL   A 1 144 ? 14.882 -16.069 3.580   1.00 18.53 ?  144 VAL   A HG22 1 
ATOM   3259 H HG23 . VAL   A 1 144 ? 14.657 -15.132 2.318   1.00 18.53 ?  144 VAL   A HG23 1 
ATOM   3260 N N    . ASP   A 1 145 ? 17.954 -17.969 0.162   1.00 13.67 ?  145 ASP   A N    1 
ATOM   3261 C CA   . ASP   A 1 145 ? 18.668 -19.084 -0.450  1.00 14.47 ?  145 ASP   A CA   1 
ATOM   3262 C C    . ASP   A 1 145 ? 20.186 -18.933 -0.399  1.00 13.97 ?  145 ASP   A C    1 
ATOM   3263 O O    . ASP   A 1 145 ? 20.895 -19.832 -0.867  1.00 16.03 ?  145 ASP   A O    1 
ATOM   3264 C CB   . ASP   A 1 145 ? 18.229 -19.247 -1.908  1.00 16.12 ?  145 ASP   A CB   1 
ATOM   3265 C CG   . ASP   A 1 145 ? 16.789 -19.702 -2.041  1.00 18.38 ?  145 ASP   A CG   1 
ATOM   3266 O OD1  . ASP   A 1 145 ? 16.224 -20.245 -1.063  1.00 19.07 ?  145 ASP   A OD1  1 
ATOM   3267 O OD2  . ASP   A 1 145 ? 16.223 -19.512 -3.136  1.00 19.90 -1 145 ASP   A OD2  1 
ATOM   3268 H H    . ASP   A 1 145 ? 17.718 -17.359 -0.398  1.00 16.38 ?  145 ASP   A H    1 
ATOM   3269 H HA   . ASP   A 1 145 ? 18.433 -19.902 0.016   1.00 17.34 ?  145 ASP   A HA   1 
ATOM   3270 H HB2  . ASP   A 1 145 ? 18.324 -18.397 -2.367  1.00 19.33 ?  145 ASP   A HB2  1 
ATOM   3271 H HB3  . ASP   A 1 145 ? 18.788 -19.917 -2.335  1.00 19.33 ?  145 ASP   A HB3  1 
ATOM   3272 N N    . THR   A 1 146 ? 20.702 -17.834 0.152   1.00 12.50 ?  146 THR   A N    1 
ATOM   3273 C CA   . THR   A 1 146 ? 22.140 -17.571 0.179   1.00 11.75 ?  146 THR   A CA   1 
ATOM   3274 C C    . THR   A 1 146 ? 22.682 -17.385 1.585   1.00 11.58 ?  146 THR   A C    1 
ATOM   3275 O O    . THR   A 1 146 ? 23.758 -17.911 1.908   1.00 12.81 ?  146 THR   A O    1 
ATOM   3276 C CB   . THR   A 1 146 ? 22.462 -16.320 -0.657  1.00 11.67 ?  146 THR   A CB   1 
ATOM   3277 O OG1  . THR   A 1 146 ? 21.946 -16.489 -1.976  1.00 12.24 ?  146 THR   A OG1  1 
ATOM   3278 C CG2  . THR   A 1 146 ? 23.959 -16.093 -0.742  1.00 12.07 ?  146 THR   A CG2  1 
ATOM   3279 H H    . THR   A 1 146 ? 20.227 -17.209 0.509   1.00 14.98 ?  146 THR   A H    1 
ATOM   3280 H HA   . THR   A 1 146 ? 22.605 -18.317 -0.217  1.00 14.07 ?  146 THR   A HA   1 
ATOM   3281 H HB   . THR   A 1 146 ? 22.060 -15.536 -0.248  1.00 13.98 ?  146 THR   A HB   1 
ATOM   3282 H HG1  . THR   A 1 146 ? 21.109 -16.565 -1.946  1.00 14.66 ?  146 THR   A HG1  1 
ATOM   3283 H HG21 . THR   A 1 146 ? 24.154 -15.428 -1.421  1.00 14.46 ?  146 THR   A HG21 1 
ATOM   3284 H HG22 . THR   A 1 146 ? 24.298 -15.779 0.111   1.00 14.46 ?  146 THR   A HG22 1 
ATOM   3285 H HG23 . THR   A 1 146 ? 24.405 -16.921 -0.976  1.00 14.46 ?  146 THR   A HG23 1 
ATOM   3286 N N    . VAL   A 1 147 ? 21.998 -16.606 2.415   1.00 11.54 ?  147 VAL   A N    1 
ATOM   3287 C CA   . VAL   A 1 147 ? 22.478 -16.307 3.755   1.00 11.58 ?  147 VAL   A CA   1 
ATOM   3288 C C    . VAL   A 1 147 ? 22.153 -17.482 4.667   1.00 11.87 ?  147 VAL   A C    1 
ATOM   3289 O O    . VAL   A 1 147 ? 21.010 -17.961 4.702   1.00 12.55 ?  147 VAL   A O    1 
ATOM   3290 C CB   . VAL   A 1 147 ? 21.850 -15.003 4.269   1.00 11.90 ?  147 VAL   A CB   1 
ATOM   3291 C CG1  . VAL   A 1 147 ? 22.363 -14.681 5.654   1.00 12.92 ?  147 VAL   A CG1  1 
ATOM   3292 C CG2  . VAL   A 1 147 ? 22.127 -13.849 3.298   1.00 11.72 ?  147 VAL   A CG2  1 
ATOM   3293 H H    . VAL   A 1 147 ? 21.240 -16.242 2.229   1.00 13.82 ?  147 VAL   A H    1 
ATOM   3294 H HA   . VAL   A 1 147 ? 23.439 -16.196 3.735   1.00 13.87 ?  147 VAL   A HA   1 
ATOM   3295 H HB   . VAL   A 1 147 ? 20.890 -15.120 4.331   1.00 14.26 ?  147 VAL   A HB   1 
ATOM   3296 H HG11 . VAL   A 1 147 ? 22.098 -13.780 5.884   1.00 15.48 ?  147 VAL   A HG11 1 
ATOM   3297 H HG12 . VAL   A 1 147 ? 21.980 -15.311 6.287   1.00 15.48 ?  147 VAL   A HG12 1 
ATOM   3298 H HG13 . VAL   A 1 147 ? 23.329 -14.756 5.656   1.00 15.48 ?  147 VAL   A HG13 1 
ATOM   3299 H HG21 . VAL   A 1 147 ? 21.788 -13.029 3.689   1.00 14.03 ?  147 VAL   A HG21 1 
ATOM   3300 H HG22 . VAL   A 1 147 ? 23.077 -13.787 3.150   1.00 14.03 ?  147 VAL   A HG22 1 
ATOM   3301 H HG23 . VAL   A 1 147 ? 21.666 -14.033 2.463   1.00 14.03 ?  147 VAL   A HG23 1 
ATOM   3302 N N    . ARG   A 1 148 ? 23.164 -17.943 5.405   1.00 11.87 ?  148 ARG   A N    1 
ATOM   3303 C CA   . ARG   A 1 148 ? 23.030 -19.023 6.369   1.00 12.31 ?  148 ARG   A CA   1 
ATOM   3304 C C    . ARG   A 1 148 ? 23.147 -18.553 7.806   1.00 12.65 ?  148 ARG   A C    1 
ATOM   3305 O O    . ARG   A 1 148 ? 22.730 -19.281 8.718   1.00 14.05 ?  148 ARG   A O    1 
ATOM   3306 C CB   . ARG   A 1 148 ? 24.074 -20.116 6.098   1.00 12.90 ?  148 ARG   A CB   1 
ATOM   3307 C CG   . ARG   A 1 148 ? 23.919 -20.756 4.733   1.00 14.25 ?  148 ARG   A CG   1 
ATOM   3308 C CD   . ARG   A 1 148 ? 25.012 -21.787 4.448   1.00 15.34 ?  148 ARG   A CD   1 
ATOM   3309 N NE   . ARG   A 1 148 ? 26.350 -21.206 4.468   1.00 15.18 ?  148 ARG   A NE   1 
ATOM   3310 C CZ   . ARG   A 1 148 ? 26.864 -20.483 3.482   1.00 14.36 ?  148 ARG   A CZ   1 
ATOM   3311 N NH1  . ARG   A 1 148 ? 26.184 -20.243 2.372   1.00 14.63 ?  148 ARG   A NH1  1 
ATOM   3312 N NH2  . ARG   A 1 148 ? 28.082 -19.964 3.623   1.00 14.80 ?  148 ARG   A NH2  1 
ATOM   3313 H H    . ARG   A 1 148 ? 23.967 -17.633 5.347   1.00 14.22 ?  148 ARG   A H    1 
ATOM   3314 H HA   . ARG   A 1 148 ? 22.156 -19.420 6.266   1.00 14.75 ?  148 ARG   A HA   1 
ATOM   3315 H HB2  . ARG   A 1 148 ? 24.959 -19.734 6.148   1.00 15.45 ?  148 ARG   A HB2  1 
ATOM   3316 H HB3  . ARG   A 1 148 ? 23.973 -20.818 6.761   1.00 15.45 ?  148 ARG   A HB3  1 
ATOM   3317 H HG2  . ARG   A 1 148 ? 23.058 -21.198 4.688   1.00 17.07 ?  148 ARG   A HG2  1 
ATOM   3318 H HG3  . ARG   A 1 148 ? 23.970 -20.059 4.056   1.00 17.07 ?  148 ARG   A HG3  1 
ATOM   3319 H HD2  . ARG   A 1 148 ? 24.975 -22.476 5.126   1.00 18.38 ?  148 ARG   A HD2  1 
ATOM   3320 H HD3  . ARG   A 1 148 ? 24.858 -22.169 3.571   1.00 18.38 ?  148 ARG   A HD3  1 
ATOM   3321 H HE   . ARG   A 1 148 ? 26.837 -21.341 5.158   1.00 18.19 ?  148 ARG   A HE   1 
ATOM   3322 H HH11 . ARG   A 1 148 ? 25.394 -20.555 2.270   1.00 17.53 ?  148 ARG   A HH11 1 
ATOM   3323 H HH12 . ARG   A 1 148 ? 26.539 -19.759 1.748   1.00 17.53 ?  148 ARG   A HH12 1 
ATOM   3324 H HH21 . ARG   A 1 148 ? 28.531 -20.112 4.339   1.00 17.73 ?  148 ARG   A HH21 1 
ATOM   3325 H HH22 . ARG   A 1 148 ? 28.427 -19.491 2.990   1.00 17.73 ?  148 ARG   A HH22 1 
ATOM   3326 N N    . THR   A 1 149 ? 23.696 -17.363 8.022   1.00 12.35 ?  149 THR   A N    1 
ATOM   3327 C CA   . THR   A 1 149 ? 23.767 -16.765 9.338   1.00 12.52 ?  149 THR   A CA   1 
ATOM   3328 C C    . THR   A 1 149 ? 22.437 -16.073 9.634   1.00 12.17 ?  149 THR   A C    1 
ATOM   3329 O O    . THR   A 1 149 ? 21.506 -16.073 8.815   1.00 12.93 ?  149 THR   A O    1 
ATOM   3330 C CB   . THR   A 1 149 ? 24.966 -15.823 9.398   1.00 13.02 ?  149 THR   A CB   1 
ATOM   3331 O OG1  . THR   A 1 149 ? 24.840 -14.890 8.322   1.00 13.05 ?  149 THR   A OG1  1 
ATOM   3332 C CG2  . THR   A 1 149 ? 26.284 -16.610 9.286   1.00 13.35 ?  149 THR   A CG2  1 
ATOM   3333 H H    . THR   A 1 149 ? 24.049 -16.868 7.403   1.00 14.79 ?  149 THR   A H    1 
ATOM   3334 H HA   . THR   A 1 149 ? 23.897 -17.469 9.994   1.00 14.99 ?  149 THR   A HA   1 
ATOM   3335 H HB   . THR   A 1 149 ? 24.953 -15.347 10.240  1.00 15.61 ?  149 THR   A HB   1 
ATOM   3336 H HG1  . THR   A 1 149 ? 25.487 -14.363 8.320   1.00 15.63 ?  149 THR   A HG1  1 
ATOM   3337 H HG21 . THR   A 1 149 ? 27.036 -16.002 9.339   1.00 16.00 ?  149 THR   A HG21 1 
ATOM   3338 H HG22 . THR   A 1 149 ? 26.349 -17.257 10.007  1.00 16.00 ?  149 THR   A HG22 1 
ATOM   3339 H HG23 . THR   A 1 149 ? 26.320 -17.083 8.438   1.00 16.00 ?  149 THR   A HG23 1 
ATOM   3340 N N    . ASN   A 1 150 ? 22.304 -15.538 10.840  1.00 12.53 ?  150 ASN   A N    1 
ATOM   3341 C CA   . ASN   A 1 150 ? 21.016 -15.026 11.306  1.00 12.87 ?  150 ASN   A CA   1 
ATOM   3342 C C    . ASN   A 1 150 ? 20.842 -13.589 10.839  1.00 12.06 ?  150 ASN   A C    1 
ATOM   3343 O O    . ASN   A 1 150 ? 21.584 -12.697 11.259  1.00 13.33 ?  150 ASN   A O    1 
ATOM   3344 C CB   . ASN   A 1 150 ? 20.932 -15.135 12.822  1.00 15.36 ?  150 ASN   A CB   1 
ATOM   3345 C CG   . ASN   A 1 150 ? 20.832 -16.568 13.281  1.00 19.27 ?  150 ASN   A CG   1 
ATOM   3346 O OD1  . ASN   A 1 150 ? 20.247 -17.404 12.594  1.00 20.42 ?  150 ASN   A OD1  1 
ATOM   3347 N ND2  . ASN   A 1 150 ? 21.419 -16.871 14.437  1.00 21.62 ?  150 ASN   A ND2  1 
ATOM   3348 H H    . ASN   A 1 150 ? 22.940 -15.467 11.414  1.00 15.01 ?  150 ASN   A H    1 
ATOM   3349 H HA   . ASN   A 1 150 ? 20.299 -15.564 10.926  1.00 15.42 ?  150 ASN   A HA   1 
ATOM   3350 H HB2  . ASN   A 1 150 ? 21.725 -14.751 13.217  1.00 18.41 ?  150 ASN   A HB2  1 
ATOM   3351 H HB3  . ASN   A 1 150 ? 20.139 -14.672 13.134  1.00 18.41 ?  150 ASN   A HB3  1 
ATOM   3352 H HD21 . ASN   A 1 150 ? 21.395 -17.679 14.745  1.00 25.92 ?  150 ASN   A HD21 1 
ATOM   3353 H HD22 . ASN   A 1 150 ? 21.822 -16.260 14.890  1.00 25.92 ?  150 ASN   A HD22 1 
ATOM   3354 N N    . VAL   A 1 151 ? 19.861 -13.360 9.975   1.00 11.84 ?  151 VAL   A N    1 
ATOM   3355 C CA   . VAL   A 1 151 ? 19.653 -12.058 9.366   1.00 11.84 ?  151 VAL   A CA   1 
ATOM   3356 C C    . VAL   A 1 151 ? 18.255 -11.554 9.708   1.00 11.50 ?  151 VAL   A C    1 
ATOM   3357 O O    . VAL   A 1 151 ? 17.252 -12.270 9.550   1.00 12.98 ?  151 VAL   A O    1 
ATOM   3358 C CB   . VAL   A 1 151 ? 19.966 -12.065 7.855   1.00 12.66 ?  151 VAL   A CB   1 
ATOM   3359 C CG1  . VAL   A 1 151 ? 19.149 -13.098 7.105   1.00 14.01 ?  151 VAL   A CG1  1 
ATOM   3360 C CG2  . VAL   A 1 151 ? 19.791 -10.665 7.266   1.00 13.20 ?  151 VAL   A CG2  1 
ATOM   3361 H H    . VAL   A 1 151 ? 19.297 -13.957 9.720   1.00 14.19 ?  151 VAL   A H    1 
ATOM   3362 H HA   . VAL   A 1 151 ? 20.286 -11.439 9.768   1.00 14.18 ?  151 VAL   A HA   1 
ATOM   3363 H HB   . VAL   A 1 151 ? 20.902 -12.302 7.736   1.00 15.17 ?  151 VAL   A HB   1 
ATOM   3364 H HG11 . VAL   A 1 151 ? 19.365 -13.057 6.159   1.00 16.79 ?  151 VAL   A HG11 1 
ATOM   3365 H HG12 . VAL   A 1 151 ? 19.366 -13.985 7.448   1.00 16.79 ?  151 VAL   A HG12 1 
ATOM   3366 H HG13 . VAL   A 1 151 ? 18.206 -12.920 7.237   1.00 16.79 ?  151 VAL   A HG13 1 
ATOM   3367 H HG21 . VAL   A 1 151 ? 20.115 -10.664 6.348   1.00 15.81 ?  151 VAL   A HG21 1 
ATOM   3368 H HG22 . VAL   A 1 151 ? 18.850 -10.430 7.278   1.00 15.81 ?  151 VAL   A HG22 1 
ATOM   3369 H HG23 . VAL   A 1 151 ? 20.300 -10.031 7.792   1.00 15.81 ?  151 VAL   A HG23 1 
ATOM   3370 N N    . TYR   A 1 152 ? 18.223 -10.315 10.197  1.00 11.58 ?  152 TYR   A N    1 
ATOM   3371 C CA   . TYR   A 1 152 ? 17.023 -9.585  10.567  1.00 11.14 ?  152 TYR   A CA   1 
ATOM   3372 C C    . TYR   A 1 152 ? 16.829 -8.488  9.531   1.00 10.73 ?  152 TYR   A C    1 
ATOM   3373 O O    . TYR   A 1 152 ? 17.603 -7.523  9.484   1.00 11.01 ?  152 TYR   A O    1 
ATOM   3374 C CB   . TYR   A 1 152 ? 17.195 -9.026  11.975  1.00 12.16 ?  152 TYR   A CB   1 
ATOM   3375 C CG   . TYR   A 1 152 ? 17.145 -10.137 12.990  1.00 12.75 ?  152 TYR   A CG   1 
ATOM   3376 C CD1  . TYR   A 1 152 ? 18.265 -10.911 13.269  1.00 14.45 ?  152 TYR   A CD1  1 
ATOM   3377 C CD2  . TYR   A 1 152 ? 15.961 -10.454 13.636  1.00 13.16 ?  152 TYR   A CD2  1 
ATOM   3378 C CE1  . TYR   A 1 152 ? 18.212 -11.956 14.175  1.00 15.96 ?  152 TYR   A CE1  1 
ATOM   3379 C CE2  . TYR   A 1 152 ? 15.895 -11.499 14.544  1.00 14.84 ?  152 TYR   A CE2  1 
ATOM   3380 C CZ   . TYR   A 1 152 ? 17.023 -12.245 14.811  1.00 16.09 ?  152 TYR   A CZ   1 
ATOM   3381 O OH   . TYR   A 1 152 ? 16.969 -13.290 15.708  1.00 18.65 ?  152 TYR   A OH   1 
ATOM   3382 H H    . TYR   A 1 152 ? 18.945 -9.844  10.317  1.00 13.88 ?  152 TYR   A H    1 
ATOM   3383 H HA   . TYR   A 1 152 ? 16.262 -10.182 10.549  1.00 13.34 ?  152 TYR   A HA   1 
ATOM   3384 H HB2  . TYR   A 1 152 ? 18.060 -8.591  12.044  1.00 14.57 ?  152 TYR   A HB2  1 
ATOM   3385 H HB3  . TYR   A 1 152 ? 16.484 -8.403  12.164  1.00 14.57 ?  152 TYR   A HB3  1 
ATOM   3386 H HD1  . TYR   A 1 152 ? 19.067 -10.722 12.835  1.00 17.32 ?  152 TYR   A HD1  1 
ATOM   3387 H HD2  . TYR   A 1 152 ? 15.194 -9.957  13.454  1.00 15.76 ?  152 TYR   A HD2  1 
ATOM   3388 H HE1  . TYR   A 1 152 ? 18.975 -12.458 14.353  1.00 19.13 ?  152 TYR   A HE1  1 
ATOM   3389 H HE2  . TYR   A 1 152 ? 15.094 -11.694 14.976  1.00 17.78 ?  152 TYR   A HE2  1 
ATOM   3390 H HH   . TYR   A 1 152 ? 16.195 -13.347 16.033  1.00 22.36 ?  152 TYR   A HH   1 
ATOM   3391 N N    . LEU   A 1 153 ? 15.826 -8.660  8.675   1.00 11.12 ?  153 LEU   A N    1 
ATOM   3392 C CA   . LEU   A 1 153 ? 15.568 -7.765  7.559   1.00 10.98 ?  153 LEU   A CA   1 
ATOM   3393 C C    . LEU   A 1 153 ? 14.560 -6.699  7.956   1.00 11.36 ?  153 LEU   A C    1 
ATOM   3394 O O    . LEU   A 1 153 ? 13.448 -7.013  8.404   1.00 12.61 ?  153 LEU   A O    1 
ATOM   3395 C CB   . LEU   A 1 153 ? 15.013 -8.552  6.371   1.00 11.17 ?  153 LEU   A CB   1 
ATOM   3396 C CG   . LEU   A 1 153 ? 15.974 -9.549  5.726   1.00 11.47 ?  153 LEU   A CG   1 
ATOM   3397 C CD1  . LEU   A 1 153 ? 15.215 -10.448 4.761   1.00 12.05 ?  153 LEU   A CD1  1 
ATOM   3398 C CD2  . LEU   A 1 153 ? 17.104 -8.816  5.014   1.00 12.68 ?  153 LEU   A CD2  1 
ATOM   3399 H H    . LEU   A 1 153 ? 15.259 -9.316  8.724   1.00 13.32 ?  153 LEU   A H    1 
ATOM   3400 H HA   . LEU   A 1 153 ? 16.392 -7.337  7.299   1.00 13.15 ?  153 LEU   A HA   1 
ATOM   3401 H HB2  . LEU   A 1 153 ? 14.232 -9.040  6.670   1.00 13.38 ?  153 LEU   A HB2  1 
ATOM   3402 H HB3  . LEU   A 1 153 ? 14.749 -7.911  5.688   1.00 13.38 ?  153 LEU   A HB3  1 
ATOM   3403 H HG   . LEU   A 1 153 ? 16.365 -10.103 6.421   1.00 13.74 ?  153 LEU   A HG   1 
ATOM   3404 H HD11 . LEU   A 1 153 ? 15.811 -11.145 4.447   1.00 14.43 ?  153 LEU   A HD11 1 
ATOM   3405 H HD12 . LEU   A 1 153 ? 14.459 -10.838 5.221   1.00 14.43 ?  153 LEU   A HD12 1 
ATOM   3406 H HD13 . LEU   A 1 153 ? 14.908 -9.913  4.011   1.00 14.43 ?  153 LEU   A HD13 1 
ATOM   3407 H HD21 . LEU   A 1 153 ? 17.673 -9.468  4.586   1.00 15.19 ?  153 LEU   A HD21 1 
ATOM   3408 H HD22 . LEU   A 1 153 ? 16.717 -8.221  4.354   1.00 15.19 ?  153 LEU   A HD22 1 
ATOM   3409 H HD23 . LEU   A 1 153 ? 17.608 -8.307  5.666   1.00 15.19 ?  153 LEU   A HD23 1 
ATOM   3410 N N    . ALA   A 1 154 ? 14.945 -5.440  7.765   1.00 11.32 ?  154 ALA   A N    1 
ATOM   3411 C CA   . ALA   A 1 154 ? 14.075 -4.296  7.985   1.00 12.03 ?  154 ALA   A CA   1 
ATOM   3412 C C    . ALA   A 1 154 ? 13.591 -3.797  6.632   1.00 11.64 ?  154 ALA   A C    1 
ATOM   3413 O O    . ALA   A 1 154 ? 14.398 -3.390  5.788   1.00 12.42 ?  154 ALA   A O    1 
ATOM   3414 C CB   . ALA   A 1 154 ? 14.823 -3.178  8.710   1.00 12.38 ?  154 ALA   A CB   1 
ATOM   3415 H H    . ALA   A 1 154 ? 15.734 -5.218  7.498   1.00 13.56 ?  154 ALA   A H    1 
ATOM   3416 H HA   . ALA   A 1 154 ? 13.309 -4.555  8.521   1.00 14.41 ?  154 ALA   A HA   1 
ATOM   3417 H HB1  . ALA   A 1 154 ? 14.223 -2.425  8.843   1.00 14.83 ?  154 ALA   A HB1  1 
ATOM   3418 H HB2  . ALA   A 1 154 ? 15.135 -3.505  9.569   1.00 14.83 ?  154 ALA   A HB2  1 
ATOM   3419 H HB3  . ALA   A 1 154 ? 15.581 -2.899  8.169   1.00 14.83 ?  154 ALA   A HB3  1 
ATOM   3420 N N    A VAL   A 1 155 ? 12.277 -3.800  6.451   0.28 11.21 ?  155 VAL   A N    1 
ATOM   3421 N N    B VAL   A 1 155 ? 12.280 -3.865  6.413   0.52 11.12 ?  155 VAL   A N    1 
ATOM   3422 C CA   A VAL   A 1 155 ? 11.626 -3.276  5.262   0.28 11.45 ?  155 VAL   A CA   1 
ATOM   3423 C CA   B VAL   A 1 155 ? 11.648 -3.485  5.155   0.52 11.54 ?  155 VAL   A CA   1 
ATOM   3424 C CA   T VAL   A 1 155 ? 11.313 -3.350  4.567   0.20 14.89 ?  155 VAL   A CA   1 
ATOM   3425 C C    A VAL   A 1 155 ? 10.946 -1.974  5.660   0.28 11.71 ?  155 VAL   A C    1 
ATOM   3426 C C    B VAL   A 1 155 ? 10.935 -2.160  5.381   0.52 12.00 ?  155 VAL   A C    1 
ATOM   3427 C C    T VAL   A 1 155 ? 10.769 -2.032  5.109   0.20 14.42 ?  155 VAL   A C    1 
ATOM   3428 O O    A VAL   A 1 155 ? 10.039 -1.971  6.502   0.28 12.25 ?  155 VAL   A O    1 
ATOM   3429 O O    B VAL   A 1 155 ? 10.021 -2.076  6.211   0.52 12.51 ?  155 VAL   A O    1 
ATOM   3430 O O    T VAL   A 1 155 ? 9.776  -2.002  5.837   0.20 14.22 ?  155 VAL   A O    1 
ATOM   3431 C CB   A VAL   A 1 155 ? 10.625 -4.290  4.690   0.28 11.64 ?  155 VAL   A CB   1 
ATOM   3432 C CB   B VAL   A 1 155 ? 10.668 -4.564  4.663   0.52 11.64 ?  155 VAL   A CB   1 
ATOM   3433 C CB   T VAL   A 1 155 ? 10.212 -4.409  4.412   0.20 15.25 ?  155 VAL   A CB   1 
ATOM   3434 C CG1  A VAL   A 1 155 ? 9.932  -3.729  3.460   0.28 11.98 ?  155 VAL   A CG1  1 
ATOM   3435 C CG1  B VAL   A 1 155 ? 9.913  -4.077  3.428   0.52 12.23 ?  155 VAL   A CG1  1 
ATOM   3436 C CG1  T VAL   A 1 155 ? 9.390  -4.153  3.158   0.20 15.52 ?  155 VAL   A CG1  1 
ATOM   3437 C CG2  A VAL   A 1 155 ? 11.344 -5.592  4.359   0.28 12.09 ?  155 VAL   A CG2  1 
ATOM   3438 C CG2  B VAL   A 1 155 ? 11.412 -5.863  4.357   0.52 12.64 ?  155 VAL   A CG2  1 
ATOM   3439 C CG2  T VAL   A 1 155 ? 10.824 -5.799  4.375   0.20 15.28 ?  155 VAL   A CG2  1 
ATOM   3440 H H    A VAL   A 1 155 ? 11.723 -4.120  7.028   0.28 13.42 ?  155 VAL   A H    1 
ATOM   3441 H H    B VAL   A 1 155 ? 11.718 -4.154  7.000   0.52 13.32 ?  155 VAL   A H    1 
ATOM   3442 H HA   A VAL   A 1 155 ? 12.291 -3.081  4.588   0.28 13.71 ?  155 VAL   A HA   1 
ATOM   3443 H HA   B VAL   A 1 155 ? 12.323 -3.365  4.473   0.52 13.83 ?  155 VAL   A HA   1 
ATOM   3444 H HB   A VAL   A 1 155 ? 9.948  -4.479  5.361   0.28 13.94 ?  155 VAL   A HB   1 
ATOM   3445 H HB   B VAL   A 1 155 ? 10.016 -4.755  5.358   0.52 13.95 ?  155 VAL   A HB   1 
ATOM   3446 H HB   T VAL   A 1 155 ? 9.617  -4.350  5.175   0.20 18.28 ?  155 VAL   A HB   1 
ATOM   3447 H HG11 A VAL   A 1 155 ? 9.413  -4.436  3.046   0.28 14.35 ?  155 VAL   A HG11 1 
ATOM   3448 H HG11 B VAL   A 1 155 ? 9.492  -4.834  2.991   0.52 14.66 ?  155 VAL   A HG11 1 
ATOM   3449 H HG11 T VAL   A 1 155 ? 8.683  -4.817  3.104   0.20 18.60 ?  155 VAL   A HG11 1 
ATOM   3450 H HG12 A VAL   A 1 155 ? 9.347  -3.003  3.726   0.28 14.35 ?  155 VAL   A HG12 1 
ATOM   3451 H HG12 B VAL   A 1 155 ? 9.237  -3.438  3.701   0.52 14.66 ?  155 VAL   A HG12 1 
ATOM   3452 H HG12 T VAL   A 1 155 ? 9.006  -3.264  3.207   0.20 18.60 ?  155 VAL   A HG12 1 
ATOM   3453 H HG13 A VAL   A 1 155 ? 10.604 -3.406  2.841   0.28 14.35 ?  155 VAL   A HG13 1 
ATOM   3454 H HG13 B VAL   A 1 155 ? 10.543 -3.657  2.821   0.52 14.66 ?  155 VAL   A HG13 1 
ATOM   3455 H HG13 T VAL   A 1 155 ? 9.968  -4.223  2.383   0.20 18.60 ?  155 VAL   A HG13 1 
ATOM   3456 H HG21 A VAL   A 1 155 ? 10.723 -6.196  3.929   0.28 14.48 ?  155 VAL   A HG21 1 
ATOM   3457 H HG21 B VAL   A 1 155 ? 10.820 -6.465  3.877   0.52 15.15 ?  155 VAL   A HG21 1 
ATOM   3458 H HG21 T VAL   A 1 155 ? 10.115 -6.456  4.298   0.20 18.32 ?  155 VAL   A HG21 1 
ATOM   3459 H HG22 A VAL   A 1 155 ? 12.086 -5.399  3.763   0.28 14.48 ?  155 VAL   A HG22 1 
ATOM   3460 H HG22 B VAL   A 1 155 ? 12.187 -5.659  3.810   0.52 15.15 ?  155 VAL   A HG22 1 
ATOM   3461 H HG22 T VAL   A 1 155 ? 11.418 -5.862  3.610   0.20 18.32 ?  155 VAL   A HG22 1 
ATOM   3462 H HG23 A VAL   A 1 155 ? 11.679 -5.989  5.180   0.28 14.48 ?  155 VAL   A HG23 1 
ATOM   3463 H HG23 B VAL   A 1 155 ? 11.694 -6.271  5.190   0.52 15.15 ?  155 VAL   A HG23 1 
ATOM   3464 H HG23 T VAL   A 1 155 ? 11.322 -5.941  5.194   0.20 18.32 ?  155 VAL   A HG23 1 
ATOM   3465 N N    A PHE   A 1 156 ? 11.395 -0.865  5.067   0.28 12.03 ?  156 PHE   A N    1 
ATOM   3466 N N    B PHE   A 1 156 ? 11.319 -1.143  4.603   0.52 12.70 ?  156 PHE   A N    1 
ATOM   3467 N N    T PHE   A 1 156 ? 11.441 -0.944  4.730   0.20 14.25 ?  156 PHE   A N    1 
ATOM   3468 C CA   A PHE   A 1 156 ? 10.865 0.444   5.445   0.28 13.23 ?  156 PHE   A CA   1 
ATOM   3469 C CA   B PHE   A 1 156 ? 10.843 0.221   4.838   0.52 13.40 ?  156 PHE   A CA   1 
ATOM   3470 C CA   T PHE   A 1 156 ? 11.031 0.395   5.146   0.20 14.18 ?  156 PHE   A CA   1 
ATOM   3471 C C    A PHE   A 1 156 ? 9.400  0.596   5.050   0.28 13.16 ?  156 PHE   A C    1 
ATOM   3472 C C    B PHE   A 1 156 ? 9.371  0.390   4.462   0.52 14.52 ?  156 PHE   A C    1 
ATOM   3473 C C    T PHE   A 1 156 ? 9.588  0.683   4.755   0.20 14.14 ?  156 PHE   A C    1 
ATOM   3474 O O    A PHE   A 1 156 ? 8.590  1.103   5.836   0.28 13.36 ?  156 PHE   A O    1 
ATOM   3475 O O    B PHE   A 1 156 ? 8.604  1.007   5.211   0.52 15.88 ?  156 PHE   A O    1 
ATOM   3476 O O    T PHE   A 1 156 ? 8.875  1.390   5.477   0.20 14.47 ?  156 PHE   A O    1 
ATOM   3477 C CB   A PHE   A 1 156 ? 11.706 1.552   4.811   0.28 14.43 ?  156 PHE   A CB   1 
ATOM   3478 C CB   B PHE   A 1 156 ? 11.739 1.188   4.053   0.52 12.60 ?  156 PHE   A CB   1 
ATOM   3479 C CB   T PHE   A 1 156 ? 11.971 1.408   4.486   0.20 14.03 ?  156 PHE   A CB   1 
ATOM   3480 C CG   A PHE   A 1 156 ? 11.207 2.937   5.116   0.28 15.68 ?  156 PHE   A CG   1 
ATOM   3481 C CG   B PHE   A 1 156 ? 11.467 2.660   4.299   0.52 13.27 ?  156 PHE   A CG   1 
ATOM   3482 C CG   T PHE   A 1 156 ? 11.560 2.852   4.654   0.20 14.23 ?  156 PHE   A CG   1 
ATOM   3483 C CD1  A PHE   A 1 156 ? 11.130 3.378   6.425   0.28 16.42 ?  156 PHE   A CD1  1 
ATOM   3484 C CD1  B PHE   A 1 156 ? 12.049 3.322   5.375   0.52 14.08 ?  156 PHE   A CD1  1 
ATOM   3485 C CD1  T PHE   A 1 156 ? 11.855 3.543   5.820   0.20 14.25 ?  156 PHE   A CD1  1 
ATOM   3486 C CD2  A PHE   A 1 156 ? 10.819 3.795   4.099   0.28 16.30 ?  156 PHE   A CD2  1 
ATOM   3487 C CD2  B PHE   A 1 156 ? 10.685 3.391   3.419   0.52 14.35 ?  156 PHE   A CD2  1 
ATOM   3488 C CD2  T PHE   A 1 156 ? 10.921 3.530   3.626   0.20 14.63 ?  156 PHE   A CD2  1 
ATOM   3489 C CE1  A PHE   A 1 156 ? 10.671 4.646   6.718   0.28 16.91 ?  156 PHE   A CE1  1 
ATOM   3490 C CE1  B PHE   A 1 156 ? 11.823 4.676   5.587   0.52 15.03 ?  156 PHE   A CE1  1 
ATOM   3491 C CE1  T PHE   A 1 156 ? 11.496 4.875   5.967   0.20 14.71 ?  156 PHE   A CE1  1 
ATOM   3492 C CE2  A PHE   A 1 156 ? 10.358 5.069   4.387   0.28 16.90 ?  156 PHE   A CE2  1 
ATOM   3493 C CE2  B PHE   A 1 156 ? 10.459 4.743   3.625   0.52 15.28 ?  156 PHE   A CE2  1 
ATOM   3494 C CE2  T PHE   A 1 156 ? 10.562 4.862   3.766   0.20 14.95 ?  156 PHE   A CE2  1 
ATOM   3495 C CZ   A PHE   A 1 156 ? 10.287 5.494   5.698   0.28 17.16 ?  156 PHE   A CZ   1 
ATOM   3496 C CZ   B PHE   A 1 156 ? 11.030 5.386   4.710   0.52 15.37 ?  156 PHE   A CZ   1 
ATOM   3497 C CZ   T PHE   A 1 156 ? 10.848 5.534   4.939   0.20 15.01 ?  156 PHE   A CZ   1 
ATOM   3498 H H    A PHE   A 1 156 ? 11.996 -0.843  4.452   0.28 14.41 ?  156 PHE   A H    1 
ATOM   3499 H H    B PHE   A 1 156 ? 11.847 -1.228  3.931   0.52 15.22 ?  156 PHE   A H    1 
ATOM   3500 H H    T PHE   A 1 156 ? 12.130 -0.962  4.219   0.20 17.07 ?  156 PHE   A H    1 
ATOM   3501 H HA   A PHE   A 1 156 ? 10.924 0.546   6.405   0.28 15.85 ?  156 PHE   A HA   1 
ATOM   3502 H HA   B PHE   A 1 156 ? 10.933 0.416   5.781   0.52 16.05 ?  156 PHE   A HA   1 
ATOM   3503 H HA   T PHE   A 1 156 ? 11.120 0.471   6.111   0.20 16.99 ?  156 PHE   A HA   1 
ATOM   3504 H HB2  A PHE   A 1 156 ? 12.617 1.487   5.143   0.28 17.29 ?  156 PHE   A HB2  1 
ATOM   3505 H HB2  B PHE   A 1 156 ? 12.657 1.012   4.306   0.52 15.09 ?  156 PHE   A HB2  1 
ATOM   3506 H HB2  T PHE   A 1 156 ? 12.854 1.305   4.870   0.20 16.82 ?  156 PHE   A HB2  1 
ATOM   3507 H HB3  A PHE   A 1 156 ? 11.701 1.442   3.847   0.28 17.29 ?  156 PHE   A HB3  1 
ATOM   3508 H HB3  B PHE   A 1 156 ? 11.622 1.017   3.106   0.52 15.09 ?  156 PHE   A HB3  1 
ATOM   3509 H HB3  T PHE   A 1 156 ? 12.003 1.218   3.535   0.20 16.82 ?  156 PHE   A HB3  1 
ATOM   3510 H HD1  A PHE   A 1 156 ? 11.389 2.811   7.116   0.28 19.68 ?  156 PHE   A HD1  1 
ATOM   3511 H HD1  B PHE   A 1 156 ? 12.583 2.841   5.973   0.52 16.87 ?  156 PHE   A HD1  1 
ATOM   3512 H HD1  T PHE   A 1 156 ? 12.288 3.103   6.516   0.20 17.08 ?  156 PHE   A HD1  1 
ATOM   3513 H HD2  A PHE   A 1 156 ? 10.868 3.511   3.214   0.28 19.53 ?  156 PHE   A HD2  1 
ATOM   3514 H HD2  B PHE   A 1 156 ? 10.297 2.965   2.693   0.52 17.20 ?  156 PHE   A HD2  1 
ATOM   3515 H HD2  T PHE   A 1 156 ? 10.723 3.084   2.835   0.20 17.54 ?  156 PHE   A HD2  1 
ATOM   3516 H HE1  A PHE   A 1 156 ? 10.624 4.930   7.603   0.28 20.27 ?  156 PHE   A HE1  1 
ATOM   3517 H HE1  B PHE   A 1 156 ? 12.208 5.097   6.323   0.52 18.01 ?  156 PHE   A HE1  1 
ATOM   3518 H HE1  T PHE   A 1 156 ? 11.692 5.324   6.759   0.20 17.63 ?  156 PHE   A HE1  1 
ATOM   3519 H HE2  A PHE   A 1 156 ? 10.102 5.635   3.697   0.28 20.26 ?  156 PHE   A HE2  1 
ATOM   3520 H HE2  B PHE   A 1 156 ? 9.920  5.218   3.039   0.52 18.31 ?  156 PHE   A HE2  1 
ATOM   3521 H HE2  T PHE   A 1 156 ? 10.125 5.303   3.073   0.20 17.91 ?  156 PHE   A HE2  1 
ATOM   3522 H HZ   A PHE   A 1 156 ? 9.979  6.348   5.895   0.28 20.56 ?  156 PHE   A HZ   1 
ATOM   3523 H HZ   B PHE   A 1 156 ? 10.873 6.289   4.857   0.52 18.42 ?  156 PHE   A HZ   1 
ATOM   3524 H HZ   T PHE   A 1 156 ? 10.607 6.428   5.037   0.20 17.99 ?  156 PHE   A HZ   1 
ATOM   3525 N N    A ASP   A 1 157 ? 9.043  0.165   3.844   0.28 13.46 ?  157 ASP   A N    1 
ATOM   3526 N N    B ASP   A 1 157 ? 8.951  -0.164  3.325   0.52 15.61 ?  157 ASP   A N    1 
ATOM   3527 N N    T ASP   A 1 157 ? 9.146  0.143   3.624   0.20 14.26 ?  157 ASP   A N    1 
ATOM   3528 C CA   A ASP   A 1 157 ? 7.715  0.404   3.291   0.28 14.60 ?  157 ASP   A CA   1 
ATOM   3529 C CA   B ASP   A 1 157 ? 7.621  0.106   2.787   0.52 16.20 ?  157 ASP   A CA   1 
ATOM   3530 C CA   T ASP   A 1 157 ? 7.829  0.425   3.069   0.20 14.71 ?  157 ASP   A CA   1 
ATOM   3531 C C    A ASP   A 1 157 ? 6.735  -0.636  3.830   0.28 15.07 ?  157 ASP   A C    1 
ATOM   3532 C C    B ASP   A 1 157 ? 6.621  -0.956  3.234   0.52 15.30 ?  157 ASP   A C    1 
ATOM   3533 C C    T ASP   A 1 157 ? 6.821  -0.581  3.616   0.20 15.40 ?  157 ASP   A C    1 
ATOM   3534 O O    A ASP   A 1 157 ? 6.944  -1.841  3.654   0.28 14.89 ?  157 ASP   A O    1 
ATOM   3535 O O    B ASP   A 1 157 ? 6.830  -2.151  3.007   0.52 14.20 ?  157 ASP   A O    1 
ATOM   3536 O O    T ASP   A 1 157 ? 6.983  -1.793  3.431   0.20 15.12 ?  157 ASP   A O    1 
ATOM   3537 C CB   A ASP   A 1 157 ? 7.796  0.314   1.769   0.28 15.25 ?  157 ASP   A CB   1 
ATOM   3538 C CB   B ASP   A 1 157 ? 7.652  0.164   1.262   0.52 17.52 ?  157 ASP   A CB   1 
ATOM   3539 C CB   T ASP   A 1 157 ? 7.915  0.328   1.547   0.20 14.56 ?  157 ASP   A CB   1 
ATOM   3540 C CG   A ASP   A 1 157 ? 6.566  0.864   1.086   0.28 16.20 ?  157 ASP   A CG   1 
ATOM   3541 C CG   B ASP   A 1 157 ? 6.304  0.537   0.669   0.52 18.85 ?  157 ASP   A CG   1 
ATOM   3542 C CG   T ASP   A 1 157 ? 6.682  0.856   0.857   0.20 14.56 ?  157 ASP   A CG   1 
ATOM   3543 O OD1  A ASP   A 1 157 ? 6.493  2.096   0.897   0.28 16.95 ?  157 ASP   A OD1  1 
ATOM   3544 O OD1  B ASP   A 1 157 ? 5.830  1.668   0.926   0.52 20.15 ?  157 ASP   A OD1  1 
ATOM   3545 O OD1  T ASP   A 1 157 ? 5.581  0.327   1.120   0.20 15.06 ?  157 ASP   A OD1  1 
ATOM   3546 O OD2  A ASP   A 1 157 ? 5.675  0.063   0.736   0.28 16.24 -1 157 ASP   A OD2  1 
ATOM   3547 O OD2  B ASP   A 1 157 ? 5.713  -0.299  -0.046  0.52 18.91 -1 157 ASP   A OD2  1 
ATOM   3548 O OD2  T ASP   A 1 157 ? 6.814  1.804   0.056   0.20 14.03 -1 157 ASP   A OD2  1 
ATOM   3549 H H    A ASP   A 1 157 ? 9.559  -0.279  3.319   0.28 16.13 ?  157 ASP   A H    1 
ATOM   3550 H H    B ASP   A 1 157 ? 9.411  -0.717  2.855   0.52 18.70 ?  157 ASP   A H    1 
ATOM   3551 H H    T ASP   A 1 157 ? 9.609  -0.397  3.144   0.20 17.09 ?  157 ASP   A H    1 
ATOM   3552 H HA   A ASP   A 1 157 ? 7.402  1.289   3.534   0.28 17.50 ?  157 ASP   A HA   1 
ATOM   3553 H HA   B ASP   A 1 157 ? 7.312  0.957   3.120   0.52 19.42 ?  157 ASP   A HA   1 
ATOM   3554 H HA   T ASP   A 1 157 ? 7.548  1.320   3.315   0.20 17.63 ?  157 ASP   A HA   1 
ATOM   3555 H HB2  A ASP   A 1 157 ? 8.558  0.824   1.461   0.28 18.28 ?  157 ASP   A HB2  1 
ATOM   3556 H HB2  B ASP   A 1 157 ? 8.309  0.821   0.991   0.52 21.00 ?  157 ASP   A HB2  1 
ATOM   3557 H HB2  T ASP   A 1 157 ? 8.678  0.842   1.243   0.20 17.44 ?  157 ASP   A HB2  1 
ATOM   3558 H HB3  A ASP   A 1 157 ? 7.900  -0.615  1.512   0.28 18.28 ?  157 ASP   A HB3  1 
ATOM   3559 H HB3  B ASP   A 1 157 ? 7.889  -0.711  0.917   0.52 21.00 ?  157 ASP   A HB3  1 
ATOM   3560 H HB3  T ASP   A 1 157 ? 8.025  -0.602  1.295   0.20 17.44 ?  157 ASP   A HB3  1 
ATOM   3561 N N    A LYS   A 1 158 ? 5.660  -0.174  4.478   0.28 16.06 ?  158 LYS   A N    1 
ATOM   3562 N N    B LYS   A 1 158 ? 5.515  -0.505  3.834   0.52 16.17 ?  158 LYS   A N    1 
ATOM   3563 N N    T LYS   A 1 158 ? 5.775  -0.079  4.280   0.20 16.73 ?  158 LYS   A N    1 
ATOM   3564 C CA   A LYS   A 1 158 ? 4.683  -1.104  5.042   0.28 17.16 ?  158 LYS   A CA   1 
ATOM   3565 C CA   B LYS   A 1 158 ? 4.523  -1.420  4.402   0.52 17.21 ?  158 LYS   A CA   1 
ATOM   3566 C CA   T LYS   A 1 158 ? 4.796  -0.970  4.899   0.20 18.03 ?  158 LYS   A CA   1 
ATOM   3567 C C    A LYS   A 1 158 ? 3.955  -1.879  3.950   0.28 16.96 ?  158 LYS   A C    1 
ATOM   3568 C C    B LYS   A 1 158 ? 3.856  -2.272  3.322   0.52 15.85 ?  158 LYS   A C    1 
ATOM   3569 C C    T LYS   A 1 158 ? 4.040  -1.781  3.853   0.20 17.93 ?  158 LYS   A C    1 
ATOM   3570 O O    A LYS   A 1 158 ? 3.760  -3.093  4.073   0.28 16.88 ?  158 LYS   A O    1 
ATOM   3571 O O    B LYS   A 1 158 ? 3.718  -3.491  3.476   0.52 15.67 ?  158 LYS   A O    1 
ATOM   3572 O O    T LYS   A 1 158 ? 3.827  -2.985  4.031   0.20 17.75 ?  158 LYS   A O    1 
ATOM   3573 C CB   A LYS   A 1 158 ? 3.686  -0.356  5.931   0.28 18.60 ?  158 LYS   A CB   1 
ATOM   3574 C CB   B LYS   A 1 158 ? 3.484  -0.615  5.195   0.52 19.81 ?  158 LYS   A CB   1 
ATOM   3575 C CB   T LYS   A 1 158 ? 3.827  -0.171  5.774   0.20 19.57 ?  158 LYS   A CB   1 
ATOM   3576 C CG   A LYS   A 1 158 ? 2.465  -1.178  6.366   0.28 20.26 ?  158 LYS   A CG   1 
ATOM   3577 C CG   B LYS   A 1 158 ? 2.278  -1.410  5.709   0.52 22.56 ?  158 LYS   A CG   1 
ATOM   3578 C CG   T LYS   A 1 158 ? 2.605  -0.958  6.250   0.20 21.17 ?  158 LYS   A CG   1 
ATOM   3579 C CD   A LYS   A 1 158 ? 2.842  -2.440  7.140   0.28 21.57 ?  158 LYS   A CD   1 
ATOM   3580 C CD   B LYS   A 1 158 ? 2.656  -2.446  6.765   0.52 24.93 ?  158 LYS   A CD   1 
ATOM   3581 C CD   T LYS   A 1 158 ? 2.991  -2.158  7.106   0.20 22.60 ?  158 LYS   A CD   1 
ATOM   3582 C CE   A LYS   A 1 158 ? 1.603  -3.147  7.682   0.28 22.26 ?  158 LYS   A CE   1 
ATOM   3583 C CE   B LYS   A 1 158 ? 1.414  -2.990  7.470   0.52 26.31 ?  158 LYS   A CE   1 
ATOM   3584 C CE   T LYS   A 1 158 ? 1.765  -2.970  7.504   0.20 23.56 ?  158 LYS   A CE   1 
ATOM   3585 N NZ   A LYS   A 1 158 ? 1.909  -4.486  8.264   0.28 22.68 ?  158 LYS   A NZ   1 
ATOM   3586 N NZ   B LYS   A 1 158 ? 1.691  -4.222  8.264   0.52 26.94 ?  158 LYS   A NZ   1 
ATOM   3587 N NZ   T LYS   A 1 158 ? 2.118  -4.198  8.273   0.20 24.14 ?  158 LYS   A NZ   1 
ATOM   3588 H H    A LYS   A 1 158 ? 5.478  0.657   4.601   0.28 19.25 ?  158 LYS   A H    1 
ATOM   3589 H H    B LYS   A 1 158 ? 5.315  0.322   3.926   0.52 19.38 ?  158 LYS   A H    1 
ATOM   3590 H H    T LYS   A 1 158 ? 5.610  0.758   4.381   0.20 20.06 ?  158 LYS   A H    1 
ATOM   3591 H HA   A LYS   A 1 158 ? 5.145  -1.746  5.597   0.28 20.57 ?  158 LYS   A HA   1 
ATOM   3592 H HA   B LYS   A 1 158 ? 4.958  -2.020  5.027   0.52 20.63 ?  158 LYS   A HA   1 
ATOM   3593 H HA   T LYS   A 1 158 ? 5.262  -1.594  5.474   0.20 21.62 ?  158 LYS   A HA   1 
ATOM   3594 H HB2  A LYS   A 1 158 ? 4.143  -0.063  6.735   0.28 22.30 ?  158 LYS   A HB2  1 
ATOM   3595 H HB2  B LYS   A 1 158 ? 3.920  -0.225  5.972   0.52 23.74 ?  158 LYS   A HB2  1 
ATOM   3596 H HB2  T LYS   A 1 158 ? 4.301  0.135   6.565   0.20 23.46 ?  158 LYS   A HB2  1 
ATOM   3597 H HB3  A LYS   A 1 158 ? 3.357  0.418   5.446   0.28 22.30 ?  158 LYS   A HB3  1 
ATOM   3598 H HB3  B LYS   A 1 158 ? 3.141  0.095   4.630   0.52 23.74 ?  158 LYS   A HB3  1 
ATOM   3599 H HB3  T LYS   A 1 158 ? 3.505  0.593   5.271   0.20 23.46 ?  158 LYS   A HB3  1 
ATOM   3600 H HG2  A LYS   A 1 158 ? 1.912  -0.630  6.944   0.28 24.29 ?  158 LYS   A HG2  1 
ATOM   3601 H HG2  B LYS   A 1 158 ? 1.647  -0.792  6.113   0.52 27.04 ?  158 LYS   A HG2  1 
ATOM   3602 H HG2  T LYS   A 1 158 ? 2.049  -0.376  6.789   0.20 25.38 ?  158 LYS   A HG2  1 
ATOM   3603 H HG3  A LYS   A 1 158 ? 1.956  -1.442  5.582   0.28 24.29 ?  158 LYS   A HG3  1 
ATOM   3604 H HG3  B LYS   A 1 158 ? 1.854  -1.871  4.969   0.52 27.04 ?  158 LYS   A HG3  1 
ATOM   3605 H HG3  T LYS   A 1 158 ? 2.099  -1.277  5.485   0.20 25.38 ?  158 LYS   A HG3  1 
ATOM   3606 H HD2  A LYS   A 1 158 ? 3.311  -3.052  6.552   0.28 25.86 ?  158 LYS   A HD2  1 
ATOM   3607 H HD2  B LYS   A 1 158 ? 3.117  -3.184  6.338   0.52 29.89 ?  158 LYS   A HD2  1 
ATOM   3608 H HD2  T LYS   A 1 158 ? 3.586  -2.737  6.605   0.20 27.09 ?  158 LYS   A HD2  1 
ATOM   3609 H HD3  A LYS   A 1 158 ? 3.403  -2.198  7.892   0.28 25.86 ?  158 LYS   A HD3  1 
ATOM   3610 H HD3  B LYS   A 1 158 ? 3.230  -2.029  7.429   0.52 29.89 ?  158 LYS   A HD3  1 
ATOM   3611 H HD3  T LYS   A 1 158 ? 3.426  -1.848  7.916   0.20 27.09 ?  158 LYS   A HD3  1 
ATOM   3612 H HE2  A LYS   A 1 158 ? 1.204  -2.598  8.376   0.28 26.68 ?  158 LYS   A HE2  1 
ATOM   3613 H HE2  B LYS   A 1 158 ? 1.075  -2.310  8.076   0.52 31.55 ?  158 LYS   A HE2  1 
ATOM   3614 H HE2  T LYS   A 1 158 ? 1.184  -2.423  8.056   0.20 28.25 ?  158 LYS   A HE2  1 
ATOM   3615 H HE3  A LYS   A 1 158 ? 0.972  -3.271  6.959   0.28 26.68 ?  158 LYS   A HE3  1 
ATOM   3616 H HE3  B LYS   A 1 158 ? 0.742  -3.202  6.804   0.52 31.55 ?  158 LYS   A HE3  1 
ATOM   3617 H HE3  T LYS   A 1 158 ? 1.294  -3.245  6.702   0.20 28.25 ?  158 LYS   A HE3  1 
ATOM   3618 H HZ1  A LYS   A 1 158 ? 1.162  -4.861  8.569   0.28 27.19 ?  158 LYS   A HZ1  1 
ATOM   3619 H HZ1  B LYS   A 1 158 ? 0.943  -4.506  8.652   0.52 32.31 ?  158 LYS   A HZ1  1 
ATOM   3620 H HZ1  T LYS   A 1 158 ? 1.379  -4.646  8.488   0.20 28.94 ?  158 LYS   A HZ1  1 
ATOM   3621 H HZ2  A LYS   A 1 158 ? 2.265  -5.012  7.641   0.28 27.19 ?  158 LYS   A HZ2  1 
ATOM   3622 H HZ2  B LYS   A 1 158 ? 2.003  -4.862  7.731   0.52 32.31 ?  158 LYS   A HZ2  1 
ATOM   3623 H HZ2  T LYS   A 1 158 ? 2.642  -4.723  7.781   0.20 28.94 ?  158 LYS   A HZ2  1 
ATOM   3624 H HZ3  A LYS   A 1 158 ? 2.486  -4.401  8.936   0.28 27.19 ?  158 LYS   A HZ3  1 
ATOM   3625 H HZ3  B LYS   A 1 158 ? 2.296  -4.048  8.893   0.52 32.31 ?  158 LYS   A HZ3  1 
ATOM   3626 H HZ3  T LYS   A 1 158 ? 2.549  -3.976  9.019   0.20 28.94 ?  158 LYS   A HZ3  1 
ATOM   3627 N N    A ASN   A 1 159 ? 3.535  -1.199  2.882   0.28 17.21 ?  159 ASN   A N    1 
ATOM   3628 N N    B ASN   A 1 159 ? 3.414  -1.647  2.228   0.52 16.62 ?  159 ASN   A N    1 
ATOM   3629 N N    T ASN   A 1 159 ? 3.618  -1.143  2.766   0.20 18.25 ?  159 ASN   A N    1 
ATOM   3630 C CA   A ASN   A 1 159 ? 2.857  -1.899  1.795   0.28 17.55 ?  159 ASN   A CA   1 
ATOM   3631 C CA   B ASN   A 1 159 ? 2.795  -2.418  1.153   0.52 17.57 ?  159 ASN   A CA   1 
ATOM   3632 C CA   T ASN   A 1 159 ? 2.884  -1.843  1.717   0.20 18.66 ?  159 ASN   A CA   1 
ATOM   3633 C C    A ASN   A 1 159 ? 3.758  -2.965  1.187   0.28 16.74 ?  159 ASN   A C    1 
ATOM   3634 C C    B ASN   A 1 159 ? 3.740  -3.509  0.659   0.52 16.38 ?  159 ASN   A C    1 
ATOM   3635 C C    T ASN   A 1 159 ? 3.732  -2.946  1.096   0.20 18.40 ?  159 ASN   A C    1 
ATOM   3636 O O    A ASN   A 1 159 ? 3.318  -4.092  0.937   0.28 16.66 ?  159 ASN   A O    1 
ATOM   3637 O O    B ASN   A 1 159 ? 3.329  -4.655  0.435   0.52 17.06 ?  159 ASN   A O    1 
ATOM   3638 O O    T ASN   A 1 159 ? 3.222  -4.012  0.757   0.20 18.52 ?  159 ASN   A O    1 
ATOM   3639 C CB   A ASN   A 1 159 ? 2.391  -0.901  0.732   0.28 19.03 ?  159 ASN   A CB   1 
ATOM   3640 C CB   B ASN   A 1 159 ? 2.386  -1.477  0.014   0.52 20.49 ?  159 ASN   A CB   1 
ATOM   3641 C CB   T ASN   A 1 159 ? 2.409  -0.866  0.639   0.20 19.55 ?  159 ASN   A CB   1 
ATOM   3642 C CG   A ASN   A 1 159 ? 1.170  -0.116  1.166   0.28 20.72 ?  159 ASN   A CG   1 
ATOM   3643 C CG   B ASN   A 1 159 ? 1.238  -0.560  0.396   0.52 23.74 ?  159 ASN   A CG   1 
ATOM   3644 C CG   T ASN   A 1 159 ? 1.202  -0.060  1.076   0.20 20.61 ?  159 ASN   A CG   1 
ATOM   3645 O OD1  A ASN   A 1 159 ? 0.307  -0.639  1.866   0.28 21.18 ?  159 ASN   A OD1  1 
ATOM   3646 O OD1  B ASN   A 1 159 ? 1.371  0.280   1.287   0.52 25.25 ?  159 ASN   A OD1  1 
ATOM   3647 O OD1  T ASN   A 1 159 ? 0.366  -0.543  1.837   0.20 20.86 ?  159 ASN   A OD1  1 
ATOM   3648 N ND2  A ASN   A 1 159 ? 1.094  1.145   0.753   0.28 21.06 ?  159 ASN   A ND2  1 
ATOM   3649 N ND2  B ASN   A 1 159 ? 0.111  -0.702  -0.293  0.52 24.77 ?  159 ASN   A ND2  1 
ATOM   3650 N ND2  T ASN   A 1 159 ? 1.106  1.175   0.598   0.20 20.86 ?  159 ASN   A ND2  1 
ATOM   3651 H H    A ASN   A 1 159 ? 3.628  -0.356  2.765   0.28 20.63 ?  159 ASN   A H    1 
ATOM   3652 H H    B ASN   A 1 159 ? 3.461  -0.803  2.092   0.52 19.92 ?  159 ASN   A H    1 
ATOM   3653 H H    T ASN   A 1 159 ? 3.738  -0.308  2.616   0.20 21.88 ?  159 ASN   A H    1 
ATOM   3654 H HA   A ASN   A 1 159 ? 2.068  -2.344  2.148   0.28 21.03 ?  159 ASN   A HA   1 
ATOM   3655 H HA   B ASN   A 1 159 ? 1.986  -2.840  1.487   0.52 21.06 ?  159 ASN   A HA   1 
ATOM   3656 H HA   T ASN   A 1 159 ? 2.101  -2.261  2.106   0.20 22.36 ?  159 ASN   A HA   1 
ATOM   3657 H HB2  A ASN   A 1 159 ? 3.104  -0.271  0.555   0.28 22.81 ?  159 ASN   A HB2  1 
ATOM   3658 H HB2  B ASN   A 1 159 ? 3.142  -0.916  -0.225  0.52 24.56 ?  159 ASN   A HB2  1 
ATOM   3659 H HB2  T ASN   A 1 159 ? 3.126  -0.247  0.435   0.20 23.43 ?  159 ASN   A HB2  1 
ATOM   3660 H HB3  A ASN   A 1 159 ? 2.163  -1.385  -0.079  0.28 22.81 ?  159 ASN   A HB3  1 
ATOM   3661 H HB3  B ASN   A 1 159 ? 2.103  -1.997  -0.750  0.52 24.56 ?  159 ASN   A HB3  1 
ATOM   3662 H HB3  T ASN   A 1 159 ? 2.165  -1.368  -0.156  0.20 23.43 ?  159 ASN   A HB3  1 
ATOM   3663 H HD21 A ASN   A 1 159 ? 0.420  1.631   0.972   0.28 25.25 ?  159 ASN   A HD21 1 
ATOM   3664 H HD21 B ASN   A 1 159 ? -0.571 -0.203  -0.119  0.52 29.70 ?  159 ASN   A HD21 1 
ATOM   3665 H HD21 T ASN   A 1 159 ? 0.438  1.669   0.817   0.20 25.01 ?  159 ASN   A HD21 1 
ATOM   3666 H HD22 A ASN   A 1 159 ? 1.721  1.476   0.267   0.28 25.25 ?  159 ASN   A HD22 1 
ATOM   3667 H HD22 B ASN   A 1 159 ? 0.058  -1.296  -0.911  0.52 29.70 ?  159 ASN   A HD22 1 
ATOM   3668 H HD22 T ASN   A 1 159 ? 1.711  1.478   0.070   0.20 25.01 ?  159 ASN   A HD22 1 
ATOM   3669 N N    A LEU   A 1 160 ? 5.030  -2.637  0.958   0.28 16.12 ?  160 LEU   A N    1 
ATOM   3670 N N    B LEU   A 1 160 ? 5.023  -3.178  0.513   0.52 15.74 ?  160 LEU   A N    1 
ATOM   3671 N N    T LEU   A 1 160 ? 5.026  -2.691  0.950   0.20 18.13 ?  160 LEU   A N    1 
ATOM   3672 C CA   A LEU   A 1 160 ? 5.946  -3.623  0.398   0.28 15.70 ?  160 LEU   A CA   1 
ATOM   3673 C CA   B LEU   A 1 160 ? 5.998  -4.178  0.102   0.52 15.06 ?  160 LEU   A CA   1 
ATOM   3674 C CA   T LEU   A 1 160 ? 5.931  -3.686  0.391   0.20 17.90 ?  160 LEU   A CA   1 
ATOM   3675 C C    A LEU   A 1 160 ? 6.113  -4.809  1.336   0.28 15.20 ?  160 LEU   A C    1 
ATOM   3676 C C    B LEU   A 1 160 ? 6.161  -5.257  1.169   0.52 14.50 ?  160 LEU   A C    1 
ATOM   3677 O O    A LEU   A 1 160 ? 6.181  -5.961  0.891   0.28 15.09 ?  160 LEU   A O    1 
ATOM   3678 O O    B LEU   A 1 160 ? 6.153  -6.451  0.855   0.52 14.84 ?  160 LEU   A O    1 
ATOM   3679 C CB   A LEU   A 1 160 ? 7.299  -2.979  0.113   0.28 15.96 ?  160 LEU   A CB   1 
ATOM   3680 C CB   B LEU   A 1 160 ? 7.338  -3.516  -0.192  0.52 15.08 ?  160 LEU   A CB   1 
ATOM   3681 C CB   T LEU   A 1 160 ? 7.295  -3.069  0.096   0.20 17.79 ?  160 LEU   A CB   1 
ATOM   3682 C CG   A LEU   A 1 160 ? 8.387  -3.963  -0.312  0.28 16.43 ?  160 LEU   A CG   1 
ATOM   3683 C CG   B LEU   A 1 160 ? 8.435  -4.526  -0.518  0.52 15.59 ?  160 LEU   A CG   1 
ATOM   3684 C CG   T LEU   A 1 160 ? 8.362  -4.068  -0.349  0.20 17.86 ?  160 LEU   A CG   1 
ATOM   3685 C CD1  A LEU   A 1 160 ? 7.958  -4.728  -1.551  0.28 16.72 ?  160 LEU   A CD1  1 
ATOM   3686 C CD1  B LEU   A 1 160 ? 8.043  -5.310  -1.762  0.52 16.51 ?  160 LEU   A CD1  1 
ATOM   3687 C CD1  T LEU   A 1 160 ? 7.923  -4.800  -1.605  0.20 17.97 ?  160 LEU   A CD1  1 
ATOM   3688 C CD2  A LEU   A 1 160 ? 9.692  -3.234  -0.550  0.28 16.65 ?  160 LEU   A CD2  1 
ATOM   3689 C CD2  B LEU   A 1 160 ? 9.760  -3.812  -0.682  0.52 15.78 ?  160 LEU   A CD2  1 
ATOM   3690 C CD2  T LEU   A 1 160 ? 9.682  -3.361  -0.572  0.20 17.92 ?  160 LEU   A CD2  1 
ATOM   3691 H H    A LEU   A 1 160 ? 5.374  -1.868  1.121   0.28 19.32 ?  160 LEU   A H    1 
ATOM   3692 H H    B LEU   A 1 160 ? 5.344  -2.400  0.652   0.52 18.86 ?  160 LEU   A H    1 
ATOM   3693 H H    T LEU   A 1 160 ? 5.405  -1.950  1.165   0.20 21.74 ?  160 LEU   A H    1 
ATOM   3694 H HA   A LEU   A 1 160 ? 5.583  -3.950  -0.436  0.28 18.82 ?  160 LEU   A HA   1 
ATOM   3695 H HA   B LEU   A 1 160 ? 5.680  -4.608  -0.710  0.52 18.05 ?  160 LEU   A HA   1 
ATOM   3696 H HB2  A LEU   A 1 160 ? 7.193  -2.317  -0.592  0.28 19.13 ?  160 LEU   A HB2  1 
ATOM   3697 H HB2  B LEU   A 1 160 ? 7.233  -2.927  -0.955  0.52 18.07 ?  160 LEU   A HB2  1 
ATOM   3698 H HB2  T LEU   A 1 160 ? 7.194  -2.406  -0.608  0.20 21.32 ?  160 LEU   A HB2  1 
ATOM   3699 H HB3  A LEU   A 1 160 ? 7.605  -2.552  0.925   0.28 19.13 ?  160 LEU   A HB3  1 
ATOM   3700 H HB3  B LEU   A 1 160 ? 7.613  -3.010  0.586   0.52 18.07 ?  160 LEU   A HB3  1 
ATOM   3701 H HB3  T LEU   A 1 160 ? 7.619  -2.644  0.904   0.20 21.32 ?  160 LEU   A HB3  1 
ATOM   3702 H HG   A LEU   A 1 160 ? 8.534  -4.603  0.403   0.28 19.69 ?  160 LEU   A HG   1 
ATOM   3703 H HG   B LEU   A 1 160 ? 8.529  -5.155  0.216   0.52 18.68 ?  160 LEU   A HG   1 
ATOM   3704 H HG   T LEU   A 1 160 ? 8.488  -4.725  0.354   0.20 21.41 ?  160 LEU   A HG   1 
ATOM   3705 H HD11 A LEU   A 1 160 ? 8.709  -5.251  -1.870  0.28 20.04 ?  160 LEU   A HD11 1 
ATOM   3706 H HD11 B LEU   A 1 160 ? 8.793  -5.851  -2.035  0.52 19.79 ?  160 LEU   A HD11 1 
ATOM   3707 H HD11 T LEU   A 1 160 ? 8.659  -5.346  -1.922  0.20 21.54 ?  160 LEU   A HD11 1 
ATOM   3708 H HD12 A LEU   A 1 160 ? 7.220  -5.316  -1.323  0.28 20.04 ?  160 LEU   A HD12 1 
ATOM   3709 H HD12 B LEU   A 1 160 ? 7.283  -5.879  -1.556  0.52 19.79 ?  160 LEU   A HD12 1 
ATOM   3710 H HD12 T LEU   A 1 160 ? 7.161  -5.362  -1.394  0.20 21.54 ?  160 LEU   A HD12 1 
ATOM   3711 H HD13 A LEU   A 1 160 ? 7.680  -4.096  -2.232  0.28 20.04 ?  160 LEU   A HD13 1 
ATOM   3712 H HD13 B LEU   A 1 160 ? 7.805  -4.683  -2.465  0.52 19.79 ?  160 LEU   A HD13 1 
ATOM   3713 H HD13 T LEU   A 1 160 ? 7.679  -4.149  -2.280  0.20 21.54 ?  160 LEU   A HD13 1 
ATOM   3714 H HD21 A LEU   A 1 160 ? 10.366 -3.879  -0.814  0.28 19.95 ?  160 LEU   A HD21 1 
ATOM   3715 H HD21 B LEU   A 1 160 ? 10.459 -4.471  -0.808  0.52 18.92 ?  160 LEU   A HD21 1 
ATOM   3716 H HD21 T LEU   A 1 160 ? 10.332 -4.004  -0.894  0.20 21.48 ?  160 LEU   A HD21 1 
ATOM   3717 H HD22 A LEU   A 1 160 ? 9.563  -2.580  -1.253  0.28 19.95 ?  160 LEU   A HD22 1 
ATOM   3718 H HD22 B LEU   A 1 160 ? 9.711  -3.226  -1.452  0.52 18.92 ?  160 LEU   A HD22 1 
ATOM   3719 H HD22 T LEU   A 1 160 ? 9.556  -2.658  -1.227  0.20 21.48 ?  160 LEU   A HD22 1 
ATOM   3720 H HD23 A LEU   A 1 160 ? 9.960  -2.791  0.271   0.28 19.95 ?  160 LEU   A HD23 1 
ATOM   3721 H HD23 B LEU   A 1 160 ? 9.938  -3.291  0.119   0.52 18.92 ?  160 LEU   A HD23 1 
ATOM   3722 H HD23 T LEU   A 1 160 ? 9.980  -2.981  0.269   0.20 21.48 ?  160 LEU   A HD23 1 
ATOM   3723 N N    A TYR   A 1 161 ? 6.186  -4.544  2.640   0.48 16.15 ?  161 TYR   A N    1 
ATOM   3724 N N    B TYR   A 1 161 ? 6.338  -4.856  2.432   0.52 15.33 ?  161 TYR   A N    1 
ATOM   3725 C CA   A TYR   A 1 161 ? 6.340  -5.623  3.608   0.48 16.11 ?  161 TYR   A CA   1 
ATOM   3726 C CA   B TYR   A 1 161 ? 6.436  -5.823  3.526   0.52 15.93 ?  161 TYR   A CA   1 
ATOM   3727 C C    A TYR   A 1 161 ? 5.224  -6.655  3.486   0.48 16.76 ?  161 TYR   A C    1 
ATOM   3728 C C    B TYR   A 1 161 ? 5.231  -6.750  3.534   0.52 17.43 ?  161 TYR   A C    1 
ATOM   3729 O O    A TYR   A 1 161 ? 5.484  -7.863  3.505   0.48 16.61 ?  161 TYR   A O    1 
ATOM   3730 O O    B TYR   A 1 161 ? 5.367  -7.978  3.505   0.52 17.36 ?  161 TYR   A O    1 
ATOM   3731 C CB   A TYR   A 1 161 ? 6.395  -5.047  5.021   0.48 16.04 ?  161 TYR   A CB   1 
ATOM   3732 C CB   B TYR   A 1 161 ? 6.554  -5.099  4.876   0.52 15.92 ?  161 TYR   A CB   1 
ATOM   3733 C CG   A TYR   A 1 161 ? 6.356  -6.109  6.080   0.48 15.64 ?  161 TYR   A CG   1 
ATOM   3734 C CG   B TYR   A 1 161 ? 6.387  -6.008  6.094   0.52 16.14 ?  161 TYR   A CG   1 
ATOM   3735 C CD1  A TYR   A 1 161 ? 7.505  -6.795  6.443   0.48 15.46 ?  161 TYR   A CD1  1 
ATOM   3736 C CD1  B TYR   A 1 161 ? 7.468  -6.708  6.619   0.52 16.48 ?  161 TYR   A CD1  1 
ATOM   3737 C CD2  A TYR   A 1 161 ? 5.165  -6.438  6.713   0.48 15.42 ?  161 TYR   A CD2  1 
ATOM   3738 C CD2  B TYR   A 1 161 ? 5.151  -6.154  6.728   0.52 16.28 ?  161 TYR   A CD2  1 
ATOM   3739 C CE1  A TYR   A 1 161 ? 7.468  -7.776  7.405   0.48 15.16 ?  161 TYR   A CE1  1 
ATOM   3740 C CE1  B TYR   A 1 161 ? 7.324  -7.542  7.724   0.52 16.87 ?  161 TYR   A CE1  1 
ATOM   3741 C CE2  A TYR   A 1 161 ? 5.118  -7.413  7.675   0.48 15.26 ?  161 TYR   A CE2  1 
ATOM   3742 C CE2  B TYR   A 1 161 ? 4.998  -6.985  7.841   0.52 16.74 ?  161 TYR   A CE2  1 
ATOM   3743 C CZ   A TYR   A 1 161 ? 6.273  -8.078  8.019   0.48 15.08 ?  161 TYR   A CZ   1 
ATOM   3744 C CZ   B TYR   A 1 161 ? 6.090  -7.672  8.332   0.52 17.33 ?  161 TYR   A CZ   1 
ATOM   3745 O OH   A TYR   A 1 161 ? 6.227  -9.048  8.986   0.48 14.81 ?  161 TYR   A OH   1 
ATOM   3746 O OH   B TYR   A 1 161 ? 5.959  -8.504  9.429   0.52 18.13 ?  161 TYR   A OH   1 
ATOM   3747 H H    A TYR   A 1 161 ? 6.148  -3.760  2.989   0.48 19.35 ?  161 TYR   A H    1 
ATOM   3748 H H    B TYR   A 1 161 ? 6.386  -4.041  2.679   0.52 18.37 ?  161 TYR   A H    1 
ATOM   3749 H HA   A TYR   A 1 161 ? 7.174  -6.080  3.446   0.48 19.31 ?  161 TYR   A HA   1 
ATOM   3750 H HA   B TYR   A 1 161 ? 7.229  -6.368  3.406   0.52 19.10 ?  161 TYR   A HA   1 
ATOM   3751 H HB2  A TYR   A 1 161 ? 7.223  -4.553  5.130   0.48 19.22 ?  161 TYR   A HB2  1 
ATOM   3752 H HB2  B TYR   A 1 161 ? 7.432  -4.694  4.934   0.52 19.08 ?  161 TYR   A HB2  1 
ATOM   3753 H HB3  A TYR   A 1 161 ? 5.637  -4.460  5.161   0.48 19.22 ?  161 TYR   A HB3  1 
ATOM   3754 H HB3  B TYR   A 1 161 ? 5.871  -4.415  4.923   0.52 19.08 ?  161 TYR   A HB3  1 
ATOM   3755 H HD1  A TYR   A 1 161 ? 8.309  -6.595  6.028   0.48 18.53 ?  161 TYR   A HD1  1 
ATOM   3756 H HD1  B TYR   A 1 161 ? 8.298  -6.628  6.220   0.52 19.76 ?  161 TYR   A HD1  1 
ATOM   3757 H HD2  A TYR   A 1 161 ? 4.382  -5.990  6.481   0.48 18.48 ?  161 TYR   A HD2  1 
ATOM   3758 H HD2  B TYR   A 1 161 ? 4.406  -5.697  6.408   0.52 19.52 ?  161 TYR   A HD2  1 
ATOM   3759 H HE1  A TYR   A 1 161 ? 8.240  -8.236  7.641   0.48 18.17 ?  161 TYR   A HE1  1 
ATOM   3760 H HE1  B TYR   A 1 161 ? 8.057  -8.006  8.064   0.52 20.22 ?  161 TYR   A HE1  1 
ATOM   3761 H HE2  A TYR   A 1 161 ? 4.307  -7.625  8.089   0.48 18.29 ?  161 TYR   A HE2  1 
ATOM   3762 H HE2  B TYR   A 1 161 ? 4.162  -7.077  8.255   0.52 20.06 ?  161 TYR   A HE2  1 
ATOM   3763 H HH   A TYR   A 1 161 ? 5.431  -9.141  9.267   0.48 17.75 ?  161 TYR   A HH   1 
ATOM   3764 H HH   B TYR   A 1 161 ? 5.164  -8.505  9.714   0.52 21.74 ?  161 TYR   A HH   1 
ATOM   3765 N N    A ASP   A 1 162 ? 3.972  -6.201  3.362   0.48 17.38 ?  162 ASP   A N    1 
ATOM   3766 N N    B ASP   A 1 162 ? 4.031  -6.165  3.584   0.52 19.22 ?  162 ASP   A N    1 
ATOM   3767 C CA   A ASP   A 1 162 ? 2.854  -7.142  3.310   0.48 17.76 ?  162 ASP   A CA   1 
ATOM   3768 C CA   B ASP   A 1 162 ? 2.814  -6.968  3.531   0.52 20.38 ?  162 ASP   A CA   1 
ATOM   3769 C C    A ASP   A 1 162 ? 2.909  -7.989  2.044   0.48 17.35 ?  162 ASP   A C    1 
ATOM   3770 C C    B ASP   A 1 162 ? 2.829  -7.899  2.323   0.52 20.60 ?  162 ASP   A C    1 
ATOM   3771 O O    A ASP   A 1 162 ? 2.597  -9.187  2.072   0.48 17.48 ?  162 ASP   A O    1 
ATOM   3772 O O    B ASP   A 1 162 ? 2.371  -9.045  2.405   0.52 20.74 ?  162 ASP   A O    1 
ATOM   3773 C CB   A ASP   A 1 162 ? 1.514  -6.400  3.401   0.48 19.01 ?  162 ASP   A CB   1 
ATOM   3774 C CB   B ASP   A 1 162 ? 1.578  -6.060  3.493   0.52 21.49 ?  162 ASP   A CB   1 
ATOM   3775 C CG   A ASP   A 1 162 ? 1.237  -5.825  4.781   0.48 20.26 ?  162 ASP   A CG   1 
ATOM   3776 C CG   B ASP   A 1 162 ? 1.339  -5.313  4.794   0.52 22.87 ?  162 ASP   A CG   1 
ATOM   3777 O OD1  A ASP   A 1 162 ? 1.879  -6.254  5.760   0.48 20.67 ?  162 ASP   A OD1  1 
ATOM   3778 O OD1  B ASP   A 1 162 ? 1.998  -5.618  5.805   0.52 23.20 ?  162 ASP   A OD1  1 
ATOM   3779 O OD2  A ASP   A 1 162 ? 0.331  -4.965  4.886   0.48 20.91 -1 162 ASP   A OD2  1 
ATOM   3780 O OD2  B ASP   A 1 162 ? 0.471  -4.411  4.795   0.52 24.01 -1 162 ASP   A OD2  1 
ATOM   3781 H H    A ASP   A 1 162 ? 3.742  -5.375  3.306   0.48 20.83 ?  162 ASP   A H    1 
ATOM   3782 H H    B ASP   A 1 162 ? 3.894  -5.319  3.659   0.52 23.04 ?  162 ASP   A H    1 
ATOM   3783 H HA   A ASP   A 1 162 ? 2.903  -7.747  4.066   0.48 21.29 ?  162 ASP   A HA   1 
ATOM   3784 H HA   B ASP   A 1 162 ? 2.755  -7.515  4.331   0.52 24.43 ?  162 ASP   A HA   1 
ATOM   3785 H HB2  A ASP   A 1 162 ? 1.504  -5.675  2.764   0.48 22.79 ?  162 ASP   A HB2  1 
ATOM   3786 H HB2  B ASP   A 1 162 ? 1.688  -5.392  2.808   0.52 25.77 ?  162 ASP   A HB2  1 
ATOM   3787 H HB3  A ASP   A 1 162 ? 0.787  -7.017  3.222   0.48 22.79 ?  162 ASP   A HB3  1 
ATOM   3788 H HB3  B ASP   A 1 162 ? 0.789  -6.597  3.323   0.52 25.77 ?  162 ASP   A HB3  1 
ATOM   3789 N N    A LYS   A 1 163 ? 3.303  -7.381  0.924   0.48 18.19 ?  163 LYS   A N    1 
ATOM   3790 N N    B LYS   A 1 163 ? 3.369  -7.430  1.195   0.52 21.59 ?  163 LYS   A N    1 
ATOM   3791 C CA   A LYS   A 1 163 ? 3.458  -8.135  -0.313  0.48 18.85 ?  163 LYS   A CA   1 
ATOM   3792 C CA   B LYS   A 1 163 ? 3.378  -8.244  -0.018  0.52 22.10 ?  163 LYS   A CA   1 
ATOM   3793 C C    A LYS   A 1 163 ? 4.554  -9.185  -0.183  0.48 17.86 ?  163 LYS   A C    1 
ATOM   3794 C C    B LYS   A 1 163 ? 4.432  -9.348  0.042   0.52 20.32 ?  163 LYS   A C    1 
ATOM   3795 O O    A LYS   A 1 163 ? 4.439  -10.288 -0.731  0.48 17.80 ?  163 LYS   A O    1 
ATOM   3796 O O    B LYS   A 1 163 ? 4.147  -10.506 -0.285  0.52 20.43 ?  163 LYS   A O    1 
ATOM   3797 C CB   A LYS   A 1 163 ? 3.772  -7.173  -1.456  0.48 21.39 ?  163 LYS   A CB   1 
ATOM   3798 C CB   B LYS   A 1 163 ? 3.575  -7.359  -1.248  0.52 24.77 ?  163 LYS   A CB   1 
ATOM   3799 C CG   A LYS   A 1 163 ? 3.787  -7.830  -2.811  0.48 24.35 ?  163 LYS   A CG   1 
ATOM   3800 C CG   B LYS   A 1 163 ? 3.625  -8.133  -2.552  0.52 27.42 ?  163 LYS   A CG   1 
ATOM   3801 C CD   A LYS   A 1 163 ? 4.205  -6.858  -3.886  0.48 27.05 ?  163 LYS   A CD   1 
ATOM   3802 C CD   B LYS   A 1 163 ? 3.350  -7.231  -3.745  0.52 29.72 ?  163 LYS   A CD   1 
ATOM   3803 C CE   A LYS   A 1 163 ? 4.171  -7.520  -5.248  0.48 29.12 ?  163 LYS   A CE   1 
ATOM   3804 C CE   B LYS   A 1 163 ? 4.624  -6.907  -4.505  0.52 31.48 ?  163 LYS   A CE   1 
ATOM   3805 N NZ   A LYS   A 1 163 ? 4.866  -6.706  -6.275  0.48 30.13 ?  163 LYS   A NZ   1 
ATOM   3806 N NZ   B LYS   A 1 163 ? 4.352  -6.149  -5.758  0.52 32.30 ?  163 LYS   A NZ   1 
ATOM   3807 H H    A LYS   A 1 163 ? 3.481  -6.543  0.860   0.48 21.80 ?  163 LYS   A H    1 
ATOM   3808 H H    B LYS   A 1 163 ? 3.726  -6.649  1.108   0.52 25.89 ?  163 LYS   A H    1 
ATOM   3809 H HA   A LYS   A 1 163 ? 2.625  -8.588  -0.518  0.48 22.59 ?  163 LYS   A HA   1 
ATOM   3810 H HA   B LYS   A 1 163 ? 2.513  -8.668  -0.104  0.52 26.50 ?  163 LYS   A HA   1 
ATOM   3811 H HB2  A LYS   A 1 163 ? 3.097  -6.474  -1.469  0.48 25.64 ?  163 LYS   A HB2  1 
ATOM   3812 H HB2  B LYS   A 1 163 ? 2.832  -6.734  -1.301  0.52 29.70 ?  163 LYS   A HB2  1 
ATOM   3813 H HB3  A LYS   A 1 163 ? 4.645  -6.782  -1.302  0.48 25.64 ?  163 LYS   A HB3  1 
ATOM   3814 H HB3  B LYS   A 1 163 ? 4.408  -6.872  -1.160  0.52 29.70 ?  163 LYS   A HB3  1 
ATOM   3815 H HG2  A LYS   A 1 163 ? 4.416  -8.567  -2.804  0.48 29.19 ?  163 LYS   A HG2  1 
ATOM   3816 H HG2  B LYS   A 1 163 ? 4.510  -8.520  -2.659  0.52 32.88 ?  163 LYS   A HG2  1 
ATOM   3817 H HG3  A LYS   A 1 163 ? 2.894  -8.152  -3.019  0.48 29.19 ?  163 LYS   A HG3  1 
ATOM   3818 H HG3  B LYS   A 1 163 ? 2.953  -8.834  -2.535  0.52 32.88 ?  163 LYS   A HG3  1 
ATOM   3819 H HD2  A LYS   A 1 163 ? 3.593  -6.104  -3.894  0.48 32.43 ?  163 LYS   A HD2  1 
ATOM   3820 H HD2  B LYS   A 1 163 ? 2.739  -7.680  -4.348  0.52 35.64 ?  163 LYS   A HD2  1 
ATOM   3821 H HD3  A LYS   A 1 163 ? 5.111  -6.555  -3.710  0.48 32.43 ?  163 LYS   A HD3  1 
ATOM   3822 H HD3  B LYS   A 1 163 ? 2.960  -6.396  -3.436  0.52 35.64 ?  163 LYS   A HD3  1 
ATOM   3823 H HE2  A LYS   A 1 163 ? 4.604  -8.386  -5.196  0.48 34.92 ?  163 LYS   A HE2  1 
ATOM   3824 H HE2  B LYS   A 1 163 ? 5.202  -6.368  -3.943  0.52 37.75 ?  163 LYS   A HE2  1 
ATOM   3825 H HE3  A LYS   A 1 163 ? 3.248  -7.630  -5.520  0.48 34.92 ?  163 LYS   A HE3  1 
ATOM   3826 H HE3  B LYS   A 1 163 ? 5.066  -7.736  -4.742  0.52 37.75 ?  163 LYS   A HE3  1 
ATOM   3827 H HZ1  A LYS   A 1 163 ? 4.831  -7.119  -7.061  0.48 36.13 ?  163 LYS   A HZ1  1 
ATOM   3828 H HZ1  B LYS   A 1 163 ? 5.116  -5.977  -6.180  0.52 38.73 ?  163 LYS   A HZ1  1 
ATOM   3829 H HZ2  A LYS   A 1 163 ? 4.472  -5.912  -6.346  0.48 36.13 ?  163 LYS   A HZ2  1 
ATOM   3830 H HZ2  B LYS   A 1 163 ? 3.827  -6.628  -6.295  0.52 38.73 ?  163 LYS   A HZ2  1 
ATOM   3831 H HZ3  A LYS   A 1 163 ? 5.717  -6.589  -6.044  0.48 36.13 ?  163 LYS   A HZ3  1 
ATOM   3832 H HZ3  B LYS   A 1 163 ? 3.947  -5.381  -5.567  0.52 38.73 ?  163 LYS   A HZ3  1 
ATOM   3833 N N    A LEU   A 1 164 ? 5.634  -8.847  0.531   0.48 16.60 ?  164 LEU   A N    1 
ATOM   3834 N N    B LEU   A 1 164 ? 5.659  -9.008  0.448   0.52 18.64 ?  164 LEU   A N    1 
ATOM   3835 C CA   A LEU   A 1 164 ? 6.746  -9.780  0.717   0.48 15.63 ?  164 LEU   A CA   1 
ATOM   3836 C CA   B LEU   A 1 164 ? 6.700  -10.025 0.581   0.52 17.56 ?  164 LEU   A CA   1 
ATOM   3837 C C    A LEU   A 1 164 ? 6.316  -11.007 1.512   0.48 15.70 ?  164 LEU   A C    1 
ATOM   3838 C C    B LEU   A 1 164 ? 6.258  -11.128 1.532   0.52 17.81 ?  164 LEU   A C    1 
ATOM   3839 O O    A LEU   A 1 164 ? 6.678  -12.140 1.171   0.48 16.12 ?  164 LEU   A O    1 
ATOM   3840 O O    B LEU   A 1 164 ? 6.452  -12.317 1.254   0.52 17.80 ?  164 LEU   A O    1 
ATOM   3841 C CB   A LEU   A 1 164 ? 7.900  -9.065  1.425   0.48 14.80 ?  164 LEU   A CB   1 
ATOM   3842 C CB   B LEU   A 1 164 ? 7.993  -9.389  1.093   0.52 16.38 ?  164 LEU   A CB   1 
ATOM   3843 C CG   A LEU   A 1 164 ? 8.680  -8.040  0.591   0.48 14.47 ?  164 LEU   A CG   1 
ATOM   3844 C CG   B LEU   A 1 164 ? 8.736  -8.423  0.173   0.52 15.69 ?  164 LEU   A CG   1 
ATOM   3845 C CD1  A LEU   A 1 164 ? 9.582  -7.177  1.471   0.48 13.86 ?  164 LEU   A CD1  1 
ATOM   3846 C CD1  B LEU   A 1 164 ? 9.765  -7.651  0.977   0.52 15.28 ?  164 LEU   A CD1  1 
ATOM   3847 C CD2  A LEU   A 1 164 ? 9.500  -8.738  -0.486  0.48 14.59 ?  164 LEU   A CD2  1 
ATOM   3848 C CD2  B LEU   A 1 164 ? 9.413  -9.187  -0.937  0.52 16.21 ?  164 LEU   A CD2  1 
ATOM   3849 H H    A LEU   A 1 164 ? 5.750  -8.079  0.910   0.48 19.90 ?  164 LEU   A H    1 
ATOM   3850 H H    B LEU   A 1 164 ? 5.909  -8.213  0.662   0.52 22.35 ?  164 LEU   A H    1 
ATOM   3851 H HA   A LEU   A 1 164 ? 7.055  -10.078 -0.145  0.48 18.73 ?  164 LEU   A HA   1 
ATOM   3852 H HA   B LEU   A 1 164 ? 6.876  -10.424 -0.283  0.52 21.04 ?  164 LEU   A HA   1 
ATOM   3853 H HB2  A LEU   A 1 164 ? 7.540  -8.595  2.197   0.48 17.74 ?  164 LEU   A HB2  1 
ATOM   3854 H HB2  B LEU   A 1 164 ? 7.787  -8.902  1.903   0.52 19.63 ?  164 LEU   A HB2  1 
ATOM   3855 H HB3  A LEU   A 1 164 ? 8.533  -9.733  1.726   0.48 17.74 ?  164 LEU   A HB3  1 
ATOM   3856 H HB3  B LEU   A 1 164 ? 8.616  -10.104 1.302   0.52 19.63 ?  164 LEU   A HB3  1 
ATOM   3857 H HG   A LEU   A 1 164 ? 8.047  -7.449  0.153   0.48 17.33 ?  164 LEU   A HG   1 
ATOM   3858 H HG   B LEU   A 1 164 ? 8.109  -7.792  -0.216  0.52 18.80 ?  164 LEU   A HG   1 
ATOM   3859 H HD11 A LEU   A 1 164 ? 10.057 -6.542  0.910   0.48 16.61 ?  164 LEU   A HD11 1 
ATOM   3860 H HD11 B LEU   A 1 164 ? 10.246 -7.053  0.386   0.52 18.31 ?  164 LEU   A HD11 1 
ATOM   3861 H HD12 A LEU   A 1 164 ? 9.036  -6.699  2.117   0.48 16.61 ?  164 LEU   A HD12 1 
ATOM   3862 H HD12 B LEU   A 1 164 ? 9.312  -7.144  1.669   0.52 18.31 ?  164 LEU   A HD12 1 
ATOM   3863 H HD13 A LEU   A 1 164 ? 10.216 -7.747  1.933   0.48 16.61 ?  164 LEU   A HD13 1 
ATOM   3864 H HD13 B LEU   A 1 164 ? 10.383 -8.282  1.384   0.52 18.31 ?  164 LEU   A HD13 1 
ATOM   3865 H HD21 A LEU   A 1 164 ? 10.045 -8.079  -0.943  0.48 17.48 ?  164 LEU   A HD21 1 
ATOM   3866 H HD21 B LEU   A 1 164 ? 9.887  -8.562  -1.506  0.52 19.43 ?  164 LEU   A HD21 1 
ATOM   3867 H HD22 A LEU   A 1 164 ? 10.064 -9.406  -0.069  0.48 17.48 ?  164 LEU   A HD22 1 
ATOM   3868 H HD22 B LEU   A 1 164 ? 10.036 -9.820  -0.546  0.52 19.43 ?  164 LEU   A HD22 1 
ATOM   3869 H HD23 A LEU   A 1 164 ? 8.894  -9.160  -1.116  0.48 17.48 ?  164 LEU   A HD23 1 
ATOM   3870 H HD23 B LEU   A 1 164 ? 8.738  -9.659  -1.449  0.52 19.43 ?  164 LEU   A HD23 1 
ATOM   3871 N N    A VAL   A 1 165 ? 5.560  -10.794 2.588   0.48 15.30 ?  165 VAL   A N    1 
ATOM   3872 N N    B VAL   A 1 165 ? 5.668  -10.746 2.665   0.52 18.41 ?  165 VAL   A N    1 
ATOM   3873 C CA   A VAL   A 1 165 ? 5.129  -11.892 3.448   0.48 15.15 ?  165 VAL   A CA   1 
ATOM   3874 C CA   B VAL   A 1 165 ? 5.174  -11.728 3.626   0.52 19.22 ?  165 VAL   A CA   1 
ATOM   3875 C C    A VAL   A 1 165 ? 4.126  -12.781 2.719   0.48 15.24 ?  165 VAL   A C    1 
ATOM   3876 C C    B VAL   A 1 165 ? 4.046  -12.543 3.011   0.52 20.56 ?  165 VAL   A C    1 
ATOM   3877 O O    A VAL   A 1 165 ? 4.243  -14.012 2.706   0.48 15.34 ?  165 VAL   A O    1 
ATOM   3878 O O    B VAL   A 1 165 ? 4.087  -13.779 2.984   0.52 20.51 ?  165 VAL   A O    1 
ATOM   3879 C CB   A VAL   A 1 165 ? 4.531  -11.318 4.747   0.48 15.43 ?  165 VAL   A CB   1 
ATOM   3880 C CB   B VAL   A 1 165 ? 4.719  -11.026 4.918   0.52 19.26 ?  165 VAL   A CB   1 
ATOM   3881 C CG1  A VAL   A 1 165 ? 3.833  -12.405 5.554   0.48 15.94 ?  165 VAL   A CG1  1 
ATOM   3882 C CG1  B VAL   A 1 165 ? 3.930  -11.987 5.798   0.52 19.35 ?  165 VAL   A CG1  1 
ATOM   3883 C CG2  A VAL   A 1 165 ? 5.605  -10.620 5.572   0.48 15.39 ?  165 VAL   A CG2  1 
ATOM   3884 C CG2  B VAL   A 1 165 ? 5.914  -10.465 5.664   0.52 19.50 ?  165 VAL   A CG2  1 
ATOM   3885 H H    A VAL   A 1 165 ? 5.277  -10.026 2.848   0.48 18.33 ?  165 VAL   A H    1 
ATOM   3886 H H    B VAL   A 1 165 ? 5.535  -9.931  2.894   0.52 22.06 ?  165 VAL   A H    1 
ATOM   3887 H HA   A VAL   A 1 165 ? 5.892  -12.439 3.686   0.48 18.15 ?  165 VAL   A HA   1 
ATOM   3888 H HA   B VAL   A 1 165 ? 5.890  -12.338 3.857   0.52 23.04 ?  165 VAL   A HA   1 
ATOM   3889 H HB   A VAL   A 1 165 ? 3.862  -10.658 4.516   0.48 18.49 ?  165 VAL   A HB   1 
ATOM   3890 H HB   B VAL   A 1 165 ? 4.135  -10.286 4.689   0.52 23.08 ?  165 VAL   A HB   1 
ATOM   3891 H HG11 A VAL   A 1 165 ? 3.682  -12.079 6.456   0.48 19.11 ?  165 VAL   A HG11 1 
ATOM   3892 H HG11 B VAL   A 1 165 ? 3.908  -11.639 6.702   0.52 23.19 ?  165 VAL   A HG11 1 
ATOM   3893 H HG12 A VAL   A 1 165 ? 2.980  -12.615 5.137   0.48 19.11 ?  165 VAL   A HG12 1 
ATOM   3894 H HG12 B VAL   A 1 165 ? 3.025  -12.065 5.454   0.52 23.19 ?  165 VAL   A HG12 1 
ATOM   3895 H HG13 A VAL   A 1 165 ? 4.394  -13.193 5.578   0.48 19.11 ?  165 VAL   A HG13 1 
ATOM   3896 H HG13 B VAL   A 1 165 ? 4.365  -12.853 5.788   0.52 23.19 ?  165 VAL   A HG13 1 
ATOM   3897 H HG21 A VAL   A 1 165 ? 5.206  -10.276 6.388   0.48 18.44 ?  165 VAL   A HG21 1 
ATOM   3898 H HG21 B VAL   A 1 165 ? 5.603  -10.025 6.470   0.52 23.37 ?  165 VAL   A HG21 1 
ATOM   3899 H HG22 A VAL   A 1 165 ? 6.304  -11.255 5.789   0.48 18.44 ?  165 VAL   A HG22 1 
ATOM   3900 H HG22 B VAL   A 1 165 ? 6.511  -11.194 5.892   0.52 23.37 ?  165 VAL   A HG22 1 
ATOM   3901 H HG23 A VAL   A 1 165 ? 5.973  -9.887  5.052   0.48 18.44 ?  165 VAL   A HG23 1 
ATOM   3902 H HG23 B VAL   A 1 165 ? 6.369  -9.829  5.092   0.52 23.37 ?  165 VAL   A HG23 1 
ATOM   3903 N N    A SER   A 1 166 ? 3.114  -12.167 2.113   0.48 15.69 ?  166 SER   A N    1 
ATOM   3904 N N    B SER   A 1 166 ? 3.013  -11.858 2.518   0.52 22.39 ?  166 SER   A N    1 
ATOM   3905 C CA   A SER   A 1 166 ? 2.013  -12.921 1.527   0.48 17.36 ?  166 SER   A CA   1 
ATOM   3906 C CA   B SER   A 1 166 ? 1.871  -12.566 1.954   0.52 23.76 ?  166 SER   A CA   1 
ATOM   3907 C C    A SER   A 1 166 ? 2.444  -13.723 0.310   0.48 18.08 ?  166 SER   A C    1 
ATOM   3908 C C    B SER   A 1 166 ? 2.284  -13.437 0.777   0.52 24.74 ?  166 SER   A C    1 
ATOM   3909 O O    A SER   A 1 166 ? 1.785  -14.711 -0.035  0.48 19.20 ?  166 SER   A O    1 
ATOM   3910 O O    B SER   A 1 166 ? 1.711  -14.514 0.575   0.52 25.47 ?  166 SER   A O    1 
ATOM   3911 C CB   A SER   A 1 166 ? 0.879  -11.962 1.144   0.48 18.67 ?  166 SER   A CB   1 
ATOM   3912 C CB   B SER   A 1 166 ? 0.789  -11.570 1.532   0.52 24.29 ?  166 SER   A CB   1 
ATOM   3913 O OG   A SER   A 1 166 ? 0.428  -11.213 2.267   0.48 20.58 ?  166 SER   A OG   1 
ATOM   3914 O OG   B SER   A 1 166 ? 1.155  -10.902 0.340   0.52 24.67 ?  166 SER   A OG   1 
ATOM   3915 H H    A SER   A 1 166 ? 3.022  -11.327 2.051   0.48 18.80 ?  166 SER   A H    1 
ATOM   3916 H H    B SER   A 1 166 ? 2.945  -11.002 2.509   0.52 26.85 ?  166 SER   A H    1 
ATOM   3917 H HA   A SER   A 1 166 ? 1.651  -13.548 2.180   0.48 20.81 ?  166 SER   A HA   1 
ATOM   3918 H HA   B SER   A 1 166 ? 1.486  -13.144 2.631   0.52 28.49 ?  166 SER   A HA   1 
ATOM   3919 H HB2  A SER   A 1 166 ? 1.200  -11.351 0.463   0.48 22.38 ?  166 SER   A HB2  1 
ATOM   3920 H HB2  B SER   A 1 166 ? -0.044 -12.047 1.382   0.52 29.12 ?  166 SER   A HB2  1 
ATOM   3921 H HB3  A SER   A 1 166 ? 0.127  -12.473 0.797   0.48 22.38 ?  166 SER   A HB3  1 
ATOM   3922 H HB3  B SER   A 1 166 ? 0.665  -10.915 2.243   0.52 29.12 ?  166 SER   A HB3  1 
ATOM   3923 H HG   A SER   A 1 166 ? 1.062  -10.745 2.573   0.48 24.67 ?  166 SER   A HG   1 
ATOM   3924 H HG   B SER   A 1 166 ? 1.925  -10.574 0.425   0.52 29.58 ?  166 SER   A HG   1 
ATOM   3925 N N    A SER   A 1 167 ? 3.533  -13.328 -0.341  0.48 17.97 ?  167 SER   A N    1 
ATOM   3926 N N    B SER   A 1 167 ? 3.278  -13.007 0.002   0.52 25.49 ?  167 SER   A N    1 
ATOM   3927 C CA   A SER   A 1 167 ? 4.038  -14.033 -1.507  0.48 18.66 ?  167 SER   A CA   1 
ATOM   3928 C CA   B SER   A 1 167 ? 3.696  -13.769 -1.168  0.52 26.21 ?  167 SER   A CA   1 
ATOM   3929 C C    A SER   A 1 167 ? 5.208  -14.947 -1.181  0.48 19.01 ?  167 SER   A C    1 
ATOM   3930 C C    B SER   A 1 167 ? 4.857  -14.715 -0.890  0.52 26.77 ?  167 SER   A C    1 
ATOM   3931 O O    A SER   A 1 167 ? 5.751  -15.579 -2.092  0.48 18.95 ?  167 SER   A O    1 
ATOM   3932 O O    B SER   A 1 167 ? 5.239  -15.476 -1.785  0.52 26.90 ?  167 SER   A O    1 
ATOM   3933 C CB   A SER   A 1 167 ? 4.449  -13.032 -2.594  0.48 18.99 ?  167 SER   A CB   1 
ATOM   3934 C CB   B SER   A 1 167 ? 4.062  -12.832 -2.326  0.52 26.79 ?  167 SER   A CB   1 
ATOM   3935 O OG   A SER   A 1 167 ? 5.560  -12.255 -2.183  0.48 18.95 ?  167 SER   A OG   1 
ATOM   3936 O OG   B SER   A 1 167 ? 5.165  -12.010 -1.992  0.52 27.15 ?  167 SER   A OG   1 
ATOM   3937 H H    A SER   A 1 167 ? 3.998  -12.640 -0.121  0.48 21.54 ?  167 SER   A H    1 
ATOM   3938 H H    B SER   A 1 167 ? 3.722  -12.275 0.134   0.52 30.56 ?  167 SER   A H    1 
ATOM   3939 H HA   A SER   A 1 167 ? 3.336  -14.588 -1.869  0.48 22.36 ?  167 SER   A HA   1 
ATOM   3940 H HA   B SER   A 1 167 ? 2.944  -14.305 -1.460  0.52 31.43 ?  167 SER   A HA   1 
ATOM   3941 H HB2  A SER   A 1 167 ? 4.683  -13.520 -3.399  0.48 22.76 ?  167 SER   A HB2  1 
ATOM   3942 H HB2  B SER   A 1 167 ? 4.293  -13.373 -3.100  0.52 32.12 ?  167 SER   A HB2  1 
ATOM   3943 H HB3  A SER   A 1 167 ? 3.699  -12.441 -2.774  0.48 22.76 ?  167 SER   A HB3  1 
ATOM   3944 H HB3  B SER   A 1 167 ? 3.298  -12.270 -2.535  0.52 32.12 ?  167 SER   A HB3  1 
ATOM   3945 H HG   A SER   A 1 167 ? 5.368  -11.828 -1.486  0.48 22.72 ?  167 SER   A HG   1 
ATOM   3946 H HG   B SER   A 1 167 ? 4.992  -11.568 -1.299  0.52 32.56 ?  167 SER   A HG   1 
ATOM   3947 N N    A PHE   A 1 168 ? 5.606  -15.045 0.086   0.48 19.45 ?  168 PHE   A N    1 
ATOM   3948 N N    B PHE   A 1 168 ? 5.425  -14.699 0.314   0.52 27.41 ?  168 PHE   A N    1 
ATOM   3949 C CA   A PHE   A 1 168 ? 6.801  -15.809 0.419   0.48 20.75 ?  168 PHE   A CA   1 
ATOM   3950 C CA   B PHE   A 1 168 ? 6.567  -15.559 0.586   0.52 28.52 ?  168 PHE   A CA   1 
ATOM   3951 C C    A PHE   A 1 168 ? 6.523  -17.301 0.322   0.48 24.52 ?  168 PHE   A C    1 
ATOM   3952 C C    B PHE   A 1 168 ? 6.149  -17.019 0.581   0.52 32.24 ?  168 PHE   A C    1 
ATOM   3953 O O    A PHE   A 1 168 ? 5.570  -17.812 0.920   0.48 25.43 ?  168 PHE   A O    1 
ATOM   3954 O O    B PHE   A 1 168 ? 5.121  -17.392 1.155   0.52 32.97 ?  168 PHE   A O    1 
ATOM   3955 C CB   A PHE   A 1 168 ? 7.309  -15.477 1.820   0.48 19.05 ?  168 PHE   A CB   1 
ATOM   3956 C CB   B PHE   A 1 168 ? 7.199  -15.238 1.937   0.52 26.04 ?  168 PHE   A CB   1 
ATOM   3957 C CG   A PHE   A 1 168 ? 8.577  -16.205 2.175   0.48 17.51 ?  168 PHE   A CG   1 
ATOM   3958 C CG   B PHE   A 1 168 ? 8.457  -16.017 2.201   0.52 23.83 ?  168 PHE   A CG   1 
ATOM   3959 C CD1  A PHE   A 1 168 ? 9.787  -15.789 1.651   0.48 16.92 ?  168 PHE   A CD1  1 
ATOM   3960 C CD1  B PHE   A 1 168 ? 9.561  -15.853 1.383   0.52 22.87 ?  168 PHE   A CD1  1 
ATOM   3961 C CD2  A PHE   A 1 168 ? 8.563  -17.319 3.003   0.48 16.70 ?  168 PHE   A CD2  1 
ATOM   3962 C CD2  B PHE   A 1 168 ? 8.536  -16.916 3.251   0.52 22.83 ?  168 PHE   A CD2  1 
ATOM   3963 C CE1  A PHE   A 1 168 ? 10.957 -16.456 1.952   0.48 16.31 ?  168 PHE   A CE1  1 
ATOM   3964 C CE1  B PHE   A 1 168 ? 10.721 -16.565 1.608   0.52 22.06 ?  168 PHE   A CE1  1 
ATOM   3965 C CE2  A PHE   A 1 168 ? 9.741  -17.991 3.312   0.48 16.35 ?  168 PHE   A CE2  1 
ATOM   3966 C CE2  B PHE   A 1 168 ? 9.697  -17.632 3.483   0.52 22.13 ?  168 PHE   A CE2  1 
ATOM   3967 C CZ   A PHE   A 1 168 ? 10.935 -17.558 2.784   0.48 16.49 ?  168 PHE   A CZ   1 
ATOM   3968 C CZ   B PHE   A 1 168 ? 10.790 -17.455 2.658   0.52 21.98 ?  168 PHE   A CZ   1 
ATOM   3969 H H    A PHE   A 1 168 ? 5.217  -14.683 0.757   0.48 23.31 ?  168 PHE   A H    1 
ATOM   3970 H H    B PHE   A 1 168 ? 5.175  -14.206 0.975   0.52 32.87 ?  168 PHE   A H    1 
ATOM   3971 H HA   A PHE   A 1 168 ? 7.511  -15.590 -0.212  0.48 24.87 ?  168 PHE   A HA   1 
ATOM   3972 H HA   B PHE   A 1 168 ? 7.232  -15.429 -0.107  0.52 34.20 ?  168 PHE   A HA   1 
ATOM   3973 H HB2  A PHE   A 1 168 ? 7.492  -14.524 1.877   0.48 22.84 ?  168 PHE   A HB2  1 
ATOM   3974 H HB2  B PHE   A 1 168 ? 7.425  -14.299 1.967   0.52 31.22 ?  168 PHE   A HB2  1 
ATOM   3975 H HB3  A PHE   A 1 168 ? 6.637  -15.725 2.469   0.48 22.84 ?  168 PHE   A HB3  1 
ATOM   3976 H HB3  B PHE   A 1 168 ? 6.561  -15.449 2.639   0.52 31.22 ?  168 PHE   A HB3  1 
ATOM   3977 H HD1  A PHE   A 1 168 ? 9.823  -15.048 1.092   0.48 20.28 ?  168 PHE   A HD1  1 
ATOM   3978 H HD1  B PHE   A 1 168 ? 9.520  -15.255 0.670   0.52 27.41 ?  168 PHE   A HD1  1 
ATOM   3979 H HD2  A PHE   A 1 168 ? 7.760  -17.617 3.359   0.48 20.01 ?  168 PHE   A HD2  1 
ATOM   3980 H HD2  B PHE   A 1 168 ? 7.801  -17.039 3.808   0.52 27.37 ?  168 PHE   A HD2  1 
ATOM   3981 H HE1  A PHE   A 1 168 ? 11.772 -16.161 1.599   0.48 19.55 ?  168 PHE   A HE1  1 
ATOM   3982 H HE1  B PHE   A 1 168 ? 11.456 -16.444 1.050   0.52 26.45 ?  168 PHE   A HE1  1 
ATOM   3983 H HE2  A PHE   A 1 168 ? 9.724  -18.738 3.869   0.48 19.60 ?  168 PHE   A HE2  1 
ATOM   3984 H HE2  B PHE   A 1 168 ? 9.741  -18.232 4.191   0.52 26.53 ?  168 PHE   A HE2  1 
ATOM   3985 H HZ   A PHE   A 1 168 ? 11.730 -18.007 2.988   0.48 19.77 ?  168 PHE   A HZ   1 
ATOM   3986 H HZ   B PHE   A 1 168 ? 11.571 -17.934 2.811   0.52 26.36 ?  168 PHE   A HZ   1 
ATOM   3987 N N    A LEU   A 1 169 ? 7.371  -18.001 -0.422  0.48 27.34 ?  169 LEU   A N    1 
ATOM   3988 N N    B LEU   A 1 169 ? 6.962  -17.849 -0.058  0.52 34.92 ?  169 LEU   A N    1 
ATOM   3989 C CA   A LEU   A 1 169 ? 7.229  -19.437 -0.571  0.48 30.49 ?  169 LEU   A CA   1 
ATOM   3990 C CA   B LEU   A 1 169 ? 6.708  -19.274 -0.078  0.52 37.34 ?  169 LEU   A CA   1 
ATOM   3991 C C    A LEU   A 1 169 ? 8.156  -20.169 0.390   0.48 31.76 ?  169 LEU   A C    1 
ATOM   3992 C C    B LEU   A 1 169 ? 7.523  -19.964 1.011   0.52 38.17 ?  169 LEU   A C    1 
ATOM   3993 O O    A LEU   A 1 169 ? 7.714  -20.746 1.385   0.48 32.32 ?  169 LEU   A O    1 
ATOM   3994 O O    B LEU   A 1 169 ? 6.964  -20.547 1.941   0.52 38.41 ?  169 LEU   A O    1 
ATOM   3995 C CB   A LEU   A 1 169 ? 7.544  -19.852 -2.006  0.48 31.75 ?  169 LEU   A CB   1 
ATOM   3996 C CB   B LEU   A 1 169 ? 7.056  -19.865 -1.453  0.52 38.55 ?  169 LEU   A CB   1 
ATOM   3997 C CG   A LEU   A 1 169 ? 7.158  -21.286 -2.368  0.48 32.75 ?  169 LEU   A CG   1 
ATOM   3998 C CG   B LEU   A 1 169 ? 5.889  -20.318 -2.338  0.52 39.41 ?  169 LEU   A CG   1 
ATOM   3999 C CD1  A LEU   A 1 169 ? 5.726  -21.573 -1.945  0.48 33.19 ?  169 LEU   A CD1  1 
ATOM   4000 C CD1  B LEU   A 1 169 ? 4.709  -20.781 -1.487  0.52 39.63 ?  169 LEU   A CD1  1 
ATOM   4001 C CD2  A LEU   A 1 169 ? 7.331  -21.513 -3.859  0.48 32.99 ?  169 LEU   A CD2  1 
ATOM   4002 C CD2  B LEU   A 1 169 ? 5.469  -19.227 -3.317  0.52 39.68 ?  169 LEU   A CD2  1 
ATOM   4003 O OXT  A LEU   A 1 169 ? 9.371  -20.195 0.196   0.48 31.68 -1 169 LEU   A OXT  1 
ATOM   4004 O OXT  B LEU   A 1 169 ? 8.756  -19.944 0.994   0.52 38.47 -1 169 LEU   A OXT  1 
ATOM   4005 H H    A LEU   A 1 169 ? 8.031  -17.661 -0.860  0.48 32.79 ?  169 LEU   A H    1 
ATOM   4006 H H    B LEU   A 1 169 ? 7.665  -17.609 -0.487  0.52 41.87 ?  169 LEU   A H    1 
ATOM   4007 H HA   A LEU   A 1 169 ? 6.310  -19.671 -0.364  0.48 36.56 ?  169 LEU   A HA   1 
ATOM   4008 H HA   B LEU   A 1 169 ? 5.767  -19.403 0.120   0.52 44.79 ?  169 LEU   A HA   1 
ATOM   4009 H HB2  A LEU   A 1 169 ? 7.073  -19.261 -2.611  0.48 38.08 ?  169 LEU   A HB2  1 
ATOM   4010 H HB2  B LEU   A 1 169 ? 7.552  -19.195 -1.957  0.52 46.24 ?  169 LEU   A HB2  1 
ATOM   4011 H HB3  A LEU   A 1 169 ? 8.501  -19.763 -2.144  0.48 38.08 ?  169 LEU   A HB3  1 
ATOM   4012 H HB3  B LEU   A 1 169 ? 7.625  -20.639 -1.317  0.52 46.24 ?  169 LEU   A HB3  1 
ATOM   4013 H HG   A LEU   A 1 169 ? 7.742  -21.903 -1.897  0.48 39.28 ?  169 LEU   A HG   1 
ATOM   4014 H HG   B LEU   A 1 169 ? 6.180  -21.079 -2.864  0.52 47.27 ?  169 LEU   A HG   1 
ATOM   4015 H HD11 A LEU   A 1 169 ? 5.406  -22.349 -2.425  0.48 39.81 ?  169 LEU   A HD11 1 
ATOM   4016 H HD11 B LEU   A 1 169 ? 4.139  -21.337 -2.022  0.52 47.53 ?  169 LEU   A HD11 1 
ATOM   4017 H HD12 A LEU   A 1 169 ? 5.706  -21.741 -0.989  0.48 39.81 ?  169 LEU   A HD12 1 
ATOM   4018 H HD12 B LEU   A 1 169 ? 5.047  -21.285 -0.726  0.52 47.53 ?  169 LEU   A HD12 1 
ATOM   4019 H HD13 A LEU   A 1 169 ? 5.176  -20.801 -2.158  0.48 39.81 ?  169 LEU   A HD13 1 
ATOM   4020 H HD13 B LEU   A 1 169 ? 4.217  -20.001 -1.175  0.52 47.53 ?  169 LEU   A HD13 1 
ATOM   4021 H HD21 A LEU   A 1 169 ? 7.093  -22.429 -4.068  0.48 39.56 ?  169 LEU   A HD21 1 
ATOM   4022 H HD21 B LEU   A 1 169 ? 4.806  -19.590 -3.927  0.52 47.59 ?  169 LEU   A HD21 1 
ATOM   4023 H HD22 A LEU   A 1 169 ? 6.751  -20.901 -4.339  0.48 39.56 ?  169 LEU   A HD22 1 
ATOM   4024 H HD22 B LEU   A 1 169 ? 5.092  -18.484 -2.822  0.52 47.59 ?  169 LEU   A HD22 1 
ATOM   4025 H HD23 A LEU   A 1 169 ? 8.256  -21.347 -4.097  0.48 39.56 ?  169 LEU   A HD23 1 
ATOM   4026 H HD23 B LEU   A 1 169 ? 6.247  -18.933 -3.818  0.52 47.59 ?  169 LEU   A HD23 1 
ATOM   4027 N N    A SER   B 1 1   ? 50.850 -9.229  -23.655 0.48 27.24 ?  1   SER   B N    1 
ATOM   4028 N N    B SER   B 1 1   ? 50.829 -9.395  -23.645 0.52 25.47 ?  1   SER   B N    1 
ATOM   4029 C CA   A SER   B 1 1   ? 51.397 -10.305 -22.804 0.48 27.28 ?  1   SER   B CA   1 
ATOM   4030 C CA   B SER   B 1 1   ? 51.304 -10.380 -22.647 0.52 25.40 ?  1   SER   B CA   1 
ATOM   4031 C C    A SER   B 1 1   ? 50.350 -11.380 -22.562 0.48 26.44 ?  1   SER   B C    1 
ATOM   4032 C C    B SER   B 1 1   ? 50.281 -11.492 -22.444 0.52 24.31 ?  1   SER   B C    1 
ATOM   4033 O O    A SER   B 1 1   ? 49.157 -11.183 -22.814 0.48 26.55 ?  1   SER   B O    1 
ATOM   4034 O O    B SER   B 1 1   ? 49.077 -11.315 -22.678 0.52 24.57 ?  1   SER   B O    1 
ATOM   4035 C CB   A SER   B 1 1   ? 51.884 -9.743  -21.471 0.48 27.95 ?  1   SER   B CB   1 
ATOM   4036 C CB   B SER   B 1 1   ? 51.589 -9.695  -21.315 0.52 26.32 ?  1   SER   B CB   1 
ATOM   4037 O OG   A SER   B 1 1   ? 50.799 -9.484  -20.600 0.48 29.16 ?  1   SER   B OG   1 
ATOM   4038 O OG   B SER   B 1 1   ? 50.382 -9.362  -20.653 0.52 27.68 ?  1   SER   B OG   1 
ATOM   4039 H H1   A SER   B 1 1   ? 50.741 -9.541  -24.480 0.48 32.66 ?  1   SER   B H1   1 
ATOM   4040 H H1   B SER   B 1 1   ? 50.878 -9.755  -24.456 0.52 30.54 ?  1   SER   B H1   1 
ATOM   4041 H H2   A SER   B 1 1   ? 50.070 -8.968  -23.325 0.48 32.66 ?  1   SER   B H2   1 
ATOM   4042 H H2   B SER   B 1 1   ? 49.989 -9.178  -23.462 0.52 30.54 ?  1   SER   B H2   1 
ATOM   4043 H H3   A SER   B 1 1   ? 51.421 -8.551  -23.661 0.48 32.66 ?  1   SER   B H3   1 
ATOM   4044 H H3   B SER   B 1 1   ? 51.344 -8.673  -23.605 0.52 30.54 ?  1   SER   B H3   1 
ATOM   4045 H HA   A SER   B 1 1   ? 52.147 -10.704 -23.262 0.48 32.71 ?  1   SER   B HA   1 
ATOM   4046 H HA   B SER   B 1 1   ? 52.125 -10.768 -22.978 0.52 30.45 ?  1   SER   B HA   1 
ATOM   4047 H HB2  A SER   B 1 1   ? 52.466 -10.395 -21.057 0.48 33.52 ?  1   SER   B HB2  1 
ATOM   4048 H HB2  B SER   B 1 1   ? 52.097 -10.304 -20.761 0.52 31.56 ?  1   SER   B HB2  1 
ATOM   4049 H HB3  A SER   B 1 1   ? 52.369 -8.919  -21.636 0.48 33.52 ?  1   SER   B HB3  1 
ATOM   4050 H HB3  B SER   B 1 1   ? 52.100 -8.886  -21.479 0.52 31.56 ?  1   SER   B HB3  1 
ATOM   4051 H HG   A SER   B 1 1   ? 51.081 -9.113  -19.900 0.48 34.97 ?  1   SER   B HG   1 
ATOM   4052 H HG   B SER   B 1 1   ? 50.557 -8.947  -19.942 0.52 33.20 ?  1   SER   B HG   1 
ATOM   4053 N N    A MET   B 1 2   ? 50.813 -12.519 -22.064 0.48 25.61 ?  2   MET   B N    1 
ATOM   4054 N N    B MET   B 1 2   ? 50.773 -12.645 -22.009 0.52 23.32 ?  2   MET   B N    1 
ATOM   4055 C CA   A MET   B 1 2   ? 49.988 -13.702 -21.877 0.48 25.38 ?  2   MET   B CA   1 
ATOM   4056 C CA   B MET   B 1 2   ? 49.968 -13.854 -21.880 0.52 23.26 ?  2   MET   B CA   1 
ATOM   4057 C C    A MET   B 1 2   ? 49.725 -13.871 -20.387 0.48 22.57 ?  2   MET   B C    1 
ATOM   4058 C C    B MET   B 1 2   ? 49.673 -14.103 -20.409 0.52 22.10 ?  2   MET   B C    1 
ATOM   4059 O O    A MET   B 1 2   ? 50.664 -14.031 -19.602 0.48 21.94 ?  2   MET   B O    1 
ATOM   4060 O O    B MET   B 1 2   ? 50.530 -14.588 -19.668 0.52 22.75 ?  2   MET   B O    1 
ATOM   4061 C CB   A MET   B 1 2   ? 50.705 -14.917 -22.461 0.48 28.80 ?  2   MET   B CB   1 
ATOM   4062 C CB   B MET   B 1 2   ? 50.722 -15.023 -22.477 0.52 25.38 ?  2   MET   B CB   1 
ATOM   4063 C CG   A MET   B 1 2   ? 49.846 -16.162 -22.588 0.48 32.06 ?  2   MET   B CG   1 
ATOM   4064 C CG   B MET   B 1 2   ? 49.864 -16.245 -22.793 0.52 27.10 ?  2   MET   B CG   1 
ATOM   4065 S SD   A MET   B 1 2   ? 50.671 -17.424 -23.574 0.48 35.17 ?  2   MET   B SD   1 
ATOM   4066 S SD   B MET   B 1 2   ? 50.694 -17.277 -24.011 0.52 28.63 ?  2   MET   B SD   1 
ATOM   4067 C CE   A MET   B 1 2   ? 51.174 -16.429 -24.974 0.48 35.68 ?  2   MET   B CE   1 
ATOM   4068 C CE   B MET   B 1 2   ? 51.391 -16.004 -25.035 0.52 29.53 ?  2   MET   B CE   1 
ATOM   4069 H H    A MET   B 1 2   ? 51.630 -12.637 -21.816 0.48 30.70 ?  2   MET   B H    1 
ATOM   4070 H H    B MET   B 1 2   ? 51.603 -12.761 -21.789 0.52 27.96 ?  2   MET   B H    1 
ATOM   4071 H HA   A MET   B 1 2   ? 49.150 -13.601 -22.352 0.48 30.43 ?  2   MET   B HA   1 
ATOM   4072 H HA   B MET   B 1 2   ? 49.141 -13.748 -22.371 0.52 27.89 ?  2   MET   B HA   1 
ATOM   4073 H HB2  A MET   B 1 2   ? 51.021 -14.661 -23.343 0.48 34.54 ?  2   MET   B HB2  1 
ATOM   4074 H HB2  B MET   B 1 2   ? 51.150 -14.657 -23.257 0.52 30.43 ?  2   MET   B HB2  1 
ATOM   4075 H HB3  A MET   B 1 2   ? 51.460 -15.150 -21.906 0.48 34.54 ?  2   MET   B HB3  1 
ATOM   4076 H HB3  B MET   B 1 2   ? 51.396 -15.329 -21.869 0.52 30.43 ?  2   MET   B HB3  1 
ATOM   4077 H HG2  A MET   B 1 2   ? 49.677 -16.526 -21.702 0.48 38.45 ?  2   MET   B HG2  1 
ATOM   4078 H HG2  B MET   B 1 2   ? 49.728 -16.771 -21.977 0.52 32.50 ?  2   MET   B HG2  1 
ATOM   4079 H HG3  A MET   B 1 2   ? 49.010 -15.938 -23.025 0.48 38.45 ?  2   MET   B HG3  1 
ATOM   4080 H HG3  B MET   B 1 2   ? 49.007 -15.974 -23.158 0.52 32.50 ?  2   MET   B HG3  1 
ATOM   4081 H HE1  A MET   B 1 2   ? 51.304 -17.003 -25.733 0.48 42.79 ?  2   MET   B HE1  1 
ATOM   4082 H HE1  B MET   B 1 2   ? 51.497 -16.383 -25.890 0.52 35.41 ?  2   MET   B HE1  1 
ATOM   4083 H HE2  A MET   B 1 2   ? 50.476 -15.777 -25.162 0.48 42.79 ?  2   MET   B HE2  1 
ATOM   4084 H HE2  B MET   B 1 2   ? 50.770 -15.255 -25.095 0.52 35.41 ?  2   MET   B HE2  1 
ATOM   4085 H HE3  A MET   B 1 2   ? 52.003 -15.965 -24.758 0.48 42.79 ?  2   MET   B HE3  1 
ATOM   4086 H HE3  B MET   B 1 2   ? 52.252 -15.710 -24.665 0.52 35.41 ?  2   MET   B HE3  1 
ATOM   4087 N N    . VAL   B 1 3   ? 48.451 -13.796 -20.000 1.00 20.29 ?  3   VAL   B N    1 
ATOM   4088 C CA   . VAL   B 1 3   ? 48.021 -13.996 -18.623 1.00 18.76 ?  3   VAL   B CA   1 
ATOM   4089 C C    . VAL   B 1 3   ? 46.785 -14.881 -18.631 1.00 17.10 ?  3   VAL   B C    1 
ATOM   4090 O O    . VAL   B 1 3   ? 46.058 -14.966 -19.623 1.00 17.59 ?  3   VAL   B O    1 
ATOM   4091 C CB   . VAL   B 1 3   ? 47.728 -12.665 -17.903 1.00 20.53 ?  3   VAL   B CB   1 
ATOM   4092 C CG1  . VAL   B 1 3   ? 48.992 -11.809 -17.795 1.00 21.08 ?  3   VAL   B CG1  1 
ATOM   4093 C CG2  . VAL   B 1 3   ? 46.611 -11.919 -18.619 1.00 21.15 ?  3   VAL   B CG2  1 
ATOM   4094 H H    A VAL   B 1 3   ? 47.806 -13.620 -20.542 0.48 24.32 ?  3   VAL   B H    1 
ATOM   4095 H H    B VAL   B 1 3   ? 47.839 -13.490 -20.520 0.52 24.32 ?  3   VAL   B H    1 
ATOM   4096 H HA   . VAL   B 1 3   ? 48.721 -14.460 -18.138 1.00 22.49 ?  3   VAL   B HA   1 
ATOM   4097 H HB   . VAL   B 1 3   ? 47.424 -12.871 -17.005 1.00 24.61 ?  3   VAL   B HB   1 
ATOM   4098 H HG11 . VAL   B 1 3   ? 48.770 -10.991 -17.328 1.00 25.27 ?  3   VAL   B HG11 1 
ATOM   4099 H HG12 . VAL   B 1 3   ? 49.663 -12.304 -17.299 1.00 25.27 ?  3   VAL   B HG12 1 
ATOM   4100 H HG13 . VAL   B 1 3   ? 49.313 -11.612 -18.686 1.00 25.27 ?  3   VAL   B HG13 1 
ATOM   4101 H HG21 . VAL   B 1 3   ? 46.529 -11.039 -18.233 1.00 25.36 ?  3   VAL   B HG21 1 
ATOM   4102 H HG22 . VAL   B 1 3   ? 46.826 -11.854 -19.562 1.00 25.36 ?  3   VAL   B HG22 1 
ATOM   4103 H HG23 . VAL   B 1 3   ? 45.778 -12.410 -18.506 1.00 25.36 ?  3   VAL   B HG23 1 
ATOM   4104 N N    . ASN   B 1 4   ? 46.544 -15.542 -17.499 1.00 15.03 ?  4   ASN   B N    1 
ATOM   4105 C CA   . ASN   B 1 4   ? 45.405 -16.445 -17.359 1.00 14.21 ?  4   ASN   B CA   1 
ATOM   4106 C C    . ASN   B 1 4   ? 45.333 -17.421 -18.532 1.00 14.58 ?  4   ASN   B C    1 
ATOM   4107 O O    . ASN   B 1 4   ? 44.275 -17.649 -19.113 1.00 15.31 ?  4   ASN   B O    1 
ATOM   4108 C CB   . ASN   B 1 4   ? 44.095 -15.666 -17.205 1.00 13.73 ?  4   ASN   B CB   1 
ATOM   4109 C CG   . ASN   B 1 4   ? 44.044 -14.862 -15.916 1.00 13.11 ?  4   ASN   B CG   1 
ATOM   4110 O OD1  . ASN   B 1 4   ? 44.329 -15.377 -14.836 1.00 13.14 ?  4   ASN   B OD1  1 
ATOM   4111 N ND2  . ASN   B 1 4   ? 43.689 -13.586 -16.026 1.00 14.16 ?  4   ASN   B ND2  1 
ATOM   4112 H H    . ASN   B 1 4   ? 47.034 -15.481 -16.797 1.00 18.01 ?  4   ASN   B H    1 
ATOM   4113 H HA   . ASN   B 1 4   ? 45.533 -16.967 -16.552 1.00 17.02 ?  4   ASN   B HA   1 
ATOM   4114 H HB2  . ASN   B 1 4   ? 44.005 -15.051 -17.948 1.00 16.45 ?  4   ASN   B HB2  1 
ATOM   4115 H HB3  . ASN   B 1 4   ? 43.356 -16.296 -17.203 1.00 16.45 ?  4   ASN   B HB3  1 
ATOM   4116 H HD21 . ASN   B 1 4   ? 43.645 -13.087 -15.323 1.00 16.96 ?  4   ASN   B HD21 1 
ATOM   4117 H HD22 . ASN   B 1 4   ? 43.502 -13.254 -16.796 1.00 16.96 ?  4   ASN   B HD22 1 
ATOM   4118 N N    . SER   B 1 5   ? 46.488 -17.993 -18.888 1.00 15.35 ?  5   SER   B N    1 
ATOM   4119 C CA   . SER   B 1 5   ? 46.588 -18.917 -20.019 1.00 17.50 ?  5   SER   B CA   1 
ATOM   4120 C C    . SER   B 1 5   ? 46.582 -20.328 -19.450 1.00 19.24 ?  5   SER   B C    1 
ATOM   4121 O O    . SER   B 1 5   ? 47.619 -20.965 -19.274 1.00 21.07 ?  5   SER   B O    1 
ATOM   4122 C CB   . SER   B 1 5   ? 47.846 -18.636 -20.840 1.00 19.24 ?  5   SER   B CB   1 
ATOM   4123 O OG   . SER   B 1 5   ? 49.018 -18.830 -20.068 1.00 22.53 ?  5   SER   B OG   1 
ATOM   4124 H H    . SER   B 1 5   ? 47.242 -17.863 -18.488 1.00 18.39 ?  5   SER   B H    1 
ATOM   4125 H HA   . SER   B 1 5   ? 45.816 -18.818 -20.592 1.00 20.97 ?  5   SER   B HA   1 
ATOM   4126 H HB2  . SER   B 1 5   ? 47.860 -19.239 -21.603 1.00 23.06 ?  5   SER   B HB2  1 
ATOM   4127 H HB3  . SER   B 1 5   ? 47.812 -17.718 -21.148 1.00 23.06 ?  5   SER   B HB3  1 
ATOM   4128 H HG   . SER   B 1 5   ? 49.075 -19.632 -19.831 1.00 27.01 ?  5   SER   B HG   1 
ATOM   4129 N N    . PHE   B 1 6   ? 45.384 -20.795 -19.120 1.00 20.62 ?  6   PHE   B N    1 
ATOM   4130 C CA   . PHE   B 1 6   ? 45.198 -22.127 -18.565 1.00 20.62 ?  6   PHE   B CA   1 
ATOM   4131 C C    . PHE   B 1 6   ? 45.116 -23.130 -19.705 1.00 24.92 ?  6   PHE   B C    1 
ATOM   4132 O O    . PHE   B 1 6   ? 44.402 -22.906 -20.685 1.00 27.05 ?  6   PHE   B O    1 
ATOM   4133 C CB   . PHE   B 1 6   ? 43.912 -22.176 -17.736 1.00 18.62 ?  6   PHE   B CB   1 
ATOM   4134 C CG   . PHE   B 1 6   ? 43.931 -21.289 -16.520 1.00 16.88 ?  6   PHE   B CG   1 
ATOM   4135 C CD1  . PHE   B 1 6   ? 44.437 -21.750 -15.318 1.00 15.50 ?  6   PHE   B CD1  1 
ATOM   4136 C CD2  . PHE   B 1 6   ? 43.442 -19.994 -16.580 1.00 16.25 ?  6   PHE   B CD2  1 
ATOM   4137 C CE1  . PHE   B 1 6   ? 44.450 -20.934 -14.193 1.00 14.85 ?  6   PHE   B CE1  1 
ATOM   4138 C CE2  . PHE   B 1 6   ? 43.459 -19.173 -15.467 1.00 16.28 ?  6   PHE   B CE2  1 
ATOM   4139 C CZ   . PHE   B 1 6   ? 43.967 -19.636 -14.274 1.00 15.43 ?  6   PHE   B CZ   1 
ATOM   4140 H H    . PHE   B 1 6   ? 44.650 -20.359 -19.220 1.00 24.72 ?  6   PHE   B H    1 
ATOM   4141 H HA   . PHE   B 1 6   ? 45.946 -22.364 -17.997 1.00 24.72 ?  6   PHE   B HA   1 
ATOM   4142 H HB2  . PHE   B 1 6   ? 43.168 -21.896 -18.291 1.00 22.32 ?  6   PHE   B HB2  1 
ATOM   4143 H HB3  . PHE   B 1 6   ? 43.765 -23.088 -17.432 1.00 22.32 ?  6   PHE   B HB3  1 
ATOM   4144 H HD1  . PHE   B 1 6   ? 44.773 -22.617 -15.258 1.00 18.57 ?  6   PHE   B HD1  1 
ATOM   4145 H HD2  . PHE   B 1 6   ? 43.098 -19.676 -17.381 1.00 19.47 ?  6   PHE   B HD2  1 
ATOM   4146 H HE1  . PHE   B 1 6   ? 44.801 -21.249 -13.390 1.00 17.80 ?  6   PHE   B HE1  1 
ATOM   4147 H HE2  . PHE   B 1 6   ? 43.123 -18.309 -15.525 1.00 19.51 ?  6   PHE   B HE2  1 
ATOM   4148 H HZ   . PHE   B 1 6   ? 43.973 -19.088 -13.524 1.00 18.49 ?  6   PHE   B HZ   1 
ATOM   4149 N N    . SER   B 1 7   ? 45.868 -24.223 -19.587 1.00 27.16 ?  7   SER   B N    1 
ATOM   4150 C CA   . SER   B 1 7   ? 45.939 -25.220 -20.644 1.00 31.00 ?  7   SER   B CA   1 
ATOM   4151 C C    . SER   B 1 7   ? 45.855 -26.616 -20.048 1.00 29.17 ?  7   SER   B C    1 
ATOM   4152 O O    . SER   B 1 7   ? 46.442 -26.892 -18.998 1.00 29.66 ?  7   SER   B O    1 
ATOM   4153 C CB   . SER   B 1 7   ? 47.235 -25.074 -21.451 1.00 35.60 ?  7   SER   B CB   1 
ATOM   4154 O OG   . SER   B 1 7   ? 47.179 -25.838 -22.642 1.00 38.35 ?  7   SER   B OG   1 
ATOM   4155 H H    . SER   B 1 7   ? 46.358 -24.404 -18.901 1.00 32.57 ?  7   SER   B H    1 
ATOM   4156 H HA   . SER   B 1 7   ? 45.191 -25.106 -21.245 1.00 37.17 ?  7   SER   B HA   1 
ATOM   4157 H HB2  . SER   B 1 7   ? 47.363 -24.137 -21.674 1.00 42.69 ?  7   SER   B HB2  1 
ATOM   4158 H HB3  . SER   B 1 7   ? 47.980 -25.389 -20.916 1.00 42.69 ?  7   SER   B HB3  1 
ATOM   4159 H HG   . SER   B 1 7   ? 47.889 -25.737 -23.081 1.00 46.00 ?  7   SER   B HG   1 
ATOM   4160 N N    . GLY   B 1 8   ? 45.119 -27.491 -20.729 1.00 28.03 ?  8   GLY   B N    1 
ATOM   4161 C CA   . GLY   B 1 8   ? 45.048 -28.880 -20.337 1.00 26.67 ?  8   GLY   B CA   1 
ATOM   4162 C C    . GLY   B 1 8   ? 44.101 -29.183 -19.205 1.00 24.82 ?  8   GLY   B C    1 
ATOM   4163 O O    . GLY   B 1 8   ? 44.234 -30.241 -18.575 1.00 26.11 ?  8   GLY   B O    1 
ATOM   4164 H H    . GLY   B 1 8   ? 44.659 -27.296 -21.424 1.00 33.61 ?  8   GLY   B H    1 
ATOM   4165 H HA2  . GLY   B 1 8   ? 44.767 -29.407 -21.099 1.00 31.97 ?  8   GLY   B HA2  1 
ATOM   4166 H HA3  . GLY   B 1 8   ? 45.925 -29.181 -20.065 1.00 31.97 ?  8   GLY   B HA3  1 
ATOM   4167 N N    . TYR   B 1 9   ? 43.122 -28.317 -18.943 1.00 22.82 ?  9   TYR   B N    1 
ATOM   4168 C CA   . TYR   B 1 9   ? 42.161 -28.564 -17.880 1.00 20.69 ?  9   TYR   B CA   1 
ATOM   4169 C C    . TYR   B 1 9   ? 40.971 -29.353 -18.392 1.00 20.31 ?  9   TYR   B C    1 
ATOM   4170 O O    . TYR   B 1 9   ? 40.550 -29.215 -19.545 1.00 22.01 ?  9   TYR   B O    1 
ATOM   4171 C CB   . TYR   B 1 9   ? 41.666 -27.262 -17.253 1.00 20.00 ?  9   TYR   B CB   1 
ATOM   4172 C CG   . TYR   B 1 9   ? 42.693 -26.649 -16.337 1.00 19.31 ?  9   TYR   B CG   1 
ATOM   4173 C CD1  . TYR   B 1 9   ? 43.793 -25.984 -16.854 1.00 19.50 ?  9   TYR   B CD1  1 
ATOM   4174 C CD2  . TYR   B 1 9   ? 42.579 -26.751 -14.958 1.00 18.45 ?  9   TYR   B CD2  1 
ATOM   4175 C CE1  . TYR   B 1 9   ? 44.752 -25.435 -16.029 1.00 19.39 ?  9   TYR   B CE1  1 
ATOM   4176 C CE2  . TYR   B 1 9   ? 43.533 -26.202 -14.121 1.00 18.66 ?  9   TYR   B CE2  1 
ATOM   4177 C CZ   . TYR   B 1 9   ? 44.620 -25.543 -14.665 1.00 19.26 ?  9   TYR   B CZ   1 
ATOM   4178 O OH   . TYR   B 1 9   ? 45.580 -24.997 -13.848 1.00 19.98 ?  9   TYR   B OH   1 
ATOM   4179 H H    . TYR   B 1 9   ? 42.968 -27.595 -19.387 1.00 27.36 ?  9   TYR   B H    1 
ATOM   4180 H HA   . TYR   B 1 9   ? 42.576 -29.083 -17.182 1.00 24.80 ?  9   TYR   B HA   1 
ATOM   4181 H HB2  . TYR   B 1 9   ? 41.456 -26.616 -17.949 1.00 23.97 ?  9   TYR   B HB2  1 
ATOM   4182 H HB3  . TYR   B 1 9   ? 40.877 -27.452 -16.726 1.00 23.97 ?  9   TYR   B HB3  1 
ATOM   4183 H HD1  . TYR   B 1 9   ? 43.883 -25.911 -17.777 1.00 23.38 ?  9   TYR   B HD1  1 
ATOM   4184 H HD2  . TYR   B 1 9   ? 41.841 -27.200 -14.594 1.00 22.11 ?  9   TYR   B HD2  1 
ATOM   4185 H HE1  . TYR   B 1 9   ? 45.474 -24.991 -16.396 1.00 23.24 ?  9   TYR   B HE1  1 
ATOM   4186 H HE2  . TYR   B 1 9   ? 43.431 -26.281 -13.200 1.00 22.37 ?  9   TYR   B HE2  1 
ATOM   4187 H HH   . TYR   B 1 9   ? 46.160 -24.628 -14.318 1.00 23.95 ?  9   TYR   B HH   1 
ATOM   4188 N N    . LEU   B 1 10  ? 40.439 -30.192 -17.510 1.00 18.57 ?  10  LEU   B N    1 
ATOM   4189 C CA   . LEU   B 1 10  ? 39.233 -30.954 -17.771 1.00 18.12 ?  10  LEU   B CA   1 
ATOM   4190 C C    . LEU   B 1 10  ? 38.052 -30.174 -17.211 1.00 17.93 ?  10  LEU   B C    1 
ATOM   4191 O O    . LEU   B 1 10  ? 38.074 -29.755 -16.050 1.00 17.58 ?  10  LEU   B O    1 
ATOM   4192 C CB   . LEU   B 1 10  ? 39.337 -32.314 -17.083 1.00 18.92 ?  10  LEU   B CB   1 
ATOM   4193 C CG   . LEU   B 1 10  ? 38.230 -33.301 -17.438 1.00 20.50 ?  10  LEU   B CG   1 
ATOM   4194 C CD1  . LEU   B 1 10  ? 38.457 -33.852 -18.839 1.00 21.35 ?  10  LEU   B CD1  1 
ATOM   4195 C CD2  . LEU   B 1 10  ? 38.142 -34.424 -16.415 1.00 21.45 ?  10  LEU   B CD2  1 
ATOM   4196 H H    . LEU   B 1 10  ? 40.751 -30.332 -16.715 1.00 22.26 ?  10  LEU   B H    1 
ATOM   4197 H HA   . LEU   B 1 10  ? 39.104 -31.081 -18.720 1.00 21.72 ?  10  LEU   B HA   1 
ATOM   4198 H HB2  . LEU   B 1 10  ? 40.181 -32.719 -17.333 1.00 22.68 ?  10  LEU   B HB2  1 
ATOM   4199 H HB3  . LEU   B 1 10  ? 39.311 -32.183 -16.121 1.00 22.68 ?  10  LEU   B HB3  1 
ATOM   4200 H HG   . LEU   B 1 10  ? 37.379 -32.835 -17.439 1.00 24.57 ?  10  LEU   B HG   1 
ATOM   4201 H HD11 . LEU   B 1 10  ? 37.771 -34.507 -19.034 1.00 25.60 ?  10  LEU   B HD11 1 
ATOM   4202 H HD12 . LEU   B 1 10  ? 38.411 -33.122 -19.475 1.00 25.60 ?  10  LEU   B HD12 1 
ATOM   4203 H HD13 . LEU   B 1 10  ? 39.333 -34.267 -18.873 1.00 25.60 ?  10  LEU   B HD13 1 
ATOM   4204 H HD21 . LEU   B 1 10  ? 37.432 -35.030 -16.677 1.00 25.71 ?  10  LEU   B HD21 1 
ATOM   4205 H HD22 . LEU   B 1 10  ? 38.988 -34.891 -16.389 1.00 25.71 ?  10  LEU   B HD22 1 
ATOM   4206 H HD23 . LEU   B 1 10  ? 37.945 -34.039 -15.546 1.00 25.71 ?  10  LEU   B HD23 1 
ATOM   4207 N N    . LYS   B 1 11  ? 37.031 -29.981 -18.041 1.00 18.97 ?  11  LYS   B N    1 
ATOM   4208 C CA   . LYS   B 1 11  ? 35.826 -29.276 -17.630 1.00 21.25 ?  11  LYS   B CA   1 
ATOM   4209 C C    . LYS   B 1 11  ? 34.971 -30.208 -16.779 1.00 19.98 ?  11  LYS   B C    1 
ATOM   4210 O O    . LYS   B 1 11  ? 34.615 -31.306 -17.222 1.00 21.50 ?  11  LYS   B O    1 
ATOM   4211 C CB   . LYS   B 1 11  ? 35.067 -28.836 -18.882 1.00 25.77 ?  11  LYS   B CB   1 
ATOM   4212 C CG   . LYS   B 1 11  ? 33.920 -27.874 -18.654 1.00 29.78 ?  11  LYS   B CG   1 
ATOM   4213 C CD   . LYS   B 1 11  ? 33.198 -27.594 -19.969 1.00 33.15 ?  11  LYS   B CD   1 
ATOM   4214 C CE   . LYS   B 1 11  ? 32.185 -26.469 -19.833 1.00 35.56 ?  11  LYS   B CE   1 
ATOM   4215 N NZ   . LYS   B 1 11  ? 32.845 -25.147 -19.653 1.00 36.80 ?  11  LYS   B NZ   1 
ATOM   4216 H H    . LYS   B 1 11  ? 37.000 -30.261 -18.857 1.00 22.75 ?  11  LYS   B H    1 
ATOM   4217 H HA   . LYS   B 1 11  ? 36.056 -28.493 -17.110 1.00 25.48 ?  11  LYS   B HA   1 
ATOM   4218 H HB2  . LYS   B 1 11  ? 35.692 -28.397 -19.481 1.00 30.90 ?  11  LYS   B HB2  1 
ATOM   4219 H HB3  . LYS   B 1 11  ? 34.701 -29.621 -19.317 1.00 30.90 ?  11  LYS   B HB3  1 
ATOM   4220 H HG2  . LYS   B 1 11  ? 33.286 -28.268 -18.035 1.00 35.71 ?  11  LYS   B HG2  1 
ATOM   4221 H HG3  . LYS   B 1 11  ? 34.262 -27.037 -18.307 1.00 35.71 ?  11  LYS   B HG3  1 
ATOM   4222 H HD2  . LYS   B 1 11  ? 33.850 -27.336 -20.641 1.00 39.76 ?  11  LYS   B HD2  1 
ATOM   4223 H HD3  . LYS   B 1 11  ? 32.727 -28.394 -20.252 1.00 39.76 ?  11  LYS   B HD3  1 
ATOM   4224 H HE2  . LYS   B 1 11  ? 31.642 -26.430 -20.636 1.00 42.64 ?  11  LYS   B HE2  1 
ATOM   4225 H HE3  . LYS   B 1 11  ? 31.626 -26.640 -19.060 1.00 42.64 ?  11  LYS   B HE3  1 
ATOM   4226 H HZ1  . LYS   B 1 11  ? 32.230 -24.507 -19.585 1.00 44.13 ?  11  LYS   B HZ1  1 
ATOM   4227 H HZ2  . LYS   B 1 11  ? 33.341 -25.152 -18.915 1.00 44.13 ?  11  LYS   B HZ2  1 
ATOM   4228 H HZ3  . LYS   B 1 11  ? 33.368 -24.971 -20.353 1.00 44.13 ?  11  LYS   B HZ3  1 
ATOM   4229 N N    . LEU   B 1 12  ? 34.646 -29.782 -15.558 1.00 18.25 ?  12  LEU   B N    1 
ATOM   4230 C CA   . LEU   B 1 12  ? 33.686 -30.488 -14.714 1.00 17.54 ?  12  LEU   B CA   1 
ATOM   4231 C C    . LEU   B 1 12  ? 32.297 -29.877 -14.803 1.00 17.37 ?  12  LEU   B C    1 
ATOM   4232 O O    . LEU   B 1 12  ? 31.308 -30.591 -14.972 1.00 17.89 ?  12  LEU   B O    1 
ATOM   4233 C CB   . LEU   B 1 12  ? 34.148 -30.502 -13.250 1.00 17.03 ?  12  LEU   B CB   1 
ATOM   4234 C CG   . LEU   B 1 12  ? 35.490 -31.180 -12.975 1.00 16.85 ?  12  LEU   B CG   1 
ATOM   4235 C CD1  . LEU   B 1 12  ? 35.856 -31.123 -11.502 1.00 16.97 ?  12  LEU   B CD1  1 
ATOM   4236 C CD2  . LEU   B 1 12  ? 35.477 -32.622 -13.460 1.00 17.60 ?  12  LEU   B CD2  1 
ATOM   4237 H H    . LEU   B 1 12  ? 34.967 -29.074 -15.190 1.00 21.88 ?  12  LEU   B H    1 
ATOM   4238 H HA   . LEU   B 1 12  ? 33.614 -31.407 -15.014 1.00 21.03 ?  12  LEU   B HA   1 
ATOM   4239 H HB2  . LEU   B 1 12  ? 34.214 -29.586 -12.944 1.00 20.41 ?  12  LEU   B HB2  1 
ATOM   4240 H HB3  . LEU   B 1 12  ? 33.473 -30.968 -12.723 1.00 20.41 ?  12  LEU   B HB3  1 
ATOM   4241 H HG   . LEU   B 1 12  ? 36.176 -30.710 -13.468 1.00 20.20 ?  12  LEU   B HG   1 
ATOM   4242 H HD11 . LEU   B 1 12  ? 36.717 -31.558 -11.374 1.00 20.34 ?  12  LEU   B HD11 1 
ATOM   4243 H HD12 . LEU   B 1 12  ? 35.914 -30.196 -11.223 1.00 20.34 ?  12  LEU   B HD12 1 
ATOM   4244 H HD13 . LEU   B 1 12  ? 35.177 -31.583 -10.984 1.00 20.34 ?  12  LEU   B HD13 1 
ATOM   4245 H HD21 . LEU   B 1 12  ? 36.279 -33.067 -13.149 1.00 21.09 ?  12  LEU   B HD21 1 
ATOM   4246 H HD22 . LEU   B 1 12  ? 34.691 -33.070 -13.105 1.00 21.09 ?  12  LEU   B HD22 1 
ATOM   4247 H HD23 . LEU   B 1 12  ? 35.448 -32.630 -14.431 1.00 21.09 ?  12  LEU   B HD23 1 
ATOM   4248 N N    . THR   B 1 13  ? 32.214 -28.561 -14.688 1.00 17.27 ?  13  THR   B N    1 
ATOM   4249 C CA   . THR   B 1 13  ? 30.995 -27.807 -14.910 1.00 17.19 ?  13  THR   B CA   1 
ATOM   4250 C C    . THR   B 1 13  ? 31.346 -26.615 -15.794 1.00 19.19 ?  13  THR   B C    1 
ATOM   4251 O O    . THR   B 1 13  ? 32.498 -26.427 -16.198 1.00 20.35 ?  13  THR   B O    1 
ATOM   4252 C CB   . THR   B 1 13  ? 30.388 -27.322 -13.587 1.00 16.59 ?  13  THR   B CB   1 
ATOM   4253 O OG1  . THR   B 1 13  ? 31.230 -26.300 -13.041 1.00 16.31 ?  13  THR   B OG1  1 
ATOM   4254 C CG2  . THR   B 1 13  ? 30.264 -28.465 -12.591 1.00 17.40 ?  13  THR   B CG2  1 
ATOM   4255 H H    . THR   B 1 13  ? 32.881 -28.064 -14.471 1.00 20.71 ?  13  THR   B H    1 
ATOM   4256 H HA   . THR   B 1 13  ? 30.340 -28.366 -15.362 1.00 20.60 ?  13  THR   B HA   1 
ATOM   4257 H HB   . THR   B 1 13  ? 29.497 -26.959 -13.752 1.00 19.88 ?  13  THR   B HB   1 
ATOM   4258 H HG1  . THR   B 1 13  ? 30.927 -25.537 -13.252 1.00 19.54 ?  13  THR   B HG1  1 
ATOM   4259 H HG21 . THR   B 1 13  ? 29.747 -28.183 -11.820 1.00 20.85 ?  13  THR   B HG21 1 
ATOM   4260 H HG22 . THR   B 1 13  ? 29.814 -29.220 -13.007 1.00 20.85 ?  13  THR   B HG22 1 
ATOM   4261 H HG23 . THR   B 1 13  ? 31.142 -28.747 -12.297 1.00 20.85 ?  13  THR   B HG23 1 
ATOM   4262 N N    A ASP   B 1 14  ? 30.341 -25.787 -16.077 0.48 20.20 ?  14  ASP   B N    1 
ATOM   4263 N N    B ASP   B 1 14  ? 30.342 -25.789 -16.088 0.52 20.05 ?  14  ASP   B N    1 
ATOM   4264 C CA   A ASP   B 1 14  ? 30.568 -24.634 -16.939 0.48 21.43 ?  14  ASP   B CA   1 
ATOM   4265 C CA   B ASP   B 1 14  ? 30.573 -24.635 -16.949 0.52 21.21 ?  14  ASP   B CA   1 
ATOM   4266 C C    A ASP   B 1 14  ? 31.660 -23.722 -16.394 0.48 19.74 ?  14  ASP   B C    1 
ATOM   4267 C C    B ASP   B 1 14  ? 31.612 -23.675 -16.387 0.52 19.58 ?  14  ASP   B C    1 
ATOM   4268 O O    A ASP   B 1 14  ? 32.337 -23.040 -17.173 0.48 20.79 ?  14  ASP   B O    1 
ATOM   4269 O O    B ASP   B 1 14  ? 32.182 -22.890 -17.153 0.52 20.64 ?  14  ASP   B O    1 
ATOM   4270 C CB   A ASP   B 1 14  ? 29.269 -23.852 -17.130 0.48 24.73 ?  14  ASP   B CB   1 
ATOM   4271 C CB   B ASP   B 1 14  ? 29.271 -23.872 -17.192 0.52 24.46 ?  14  ASP   B CB   1 
ATOM   4272 C CG   A ASP   B 1 14  ? 28.268 -24.584 -18.003 0.48 27.83 ?  14  ASP   B CG   1 
ATOM   4273 C CG   B ASP   B 1 14  ? 28.374 -24.555 -18.205 0.52 27.62 ?  14  ASP   B CG   1 
ATOM   4274 O OD1  A ASP   B 1 14  ? 28.619 -25.637 -18.581 0.48 28.61 ?  14  ASP   B OD1  1 
ATOM   4275 O OD1  B ASP   B 1 14  ? 28.892 -25.321 -19.046 0.52 28.60 ?  14  ASP   B OD1  1 
ATOM   4276 O OD2  A ASP   B 1 14  ? 27.119 -24.107 -18.101 0.48 29.23 -1 14  ASP   B OD2  1 
ATOM   4277 O OD2  B ASP   B 1 14  ? 27.148 -24.329 -18.162 0.52 28.98 -1 14  ASP   B OD2  1 
ATOM   4278 H H    A ASP   B 1 14  ? 29.539 -25.859 -15.779 0.48 24.22 ?  14  ASP   B H    1 
ATOM   4279 H H    B ASP   B 1 14  ? 29.537 -25.867 -15.802 0.52 24.04 ?  14  ASP   B H    1 
ATOM   4280 H HA   A ASP   B 1 14  ? 30.863 -24.939 -17.807 0.48 25.69 ?  14  ASP   B HA   1 
ATOM   4281 H HA   B ASP   B 1 14  ? 30.902 -24.945 -17.805 0.52 25.42 ?  14  ASP   B HA   1 
ATOM   4282 H HB2  A ASP   B 1 14  ? 28.843 -23.724 -16.271 0.48 29.66 ?  14  ASP   B HB2  1 
ATOM   4283 H HB2  B ASP   B 1 14  ? 28.783 -23.809 -16.358 0.52 29.33 ?  14  ASP   B HB2  1 
ATOM   4284 H HB3  A ASP   B 1 14  ? 29.472 -22.991 -17.533 0.48 29.66 ?  14  ASP   B HB3  1 
ATOM   4285 H HB3  B ASP   B 1 14  ? 29.487 -22.980 -17.516 0.52 29.33 ?  14  ASP   B HB3  1 
ATOM   4286 N N    . ASN   B 1 15  ? 31.860 -23.699 -15.072 1.00 17.60 ?  15  ASN   B N    1 
ATOM   4287 C CA   . ASN   B 1 15  ? 32.823 -22.787 -14.460 1.00 15.14 ?  15  ASN   B CA   1 
ATOM   4288 C C    . ASN   B 1 15  ? 33.913 -23.449 -13.625 1.00 13.71 ?  15  ASN   B C    1 
ATOM   4289 O O    . ASN   B 1 15  ? 34.772 -22.730 -13.103 1.00 13.77 ?  15  ASN   B O    1 
ATOM   4290 C CB   . ASN   B 1 15  ? 32.108 -21.731 -13.601 1.00 14.83 ?  15  ASN   B CB   1 
ATOM   4291 C CG   . ASN   B 1 15  ? 31.484 -22.328 -12.357 1.00 14.82 ?  15  ASN   B CG   1 
ATOM   4292 O OD1  . ASN   B 1 15  ? 30.538 -23.123 -12.443 1.00 16.58 ?  15  ASN   B OD1  1 
ATOM   4293 N ND2  . ASN   B 1 15  ? 32.011 -21.972 -11.197 1.00 14.00 ?  15  ASN   B ND2  1 
ATOM   4294 H H    A ASN   B 1 15  ? 31.443 -24.200 -14.507 0.48 21.09 ?  15  ASN   B H    1 
ATOM   4295 H H    B ASN   B 1 15  ? 31.460 -24.215 -14.510 0.52 21.09 ?  15  ASN   B H    1 
ATOM   4296 H HA   . ASN   B 1 15  ? 33.271 -22.299 -15.159 1.00 18.15 ?  15  ASN   B HA   1 
ATOM   4297 H HB2  . ASN   B 1 15  ? 32.750 -21.050 -13.323 1.00 17.77 ?  15  ASN   B HB2  1 
ATOM   4298 H HB3  . ASN   B 1 15  ? 31.400 -21.309 -14.122 1.00 17.77 ?  15  ASN   B HB3  1 
ATOM   4299 H HD21 . ASN   B 1 15  ? 31.691 -22.278 -10.459 1.00 16.78 ?  15  ASN   B HD21 1 
ATOM   4300 H HD22 . ASN   B 1 15  ? 32.681 -21.420 -11.168 1.00 16.78 ?  15  ASN   B HD22 1 
ATOM   4301 N N    . VAL   B 1 16  ? 33.916 -24.771 -13.473 1.00 13.72 ?  16  VAL   B N    1 
ATOM   4302 C CA   . VAL   B 1 16  ? 34.915 -25.462 -12.661 1.00 13.28 ?  16  VAL   B CA   1 
ATOM   4303 C C    . VAL   B 1 16  ? 35.711 -26.398 -13.555 1.00 13.53 ?  16  VAL   B C    1 
ATOM   4304 O O    . VAL   B 1 16  ? 35.136 -27.281 -14.213 1.00 14.52 ?  16  VAL   B O    1 
ATOM   4305 C CB   . VAL   B 1 16  ? 34.288 -26.221 -11.483 1.00 13.56 ?  16  VAL   B CB   1 
ATOM   4306 C CG1  . VAL   B 1 16  ? 35.367 -26.951 -10.687 1.00 13.78 ?  16  VAL   B CG1  1 
ATOM   4307 C CG2  . VAL   B 1 16  ? 33.492 -25.267 -10.593 1.00 14.35 ?  16  VAL   B CG2  1 
ATOM   4308 H H    . VAL   B 1 16  ? 33.325 -25.293 -13.823 1.00 16.44 ?  16  VAL   B H    1 
ATOM   4309 H HA   . VAL   B 1 16  ? 35.524 -24.803 -12.293 1.00 15.91 ?  16  VAL   B HA   1 
ATOM   4310 H HB   . VAL   B 1 16  ? 33.671 -26.887 -11.827 1.00 16.24 ?  16  VAL   B HB   1 
ATOM   4311 H HG11 . VAL   B 1 16  ? 34.990 -27.250 -9.844  1.00 16.51 ?  16  VAL   B HG11 1 
ATOM   4312 H HG12 . VAL   B 1 16  ? 35.678 -27.713 -11.198 1.00 16.51 ?  16  VAL   B HG12 1 
ATOM   4313 H HG13 . VAL   B 1 16  ? 36.101 -26.339 -10.519 1.00 16.51 ?  16  VAL   B HG13 1 
ATOM   4314 H HG21 . VAL   B 1 16  ? 33.158 -25.755 -9.822  1.00 17.20 ?  16  VAL   B HG21 1 
ATOM   4315 H HG22 . VAL   B 1 16  ? 34.071 -24.547 -10.302 1.00 17.20 ?  16  VAL   B HG22 1 
ATOM   4316 H HG23 . VAL   B 1 16  ? 32.747 -24.907 -11.101 1.00 17.20 ?  16  VAL   B HG23 1 
ATOM   4317 N N    . TYR   B 1 17  ? 37.033 -26.230 -13.534 1.00 13.85 ?  17  TYR   B N    1 
ATOM   4318 C CA   . TYR   B 1 17  ? 37.973 -26.986 -14.346 1.00 14.52 ?  17  TYR   B CA   1 
ATOM   4319 C C    . TYR   B 1 17  ? 39.025 -27.597 -13.431 1.00 13.31 ?  17  TYR   B C    1 
ATOM   4320 O O    . TYR   B 1 17  ? 39.305 -27.066 -12.355 1.00 13.38 ?  17  TYR   B O    1 
ATOM   4321 C CB   . TYR   B 1 17  ? 38.683 -26.068 -15.349 1.00 17.43 ?  17  TYR   B CB   1 
ATOM   4322 C CG   . TYR   B 1 17  ? 37.759 -25.296 -16.260 1.00 20.86 ?  17  TYR   B CG   1 
ATOM   4323 C CD1  . TYR   B 1 17  ? 37.205 -24.085 -15.863 1.00 22.69 ?  17  TYR   B CD1  1 
ATOM   4324 C CD2  . TYR   B 1 17  ? 37.441 -25.777 -17.523 1.00 23.13 ?  17  TYR   B CD2  1 
ATOM   4325 C CE1  . TYR   B 1 17  ? 36.357 -23.376 -16.698 1.00 24.58 ?  17  TYR   B CE1  1 
ATOM   4326 C CE2  . TYR   B 1 17  ? 36.599 -25.075 -18.367 1.00 24.78 ?  17  TYR   B CE2  1 
ATOM   4327 C CZ   . TYR   B 1 17  ? 36.060 -23.875 -17.949 1.00 25.59 ?  17  TYR   B CZ   1 
ATOM   4328 O OH   . TYR   B 1 17  ? 35.221 -23.176 -18.787 1.00 26.76 ?  17  TYR   B OH   1 
ATOM   4329 H H    . TYR   B 1 17  ? 37.424 -25.645 -13.032 1.00 16.60 ?  17  TYR   B H    1 
ATOM   4330 H HA   . TYR   B 1 17  ? 37.507 -27.688 -14.827 1.00 17.40 ?  17  TYR   B HA   1 
ATOM   4331 H HB2  . TYR   B 1 17  ? 39.227 -25.430 -14.866 1.00 20.89 ?  17  TYR   B HB2  1 
ATOM   4332 H HB3  . TYR   B 1 17  ? 39.240 -26.616 -15.916 1.00 20.89 ?  17  TYR   B HB3  1 
ATOM   4333 H HD1  . TYR   B 1 17  ? 37.405 -23.744 -15.023 1.00 27.20 ?  17  TYR   B HD1  1 
ATOM   4334 H HD2  . TYR   B 1 17  ? 37.798 -26.585 -17.809 1.00 27.73 ?  17  TYR   B HD2  1 
ATOM   4335 H HE1  . TYR   B 1 17  ? 35.993 -22.564 -16.421 1.00 29.47 ?  17  TYR   B HE1  1 
ATOM   4336 H HE2  . TYR   B 1 17  ? 36.389 -25.412 -19.211 1.00 29.71 ?  17  TYR   B HE2  1 
ATOM   4337 H HH   . TYR   B 1 17  ? 35.119 -23.592 -19.510 1.00 32.09 ?  17  TYR   B HH   1 
ATOM   4338 N N    . ILE   B 1 18  ? 39.628 -28.707 -13.858 1.00 13.49 ?  18  ILE   B N    1 
ATOM   4339 C CA   . ILE   B 1 18  ? 40.552 -29.431 -12.992 1.00 13.41 ?  18  ILE   B CA   1 
ATOM   4340 C C    . ILE   B 1 18  ? 41.716 -29.992 -13.804 1.00 13.76 ?  18  ILE   B C    1 
ATOM   4341 O O    . ILE   B 1 18  ? 41.562 -30.390 -14.963 1.00 15.18 ?  18  ILE   B O    1 
ATOM   4342 C CB   . ILE   B 1 18  ? 39.798 -30.527 -12.194 1.00 13.99 ?  18  ILE   B CB   1 
ATOM   4343 C CG1  . ILE   B 1 18  ? 40.659 -31.073 -11.052 1.00 14.32 ?  18  ILE   B CG1  1 
ATOM   4344 C CG2  . ILE   B 1 18  ? 39.286 -31.632 -13.134 1.00 14.46 ?  18  ILE   B CG2  1 
ATOM   4345 C CD1  . ILE   B 1 18  ? 39.861 -31.877 -10.034 1.00 15.74 ?  18  ILE   B CD1  1 
ATOM   4346 H H    . ILE   B 1 18  ? 39.524 -29.051 -14.637 1.00 16.17 ?  18  ILE   B H    1 
ATOM   4347 H HA   . ILE   B 1 18  ? 40.907 -28.814 -12.336 1.00 16.07 ?  18  ILE   B HA   1 
ATOM   4348 H HB   . ILE   B 1 18  ? 39.012 -30.124 -11.791 1.00 16.76 ?  18  ILE   B HB   1 
ATOM   4349 H HG12 . ILE   B 1 18  ? 41.339 -31.652 -11.418 1.00 17.16 ?  18  ILE   B HG12 1 
ATOM   4350 H HG13 . ILE   B 1 18  ? 41.061 -30.327 -10.586 1.00 17.16 ?  18  ILE   B HG13 1 
ATOM   4351 H HG21 . ILE   B 1 18  ? 38.698 -32.230 -12.638 1.00 17.33 ?  18  ILE   B HG21 1 
ATOM   4352 H HG22 . ILE   B 1 18  ? 38.788 -31.221 -13.862 1.00 17.33 ?  18  ILE   B HG22 1 
ATOM   4353 H HG23 . ILE   B 1 18  ? 40.037 -32.128 -13.487 1.00 17.33 ?  18  ILE   B HG23 1 
ATOM   4354 H HD11 . ILE   B 1 18  ? 40.458 -32.169 -9.326  1.00 18.86 ?  18  ILE   B HD11 1 
ATOM   4355 H HD12 . ILE   B 1 18  ? 39.159 -31.317 -9.665  1.00 18.86 ?  18  ILE   B HD12 1 
ATOM   4356 H HD13 . ILE   B 1 18  ? 39.470 -32.648 -10.474 1.00 18.86 ?  18  ILE   B HD13 1 
ATOM   4357 N N    . LYS   B 1 19  ? 42.892 -30.025 -13.176 1.00 14.10 ?  19  LYS   B N    1 
ATOM   4358 C CA   . LYS   B 1 19  ? 44.101 -30.502 -13.830 1.00 15.18 ?  19  LYS   B CA   1 
ATOM   4359 C C    . LYS   B 1 19  ? 45.003 -31.181 -12.811 1.00 15.02 ?  19  LYS   B C    1 
ATOM   4360 O O    . LYS   B 1 19  ? 45.090 -30.743 -11.662 1.00 14.47 ?  19  LYS   B O    1 
ATOM   4361 C CB   . LYS   B 1 19  ? 44.861 -29.337 -14.475 1.00 16.78 ?  19  LYS   B CB   1 
ATOM   4362 C CG   . LYS   B 1 19  ? 46.064 -29.759 -15.297 1.00 18.71 ?  19  LYS   B CG   1 
ATOM   4363 C CD   . LYS   B 1 19  ? 46.796 -28.543 -15.858 1.00 20.29 ?  19  LYS   B CD   1 
ATOM   4364 C CE   . LYS   B 1 19  ? 47.985 -28.940 -16.717 1.00 22.01 ?  19  LYS   B CE   1 
ATOM   4365 N NZ   . LYS   B 1 19  ? 48.729 -27.754 -17.221 1.00 22.77 ?  19  LYS   B NZ   1 
ATOM   4366 H H    . LYS   B 1 19  ? 42.998 -29.769 -12.356 1.00 16.90 ?  19  LYS   B H    1 
ATOM   4367 H HA   . LYS   B 1 19  ? 43.855 -31.142 -14.515 1.00 18.19 ?  19  LYS   B HA   1 
ATOM   4368 H HB2  . LYS   B 1 19  ? 44.248 -28.861 -15.058 1.00 20.11 ?  19  LYS   B HB2  1 
ATOM   4369 H HB3  . LYS   B 1 19  ? 45.163 -28.743 -13.767 1.00 20.11 ?  19  LYS   B HB3  1 
ATOM   4370 H HG2  . LYS   B 1 19  ? 46.672 -30.258 -14.733 1.00 22.43 ?  19  LYS   B HG2  1 
ATOM   4371 H HG3  . LYS   B 1 19  ? 45.757 -30.309 -16.036 1.00 22.43 ?  19  LYS   B HG3  1 
ATOM   4372 H HD2  . LYS   B 1 19  ? 46.181 -28.027 -16.403 1.00 24.32 ?  19  LYS   B HD2  1 
ATOM   4373 H HD3  . LYS   B 1 19  ? 47.118 -28.002 -15.119 1.00 24.32 ?  19  LYS   B HD3  1 
ATOM   4374 H HE2  . LYS   B 1 19  ? 48.591 -29.481 -16.186 1.00 26.39 ?  19  LYS   B HE2  1 
ATOM   4375 H HE3  . LYS   B 1 19  ? 47.665 -29.451 -17.479 1.00 26.39 ?  19  LYS   B HE3  1 
ATOM   4376 H HZ1  . LYS   B 1 19  ? 49.396 -28.016 -17.748 1.00 27.30 ?  19  LYS   B HZ1  1 
ATOM   4377 H HZ2  . LYS   B 1 19  ? 48.182 -27.228 -17.688 1.00 27.30 ?  19  LYS   B HZ2  1 
ATOM   4378 H HZ3  . LYS   B 1 19  ? 49.062 -27.291 -16.539 1.00 27.30 ?  19  LYS   B HZ3  1 
ATOM   4379 N N    . ASN   B 1 20  ? 45.687 -32.239 -13.242 1.00 16.02 ?  20  ASN   B N    1 
ATOM   4380 C CA   . ASN   B 1 20  ? 46.718 -32.873 -12.423 1.00 17.15 ?  20  ASN   B CA   1 
ATOM   4381 C C    . ASN   B 1 20  ? 47.994 -32.057 -12.612 1.00 17.59 ?  20  ASN   B C    1 
ATOM   4382 O O    . ASN   B 1 20  ? 48.634 -32.120 -13.665 1.00 19.45 ?  20  ASN   B O    1 
ATOM   4383 C CB   . ASN   B 1 20  ? 46.891 -34.329 -12.852 1.00 18.90 ?  20  ASN   B CB   1 
ATOM   4384 C CG   . ASN   B 1 20  ? 48.056 -35.028 -12.168 1.00 20.30 ?  20  ASN   B CG   1 
ATOM   4385 O OD1  . ASN   B 1 20  ? 48.727 -35.867 -12.779 1.00 22.44 ?  20  ASN   B OD1  1 
ATOM   4386 N ND2  . ASN   B 1 20  ? 48.296 -34.705 -10.904 1.00 19.88 ?  20  ASN   B ND2  1 
ATOM   4387 H H    . ASN   B 1 20  ? 45.572 -32.604 -14.010 1.00 19.20 ?  20  ASN   B H    1 
ATOM   4388 H HA   . ASN   B 1 20  ? 46.447 -32.849 -11.491 1.00 20.55 ?  20  ASN   B HA   1 
ATOM   4389 H HB2  . ASN   B 1 20  ? 46.077 -34.819 -12.636 1.00 22.66 ?  20  ASN   B HB2  1 
ATOM   4390 H HB3  . ASN   B 1 20  ? 47.043 -34.357 -13.809 1.00 22.66 ?  20  ASN   B HB3  1 
ATOM   4391 H HD21 . ASN   B 1 20  ? 48.944 -35.076 -10.481 1.00 23.84 ?  20  ASN   B HD21 1 
ATOM   4392 H HD22 . ASN   B 1 20  ? 47.804 -34.119 -10.503 1.00 23.84 ?  20  ASN   B HD22 1 
ATOM   4393 N N    . ALA   B 1 21  ? 48.357 -31.255 -11.608 1.00 16.97 ?  21  ALA   B N    1 
ATOM   4394 C CA   . ALA   B 1 21  ? 49.476 -30.335 -11.762 1.00 17.43 ?  21  ALA   B CA   1 
ATOM   4395 C C    . ALA   B 1 21  ? 49.939 -29.829 -10.403 1.00 16.26 ?  21  ALA   B C    1 
ATOM   4396 O O    . ALA   B 1 21  ? 49.199 -29.862 -9.413  1.00 15.71 ?  21  ALA   B O    1 
ATOM   4397 C CB   . ALA   B 1 21  ? 49.095 -29.159 -12.664 1.00 19.12 ?  21  ALA   B CB   1 
ATOM   4398 H H    . ALA   B 1 21  ? 47.963 -31.219 -10.838 1.00 20.34 ?  21  ALA   B H    1 
ATOM   4399 H HA   . ALA   B 1 21  ? 50.210 -30.813 -12.178 1.00 20.89 ?  21  ALA   B HA   1 
ATOM   4400 H HB1  . ALA   B 1 21  ? 49.883 -28.617 -12.808 1.00 22.92 ?  21  ALA   B HB1  1 
ATOM   4401 H HB2  . ALA   B 1 21  ? 48.771 -29.506 -13.510 1.00 22.92 ?  21  ALA   B HB2  1 
ATOM   4402 H HB3  . ALA   B 1 21  ? 48.401 -28.641 -12.230 1.00 22.92 ?  21  ALA   B HB3  1 
ATOM   4403 N N    . ASP   B 1 22  ? 51.194 -29.376 -10.387 1.00 15.53 ?  22  ASP   B N    1 
ATOM   4404 C CA   . ASP   B 1 22  ? 51.808 -28.688 -9.257  1.00 14.95 ?  22  ASP   B CA   1 
ATOM   4405 C C    . ASP   B 1 22  ? 51.403 -27.218 -9.341  1.00 13.30 ?  22  ASP   B C    1 
ATOM   4406 O O    . ASP   B 1 22  ? 51.713 -26.546 -10.329 1.00 13.72 ?  22  ASP   B O    1 
ATOM   4407 C CB   . ASP   B 1 22  ? 53.324 -28.868 -9.413  1.00 16.26 ?  22  ASP   B CB   1 
ATOM   4408 C CG   . ASP   B 1 22  ? 54.155 -28.119 -8.378  1.00 18.20 ?  22  ASP   B CG   1 
ATOM   4409 O OD1  . ASP   B 1 22  ? 53.815 -26.989 -8.001  1.00 17.89 ?  22  ASP   B OD1  1 
ATOM   4410 O OD2  . ASP   B 1 22  ? 55.206 -28.660 -7.966  1.00 21.06 -1 22  ASP   B OD2  1 
ATOM   4411 H H    . ASP   B 1 22  ? 51.730 -29.458 -11.057 1.00 18.61 ?  22  ASP   B H    1 
ATOM   4412 H HA   . ASP   B 1 22  ? 51.513 -29.074 -8.415  1.00 17.92 ?  22  ASP   B HA   1 
ATOM   4413 H HB2  . ASP   B 1 22  ? 53.542 -29.808 -9.335  1.00 19.48 ?  22  ASP   B HB2  1 
ATOM   4414 H HB3  . ASP   B 1 22  ? 53.589 -28.539 -10.287 1.00 19.48 ?  22  ASP   B HB3  1 
ATOM   4415 N N    . ILE   B 1 23  ? 50.696 -26.724 -8.320  1.00 12.79 ?  23  ILE   B N    1 
ATOM   4416 C CA   . ILE   B 1 23  ? 50.108 -25.383 -8.391  1.00 12.09 ?  23  ILE   B CA   1 
ATOM   4417 C C    . ILE   B 1 23  ? 51.167 -24.297 -8.538  1.00 11.84 ?  23  ILE   B C    1 
ATOM   4418 O O    . ILE   B 1 23  ? 50.900 -23.257 -9.148  1.00 11.39 ?  23  ILE   B O    1 
ATOM   4419 C CB   . ILE   B 1 23  ? 49.172 -25.132 -7.191  1.00 12.37 ?  23  ILE   B CB   1 
ATOM   4420 C CG1  . ILE   B 1 23  ? 48.350 -23.857 -7.385  1.00 12.87 ?  23  ILE   B CG1  1 
ATOM   4421 C CG2  . ILE   B 1 23  ? 49.951 -25.113 -5.883  1.00 13.43 ?  23  ILE   B CG2  1 
ATOM   4422 C CD1  . ILE   B 1 23  ? 47.217 -23.703 -6.378  1.00 13.57 ?  23  ILE   B CD1  1 
ATOM   4423 H H    . ILE   B 1 23  ? 50.539 -27.143 -7.583  1.00 15.33 ?  23  ILE   B H    1 
ATOM   4424 H HA   . ILE   B 1 23  ? 49.557 -25.343 -9.185  1.00 14.49 ?  23  ILE   B HA   1 
ATOM   4425 H HB   . ILE   B 1 23  ? 48.548 -25.871 -7.149  1.00 14.82 ?  23  ILE   B HB   1 
ATOM   4426 H HG12 . ILE   B 1 23  ? 48.941 -23.085 -7.292  1.00 15.42 ?  23  ILE   B HG12 1 
ATOM   4427 H HG13 . ILE   B 1 23  ? 47.966 -23.861 -8.276  1.00 15.42 ?  23  ILE   B HG13 1 
ATOM   4428 H HG21 . ILE   B 1 23  ? 49.325 -25.087 -5.145  1.00 16.10 ?  23  ILE   B HG21 1 
ATOM   4429 H HG22 . ILE   B 1 23  ? 50.491 -25.918 -5.830  1.00 16.10 ?  23  ILE   B HG22 1 
ATOM   4430 H HG23 . ILE   B 1 23  ? 50.522 -24.331 -5.865  1.00 16.10 ?  23  ILE   B HG23 1 
ATOM   4431 H HD11 . ILE   B 1 23  ? 46.702 -22.914 -6.603  1.00 16.26 ?  23  ILE   B HD11 1 
ATOM   4432 H HD12 . ILE   B 1 23  ? 46.657 -24.492 -6.421  1.00 16.26 ?  23  ILE   B HD12 1 
ATOM   4433 H HD13 . ILE   B 1 23  ? 47.597 -23.611 -5.491  1.00 16.26 ?  23  ILE   B HD13 1 
ATOM   4434 N N    . VAL   B 1 24  ? 52.364 -24.498 -7.976  1.00 11.97 ?  24  VAL   B N    1 
ATOM   4435 C CA   . VAL   B 1 24  ? 53.439 -23.520 -8.146  1.00 12.64 ?  24  VAL   B CA   1 
ATOM   4436 C C    . VAL   B 1 24  ? 53.895 -23.481 -9.597  1.00 12.51 ?  24  VAL   B C    1 
ATOM   4437 O O    . VAL   B 1 24  ? 54.026 -22.407 -10.197 1.00 13.29 ?  24  VAL   B O    1 
ATOM   4438 C CB   . VAL   B 1 24  ? 54.613 -23.828 -7.194  1.00 13.36 ?  24  VAL   B CB   1 
ATOM   4439 C CG1  . VAL   B 1 24  ? 55.825 -22.946 -7.514  1.00 14.01 ?  24  VAL   B CG1  1 
ATOM   4440 C CG2  . VAL   B 1 24  ? 54.183 -23.650 -5.762  1.00 14.28 ?  24  VAL   B CG2  1 
ATOM   4441 H H    . VAL   B 1 24  ? 52.576 -25.184 -7.505  1.00 14.34 ?  24  VAL   B H    1 
ATOM   4442 H HA   . VAL   B 1 24  ? 53.101 -22.640 -7.921  1.00 15.15 ?  24  VAL   B HA   1 
ATOM   4443 H HB   . VAL   B 1 24  ? 54.879 -24.753 -7.310  1.00 16.01 ?  24  VAL   B HB   1 
ATOM   4444 H HG11 . VAL   B 1 24  ? 56.422 -22.944 -6.747  1.00 16.79 ?  24  VAL   B HG11 1 
ATOM   4445 H HG12 . VAL   B 1 24  ? 56.284 -23.308 -8.286  1.00 16.79 ?  24  VAL   B HG12 1 
ATOM   4446 H HG13 . VAL   B 1 24  ? 55.520 -22.044 -7.695  1.00 16.79 ?  24  VAL   B HG13 1 
ATOM   4447 H HG21 . VAL   B 1 24  ? 54.914 -23.893 -5.176  1.00 17.11 ?  24  VAL   B HG21 1 
ATOM   4448 H HG22 . VAL   B 1 24  ? 53.937 -22.722 -5.619  1.00 17.11 ?  24  VAL   B HG22 1 
ATOM   4449 H HG23 . VAL   B 1 24  ? 53.416 -24.223 -5.588  1.00 17.11 ?  24  VAL   B HG23 1 
ATOM   4450 N N    . GLU   B 1 25  ? 54.161 -24.656 -10.177 1.00 13.63 ?  25  GLU   B N    1 
ATOM   4451 C CA   . GLU   B 1 25  ? 54.550 -24.704 -11.580 1.00 15.29 ?  25  GLU   B CA   1 
ATOM   4452 C C    . GLU   B 1 25  ? 53.442 -24.161 -12.471 1.00 14.15 ?  25  GLU   B C    1 
ATOM   4453 O O    . GLU   B 1 25  ? 53.710 -23.439 -13.440 1.00 15.11 ?  25  GLU   B O    1 
ATOM   4454 C CB   . GLU   B 1 25  ? 54.945 -26.130 -11.967 1.00 19.68 ?  25  GLU   B CB   1 
ATOM   4455 C CG   . GLU   B 1 25  ? 56.256 -26.576 -11.329 1.00 25.83 ?  25  GLU   B CG   1 
ATOM   4456 C CD   . GLU   B 1 25  ? 57.368 -25.539 -11.432 1.00 30.95 ?  25  GLU   B CD   1 
ATOM   4457 O OE1  . GLU   B 1 25  ? 57.724 -25.145 -12.564 1.00 32.94 ?  25  GLU   B OE1  1 
ATOM   4458 O OE2  . GLU   B 1 25  ? 57.883 -25.105 -10.375 1.00 32.57 -1 25  GLU   B OE2  1 
ATOM   4459 H H    . GLU   B 1 25  ? 54.135 -25.420 -9.780  1.00 16.34 ?  25  GLU   B H    1 
ATOM   4460 H HA   . GLU   B 1 25  ? 55.311 -24.125 -11.713 1.00 18.32 ?  25  GLU   B HA   1 
ATOM   4461 H HB2  . GLU   B 1 25  ? 54.249 -26.744 -11.672 1.00 23.59 ?  25  GLU   B HB2  1 
ATOM   4462 H HB3  . GLU   B 1 25  ? 55.042 -26.184 -12.931 1.00 23.59 ?  25  GLU   B HB3  1 
ATOM   4463 H HG2  . GLU   B 1 25  ? 56.114 -26.737 -10.390 1.00 30.98 ?  25  GLU   B HG2  1 
ATOM   4464 H HG3  . GLU   B 1 25  ? 56.565 -27.381 -11.772 1.00 30.98 ?  25  GLU   B HG3  1 
ATOM   4465 N N    . GLU   B 1 26  ? 52.186 -24.475 -12.142 1.00 13.07 ?  26  GLU   B N    1 
ATOM   4466 C CA   . GLU   B 1 26  ? 51.063 -23.948 -12.910 1.00 13.93 ?  26  GLU   B CA   1 
ATOM   4467 C C    . GLU   B 1 26  ? 51.014 -22.429 -12.835 1.00 12.99 ?  26  GLU   B C    1 
ATOM   4468 O O    . GLU   B 1 26  ? 50.811 -21.755 -13.849 1.00 14.34 ?  26  GLU   B O    1 
ATOM   4469 C CB   . GLU   B 1 26  ? 49.745 -24.522 -12.393 1.00 15.46 ?  26  GLU   B CB   1 
ATOM   4470 C CG   . GLU   B 1 26  ? 49.280 -25.785 -13.087 1.00 19.42 ?  26  GLU   B CG   1 
ATOM   4471 C CD   . GLU   B 1 26  ? 49.038 -25.616 -14.586 1.00 20.88 ?  26  GLU   B CD   1 
ATOM   4472 O OE1  . GLU   B 1 26  ? 48.055 -24.970 -15.007 1.00 21.56 ?  26  GLU   B OE1  1 
ATOM   4473 O OE2  . GLU   B 1 26  ? 49.833 -26.174 -15.348 1.00 23.51 -1 26  GLU   B OE2  1 
ATOM   4474 H H    . GLU   B 1 26  ? 51.956 -24.985 -11.481 1.00 15.66 ?  26  GLU   B H    1 
ATOM   4475 H HA   . GLU   B 1 26  ? 51.167 -24.204 -13.838 1.00 16.69 ?  26  GLU   B HA   1 
ATOM   4476 H HB2  . GLU   B 1 26  ? 49.842 -24.727 -11.448 1.00 18.53 ?  26  GLU   B HB2  1 
ATOM   4477 H HB3  . GLU   B 1 26  ? 49.049 -23.852 -12.506 1.00 18.53 ?  26  GLU   B HB3  1 
ATOM   4478 H HG2  . GLU   B 1 26  ? 49.961 -26.459 -12.978 1.00 23.27 ?  26  GLU   B HG2  1 
ATOM   4479 H HG3  . GLU   B 1 26  ? 48.447 -26.075 -12.687 1.00 23.27 ?  26  GLU   B HG3  1 
ATOM   4480 N N    . ALA   B 1 27  ? 51.156 -21.875 -11.631 1.00 12.11 ?  27  ALA   B N    1 
ATOM   4481 C CA   . ALA   B 1 27  ? 51.120 -20.425 -11.486 1.00 12.59 ?  27  ALA   B CA   1 
ATOM   4482 C C    . ALA   B 1 27  ? 52.184 -19.764 -12.353 1.00 13.62 ?  27  ALA   B C    1 
ATOM   4483 O O    . ALA   B 1 27  ? 51.915 -18.770 -13.040 1.00 14.18 ?  27  ALA   B O    1 
ATOM   4484 C CB   . ALA   B 1 27  ? 51.296 -20.040 -10.017 1.00 12.78 ?  27  ALA   B CB   1 
ATOM   4485 H H    . ALA   B 1 27  ? 51.263 -22.311 -10.895 1.00 14.51 ?  27  ALA   B H    1 
ATOM   4486 H HA   . ALA   B 1 27  ? 50.258 -20.099 -11.773 1.00 15.08 ?  27  ALA   B HA   1 
ATOM   4487 H HB1  . ALA   B 1 27  ? 51.269 -19.073 -9.936  1.00 15.31 ?  27  ALA   B HB1  1 
ATOM   4488 H HB2  . ALA   B 1 27  ? 50.577 -20.434 -9.497  1.00 15.31 ?  27  ALA   B HB2  1 
ATOM   4489 H HB3  . ALA   B 1 27  ? 52.152 -20.372 -9.699  1.00 15.31 ?  27  ALA   B HB3  1 
ATOM   4490 N N    . LYS   B 1 28  ? 53.401 -20.308 -12.346 1.00 14.78 ?  28  LYS   B N    1 
ATOM   4491 C CA   . LYS   B 1 28  ? 54.475 -19.697 -13.123 1.00 17.15 ?  28  LYS   B CA   1 
ATOM   4492 C C    . LYS   B 1 28  ? 54.215 -19.786 -14.621 1.00 17.47 ?  28  LYS   B C    1 
ATOM   4493 O O    . LYS   B 1 28  ? 54.612 -18.885 -15.370 1.00 18.48 ?  28  LYS   B O    1 
ATOM   4494 C CB   . LYS   B 1 28  ? 55.832 -20.294 -12.731 1.00 20.90 ?  28  LYS   B CB   1 
ATOM   4495 C CG   . LYS   B 1 28  ? 56.234 -19.943 -11.299 1.00 24.84 ?  28  LYS   B CG   1 
ATOM   4496 C CD   . LYS   B 1 28  ? 57.650 -20.372 -10.938 1.00 29.69 ?  28  LYS   B CD   1 
ATOM   4497 C CE   . LYS   B 1 28  ? 57.734 -21.855 -10.669 1.00 34.11 ?  28  LYS   B CE   1 
ATOM   4498 N NZ   . LYS   B 1 28  ? 59.074 -22.235 -10.138 1.00 36.45 ?  28  LYS   B NZ   1 
ATOM   4499 H H    . LYS   B 1 28  ? 53.634 -21.005 -11.898 1.00 17.71 ?  28  LYS   B H    1 
ATOM   4500 H HA   . LYS   B 1 28  ? 54.512 -18.757 -12.906 1.00 20.55 ?  28  LYS   B HA   1 
ATOM   4501 H HB2  . LYS   B 1 28  ? 55.794 -21.258 -12.802 1.00 25.06 ?  28  LYS   B HB2  1 
ATOM   4502 H HB3  . LYS   B 1 28  ? 56.519 -19.944 -13.327 1.00 25.06 ?  28  LYS   B HB3  1 
ATOM   4503 H HG2  . LYS   B 1 28  ? 56.176 -18.978 -11.189 1.00 29.78 ?  28  LYS   B HG2  1 
ATOM   4504 H HG3  . LYS   B 1 28  ? 55.624 -20.380 -10.690 1.00 29.78 ?  28  LYS   B HG3  1 
ATOM   4505 H HD2  . LYS   B 1 28  ? 58.244 -20.158 -11.674 1.00 35.61 ?  28  LYS   B HD2  1 
ATOM   4506 H HD3  . LYS   B 1 28  ? 57.927 -19.897 -10.137 1.00 35.61 ?  28  LYS   B HD3  1 
ATOM   4507 H HE2  . LYS   B 1 28  ? 57.064 -22.098 -10.010 1.00 40.91 ?  28  LYS   B HE2  1 
ATOM   4508 H HE3  . LYS   B 1 28  ? 57.584 -22.339 -11.495 1.00 40.91 ?  28  LYS   B HE3  1 
ATOM   4509 H HZ1  . LYS   B 1 28  ? 59.104 -23.110 -9.986  1.00 43.71 ?  28  LYS   B HZ1  1 
ATOM   4510 H HZ2  . LYS   B 1 28  ? 59.705 -22.021 -10.728 1.00 43.71 ?  28  LYS   B HZ2  1 
ATOM   4511 H HZ3  . LYS   B 1 28  ? 59.233 -21.803 -9.376  1.00 43.71 ?  28  LYS   B HZ3  1 
ATOM   4512 N N    . LYS   B 1 29  ? 53.520 -20.831 -15.072 1.00 18.39 ?  29  LYS   B N    1 
ATOM   4513 C CA   . LYS   B 1 29  ? 53.253 -20.997 -16.496 1.00 21.19 ?  29  LYS   B CA   1 
ATOM   4514 C C    . LYS   B 1 29  ? 52.002 -20.254 -16.955 1.00 19.73 ?  29  LYS   B C    1 
ATOM   4515 O O    . LYS   B 1 29  ? 52.005 -19.651 -18.034 1.00 20.96 ?  29  LYS   B O    1 
ATOM   4516 C CB   . LYS   B 1 29  ? 53.125 -22.484 -16.837 1.00 26.20 ?  29  LYS   B CB   1 
ATOM   4517 C CG   . LYS   B 1 29  ? 52.900 -22.759 -18.314 1.00 30.91 ?  29  LYS   B CG   1 
ATOM   4518 C CD   . LYS   B 1 29  ? 53.095 -24.233 -18.643 1.00 34.65 ?  29  LYS   B CD   1 
ATOM   4519 C CE   . LYS   B 1 29  ? 51.957 -25.092 -18.115 1.00 37.15 ?  29  LYS   B CE   1 
ATOM   4520 N NZ   . LYS   B 1 29  ? 52.186 -26.541 -18.392 1.00 38.49 ?  29  LYS   B NZ   1 
ATOM   4521 H H    . LYS   B 1 29  ? 53.184 -21.456 -14.571 1.00 22.05 ?  29  LYS   B H    1 
ATOM   4522 H HA   . LYS   B 1 29  ? 54.006 -20.646 -16.993 1.00 25.40 ?  29  LYS   B HA   1 
ATOM   4523 H HB2  . LYS   B 1 29  ? 53.945 -22.936 -16.576 1.00 31.41 ?  29  LYS   B HB2  1 
ATOM   4524 H HB3  . LYS   B 1 29  ? 52.376 -22.856 -16.350 1.00 31.41 ?  29  LYS   B HB3  1 
ATOM   4525 H HG2  . LYS   B 1 29  ? 51.992 -22.511 -18.550 1.00 37.07 ?  29  LYS   B HG2  1 
ATOM   4526 H HG3  . LYS   B 1 29  ? 53.535 -22.242 -18.836 1.00 37.07 ?  29  LYS   B HG3  1 
ATOM   4527 H HD2  . LYS   B 1 29  ? 53.134 -24.343 -19.605 1.00 41.56 ?  29  LYS   B HD2  1 
ATOM   4528 H HD3  . LYS   B 1 29  ? 53.920 -24.545 -18.237 1.00 41.56 ?  29  LYS   B HD3  1 
ATOM   4529 H HE2  . LYS   B 1 29  ? 51.884 -24.975 -17.155 1.00 44.55 ?  29  LYS   B HE2  1 
ATOM   4530 H HE3  . LYS   B 1 29  ? 51.129 -24.827 -18.548 1.00 44.55 ?  29  LYS   B HE3  1 
ATOM   4531 H HZ1  . LYS   B 1 29  ? 51.508 -27.023 -18.076 1.00 46.16 ?  29  LYS   B HZ1  1 
ATOM   4532 H HZ2  . LYS   B 1 29  ? 52.251 -26.676 -19.270 1.00 46.16 ?  29  LYS   B HZ2  1 
ATOM   4533 H HZ3  . LYS   B 1 29  ? 52.939 -26.810 -18.002 1.00 46.16 ?  29  LYS   B HZ3  1 
ATOM   4534 N N    . VAL   B 1 30  ? 50.933 -20.299 -16.156 1.00 17.67 ?  30  VAL   B N    1 
ATOM   4535 C CA   . VAL   B 1 30  ? 49.643 -19.718 -16.532 1.00 17.86 ?  30  VAL   B CA   1 
ATOM   4536 C C    . VAL   B 1 30  ? 49.640 -18.207 -16.383 1.00 16.33 ?  30  VAL   B C    1 
ATOM   4537 O O    . VAL   B 1 30  ? 48.896 -17.505 -17.089 1.00 16.78 ?  30  VAL   B O    1 
ATOM   4538 C CB   . VAL   B 1 30  ? 48.553 -20.331 -15.632 1.00 19.82 ?  30  VAL   B CB   1 
ATOM   4539 C CG1  . VAL   B 1 30  ? 47.269 -19.514 -15.681 1.00 20.68 ?  30  VAL   B CG1  1 
ATOM   4540 C CG2  . VAL   B 1 30  ? 48.302 -21.790 -16.009 1.00 20.69 ?  30  VAL   B CG2  1 
ATOM   4541 H H    . VAL   B 1 30  ? 50.922 -20.692 -15.381 1.00 21.18 ?  30  VAL   B H    1 
ATOM   4542 H HA   . VAL   B 1 30  ? 49.442 -19.954 -17.452 1.00 21.40 ?  30  VAL   B HA   1 
ATOM   4543 H HB   . VAL   B 1 30  ? 48.864 -20.327 -14.714 1.00 23.76 ?  30  VAL   B HB   1 
ATOM   4544 H HG11 . VAL   B 1 30  ? 46.532 -20.089 -15.427 1.00 24.79 ?  30  VAL   B HG11 1 
ATOM   4545 H HG12 . VAL   B 1 30  ? 47.337 -18.776 -15.057 1.00 24.79 ?  30  VAL   B HG12 1 
ATOM   4546 H HG13 . VAL   B 1 30  ? 47.130 -19.191 -16.580 1.00 24.79 ?  30  VAL   B HG13 1 
ATOM   4547 H HG21 . VAL   B 1 30  ? 47.616 -22.160 -15.425 1.00 24.80 ?  30  VAL   B HG21 1 
ATOM   4548 H HG22 . VAL   B 1 30  ? 48.000 -21.834 -16.932 1.00 24.80 ?  30  VAL   B HG22 1 
ATOM   4549 H HG23 . VAL   B 1 30  ? 49.124 -22.292 -15.908 1.00 24.80 ?  30  VAL   B HG23 1 
ATOM   4550 N N    A LYS   B 1 31  ? 50.446 -17.686 -15.465 0.48 15.96 ?  31  LYS   B N    1 
ATOM   4551 N N    B LYS   B 1 31  ? 50.444 -17.688 -15.463 0.52 15.82 ?  31  LYS   B N    1 
ATOM   4552 C CA   A LYS   B 1 31  ? 50.454 -16.271 -15.118 0.48 16.57 ?  31  LYS   B CA   1 
ATOM   4553 C CA   B LYS   B 1 31  ? 50.454 -16.272 -15.118 0.52 16.39 ?  31  LYS   B CA   1 
ATOM   4554 C C    A LYS   B 1 31  ? 49.060 -15.771 -14.724 0.48 14.61 ?  31  LYS   B C    1 
ATOM   4555 C C    B LYS   B 1 31  ? 49.059 -15.774 -14.726 0.52 14.48 ?  31  LYS   B C    1 
ATOM   4556 O O    A LYS   B 1 31  ? 48.522 -14.854 -15.352 0.48 14.96 ?  31  LYS   B O    1 
ATOM   4557 O O    B LYS   B 1 31  ? 48.519 -14.859 -15.359 0.52 14.84 ?  31  LYS   B O    1 
ATOM   4558 C CB   A LYS   B 1 31  ? 51.056 -15.431 -16.236 0.48 19.05 ?  31  LYS   B CB   1 
ATOM   4559 C CB   B LYS   B 1 31  ? 51.055 -15.440 -16.243 0.52 18.79 ?  31  LYS   B CB   1 
ATOM   4560 C CG   A LYS   B 1 31  ? 52.505 -15.812 -16.539 0.48 21.78 ?  31  LYS   B CG   1 
ATOM   4561 C CG   B LYS   B 1 31  ? 52.473 -15.886 -16.598 0.52 21.52 ?  31  LYS   B CG   1 
ATOM   4562 C CD   A LYS   B 1 31  ? 53.100 -14.968 -17.647 0.48 24.56 ?  31  LYS   B CD   1 
ATOM   4563 C CD   B LYS   B 1 31  ? 53.063 -15.081 -17.735 0.52 24.38 ?  31  LYS   B CD   1 
ATOM   4564 C CE   A LYS   B 1 31  ? 54.575 -15.268 -17.828 0.48 26.70 ?  31  LYS   B CE   1 
ATOM   4565 C CE   B LYS   B 1 31  ? 54.559 -15.306 -17.838 0.52 26.55 ?  31  LYS   B CE   1 
ATOM   4566 N NZ   A LYS   B 1 31  ? 55.355 -14.958 -16.596 0.48 27.80 ?  31  LYS   B NZ   1 
ATOM   4567 N NZ   B LYS   B 1 31  ? 55.262 -14.897 -16.588 0.52 27.63 ?  31  LYS   B NZ   1 
ATOM   4568 H H    A LYS   B 1 31  ? 51.022 -18.156 -15.025 0.48 19.13 ?  31  LYS   B H    1 
ATOM   4569 H H    B LYS   B 1 31  ? 51.021 -18.159 -15.024 0.52 18.95 ?  31  LYS   B H    1 
ATOM   4570 H HA   A LYS   B 1 31  ? 51.020 -16.171 -14.347 0.48 19.86 ?  31  LYS   B HA   1 
ATOM   4571 H HA   B LYS   B 1 31  ? 51.019 -16.169 -14.347 0.52 19.64 ?  31  LYS   B HA   1 
ATOM   4572 H HB2  A LYS   B 1 31  ? 50.539 -15.556 -17.046 0.48 22.84 ?  31  LYS   B HB2  1 
ATOM   4573 H HB2  B LYS   B 1 31  ? 50.506 -15.527 -17.036 0.52 22.53 ?  31  LYS   B HB2  1 
ATOM   4574 H HB3  A LYS   B 1 31  ? 51.041 -14.502 -15.966 0.48 22.84 ?  31  LYS   B HB3  1 
ATOM   4575 H HB3  B LYS   B 1 31  ? 51.093 -14.516 -15.958 0.52 22.53 ?  31  LYS   B HB3  1 
ATOM   4576 H HG2  A LYS   B 1 31  ? 53.037 -15.685 -15.737 0.48 26.12 ?  31  LYS   B HG2  1 
ATOM   4577 H HG2  B LYS   B 1 31  ? 53.038 -15.779 -15.817 0.52 25.80 ?  31  LYS   B HG2  1 
ATOM   4578 H HG3  A LYS   B 1 31  ? 52.538 -16.743 -16.814 0.48 26.12 ?  31  LYS   B HG3  1 
ATOM   4579 H HG3  B LYS   B 1 31  ? 52.456 -16.819 -16.867 0.52 25.80 ?  31  LYS   B HG3  1 
ATOM   4580 H HD2  A LYS   B 1 31  ? 52.641 -15.167 -18.478 0.48 29.45 ?  31  LYS   B HD2  1 
ATOM   4581 H HD2  B LYS   B 1 31  ? 52.652 -15.360 -18.568 0.52 29.23 ?  31  LYS   B HD2  1 
ATOM   4582 H HD3  A LYS   B 1 31  ? 53.001 -14.031 -17.421 0.48 29.45 ?  31  LYS   B HD3  1 
ATOM   4583 H HD3  B LYS   B 1 31  ? 52.903 -14.140 -17.575 0.52 29.23 ?  31  LYS   B HD3  1 
ATOM   4584 H HE2  A LYS   B 1 31  ? 54.688 -16.211 -18.029 0.48 32.01 ?  31  LYS   B HE2  1 
ATOM   4585 H HE2  B LYS   B 1 31  ? 54.733 -16.249 -17.989 0.52 31.84 ?  31  LYS   B HE2  1 
ATOM   4586 H HE3  A LYS   B 1 31  ? 54.924 -14.727 -18.553 0.48 32.01 ?  31  LYS   B HE3  1 
ATOM   4587 H HE3  B LYS   B 1 31  ? 54.911 -14.779 -18.571 0.52 31.84 ?  31  LYS   B HE3  1 
ATOM   4588 H HZ1  A LYS   B 1 31  ? 56.225 -15.054 -16.754 0.48 33.34 ?  31  LYS   B HZ1  1 
ATOM   4589 H HZ1  B LYS   B 1 31  ? 56.141 -14.883 -16.724 0.52 33.13 ?  31  LYS   B HZ1  1 
ATOM   4590 H HZ2  A LYS   B 1 31  ? 55.198 -14.120 -16.340 0.48 33.34 ?  31  LYS   B HZ2  1 
ATOM   4591 H HZ2  B LYS   B 1 31  ? 54.994 -14.085 -16.341 0.52 33.13 ?  31  LYS   B HZ2  1 
ATOM   4592 H HZ3  A LYS   B 1 31  ? 55.119 -15.509 -15.938 0.48 33.34 ?  31  LYS   B HZ3  1 
ATOM   4593 H HZ3  B LYS   B 1 31  ? 55.081 -15.472 -15.932 0.52 33.13 ?  31  LYS   B HZ3  1 
ATOM   4594 N N    . PRO   B 1 32  ? 48.462 -16.345 -13.677 1.00 13.06 ?  32  PRO   B N    1 
ATOM   4595 C CA   . PRO   B 1 32  ? 47.090 -15.975 -13.304 1.00 12.11 ?  32  PRO   B CA   1 
ATOM   4596 C C    . PRO   B 1 32  ? 47.027 -14.629 -12.599 1.00 12.23 ?  32  PRO   B C    1 
ATOM   4597 O O    . PRO   B 1 32  ? 47.961 -14.216 -11.904 1.00 13.52 ?  32  PRO   B O    1 
ATOM   4598 C CB   . PRO   B 1 32  ? 46.697 -17.086 -12.322 1.00 12.71 ?  32  PRO   B CB   1 
ATOM   4599 C CG   . PRO   B 1 32  ? 48.008 -17.413 -11.647 1.00 12.89 ?  32  PRO   B CG   1 
ATOM   4600 C CD   . PRO   B 1 32  ? 49.057 -17.301 -12.720 1.00 13.18 ?  32  PRO   B CD   1 
ATOM   4601 H HA   . PRO   B 1 32  ? 46.498 -15.991 -14.083 1.00 14.51 ?  32  PRO   B HA   1 
ATOM   4602 H HB2  . PRO   B 1 32  ? 46.045 -16.752 -11.687 1.00 15.23 ?  32  PRO   B HB2  1 
ATOM   4603 H HB3  . PRO   B 1 32  ? 46.349 -17.856 -12.806 1.00 15.23 ?  32  PRO   B HB3  1 
ATOM   4604 H HG2  . PRO   B 1 32  ? 48.176 -16.775 -10.937 1.00 15.44 ?  32  PRO   B HG2  1 
ATOM   4605 H HG3  . PRO   B 1 32  ? 47.978 -18.317 -11.294 1.00 15.44 ?  32  PRO   B HG3  1 
ATOM   4606 H HD2  . PRO   B 1 32  ? 49.874 -16.938 -12.350 1.00 15.79 ?  32  PRO   B HD2  1 
ATOM   4607 H HD3  . PRO   B 1 32  ? 49.200 -18.162 -13.137 1.00 15.79 ?  32  PRO   B HD3  1 
ATOM   4608 N N    . THR   B 1 33  ? 45.873 -13.969 -12.750 1.00 12.01 ?  33  THR   B N    1 
ATOM   4609 C CA   . THR   B 1 33  ? 45.594 -12.794 -11.930 1.00 12.38 ?  33  THR   B CA   1 
ATOM   4610 C C    . THR   B 1 33  ? 45.553 -13.152 -10.449 1.00 12.01 ?  33  THR   B C    1 
ATOM   4611 O O    . THR   B 1 33  ? 46.029 -12.377 -9.606  1.00 13.09 ?  33  THR   B O    1 
ATOM   4612 C CB   . THR   B 1 33  ? 44.273 -12.153 -12.366 1.00 12.84 ?  33  THR   B CB   1 
ATOM   4613 O OG1  . THR   B 1 33  ? 44.293 -11.908 -13.776 1.00 12.85 ?  33  THR   B OG1  1 
ATOM   4614 C CG2  . THR   B 1 33  ? 44.043 -10.852 -11.625 1.00 14.32 ?  33  THR   B CG2  1 
ATOM   4615 H H    . THR   B 1 33  ? 45.248 -14.183 -13.315 1.00 14.38 ?  33  THR   B H    1 
ATOM   4616 H HA   . THR   B 1 33  ? 46.298 -12.147 -12.077 1.00 14.83 ?  33  THR   B HA   1 
ATOM   4617 H HB   . THR   B 1 33  ? 43.538 -12.759 -12.162 1.00 15.38 ?  33  THR   B HB   1 
ATOM   4618 H HG1  . THR   B 1 33  ? 43.570 -11.543 -14.018 1.00 15.40 ?  33  THR   B HG1  1 
ATOM   4619 H HG21 . THR   B 1 33  ? 43.285 -10.386 -12.001 1.00 17.16 ?  33  THR   B HG21 1 
ATOM   4620 H HG22 . THR   B 1 33  ? 43.874 -11.032 -10.687 1.00 17.16 ?  33  THR   B HG22 1 
ATOM   4621 H HG23 . THR   B 1 33  ? 44.831 -10.291 -11.702 1.00 17.16 ?  33  THR   B HG23 1 
ATOM   4622 N N    . VAL   B 1 34  ? 44.984 -14.314 -10.108 1.00 11.40 ?  34  VAL   B N    1 
ATOM   4623 C CA   . VAL   B 1 34  ? 44.779 -14.705 -8.715  1.00 11.04 ?  34  VAL   B CA   1 
ATOM   4624 C C    . VAL   B 1 34  ? 45.193 -16.155 -8.532  1.00 10.10 ?  34  VAL   B C    1 
ATOM   4625 O O    . VAL   B 1 34  ? 44.674 -17.040 -9.222  1.00 10.68 ?  34  VAL   B O    1 
ATOM   4626 C CB   . VAL   B 1 34  ? 43.308 -14.550 -8.279  1.00 11.97 ?  34  VAL   B CB   1 
ATOM   4627 C CG1  . VAL   B 1 34  ? 43.136 -15.005 -6.832  1.00 12.23 ?  34  VAL   B CG1  1 
ATOM   4628 C CG2  . VAL   B 1 34  ? 42.832 -13.124 -8.477  1.00 12.81 ?  34  VAL   B CG2  1 
ATOM   4629 H H    . VAL   B 1 34  ? 44.720 -14.906 -10.680 1.00 13.65 ?  34  VAL   B H    1 
ATOM   4630 H HA   . VAL   B 1 34  ? 45.338 -14.155 -8.143  1.00 13.22 ?  34  VAL   B HA   1 
ATOM   4631 H HB   . VAL   B 1 34  ? 42.764 -15.119 -8.845  1.00 14.34 ?  34  VAL   B HB   1 
ATOM   4632 H HG11 . VAL   B 1 34  ? 42.288 -14.668 -6.501  1.00 14.66 ?  34  VAL   B HG11 1 
ATOM   4633 H HG12 . VAL   B 1 34  ? 43.139 -15.973 -6.802  1.00 14.66 ?  34  VAL   B HG12 1 
ATOM   4634 H HG13 . VAL   B 1 34  ? 43.863 -14.649 -6.300  1.00 14.66 ?  34  VAL   B HG13 1 
ATOM   4635 H HG21 . VAL   B 1 34  ? 41.915 -13.055 -8.174  1.00 15.34 ?  34  VAL   B HG21 1 
ATOM   4636 H HG22 . VAL   B 1 34  ? 43.398 -12.526 -7.968  1.00 15.34 ?  34  VAL   B HG22 1 
ATOM   4637 H HG23 . VAL   B 1 34  ? 42.882 -12.898 -9.424  1.00 15.34 ?  34  VAL   B HG23 1 
ATOM   4638 N N    . VAL   B 1 35  ? 46.092 -16.406 -7.582  1.00 9.39  ?  35  VAL   B N    1 
ATOM   4639 C CA   . VAL   B 1 35  ? 46.321 -17.748 -7.064  1.00 9.33  ?  35  VAL   B CA   1 
ATOM   4640 C C    . VAL   B 1 35  ? 45.772 -17.801 -5.648  1.00 9.16  ?  35  VAL   B C    1 
ATOM   4641 O O    . VAL   B 1 35  ? 45.990 -16.879 -4.855  1.00 9.49  ?  35  VAL   B O    1 
ATOM   4642 C CB   . VAL   B 1 35  ? 47.802 -18.186 -7.143  1.00 10.12 ?  35  VAL   B CB   1 
ATOM   4643 C CG1  . VAL   B 1 35  ? 48.711 -17.352 -6.228  1.00 10.68 ?  35  VAL   B CG1  1 
ATOM   4644 C CG2  . VAL   B 1 35  ? 47.929 -19.682 -6.826  1.00 10.68 ?  35  VAL   B CG2  1 
ATOM   4645 H H    . VAL   B 1 35  ? 46.583 -15.803 -7.215  1.00 11.24 ?  35  VAL   B H    1 
ATOM   4646 H HA   . VAL   B 1 35  ? 45.802 -18.374 -7.592  1.00 11.18 ?  35  VAL   B HA   1 
ATOM   4647 H HB   . VAL   B 1 35  ? 48.107 -18.065 -8.058  1.00 12.12 ?  35  VAL   B HB   1 
ATOM   4648 H HG11 . VAL   B 1 35  ? 49.631 -17.598 -6.402  1.00 12.80 ?  35  VAL   B HG11 1 
ATOM   4649 H HG12 . VAL   B 1 35  ? 48.566 -16.419 -6.419  1.00 12.80 ?  35  VAL   B HG12 1 
ATOM   4650 H HG13 . VAL   B 1 35  ? 48.482 -17.548 -5.305  1.00 12.80 ?  35  VAL   B HG13 1 
ATOM   4651 H HG21 . VAL   B 1 35  ? 48.848 -19.960 -6.934  1.00 12.80 ?  35  VAL   B HG21 1 
ATOM   4652 H HG22 . VAL   B 1 35  ? 47.638 -19.843 -5.911  1.00 12.80 ?  35  VAL   B HG22 1 
ATOM   4653 H HG23 . VAL   B 1 35  ? 47.358 -20.192 -7.436  1.00 12.80 ?  35  VAL   B HG23 1 
ATOM   4654 N N    . VAL   B 1 36  ? 45.054 -18.877 -5.333  1.00 9.25  ?  36  VAL   B N    1 
ATOM   4655 C CA   . VAL   B 1 36  ? 44.511 -19.078 -3.999  1.00 9.09  ?  36  VAL   B CA   1 
ATOM   4656 C C    . VAL   B 1 36  ? 45.521 -19.836 -3.145  1.00 8.54  ?  36  VAL   B C    1 
ATOM   4657 O O    . VAL   B 1 36  ? 46.056 -20.875 -3.559  1.00 9.79  ?  36  VAL   B O    1 
ATOM   4658 C CB   . VAL   B 1 36  ? 43.171 -19.833 -4.069  1.00 9.46  ?  36  VAL   B CB   1 
ATOM   4659 C CG1  . VAL   B 1 36  ? 42.665 -20.197 -2.676  1.00 10.02 ?  36  VAL   B CG1  1 
ATOM   4660 C CG2  . VAL   B 1 36  ? 42.140 -19.011 -4.810  1.00 10.10 ?  36  VAL   B CG2  1 
ATOM   4661 H H    . VAL   B 1 36  ? 44.869 -19.514 -5.881  1.00 11.07 ?  36  VAL   B H    1 
ATOM   4662 H HA   . VAL   B 1 36  ? 44.347 -18.218 -3.583  1.00 10.88 ?  36  VAL   B HA   1 
ATOM   4663 H HB   . VAL   B 1 36  ? 43.297 -20.657 -4.558  1.00 11.33 ?  36  VAL   B HB   1 
ATOM   4664 H HG11 . VAL   B 1 36  ? 41.727 -20.441 -2.731  1.00 12.00 ?  36  VAL   B HG11 1 
ATOM   4665 H HG12 . VAL   B 1 36  ? 43.179 -20.942 -2.332  1.00 12.00 ?  36  VAL   B HG12 1 
ATOM   4666 H HG13 . VAL   B 1 36  ? 42.766 -19.426 -2.089  1.00 12.00 ?  36  VAL   B HG13 1 
ATOM   4667 H HG21 . VAL   B 1 36  ? 41.297 -19.493 -4.828  1.00 12.10 ?  36  VAL   B HG21 1 
ATOM   4668 H HG22 . VAL   B 1 36  ? 42.022 -18.160 -4.358  1.00 12.10 ?  36  VAL   B HG22 1 
ATOM   4669 H HG23 . VAL   B 1 36  ? 42.449 -18.860 -5.719  1.00 12.10 ?  36  VAL   B HG23 1 
ATOM   4670 N N    . ASN   B 1 37  ? 45.731 -19.346 -1.927  1.00 8.80  ?  37  ASN   B N    1 
ATOM   4671 C CA   . ASN   B 1 37  ? 46.479 -20.068 -0.912  1.00 9.14  ?  37  ASN   B CA   1 
ATOM   4672 C C    . ASN   B 1 37  ? 45.523 -20.738 0.066   1.00 9.45  ?  37  ASN   B C    1 
ATOM   4673 O O    . ASN   B 1 37  ? 44.511 -20.159 0.469   1.00 9.83  ?  37  ASN   B O    1 
ATOM   4674 C CB   . ASN   B 1 37  ? 47.400 -19.123 -0.145  1.00 9.07  ?  37  ASN   B CB   1 
ATOM   4675 C CG   . ASN   B 1 37  ? 48.253 -19.836 0.868   1.00 9.43  ?  37  ASN   B CG   1 
ATOM   4676 O OD1  . ASN   B 1 37  ? 48.589 -21.012 0.692   1.00 10.45 ?  37  ASN   B OD1  1 
ATOM   4677 N ND2  . ASN   B 1 37  ? 48.606 -19.137 1.938   1.00 9.61  ?  37  ASN   B ND2  1 
ATOM   4678 H H    . ASN   B 1 37  ? 45.448 -18.576 -1.656  1.00 10.54 ?  37  ASN   B H    1 
ATOM   4679 H HA   . ASN   B 1 37  ? 47.019 -20.759 -1.327  1.00 10.94 ?  37  ASN   B HA   1 
ATOM   4680 H HB2  . ASN   B 1 37  ? 47.992 -18.688 -0.768  1.00 10.86 ?  37  ASN   B HB2  1 
ATOM   4681 H HB3  . ASN   B 1 37  ? 46.863 -18.471 0.329   1.00 10.86 ?  37  ASN   B HB3  1 
ATOM   4682 H HD21 . ASN   B 1 37  ? 49.100 -19.497 2.544   1.00 11.51 ?  37  ASN   B HD21 1 
ATOM   4683 H HD22 . ASN   B 1 37  ? 48.358 -18.323 2.022   1.00 11.51 ?  37  ASN   B HD22 1 
ATOM   4684 N N    . ALA   B 1 38  ? 45.866 -21.973 0.441   1.00 9.52  ?  38  ALA   B N    1 
ATOM   4685 C CA   . ALA   B 1 38  ? 45.214 -22.712 1.523   1.00 9.82  ?  38  ALA   B CA   1 
ATOM   4686 C C    . ALA   B 1 38  ? 45.799 -22.225 2.848   1.00 9.58  ?  38  ALA   B C    1 
ATOM   4687 O O    . ALA   B 1 38  ? 46.696 -22.838 3.436   1.00 10.71 ?  38  ALA   B O    1 
ATOM   4688 C CB   . ALA   B 1 38  ? 45.435 -24.207 1.343   1.00 11.08 ?  38  ALA   B CB   1 
ATOM   4689 H H    . ALA   B 1 38  ? 46.505 -22.416 0.077   1.00 11.40 ?  38  ALA   B H    1 
ATOM   4690 H HA   . ALA   B 1 38  ? 44.262 -22.531 1.521   1.00 11.76 ?  38  ALA   B HA   1 
ATOM   4691 H HB1  . ALA   B 1 38  ? 44.990 -24.680 2.072   1.00 13.27 ?  38  ALA   B HB1  1 
ATOM   4692 H HB2  . ALA   B 1 38  ? 45.049 -24.481 0.497   1.00 13.27 ?  38  ALA   B HB2  1 
ATOM   4693 H HB3  . ALA   B 1 38  ? 46.381 -24.395 1.359   1.00 13.27 ?  38  ALA   B HB3  1 
ATOM   4694 N N    . ALA   B 1 39  ? 45.283 -21.085 3.309   1.00 9.67  ?  39  ALA   B N    1 
ATOM   4695 C CA   . ALA   B 1 39  ? 45.833 -20.354 4.440   1.00 10.22 ?  39  ALA   B CA   1 
ATOM   4696 C C    . ALA   B 1 39  ? 45.217 -20.804 5.760   1.00 9.88  ?  39  ALA   B C    1 
ATOM   4697 O O    . ALA   B 1 39  ? 44.183 -21.472 5.805   1.00 11.06 ?  39  ALA   B O    1 
ATOM   4698 C CB   . ALA   B 1 39  ? 45.593 -18.853 4.250   1.00 10.62 ?  39  ALA   B CB   1 
ATOM   4699 H H    . ALA   B 1 39  ? 44.594 -20.705 2.961   1.00 11.58 ?  39  ALA   B H    1 
ATOM   4700 H HA   . ALA   B 1 39  ? 46.789 -20.503 4.482   1.00 12.24 ?  39  ALA   B HA   1 
ATOM   4701 H HB1  . ALA   B 1 39  ? 45.963 -18.374 5.008   1.00 12.72 ?  39  ALA   B HB1  1 
ATOM   4702 H HB2  . ALA   B 1 39  ? 46.030 -18.561 3.432   1.00 12.72 ?  39  ALA   B HB2  1 
ATOM   4703 H HB3  . ALA   B 1 39  ? 44.639 -18.688 4.188   1.00 12.72 ?  39  ALA   B HB3  1 
ATOM   4704 N N    . ASN   B 1 40  ? 45.859 -20.387 6.847   1.00 10.69 ?  40  ASN   B N    1 
ATOM   4705 C CA   . ASN   B 1 40  ? 45.294 -20.433 8.186   1.00 11.49 ?  40  ASN   B CA   1 
ATOM   4706 C C    . ASN   B 1 40  ? 45.113 -19.004 8.710   1.00 10.95 ?  40  ASN   B C    1 
ATOM   4707 O O    . ASN   B 1 40  ? 45.515 -18.023 8.072   1.00 10.91 ?  40  ASN   B O    1 
ATOM   4708 C CB   . ASN   B 1 40  ? 46.145 -21.313 9.121   1.00 12.02 ?  40  ASN   B CB   1 
ATOM   4709 C CG   . ASN   B 1 40  ? 47.601 -20.901 9.155   1.00 13.31 ?  40  ASN   B CG   1 
ATOM   4710 O OD1  . ASN   B 1 40  ? 47.912 -19.717 9.217   1.00 15.26 ?  40  ASN   B OD1  1 
ATOM   4711 N ND2  . ASN   B 1 40  ? 48.500 -21.872 9.123   1.00 13.48 ?  40  ASN   B ND2  1 
ATOM   4712 H H    . ASN   B 1 40  ? 46.656 -20.063 6.828   1.00 12.81 ?  40  ASN   B H    1 
ATOM   4713 H HA   . ASN   B 1 40  ? 44.411 -20.830 8.136   1.00 13.77 ?  40  ASN   B HA   1 
ATOM   4714 H HB2  . ASN   B 1 40  ? 45.786 -21.247 10.021  1.00 14.40 ?  40  ASN   B HB2  1 
ATOM   4715 H HB3  . ASN   B 1 40  ? 46.095 -22.229 8.811   1.00 14.40 ?  40  ASN   B HB3  1 
ATOM   4716 H HD21 . ASN   B 1 40  ? 49.337 -21.681 9.147   1.00 16.15 ?  40  ASN   B HD21 1 
ATOM   4717 H HD22 . ASN   B 1 40  ? 48.243 -22.690 9.079   1.00 16.15 ?  40  ASN   B HD22 1 
ATOM   4718 N N    . VAL   B 1 41  ? 44.450 -18.877 9.864   1.00 11.49 ?  41  VAL   B N    1 
ATOM   4719 C CA   . VAL   B 1 41  ? 43.988 -17.558 10.309  1.00 11.97 ?  41  VAL   B CA   1 
ATOM   4720 C C    . VAL   B 1 41  ? 45.136 -16.602 10.601  1.00 11.97 ?  41  VAL   B C    1 
ATOM   4721 O O    . VAL   B 1 41  ? 44.957 -15.380 10.515  1.00 12.03 ?  41  VAL   B O    1 
ATOM   4722 C CB   . VAL   B 1 41  ? 43.019 -17.639 11.508  1.00 13.85 ?  41  VAL   B CB   1 
ATOM   4723 C CG1  . VAL   B 1 41  ? 41.710 -18.309 11.113  1.00 14.12 ?  41  VAL   B CG1  1 
ATOM   4724 C CG2  . VAL   B 1 41  ? 43.676 -18.323 12.696  1.00 14.56 ?  41  VAL   B CG2  1 
ATOM   4725 H H    . VAL   B 1 41  ? 44.255 -19.522 10.389  1.00 13.76 ?  41  VAL   B H    1 
ATOM   4726 H HA   . VAL   B 1 41  ? 43.482 -17.164 9.579   1.00 14.34 ?  41  VAL   B HA   1 
ATOM   4727 H HB   . VAL   B 1 41  ? 42.800 -16.732 11.783  1.00 16.60 ?  41  VAL   B HB   1 
ATOM   4728 H HG11 . VAL   B 1 41  ? 41.115 -18.319 11.880  1.00 16.92 ?  41  VAL   B HG11 1 
ATOM   4729 H HG12 . VAL   B 1 41  ? 41.304 -17.809 10.387  1.00 16.92 ?  41  VAL   B HG12 1 
ATOM   4730 H HG13 . VAL   B 1 41  ? 41.896 -19.217 10.827  1.00 16.92 ?  41  VAL   B HG13 1 
ATOM   4731 H HG21 . VAL   B 1 41  ? 43.045 -18.358 13.430  1.00 17.44 ?  41  VAL   B HG21 1 
ATOM   4732 H HG22 . VAL   B 1 41  ? 43.932 -19.225 12.439  1.00 17.44 ?  41  VAL   B HG22 1 
ATOM   4733 H HG23 . VAL   B 1 41  ? 44.462 -17.820 12.957  1.00 17.44 ?  41  VAL   B HG23 1 
ATOM   4734 N N    . TYR   B 1 42  ? 46.302 -17.119 10.986  1.00 12.36 ?  42  TYR   B N    1 
ATOM   4735 C CA   . TYR   B 1 42  ? 47.452 -16.275 11.272  1.00 12.37 ?  42  TYR   B CA   1 
ATOM   4736 C C    . TYR   B 1 42  ? 48.420 -16.192 10.092  1.00 11.85 ?  42  TYR   B C    1 
ATOM   4737 O O    . TYR   B 1 42  ? 49.511 -15.627 10.232  1.00 13.07 ?  42  TYR   B O    1 
ATOM   4738 C CB   . TYR   B 1 42  ? 48.128 -16.702 12.582  1.00 14.33 ?  42  TYR   B CB   1 
ATOM   4739 C CG   . TYR   B 1 42  ? 47.566 -15.978 13.810  1.00 14.00 ?  42  TYR   B CG   1 
ATOM   4740 C CD1  . TYR   B 1 42  ? 47.815 -14.625 14.002  1.00 12.98 ?  42  TYR   B CD1  1 
ATOM   4741 C CD2  . TYR   B 1 42  ? 46.806 -16.639 14.773  1.00 15.28 ?  42  TYR   B CD2  1 
ATOM   4742 C CE1  . TYR   B 1 42  ? 47.327 -13.948 15.089  1.00 13.49 ?  42  TYR   B CE1  1 
ATOM   4743 C CE2  . TYR   B 1 42  ? 46.314 -15.954 15.890  1.00 15.19 ?  42  TYR   B CE2  1 
ATOM   4744 C CZ   . TYR   B 1 42  ? 46.585 -14.603 16.039  1.00 14.84 ?  42  TYR   B CZ   1 
ATOM   4745 O OH   . TYR   B 1 42  ? 46.129 -13.877 17.127  1.00 16.90 ?  42  TYR   B OH   1 
ATOM   4746 H H    . TYR   B 1 42  ? 46.449 -17.966 11.077  1.00 14.81 ?  42  TYR   B H    1 
ATOM   4747 H HA   . TYR   B 1 42  ? 47.122 -15.378 11.410  1.00 14.81 ?  42  TYR   B HA   1 
ATOM   4748 H HB2  . TYR   B 1 42  ? 47.995 -17.654 12.708  1.00 17.17 ?  42  TYR   B HB2  1 
ATOM   4749 H HB3  . TYR   B 1 42  ? 49.075 -16.504 12.522  1.00 17.17 ?  42  TYR   B HB3  1 
ATOM   4750 H HD1  . TYR   B 1 42  ? 48.325 -14.166 13.363  1.00 15.55 ?  42  TYR   B HD1  1 
ATOM   4751 H HD2  . TYR   B 1 42  ? 46.626 -17.549 14.669  1.00 18.31 ?  42  TYR   B HD2  1 
ATOM   4752 H HE1  . TYR   B 1 42  ? 47.518 -13.040 15.190  1.00 16.16 ?  42  TYR   B HE1  1 
ATOM   4753 H HE2  . TYR   B 1 42  ? 45.806 -16.405 16.526  1.00 18.20 ?  42  TYR   B HE2  1 
ATOM   4754 H HH   . TYR   B 1 42  ? 46.382 -13.077 17.056  1.00 20.25 ?  42  TYR   B HH   1 
ATOM   4755 N N    . LEU   B 1 43  ? 48.028 -16.705 8.927   1.00 10.82 ?  43  LEU   B N    1 
ATOM   4756 C CA   . LEU   B 1 43  ? 48.851 -16.638 7.718   1.00 10.77 ?  43  LEU   B CA   1 
ATOM   4757 C C    . LEU   B 1 43  ? 50.263 -17.149 7.977   1.00 11.01 ?  43  LEU   B C    1 
ATOM   4758 O O    . LEU   B 1 43  ? 51.246 -16.555 7.533   1.00 11.68 ?  43  LEU   B O    1 
ATOM   4759 C CB   . LEU   B 1 43  ? 48.875 -15.234 7.102   1.00 11.08 ?  43  LEU   B CB   1 
ATOM   4760 C CG   . LEU   B 1 43  ? 47.519 -14.620 6.738   1.00 11.25 ?  43  LEU   B CG   1 
ATOM   4761 C CD1  . LEU   B 1 43  ? 47.723 -13.219 6.164   1.00 12.76 ?  43  LEU   B CD1  1 
ATOM   4762 C CD2  . LEU   B 1 43  ? 46.735 -15.504 5.777   1.00 11.64 ?  43  LEU   B CD2  1 
ATOM   4763 H H    . LEU   B 1 43  ? 47.286 -17.119 8.807   1.00 12.96 ?  43  LEU   B H    1 
ATOM   4764 H HA   . LEU   B 1 43  ? 48.460 -17.232 7.055   1.00 12.89 ?  43  LEU   B HA   1 
ATOM   4765 H HB2  . LEU   B 1 43  ? 49.307 -14.639 7.727   1.00 13.27 ?  43  LEU   B HB2  1 
ATOM   4766 H HB3  . LEU   B 1 43  ? 49.398 -15.279 6.283   1.00 13.27 ?  43  LEU   B HB3  1 
ATOM   4767 H HG   . LEU   B 1 43  ? 46.998 -14.532 7.548   1.00 13.47 ?  43  LEU   B HG   1 
ATOM   4768 H HD11 . LEU   B 1 43  ? 46.855 -12.840 5.942   1.00 15.29 ?  43  LEU   B HD11 1 
ATOM   4769 H HD12 . LEU   B 1 43  ? 48.160 -12.663 6.831   1.00 15.29 ?  43  LEU   B HD12 1 
ATOM   4770 H HD13 . LEU   B 1 43  ? 48.272 -13.273 5.369   1.00 15.29 ?  43  LEU   B HD13 1 
ATOM   4771 H HD21 . LEU   B 1 43  ? 45.927 -15.038 5.509   1.00 13.95 ?  43  LEU   B HD21 1 
ATOM   4772 H HD22 . LEU   B 1 43  ? 47.281 -15.695 5.000   1.00 13.95 ?  43  LEU   B HD22 1 
ATOM   4773 H HD23 . LEU   B 1 43  ? 46.501 -16.332 6.229   1.00 13.95 ?  43  LEU   B HD23 1 
ATOM   4774 N N    . LYS   B 1 44  ? 50.360 -18.274 8.688   1.00 11.17 ?  44  LYS   B N    1 
ATOM   4775 C CA   . LYS   B 1 44  ? 51.628 -18.946 8.933   1.00 11.74 ?  44  LYS   B CA   1 
ATOM   4776 C C    . LYS   B 1 44  ? 51.749 -20.068 7.910   1.00 11.36 ?  44  LYS   B C    1 
ATOM   4777 O O    . LYS   B 1 44  ? 51.051 -21.083 7.999   1.00 12.60 ?  44  LYS   B O    1 
ATOM   4778 C CB   . LYS   B 1 44  ? 51.678 -19.460 10.369  1.00 13.34 ?  44  LYS   B CB   1 
ATOM   4779 C CG   . LYS   B 1 44  ? 51.887 -18.348 11.385  1.00 16.32 ?  44  LYS   B CG   1 
ATOM   4780 C CD   . LYS   B 1 44  ? 53.063 -17.471 10.946  1.00 20.01 ?  44  LYS   B CD   1 
ATOM   4781 C CE   . LYS   B 1 44  ? 53.723 -16.717 12.074  1.00 23.05 ?  44  LYS   B CE   1 
ATOM   4782 N NZ   . LYS   B 1 44  ? 54.819 -15.837 11.603  1.00 23.89 ?  44  LYS   B NZ   1 
ATOM   4783 H H    . LYS   B 1 44  ? 49.686 -18.668 9.053   1.00 13.37 ?  44  LYS   B H    1 
ATOM   4784 H HA   . LYS   B 1 44  ? 52.356 -18.333 8.768   1.00 14.06 ?  44  LYS   B HA   1 
ATOM   4785 H HB2  . LYS   B 1 44  ? 50.832 -19.900 10.579  1.00 15.99 ?  44  LYS   B HB2  1 
ATOM   4786 H HB3  . LYS   B 1 44  ? 52.406 -20.092 10.459  1.00 15.99 ?  44  LYS   B HB3  1 
ATOM   4787 H HG2  . LYS   B 1 44  ? 51.090 -17.801 11.440  1.00 19.56 ?  44  LYS   B HG2  1 
ATOM   4788 H HG3  . LYS   B 1 44  ? 52.098 -18.735 12.252  1.00 19.56 ?  44  LYS   B HG3  1 
ATOM   4789 H HD2  . LYS   B 1 44  ? 53.731 -18.042 10.522  1.00 23.99 ?  44  LYS   B HD2  1 
ATOM   4790 H HD3  . LYS   B 1 44  ? 52.736 -16.822 10.300  1.00 23.99 ?  44  LYS   B HD3  1 
ATOM   4791 H HE2  . LYS   B 1 44  ? 53.075 -16.137 12.472  1.00 27.63 ?  44  LYS   B HE2  1 
ATOM   4792 H HE3  . LYS   B 1 44  ? 54.075 -17.349 12.723  1.00 27.63 ?  44  LYS   B HE3  1 
ATOM   4793 H HZ1  . LYS   B 1 44  ? 55.177 -15.404 12.294  1.00 28.65 ?  44  LYS   B HZ1  1 
ATOM   4794 H HZ2  . LYS   B 1 44  ? 55.450 -16.316 11.202  1.00 28.65 ?  44  LYS   B HZ2  1 
ATOM   4795 H HZ3  . LYS   B 1 44  ? 54.499 -15.238 11.024  1.00 28.65 ?  44  LYS   B HZ3  1 
ATOM   4796 N N    . HIS   B 1 45  ? 52.605 -19.856 6.914   1.00 10.96 ?  45  HIS   B N    1 
ATOM   4797 C CA   . HIS   B 1 45  ? 52.621 -20.685 5.708   1.00 11.21 ?  45  HIS   B CA   1 
ATOM   4798 C C    . HIS   B 1 45  ? 53.630 -21.815 5.865   1.00 13.38 ?  45  HIS   B C    1 
ATOM   4799 O O    . HIS   B 1 45  ? 54.695 -21.838 5.252   1.00 15.84 ?  45  HIS   B O    1 
ATOM   4800 C CB   . HIS   B 1 45  ? 52.942 -19.829 4.495   1.00 10.98 ?  45  HIS   B CB   1 
ATOM   4801 C CG   . HIS   B 1 45  ? 52.071 -18.627 4.383   1.00 10.93 ?  45  HIS   B CG   1 
ATOM   4802 N ND1  . HIS   B 1 45  ? 50.694 -18.705 4.360   1.00 11.18 ?  45  HIS   B ND1  1 
ATOM   4803 C CD2  . HIS   B 1 45  ? 52.389 -17.314 4.298   1.00 11.92 ?  45  HIS   B CD2  1 
ATOM   4804 C CE1  . HIS   B 1 45  ? 50.208 -17.480 4.255   1.00 10.94 ?  45  HIS   B CE1  1 
ATOM   4805 N NE2  . HIS   B 1 45  ? 51.211 -16.620 4.214   1.00 11.57 ?  45  HIS   B NE2  1 
ATOM   4806 H H    . HIS   B 1 45  ? 53.176 -19.214 6.901   1.00 13.13 ?  45  HIS   B H    1 
ATOM   4807 H HA   . HIS   B 1 45  ? 51.736 -21.073 5.572   1.00 13.42 ?  45  HIS   B HA   1 
ATOM   4808 H HB2  . HIS   B 1 45  ? 53.861 -19.533 4.552   1.00 13.16 ?  45  HIS   B HB2  1 
ATOM   4809 H HB3  . HIS   B 1 45  ? 52.818 -20.365 3.689   1.00 13.16 ?  45  HIS   B HB3  1 
ATOM   4810 H HD2  . HIS   B 1 45  ? 53.247 -16.948 4.292   1.00 14.28 ?  45  HIS   B HD2  1 
ATOM   4811 H HE1  . HIS   B 1 45  ? 49.304 -17.258 4.214   1.00 13.11 ?  45  HIS   B HE1  1 
ATOM   4812 H HE2  . HIS   B 1 45  ? 51.135 -15.763 4.155   1.00 13.86 ?  45  HIS   B HE2  1 
ATOM   4813 N N    A GLY   B 1 46  ? 53.253 -22.787 6.691   0.48 14.53 ?  46  GLY   B N    1 
ATOM   4814 N N    B GLY   B 1 46  ? 53.264 -22.774 6.706   0.52 14.41 ?  46  GLY   B N    1 
ATOM   4815 C CA   A GLY   B 1 46  ? 54.178 -23.832 7.088   0.48 16.43 ?  46  GLY   B CA   1 
ATOM   4816 C CA   B GLY   B 1 46  ? 54.186 -23.832 7.061   0.52 16.18 ?  46  GLY   B CA   1 
ATOM   4817 C C    A GLY   B 1 46  ? 54.233 -25.064 6.206   0.48 18.08 ?  46  GLY   B C    1 
ATOM   4818 C C    B GLY   B 1 46  ? 54.222 -24.997 6.093   0.52 17.90 ?  46  GLY   B C    1 
ATOM   4819 O O    A GLY   B 1 46  ? 55.320 -25.513 5.831   0.48 20.44 ?  46  GLY   B O    1 
ATOM   4820 O O    B GLY   B 1 46  ? 55.273 -25.314 5.526   0.52 20.01 ?  46  GLY   B O    1 
ATOM   4821 H H    A GLY   B 1 46  ? 52.468 -22.845 7.048   0.48 17.42 ?  46  GLY   B H    1 
ATOM   4822 H H    B GLY   B 1 46  ? 52.491 -22.817 7.094   0.52 17.27 ?  46  GLY   B H    1 
ATOM   4823 H HA2  A GLY   B 1 46  ? 55.069 -23.450 7.126   0.48 19.69 ?  46  GLY   B HA2  1 
ATOM   4824 H HA2  B GLY   B 1 46  ? 55.078 -23.457 7.120   0.52 19.39 ?  46  GLY   B HA2  1 
ATOM   4825 H HA3  A GLY   B 1 46  ? 53.942 -24.125 7.981   0.48 19.69 ?  46  GLY   B HA3  1 
ATOM   4826 H HA3  B GLY   B 1 46  ? 53.944 -24.172 7.936   0.52 19.39 ?  46  GLY   B HA3  1 
ATOM   4827 N N    . GLY   B 1 47  ? 53.077 -25.643 5.881   1.00 17.58 ?  47  GLY   B N    1 
ATOM   4828 C CA   . GLY   B 1 47  ? 53.028 -26.911 5.183   1.00 15.23 ?  47  GLY   B CA   1 
ATOM   4829 C C    . GLY   B 1 47  ? 52.121 -26.888 3.968   1.00 13.17 ?  47  GLY   B C    1 
ATOM   4830 O O    . GLY   B 1 47  ? 51.474 -25.885 3.670   1.00 13.44 ?  47  GLY   B O    1 
ATOM   4831 H H    A GLY   B 1 47  ? 52.300 -25.321 6.076   0.48 21.08 ?  47  GLY   B H    1 
ATOM   4832 H H    B GLY   B 1 47  ? 52.305 -25.362 6.146   0.52 21.08 ?  47  GLY   B H    1 
ATOM   4833 H HA2  . GLY   B 1 47  ? 53.919 -27.158 4.891   1.00 18.25 ?  47  GLY   B HA2  1 
ATOM   4834 H HA3  . GLY   B 1 47  ? 52.706 -27.595 5.790   1.00 18.25 ?  47  GLY   B HA3  1 
ATOM   4835 N N    . GLY   B 1 48  ? 52.075 -28.028 3.282   1.00 12.36 ?  48  GLY   B N    1 
ATOM   4836 C CA   . GLY   B 1 48  ? 51.161 -28.177 2.167   1.00 12.18 ?  48  GLY   B CA   1 
ATOM   4837 C C    . GLY   B 1 48  ? 51.295 -27.061 1.160   1.00 11.67 ?  48  GLY   B C    1 
ATOM   4838 O O    . GLY   B 1 48  ? 52.397 -26.597 0.845   1.00 12.03 ?  48  GLY   B O    1 
ATOM   4839 H H    . GLY   B 1 48  ? 52.560 -28.716 3.440   1.00 14.81 ?  48  GLY   B H    1 
ATOM   4840 H HA2  . GLY   B 1 48  ? 51.335 -29.020 1.713   1.00 14.60 ?  48  GLY   B HA2  1 
ATOM   4841 H HA3  . GLY   B 1 48  ? 50.248 -28.185 2.487   1.00 14.60 ?  48  GLY   B HA3  1 
ATOM   4842 N N    . VAL   B 1 49  ? 50.150 -26.627 0.632   1.00 11.47 ?  49  VAL   B N    1 
ATOM   4843 C CA   . VAL   B 1 49  ? 50.137 -25.603 -0.409  1.00 11.42 ?  49  VAL   B CA   1 
ATOM   4844 C C    . VAL   B 1 49  ? 50.796 -24.314 0.079   1.00 10.39 ?  49  VAL   B C    1 
ATOM   4845 O O    . VAL   B 1 49  ? 51.585 -23.692 -0.643  1.00 11.34 ?  49  VAL   B O    1 
ATOM   4846 C CB   . VAL   B 1 49  ? 48.695 -25.352 -0.892  1.00 12.45 ?  49  VAL   B CB   1 
ATOM   4847 C CG1  . VAL   B 1 49  ? 48.626 -24.106 -1.772  1.00 12.80 ?  49  VAL   B CG1  1 
ATOM   4848 C CG2  . VAL   B 1 49  ? 48.167 -26.568 -1.639  1.00 13.93 ?  49  VAL   B CG2  1 
ATOM   4849 H H    . VAL   B 1 49  ? 49.363 -26.900 0.860   1.00 13.74 ?  49  VAL   B H    1 
ATOM   4850 H HA   . VAL   B 1 49  ? 50.640 -25.922 -1.172  1.00 13.68 ?  49  VAL   B HA   1 
ATOM   4851 H HB   . VAL   B 1 49  ? 48.118 -25.203 -0.127  1.00 14.91 ?  49  VAL   B HB   1 
ATOM   4852 H HG11 . VAL   B 1 49  ? 47.796 -24.121 -2.282  1.00 15.33 ?  49  VAL   B HG11 1 
ATOM   4853 H HG12 . VAL   B 1 49  ? 48.647 -23.315 -1.211  1.00 15.33 ?  49  VAL   B HG12 1 
ATOM   4854 H HG13 . VAL   B 1 49  ? 49.381 -24.104 -2.381  1.00 15.33 ?  49  VAL   B HG13 1 
ATOM   4855 H HG21 . VAL   B 1 49  ? 47.259 -26.393 -1.939  1.00 16.69 ?  49  VAL   B HG21 1 
ATOM   4856 H HG22 . VAL   B 1 49  ? 48.737 -26.743 -2.405  1.00 16.69 ?  49  VAL   B HG22 1 
ATOM   4857 H HG23 . VAL   B 1 49  ? 48.173 -27.332 -1.041  1.00 16.69 ?  49  VAL   B HG23 1 
ATOM   4858 N N    . ALA   B 1 50  ? 50.449 -23.869 1.289   1.00 10.33 ?  50  ALA   B N    1 
ATOM   4859 C CA   . ALA   B 1 50  ? 50.972 -22.594 1.770   1.00 10.35 ?  50  ALA   B CA   1 
ATOM   4860 C C    . ALA   B 1 50  ? 52.492 -22.630 1.879   1.00 10.59 ?  50  ALA   B C    1 
ATOM   4861 O O    . ALA   B 1 50  ? 53.175 -21.666 1.514   1.00 10.57 ?  50  ALA   B O    1 
ATOM   4862 C CB   . ALA   B 1 50  ? 50.337 -22.237 3.111   1.00 10.61 ?  50  ALA   B CB   1 
ATOM   4863 H H    . ALA   B 1 50  ? 49.927 -24.276 1.836   1.00 12.37 ?  50  ALA   B H    1 
ATOM   4864 H HA   . ALA   B 1 50  ? 50.744 -21.899 1.139   1.00 12.40 ?  50  ALA   B HA   1 
ATOM   4865 H HB1  . ALA   B 1 50  ? 50.696 -21.387 3.417   1.00 12.71 ?  50  ALA   B HB1  1 
ATOM   4866 H HB2  . ALA   B 1 50  ? 49.376 -22.165 2.997   1.00 12.71 ?  50  ALA   B HB2  1 
ATOM   4867 H HB3  . ALA   B 1 50  ? 50.541 -22.931 3.757   1.00 12.71 ?  50  ALA   B HB3  1 
ATOM   4868 N N    . GLY   B 1 51  ? 53.040 -23.729 2.386   1.00 11.16 ?  51  GLY   B N    1 
ATOM   4869 C CA   . GLY   B 1 51  ? 54.482 -23.835 2.460   1.00 11.87 ?  51  GLY   B CA   1 
ATOM   4870 C C    . GLY   B 1 51  ? 55.129 -23.778 1.091   1.00 11.65 ?  51  GLY   B C    1 
ATOM   4871 O O    . GLY   B 1 51  ? 56.179 -23.150 0.917   1.00 12.53 ?  51  GLY   B O    1 
ATOM   4872 H H    . GLY   B 1 51  ? 52.611 -24.415 2.682   1.00 13.36 ?  51  GLY   B H    1 
ATOM   4873 H HA2  . GLY   B 1 51  ? 54.835 -23.102 2.994   1.00 14.22 ?  51  GLY   B HA2  1 
ATOM   4874 H HA3  . GLY   B 1 51  ? 54.731 -24.670 2.884   1.00 14.22 ?  51  GLY   B HA3  1 
ATOM   4875 N N    . ALA   B 1 52  ? 54.522 -24.438 0.103   1.00 11.04 ?  52  ALA   B N    1 
ATOM   4876 C CA   . ALA   B 1 52  ? 55.093 -24.444 -1.238  1.00 11.49 ?  52  ALA   B CA   1 
ATOM   4877 C C    . ALA   B 1 52  ? 55.011 -23.067 -1.890  1.00 11.14 ?  52  ALA   B C    1 
ATOM   4878 O O    . ALA   B 1 52  ? 55.982 -22.611 -2.516  1.00 11.81 ?  52  ALA   B O    1 
ATOM   4879 C CB   . ALA   B 1 52  ? 54.391 -25.488 -2.098  1.00 12.25 ?  52  ALA   B CB   1 
ATOM   4880 H H    . ALA   B 1 52  ? 53.783 -24.873 0.186   1.00 13.23 ?  52  ALA   B H    1 
ATOM   4881 H HA   . ALA   B 1 52  ? 56.028 -24.685 -1.171  1.00 13.76 ?  52  ALA   B HA   1 
ATOM   4882 H HB1  . ALA   B 1 52  ? 54.790 -25.478 -2.983  1.00 14.67 ?  52  ALA   B HB1  1 
ATOM   4883 H HB2  . ALA   B 1 52  ? 54.515 -26.361 -1.691  1.00 14.67 ?  52  ALA   B HB2  1 
ATOM   4884 H HB3  . ALA   B 1 52  ? 53.451 -25.275 -2.152  1.00 14.67 ?  52  ALA   B HB3  1 
ATOM   4885 N N    . LEU   B 1 53  ? 53.869 -22.385 -1.761  1.00 10.81 ?  53  LEU   B N    1 
ATOM   4886 C CA   . LEU   B 1 53  ? 53.766 -21.046 -2.332  1.00 10.79 ?  53  LEU   B CA   1 
ATOM   4887 C C    . LEU   B 1 53  ? 54.772 -20.108 -1.679  1.00 10.77 ?  53  LEU   B C    1 
ATOM   4888 O O    . LEU   B 1 53  ? 55.476 -19.358 -2.363  1.00 11.57 ?  53  LEU   B O    1 
ATOM   4889 C CB   . LEU   B 1 53  ? 52.340 -20.502 -2.172  1.00 11.28 ?  53  LEU   B CB   1 
ATOM   4890 C CG   . LEU   B 1 53  ? 51.201 -21.223 -2.906  1.00 11.29 ?  53  LEU   B CG   1 
ATOM   4891 C CD1  . LEU   B 1 53  ? 49.852 -20.614 -2.549  1.00 12.87 ?  53  LEU   B CD1  1 
ATOM   4892 C CD2  . LEU   B 1 53  ? 51.405 -21.197 -4.416  1.00 13.20 ?  53  LEU   B CD2  1 
ATOM   4893 H H    . LEU   B 1 53  ? 53.166 -22.663 -1.357  1.00 12.95 ?  53  LEU   B H    1 
ATOM   4894 H HA   . LEU   B 1 53  ? 53.971 -21.091 -3.283  1.00 12.93 ?  53  LEU   B HA   1 
ATOM   4895 H HB2  . LEU   B 1 53  ? 52.122 -20.526 -1.229  1.00 13.51 ?  53  LEU   B HB2  1 
ATOM   4896 H HB3  . LEU   B 1 53  ? 52.335 -19.588 -2.480  1.00 13.51 ?  53  LEU   B HB3  1 
ATOM   4897 H HG   . LEU   B 1 53  ? 51.183 -22.154 -2.628  1.00 13.52 ?  53  LEU   B HG   1 
ATOM   4898 H HD11 . LEU   B 1 53  ? 49.153 -21.094 -3.026  1.00 15.42 ?  53  LEU   B HD11 1 
ATOM   4899 H HD12 . LEU   B 1 53  ? 49.712 -20.700 -1.591  1.00 15.42 ?  53  LEU   B HD12 1 
ATOM   4900 H HD13 . LEU   B 1 53  ? 49.848 -19.682 -2.804  1.00 15.42 ?  53  LEU   B HD13 1 
ATOM   4901 H HD21 . LEU   B 1 53  ? 50.740 -21.762 -4.837  1.00 15.81 ?  53  LEU   B HD21 1 
ATOM   4902 H HD22 . LEU   B 1 53  ? 51.308 -20.284 -4.730  1.00 15.81 ?  53  LEU   B HD22 1 
ATOM   4903 H HD23 . LEU   B 1 53  ? 52.294 -21.526 -4.624  1.00 15.81 ?  53  LEU   B HD23 1 
ATOM   4904 N N    . ASN   B 1 54  ? 54.857 -20.140 -0.351  1.00 10.57 ?  54  ASN   B N    1 
ATOM   4905 C CA   . ASN   B 1 54  ? 55.777 -19.234 0.322   1.00 11.13 ?  54  ASN   B CA   1 
ATOM   4906 C C    . ASN   B 1 54  ? 57.225 -19.513 -0.073  1.00 11.64 ?  54  ASN   B C    1 
ATOM   4907 O O    . ASN   B 1 54  ? 58.000 -18.576 -0.310  1.00 11.83 ?  54  ASN   B O    1 
ATOM   4908 C CB   . ASN   B 1 54  ? 55.610 -19.308 1.830   1.00 11.80 ?  54  ASN   B CB   1 
ATOM   4909 C CG   . ASN   B 1 54  ? 56.580 -18.392 2.538   1.00 11.88 ?  54  ASN   B CG   1 
ATOM   4910 O OD1  . ASN   B 1 54  ? 56.598 -17.186 2.289   1.00 12.02 ?  54  ASN   B OD1  1 
ATOM   4911 N ND2  . ASN   B 1 54  ? 57.419 -18.962 3.399   1.00 13.64 ?  54  ASN   B ND2  1 
ATOM   4912 H H    . ASN   B 1 54  ? 54.406 -20.660 0.162   1.00 12.67 ?  54  ASN   B H    1 
ATOM   4913 H HA   . ASN   B 1 54  ? 55.567 -18.326 0.048   1.00 13.34 ?  54  ASN   B HA   1 
ATOM   4914 H HB2  . ASN   B 1 54  ? 54.707 -19.034 2.067   1.00 14.14 ?  54  ASN   B HB2  1 
ATOM   4915 H HB3  . ASN   B 1 54  ? 55.773 -20.214 2.128   1.00 14.14 ?  54  ASN   B HB3  1 
ATOM   4916 H HD21 . ASN   B 1 54  ? 57.996 -18.483 3.824   1.00 16.34 ?  54  ASN   B HD21 1 
ATOM   4917 H HD22 . ASN   B 1 54  ? 57.387 -19.812 3.537   1.00 16.34 ?  54  ASN   B HD22 1 
ATOM   4918 N N    . LYS   B 1 55  ? 57.607 -20.795 -0.140  1.00 12.18 ?  55  LYS   B N    1 
ATOM   4919 C CA   . LYS   B 1 55  ? 58.959 -21.143 -0.561  1.00 13.30 ?  55  LYS   B CA   1 
ATOM   4920 C C    . LYS   B 1 55  ? 59.253 -20.593 -1.950  1.00 13.02 ?  55  LYS   B C    1 
ATOM   4921 O O    . LYS   B 1 55  ? 60.357 -20.089 -2.203  1.00 13.62 ?  55  LYS   B O    1 
ATOM   4922 C CB   . LYS   B 1 55  ? 59.140 -22.661 -0.518  1.00 15.10 ?  55  LYS   B CB   1 
ATOM   4923 C CG   . LYS   B 1 55  ? 60.516 -23.137 -0.948  1.00 18.80 ?  55  LYS   B CG   1 
ATOM   4924 C CD   . LYS   B 1 55  ? 60.673 -24.638 -0.755  1.00 22.54 ?  55  LYS   B CD   1 
ATOM   4925 C CE   . LYS   B 1 55  ? 60.810 -25.007 0.722   1.00 25.47 ?  55  LYS   B CE   1 
ATOM   4926 N NZ   . LYS   B 1 55  ? 61.145 -26.437 0.917   1.00 27.10 ?  55  LYS   B NZ   1 
ATOM   4927 H H    . LYS   B 1 55  ? 57.101 -21.465 0.050   1.00 14.59 ?  55  LYS   B H    1 
ATOM   4928 H HA   . LYS   B 1 55  ? 59.590 -20.746 0.053   1.00 15.93 ?  55  LYS   B HA   1 
ATOM   4929 H HB2  . LYS   B 1 55  ? 58.990 -22.960 0.393   1.00 18.10 ?  55  LYS   B HB2  1 
ATOM   4930 H HB3  . LYS   B 1 55  ? 58.486 -23.069 -1.107  1.00 18.10 ?  55  LYS   B HB3  1 
ATOM   4931 H HG2  . LYS   B 1 55  ? 60.644 -22.936 -1.889  1.00 22.54 ?  55  LYS   B HG2  1 
ATOM   4932 H HG3  . LYS   B 1 55  ? 61.190 -22.687 -0.414  1.00 22.54 ?  55  LYS   B HG3  1 
ATOM   4933 H HD2  . LYS   B 1 55  ? 59.891 -25.092 -1.108  1.00 27.03 ?  55  LYS   B HD2  1 
ATOM   4934 H HD3  . LYS   B 1 55  ? 61.472 -24.940 -1.216  1.00 27.03 ?  55  LYS   B HD3  1 
ATOM   4935 H HE2  . LYS   B 1 55  ? 61.516 -24.467 1.115   1.00 30.54 ?  55  LYS   B HE2  1 
ATOM   4936 H HE3  . LYS   B 1 55  ? 59.967 -24.824 1.171   1.00 30.54 ?  55  LYS   B HE3  1 
ATOM   4937 H HZ1  . LYS   B 1 55  ? 61.181 -26.622 1.787   1.00 32.50 ?  55  LYS   B HZ1  1 
ATOM   4938 H HZ2  . LYS   B 1 55  ? 60.523 -26.946 0.538   1.00 32.50 ?  55  LYS   B HZ2  1 
ATOM   4939 H HZ3  . LYS   B 1 55  ? 61.933 -26.616 0.549   1.00 32.50 ?  55  LYS   B HZ3  1 
ATOM   4940 N N    . ALA   B 1 56  ? 58.278 -20.676 -2.863  1.00 12.38 ?  56  ALA   B N    1 
ATOM   4941 C CA   . ALA   B 1 56  ? 58.503 -20.182 -4.216  1.00 13.31 ?  56  ALA   B CA   1 
ATOM   4942 C C    . ALA   B 1 56  ? 58.789 -18.687 -4.217  1.00 13.03 ?  56  ALA   B C    1 
ATOM   4943 O O    . ALA   B 1 56  ? 59.530 -18.197 -5.081  1.00 14.02 ?  56  ALA   B O    1 
ATOM   4944 C CB   . ALA   B 1 56  ? 57.306 -20.516 -5.107  1.00 14.00 ?  56  ALA   B CB   1 
ATOM   4945 H H    . ALA   B 1 56  ? 57.486 -20.994 -2.723  1.00 14.84 ?  56  ALA   B H    1 
ATOM   4946 H HA   . ALA   B 1 56  ? 59.278 -20.625 -4.584  1.00 15.94 ?  56  ALA   B HA   1 
ATOM   4947 H HB1  . ALA   B 1 56  ? 57.478 -20.188 -6.006  1.00 16.78 ?  56  ALA   B HB1  1 
ATOM   4948 H HB2  . ALA   B 1 56  ? 57.188 -21.480 -5.128  1.00 16.78 ?  56  ALA   B HB2  1 
ATOM   4949 H HB3  . ALA   B 1 56  ? 56.511 -20.093 -4.748  1.00 16.78 ?  56  ALA   B HB3  1 
ATOM   4950 N N    . THR   B 1 57  ? 58.218 -17.950 -3.260  1.00 12.78 ?  57  THR   B N    1 
ATOM   4951 C CA   . THR   B 1 57  ? 58.455 -16.513 -3.137  1.00 12.70 ?  57  THR   B CA   1 
ATOM   4952 C C    . THR   B 1 57  ? 59.707 -16.184 -2.328  1.00 13.45 ?  57  THR   B C    1 
ATOM   4953 O O    . THR   B 1 57  ? 59.943 -15.010 -2.026  1.00 13.74 ?  57  THR   B O    1 
ATOM   4954 C CB   . THR   B 1 57  ? 57.254 -15.784 -2.505  1.00 11.91 ?  57  THR   B CB   1 
ATOM   4955 O OG1  . THR   B 1 57  ? 57.233 -15.993 -1.084  1.00 12.26 ?  57  THR   B OG1  1 
ATOM   4956 C CG2  . THR   B 1 57  ? 55.929 -16.202 -3.145  1.00 12.01 ?  57  THR   B CG2  1 
ATOM   4957 H H    . THR   B 1 57  ? 57.669 -18.260 -2.670  1.00 15.31 ?  57  THR   B H    1 
ATOM   4958 H HA   . THR   B 1 57  ? 58.574 -16.146 -4.027  1.00 15.22 ?  57  THR   B HA   1 
ATOM   4959 H HB   . THR   B 1 57  ? 57.356 -14.831 -2.671  1.00 14.27 ?  57  THR   B HB   1 
ATOM   4960 H HG1  . THR   B 1 57  ? 57.159 -16.814 -0.920  1.00 14.69 ?  57  THR   B HG1  1 
ATOM   4961 H HG21 . THR   B 1 57  ? 55.200 -15.676 -2.782  1.00 14.39 ?  57  THR   B HG21 1 
ATOM   4962 H HG22 . THR   B 1 57  ? 55.966 -16.067 -4.107  1.00 14.39 ?  57  THR   B HG22 1 
ATOM   4963 H HG23 . THR   B 1 57  ? 55.757 -17.140 -2.970  1.00 14.39 ?  57  THR   B HG23 1 
ATOM   4964 N N    . ASN   B 1 58  ? 60.502 -17.186 -1.959  1.00 14.68 ?  58  ASN   B N    1 
ATOM   4965 C CA   . ASN   B 1 58  ? 61.693 -16.972 -1.143  1.00 17.24 ?  58  ASN   B CA   1 
ATOM   4966 C C    . ASN   B 1 58  ? 61.350 -16.258 0.165   1.00 14.89 ?  58  ASN   B C    1 
ATOM   4967 O O    . ASN   B 1 58  ? 62.086 -15.386 0.634   1.00 15.40 ?  58  ASN   B O    1 
ATOM   4968 C CB   . ASN   B 1 58  ? 62.785 -16.227 -1.918  1.00 24.02 ?  58  ASN   B CB   1 
ATOM   4969 C CG   . ASN   B 1 58  ? 64.155 -16.391 -1.290  1.00 32.10 ?  58  ASN   B CG   1 
ATOM   4970 O OD1  . ASN   B 1 58  ? 64.456 -17.423 -0.689  1.00 34.80 ?  58  ASN   B OD1  1 
ATOM   4971 N ND2  . ASN   B 1 58  ? 64.993 -15.370 -1.423  1.00 36.65 ?  58  ASN   B ND2  1 
ATOM   4972 H H    . ASN   B 1 58  ? 60.360 -18.013 -2.163  1.00 17.59 ?  58  ASN   B H    1 
ATOM   4973 H HA   . ASN   B 1 58  ? 62.051 -17.843 -0.914  1.00 20.67 ?  58  ASN   B HA   1 
ATOM   4974 H HB2  . ASN   B 1 58  ? 62.824 -16.576 -2.825  1.00 28.80 ?  58  ASN   B HB2  1 
ATOM   4975 H HB3  . ASN   B 1 58  ? 62.574 -15.282 -1.935  1.00 28.80 ?  58  ASN   B HB3  1 
ATOM   4976 H HD21 . ASN   B 1 58  ? 65.782 -15.414 -1.085  1.00 43.95 ?  58  ASN   B HD21 1 
ATOM   4977 H HD22 . ASN   B 1 58  ? 64.745 -14.664 -1.847  1.00 43.95 ?  58  ASN   B HD22 1 
ATOM   4978 N N    . ASN   B 1 59  ? 60.225 -16.642 0.767   1.00 13.72 ?  59  ASN   B N    1 
ATOM   4979 C CA   . ASN   B 1 59  ? 59.748 -16.169 2.065   1.00 13.59 ?  59  ASN   B CA   1 
ATOM   4980 C C    . ASN   B 1 59  ? 59.154 -14.764 2.003   1.00 12.86 ?  59  ASN   B C    1 
ATOM   4981 O O    . ASN   B 1 59  ? 58.721 -14.253 3.042   1.00 13.04 ?  59  ASN   B O    1 
ATOM   4982 C CB   . ASN   B 1 59  ? 60.823 -16.226 3.168   1.00 14.60 ?  59  ASN   B CB   1 
ATOM   4983 C CG   . ASN   B 1 59  ? 60.239 -16.393 4.549   1.00 15.52 ?  59  ASN   B CG   1 
ATOM   4984 O OD1  . ASN   B 1 59  ? 59.404 -17.271 4.781   1.00 15.58 ?  59  ASN   B OD1  1 
ATOM   4985 N ND2  . ASN   B 1 59  ? 60.667 -15.551 5.479   1.00 16.15 ?  59  ASN   B ND2  1 
ATOM   4986 H H    . ASN   B 1 59  ? 59.691 -17.225 0.421   1.00 16.44 ?  59  ASN   B H    1 
ATOM   4987 H HA   . ASN   B 1 59  ? 59.039 -16.766 2.348   1.00 16.28 ?  59  ASN   B HA   1 
ATOM   4988 H HB2  . ASN   B 1 59  ? 61.410 -16.982 3.011   1.00 17.50 ?  59  ASN   B HB2  1 
ATOM   4989 H HB3  . ASN   B 1 59  ? 61.331 -15.402 3.164   1.00 17.50 ?  59  ASN   B HB3  1 
ATOM   4990 H HD21 . ASN   B 1 59  ? 60.362 -15.602 6.283   1.00 19.36 ?  59  ASN   B HD21 1 
ATOM   4991 H HD22 . ASN   B 1 59  ? 61.250 -14.951 5.281   1.00 19.36 ?  59  ASN   B HD22 1 
ATOM   4992 N N    . ALA   B 1 60  ? 59.104 -14.123 0.830   1.00 12.79 ?  60  ALA   B N    1 
ATOM   4993 C CA   . ALA   B 1 60  ? 58.512 -12.789 0.752   1.00 12.71 ?  60  ALA   B CA   1 
ATOM   4994 C C    . ALA   B 1 60  ? 57.042 -12.810 1.152   1.00 11.87 ?  60  ALA   B C    1 
ATOM   4995 O O    . ALA   B 1 60  ? 56.541 -11.861 1.767   1.00 12.85 ?  60  ALA   B O    1 
ATOM   4996 C CB   . ALA   B 1 60  ? 58.673 -12.222 -0.658  1.00 13.83 ?  60  ALA   B CB   1 
ATOM   4997 H H    . ALA   B 1 60  ? 59.406 -14.435 0.089   1.00 15.33 ?  60  ALA   B H    1 
ATOM   4998 H HA   . ALA   B 1 60  ? 58.980 -12.204 1.367   1.00 15.22 ?  60  ALA   B HA   1 
ATOM   4999 H HB1  . ALA   B 1 60  ? 58.275 -11.342 -0.687  1.00 16.57 ?  60  ALA   B HB1  1 
ATOM   5000 H HB2  . ALA   B 1 60  ? 59.619 -12.169 -0.869  1.00 16.57 ?  60  ALA   B HB2  1 
ATOM   5001 H HB3  . ALA   B 1 60  ? 58.227 -12.813 -1.285  1.00 16.57 ?  60  ALA   B HB3  1 
ATOM   5002 N N    . MET   B 1 61  ? 56.331 -13.885 0.802   1.00 11.40 ?  61  MET   B N    1 
ATOM   5003 C CA   . MET   B 1 61  ? 54.935 -14.013 1.197   1.00 10.88 ?  61  MET   B CA   1 
ATOM   5004 C C    . MET   B 1 61  ? 54.795 -14.016 2.718   1.00 11.04 ?  61  MET   B C    1 
ATOM   5005 O O    . MET   B 1 61  ? 53.893 -13.368 3.264   1.00 10.91 ?  61  MET   B O    1 
ATOM   5006 C CB   . MET   B 1 61  ? 54.356 -15.282 0.568   1.00 10.89 ?  61  MET   B CB   1 
ATOM   5007 C CG   . MET   B 1 61  ? 52.909 -15.564 0.967   1.00 10.76 ?  61  MET   B CG   1 
ATOM   5008 S SD   . MET   B 1 61  ? 52.267 -17.074 0.217   1.00 11.44 ?  61  MET   B SD   1 
ATOM   5009 C CE   . MET   B 1 61  ? 52.009 -16.489 -1.457  1.00 12.37 ?  61  MET   B CE   1 
ATOM   5010 H H    . MET   B 1 61  ? 56.637 -14.548 0.335   1.00 13.66 ?  61  MET   B H    1 
ATOM   5011 H HA   . MET   B 1 61  ? 54.443 -13.264 0.833   1.00 13.04 ?  61  MET   B HA   1 
ATOM   5012 H HB2  . MET   B 1 61  ? 54.385 -15.199 -0.400  1.00 13.05 ?  61  MET   B HB2  1 
ATOM   5013 H HB3  . MET   B 1 61  ? 54.894 -16.044 0.843   1.00 13.05 ?  61  MET   B HB3  1 
ATOM   5014 H HG2  . MET   B 1 61  ? 52.860 -15.676 1.929   1.00 12.89 ?  61  MET   B HG2  1 
ATOM   5015 H HG3  . MET   B 1 61  ? 52.354 -14.826 0.685   1.00 12.89 ?  61  MET   B HG3  1 
ATOM   5016 H HE1  . MET   B 1 61  ? 51.631 -17.206 -1.985  1.00 14.81 ?  61  MET   B HE1  1 
ATOM   5017 H HE2  . MET   B 1 61  ? 51.401 -15.733 -1.436  1.00 14.81 ?  61  MET   B HE2  1 
ATOM   5018 H HE3  . MET   B 1 61  ? 52.863 -16.214 -1.831  1.00 14.81 ?  61  MET   B HE3  1 
ATOM   5019 N N    . GLN   B 1 62  ? 55.671 -14.737 3.423   1.00 10.86 ?  62  GLN   B N    1 
ATOM   5020 C CA   . GLN   B 1 62  ? 55.560 -14.790 4.877   1.00 11.31 ?  62  GLN   B CA   1 
ATOM   5021 C C    . GLN   B 1 62  ? 55.834 -13.431 5.505   1.00 11.51 ?  62  GLN   B C    1 
ATOM   5022 O O    . GLN   B 1 62  ? 55.144 -13.032 6.450   1.00 12.02 ?  62  GLN   B O    1 
ATOM   5023 C CB   . GLN   B 1 62  ? 56.509 -15.841 5.451   1.00 11.66 ?  62  GLN   B CB   1 
ATOM   5024 C CG   . GLN   B 1 62  ? 56.279 -16.117 6.928   1.00 11.80 ?  62  GLN   B CG   1 
ATOM   5025 C CD   . GLN   B 1 62  ? 54.901 -16.706 7.161   1.00 11.38 ?  62  GLN   B CD   1 
ATOM   5026 O OE1  . GLN   B 1 62  ? 54.643 -17.855 6.796   1.00 12.08 ?  62  GLN   B OE1  1 
ATOM   5027 N NE2  . GLN   B 1 62  ? 53.990 -15.914 7.718   1.00 11.87 ?  62  GLN   B NE2  1 
ATOM   5028 H H    . GLN   B 1 62  ? 56.315 -15.197 3.087   1.00 13.01 ?  62  GLN   B H    1 
ATOM   5029 H HA   . GLN   B 1 62  ? 54.653 -15.046 5.109   1.00 13.55 ?  62  GLN   B HA   1 
ATOM   5030 H HB2  . GLN   B 1 62  ? 56.388 -16.675 4.968   1.00 13.97 ?  62  GLN   B HB2  1 
ATOM   5031 H HB3  . GLN   B 1 62  ? 57.422 -15.530 5.345   1.00 13.97 ?  62  GLN   B HB3  1 
ATOM   5032 H HG2  . GLN   B 1 62  ? 56.940 -16.756 7.239   1.00 14.13 ?  62  GLN   B HG2  1 
ATOM   5033 H HG3  . GLN   B 1 62  ? 56.346 -15.291 7.425   1.00 14.13 ?  62  GLN   B HG3  1 
ATOM   5034 H HE21 . GLN   B 1 62  ? 54.196 -15.111 7.944   1.00 14.21 ?  62  GLN   B HE21 1 
ATOM   5035 H HE22 . GLN   B 1 62  ? 53.192 -16.208 7.859   1.00 14.21 ?  62  GLN   B HE22 1 
ATOM   5036 N N    . VAL   B 1 63  ? 56.848 -12.716 5.014   1.00 11.91 ?  63  VAL   B N    1 
ATOM   5037 C CA   . VAL   B 1 63  ? 57.155 -11.400 5.571   1.00 12.61 ?  63  VAL   B CA   1 
ATOM   5038 C C    . VAL   B 1 63  ? 55.964 -10.465 5.390   1.00 12.00 ?  63  VAL   B C    1 
ATOM   5039 O O    . VAL   B 1 63  ? 55.552 -9.756  6.319   1.00 12.79 ?  63  VAL   B O    1 
ATOM   5040 C CB   . VAL   B 1 63  ? 58.443 -10.837 4.942   1.00 14.00 ?  63  VAL   B CB   1 
ATOM   5041 C CG1  . VAL   B 1 63  ? 58.666 -9.400  5.392   1.00 14.56 ?  63  VAL   B CG1  1 
ATOM   5042 C CG2  . VAL   B 1 63  ? 59.629 -11.709 5.319   1.00 14.73 ?  63  VAL   B CG2  1 
ATOM   5043 H H    . VAL   B 1 63  ? 57.360 -12.969 4.363   1.00 14.27 ?  63  VAL   B H    1 
ATOM   5044 H HA   . VAL   B 1 63  ? 57.312 -11.500 6.517   1.00 15.10 ?  63  VAL   B HA   1 
ATOM   5045 H HB   . VAL   B 1 63  ? 58.362 -10.847 3.974   1.00 16.77 ?  63  VAL   B HB   1 
ATOM   5046 H HG11 . VAL   B 1 63  ? 59.582 -9.149  5.205   1.00 17.44 ?  63  VAL   B HG11 1 
ATOM   5047 H HG12 . VAL   B 1 63  ? 58.058 -8.819  4.909   1.00 17.44 ?  63  VAL   B HG12 1 
ATOM   5048 H HG13 . VAL   B 1 63  ? 58.495 -9.341  6.346   1.00 17.44 ?  63  VAL   B HG13 1 
ATOM   5049 H HG21 . VAL   B 1 63  ? 60.437 -11.330 4.936   1.00 17.66 ?  63  VAL   B HG21 1 
ATOM   5050 H HG22 . VAL   B 1 63  ? 59.706 -11.735 6.288   1.00 17.66 ?  63  VAL   B HG22 1 
ATOM   5051 H HG23 . VAL   B 1 63  ? 59.490 -12.606 4.976   1.00 17.66 ?  63  VAL   B HG23 1 
ATOM   5052 N N    . GLU   B 1 64  ? 55.396 -10.457 4.186   1.00 11.50 ?  64  GLU   B N    1 
ATOM   5053 C CA   . GLU   B 1 64  ? 54.233 -9.621  3.906   1.00 11.44 ?  64  GLU   B CA   1 
ATOM   5054 C C    . GLU   B 1 64  ? 53.044 -10.023 4.773   1.00 11.06 ?  64  GLU   B C    1 
ATOM   5055 O O    . GLU   B 1 64  ? 52.297 -9.165  5.269   1.00 11.65 ?  64  GLU   B O    1 
ATOM   5056 C CB   . GLU   B 1 64  ? 53.879 -9.769  2.425   1.00 11.48 ?  64  GLU   B CB   1 
ATOM   5057 C CG   . GLU   B 1 64  ? 52.611 -9.040  1.989   1.00 12.05 ?  64  GLU   B CG   1 
ATOM   5058 C CD   . GLU   B 1 64  ? 52.087 -9.537  0.651   1.00 12.58 ?  64  GLU   B CD   1 
ATOM   5059 O OE1  . GLU   B 1 64  ? 52.270 -10.745 0.342   1.00 13.28 ?  64  GLU   B OE1  1 
ATOM   5060 O OE2  . GLU   B 1 64  ? 51.472 -8.724  -0.082  1.00 13.52 -1 64  GLU   B OE2  1 
ATOM   5061 H H    . GLU   B 1 64  ? 55.659 -10.927 3.509   1.00 13.78 ?  64  GLU   B H    1 
ATOM   5062 H HA   . GLU   B 1 64  ? 54.444 -8.694  4.080   1.00 13.71 ?  64  GLU   B HA   1 
ATOM   5063 H HB2  . GLU   B 1 64  ? 54.608 -9.410  1.891   1.00 13.75 ?  64  GLU   B HB2  1 
ATOM   5064 H HB3  . GLU   B 1 64  ? 53.759 -10.707 2.222   1.00 13.75 ?  64  GLU   B HB3  1 
ATOM   5065 H HG2  . GLU   B 1 64  ? 51.904 -9.183  2.643   1.00 14.43 ?  64  GLU   B HG2  1 
ATOM   5066 H HG3  . GLU   B 1 64  ? 52.796 -8.092  1.911   1.00 14.43 ?  64  GLU   B HG3  1 
ATOM   5067 N N    . SER   B 1 65  ? 52.859 -11.331 4.962   1.00 10.98 ?  65  SER   B N    1 
ATOM   5068 C CA   . SER   B 1 65  ? 51.751 -11.838 5.763   1.00 10.92 ?  65  SER   B CA   1 
ATOM   5069 C C    . SER   B 1 65  ? 51.882 -11.434 7.224   1.00 11.03 ?  65  SER   B C    1 
ATOM   5070 O O    . SER   B 1 65  ? 50.885 -11.066 7.858   1.00 11.39 ?  65  SER   B O    1 
ATOM   5071 C CB   . SER   B 1 65  ? 51.683 -13.362 5.642   1.00 11.24 ?  65  SER   B CB   1 
ATOM   5072 O OG   . SER   B 1 65  ? 51.335 -13.765 4.326   1.00 11.18 ?  65  SER   B OG   1 
ATOM   5073 H H    . SER   B 1 65  ? 53.363 -11.951 4.639   1.00 13.16 ?  65  SER   B H    1 
ATOM   5074 H HA   . SER   B 1 65  ? 50.915 -11.478 5.425   1.00 13.08 ?  65  SER   B HA   1 
ATOM   5075 H HB2  . SER   B 1 65  ? 52.548 -13.734 5.873   1.00 13.47 ?  65  SER   B HB2  1 
ATOM   5076 H HB3  . SER   B 1 65  ? 51.009 -13.696 6.263   1.00 13.47 ?  65  SER   B HB3  1 
ATOM   5077 H HG   . SER   B 1 65  ? 51.910 -13.479 3.781   1.00 13.40 ?  65  SER   B HG   1 
ATOM   5078 N N    . ASP   B 1 66  ? 53.087 -11.536 7.795   1.00 11.41 ?  66  ASP   B N    1 
ATOM   5079 C CA   . ASP   B 1 66  ? 53.270 -11.140 9.188   1.00 11.88 ?  66  ASP   B CA   1 
ATOM   5080 C C    . ASP   B 1 66  ? 52.956 -9.660  9.381   1.00 11.83 ?  66  ASP   B C    1 
ATOM   5081 O O    . ASP   B 1 66  ? 52.384 -9.265  10.403  1.00 12.39 ?  66  ASP   B O    1 
ATOM   5082 C CB   . ASP   B 1 66  ? 54.697 -11.452 9.650   1.00 12.99 ?  66  ASP   B CB   1 
ATOM   5083 C CG   . ASP   B 1 66  ? 54.961 -12.949 9.817   1.00 14.78 ?  66  ASP   B CG   1 
ATOM   5084 O OD1  . ASP   B 1 66  ? 54.009 -13.761 9.724   1.00 15.39 ?  66  ASP   B OD1  1 
ATOM   5085 O OD2  . ASP   B 1 66  ? 56.136 -13.308 10.058  1.00 17.57 -1 66  ASP   B OD2  1 
ATOM   5086 H H    . ASP   B 1 66  ? 53.788 -11.831 7.409   1.00 13.67 ?  66  ASP   B H    1 
ATOM   5087 H HA   . ASP   B 1 66  ? 52.661 -11.638 9.752   1.00 14.23 ?  66  ASP   B HA   1 
ATOM   5088 H HB2  . ASP   B 1 66  ? 55.323 -11.108 8.993   1.00 15.57 ?  66  ASP   B HB2  1 
ATOM   5089 H HB3  . ASP   B 1 66  ? 54.854 -11.020 10.509  1.00 15.57 ?  66  ASP   B HB3  1 
ATOM   5090 N N    . ASP   B 1 67  ? 53.336 -8.820  8.417   1.00 11.63 ?  67  ASP   B N    1 
ATOM   5091 C CA   . ASP   B 1 67  ? 52.992 -7.408  8.499   1.00 12.24 ?  67  ASP   B CA   1 
ATOM   5092 C C    . ASP   B 1 67  ? 51.481 -7.204  8.419   1.00 12.39 ?  67  ASP   B C    1 
ATOM   5093 O O    . ASP   B 1 67  ? 50.915 -6.393  9.165   1.00 13.07 ?  67  ASP   B O    1 
ATOM   5094 C CB   . ASP   B 1 67  ? 53.710 -6.644  7.393   1.00 13.43 ?  67  ASP   B CB   1 
ATOM   5095 C CG   . ASP   B 1 67  ? 53.281 -5.205  7.334   1.00 14.66 ?  67  ASP   B CG   1 
ATOM   5096 O OD1  . ASP   B 1 67  ? 53.782 -4.381  8.134   1.00 15.93 ?  67  ASP   B OD1  1 
ATOM   5097 O OD2  . ASP   B 1 67  ? 52.406 -4.914  6.504   1.00 15.79 -1 67  ASP   B OD2  1 
ATOM   5098 H H    . ASP   B 1 67  ? 53.792 -9.040  7.723   1.00 13.93 ?  67  ASP   B H    1 
ATOM   5099 H HA   . ASP   B 1 67  ? 53.295 -7.053  9.349   1.00 14.67 ?  67  ASP   B HA   1 
ATOM   5100 H HB2  . ASP   B 1 67  ? 54.667 -6.675  7.555   1.00 16.09 ?  67  ASP   B HB2  1 
ATOM   5101 H HB3  . ASP   B 1 67  ? 53.510 -7.064  6.537   1.00 16.09 ?  67  ASP   B HB3  1 
ATOM   5102 N N    . TYR   B 1 68  ? 50.805 -7.937  7.525   1.00 12.03 ?  68  TYR   B N    1 
ATOM   5103 C CA   . TYR   B 1 68  ? 49.347 -7.860  7.450   1.00 12.90 ?  68  TYR   B CA   1 
ATOM   5104 C C    . TYR   B 1 68  ? 48.705 -8.200  8.794   1.00 12.29 ?  68  TYR   B C    1 
ATOM   5105 O O    . TYR   B 1 68  ? 47.774 -7.516  9.243   1.00 13.02 ?  68  TYR   B O    1 
ATOM   5106 C CB   . TYR   B 1 68  ? 48.814 -8.792  6.352   1.00 13.53 ?  68  TYR   B CB   1 
ATOM   5107 C CG   . TYR   B 1 68  ? 47.303 -8.944  6.411   1.00 14.41 ?  68  TYR   B CG   1 
ATOM   5108 C CD1  . TYR   B 1 68  ? 46.715 -9.890  7.244   1.00 15.05 ?  68  TYR   B CD1  1 
ATOM   5109 C CD2  . TYR   B 1 68  ? 46.470 -8.117  5.673   1.00 15.52 ?  68  TYR   B CD2  1 
ATOM   5110 C CE1  . TYR   B 1 68  ? 45.349 -10.012 7.339   1.00 16.35 ?  68  TYR   B CE1  1 
ATOM   5111 C CE2  . TYR   B 1 68  ? 45.085 -8.248  5.750   1.00 15.64 ?  68  TYR   B CE2  1 
ATOM   5112 C CZ   . TYR   B 1 68  ? 44.544 -9.194  6.590   1.00 16.13 ?  68  TYR   B CZ   1 
ATOM   5113 O OH   . TYR   B 1 68  ? 43.176 -9.311  6.687   1.00 17.09 ?  68  TYR   B OH   1 
ATOM   5114 H H    . TYR   B 1 68  ? 51.165 -8.487  6.962   1.00 14.41 ?  68  TYR   B H    1 
ATOM   5115 H HA   . TYR   B 1 68  ? 49.096 -6.956  7.222   1.00 15.45 ?  68  TYR   B HA   1 
ATOM   5116 H HB2  . TYR   B 1 68  ? 49.040 -8.423  5.486   1.00 16.22 ?  68  TYR   B HB2  1 
ATOM   5117 H HB3  . TYR   B 1 68  ? 49.207 -9.670  6.458   1.00 16.22 ?  68  TYR   B HB3  1 
ATOM   5118 H HD1  . TYR   B 1 68  ? 47.257 -10.449 7.754   1.00 18.04 ?  68  TYR   B HD1  1 
ATOM   5119 H HD2  . TYR   B 1 68  ? 46.840 -7.471  5.119   1.00 18.60 ?  68  TYR   B HD2  1 
ATOM   5120 H HE1  . TYR   B 1 68  ? 44.970 -10.662 7.891   1.00 19.60 ?  68  TYR   B HE1  1 
ATOM   5121 H HE2  . TYR   B 1 68  ? 44.525 -7.689  5.257   1.00 18.75 ?  68  TYR   B HE2  1 
ATOM   5122 H HH   . TYR   B 1 68  ? 42.789 -8.763  6.170   1.00 20.49 ?  68  TYR   B HH   1 
ATOM   5123 N N    . ILE   B 1 69  ? 49.185 -9.265  9.445   1.00 12.10 ?  69  ILE   B N    1 
ATOM   5124 C CA   . ILE   B 1 69  ? 48.636 -9.681  10.734  1.00 12.20 ?  69  ILE   B CA   1 
ATOM   5125 C C    . ILE   B 1 69  ? 48.888 -8.621  11.799  1.00 12.14 ?  69  ILE   B C    1 
ATOM   5126 O O    . ILE   B 1 69  ? 48.021 -8.338  12.634  1.00 12.34 ?  69  ILE   B O    1 
ATOM   5127 C CB   . ILE   B 1 69  ? 49.219 -11.049 11.139  1.00 13.07 ?  69  ILE   B CB   1 
ATOM   5128 C CG1  . ILE   B 1 69  ? 48.699 -12.160 10.216  1.00 13.70 ?  69  ILE   B CG1  1 
ATOM   5129 C CG2  . ILE   B 1 69  ? 48.922 -11.360 12.599  1.00 13.93 ?  69  ILE   B CG2  1 
ATOM   5130 C CD1  . ILE   B 1 69  ? 47.222 -12.467 10.370  1.00 13.96 ?  69  ILE   B CD1  1 
ATOM   5131 H H    . ILE   B 1 69  ? 49.835 -9.758  9.164   1.00 14.50 ?  69  ILE   B H    1 
ATOM   5132 H HA   . ILE   B 1 69  ? 47.682 -9.780  10.643  1.00 14.62 ?  69  ILE   B HA   1 
ATOM   5133 H HB   . ILE   B 1 69  ? 50.186 -11.005 11.037  1.00 15.66 ?  69  ILE   B HB   1 
ATOM   5134 H HG12 . ILE   B 1 69  ? 48.854 -11.891 9.297   1.00 16.41 ?  69  ILE   B HG12 1 
ATOM   5135 H HG13 . ILE   B 1 69  ? 49.194 -12.972 10.407  1.00 16.41 ?  69  ILE   B HG13 1 
ATOM   5136 H HG21 . ILE   B 1 69  ? 49.062 -12.307 12.751  1.00 16.70 ?  69  ILE   B HG21 1 
ATOM   5137 H HG22 . ILE   B 1 69  ? 49.518 -10.845 13.164  1.00 16.70 ?  69  ILE   B HG22 1 
ATOM   5138 H HG23 . ILE   B 1 69  ? 47.999 -11.129 12.787  1.00 16.70 ?  69  ILE   B HG23 1 
ATOM   5139 H HD11 . ILE   B 1 69  ? 46.995 -13.185 9.762   1.00 16.73 ?  69  ILE   B HD11 1 
ATOM   5140 H HD12 . ILE   B 1 69  ? 47.049 -12.739 11.283  1.00 16.73 ?  69  ILE   B HD12 1 
ATOM   5141 H HD13 . ILE   B 1 69  ? 46.710 -11.675 10.154  1.00 16.73 ?  69  ILE   B HD13 1 
ATOM   5142 N N    . ALA   B 1 70  ? 50.082 -8.032  11.810  1.00 12.02 ?  70  ALA   B N    1 
ATOM   5143 C CA   . ALA   B 1 70  ? 50.360 -6.989  12.792  1.00 11.80 ?  70  ALA   B CA   1 
ATOM   5144 C C    . ALA   B 1 70  ? 49.357 -5.852  12.681  1.00 12.30 ?  70  ALA   B C    1 
ATOM   5145 O O    . ALA   B 1 70  ? 48.924 -5.300  13.693  1.00 12.83 ?  70  ALA   B O    1 
ATOM   5146 C CB   . ALA   B 1 70  ? 51.785 -6.467  12.614  1.00 12.46 ?  70  ALA   B CB   1 
ATOM   5147 H H    . ALA   B 1 70  ? 50.727 -8.207  11.277  1.00 14.40 ?  70  ALA   B H    1 
ATOM   5148 H HA   . ALA   B 1 70  ? 50.293 -7.365  13.687  1.00 14.13 ?  70  ALA   B HA   1 
ATOM   5149 H HB1  . ALA   B 1 70  ? 51.975 -5.812  13.308  1.00 14.93 ?  70  ALA   B HB1  1 
ATOM   5150 H HB2  . ALA   B 1 70  ? 52.409 -7.207  12.686  1.00 14.93 ?  70  ALA   B HB2  1 
ATOM   5151 H HB3  . ALA   B 1 70  ? 51.866 -6.053  11.740  1.00 14.93 ?  70  ALA   B HB3  1 
ATOM   5152 N N    . THR   B 1 71  ? 48.975 -5.495  11.459  1.00 12.68 ?  71  THR   B N    1 
ATOM   5153 C CA   . THR   B 1 71  ? 48.071 -4.370  11.255  1.00 13.87 ?  71  THR   B CA   1 
ATOM   5154 C C    . THR   B 1 71  ? 46.607 -4.750  11.468  1.00 14.48 ?  71  THR   B C    1 
ATOM   5155 O O    . THR   B 1 71  ? 45.824 -3.946  11.992  1.00 16.00 ?  71  THR   B O    1 
ATOM   5156 C CB   . THR   B 1 71  ? 48.283 -3.800  9.851   1.00 15.73 ?  71  THR   B CB   1 
ATOM   5157 O OG1  . THR   B 1 71  ? 49.594 -3.234  9.753   1.00 17.61 ?  71  THR   B OG1  1 
ATOM   5158 C CG2  . THR   B 1 71  ? 47.240 -2.741  9.528   1.00 16.79 ?  71  THR   B CG2  1 
ATOM   5159 H H    . THR   B 1 71  ? 49.230 -5.890  10.738  1.00 15.19 ?  71  THR   B H    1 
ATOM   5160 H HA   . THR   B 1 71  ? 48.293 -3.676  11.891  1.00 16.63 ?  71  THR   B HA   1 
ATOM   5161 H HB   . THR   B 1 71  ? 48.208 -4.510  9.195   1.00 18.86 ?  71  THR   B HB   1 
ATOM   5162 H HG1  . THR   B 1 71  ? 49.709 -2.894  8.987   1.00 21.10 ?  71  THR   B HG1  1 
ATOM   5163 H HG21 . THR   B 1 71  ? 47.533 -2.202  8.775   1.00 20.13 ?  71  THR   B HG21 1 
ATOM   5164 H HG22 . THR   B 1 71  ? 46.395 -3.159  9.302   1.00 20.13 ?  71  THR   B HG22 1 
ATOM   5165 H HG23 . THR   B 1 71  ? 47.109 -2.158  10.294  1.00 20.13 ?  71  THR   B HG23 1 
ATOM   5166 N N    . ASN   B 1 72  ? 46.218 -5.968  11.076  1.00 14.10 ?  72  ASN   B N    1 
ATOM   5167 C CA   . ASN   B 1 72  ? 44.816 -6.338  10.957  1.00 14.65 ?  72  ASN   B CA   1 
ATOM   5168 C C    . ASN   B 1 72  ? 44.353 -7.433  11.910  1.00 14.90 ?  72  ASN   B C    1 
ATOM   5169 O O    . ASN   B 1 72  ? 43.138 -7.592  12.086  1.00 16.26 ?  72  ASN   B O    1 
ATOM   5170 C CB   . ASN   B 1 72  ? 44.506 -6.775  9.515   1.00 15.37 ?  72  ASN   B CB   1 
ATOM   5171 C CG   . ASN   B 1 72  ? 44.784 -5.678  8.507   1.00 16.56 ?  72  ASN   B CG   1 
ATOM   5172 O OD1  . ASN   B 1 72  ? 45.812 -5.682  7.822   1.00 17.82 ?  72  ASN   B OD1  1 
ATOM   5173 N ND2  . ASN   B 1 72  ? 43.893 -4.710  8.440   1.00 18.38 ?  72  ASN   B ND2  1 
ATOM   5174 H H    . ASN   B 1 72  ? 46.764 -6.610  10.874  1.00 16.90 ?  72  ASN   B H    1 
ATOM   5175 H HA   . ASN   B 1 72  ? 44.283 -5.554  11.143  1.00 17.56 ?  72  ASN   B HA   1 
ATOM   5176 H HB2  . ASN   B 1 72  ? 45.061 -7.538  9.289   1.00 18.42 ?  72  ASN   B HB2  1 
ATOM   5177 H HB3  . ASN   B 1 72  ? 43.571 -7.008  9.451   1.00 18.42 ?  72  ASN   B HB3  1 
ATOM   5178 H HD21 . ASN   B 1 72  ? 43.999 -4.061  7.884   1.00 22.03 ?  72  ASN   B HD21 1 
ATOM   5179 H HD22 . ASN   B 1 72  ? 43.187 -4.740  8.931   1.00 22.03 ?  72  ASN   B HD22 1 
ATOM   5180 N N    . GLY   B 1 73  ? 45.259 -8.186  12.527  1.00 14.34 ?  73  GLY   B N    1 
ATOM   5181 C CA   . GLY   B 1 73  ? 44.863 -9.330  13.312  1.00 13.83 ?  73  GLY   B CA   1 
ATOM   5182 C C    . GLY   B 1 73  ? 44.503 -10.513 12.438  1.00 12.38 ?  73  GLY   B C    1 
ATOM   5183 O O    . GLY   B 1 73  ? 44.490 -10.421 11.208  1.00 12.83 ?  73  GLY   B O    1 
ATOM   5184 H H    . GLY   B 1 73  ? 46.110 -8.057  12.498  1.00 17.19 ?  73  GLY   B H    1 
ATOM   5185 H HA2  . GLY   B 1 73  ? 45.586 -9.588  13.903  1.00 16.57 ?  73  GLY   B HA2  1 
ATOM   5186 H HA3  . GLY   B 1 73  ? 44.089 -9.100  13.853  1.00 16.57 ?  73  GLY   B HA3  1 
ATOM   5187 N N    . PRO   B 1 74  ? 44.211 -11.649 13.070  1.00 13.04 ?  74  PRO   B N    1 
ATOM   5188 C CA   . PRO   B 1 74  ? 43.958 -12.876 12.313  1.00 12.39 ?  74  PRO   B CA   1 
ATOM   5189 C C    . PRO   B 1 74  ? 42.656 -12.817 11.529  1.00 11.69 ?  74  PRO   B C    1 
ATOM   5190 O O    . PRO   B 1 74  ? 41.715 -12.091 11.869  1.00 13.24 ?  74  PRO   B O    1 
ATOM   5191 C CB   . PRO   B 1 74  ? 43.893 -13.951 13.406  1.00 13.38 ?  74  PRO   B CB   1 
ATOM   5192 C CG   . PRO   B 1 74  ? 43.432 -13.214 14.620  1.00 15.05 ?  74  PRO   B CG   1 
ATOM   5193 C CD   . PRO   B 1 74  ? 44.101 -11.869 14.522  1.00 14.34 ?  74  PRO   B CD   1 
ATOM   5194 H HA   . PRO   B 1 74  ? 44.699 -13.062 11.709  1.00 14.85 ?  74  PRO   B HA   1 
ATOM   5195 H HB2  . PRO   B 1 74  ? 43.257 -14.637 13.149  1.00 16.03 ?  74  PRO   B HB2  1 
ATOM   5196 H HB3  . PRO   B 1 74  ? 44.775 -14.331 13.543  1.00 16.03 ?  74  PRO   B HB3  1 
ATOM   5197 H HG2  . PRO   B 1 74  ? 42.464 -13.120 14.595  1.00 18.04 ?  74  PRO   B HG2  1 
ATOM   5198 H HG3  . PRO   B 1 74  ? 43.713 -13.685 15.416  1.00 18.04 ?  74  PRO   B HG3  1 
ATOM   5199 H HD2  . PRO   B 1 74  ? 43.544 -11.186 14.933  1.00 17.19 ?  74  PRO   B HD2  1 
ATOM   5200 H HD3  . PRO   B 1 74  ? 44.980 -11.901 14.926  1.00 17.19 ?  74  PRO   B HD3  1 
ATOM   5201 N N    . LEU   B 1 75  ? 42.620 -13.612 10.465  1.00 11.31 ?  75  LEU   B N    1 
ATOM   5202 C CA   . LEU   B 1 75  ? 41.406 -13.830 9.701   1.00 11.56 ?  75  LEU   B CA   1 
ATOM   5203 C C    . LEU   B 1 75  ? 40.425 -14.678 10.506  1.00 12.19 ?  75  LEU   B C    1 
ATOM   5204 O O    . LEU   B 1 75  ? 40.767 -15.266 11.534  1.00 13.30 ?  75  LEU   B O    1 
ATOM   5205 C CB   . LEU   B 1 75  ? 41.731 -14.544 8.390   1.00 11.34 ?  75  LEU   B CB   1 
ATOM   5206 C CG   . LEU   B 1 75  ? 42.569 -13.786 7.356   1.00 13.32 ?  75  LEU   B CG   1 
ATOM   5207 C CD1  . LEU   B 1 75  ? 42.777 -14.623 6.098   1.00 14.72 ?  75  LEU   B CD1  1 
ATOM   5208 C CD2  . LEU   B 1 75  ? 41.950 -12.463 7.003   1.00 16.93 ?  75  LEU   B CD2  1 
ATOM   5209 H H    . LEU   B 1 75  ? 43.300 -14.040 10.161  1.00 13.55 ?  75  LEU   B H    1 
ATOM   5210 H HA   . LEU   B 1 75  ? 40.987 -12.980 9.495   1.00 13.84 ?  75  LEU   B HA   1 
ATOM   5211 H HB2  . LEU   B 1 75  ? 42.220 -15.358 8.603   1.00 13.58 ?  75  LEU   B HB2  1 
ATOM   5212 H HB3  . LEU   B 1 75  ? 40.897 -14.783 7.957   1.00 13.58 ?  75  LEU   B HB3  1 
ATOM   5213 H HG   . LEU   B 1 75  ? 43.443 -13.608 7.734   1.00 15.96 ?  75  LEU   B HG   1 
ATOM   5214 H HD11 . LEU   B 1 75  ? 43.318 -14.115 5.465   1.00 17.63 ?  75  LEU   B HD11 1 
ATOM   5215 H HD12 . LEU   B 1 75  ? 43.242 -15.443 6.334   1.00 17.63 ?  75  LEU   B HD12 1 
ATOM   5216 H HD13 . LEU   B 1 75  ? 41.919 -14.830 5.703   1.00 17.63 ?  75  LEU   B HD13 1 
ATOM   5217 H HD21 . LEU   B 1 75  ? 42.444 -12.065 6.270   1.00 20.29 ?  75  LEU   B HD21 1 
ATOM   5218 H HD22 . LEU   B 1 75  ? 41.026 -12.604 6.742   1.00 20.29 ?  75  LEU   B HD22 1 
ATOM   5219 H HD23 . LEU   B 1 75  ? 41.987 -11.880 7.780   1.00 20.29 ?  75  LEU   B HD23 1 
ATOM   5220 N N    . LYS   B 1 76  ? 39.186 -14.731 10.020  1.00 13.49 ?  76  LYS   B N    1 
ATOM   5221 C CA   . LYS   B 1 76  ? 38.203 -15.696 10.490  1.00 14.51 ?  76  LYS   B CA   1 
ATOM   5222 C C    . LYS   B 1 76  ? 38.310 -16.972 9.659   1.00 13.33 ?  76  LYS   B C    1 
ATOM   5223 O O    . LYS   B 1 76  ? 38.594 -16.920 8.464   1.00 12.80 ?  76  LYS   B O    1 
ATOM   5224 C CB   . LYS   B 1 76  ? 36.785 -15.140 10.297  1.00 16.72 ?  76  LYS   B CB   1 
ATOM   5225 C CG   . LYS   B 1 76  ? 36.506 -13.758 10.907  1.00 18.75 ?  76  LYS   B CG   1 
ATOM   5226 C CD   . LYS   B 1 76  ? 35.100 -13.242 10.558  1.00 19.86 ?  76  LYS   B CD   1 
ATOM   5227 C CE   . LYS   B 1 76  ? 34.853 -11.856 11.135  1.00 21.55 ?  76  LYS   B CE   1 
ATOM   5228 N NZ   . LYS   B 1 76  ? 33.551 -11.278 10.714  1.00 21.79 ?  76  LYS   B NZ   1 
ATOM   5229 H H    . LYS   B 1 76  ? 38.888 -14.213 9.401   1.00 16.16 ?  76  LYS   B H    1 
ATOM   5230 H HA   . LYS   B 1 76  ? 38.350 -15.908 11.427  1.00 17.38 ?  76  LYS   B HA   1 
ATOM   5231 H HB2  . LYS   B 1 76  ? 36.612 -15.074 9.346   1.00 20.04 ?  76  LYS   B HB2  1 
ATOM   5232 H HB3  . LYS   B 1 76  ? 36.157 -15.761 10.697  1.00 20.04 ?  76  LYS   B HB3  1 
ATOM   5233 H HG2  . LYS   B 1 76  ? 36.576 -13.814 11.873  1.00 22.48 ?  76  LYS   B HG2  1 
ATOM   5234 H HG3  . LYS   B 1 76  ? 37.155 -13.121 10.564  1.00 22.48 ?  76  LYS   B HG3  1 
ATOM   5235 H HD2  . LYS   B 1 76  ? 35.006 -13.188 9.593   1.00 23.81 ?  76  LYS   B HD2  1 
ATOM   5236 H HD3  . LYS   B 1 76  ? 34.435 -13.844 10.926  1.00 23.81 ?  76  LYS   B HD3  1 
ATOM   5237 H HE2  . LYS   B 1 76  ? 34.859 -11.911 12.102  1.00 25.84 ?  76  LYS   B HE2  1 
ATOM   5238 H HE3  . LYS   B 1 76  ? 35.557 -11.259 10.832  1.00 25.84 ?  76  LYS   B HE3  1 
ATOM   5239 H HZ1  . LYS   B 1 76  ? 33.446 -10.468 11.072  1.00 26.13 ?  76  LYS   B HZ1  1 
ATOM   5240 H HZ2  . LYS   B 1 76  ? 33.519 -11.205 9.827   1.00 26.13 ?  76  LYS   B HZ2  1 
ATOM   5241 H HZ3  . LYS   B 1 76  ? 32.883 -11.800 10.985  1.00 26.13 ?  76  LYS   B HZ3  1 
ATOM   5242 N N    . VAL   B 1 77  ? 38.064 -18.125 10.292  1.00 14.15 ?  77  VAL   B N    1 
ATOM   5243 C CA   . VAL   B 1 77  ? 37.861 -19.340 9.510   1.00 14.42 ?  77  VAL   B CA   1 
ATOM   5244 C C    . VAL   B 1 77  ? 36.670 -19.112 8.590   1.00 13.20 ?  77  VAL   B C    1 
ATOM   5245 O O    . VAL   B 1 77  ? 35.603 -18.669 9.032   1.00 13.27 ?  77  VAL   B O    1 
ATOM   5246 C CB   . VAL   B 1 77  ? 37.667 -20.561 10.420  1.00 16.38 ?  77  VAL   B CB   1 
ATOM   5247 C CG1  . VAL   B 1 77  ? 37.376 -21.797 9.572   1.00 16.79 ?  77  VAL   B CG1  1 
ATOM   5248 C CG2  . VAL   B 1 77  ? 38.897 -20.780 11.303  1.00 17.39 ?  77  VAL   B CG2  1 
ATOM   5249 H H    . VAL   B 1 77  ? 38.017 -18.226 11.142  1.00 16.95 ?  77  VAL   B H    1 
ATOM   5250 H HA   . VAL   B 1 77  ? 38.639 -19.495 8.951   1.00 17.28 ?  77  VAL   B HA   1 
ATOM   5251 H HB   . VAL   B 1 77  ? 36.899 -20.405 10.993  1.00 19.64 ?  77  VAL   B HB   1 
ATOM   5252 H HG11 . VAL   B 1 77  ? 37.422 -22.581 10.138  1.00 20.13 ?  77  VAL   B HG11 1 
ATOM   5253 H HG12 . VAL   B 1 77  ? 36.485 -21.721 9.188   1.00 20.13 ?  77  VAL   B HG12 1 
ATOM   5254 H HG13 . VAL   B 1 77  ? 38.035 -21.857 8.865   1.00 20.13 ?  77  VAL   B HG13 1 
ATOM   5255 H HG21 . VAL   B 1 77  ? 38.758 -21.579 11.834  1.00 20.84 ?  77  VAL   B HG21 1 
ATOM   5256 H HG22 . VAL   B 1 77  ? 39.674 -20.884 10.737  1.00 20.84 ?  77  VAL   B HG22 1 
ATOM   5257 H HG23 . VAL   B 1 77  ? 39.004 -20.010 11.883  1.00 20.84 ?  77  VAL   B HG23 1 
ATOM   5258 N N    . GLY   B 1 78  ? 36.851 -19.392 7.299   1.00 12.58 ?  78  GLY   B N    1 
ATOM   5259 C CA   . GLY   B 1 78  ? 35.868 -19.074 6.289   1.00 12.12 ?  78  GLY   B CA   1 
ATOM   5260 C C    . GLY   B 1 78  ? 36.110 -17.757 5.587   1.00 11.54 ?  78  GLY   B C    1 
ATOM   5261 O O    . GLY   B 1 78  ? 35.426 -17.472 4.600   1.00 11.88 ?  78  GLY   B O    1 
ATOM   5262 H H    . GLY   B 1 78  ? 37.548 -19.787 6.983   1.00 15.07 ?  78  GLY   B H    1 
ATOM   5263 H HA2  . GLY   B 1 78  ? 35.860 -19.768 5.618   1.00 14.52 ?  78  GLY   B HA2  1 
ATOM   5264 H HA3  . GLY   B 1 78  ? 34.990 -19.033 6.700   1.00 14.52 ?  78  GLY   B HA3  1 
ATOM   5265 N N    . GLY   B 1 79  ? 37.064 -16.953 6.069   1.00 11.64 ?  79  GLY   B N    1 
ATOM   5266 C CA   . GLY   B 1 79  ? 37.369 -15.662 5.488   1.00 11.46 ?  79  GLY   B CA   1 
ATOM   5267 C C    . GLY   B 1 79  ? 38.611 -15.687 4.605   1.00 10.74 ?  79  GLY   B C    1 
ATOM   5268 O O    . GLY   B 1 79  ? 39.225 -16.724 4.361   1.00 11.24 ?  79  GLY   B O    1 
ATOM   5269 H H    . GLY   B 1 79  ? 37.561 -17.142 6.742   1.00 13.94 ?  79  GLY   B H    1 
ATOM   5270 H HA2  . GLY   B 1 79  ? 36.618 -15.362 4.945   1.00 13.73 ?  79  GLY   B HA2  1 
ATOM   5271 H HA3  . GLY   B 1 79  ? 37.512 -15.012 6.192   1.00 13.73 ?  79  GLY   B HA3  1 
ATOM   5272 N N    . SER   B 1 80  ? 38.977 -14.496 4.125   1.00 10.78 ?  80  SER   B N    1 
ATOM   5273 C CA   . SER   B 1 80  ? 40.085 -14.365 3.191   1.00 10.32 ?  80  SER   B CA   1 
ATOM   5274 C C    . SER   B 1 80  ? 40.667 -12.958 3.246   1.00 10.15 ?  80  SER   B C    1 
ATOM   5275 O O    . SER   B 1 80  ? 40.053 -12.024 3.766   1.00 11.68 ?  80  SER   B O    1 
ATOM   5276 C CB   . SER   B 1 80  ? 39.647 -14.664 1.753   1.00 10.73 ?  80  SER   B CB   1 
ATOM   5277 O OG   . SER   B 1 80  ? 38.815 -13.636 1.247   1.00 12.09 ?  80  SER   B OG   1 
ATOM   5278 H H    . SER   B 1 80  ? 38.602 -13.753 4.324   1.00 12.91 ?  80  SER   B H    1 
ATOM   5279 H HA   . SER   B 1 80  ? 40.778 -14.995 3.437   1.00 12.36 ?  80  SER   B HA   1 
ATOM   5280 H HB2  . SER   B 1 80  ? 40.432 -14.731 1.185   1.00 12.85 ?  80  SER   B HB2  1 
ATOM   5281 H HB3  . SER   B 1 80  ? 39.158 -15.503 1.736   1.00 12.85 ?  80  SER   B HB3  1 
ATOM   5282 H HG   . SER   B 1 80  ? 38.118 -13.569 1.722   1.00 14.48 ?  80  SER   B HG   1 
ATOM   5283 N N    . CYS   B 1 81  ? 41.858 -12.815 2.664   1.00 10.10 ?  81  CYS   B N    1 
ATOM   5284 C CA   . CYS   B 1 81  ? 42.407 -11.505 2.351   1.00 10.23 ?  81  CYS   B CA   1 
ATOM   5285 C C    . CYS   B 1 81  ? 43.181 -11.596 1.043   1.00 9.58  ?  81  CYS   B C    1 
ATOM   5286 O O    . CYS   B 1 81  ? 43.693 -12.658 0.675   1.00 10.74 ?  81  CYS   B O    1 
ATOM   5287 C CB   . CYS   B 1 81  ? 43.293 -10.949 3.475   1.00 11.17 ?  81  CYS   B CB   1 
ATOM   5288 S SG   . CYS   B 1 81  ? 44.819 -11.896 3.723   1.00 11.40 ?  81  CYS   B SG   1 
ATOM   5289 H H    . CYS   B 1 81  ? 42.363 -13.468 2.419   1.00 12.10 ?  81  CYS   B H    1 
ATOM   5290 H HA   . CYS   B 1 81  ? 41.679 -10.876 2.218   1.00 12.26 ?  81  CYS   B HA   1 
ATOM   5291 H HB2  . CYS   B 1 81  ? 43.545 -10.037 3.269   1.00 13.38 ?  81  CYS   B HB2  1 
ATOM   5292 H HB3  . CYS   B 1 81  ? 42.791 -10.967 4.312   1.00 13.38 ?  81  CYS   B HB3  1 
ATOM   5293 H HG   . CYS   B 1 81  ? 45.441 -11.405 4.625   1.00 13.65 ?  81  CYS   B HG   1 
ATOM   5294 N N    . VAL   B 1 82  ? 43.288 -10.455 0.366   1.00 10.32 ?  82  VAL   B N    1 
ATOM   5295 C CA   . VAL   B 1 82  ? 44.053 -10.328 -0.871  1.00 10.37 ?  82  VAL   B CA   1 
ATOM   5296 C C    . VAL   B 1 82  ? 45.392 -9.685  -0.548  1.00 10.42 ?  82  VAL   B C    1 
ATOM   5297 O O    . VAL   B 1 82  ? 45.443 -8.571  -0.009  1.00 11.46 ?  82  VAL   B O    1 
ATOM   5298 C CB   . VAL   B 1 82  ? 43.305 -9.489  -1.920  1.00 11.47 ?  82  VAL   B CB   1 
ATOM   5299 C CG1  . VAL   B 1 82  ? 44.147 -9.347  -3.179  1.00 12.50 ?  82  VAL   B CG1  1 
ATOM   5300 C CG2  . VAL   B 1 82  ? 41.948 -10.094 -2.243  1.00 12.41 ?  82  VAL   B CG2  1 
ATOM   5301 H H    . VAL   B 1 82  ? 42.909 -9.714  0.604   1.00 12.36 ?  82  VAL   B H    1 
ATOM   5302 H HA   . VAL   B 1 82  ? 44.212 -11.206 -1.244  1.00 12.42 ?  82  VAL   B HA   1 
ATOM   5303 H HB   . VAL   B 1 82  ? 43.154 -8.600  -1.567  1.00 13.74 ?  82  VAL   B HB   1 
ATOM   5304 H HG11 . VAL   B 1 82  ? 43.584 -9.023  -3.903  1.00 14.97 ?  82  VAL   B HG11 1 
ATOM   5305 H HG12 . VAL   B 1 82  ? 44.863 -8.710  -3.016  1.00 14.97 ?  82  VAL   B HG12 1 
ATOM   5306 H HG13 . VAL   B 1 82  ? 44.518 -10.210 -3.414  1.00 14.97 ?  82  VAL   B HG13 1 
ATOM   5307 H HG21 . VAL   B 1 82  ? 41.515 -9.562  -2.931  1.00 14.87 ?  82  VAL   B HG21 1 
ATOM   5308 H HG22 . VAL   B 1 82  ? 42.072 -11.004 -2.562  1.00 14.87 ?  82  VAL   B HG22 1 
ATOM   5309 H HG23 . VAL   B 1 82  ? 41.403 -10.099 -1.441  1.00 14.87 ?  82  VAL   B HG23 1 
ATOM   5310 N N    . LEU   B 1 83  ? 46.470 -10.373 -0.913  1.00 10.16 ?  83  LEU   B N    1 
ATOM   5311 C CA   . LEU   B 1 83  ? 47.828 -9.859  -0.791  1.00 10.15 ?  83  LEU   B CA   1 
ATOM   5312 C C    . LEU   B 1 83  ? 48.531 -10.013 -2.139  1.00 9.97  ?  83  LEU   B C    1 
ATOM   5313 O O    . LEU   B 1 83  ? 47.930 -10.436 -3.128  1.00 9.98  ?  83  LEU   B O    1 
ATOM   5314 C CB   . LEU   B 1 83  ? 48.575 -10.541 0.364   1.00 10.50 ?  83  LEU   B CB   1 
ATOM   5315 C CG   . LEU   B 1 83  ? 48.067 -10.171 1.764   1.00 11.78 ?  83  LEU   B CG   1 
ATOM   5316 C CD1  . LEU   B 1 83  ? 48.717 -11.029 2.835   1.00 12.39 ?  83  LEU   B CD1  1 
ATOM   5317 C CD2  . LEU   B 1 83  ? 48.264 -8.684  2.069   1.00 12.97 ?  83  LEU   B CD2  1 
ATOM   5318 H H    . LEU   B 1 83  ? 46.430 -11.169 -1.248  1.00 12.17 ?  83  LEU   B H    1 
ATOM   5319 H HA   . LEU   B 1 83  ? 47.778 -8.915  -0.600  1.00 12.15 ?  83  LEU   B HA   1 
ATOM   5320 H HB2  . LEU   B 1 83  ? 48.488 -11.501 0.261   1.00 12.58 ?  83  LEU   B HB2  1 
ATOM   5321 H HB3  . LEU   B 1 83  ? 49.508 -10.290 0.309   1.00 12.58 ?  83  LEU   B HB3  1 
ATOM   5322 H HG   . LEU   B 1 83  ? 47.116 -10.347 1.794   1.00 14.12 ?  83  LEU   B HG   1 
ATOM   5323 H HD11 . LEU   B 1 83  ? 48.366 -10.769 3.704   1.00 14.84 ?  83  LEU   B HD11 1 
ATOM   5324 H HD12 . LEU   B 1 83  ? 48.510 -11.963 2.666   1.00 14.84 ?  83  LEU   B HD12 1 
ATOM   5325 H HD13 . LEU   B 1 83  ? 49.677 -10.895 2.816   1.00 14.84 ?  83  LEU   B HD13 1 
ATOM   5326 H HD21 . LEU   B 1 83  ? 48.075 -8.528  3.007   1.00 15.53 ?  83  LEU   B HD21 1 
ATOM   5327 H HD22 . LEU   B 1 83  ? 49.180 -8.438  1.869   1.00 15.53 ?  83  LEU   B HD22 1 
ATOM   5328 H HD23 . LEU   B 1 83  ? 47.655 -8.166  1.519   1.00 15.53 ?  83  LEU   B HD23 1 
ATOM   5329 N N    . SER   B 1 84  ? 49.808 -9.645  -2.197  1.00 10.94 ?  84  SER   B N    1 
ATOM   5330 C CA   . SER   B 1 84  ? 50.539 -9.769  -3.450  1.00 11.16 ?  84  SER   B CA   1 
ATOM   5331 C C    . SER   B 1 84  ? 50.705 -11.232 -3.848  1.00 10.46 ?  84  SER   B C    1 
ATOM   5332 O O    . SER   B 1 84  ? 50.814 -12.120 -3.005  1.00 10.50 ?  84  SER   B O    1 
ATOM   5333 C CB   . SER   B 1 84  ? 51.930 -9.154  -3.311  1.00 12.99 ?  84  SER   B CB   1 
ATOM   5334 O OG   . SER   B 1 84  ? 52.678 -9.369  -4.495  1.00 14.19 ?  84  SER   B OG   1 
ATOM   5335 H H    . SER   B 1 84  ? 50.255 -9.315  -1.541  1.00 13.10 ?  84  SER   B H    1 
ATOM   5336 H HA   . SER   B 1 84  ? 50.063 -9.309  -4.157  1.00 13.37 ?  84  SER   B HA   1 
ATOM   5337 H HB2  . SER   B 1 84  ? 51.840 -8.196  -3.162  1.00 15.57 ?  84  SER   B HB2  1 
ATOM   5338 H HB3  . SER   B 1 84  ? 52.388 -9.562  -2.561  1.00 15.57 ?  84  SER   B HB3  1 
ATOM   5339 H HG   . SER   B 1 84  ? 53.448 -9.027  -4.414  1.00 17.01 ?  84  SER   B HG   1 
ATOM   5340 N N    . GLY   B 1 85  ? 50.756 -11.474 -5.152  1.00 11.55 ?  85  GLY   B N    1 
ATOM   5341 C CA   . GLY   B 1 85  ? 51.117 -12.771 -5.674  1.00 12.26 ?  85  GLY   B CA   1 
ATOM   5342 C C    . GLY   B 1 85  ? 52.584 -12.950 -5.985  1.00 11.47 ?  85  GLY   B C    1 
ATOM   5343 O O    . GLY   B 1 85  ? 52.971 -14.028 -6.440  1.00 12.24 ?  85  GLY   B O    1 
ATOM   5344 H H    . GLY   B 1 85  ? 50.593 -10.898 -5.760  1.00 13.83 ?  85  GLY   B H    1 
ATOM   5345 H HA2  . GLY   B 1 85  ? 50.866 -13.458 -5.031  1.00 14.69 ?  85  GLY   B HA2  1 
ATOM   5346 H HA3  . GLY   B 1 85  ? 50.621 -12.938 -6.489  1.00 14.69 ?  85  GLY   B HA3  1 
ATOM   5347 N N    . HIS   B 1 86  ? 53.425 -11.941 -5.771  1.00 11.54 ?  86  HIS   B N    1 
ATOM   5348 C CA   . HIS   B 1 86  ? 54.889 -12.097 -5.853  1.00 11.25 ?  86  HIS   B CA   1 
ATOM   5349 C C    . HIS   B 1 86  ? 55.270 -12.611 -7.239  1.00 11.57 ?  86  HIS   B C    1 
ATOM   5350 O O    . HIS   B 1 86  ? 54.883 -11.999 -8.246  1.00 12.44 ?  86  HIS   B O    1 
ATOM   5351 C CB   . HIS   B 1 86  ? 55.384 -12.935 -4.678  1.00 12.04 ?  86  HIS   B CB   1 
ATOM   5352 C CG   . HIS   B 1 86  ? 55.070 -12.327 -3.355  1.00 11.92 ?  86  HIS   B CG   1 
ATOM   5353 N ND1  . HIS   B 1 86  ? 55.889 -11.401 -2.746  1.00 13.38 ?  86  HIS   B ND1  1 
ATOM   5354 C CD2  . HIS   B 1 86  ? 53.997 -12.478 -2.542  1.00 12.19 ?  86  HIS   B CD2  1 
ATOM   5355 C CE1  . HIS   B 1 86  ? 55.333 -11.015 -1.610  1.00 13.12 ?  86  HIS   B CE1  1 
ATOM   5356 N NE2  . HIS   B 1 86  ? 54.182 -11.648 -1.467  1.00 12.42 ?  86  HIS   B NE2  1 
ATOM   5357 H H    . HIS   B 1 86  ? 53.177 -11.145 -5.576  1.00 13.82 ?  86  HIS   B H    1 
ATOM   5358 H HA   . HIS   B 1 86  ? 55.294 -11.223 -5.757  1.00 13.48 ?  86  HIS   B HA   1 
ATOM   5359 H HB2  . HIS   B 1 86  ? 54.971 -13.811 -4.715  1.00 14.42 ?  86  HIS   B HB2  1 
ATOM   5360 H HB3  . HIS   B 1 86  ? 56.352 -13.027 -4.738  1.00 14.42 ?  86  HIS   B HB3  1 
ATOM   5361 H HD2  . HIS   B 1 86  ? 53.261 -13.033 -2.697  1.00 14.60 ?  86  HIS   B HD2  1 
ATOM   5362 H HE1  . HIS   B 1 86  ? 55.694 -10.413 -1.003  1.00 15.72 ?  86  HIS   B HE1  1 
ATOM   5363 H HE2  . HIS   B 1 86  ? 53.642 -11.576 -0.799  1.00 14.88 ?  86  HIS   B HE2  1 
ATOM   5364 N N    . ASN   B 1 87  ? 56.039 -13.696 -7.340  1.00 12.14 ?  87  ASN   B N    1 
ATOM   5365 C CA   . ASN   B 1 87  ? 56.449 -14.272 -8.611  1.00 12.97 ?  87  ASN   B CA   1 
ATOM   5366 C C    . ASN   B 1 87  ? 55.465 -15.309 -9.124  1.00 12.81 ?  87  ASN   B C    1 
ATOM   5367 O O    . ASN   B 1 87  ? 55.781 -16.008 -10.093 1.00 14.47 ?  87  ASN   B O    1 
ATOM   5368 C CB   . ASN   B 1 87  ? 57.842 -14.904 -8.487  1.00 14.51 ?  87  ASN   B CB   1 
ATOM   5369 C CG   . ASN   B 1 87  ? 57.901 -15.999 -7.431  1.00 15.50 ?  87  ASN   B CG   1 
ATOM   5370 O OD1  . ASN   B 1 87  ? 57.248 -15.909 -6.389  1.00 14.61 ?  87  ASN   B OD1  1 
ATOM   5371 N ND2  . ASN   B 1 87  ? 58.672 -17.057 -7.711  1.00 17.84 ?  87  ASN   B ND2  1 
ATOM   5372 H H    . ASN   B 1 87  ? 56.339 -14.131 -6.663  1.00 14.54 ?  87  ASN   B H    1 
ATOM   5373 H HA   . ASN   B 1 87  ? 56.498 -13.572 -9.272  1.00 15.54 ?  87  ASN   B HA   1 
ATOM   5374 H HB2  . ASN   B 1 87  ? 58.090 -15.296 -9.343  1.00 17.39 ?  87  ASN   B HB2  1 
ATOM   5375 H HB3  . ASN   B 1 87  ? 58.478 -14.217 -8.244  1.00 17.39 ?  87  ASN   B HB3  1 
ATOM   5376 H HD21 . ASN   B 1 87  ? 58.748 -17.698 -7.146  1.00 21.38 ?  87  ASN   B HD21 1 
ATOM   5377 H HD22 . ASN   B 1 87  ? 59.116 -17.086 -8.453  1.00 21.38 ?  87  ASN   B HD22 1 
ATOM   5378 N N    . LEU   B 1 88  ? 54.288 -15.422 -8.503  1.00 11.74 ?  88  LEU   B N    1 
ATOM   5379 C CA   . LEU   B 1 88  ? 53.310 -16.453 -8.838  1.00 12.17 ?  88  LEU   B CA   1 
ATOM   5380 C C    . LEU   B 1 88  ? 52.078 -15.933 -9.560  1.00 11.72 ?  88  LEU   B C    1 
ATOM   5381 O O    . LEU   B 1 88  ? 51.483 -16.672 -10.355 1.00 13.44 ?  88  LEU   B O    1 
ATOM   5382 C CB   . LEU   B 1 88  ? 52.839 -17.150 -7.557  1.00 13.07 ?  88  LEU   B CB   1 
ATOM   5383 C CG   . LEU   B 1 88  ? 53.980 -17.784 -6.769  1.00 15.55 ?  88  LEU   B CG   1 
ATOM   5384 C CD1  . LEU   B 1 88  ? 53.496 -18.236 -5.403  1.00 17.00 ?  88  LEU   B CD1  1 
ATOM   5385 C CD2  . LEU   B 1 88  ? 54.573 -18.938 -7.553  1.00 18.90 ?  88  LEU   B CD2  1 
ATOM   5386 H H    . LEU   B 1 88  ? 54.027 -14.905 -7.863  1.00 14.06 ?  88  LEU   B H    1 
ATOM   5387 H HA   . LEU   B 1 88  ? 53.728 -17.117 -9.403  1.00 14.58 ?  88  LEU   B HA   1 
ATOM   5388 H HB2  . LEU   B 1 88  ? 52.402 -16.501 -6.982  1.00 15.66 ?  88  LEU   B HB2  1 
ATOM   5389 H HB3  . LEU   B 1 88  ? 52.210 -17.855 -7.791  1.00 15.66 ?  88  LEU   B HB3  1 
ATOM   5390 H HG   . LEU   B 1 88  ? 54.676 -17.123 -6.635  1.00 18.63 ?  88  LEU   B HG   1 
ATOM   5391 H HD11 . LEU   B 1 88  ? 54.236 -18.641 -4.926  1.00 20.38 ?  88  LEU   B HD11 1 
ATOM   5392 H HD12 . LEU   B 1 88  ? 53.166 -17.466 -4.914  1.00 20.38 ?  88  LEU   B HD12 1 
ATOM   5393 H HD13 . LEU   B 1 88  ? 52.785 -18.883 -5.524  1.00 20.38 ?  88  LEU   B HD13 1 
ATOM   5394 H HD21 . LEU   B 1 88  ? 55.182 -19.427 -6.979  1.00 22.66 ?  88  LEU   B HD21 1 
ATOM   5395 H HD22 . LEU   B 1 88  ? 53.856 -19.521 -7.847  1.00 22.66 ?  88  LEU   B HD22 1 
ATOM   5396 H HD23 . LEU   B 1 88  ? 55.051 -18.588 -8.321  1.00 22.66 ?  88  LEU   B HD23 1 
ATOM   5397 N N    . ALA   B 1 89  ? 51.667 -14.701 -9.282  1.00 11.03 ?  89  ALA   B N    1 
ATOM   5398 C CA   . ALA   B 1 89  ? 50.377 -14.202 -9.735  1.00 10.68 ?  89  ALA   B CA   1 
ATOM   5399 C C    . ALA   B 1 89  ? 50.360 -12.712 -9.446  1.00 10.89 ?  89  ALA   B C    1 
ATOM   5400 O O    . ALA   B 1 89  ? 51.185 -12.204 -8.688  1.00 11.52 ?  89  ALA   B O    1 
ATOM   5401 C CB   . ALA   B 1 89  ? 49.236 -14.871 -8.975  1.00 10.83 ?  89  ALA   B CB   1 
ATOM   5402 H H    . ALA   B 1 89  ? 52.116 -14.129 -8.826  1.00 13.21 ?  89  ALA   B H    1 
ATOM   5403 H HA   . ALA   B 1 89  ? 50.266 -14.351 -10.692 1.00 12.79 ?  89  ALA   B HA   1 
ATOM   5404 H HB1  . ALA   B 1 89  ? 48.390 -14.529 -9.311  1.00 12.97 ?  89  ALA   B HB1  1 
ATOM   5405 H HB2  . ALA   B 1 89  ? 49.280 -15.831 -9.121  1.00 12.97 ?  89  ALA   B HB2  1 
ATOM   5406 H HB3  . ALA   B 1 89  ? 49.325 -14.673 -8.035  1.00 12.97 ?  89  ALA   B HB3  1 
ATOM   5407 N N    . LYS   B 1 90  ? 49.389 -12.011 -10.018 1.00 11.94 ?  90  LYS   B N    1 
ATOM   5408 C CA   . LYS   B 1 90  ? 49.210 -10.624 -9.610  1.00 12.17 ?  90  LYS   B CA   1 
ATOM   5409 C C    . LYS   B 1 90  ? 48.877 -10.546 -8.123  1.00 11.66 ?  90  LYS   B C    1 
ATOM   5410 O O    . LYS   B 1 90  ? 49.516 -9.797  -7.367  1.00 12.52 ?  90  LYS   B O    1 
ATOM   5411 C CB   . LYS   B 1 90  ? 48.143 -9.953  -10.470 1.00 13.51 ?  90  LYS   B CB   1 
ATOM   5412 C CG   . LYS   B 1 90  ? 47.835 -8.519  -10.068 1.00 14.06 ?  90  LYS   B CG   1 
ATOM   5413 C CD   . LYS   B 1 90  ? 49.033 -7.603  -10.117 1.00 15.91 ?  90  LYS   B CD   1 
ATOM   5414 C CE   . LYS   B 1 90  ? 48.557 -6.201  -9.817  1.00 18.10 ?  90  LYS   B CE   1 
ATOM   5415 N NZ   . LYS   B 1 90  ? 49.670 -5.228  -9.760  1.00 18.51 ?  90  LYS   B NZ   1 
ATOM   5416 H H    . LYS   B 1 90  ? 48.846 -12.301 -10.616 1.00 14.30 ?  90  LYS   B H    1 
ATOM   5417 H HA   . LYS   B 1 90  ? 50.044 -10.153 -9.747  1.00 14.58 ?  90  LYS   B HA   1 
ATOM   5418 H HB2  . LYS   B 1 90  ? 48.451 -9.939  -11.392 1.00 16.19 ?  90  LYS   B HB2  1 
ATOM   5419 H HB3  . LYS   B 1 90  ? 47.322 -10.461 -10.408 1.00 16.19 ?  90  LYS   B HB3  1 
ATOM   5420 H HG2  . LYS   B 1 90  ? 47.167 -8.162  -10.673 1.00 16.84 ?  90  LYS   B HG2  1 
ATOM   5421 H HG3  . LYS   B 1 90  ? 47.489 -8.510  -9.160  1.00 16.84 ?  90  LYS   B HG3  1 
ATOM   5422 H HD2  . LYS   B 1 90  ? 49.684 -7.860  -9.441  1.00 19.07 ?  90  LYS   B HD2  1 
ATOM   5423 H HD3  . LYS   B 1 90  ? 49.432 -7.615  -11.001 1.00 19.07 ?  90  LYS   B HD3  1 
ATOM   5424 H HE2  . LYS   B 1 90  ? 47.946 -5.910  -10.513 1.00 21.69 ?  90  LYS   B HE2  1 
ATOM   5425 H HE3  . LYS   B 1 90  ? 48.110 -6.186  -8.956  1.00 21.69 ?  90  LYS   B HE3  1 
ATOM   5426 H HZ1  . LYS   B 1 90  ? 49.361 -4.409  -9.585  1.00 22.19 ?  90  LYS   B HZ1  1 
ATOM   5427 H HZ2  . LYS   B 1 90  ? 50.249 -5.457  -9.124  1.00 22.19 ?  90  LYS   B HZ2  1 
ATOM   5428 H HZ3  . LYS   B 1 90  ? 50.100 -5.206  -10.543 1.00 22.19 ?  90  LYS   B HZ3  1 
ATOM   5429 N N    . HIS   B 1 91  ? 47.899 -11.348 -7.683  1.00 10.34 ?  91  HIS   B N    1 
ATOM   5430 C CA   . HIS   B 1 91  ? 47.422 -11.382 -6.312  1.00 10.30 ?  91  HIS   B CA   1 
ATOM   5431 C C    . HIS   B 1 91  ? 47.413 -12.810 -5.796  1.00 9.63  ?  91  HIS   B C    1 
ATOM   5432 O O    . HIS   B 1 91  ? 47.188 -13.759 -6.556  1.00 10.24 ?  91  HIS   B O    1 
ATOM   5433 C CB   . HIS   B 1 91  ? 45.971 -10.898 -6.209  1.00 11.77 ?  91  HIS   B CB   1 
ATOM   5434 C CG   . HIS   B 1 91  ? 45.764 -9.487  -6.637  1.00 15.01 ?  91  HIS   B CG   1 
ATOM   5435 N ND1  . HIS   B 1 91  ? 46.381 -8.418  -6.023  1.00 17.54 ?  91  HIS   B ND1  1 
ATOM   5436 C CD2  . HIS   B 1 91  ? 44.967 -8.963  -7.594  1.00 17.42 ?  91  HIS   B CD2  1 
ATOM   5437 C CE1  . HIS   B 1 91  ? 45.996 -7.294  -6.605  1.00 18.68 ?  91  HIS   B CE1  1 
ATOM   5438 N NE2  . HIS   B 1 91  ? 45.132 -7.599  -7.557  1.00 18.97 ?  91  HIS   B NE2  1 
ATOM   5439 H H    . HIS   B 1 91  ? 47.475 -11.900 -8.189  1.00 12.38 ?  91  HIS   B H    1 
ATOM   5440 H HA   . HIS   B 1 91  ? 47.988 -10.825 -5.741  1.00 12.34 ?  91  HIS   B HA   1 
ATOM   5441 H HB2  . HIS   B 1 91  ? 45.413 -11.457 -6.767  1.00 14.10 ?  91  HIS   B HB2  1 
ATOM   5442 H HB3  . HIS   B 1 91  ? 45.681 -10.966 -5.282  1.00 14.10 ?  91  HIS   B HB3  1 
ATOM   5443 H HD1  . HIS   B 1 91  ? 46.942 -8.468  -5.372  1.00 21.03 ?  91  HIS   B HD1  1 
ATOM   5444 H HD2  . HIS   B 1 91  ? 44.419 -9.428  -8.180  1.00 20.88 ?  91  HIS   B HD2  1 
ATOM   5445 H HE1  . HIS   B 1 91  ? 46.278 -6.433  -6.377  1.00 22.39 ?  91  HIS   B HE1  1 
ATOM   5446 N N    . CYS   B 1 92  ? 47.596 -12.942 -4.490  1.00 9.46  ?  92  CYS   B N    1 
ATOM   5447 C CA   . CYS   B 1 92  ? 47.298 -14.174 -3.776  1.00 9.56  ?  92  CYS   B CA   1 
ATOM   5448 C C    . CYS   B 1 92  ? 46.078 -13.936 -2.897  1.00 9.08  ?  92  CYS   B C    1 
ATOM   5449 O O    . CYS   B 1 92  ? 46.076 -13.024 -2.057  1.00 10.12 ?  92  CYS   B O    1 
ATOM   5450 C CB   . CYS   B 1 92  ? 48.473 -14.639 -2.920  1.00 9.76  ?  92  CYS   B CB   1 
ATOM   5451 S SG   . CYS   B 1 92  ? 48.115 -16.169 -2.021  1.00 9.93  ?  92  CYS   B SG   1 
ATOM   5452 H H    . CYS   B 1 92  ? 47.911 -12.317 -3.980  1.00 11.33 ?  92  CYS   B H    1 
ATOM   5453 H HA   . CYS   B 1 92  ? 47.094 -14.872 -4.422  1.00 11.45 ?  92  CYS   B HA   1 
ATOM   5454 H HB2  . CYS   B 1 92  ? 49.237 -14.793 -3.489  1.00 11.69 ?  92  CYS   B HB2  1 
ATOM   5455 H HB3  . CYS   B 1 92  ? 48.670 -13.948 -2.268  1.00 11.69 ?  92  CYS   B HB3  1 
ATOM   5456 H HG   . CYS   B 1 92  ? 49.082 -16.484 -1.388  1.00 11.90 ?  92  CYS   B HG   1 
ATOM   5457 N N    . LEU   B 1 93  ? 45.044 -14.749 -3.105  1.00 9.25  ?  93  LEU   B N    1 
ATOM   5458 C CA   . LEU   B 1 93  ? 43.867 -14.753 -2.249  1.00 9.30  ?  93  LEU   B CA   1 
ATOM   5459 C C    . LEU   B 1 93  ? 44.086 -15.818 -1.182  1.00 8.74  ?  93  LEU   B C    1 
ATOM   5460 O O    . LEU   B 1 93  ? 44.040 -17.019 -1.475  1.00 9.52  ?  93  LEU   B O    1 
ATOM   5461 C CB   . LEU   B 1 93  ? 42.607 -15.042 -3.062  1.00 9.56  ?  93  LEU   B CB   1 
ATOM   5462 C CG   . LEU   B 1 93  ? 41.303 -15.060 -2.258  1.00 10.25 ?  93  LEU   B CG   1 
ATOM   5463 C CD1  . LEU   B 1 93  ? 40.934 -13.669 -1.775  1.00 10.72 ?  93  LEU   B CD1  1 
ATOM   5464 C CD2  . LEU   B 1 93  ? 40.174 -15.658 -3.082  1.00 10.59 ?  93  LEU   B CD2  1 
ATOM   5465 H H    . LEU   B 1 93  ? 45.001 -15.325 -3.756  1.00 11.07 ?  93  LEU   B H    1 
ATOM   5466 H HA   . LEU   B 1 93  ? 43.774 -13.889 -1.824  1.00 11.13 ?  93  LEU   B HA   1 
ATOM   5467 H HB2  . LEU   B 1 93  ? 42.515 -14.352 -3.742  1.00 11.45 ?  93  LEU   B HB2  1 
ATOM   5468 H HB3  . LEU   B 1 93  ? 42.697 -15.904 -3.483  1.00 11.45 ?  93  LEU   B HB3  1 
ATOM   5469 H HG   . LEU   B 1 93  ? 41.420 -15.613 -1.475  1.00 12.28 ?  93  LEU   B HG   1 
ATOM   5470 H HD11 . LEU   B 1 93  ? 40.082 -13.708 -1.314  1.00 12.84 ?  93  LEU   B HD11 1 
ATOM   5471 H HD12 . LEU   B 1 93  ? 41.623 -13.346 -1.179  1.00 12.84 ?  93  LEU   B HD12 1 
ATOM   5472 H HD13 . LEU   B 1 93  ? 40.860 -13.077 -2.547  1.00 12.84 ?  93  LEU   B HD13 1 
ATOM   5473 H HD21 . LEU   B 1 93  ? 39.357 -15.650 -2.556  1.00 12.68 ?  93  LEU   B HD21 1 
ATOM   5474 H HD22 . LEU   B 1 93  ? 40.053 -15.134 -3.888  1.00 12.68 ?  93  LEU   B HD22 1 
ATOM   5475 H HD23 . LEU   B 1 93  ? 40.406 -16.572 -3.314  1.00 12.68 ?  93  LEU   B HD23 1 
ATOM   5476 N N    . HIS   B 1 94  ? 44.359 -15.379 0.041   1.00 8.98  ?  94  HIS   B N    1 
ATOM   5477 C CA   . HIS   B 1 94  ? 44.575 -16.284 1.162   1.00 8.89  ?  94  HIS   B CA   1 
ATOM   5478 C C    . HIS   B 1 94  ? 43.213 -16.635 1.739   1.00 9.34  ?  94  HIS   B C    1 
ATOM   5479 O O    . HIS   B 1 94  ? 42.544 -15.760 2.290   1.00 10.51 ?  94  HIS   B O    1 
ATOM   5480 C CB   . HIS   B 1 94  ? 45.443 -15.608 2.219   1.00 9.47  ?  94  HIS   B CB   1 
ATOM   5481 C CG   . HIS   B 1 94  ? 46.827 -15.308 1.752   1.00 9.41  ?  94  HIS   B CG   1 
ATOM   5482 N ND1  . HIS   B 1 94  ? 47.850 -16.224 1.843   1.00 9.50  ?  94  HIS   B ND1  1 
ATOM   5483 C CD2  . HIS   B 1 94  ? 47.338 -14.205 1.152   1.00 9.79  ?  94  HIS   B CD2  1 
ATOM   5484 C CE1  . HIS   B 1 94  ? 48.942 -15.678 1.336   1.00 9.51  ?  94  HIS   B CE1  1 
ATOM   5485 N NE2  . HIS   B 1 94  ? 48.660 -14.456 0.910   1.00 9.88  ?  94  HIS   B NE2  1 
ATOM   5486 H H    . HIS   B 1 94  ? 44.427 -14.542 0.245   1.00 10.75 ?  94  HIS   B H    1 
ATOM   5487 H HA   . HIS   B 1 94  ? 45.009 -17.091 0.853   1.00 10.64 ?  94  HIS   B HA   1 
ATOM   5488 H HB2  . HIS   B 1 94  ? 45.025 -14.772 2.475   1.00 11.34 ?  94  HIS   B HB2  1 
ATOM   5489 H HB3  . HIS   B 1 94  ? 45.506 -16.197 2.984   1.00 11.34 ?  94  HIS   B HB3  1 
ATOM   5490 H HD2  . HIS   B 1 94  ? 46.886 -13.421 0.952   1.00 11.72 ?  94  HIS   B HD2  1 
ATOM   5491 H HE1  . HIS   B 1 94  ? 49.773 -16.103 1.284   1.00 11.38 ?  94  HIS   B HE1  1 
ATOM   5492 H HE2  . HIS   B 1 94  ? 49.222 -13.923 0.545   1.00 11.83 ?  94  HIS   B HE2  1 
ATOM   5493 N N    . VAL   B 1 95  ? 42.782 -17.889 1.592   1.00 9.32  ?  95  VAL   B N    1 
ATOM   5494 C CA   . VAL   B 1 95  ? 41.450 -18.324 2.020   1.00 9.49  ?  95  VAL   B CA   1 
ATOM   5495 C C    . VAL   B 1 95  ? 41.611 -19.362 3.118   1.00 9.47  ?  95  VAL   B C    1 
ATOM   5496 O O    . VAL   B 1 95  ? 42.391 -20.308 2.965   1.00 10.20 ?  95  VAL   B O    1 
ATOM   5497 C CB   . VAL   B 1 95  ? 40.629 -18.926 0.863   1.00 9.88  ?  95  VAL   B CB   1 
ATOM   5498 C CG1  . VAL   B 1 95  ? 39.251 -19.364 1.354   1.00 11.06 ?  95  VAL   B CG1  1 
ATOM   5499 C CG2  . VAL   B 1 95  ? 40.509 -17.946 -0.282  1.00 9.97  ?  95  VAL   B CG2  1 
ATOM   5500 H H    . VAL   B 1 95  ? 43.250 -18.519 1.236   1.00 11.16 ?  95  VAL   B H    1 
ATOM   5501 H HA   . VAL   B 1 95  ? 40.962 -17.565 2.381   1.00 11.36 ?  95  VAL   B HA   1 
ATOM   5502 H HB   . VAL   B 1 95  ? 41.083 -19.708 0.532   1.00 11.83 ?  95  VAL   B HB   1 
ATOM   5503 H HG11 . VAL   B 1 95  ? 38.680 -19.548 0.587   1.00 13.25 ?  95  VAL   B HG11 1 
ATOM   5504 H HG12 . VAL   B 1 95  ? 39.338 -20.164 1.894   1.00 13.25 ?  95  VAL   B HG12 1 
ATOM   5505 H HG13 . VAL   B 1 95  ? 38.853 -18.650 1.885   1.00 13.25 ?  95  VAL   B HG13 1 
ATOM   5506 H HG21 . VAL   B 1 95  ? 39.938 -18.339 -0.962  1.00 11.94 ?  95  VAL   B HG21 1 
ATOM   5507 H HG22 . VAL   B 1 95  ? 40.116 -17.126 0.048   1.00 11.94 ?  95  VAL   B HG22 1 
ATOM   5508 H HG23 . VAL   B 1 95  ? 41.390 -17.781 -0.639  1.00 11.94 ?  95  VAL   B HG23 1 
ATOM   5509 N N    . VAL   B 1 96  ? 40.880 -19.187 4.213   1.00 10.06 ?  96  VAL   B N    1 
ATOM   5510 C CA   . VAL   B 1 96  ? 40.957 -20.102 5.349   1.00 10.39 ?  96  VAL   B CA   1 
ATOM   5511 C C    . VAL   B 1 96  ? 39.766 -21.057 5.300   1.00 10.91 ?  96  VAL   B C    1 
ATOM   5512 O O    . VAL   B 1 96  ? 38.649 -20.703 5.684   1.00 11.83 ?  96  VAL   B O    1 
ATOM   5513 C CB   . VAL   B 1 96  ? 41.008 -19.357 6.684   1.00 11.16 ?  96  VAL   B CB   1 
ATOM   5514 C CG1  . VAL   B 1 96  ? 41.165 -20.352 7.827   1.00 11.70 ?  96  VAL   B CG1  1 
ATOM   5515 C CG2  . VAL   B 1 96  ? 42.125 -18.323 6.697   1.00 11.71 ?  96  VAL   B CG2  1 
ATOM   5516 H H    . VAL   B 1 96  ? 40.323 -18.541 4.325   1.00 12.05 ?  96  VAL   B H    1 
ATOM   5517 H HA   . VAL   B 1 96  ? 41.766 -20.632 5.273   1.00 12.44 ?  96  VAL   B HA   1 
ATOM   5518 H HB   . VAL   B 1 96  ? 40.167 -18.893 6.814   1.00 13.37 ?  96  VAL   B HB   1 
ATOM   5519 H HG11 . VAL   B 1 96  ? 41.357 -19.865 8.647   1.00 14.02 ?  96  VAL   B HG11 1 
ATOM   5520 H HG12 . VAL   B 1 96  ? 40.339 -20.854 7.935   1.00 14.02 ?  96  VAL   B HG12 1 
ATOM   5521 H HG13 . VAL   B 1 96  ? 41.896 -20.957 7.628   1.00 14.02 ?  96  VAL   B HG13 1 
ATOM   5522 H HG21 . VAL   B 1 96  ? 42.173 -17.914 7.578   1.00 14.03 ?  96  VAL   B HG21 1 
ATOM   5523 H HG22 . VAL   B 1 96  ? 42.966 -18.754 6.488   1.00 14.03 ?  96  VAL   B HG22 1 
ATOM   5524 H HG23 . VAL   B 1 96  ? 41.932 -17.638 6.033   1.00 14.03 ?  96  VAL   B HG23 1 
ATOM   5525 N N    . GLY   B 1 97  ? 39.999 -22.288 4.855   1.00 11.02 ?  97  GLY   B N    1 
ATOM   5526 C CA   . GLY   B 1 97  ? 39.020 -23.341 5.015   1.00 12.16 ?  97  GLY   B CA   1 
ATOM   5527 C C    . GLY   B 1 97  ? 39.148 -23.957 6.392   1.00 12.94 ?  97  GLY   B C    1 
ATOM   5528 O O    . GLY   B 1 97  ? 40.190 -23.838 7.050   1.00 13.65 ?  97  GLY   B O    1 
ATOM   5529 H H    . GLY   B 1 97  ? 40.719 -22.536 4.446   1.00 13.20 ?  97  GLY   B H    1 
ATOM   5530 H HA2  . GLY   B 1 97  ? 38.124 -22.970 4.899   1.00 14.56 ?  97  GLY   B HA2  1 
ATOM   5531 H HA3  . GLY   B 1 97  ? 39.154 -24.027 4.340   1.00 14.56 ?  97  GLY   B HA3  1 
ATOM   5532 N N    . PRO   B 1 98  ? 38.098 -24.639 6.855   1.00 14.28 ?  98  PRO   B N    1 
ATOM   5533 C CA   . PRO   B 1 98  ? 38.193 -25.337 8.142   1.00 15.30 ?  98  PRO   B CA   1 
ATOM   5534 C C    . PRO   B 1 98  ? 39.217 -26.461 8.097   1.00 15.10 ?  98  PRO   B C    1 
ATOM   5535 O O    . PRO   B 1 98  ? 39.327 -27.194 7.115   1.00 15.45 ?  98  PRO   B O    1 
ATOM   5536 C CB   . PRO   B 1 98  ? 36.775 -25.878 8.353   1.00 15.67 ?  98  PRO   B CB   1 
ATOM   5537 C CG   . PRO   B 1 98  ? 36.204 -25.999 6.984   1.00 15.33 ?  98  PRO   B CG   1 
ATOM   5538 C CD   . PRO   B 1 98  ? 36.781 -24.839 6.218   1.00 14.35 ?  98  PRO   B CD   1 
ATOM   5539 H HA   . PRO   B 1 98  ? 38.415 -24.711 8.845   1.00 18.34 ?  98  PRO   B HA   1 
ATOM   5540 H HB2  . PRO   B 1 98  ? 36.822 -26.747 8.787   1.00 18.78 ?  98  PRO   B HB2  1 
ATOM   5541 H HB3  . PRO   B 1 98  ? 36.261 -25.256 8.887   1.00 18.78 ?  98  PRO   B HB3  1 
ATOM   5542 H HG2  . PRO   B 1 98  ? 36.477 -26.848 6.593   1.00 18.38 ?  98  PRO   B HG2  1 
ATOM   5543 H HG3  . PRO   B 1 98  ? 35.236 -25.944 7.031   1.00 18.38 ?  98  PRO   B HG3  1 
ATOM   5544 H HD2  . PRO   B 1 98  ? 36.879 -25.075 5.277   1.00 17.19 ?  98  PRO   B HD2  1 
ATOM   5545 H HD3  . PRO   B 1 98  ? 36.224 -24.053 6.327   1.00 17.19 ?  98  PRO   B HD3  1 
ATOM   5546 N N    . ASN   B 1 99  ? 39.969 -26.590 9.182   1.00 16.37 ?  99  ASN   B N    1 
ATOM   5547 C CA   . ASN   B 1 99  ? 40.948 -27.663 9.340   1.00 17.50 ?  99  ASN   B CA   1 
ATOM   5548 C C    . ASN   B 1 99  ? 40.326 -28.743 10.222  1.00 20.46 ?  99  ASN   B C    1 
ATOM   5549 O O    . ASN   B 1 99  ? 40.254 -28.595 11.444  1.00 21.03 ?  99  ASN   B O    1 
ATOM   5550 C CB   . ASN   B 1 99  ? 42.226 -27.109 9.953   1.00 17.60 ?  99  ASN   B CB   1 
ATOM   5551 C CG   . ASN   B 1 99  ? 43.358 -28.117 9.953   1.00 18.33 ?  99  ASN   B CG   1 
ATOM   5552 O OD1  . ASN   B 1 99  ? 43.139 -29.309 10.122  1.00 19.19 ?  99  ASN   B OD1  1 
ATOM   5553 N ND2  . ASN   B 1 99  ? 44.574 -27.641 9.757   1.00 18.67 ?  99  ASN   B ND2  1 
ATOM   5554 H H    . ASN   B 1 99  ? 39.932 -26.052 9.849   1.00 19.62 ?  99  ASN   B H    1 
ATOM   5555 H HA   . ASN   B 1 99  ? 41.152 -28.053 8.477   1.00 20.98 ?  99  ASN   B HA   1 
ATOM   5556 H HB2  . ASN   B 1 99  ? 42.506 -26.338 9.450   1.00 21.10 ?  99  ASN   B HB2  1 
ATOM   5557 H HB3  . ASN   B 1 99  ? 42.043 -26.863 10.877  1.00 21.10 ?  99  ASN   B HB3  1 
ATOM   5558 H HD21 . ASN   B 1 99  ? 45.246 -28.175 9.749   1.00 22.38 ?  99  ASN   B HD21 1 
ATOM   5559 H HD22 . ASN   B 1 99  ? 44.685 -26.799 9.647   1.00 22.38 ?  99  ASN   B HD22 1 
ATOM   5560 N N    A VAL   B 1 100 ? 39.856 -29.824 9.596   0.48 22.73 ?  100 VAL   B N    1 
ATOM   5561 N N    B VAL   B 1 100 ? 39.879 -29.833 9.590   0.52 22.67 ?  100 VAL   B N    1 
ATOM   5562 C CA   A VAL   B 1 100 ? 39.248 -30.913 10.358  0.48 25.18 ?  100 VAL   B CA   1 
ATOM   5563 C CA   B VAL   B 1 100 ? 39.254 -30.929 10.326  0.52 25.07 ?  100 VAL   B CA   1 
ATOM   5564 C C    A VAL   B 1 100 ? 40.264 -31.565 11.290  0.48 25.72 ?  100 VAL   B C    1 
ATOM   5565 C C    B VAL   B 1 100 ? 40.255 -31.606 11.256  0.52 25.51 ?  100 VAL   B C    1 
ATOM   5566 O O    A VAL   B 1 100 ? 39.906 -32.036 12.377  0.48 26.31 ?  100 VAL   B O    1 
ATOM   5567 O O    B VAL   B 1 100 ? 39.875 -32.140 12.306  0.52 25.84 ?  100 VAL   B O    1 
ATOM   5568 C CB   A VAL   B 1 100 ? 38.580 -31.927 9.409   0.48 26.95 ?  100 VAL   B CB   1 
ATOM   5569 C CB   B VAL   B 1 100 ? 38.608 -31.920 9.338   0.52 26.83 ?  100 VAL   B CB   1 
ATOM   5570 C CG1  A VAL   B 1 100 ? 38.100 -33.147 10.181  0.48 27.68 ?  100 VAL   B CG1  1 
ATOM   5571 C CG1  B VAL   B 1 100 ? 38.114 -33.163 10.063  0.52 27.61 ?  100 VAL   B CG1  1 
ATOM   5572 C CG2  A VAL   B 1 100 ? 37.417 -31.270 8.678   0.48 27.46 ?  100 VAL   B CG2  1 
ATOM   5573 C CG2  B VAL   B 1 100 ? 37.463 -31.246 8.596   0.52 27.31 ?  100 VAL   B CG2  1 
ATOM   5574 H H    A VAL   B 1 100 ? 39.863 -29.941 8.741   0.48 27.25 ?  100 VAL   B H    1 
ATOM   5575 H H    B VAL   B 1 100 ? 39.924 -29.957 8.738   0.52 27.18 ?  100 VAL   B H    1 
ATOM   5576 H HA   A VAL   B 1 100 ? 38.542 -30.540 10.910  0.48 30.19 ?  100 VAL   B HA   1 
ATOM   5577 H HA   B VAL   B 1 100 ? 38.542 -30.565 10.873  0.52 30.06 ?  100 VAL   B HA   1 
ATOM   5578 H HB   A VAL   B 1 100 ? 39.226 -32.223 8.749   0.48 32.31 ?  100 VAL   B HB   1 
ATOM   5579 H HB   B VAL   B 1 100 ? 39.269 -32.199 8.685   0.52 32.18 ?  100 VAL   B HB   1 
ATOM   5580 H HG11 A VAL   B 1 100 ? 37.498 -33.659 9.617   0.48 33.20 ?  100 VAL   B HG11 1 
ATOM   5581 H HG11 B VAL   B 1 100 ? 37.528 -33.661 9.471   0.52 33.10 ?  100 VAL   B HG11 1 
ATOM   5582 H HG12 A VAL   B 1 100 ? 38.864 -33.692 10.425  0.48 33.20 ?  100 VAL   B HG12 1 
ATOM   5583 H HG12 B VAL   B 1 100 ? 38.874 -33.712 10.311  0.52 33.10 ?  100 VAL   B HG12 1 
ATOM   5584 H HG13 A VAL   B 1 100 ? 37.632 -32.853 10.978  0.48 33.20 ?  100 VAL   B HG13 1 
ATOM   5585 H HG13 B VAL   B 1 100 ? 37.626 -32.893 10.856  0.52 33.10 ?  100 VAL   B HG13 1 
ATOM   5586 H HG21 A VAL   B 1 100 ? 37.000 -31.923 8.095   0.48 32.93 ?  100 VAL   B HG21 1 
ATOM   5587 H HG21 B VAL   B 1 100 ? 37.053 -31.889 7.997   0.52 32.75 ?  100 VAL   B HG21 1 
ATOM   5588 H HG22 A VAL   B 1 100 ? 36.772 -30.953 9.332   0.48 32.93 ?  100 VAL   B HG22 1 
ATOM   5589 H HG22 B VAL   B 1 100 ? 36.810 -30.934 9.243   0.52 32.75 ?  100 VAL   B HG22 1 
ATOM   5590 H HG23 A VAL   B 1 100 ? 37.751 -30.525 8.156   0.48 32.93 ?  100 VAL   B HG23 1 
ATOM   5591 H HG23 B VAL   B 1 100 ? 37.813 -30.498 8.090   0.52 32.75 ?  100 VAL   B HG23 1 
ATOM   5592 N N    . ASN   B 1 101 ? 41.538 -31.613 10.889  1.00 26.05 ?  101 ASN   B N    1 
ATOM   5593 C CA   . ASN   B 1 101 ? 42.579 -32.147 11.766  1.00 27.75 ?  101 ASN   B CA   1 
ATOM   5594 C C    . ASN   B 1 101 ? 42.786 -31.303 13.018  1.00 30.16 ?  101 ASN   B C    1 
ATOM   5595 O O    . ASN   B 1 101 ? 43.454 -31.765 13.952  1.00 31.44 ?  101 ASN   B O    1 
ATOM   5596 C CB   . ASN   B 1 101 ? 43.899 -32.292 11.005  1.00 27.47 ?  101 ASN   B CB   1 
ATOM   5597 C CG   . ASN   B 1 101 ? 43.882 -33.452 10.028  1.00 26.99 ?  101 ASN   B CG   1 
ATOM   5598 O OD1  . ASN   B 1 101 ? 43.196 -34.444 10.246  1.00 27.44 ?  101 ASN   B OD1  1 
ATOM   5599 N ND2  . ASN   B 1 101 ? 44.629 -33.325 8.939   1.00 26.52 ?  101 ASN   B ND2  1 
ATOM   5600 H H    A ASN   B 1 101 ? 41.816 -31.357 10.116  0.48 31.24 ?  101 ASN   B H    1 
ATOM   5601 H H    B ASN   B 1 101 ? 41.825 -31.325 10.130  0.52 31.24 ?  101 ASN   B H    1 
ATOM   5602 H HA   . ASN   B 1 101 ? 42.309 -33.027 12.056  1.00 33.27 ?  101 ASN   B HA   1 
ATOM   5603 H HB2  . ASN   B 1 101 ? 44.073 -31.481 10.503  1.00 32.94 ?  101 ASN   B HB2  1 
ATOM   5604 H HB3  . ASN   B 1 101 ? 44.614 -32.448 11.641  1.00 32.94 ?  101 ASN   B HB3  1 
ATOM   5605 H HD21 . ASN   B 1 101 ? 44.649 -33.958 8.357   1.00 31.80 ?  101 ASN   B HD21 1 
ATOM   5606 H HD22 . ASN   B 1 101 ? 45.093 -32.613 8.818   1.00 31.80 ?  101 ASN   B HD22 1 
ATOM   5607 N N    . LYS   B 1 102 ? 42.241 -30.084 13.051  1.00 32.83 ?  102 LYS   B N    1 
ATOM   5608 C CA   . LYS   B 1 102 ? 42.197 -29.260 14.252  1.00 35.77 ?  102 LYS   B CA   1 
ATOM   5609 C C    . LYS   B 1 102 ? 40.799 -29.203 14.856  1.00 35.26 ?  102 LYS   B C    1 
ATOM   5610 O O    . LYS   B 1 102 ? 40.548 -28.376 15.739  1.00 35.68 ?  102 LYS   B O    1 
ATOM   5611 C CB   . LYS   B 1 102 ? 42.675 -27.838 13.949  1.00 39.32 ?  102 LYS   B CB   1 
ATOM   5612 C CG   . LYS   B 1 102 ? 44.136 -27.718 13.555  1.00 42.62 ?  102 LYS   B CG   1 
ATOM   5613 C CD   . LYS   B 1 102 ? 44.434 -26.303 13.084  1.00 45.78 ?  102 LYS   B CD   1 
ATOM   5614 C CE   . LYS   B 1 102 ? 45.922 -26.055 12.910  1.00 48.18 ?  102 LYS   B CE   1 
ATOM   5615 N NZ   . LYS   B 1 102 ? 46.184 -24.656 12.459  1.00 49.59 ?  102 LYS   B NZ   1 
ATOM   5616 H H    . LYS   B 1 102 ? 41.875 -29.704 12.370  1.00 39.37 ?  102 LYS   B H    1 
ATOM   5617 H HA   . LYS   B 1 102 ? 42.795 -29.636 14.914  1.00 42.90 ?  102 LYS   B HA   1 
ATOM   5618 H HB2  . LYS   B 1 102 ? 42.146 -27.483 13.219  1.00 47.16 ?  102 LYS   B HB2  1 
ATOM   5619 H HB3  . LYS   B 1 102 ? 42.542 -27.291 14.741  1.00 47.16 ?  102 LYS   B HB3  1 
ATOM   5620 H HG2  . LYS   B 1 102 ? 44.698 -27.913 14.322  1.00 51.12 ?  102 LYS   B HG2  1 
ATOM   5621 H HG3  . LYS   B 1 102 ? 44.328 -28.333 12.829  1.00 51.12 ?  102 LYS   B HG3  1 
ATOM   5622 H HD2  . LYS   B 1 102 ? 44.002 -26.156 12.227  1.00 54.92 ?  102 LYS   B HD2  1 
ATOM   5623 H HD3  . LYS   B 1 102 ? 44.097 -25.672 13.739  1.00 54.92 ?  102 LYS   B HD3  1 
ATOM   5624 H HE2  . LYS   B 1 102 ? 46.372 -26.191 13.759  1.00 57.80 ?  102 LYS   B HE2  1 
ATOM   5625 H HE3  . LYS   B 1 102 ? 46.274 -26.662 12.240  1.00 57.80 ?  102 LYS   B HE3  1 
ATOM   5626 H HZ1  . LYS   B 1 102 ? 47.058 -24.526 12.362  1.00 59.49 ?  102 LYS   B HZ1  1 
ATOM   5627 H HZ2  . LYS   B 1 102 ? 45.781 -24.508 11.679  1.00 59.49 ?  102 LYS   B HZ2  1 
ATOM   5628 H HZ3  . LYS   B 1 102 ? 45.870 -24.079 13.060  1.00 59.49 ?  102 LYS   B HZ3  1 
ATOM   5629 N N    . GLY   B 1 103 ? 39.878 -30.041 14.387  1.00 34.77 ?  103 GLY   B N    1 
ATOM   5630 C CA   . GLY   B 1 103 ? 38.543 -30.101 14.945  1.00 34.50 ?  103 GLY   B CA   1 
ATOM   5631 C C    . GLY   B 1 103 ? 37.604 -29.005 14.499  1.00 33.57 ?  103 GLY   B C    1 
ATOM   5632 O O    . GLY   B 1 103 ? 36.513 -28.879 15.067  1.00 33.75 ?  103 GLY   B O    1 
ATOM   5633 H H    . GLY   B 1 103 ? 40.006 -30.583 13.734  1.00 41.70 ?  103 GLY   B H    1 
ATOM   5634 H HA2  . GLY   B 1 103 ? 38.145 -30.954 14.709  1.00 41.38 ?  103 GLY   B HA2  1 
ATOM   5635 H HA3  . GLY   B 1 103 ? 38.604 -30.057 15.911  1.00 41.38 ?  103 GLY   B HA3  1 
ATOM   5636 N N    A GLU   B 1 104 ? 37.999 -28.194 13.520  0.48 32.84 ?  104 GLU   B N    1 
ATOM   5637 N N    B GLU   B 1 104 ? 37.973 -28.221 13.490  0.52 32.63 ?  104 GLU   B N    1 
ATOM   5638 C CA   A GLU   B 1 104 ? 37.163 -27.093 13.071  0.48 31.95 ?  104 GLU   B CA   1 
ATOM   5639 C CA   B GLU   B 1 104 ? 37.113 -27.144 13.027  0.52 31.56 ?  104 GLU   B CA   1 
ATOM   5640 C C    A GLU   B 1 104 ? 35.972 -27.614 12.267  0.48 32.01 ?  104 GLU   B C    1 
ATOM   5641 C C    B GLU   B 1 104 ? 35.944 -27.696 12.210  0.52 31.52 ?  104 GLU   B C    1 
ATOM   5642 O O    A GLU   B 1 104 ? 36.002 -28.705 11.689  0.48 32.39 ?  104 GLU   B O    1 
ATOM   5643 O O    B GLU   B 1 104 ? 36.005 -28.791 11.643  0.52 31.94 ?  104 GLU   B O    1 
ATOM   5644 C CB   A GLU   B 1 104 ? 37.996 -26.100 12.257  0.48 31.05 ?  104 GLU   B CB   1 
ATOM   5645 C CB   B GLU   B 1 104 ? 37.928 -26.127 12.227  0.52 30.58 ?  104 GLU   B CB   1 
ATOM   5646 C CG   A GLU   B 1 104 ? 39.105 -25.449 13.078  0.48 30.07 ?  104 GLU   B CG   1 
ATOM   5647 C CG   B GLU   B 1 104 ? 39.014 -25.469 13.072  0.52 29.51 ?  104 GLU   B CG   1 
ATOM   5648 C CD   A GLU   B 1 104 ? 40.027 -24.567 12.264  0.48 29.07 ?  104 GLU   B CD   1 
ATOM   5649 C CD   B GLU   B 1 104 ? 39.982 -24.621 12.275  0.52 28.41 ?  104 GLU   B CD   1 
ATOM   5650 O OE1  A GLU   B 1 104 ? 40.017 -24.661 11.019  0.48 27.98 ?  104 GLU   B OE1  1 
ATOM   5651 O OE1  B GLU   B 1 104 ? 39.970 -24.688 11.028  0.52 27.37 ?  104 GLU   B OE1  1 
ATOM   5652 O OE2  A GLU   B 1 104 ? 40.771 -23.775 12.881  0.48 28.75 -1 104 GLU   B OE2  1 
ATOM   5653 O OE2  B GLU   B 1 104 ? 40.765 -23.882 12.908  0.52 27.92 -1 104 GLU   B OE2  1 
ATOM   5654 H H    A GLU   B 1 104 ? 38.751 -28.257 13.109  0.48 39.38 ?  104 GLU   B H    1 
ATOM   5655 H H    B GLU   B 1 104 ? 38.719 -28.287 13.065  0.52 39.13 ?  104 GLU   B H    1 
ATOM   5656 H HA   A GLU   B 1 104 ? 36.819 -26.624 13.847  0.48 38.32 ?  104 GLU   B HA   1 
ATOM   5657 H HA   B GLU   B 1 104 ? 36.745 -26.688 13.798  0.52 37.85 ?  104 GLU   B HA   1 
ATOM   5658 H HB2  A GLU   B 1 104 ? 38.408 -26.565 11.514  0.48 37.24 ?  104 GLU   B HB2  1 
ATOM   5659 H HB2  B GLU   B 1 104 ? 38.354 -26.577 11.482  0.52 36.67 ?  104 GLU   B HB2  1 
ATOM   5660 H HB3  A GLU   B 1 104 ? 37.416 -25.395 11.928  0.48 37.24 ?  104 GLU   B HB3  1 
ATOM   5661 H HB3  B GLU   B 1 104 ? 37.335 -25.431 11.903  0.52 36.67 ?  104 GLU   B HB3  1 
ATOM   5662 H HG2  A GLU   B 1 104 ? 38.705 -24.901 13.771  0.48 36.06 ?  104 GLU   B HG2  1 
ATOM   5663 H HG2  B GLU   B 1 104 ? 38.593 -24.897 13.732  0.52 35.38 ?  104 GLU   B HG2  1 
ATOM   5664 H HG3  A GLU   B 1 104 ? 39.651 -26.142 13.478  0.48 36.06 ?  104 GLU   B HG3  1 
ATOM   5665 H HG3  B GLU   B 1 104 ? 39.529 -26.160 13.515  0.52 35.38 ?  104 GLU   B HG3  1 
ATOM   5666 N N    A ASP   B 1 105 ? 34.909 -26.813 12.244  0.48 31.44 ?  105 ASP   B N    1 
ATOM   5667 N N    B ASP   B 1 105 ? 34.865 -26.916 12.163  0.52 30.70 ?  105 ASP   B N    1 
ATOM   5668 C CA   A ASP   B 1 105 ? 33.635 -27.254 11.686  0.48 31.55 ?  105 ASP   B CA   1 
ATOM   5669 C CA   B ASP   B 1 105 ? 33.598 -27.379 11.606  0.52 30.63 ?  105 ASP   B CA   1 
ATOM   5670 C C    A ASP   B 1 105 ? 33.708 -27.305 10.165  0.48 29.50 ?  105 ASP   B C    1 
ATOM   5671 C C    B ASP   B 1 105 ? 33.664 -27.389 10.083  0.52 28.60 ?  105 ASP   B C    1 
ATOM   5672 O O    A ASP   B 1 105 ? 33.908 -26.277 9.509   0.48 28.75 ?  105 ASP   B O    1 
ATOM   5673 O O    B ASP   B 1 105 ? 33.835 -26.339 9.455   0.52 27.68 ?  105 ASP   B O    1 
ATOM   5674 C CB   A ASP   B 1 105 ? 32.526 -26.303 12.130  0.48 33.81 ?  105 ASP   B CB   1 
ATOM   5675 C CB   B ASP   B 1 105 ? 32.461 -26.475 12.080  0.52 32.78 ?  105 ASP   B CB   1 
ATOM   5676 C CG   A ASP   B 1 105 ? 31.150 -26.764 11.692  0.48 35.86 ?  105 ASP   B CG   1 
ATOM   5677 C CG   B ASP   B 1 105 ? 31.091 -27.026 11.727  0.52 34.62 ?  105 ASP   B CG   1 
ATOM   5678 O OD1  A ASP   B 1 105 ? 31.036 -27.886 11.154  0.48 36.28 ?  105 ASP   B OD1  1 
ATOM   5679 O OD1  B ASP   B 1 105 ? 31.022 -28.044 11.006  0.52 35.06 ?  105 ASP   B OD1  1 
ATOM   5680 O OD2  A ASP   B 1 105 ? 30.180 -25.999 11.883  0.48 36.93 -1 105 ASP   B OD2  1 
ATOM   5681 O OD2  B ASP   B 1 105 ? 30.080 -26.447 12.181  0.52 35.34 -1 105 ASP   B OD2  1 
ATOM   5682 H H    A ASP   B 1 105 ? 34.902 -26.008 12.546  0.48 37.70 ?  105 ASP   B H    1 
ATOM   5683 H H    B ASP   B 1 105 ? 34.842 -26.107 12.451  0.52 36.81 ?  105 ASP   B H    1 
ATOM   5684 H HA   A ASP   B 1 105 ? 33.431 -28.143 12.014  0.48 37.83 ?  105 ASP   B HA   1 
ATOM   5685 H HA   B ASP   B 1 105 ? 33.418 -28.281 11.910  0.52 36.74 ?  105 ASP   B HA   1 
ATOM   5686 H HB2  A ASP   B 1 105 ? 32.537 -26.234 13.098  0.48 40.55 ?  105 ASP   B HB2  1 
ATOM   5687 H HB2  B ASP   B 1 105 ? 32.507 -26.385 13.044  0.52 39.32 ?  105 ASP   B HB2  1 
ATOM   5688 H HB3  A ASP   B 1 105 ? 32.675 -25.433 11.733  0.48 40.55 ?  105 ASP   B HB3  1 
ATOM   5689 H HB3  B ASP   B 1 105 ? 32.554 -25.603 11.662  0.52 39.32 ?  105 ASP   B HB3  1 
ATOM   5690 N N    A ILE   B 1 106 ? 33.519 -28.504 9.606   0.48 28.64 ?  106 ILE   B N    1 
ATOM   5691 N N    B ILE   B 1 106 ? 33.497 -28.577 9.494   0.52 27.89 ?  106 ILE   B N    1 
ATOM   5692 C CA   A ILE   B 1 106 ? 33.524 -28.688 8.160   0.48 27.77 ?  106 ILE   B CA   1 
ATOM   5693 C CA   B ILE   B 1 106 ? 33.496 -28.723 8.043   0.52 27.25 ?  106 ILE   B CA   1 
ATOM   5694 C C    A ILE   B 1 106 ? 32.436 -27.866 7.478   0.48 26.68 ?  106 ILE   B C    1 
ATOM   5695 C C    B ILE   B 1 106 ? 32.403 -27.885 7.390   0.52 26.14 ?  106 ILE   B C    1 
ATOM   5696 O O    A ILE   B 1 106 ? 32.540 -27.573 6.282   0.48 26.11 ?  106 ILE   B O    1 
ATOM   5697 O O    B ILE   B 1 106 ? 32.488 -27.579 6.196   0.52 25.41 ?  106 ILE   B O    1 
ATOM   5698 C CB   A ILE   B 1 106 ? 33.403 -30.193 7.828   0.48 28.06 ?  106 ILE   B CB   1 
ATOM   5699 C CB   B ILE   B 1 106 ? 33.379 -30.222 7.675   0.52 27.73 ?  106 ILE   B CB   1 
ATOM   5700 C CG1  A ILE   B 1 106 ? 33.651 -30.450 6.339   0.48 27.96 ?  106 ILE   B CG1  1 
ATOM   5701 C CG1  B ILE   B 1 106 ? 33.671 -30.449 6.190   0.52 27.84 ?  106 ILE   B CG1  1 
ATOM   5702 C CG2  A ILE   B 1 106 ? 32.035 -30.724 8.240   0.48 28.58 ?  106 ILE   B CG2  1 
ATOM   5703 C CG2  B ILE   B 1 106 ? 31.996 -30.756 8.030   0.52 28.30 ?  106 ILE   B CG2  1 
ATOM   5704 C CD1  A ILE   B 1 106 ? 35.018 -30.009 5.866   0.48 27.80 ?  106 ILE   B CD1  1 
ATOM   5705 C CD1  B ILE   B 1 106 ? 35.047 -29.987 5.766   0.52 27.87 ?  106 ILE   B CD1  1 
ATOM   5706 H H    A ILE   B 1 106 ? 33.389 -29.226 10.049  0.48 34.34 ?  106 ILE   B H    1 
ATOM   5707 H H    B ILE   B 1 106 ? 33.384 -29.314 9.918   0.52 33.45 ?  106 ILE   B H    1 
ATOM   5708 H HA   A ILE   B 1 106 ? 34.375 -28.378 7.820   0.48 33.30 ?  106 ILE   B HA   1 
ATOM   5709 H HA   B ILE   B 1 106 ? 34.342 -28.401 7.707   0.52 32.68 ?  106 ILE   B HA   1 
ATOM   5710 H HB   A ILE   B 1 106 ? 34.078 -30.672 8.334   0.48 33.65 ?  106 ILE   B HB   1 
ATOM   5711 H HB   B ILE   B 1 106 ? 34.034 -30.715 8.192   0.52 33.25 ?  106 ILE   B HB   1 
ATOM   5712 H HG12 A ILE   B 1 106 ? 33.576 -31.404 6.171   0.48 33.53 ?  106 ILE   B HG12 1 
ATOM   5713 H HG12 B ILE   B 1 106 ? 33.610 -31.400 6.001   0.52 33.39 ?  106 ILE   B HG12 1 
ATOM   5714 H HG13 A ILE   B 1 106 ? 32.987 -29.974 5.819   0.48 33.53 ?  106 ILE   B HG13 1 
ATOM   5715 H HG13 B ILE   B 1 106 ? 33.018 -29.968 5.661   0.52 33.39 ?  106 ILE   B HG13 1 
ATOM   5716 H HG21 A ILE   B 1 106 ? 32.037 -31.691 8.162   0.48 34.27 ?  106 ILE   B HG21 1 
ATOM   5717 H HG21 B ILE   B 1 106 ? 32.005 -31.724 7.963   0.52 33.93 ?  106 ILE   B HG21 1 
ATOM   5718 H HG22 A ILE   B 1 106 ? 31.861 -30.467 9.159   0.48 34.27 ?  106 ILE   B HG22 1 
ATOM   5719 H HG22 B ILE   B 1 106 ? 31.779 -30.490 8.937   0.52 33.93 ?  106 ILE   B HG22 1 
ATOM   5720 H HG23 A ILE   B 1 106 ? 31.359 -30.347 7.657   0.48 34.27 ?  106 ILE   B HG23 1 
ATOM   5721 H HG23 B ILE   B 1 106 ? 31.345 -30.388 7.413   0.52 33.93 ?  106 ILE   B HG23 1 
ATOM   5722 H HD11 A ILE   B 1 106 ? 35.200 -30.414 5.005   0.48 33.34 ?  106 ILE   B HD11 1 
ATOM   5723 H HD11 B ILE   B 1 106 ? 35.268 -30.394 4.915   0.52 33.42 ?  106 ILE   B HD11 1 
ATOM   5724 H HD12 A ILE   B 1 106 ? 35.029 -29.042 5.785   0.48 33.34 ?  106 ILE   B HD12 1 
ATOM   5725 H HD12 B ILE   B 1 106 ? 35.043 -29.020 5.678   0.52 33.42 ?  106 ILE   B HD12 1 
ATOM   5726 H HD13 A ILE   B 1 106 ? 35.684 -30.294 6.512   0.48 33.34 ?  106 ILE   B HD13 1 
ATOM   5727 H HD13 B ILE   B 1 106 ? 35.692 -30.257 6.439   0.52 33.42 ?  106 ILE   B HD13 1 
ATOM   5728 N N    A GLN   B 1 107 ? 31.392 -27.476 8.213   0.48 26.61 ?  107 GLN   B N    1 
ATOM   5729 N N    B GLN   B 1 107 ? 31.378 -27.494 8.150   0.52 26.24 ?  107 GLN   B N    1 
ATOM   5730 C CA   A GLN   B 1 107 ? 30.315 -26.690 7.620   0.48 26.63 ?  107 GLN   B CA   1 
ATOM   5731 C CA   B GLN   B 1 107 ? 30.300 -26.685 7.592   0.52 26.42 ?  107 GLN   B CA   1 
ATOM   5732 C C    A GLN   B 1 107 ? 30.804 -25.342 7.107   0.48 24.11 ?  107 GLN   B C    1 
ATOM   5733 C C    B GLN   B 1 107 ? 30.786 -25.319 7.119   0.52 23.98 ?  107 GLN   B C    1 
ATOM   5734 O O    A GLN   B 1 107 ? 30.175 -24.769 6.212   0.48 24.50 ?  107 GLN   B O    1 
ATOM   5735 O O    B GLN   B 1 107 ? 30.138 -24.710 6.263   0.52 24.48 ?  107 GLN   B O    1 
ATOM   5736 C CB   A GLN   B 1 107 ? 29.195 -26.490 8.645   0.48 29.85 ?  107 GLN   B CB   1 
ATOM   5737 C CB   B GLN   B 1 107 ? 29.184 -26.528 8.629   0.52 29.83 ?  107 GLN   B CB   1 
ATOM   5738 C CG   A GLN   B 1 107 ? 27.876 -25.991 8.063   0.48 32.85 ?  107 GLN   B CG   1 
ATOM   5739 C CG   B GLN   B 1 107 ? 27.844 -26.078 8.059   0.52 33.02 ?  107 GLN   B CG   1 
ATOM   5740 C CD   A GLN   B 1 107 ? 27.813 -24.479 7.944   0.48 35.17 ?  107 GLN   B CD   1 
ATOM   5741 C CD   B GLN   B 1 107 ? 27.712 -24.568 7.985   0.52 35.50 ?  107 GLN   B CD   1 
ATOM   5742 O OE1  A GLN   B 1 107 ? 28.639 -23.763 8.512   0.48 36.01 ?  107 GLN   B OE1  1 
ATOM   5743 O OE1  B GLN   B 1 107 ? 28.508 -23.832 8.570   0.52 36.41 ?  107 GLN   B OE1  1 
ATOM   5744 N NE2  A GLN   B 1 107 ? 26.824 -23.985 7.204   0.48 35.97 ?  107 GLN   B NE2  1 
ATOM   5745 N NE2  B GLN   B 1 107 ? 26.698 -24.099 7.265   0.52 36.36 ?  107 GLN   B NE2  1 
ATOM   5746 H H    A GLN   B 1 107 ? 31.289 -27.646 9.046   0.48 31.90 ?  107 GLN   B H    1 
ATOM   5747 H H    B GLN   B 1 107 ? 31.285 -27.680 8.980   0.52 31.46 ?  107 GLN   B H    1 
ATOM   5748 H HA   A GLN   B 1 107 ? 29.946 -27.182 6.870   0.48 31.93 ?  107 GLN   B HA   1 
ATOM   5749 H HA   B GLN   B 1 107 ? 29.928 -27.147 6.825   0.52 31.68 ?  107 GLN   B HA   1 
ATOM   5750 H HB2  A GLN   B 1 107 ? 29.019 -27.339 9.075   0.48 35.80 ?  107 GLN   B HB2  1 
ATOM   5751 H HB2  B GLN   B 1 107 ? 29.044 -27.384 9.059   0.52 35.77 ?  107 GLN   B HB2  1 
ATOM   5752 H HB3  A GLN   B 1 107 ? 29.490 -25.844 9.305   0.48 35.80 ?  107 GLN   B HB3  1 
ATOM   5753 H HB3  B GLN   B 1 107 ? 29.461 -25.873 9.288   0.52 35.77 ?  107 GLN   B HB3  1 
ATOM   5754 H HG2  A GLN   B 1 107 ? 27.758 -26.363 7.176   0.48 39.39 ?  107 GLN   B HG2  1 
ATOM   5755 H HG2  B GLN   B 1 107 ? 27.746 -26.431 7.161   0.52 39.60 ?  107 GLN   B HG2  1 
ATOM   5756 H HG3  A GLN   B 1 107 ? 27.148 -26.278 8.640   0.48 39.39 ?  107 GLN   B HG3  1 
ATOM   5757 H HG3  B GLN   B 1 107 ? 27.131 -26.418 8.626   0.52 39.60 ?  107 GLN   B HG3  1 
ATOM   5758 H HE21 A GLN   B 1 107 ? 26.266 -24.517 6.820   0.48 43.14 ?  107 GLN   B HE21 1 
ATOM   5759 H HE21 B GLN   B 1 107 ? 26.163 -24.643 6.868   0.52 43.60 ?  107 GLN   B HE21 1 
ATOM   5760 H HE22 A GLN   B 1 107 ? 26.741 -23.134 7.108   0.48 43.14 ?  107 GLN   B HE22 1 
ATOM   5761 H HE22 B GLN   B 1 107 ? 26.578 -23.250 7.196   0.52 43.60 ?  107 GLN   B HE22 1 
ATOM   5762 N N    . LEU   B 1 108 ? 31.917 -24.831 7.640   1.00 21.88 ?  108 LEU   B N    1 
ATOM   5763 C CA   . LEU   B 1 108 ? 32.467 -23.535 7.229   1.00 18.79 ?  108 LEU   B CA   1 
ATOM   5764 C C    . LEU   B 1 108 ? 33.117 -23.564 5.854   1.00 15.89 ?  108 LEU   B C    1 
ATOM   5765 O O    . LEU   B 1 108 ? 33.552 -22.510 5.365   1.00 14.85 ?  108 LEU   B O    1 
ATOM   5766 C CB   . LEU   B 1 108 ? 33.475 -23.050 8.269   1.00 19.21 ?  108 LEU   B CB   1 
ATOM   5767 C CG   . LEU   B 1 108 ? 32.863 -22.465 9.542   1.00 21.02 ?  108 LEU   B CG   1 
ATOM   5768 C CD1  . LEU   B 1 108 ? 33.845 -22.530 10.694  1.00 21.57 ?  108 LEU   B CD1  1 
ATOM   5769 C CD2  . LEU   B 1 108 ? 32.428 -21.025 9.300   1.00 21.56 ?  108 LEU   B CD2  1 
ATOM   5770 H H    A LEU   B 1 108 ? 32.366 -25.217 8.259   0.48 26.23 ?  108 LEU   B H    1 
ATOM   5771 H H    B LEU   B 1 108 ? 32.377 -25.231 8.241   0.52 26.23 ?  108 LEU   B H    1 
ATOM   5772 H HA   . LEU   B 1 108 ? 31.744 -22.892 7.199   1.00 22.53 ?  108 LEU   B HA   1 
ATOM   5773 H HB2  . LEU   B 1 108 ? 34.029 -23.799 8.536   1.00 23.03 ?  108 LEU   B HB2  1 
ATOM   5774 H HB3  . LEU   B 1 108 ? 34.024 -22.362 7.868   1.00 23.03 ?  108 LEU   B HB3  1 
ATOM   5775 H HG   . LEU   B 1 108 ? 32.074 -22.974 9.786   1.00 25.20 ?  108 LEU   B HG   1 
ATOM   5776 H HD11 . LEU   B 1 108 ? 33.419 -22.180 11.495  1.00 25.86 ?  108 LEU   B HD11 1 
ATOM   5777 H HD12 . LEU   B 1 108 ? 34.105 -23.452 10.835  1.00 25.86 ?  108 LEU   B HD12 1 
ATOM   5778 H HD13 . LEU   B 1 108 ? 34.624 -21.994 10.477  1.00 25.86 ?  108 LEU   B HD13 1 
ATOM   5779 H HD21 . LEU   B 1 108 ? 32.040 -20.668 10.114  1.00 25.85 ?  108 LEU   B HD21 1 
ATOM   5780 H HD22 . LEU   B 1 108 ? 33.204 -20.499 9.046   1.00 25.85 ?  108 LEU   B HD22 1 
ATOM   5781 H HD23 . LEU   B 1 108 ? 31.771 -21.008 8.586   1.00 25.85 ?  108 LEU   B HD23 1 
ATOM   5782 N N    . LEU   B 1 109 ? 33.179 -24.733 5.223   1.00 14.44 ?  109 LEU   B N    1 
ATOM   5783 C CA   . LEU   B 1 109 ? 33.812 -24.853 3.918   1.00 13.52 ?  109 LEU   B CA   1 
ATOM   5784 C C    . LEU   B 1 109 ? 33.048 -24.081 2.848   1.00 12.97 ?  109 LEU   B C    1 
ATOM   5785 O O    . LEU   B 1 109 ? 33.663 -23.497 1.948   1.00 12.42 ?  109 LEU   B O    1 
ATOM   5786 C CB   . LEU   B 1 109 ? 33.920 -26.330 3.552   1.00 13.83 ?  109 LEU   B CB   1 
ATOM   5787 C CG   . LEU   B 1 109 ? 34.704 -26.682 2.293   1.00 13.43 ?  109 LEU   B CG   1 
ATOM   5788 C CD1  . LEU   B 1 109 ? 36.088 -26.038 2.301   1.00 13.40 ?  109 LEU   B CD1  1 
ATOM   5789 C CD2  . LEU   B 1 109 ? 34.811 -28.200 2.163   1.00 14.17 ?  109 LEU   B CD2  1 
ATOM   5790 H H    . LEU   B 1 109 ? 32.869 -25.469 5.529   1.00 17.30 ?  109 LEU   B H    1 
ATOM   5791 H HA   . LEU   B 1 109 ? 34.711 -24.484 3.964   1.00 16.20 ?  109 LEU   B HA   1 
ATOM   5792 H HB2  . LEU   B 1 109 ? 34.345 -26.792 4.288   1.00 16.57 ?  109 LEU   B HB2  1 
ATOM   5793 H HB3  . LEU   B 1 109 ? 33.021 -26.676 3.433   1.00 16.57 ?  109 LEU   B HB3  1 
ATOM   5794 H HG   . LEU   B 1 109 ? 34.221 -26.361 1.514   1.00 16.10 ?  109 LEU   B HG   1 
ATOM   5795 H HD11 . LEU   B 1 109 ? 36.617 -26.415 1.579   1.00 16.06 ?  109 LEU   B HD11 1 
ATOM   5796 H HD12 . LEU   B 1 109 ? 35.990 -25.084 2.177   1.00 16.06 ?  109 LEU   B HD12 1 
ATOM   5797 H HD13 . LEU   B 1 109 ? 36.515 -26.224 3.152   1.00 16.06 ?  109 LEU   B HD13 1 
ATOM   5798 H HD21 . LEU   B 1 109 ? 35.371 -28.416 1.399   1.00 16.98 ?  109 LEU   B HD21 1 
ATOM   5799 H HD22 . LEU   B 1 109 ? 35.203 -28.562 2.972   1.00 16.98 ?  109 LEU   B HD22 1 
ATOM   5800 H HD23 . LEU   B 1 109 ? 33.922 -28.574 2.033   1.00 16.98 ?  109 LEU   B HD23 1 
ATOM   5801 N N    . LYS   B 1 110 ? 31.715 -24.042 2.933   1.00 12.52 ?  110 LYS   B N    1 
ATOM   5802 C CA   . LYS   B 1 110 ? 30.958 -23.281 1.945   1.00 12.40 ?  110 LYS   B CA   1 
ATOM   5803 C C    . LYS   B 1 110 ? 31.297 -21.793 2.035   1.00 12.30 ?  110 LYS   B C    1 
ATOM   5804 O O    . LYS   B 1 110 ? 31.555 -21.141 1.016   1.00 12.09 ?  110 LYS   B O    1 
ATOM   5805 C CB   . LYS   B 1 110 ? 29.454 -23.529 2.094   1.00 13.25 ?  110 LYS   B CB   1 
ATOM   5806 C CG   . LYS   B 1 110 ? 28.653 -22.918 0.942   1.00 13.41 ?  110 LYS   B CG   1 
ATOM   5807 C CD   . LYS   B 1 110 ? 27.184 -23.350 0.965   1.00 13.61 ?  110 LYS   B CD   1 
ATOM   5808 C CE   . LYS   B 1 110 ? 26.418 -22.817 -0.250  1.00 14.83 ?  110 LYS   B CE   1 
ATOM   5809 N NZ   . LYS   B 1 110 ? 26.752 -23.527 -1.515  1.00 15.10 ?  110 LYS   B NZ   1 
ATOM   5810 H H    . LYS   B 1 110 ? 31.244 -24.430 3.535   1.00 14.99 ?  110 LYS   B H    1 
ATOM   5811 H HA   . LYS   B 1 110 ? 31.215 -23.582 1.061   1.00 14.86 ?  110 LYS   B HA   1 
ATOM   5812 H HB2  . LYS   B 1 110 ? 29.290 -24.485 2.102   1.00 15.88 ?  110 LYS   B HB2  1 
ATOM   5813 H HB3  . LYS   B 1 110 ? 29.144 -23.130 2.921   1.00 15.88 ?  110 LYS   B HB3  1 
ATOM   5814 H HG2  . LYS   B 1 110 ? 28.678 -21.953 1.010   1.00 16.07 ?  110 LYS   B HG2  1 
ATOM   5815 H HG3  . LYS   B 1 110 ? 29.033 -23.206 0.099   1.00 16.07 ?  110 LYS   B HG3  1 
ATOM   5816 H HD2  . LYS   B 1 110 ? 27.132 -24.322 0.953   1.00 16.30 ?  110 LYS   B HD2  1 
ATOM   5817 H HD3  . LYS   B 1 110 ? 26.757 -23.006 1.766   1.00 16.30 ?  110 LYS   B HD3  1 
ATOM   5818 H HE2  . LYS   B 1 110 ? 25.469 -22.918 -0.098  1.00 17.77 ?  110 LYS   B HE2  1 
ATOM   5819 H HE3  . LYS   B 1 110 ? 26.639 -21.879 -0.371  1.00 17.77 ?  110 LYS   B HE3  1 
ATOM   5820 H HZ1  . LYS   B 1 110 ? 26.294 -23.184 -2.193  1.00 18.10 ?  110 LYS   B HZ1  1 
ATOM   5821 H HZ2  . LYS   B 1 110 ? 27.627 -23.446 -1.690  1.00 18.10 ?  110 LYS   B HZ2  1 
ATOM   5822 H HZ3  . LYS   B 1 110 ? 26.560 -24.393 -1.441  1.00 18.10 ?  110 LYS   B HZ3  1 
ATOM   5823 N N    . SER   B 1 111 ? 31.318 -21.244 3.255   1.00 12.60 ?  111 SER   B N    1 
ATOM   5824 C CA   . SER   B 1 111 ? 31.711 -19.848 3.434   1.00 12.42 ?  111 SER   B CA   1 
ATOM   5825 C C    . SER   B 1 111 ? 33.092 -19.591 2.839   1.00 11.52 ?  111 SER   B C    1 
ATOM   5826 O O    . SER   B 1 111 ? 33.322 -18.561 2.188   1.00 12.10 ?  111 SER   B O    1 
ATOM   5827 C CB   . SER   B 1 111 ? 31.713 -19.495 4.920   1.00 13.72 ?  111 SER   B CB   1 
ATOM   5828 O OG   . SER   B 1 111 ? 30.406 -19.492 5.460   1.00 15.19 ?  111 SER   B OG   1 
ATOM   5829 H H    . SER   B 1 111 ? 31.122 -21.660 3.981   1.00 15.10 ?  111 SER   B H    1 
ATOM   5830 H HA   . SER   B 1 111 ? 31.078 -19.276 2.983   1.00 14.88 ?  111 SER   B HA   1 
ATOM   5831 H HB2  . SER   B 1 111 ? 32.243 -20.156 5.400   1.00 16.44 ?  111 SER   B HB2  1 
ATOM   5832 H HB3  . SER   B 1 111 ? 32.105 -18.618 5.035   1.00 16.44 ?  111 SER   B HB3  1 
ATOM   5833 H HG   . SER   B 1 111 ? 30.433 -19.290 6.283   1.00 18.20 ?  111 SER   B HG   1 
ATOM   5834 N N    . ALA   B 1 112 ? 34.028 -20.516 3.054   1.00 11.82 ?  112 ALA   B N    1 
ATOM   5835 C CA   . ALA   B 1 112 ? 35.371 -20.345 2.516   1.00 11.53 ?  112 ALA   B CA   1 
ATOM   5836 C C    . ALA   B 1 112 ? 35.343 -20.256 0.992   1.00 11.11 ?  112 ALA   B C    1 
ATOM   5837 O O    . ALA   B 1 112 ? 35.963 -19.366 0.398   1.00 11.02 ?  112 ALA   B O    1 
ATOM   5838 C CB   . ALA   B 1 112 ? 36.276 -21.479 3.004   1.00 12.05 ?  112 ALA   B CB   1 
ATOM   5839 H H    . ALA   B 1 112 ? 33.912 -21.244 3.505   1.00 14.15 ?  112 ALA   B H    1 
ATOM   5840 H HA   . ALA   B 1 112 ? 35.735 -19.512 2.853   1.00 13.81 ?  112 ALA   B HA   1 
ATOM   5841 H HB1  . ALA   B 1 112 ? 37.168 -21.346 2.643   1.00 14.44 ?  112 ALA   B HB1  1 
ATOM   5842 H HB2  . ALA   B 1 112 ? 36.311 -21.456 3.976   1.00 14.44 ?  112 ALA   B HB2  1 
ATOM   5843 H HB3  . ALA   B 1 112 ? 35.917 -22.324 2.705   1.00 14.44 ?  112 ALA   B HB3  1 
ATOM   5844 N N    . TYR   B 1 113 ? 34.610 -21.158 0.335   1.00 11.20 ?  113 TYR   B N    1 
ATOM   5845 C CA   . TYR   B 1 113 ? 34.537 -21.108 -1.121  1.00 10.88 ?  113 TYR   B CA   1 
ATOM   5846 C C    . TYR   B 1 113 ? 33.833 -19.855 -1.638  1.00 10.62 ?  113 TYR   B C    1 
ATOM   5847 O O    . TYR   B 1 113 ? 34.106 -19.423 -2.763  1.00 10.72 ?  113 TYR   B O    1 
ATOM   5848 C CB   . TYR   B 1 113 ? 33.865 -22.366 -1.666  1.00 11.02 ?  113 TYR   B CB   1 
ATOM   5849 C CG   . TYR   B 1 113 ? 34.826 -23.519 -1.911  1.00 11.49 ?  113 TYR   B CG   1 
ATOM   5850 C CD1  . TYR   B 1 113 ? 35.823 -23.421 -2.874  1.00 11.92 ?  113 TYR   B CD1  1 
ATOM   5851 C CD2  . TYR   B 1 113 ? 34.720 -24.708 -1.205  1.00 11.61 ?  113 TYR   B CD2  1 
ATOM   5852 C CE1  . TYR   B 1 113 ? 36.699 -24.456 -3.111  1.00 11.83 ?  113 TYR   B CE1  1 
ATOM   5853 C CE2  . TYR   B 1 113 ? 35.600 -25.763 -1.440  1.00 11.85 ?  113 TYR   B CE2  1 
ATOM   5854 C CZ   . TYR   B 1 113 ? 36.575 -25.630 -2.403  1.00 12.10 ?  113 TYR   B CZ   1 
ATOM   5855 O OH   . TYR   B 1 113 ? 37.464 -26.641 -2.676  1.00 12.84 ?  113 TYR   B OH   1 
ATOM   5856 H H    . TYR   B 1 113 ? 34.142 -21.783 0.706   1.00 13.42 ?  113 TYR   B H    1 
ATOM   5857 H HA   . TYR   B 1 113 ? 35.438 -21.093 -1.460  1.00 13.04 ?  113 TYR   B HA   1 
ATOM   5858 H HB2  . TYR   B 1 113 ? 33.197 -22.674 -1.027  1.00 13.20 ?  113 TYR   B HB2  1 
ATOM   5859 H HB3  . TYR   B 1 113 ? 33.433 -22.154 -2.508  1.00 13.20 ?  113 TYR   B HB3  1 
ATOM   5860 H HD1  . TYR   B 1 113 ? 35.909 -22.629 -3.359  1.00 14.28 ?  113 TYR   B HD1  1 
ATOM   5861 H HD2  . TYR   B 1 113 ? 34.053 -24.801 -0.563  1.00 13.91 ?  113 TYR   B HD2  1 
ATOM   5862 H HE1  . TYR   B 1 113 ? 37.362 -24.369 -3.761  1.00 14.17 ?  113 TYR   B HE1  1 
ATOM   5863 H HE2  . TYR   B 1 113 ? 35.517 -26.559 -0.965  1.00 14.20 ?  113 TYR   B HE2  1 
ATOM   5864 H HH   . TYR   B 1 113 ? 37.293 -27.311 -2.195  1.00 15.39 ?  113 TYR   B HH   1 
ATOM   5865 N N    . GLU   B 1 114 ? 32.906 -19.281 -0.865  1.00 10.65 ?  114 GLU   B N    1 
ATOM   5866 C CA   . GLU   B 1 114 ? 32.226 -18.069 -1.318  1.00 10.52 ?  114 GLU   B CA   1 
ATOM   5867 C C    . GLU   B 1 114 ? 33.214 -16.947 -1.614  1.00 10.45 ?  114 GLU   B C    1 
ATOM   5868 O O    . GLU   B 1 114 ? 32.942 -16.088 -2.456  1.00 10.94 ?  114 GLU   B O    1 
ATOM   5869 C CB   . GLU   B 1 114 ? 31.170 -17.638 -0.295  1.00 11.07 ?  114 GLU   B CB   1 
ATOM   5870 C CG   . GLU   B 1 114 ? 29.946 -18.553 -0.364  1.00 11.34 ?  114 GLU   B CG   1 
ATOM   5871 C CD   . GLU   B 1 114 ? 28.925 -18.369 0.743   1.00 11.56 ?  114 GLU   B CD   1 
ATOM   5872 O OE1  . GLU   B 1 114 ? 29.213 -17.748 1.786   1.00 11.83 ?  114 GLU   B OE1  1 
ATOM   5873 O OE2  . GLU   B 1 114 ? 27.803 -18.908 0.573   1.00 12.56 -1 114 GLU   B OE2  1 
ATOM   5874 H H    . GLU   B 1 114 ? 32.645 -19.579 -0.099  1.00 12.76 ?  114 GLU   B H    1 
ATOM   5875 H HA   . GLU   B 1 114 ? 31.760 -18.268 -2.144  1.00 12.60 ?  114 GLU   B HA   1 
ATOM   5876 H HB2  . GLU   B 1 114 ? 31.544 -17.698 0.600   1.00 13.26 ?  114 GLU   B HB2  1 
ATOM   5877 H HB3  . GLU   B 1 114 ? 30.886 -16.733 -0.483  1.00 13.26 ?  114 GLU   B HB3  1 
ATOM   5878 H HG2  . GLU   B 1 114 ? 29.494 -18.389 -1.204  1.00 13.59 ?  114 GLU   B HG2  1 
ATOM   5879 H HG3  . GLU   B 1 114 ? 30.252 -19.473 -0.333  1.00 13.59 ?  114 GLU   B HG3  1 
ATOM   5880 N N    . ASN   B 1 115 ? 34.384 -16.947 -0.967  1.00 10.38 ?  115 ASN   B N    1 
ATOM   5881 C CA   . ASN   B 1 115 ? 35.374 -15.914 -1.259  1.00 10.31 ?  115 ASN   B CA   1 
ATOM   5882 C C    . ASN   B 1 115 ? 35.792 -15.939 -2.722  1.00 10.20 ?  115 ASN   B C    1 
ATOM   5883 O O    . ASN   B 1 115 ? 36.173 -14.899 -3.278  1.00 10.82 ?  115 ASN   B O    1 
ATOM   5884 C CB   . ASN   B 1 115 ? 36.613 -16.081 -0.368  1.00 11.05 ?  115 ASN   B CB   1 
ATOM   5885 C CG   . ASN   B 1 115 ? 36.332 -15.820 1.093   1.00 11.11 ?  115 ASN   B CG   1 
ATOM   5886 O OD1  . ASN   B 1 115 ? 36.329 -14.675 1.534   1.00 13.31 ?  115 ASN   B OD1  1 
ATOM   5887 N ND2  . ASN   B 1 115 ? 36.163 -16.885 1.872   1.00 11.36 ?  115 ASN   B ND2  1 
ATOM   5888 H H    . ASN   B 1 115 ? 34.618 -17.514 -0.359  1.00 12.44 ?  115 ASN   B H    1 
ATOM   5889 H HA   . ASN   B 1 115 ? 34.990 -15.043 -1.075  1.00 12.35 ?  115 ASN   B HA   1 
ATOM   5890 H HB2  . ASN   B 1 115 ? 36.946 -16.984 -0.454  1.00 13.23 ?  115 ASN   B HB2  1 
ATOM   5891 H HB3  . ASN   B 1 115 ? 37.293 -15.447 -0.654  1.00 13.23 ?  115 ASN   B HB3  1 
ATOM   5892 H HD21 . ASN   B 1 115 ? 36.016 -16.782 2.716   1.00 13.61 ?  115 ASN   B HD21 1 
ATOM   5893 H HD22 . ASN   B 1 115 ? 36.193 -17.673 1.536   1.00 13.61 ?  115 ASN   B HD22 1 
ATOM   5894 N N    . PHE   B 1 116 ? 35.761 -17.117 -3.354  1.00 10.14 ?  116 PHE   B N    1 
ATOM   5895 C CA   . PHE   B 1 116 ? 36.197 -17.213 -4.742  1.00 10.11 ?  116 PHE   B CA   1 
ATOM   5896 C C    . PHE   B 1 116 ? 35.299 -16.385 -5.660  1.00 9.97  ?  116 PHE   B C    1 
ATOM   5897 O O    . PHE   B 1 116 ? 35.739 -15.958 -6.733  1.00 10.63 ?  116 PHE   B O    1 
ATOM   5898 C CB   . PHE   B 1 116 ? 36.164 -18.660 -5.264  1.00 9.77  ?  116 PHE   B CB   1 
ATOM   5899 C CG   . PHE   B 1 116 ? 37.229 -19.618 -4.709  1.00 9.93  ?  116 PHE   B CG   1 
ATOM   5900 C CD1  . PHE   B 1 116 ? 37.868 -19.437 -3.495  1.00 10.71 ?  116 PHE   B CD1  1 
ATOM   5901 C CD2  . PHE   B 1 116 ? 37.537 -20.754 -5.445  1.00 10.36 ?  116 PHE   B CD2  1 
ATOM   5902 C CE1  . PHE   B 1 116 ? 38.793 -20.382 -3.036  1.00 11.06 ?  116 PHE   B CE1  1 
ATOM   5903 C CE2  . PHE   B 1 116 ? 38.456 -21.691 -5.000  1.00 10.26 ?  116 PHE   B CE2  1 
ATOM   5904 C CZ   . PHE   B 1 116 ? 39.081 -21.511 -3.798  1.00 10.30 ?  116 PHE   B CZ   1 
ATOM   5905 H H    . PHE   B 1 116 ? 35.488 -17.862 -3.007  1.00 12.14 ?  116 PHE   B H    1 
ATOM   5906 H HA   . PHE   B 1 116 ? 37.100 -16.887 -4.819  1.00 12.11 ?  116 PHE   B HA   1 
ATOM   5907 H HB2  . PHE   B 1 116 ? 35.288 -19.040 -5.052  1.00 11.70 ?  116 PHE   B HB2  1 
ATOM   5908 H HB3  . PHE   B 1 116 ? 36.266 -18.638 -6.228  1.00 11.70 ?  116 PHE   B HB3  1 
ATOM   5909 H HD1  . PHE   B 1 116 ? 37.659 -18.689 -2.972  1.00 12.83 ?  116 PHE   B HD1  1 
ATOM   5910 H HD2  . PHE   B 1 116 ? 37.103 -20.899 -6.256  1.00 12.40 ?  116 PHE   B HD2  1 
ATOM   5911 H HE1  . PHE   B 1 116 ? 39.219 -20.248 -2.220  1.00 13.25 ?  116 PHE   B HE1  1 
ATOM   5912 H HE2  . PHE   B 1 116 ? 38.643 -22.438 -5.516  1.00 12.29 ?  116 PHE   B HE2  1 
ATOM   5913 H HZ   . PHE   B 1 116 ? 39.707 -22.121 -3.495  1.00 12.34 ?  116 PHE   B HZ   1 
ATOM   5914 N N    . ASN   B 1 117 ? 34.029 -16.184 -5.284  1.00 10.48 ?  117 ASN   B N    1 
ATOM   5915 C CA   . ASN   B 1 117 ? 33.087 -15.485 -6.158  1.00 10.85 ?  117 ASN   B CA   1 
ATOM   5916 C C    . ASN   B 1 117 ? 33.405 -14.008 -6.307  1.00 11.19 ?  117 ASN   B C    1 
ATOM   5917 O O    . ASN   B 1 117 ? 32.806 -13.353 -7.161  1.00 12.12 ?  117 ASN   B O    1 
ATOM   5918 C CB   . ASN   B 1 117 ? 31.661 -15.697 -5.669  1.00 10.98 ?  117 ASN   B CB   1 
ATOM   5919 C CG   . ASN   B 1 117 ? 31.205 -17.107 -5.913  1.00 11.24 ?  117 ASN   B CG   1 
ATOM   5920 O OD1  . ASN   B 1 117 ? 31.564 -17.702 -6.927  1.00 12.18 ?  117 ASN   B OD1  1 
ATOM   5921 N ND2  . ASN   B 1 117 ? 30.463 -17.674 -4.973  1.00 11.16 ?  117 ASN   B ND2  1 
ATOM   5922 H H    . ASN   B 1 117 ? 33.694 -16.439 -4.531  1.00 12.56 ?  117 ASN   B H    1 
ATOM   5923 H HA   . ASN   B 1 117 ? 33.147 -15.878 -7.037  1.00 13.00 ?  117 ASN   B HA   1 
ATOM   5924 H HB2  . ASN   B 1 117 ? 31.616 -15.521 -4.712  1.00 13.15 ?  117 ASN   B HB2  1 
ATOM   5925 H HB3  . ASN   B 1 117 ? 31.066 -15.088 -6.142  1.00 13.15 ?  117 ASN   B HB3  1 
ATOM   5926 H HD21 . ASN   B 1 117 ? 30.178 -18.479 -5.076  1.00 13.37 ?  117 ASN   B HD21 1 
ATOM   5927 H HD22 . ASN   B 1 117 ? 30.234 -17.226 -4.273  1.00 13.37 ?  117 ASN   B HD22 1 
ATOM   5928 N N    . GLN   B 1 118 ? 34.340 -13.482 -5.524  1.00 10.67 ?  118 GLN   B N    1 
ATOM   5929 C CA   . GLN   B 1 118 ? 34.769 -12.095 -5.656  1.00 11.35 ?  118 GLN   B CA   1 
ATOM   5930 C C    . GLN   B 1 118 ? 35.837 -11.904 -6.727  1.00 11.31 ?  118 GLN   B C    1 
ATOM   5931 O O    . GLN   B 1 118 ? 36.312 -10.776 -6.912  1.00 12.86 ?  118 GLN   B O    1 
ATOM   5932 C CB   . GLN   B 1 118 ? 35.249 -11.565 -4.298  1.00 11.89 ?  118 GLN   B CB   1 
ATOM   5933 C CG   . GLN   B 1 118 ? 34.163 -11.603 -3.230  1.00 11.99 ?  118 GLN   B CG   1 
ATOM   5934 C CD   . GLN   B 1 118 ? 33.000 -10.688 -3.558  1.00 11.95 ?  118 GLN   B CD   1 
ATOM   5935 O OE1  . GLN   B 1 118 ? 33.197 -9.548  -3.989  1.00 12.64 ?  118 GLN   B OE1  1 
ATOM   5936 N NE2  . GLN   B 1 118 ? 31.784 -11.182 -3.375  1.00 12.28 ?  118 GLN   B NE2  1 
ATOM   5937 H H    . GLN   B 1 118 ? 34.756 -13.909 -4.902  1.00 12.78 ?  118 GLN   B H    1 
ATOM   5938 H HA   . GLN   B 1 118 ? 34.007 -11.561 -5.921  1.00 13.60 ?  118 GLN   B HA   1 
ATOM   5939 H HB2  . GLN   B 1 118 ? 35.994 -12.101 -3.989  1.00 14.24 ?  118 GLN   B HB2  1 
ATOM   5940 H HB3  . GLN   B 1 118 ? 35.531 -10.637 -4.399  1.00 14.24 ?  118 GLN   B HB3  1 
ATOM   5941 H HG2  . GLN   B 1 118 ? 33.824 -12.511 -3.158  1.00 14.36 ?  118 GLN   B HG2  1 
ATOM   5942 H HG3  . GLN   B 1 118 ? 34.539 -11.321 -2.382  1.00 14.36 ?  118 GLN   B HG3  1 
ATOM   5943 H HE21 . GLN   B 1 118 ? 31.685 -11.981 -3.071  1.00 14.71 ?  118 GLN   B HE21 1 
ATOM   5944 H HE22 . GLN   B 1 118 ? 31.097 -10.701 -3.554  1.00 14.71 ?  118 GLN   B HE22 1 
ATOM   5945 N N    . HIS   B 1 119 ? 36.187 -12.964 -7.459  1.00 10.67 ?  119 HIS   B N    1 
ATOM   5946 C CA   . HIS   B 1 119 ? 37.236 -12.920 -8.469  1.00 10.95 ?  119 HIS   B CA   1 
ATOM   5947 C C    . HIS   B 1 119 ? 36.756 -13.651 -9.712  1.00 10.86 ?  119 HIS   B C    1 
ATOM   5948 O O    . HIS   B 1 119 ? 36.246 -14.766 -9.613  1.00 11.91 ?  119 HIS   B O    1 
ATOM   5949 C CB   . HIS   B 1 119 ? 38.508 -13.560 -7.913  1.00 11.54 ?  119 HIS   B CB   1 
ATOM   5950 C CG   . HIS   B 1 119 ? 38.992 -12.866 -6.690  1.00 12.71 ?  119 HIS   B CG   1 
ATOM   5951 N ND1  . HIS   B 1 119 ? 39.798 -11.749 -6.748  1.00 14.57 ?  119 HIS   B ND1  1 
ATOM   5952 C CD2  . HIS   B 1 119 ? 38.706 -13.061 -5.383  1.00 13.90 ?  119 HIS   B CD2  1 
ATOM   5953 C CE1  . HIS   B 1 119 ? 40.014 -11.307 -5.524  1.00 15.61 ?  119 HIS   B CE1  1 
ATOM   5954 N NE2  . HIS   B 1 119 ? 39.360 -12.082 -4.677  1.00 15.40 ?  119 HIS   B NE2  1 
ATOM   5955 H H    . HIS   B 1 119 ? 35.806 -13.739 -7.396  1.00 12.79 ?  119 HIS   B H    1 
ATOM   5956 H HA   . HIS   B 1 119 ? 37.421 -11.996 -8.704  1.00 13.11 ?  119 HIS   B HA   1 
ATOM   5957 H HB2  . HIS   B 1 119 ? 38.329 -14.484 -7.685  1.00 13.83 ?  119 HIS   B HB2  1 
ATOM   5958 H HB3  . HIS   B 1 119 ? 39.208 -13.511 -8.585  1.00 13.83 ?  119 HIS   B HB3  1 
ATOM   5959 H HD2  . HIS   B 1 119 ? 38.177 -13.735 -5.024  1.00 16.66 ?  119 HIS   B HD2  1 
ATOM   5960 H HE1  . HIS   B 1 119 ? 40.551 -10.580 -5.291  1.00 18.70 ?  119 HIS   B HE1  1 
ATOM   5961 H HE2  . HIS   B 1 119 ? 39.371 -12.001 -3.816  1.00 18.45 ?  119 HIS   B HE2  1 
ATOM   5962 N N    . GLU   B 1 120 ? 36.913 -13.028 -10.881 1.00 11.85 ?  120 GLU   B N    1 
ATOM   5963 C CA   . GLU   B 1 120 ? 36.319 -13.606 -12.082 1.00 12.89 ?  120 GLU   B CA   1 
ATOM   5964 C C    . GLU   B 1 120 ? 36.993 -14.904 -12.505 1.00 11.81 ?  120 GLU   B C    1 
ATOM   5965 O O    . GLU   B 1 120 ? 36.330 -15.775 -13.084 1.00 12.47 ?  120 GLU   B O    1 
ATOM   5966 C CB   . GLU   B 1 120 ? 36.317 -12.590 -13.223 1.00 17.52 ?  120 GLU   B CB   1 
ATOM   5967 C CG   . GLU   B 1 120 ? 35.310 -11.475 -13.010 1.00 23.82 ?  120 GLU   B CG   1 
ATOM   5968 C CD   . GLU   B 1 120 ? 35.138 -10.580 -14.219 1.00 29.31 ?  120 GLU   B CD   1 
ATOM   5969 O OE1  . GLU   B 1 120 ? 36.144 -10.289 -14.899 1.00 31.14 ?  120 GLU   B OE1  1 
ATOM   5970 O OE2  . GLU   B 1 120 ? 33.990 -10.164 -14.481 1.00 31.95 -1 120 GLU   B OE2  1 
ATOM   5971 H H    . GLU   B 1 120 ? 37.343 -12.289 -11.004 1.00 14.19 ?  120 GLU   B H    1 
ATOM   5972 H HA   . GLU   B 1 120 ? 35.396 -13.818 -11.889 1.00 15.44 ?  120 GLU   B HA   1 
ATOM   5973 H HB2  . GLU   B 1 120 ? 37.193 -12.190 -13.299 1.00 21.00 ?  120 GLU   B HB2  1 
ATOM   5974 H HB3  . GLU   B 1 120 ? 36.086 -13.046 -14.052 1.00 21.00 ?  120 GLU   B HB3  1 
ATOM   5975 H HG2  . GLU   B 1 120 ? 34.443 -11.863 -12.807 1.00 28.56 ?  120 GLU   B HG2  1 
ATOM   5976 H HG3  . GLU   B 1 120 ? 35.604 -10.916 -12.279 1.00 28.56 ?  120 GLU   B HG3  1 
ATOM   5977 N N    . VAL   B 1 121 ? 38.291 -15.053 -12.242 1.00 11.62 ?  121 VAL   B N    1 
ATOM   5978 C CA   . VAL   B 1 121 ? 39.034 -16.264 -12.590 1.00 11.05 ?  121 VAL   B CA   1 
ATOM   5979 C C    . VAL   B 1 121 ? 40.148 -16.471 -11.570 1.00 10.95 ?  121 VAL   B C    1 
ATOM   5980 O O    . VAL   B 1 121 ? 40.826 -15.518 -11.175 1.00 11.68 ?  121 VAL   B O    1 
ATOM   5981 C CB   . VAL   B 1 121 ? 39.545 -16.221 -14.048 1.00 13.12 ?  121 VAL   B CB   1 
ATOM   5982 C CG1  . VAL   B 1 121 ? 40.399 -14.980 -14.303 1.00 14.64 ?  121 VAL   B CG1  1 
ATOM   5983 C CG2  . VAL   B 1 121 ? 40.294 -17.502 -14.405 1.00 14.78 ?  121 VAL   B CG2  1 
ATOM   5984 H H    . VAL   B 1 121 ? 38.777 -14.452 -11.861 1.00 13.92 ?  121 VAL   B H    1 
ATOM   5985 H HA   . VAL   B 1 121 ? 38.425 -17.017 -12.518 1.00 13.24 ?  121 VAL   B HA   1 
ATOM   5986 H HB   . VAL   B 1 121 ? 38.771 -16.167 -14.637 1.00 15.72 ?  121 VAL   B HB   1 
ATOM   5987 H HG11 . VAL   B 1 121 ? 40.714 -14.998 -15.220 1.00 17.55 ?  121 VAL   B HG11 1 
ATOM   5988 H HG12 . VAL   B 1 121 ? 39.855 -14.187 -14.158 1.00 17.55 ?  121 VAL   B HG12 1 
ATOM   5989 H HG13 . VAL   B 1 121 ? 41.149 -14.983 -13.693 1.00 17.55 ?  121 VAL   B HG13 1 
ATOM   5990 H HG21 . VAL   B 1 121 ? 40.496 -17.495 -15.356 1.00 17.71 ?  121 VAL   B HG21 1 
ATOM   5991 H HG22 . VAL   B 1 121 ? 41.118 -17.540 -13.895 1.00 17.71 ?  121 VAL   B HG22 1 
ATOM   5992 H HG23 . VAL   B 1 121 ? 39.737 -18.268 -14.194 1.00 17.71 ?  121 VAL   B HG23 1 
ATOM   5993 N N    . LEU   B 1 122 ? 40.331 -17.723 -11.142 1.00 10.61 ?  122 LEU   B N    1 
ATOM   5994 C CA   . LEU   B 1 122 ? 41.306 -18.076 -10.114 1.00 10.23 ?  122 LEU   B CA   1 
ATOM   5995 C C    . LEU   B 1 122 ? 41.959 -19.408 -10.439 1.00 10.07 ?  122 LEU   B C    1 
ATOM   5996 O O    . LEU   B 1 122 ? 41.298 -20.330 -10.934 1.00 11.23 ?  122 LEU   B O    1 
ATOM   5997 C CB   . LEU   B 1 122 ? 40.647 -18.313 -8.741  1.00 12.10 ?  122 LEU   B CB   1 
ATOM   5998 C CG   . LEU   B 1 122 ? 39.621 -17.287 -8.261  1.00 12.13 ?  122 LEU   B CG   1 
ATOM   5999 C CD1  . LEU   B 1 122 ? 38.236 -17.664 -8.743  1.00 12.50 ?  122 LEU   B CD1  1 
ATOM   6000 C CD2  . LEU   B 1 122 ? 39.651 -17.172 -6.748  1.00 11.59 ?  122 LEU   B CD2  1 
ATOM   6001 H H    . LEU   B 1 122 ? 39.901 -18.405 -11.443 1.00 12.70 ?  122 LEU   B H    1 
ATOM   6002 H HA   . LEU   B 1 122 ? 41.984 -17.385 -10.028 1.00 12.25 ?  122 LEU   B HA   1 
ATOM   6003 H HB2  . LEU   B 1 122 ? 40.197 -19.169 -8.769  1.00 14.50 ?  122 LEU   B HB2  1 
ATOM   6004 H HB3  . LEU   B 1 122 ? 41.347 -18.340 -8.071  1.00 14.50 ?  122 LEU   B HB3  1 
ATOM   6005 H HG   . LEU   B 1 122 ? 39.840 -16.418 -8.633  1.00 14.54 ?  122 LEU   B HG   1 
ATOM   6006 H HD11 . LEU   B 1 122 ? 37.598 -17.017 -8.406  1.00 14.97 ?  122 LEU   B HD11 1 
ATOM   6007 H HD12 . LEU   B 1 122 ? 38.227 -17.661 -9.714  1.00 14.97 ?  122 LEU   B HD12 1 
ATOM   6008 H HD13 . LEU   B 1 122 ? 38.017 -18.549 -8.414  1.00 14.97 ?  122 LEU   B HD13 1 
ATOM   6009 H HD21 . LEU   B 1 122 ? 38.974 -16.538 -6.462  1.00 13.88 ?  122 LEU   B HD21 1 
ATOM   6010 H HD22 . LEU   B 1 122 ? 39.475 -18.042 -6.358  1.00 13.88 ?  122 LEU   B HD22 1 
ATOM   6011 H HD23 . LEU   B 1 122 ? 40.530 -16.859 -6.472  1.00 13.88 ?  122 LEU   B HD23 1 
ATOM   6012 N N    . LEU   B 1 123 ? 43.243 -19.516 -10.081 1.00 9.60  ?  123 LEU   B N    1 
ATOM   6013 C CA   . LEU   B 1 123 ? 43.955 -20.787 -9.956  1.00 10.08 ?  123 LEU   B CA   1 
ATOM   6014 C C    . LEU   B 1 123 ? 43.927 -21.184 -8.482  1.00 9.73  ?  123 LEU   B C    1 
ATOM   6015 O O    . LEU   B 1 123 ? 44.281 -20.356 -7.631  1.00 10.07 ?  123 LEU   B O    1 
ATOM   6016 C CB   . LEU   B 1 123 ? 45.408 -20.605 -10.408 1.00 10.44 ?  123 LEU   B CB   1 
ATOM   6017 C CG   . LEU   B 1 123 ? 46.347 -21.793 -10.172 1.00 10.72 ?  123 LEU   B CG   1 
ATOM   6018 C CD1  . LEU   B 1 123 ? 45.912 -23.043 -10.941 1.00 11.53 ?  123 LEU   B CD1  1 
ATOM   6019 C CD2  . LEU   B 1 123 ? 47.763 -21.407 -10.542 1.00 11.77 ?  123 LEU   B CD2  1 
ATOM   6020 H H    . LEU   B 1 123 ? 43.738 -18.838 -9.874  1.00 11.50 ?  123 LEU   B H    1 
ATOM   6021 H HA   . LEU   B 1 123 ? 43.524 -21.474 -10.484 1.00 12.07 ?  123 LEU   B HA   1 
ATOM   6022 H HB2  . LEU   B 1 123 ? 45.403 -20.423 -11.361 1.00 12.50 ?  123 LEU   B HB2  1 
ATOM   6023 H HB3  . LEU   B 1 123 ? 45.780 -19.845 -9.936  1.00 12.50 ?  123 LEU   B HB3  1 
ATOM   6024 H HG   . LEU   B 1 123 ? 46.340 -22.017 -9.229  1.00 12.84 ?  123 LEU   B HG   1 
ATOM   6025 H HD11 . LEU   B 1 123 ? 46.547 -23.755 -10.769 1.00 13.81 ?  123 LEU   B HD11 1 
ATOM   6026 H HD12 . LEU   B 1 123 ? 45.027 -23.309 -10.639 1.00 13.81 ?  123 LEU   B HD12 1 
ATOM   6027 H HD13 . LEU   B 1 123 ? 45.889 -22.839 -11.888 1.00 13.81 ?  123 LEU   B HD13 1 
ATOM   6028 H HD21 . LEU   B 1 123 ? 48.346 -22.167 -10.393 1.00 14.10 ?  123 LEU   B HD21 1 
ATOM   6029 H HD22 . LEU   B 1 123 ? 47.785 -21.154 -11.480 1.00 14.10 ?  123 LEU   B HD22 1 
ATOM   6030 H HD23 . LEU   B 1 123 ? 48.040 -20.661 -9.991  1.00 14.10 ?  123 LEU   B HD23 1 
ATOM   6031 N N    . ALA   B 1 124 ? 43.493 -22.413 -8.168  1.00 9.49  ?  124 ALA   B N    1 
ATOM   6032 C CA   . ALA   B 1 124 ? 43.232 -22.722 -6.769  1.00 9.80  ?  124 ALA   B CA   1 
ATOM   6033 C C    . ALA   B 1 124 ? 43.505 -24.182 -6.447  1.00 9.46  ?  124 ALA   B C    1 
ATOM   6034 O O    . ALA   B 1 124 ? 43.358 -25.058 -7.311  1.00 10.11 ?  124 ALA   B O    1 
ATOM   6035 C CB   . ALA   B 1 124 ? 41.779 -22.416 -6.398  1.00 10.24 ?  124 ALA   B CB   1 
ATOM   6036 H H    . ALA   B 1 124 ? 43.329 -23.051 -8.730  1.00 11.36 ?  124 ALA   B H    1 
ATOM   6037 H HA   . ALA   B 1 124 ? 43.809 -22.176 -6.225  1.00 11.73 ?  124 ALA   B HA   1 
ATOM   6038 H HB1  . ALA   B 1 124 ? 41.633 -22.634 -5.464  1.00 12.26 ?  124 ALA   B HB1  1 
ATOM   6039 H HB2  . ALA   B 1 124 ? 41.610 -21.470 -6.545  1.00 12.26 ?  124 ALA   B HB2  1 
ATOM   6040 H HB3  . ALA   B 1 124 ? 41.185 -22.944 -6.956  1.00 12.26 ?  124 ALA   B HB3  1 
ATOM   6041 N N    . PRO   B 1 125 ? 43.802 -24.479 -5.185  1.00 9.73  ?  125 PRO   B N    1 
ATOM   6042 C CA   . PRO   B 1 125 ? 43.730 -25.845 -4.666  1.00 10.56 ?  125 PRO   B CA   1 
ATOM   6043 C C    . PRO   B 1 125 ? 42.326 -26.114 -4.123  1.00 10.62 ?  125 PRO   B C    1 
ATOM   6044 O O    . PRO   B 1 125 ? 41.533 -25.195 -3.912  1.00 10.93 ?  125 PRO   B O    1 
ATOM   6045 C CB   . PRO   B 1 125 ? 44.720 -25.784 -3.496  1.00 11.79 ?  125 PRO   B CB   1 
ATOM   6046 C CG   . PRO   B 1 125 ? 44.477 -24.380 -2.919  1.00 11.56 ?  125 PRO   B CG   1 
ATOM   6047 C CD   . PRO   B 1 125 ? 44.119 -23.512 -4.121  1.00 10.68 ?  125 PRO   B CD   1 
ATOM   6048 H HA   . PRO   B 1 125 ? 44.000 -26.512 -5.320  1.00 12.64 ?  125 PRO   B HA   1 
ATOM   6049 H HB2  . PRO   B 1 125 ? 44.508 -26.475 -2.842  1.00 14.13 ?  125 PRO   B HB2  1 
ATOM   6050 H HB3  . PRO   B 1 125 ? 45.630 -25.881 -3.818  1.00 14.13 ?  125 PRO   B HB3  1 
ATOM   6051 H HG2  . PRO   B 1 125 ? 43.741 -24.402 -2.283  1.00 13.85 ?  125 PRO   B HG2  1 
ATOM   6052 H HG3  . PRO   B 1 125 ? 45.286 -24.054 -2.484  1.00 13.85 ?  125 PRO   B HG3  1 
ATOM   6053 H HD2  . PRO   B 1 125 ? 43.350 -22.961 -3.924  1.00 12.79 ?  125 PRO   B HD2  1 
ATOM   6054 H HD3  . PRO   B 1 125 ? 44.888 -22.965 -4.374  1.00 12.79 ?  125 PRO   B HD3  1 
ATOM   6055 N N    . LEU   B 1 126 ? 42.054 -27.390 -3.834  1.00 11.24 ?  126 LEU   B N    1 
ATOM   6056 C CA   . LEU   B 1 126 ? 40.836 -27.752 -3.113  1.00 11.84 ?  126 LEU   B CA   1 
ATOM   6057 C C    . LEU   B 1 126 ? 40.953 -27.349 -1.650  1.00 11.99 ?  126 LEU   B C    1 
ATOM   6058 O O    . LEU   B 1 126 ? 41.845 -27.810 -0.932  1.00 14.06 ?  126 LEU   B O    1 
ATOM   6059 C CB   . LEU   B 1 126 ? 40.571 -29.245 -3.221  1.00 13.22 ?  126 LEU   B CB   1 
ATOM   6060 C CG   . LEU   B 1 126 ? 40.045 -29.745 -4.568  1.00 14.11 ?  126 LEU   B CG   1 
ATOM   6061 C CD1  . LEU   B 1 126 ? 40.081 -31.255 -4.612  1.00 15.70 ?  126 LEU   B CD1  1 
ATOM   6062 C CD2  . LEU   B 1 126 ? 38.635 -29.237 -4.848  1.00 14.22 ?  126 LEU   B CD2  1 
ATOM   6063 H H    . LEU   B 1 126 ? 42.559 -28.059 -4.037  1.00 13.47 ?  126 LEU   B H    1 
ATOM   6064 H HA   . LEU   B 1 126 ? 40.087 -27.272 -3.502  1.00 14.18 ?  126 LEU   B HA   1 
ATOM   6065 H HB2  . LEU   B 1 126 ? 41.398 -29.711 -3.043  1.00 15.84 ?  126 LEU   B HB2  1 
ATOM   6066 H HB3  . LEU   B 1 126 ? 39.911 -29.480 -2.552  1.00 15.84 ?  126 LEU   B HB3  1 
ATOM   6067 H HG   . LEU   B 1 126 ? 40.627 -29.412 -5.273  1.00 16.91 ?  126 LEU   B HG   1 
ATOM   6068 H HD11 . LEU   B 1 126 ? 39.741 -31.553 -5.469  1.00 18.81 ?  126 LEU   B HD11 1 
ATOM   6069 H HD12 . LEU   B 1 126 ? 40.993 -31.554 -4.490  1.00 18.81 ?  126 LEU   B HD12 1 
ATOM   6070 H HD13 . LEU   B 1 126 ? 39.520 -31.600 -3.896  1.00 18.81 ?  126 LEU   B HD13 1 
ATOM   6071 H HD21 . LEU   B 1 126 ? 38.307 -29.647 -5.666  1.00 17.03 ?  126 LEU   B HD21 1 
ATOM   6072 H HD22 . LEU   B 1 126 ? 38.059 -29.475 -4.106  1.00 17.03 ?  126 LEU   B HD22 1 
ATOM   6073 H HD23 . LEU   B 1 126 ? 38.656 -28.271 -4.953  1.00 17.03 ?  126 LEU   B HD23 1 
ATOM   6074 N N    . LEU   B 1 127 ? 40.019 -26.527 -1.192  1.00 11.96 ?  127 LEU   B N    1 
ATOM   6075 C CA   . LEU   B 1 127 ? 40.075 -26.034 0.171   1.00 12.46 ?  127 LEU   B CA   1 
ATOM   6076 C C    . LEU   B 1 127 ? 39.799 -27.150 1.166   1.00 12.01 ?  127 LEU   B C    1 
ATOM   6077 O O    . LEU   B 1 127 ? 38.973 -28.041 0.944   1.00 12.46 ?  127 LEU   B O    1 
ATOM   6078 C CB   . LEU   B 1 127 ? 39.058 -24.914 0.381   1.00 13.01 ?  127 LEU   B CB   1 
ATOM   6079 C CG   . LEU   B 1 127 ? 39.244 -23.652 -0.459  1.00 13.39 ?  127 LEU   B CG   1 
ATOM   6080 C CD1  . LEU   B 1 127 ? 38.135 -22.671 -0.123  1.00 13.84 ?  127 LEU   B CD1  1 
ATOM   6081 C CD2  . LEU   B 1 127 ? 40.624 -23.024 -0.233  1.00 13.94 ?  127 LEU   B CD2  1 
ATOM   6082 H H    . LEU   B 1 127 ? 39.347 -26.230 -1.651  1.00 14.32 ?  127 LEU   B H    1 
ATOM   6083 H HA   . LEU   B 1 127 ? 40.960 -25.674 0.346   1.00 14.92 ?  127 LEU   B HA   1 
ATOM   6084 H HB2  . LEU   B 1 127 ? 38.174 -25.263 0.178   1.00 15.59 ?  127 LEU   B HB2  1 
ATOM   6085 H HB3  . LEU   B 1 127 ? 39.087 -24.644 1.312   1.00 15.59 ?  127 LEU   B HB3  1 
ATOM   6086 H HG   . LEU   B 1 127 ? 39.161 -23.876 -1.397  1.00 16.05 ?  127 LEU   B HG   1 
ATOM   6087 H HD11 . LEU   B 1 127 ? 38.262 -21.856 -0.645  1.00 16.58 ?  127 LEU   B HD11 1 
ATOM   6088 H HD12 . LEU   B 1 127 ? 37.279 -23.065 -0.333  1.00 16.58 ?  127 LEU   B HD12 1 
ATOM   6089 H HD13 . LEU   B 1 127 ? 38.179 -22.454 0.825   1.00 16.58 ?  127 LEU   B HD13 1 
ATOM   6090 H HD21 . LEU   B 1 127 ? 40.663 -22.167 -0.684  1.00 16.71 ?  127 LEU   B HD21 1 
ATOM   6091 H HD22 . LEU   B 1 127 ? 40.764 -22.902 0.720   1.00 16.71 ?  127 LEU   B HD22 1 
ATOM   6092 H HD23 . LEU   B 1 127 ? 41.302 -23.618 -0.592  1.00 16.71 ?  127 LEU   B HD23 1 
ATOM   6093 N N    . SER   B 1 128 ? 40.480 -27.065 2.296   1.00 12.12 ?  128 SER   B N    1 
ATOM   6094 C CA   . SER   B 1 128 ? 40.361 -27.979 3.419   1.00 12.72 ?  128 SER   B CA   1 
ATOM   6095 C C    . SER   B 1 128 ? 40.854 -29.389 3.099   1.00 14.08 ?  128 SER   B C    1 
ATOM   6096 O O    . SER   B 1 128 ? 40.753 -30.268 3.954   1.00 15.62 ?  128 SER   B O    1 
ATOM   6097 C CB   . SER   B 1 128 ? 38.952 -27.978 4.035   1.00 13.03 ?  128 SER   B CB   1 
ATOM   6098 O OG   . SER   B 1 128 ? 38.646 -26.702 4.596   1.00 13.78 ?  128 SER   B OG   1 
ATOM   6099 H H    . SER   B 1 128 ? 41.042 -26.434 2.445   1.00 14.52 ?  128 SER   B H    1 
ATOM   6100 H HA   . SER   B 1 128 ? 40.943 -27.643 4.106   1.00 15.24 ?  128 SER   B HA   1 
ATOM   6101 H HB2  . SER   B 1 128 ? 38.296 -28.202 3.355   1.00 15.61 ?  128 SER   B HB2  1 
ATOM   6102 H HB3  . SER   B 1 128 ? 38.920 -28.654 4.746   1.00 15.61 ?  128 SER   B HB3  1 
ATOM   6103 H HG   . SER   B 1 128 ? 39.210 -26.512 5.185   1.00 16.51 ?  128 SER   B HG   1 
ATOM   6104 N N    . ALA   B 1 129 ? 41.434 -29.615 1.915   1.00 15.17 ?  129 ALA   B N    1 
ATOM   6105 C CA   . ALA   B 1 129 ? 41.977 -30.914 1.554   1.00 16.08 ?  129 ALA   B CA   1 
ATOM   6106 C C    . ALA   B 1 129 ? 43.366 -31.095 2.154   1.00 15.10 ?  129 ALA   B C    1 
ATOM   6107 O O    . ALA   B 1 129 ? 43.927 -30.199 2.799   1.00 14.56 ?  129 ALA   B O    1 
ATOM   6108 C CB   . ALA   B 1 129 ? 42.031 -31.067 0.036   1.00 18.29 ?  129 ALA   B CB   1 
ATOM   6109 H H    . ALA   B 1 129 ? 41.519 -29.018 1.293   1.00 18.18 ?  129 ALA   B H    1 
ATOM   6110 H HA   . ALA   B 1 129 ? 41.403 -31.606 1.906   1.00 19.27 ?  129 ALA   B HA   1 
ATOM   6111 H HB1  . ALA   B 1 129 ? 42.388 -31.943 -0.181  1.00 21.92 ?  129 ALA   B HB1  1 
ATOM   6112 H HB2  . ALA   B 1 129 ? 41.134 -30.977 -0.322  1.00 21.92 ?  129 ALA   B HB2  1 
ATOM   6113 H HB3  . ALA   B 1 129 ? 42.605 -30.376 -0.333  1.00 21.92 ?  129 ALA   B HB3  1 
ATOM   6114 N N    . GLY   B 1 130 ? 43.926 -32.281 1.931   1.00 15.32 ?  130 GLY   B N    1 
ATOM   6115 C CA   . GLY   B 1 130 ? 45.314 -32.518 2.285   1.00 15.86 ?  130 GLY   B CA   1 
ATOM   6116 C C    . GLY   B 1 130 ? 45.526 -32.422 3.779   1.00 15.93 ?  130 GLY   B C    1 
ATOM   6117 O O    . GLY   B 1 130 ? 44.824 -33.065 4.574   1.00 16.74 ?  130 GLY   B O    1 
ATOM   6118 H H    . GLY   B 1 130 ? 43.534 -32.952 1.565   1.00 18.36 ?  130 GLY   B H    1 
ATOM   6119 H HA2  . GLY   B 1 130 ? 45.581 -33.407 1.990   1.00 19.01 ?  130 GLY   B HA2  1 
ATOM   6120 H HA3  . GLY   B 1 130 ? 45.886 -31.868 1.847   1.00 19.01 ?  130 GLY   B HA3  1 
ATOM   6121 N N    . ILE   B 1 131 ? 46.507 -31.600 4.168   1.00 16.44 ?  131 ILE   B N    1 
ATOM   6122 C CA   . ILE   B 1 131 ? 46.878 -31.463 5.567   1.00 17.67 ?  131 ILE   B CA   1 
ATOM   6123 C C    . ILE   B 1 131 ? 45.760 -30.872 6.405   1.00 16.70 ?  131 ILE   B C    1 
ATOM   6124 O O    . ILE   B 1 131 ? 45.831 -30.939 7.633   1.00 18.00 ?  131 ILE   B O    1 
ATOM   6125 C CB   . ILE   B 1 131 ? 48.200 -30.672 5.748   1.00 19.56 ?  131 ILE   B CB   1 
ATOM   6126 C CG1  . ILE   B 1 131 ? 48.017 -29.193 5.374   1.00 20.57 ?  131 ILE   B CG1  1 
ATOM   6127 C CG2  . ILE   B 1 131 ? 49.318 -31.308 4.928   1.00 20.22 ?  131 ILE   B CG2  1 
ATOM   6128 C CD1  . ILE   B 1 131 ? 49.221 -28.320 5.694   1.00 21.61 ?  131 ILE   B CD1  1 
ATOM   6129 H H    . ILE   B 1 131 ? 46.969 -31.104 3.638   1.00 19.71 ?  131 ILE   B H    1 
ATOM   6130 H HA   . ILE   B 1 131 ? 47.034 -32.349 5.919   1.00 21.17 ?  131 ILE   B HA   1 
ATOM   6131 H HB   . ILE   B 1 131 ? 48.447 -30.715 6.685   1.00 23.44 ?  131 ILE   B HB   1 
ATOM   6132 H HG12 . ILE   B 1 131 ? 47.846 -29.135 4.421   1.00 24.67 ?  131 ILE   B HG12 1 
ATOM   6133 H HG13 . ILE   B 1 131 ? 47.256 -28.831 5.862   1.00 24.67 ?  131 ILE   B HG13 1 
ATOM   6134 H HG21 . ILE   B 1 131 ? 50.158 -30.894 5.172   1.00 24.24 ?  131 ILE   B HG21 1 
ATOM   6135 H HG22 . ILE   B 1 131 ? 49.343 -32.256 5.117   1.00 24.24 ?  131 ILE   B HG22 1 
ATOM   6136 H HG23 . ILE   B 1 131 ? 49.135 -31.161 3.986   1.00 24.24 ?  131 ILE   B HG23 1 
ATOM   6137 H HD11 . ILE   B 1 131 ? 48.994 -27.395 5.511   1.00 25.91 ?  131 ILE   B HD11 1 
ATOM   6138 H HD12 . ILE   B 1 131 ? 49.444 -28.427 6.632   1.00 25.91 ?  131 ILE   B HD12 1 
ATOM   6139 H HD13 . ILE   B 1 131 ? 49.965 -28.597 5.141   1.00 25.91 ?  131 ILE   B HD13 1 
ATOM   6140 N N    . PHE   B 1 132 ? 44.726 -30.301 5.772   1.00 15.37 ?  132 PHE   B N    1 
ATOM   6141 C CA   . PHE   B 1 132 ? 43.570 -29.786 6.498   1.00 15.85 ?  132 PHE   B CA   1 
ATOM   6142 C C    . PHE   B 1 132 ? 42.541 -30.868 6.825   1.00 17.04 ?  132 PHE   B C    1 
ATOM   6143 O O    . PHE   B 1 132 ? 41.630 -30.605 7.619   1.00 18.32 ?  132 PHE   B O    1 
ATOM   6144 C CB   . PHE   B 1 132 ? 42.896 -28.648 5.715   1.00 14.74 ?  132 PHE   B CB   1 
ATOM   6145 C CG   . PHE   B 1 132 ? 43.598 -27.306 5.824   1.00 14.12 ?  132 PHE   B CG   1 
ATOM   6146 C CD1  . PHE   B 1 132 ? 44.898 -27.134 5.372   1.00 15.42 ?  132 PHE   B CD1  1 
ATOM   6147 C CD2  . PHE   B 1 132 ? 42.920 -26.202 6.324   1.00 13.63 ?  132 PHE   B CD2  1 
ATOM   6148 C CE1  . PHE   B 1 132 ? 45.523 -25.901 5.462   1.00 15.78 ?  132 PHE   B CE1  1 
ATOM   6149 C CE2  . PHE   B 1 132 ? 43.534 -24.963 6.406   1.00 14.16 ?  132 PHE   B CE2  1 
ATOM   6150 C CZ   . PHE   B 1 132 ? 44.836 -24.817 5.975   1.00 15.36 ?  132 PHE   B CZ   1 
ATOM   6151 H H    . PHE   B 1 132 ? 44.671 -30.203 4.918   1.00 18.42 ?  132 PHE   B H    1 
ATOM   6152 H HA   . PHE   B 1 132 ? 43.875 -29.416 7.339   1.00 18.99 ?  132 PHE   B HA   1 
ATOM   6153 H HB2  . PHE   B 1 132 ? 42.877 -28.893 4.780   1.00 17.67 ?  132 PHE   B HB2  1 
ATOM   6154 H HB3  . PHE   B 1 132 ? 41.990 -28.539 6.047   1.00 17.67 ?  132 PHE   B HB3  1 
ATOM   6155 H HD1  . PHE   B 1 132 ? 45.364 -27.872 5.035   1.00 18.48 ?  132 PHE   B HD1  1 
ATOM   6156 H HD2  . PHE   B 1 132 ? 42.040 -26.301 6.619   1.00 16.33 ?  132 PHE   B HD2  1 
ATOM   6157 H HE1  . PHE   B 1 132 ? 46.400 -25.808 5.173   1.00 18.91 ?  132 PHE   B HE1  1 
ATOM   6158 H HE2  . PHE   B 1 132 ? 43.072 -24.234 6.758   1.00 16.96 ?  132 PHE   B HE2  1 
ATOM   6159 H HZ   . PHE   B 1 132 ? 45.253 -23.986 6.038   1.00 18.41 ?  132 PHE   B HZ   1 
ATOM   6160 N N    . GLY   B 1 133 ? 42.639 -32.064 6.226   1.00 16.71 ?  133 GLY   B N    1 
ATOM   6161 C CA   . GLY   B 1 133 ? 41.926 -33.230 6.718   1.00 17.82 ?  133 GLY   B CA   1 
ATOM   6162 C C    . GLY   B 1 133 ? 40.528 -33.484 6.185   1.00 18.31 ?  133 GLY   B C    1 
ATOM   6163 O O    . GLY   B 1 133 ? 39.938 -34.504 6.549   1.00 20.20 ?  133 GLY   B O    1 
ATOM   6164 H H    . GLY   B 1 133 ? 43.120 -32.216 5.526   1.00 20.03 ?  133 GLY   B H    1 
ATOM   6165 H HA2  . GLY   B 1 133 ? 42.462 -34.014 6.526   1.00 21.36 ?  133 GLY   B HA2  1 
ATOM   6166 H HA3  . GLY   B 1 133 ? 41.851 -33.152 7.680   1.00 21.36 ?  133 GLY   B HA3  1 
ATOM   6167 N N    . ALA   B 1 134 ? 39.968 -32.608 5.357   1.00 17.40 ?  134 ALA   B N    1 
ATOM   6168 C CA   . ALA   B 1 134 ? 38.643 -32.884 4.819   1.00 17.24 ?  134 ALA   B CA   1 
ATOM   6169 C C    . ALA   B 1 134 ? 38.724 -33.881 3.667   1.00 16.87 ?  134 ALA   B C    1 
ATOM   6170 O O    . ALA   B 1 134 ? 39.773 -34.069 3.043   1.00 17.75 ?  134 ALA   B O    1 
ATOM   6171 C CB   . ALA   B 1 134 ? 37.975 -31.597 4.334   1.00 17.88 ?  134 ALA   B CB   1 
ATOM   6172 H H    . ALA   B 1 134 ? 40.317 -31.861 5.107   1.00 20.86 ?  134 ALA   B H    1 
ATOM   6173 H HA   . ALA   B 1 134 ? 38.090 -33.267 5.517   1.00 20.67 ?  134 ALA   B HA   1 
ATOM   6174 H HB1  . ALA   B 1 134 ? 37.087 -31.811 4.003   1.00 21.43 ?  134 ALA   B HB1  1 
ATOM   6175 H HB2  . ALA   B 1 134 ? 37.910 -30.976 5.075   1.00 21.43 ?  134 ALA   B HB2  1 
ATOM   6176 H HB3  . ALA   B 1 134 ? 38.509 -31.212 3.623   1.00 21.43 ?  134 ALA   B HB3  1 
ATOM   6177 N N    . ASP   B 1 135 ? 37.590 -34.512 3.384   1.00 17.30 ?  135 ASP   B N    1 
ATOM   6178 C CA   . ASP   B 1 135 ? 37.485 -35.400 2.236   1.00 17.97 ?  135 ASP   B CA   1 
ATOM   6179 C C    . ASP   B 1 135 ? 37.584 -34.565 0.966   1.00 16.43 ?  135 ASP   B C    1 
ATOM   6180 O O    . ASP   B 1 135 ? 36.729 -33.695 0.741   1.00 16.39 ?  135 ASP   B O    1 
ATOM   6181 C CB   . ASP   B 1 135 ? 36.147 -36.134 2.288   1.00 19.83 ?  135 ASP   B CB   1 
ATOM   6182 C CG   . ASP   B 1 135 ? 35.974 -37.130 1.160   1.00 21.63 ?  135 ASP   B CG   1 
ATOM   6183 O OD1  . ASP   B 1 135 ? 36.838 -37.167 0.258   1.00 21.35 ?  135 ASP   B OD1  1 
ATOM   6184 O OD2  . ASP   B 1 135 ? 34.974 -37.887 1.185   1.00 24.56 -1 135 ASP   B OD2  1 
ATOM   6185 H H    . ASP   B 1 135 ? 36.866 -34.442 3.842   1.00 20.74 ?  135 ASP   B H    1 
ATOM   6186 H HA   . ASP   B 1 135 ? 38.204 -36.052 2.263   1.00 21.54 ?  135 ASP   B HA   1 
ATOM   6187 H HB2  . ASP   B 1 135 ? 36.091 -36.616 3.125   1.00 23.77 ?  135 ASP   B HB2  1 
ATOM   6188 H HB3  . ASP   B 1 135 ? 35.434 -35.485 2.223   1.00 23.77 ?  135 ASP   B HB3  1 
ATOM   6189 N N    . PRO   B 1 136 ? 38.599 -34.771 0.122   1.00 16.65 ?  136 PRO   B N    1 
ATOM   6190 C CA   . PRO   B 1 136 ? 38.694 -33.955 -1.099  1.00 15.97 ?  136 PRO   B CA   1 
ATOM   6191 C C    . PRO   B 1 136 ? 37.503 -34.112 -2.024  1.00 15.14 ?  136 PRO   B C    1 
ATOM   6192 O O    . PRO   B 1 136 ? 37.182 -33.167 -2.753  1.00 14.33 ?  136 PRO   B O    1 
ATOM   6193 C CB   . PRO   B 1 136 ? 40.008 -34.429 -1.741  1.00 17.12 ?  136 PRO   B CB   1 
ATOM   6194 C CG   . PRO   B 1 136 ? 40.220 -35.813 -1.181  1.00 18.15 ?  136 PRO   B CG   1 
ATOM   6195 C CD   . PRO   B 1 136 ? 39.698 -35.746 0.220   1.00 17.95 ?  136 PRO   B CD   1 
ATOM   6196 H HA   . PRO   B 1 136 ? 38.777 -33.018 -0.871  1.00 19.14 ?  136 PRO   B HA   1 
ATOM   6197 H HB2  . PRO   B 1 136 ? 39.916 -34.455 -2.710  1.00 20.52 ?  136 PRO   B HB2  1 
ATOM   6198 H HB3  . PRO   B 1 136 ? 40.730 -33.833 -1.484  1.00 20.52 ?  136 PRO   B HB3  1 
ATOM   6199 H HG2  . PRO   B 1 136 ? 39.719 -36.461 -1.703  1.00 21.76 ?  136 PRO   B HG2  1 
ATOM   6200 H HG3  . PRO   B 1 136 ? 41.166 -36.029 -1.183  1.00 21.76 ?  136 PRO   B HG3  1 
ATOM   6201 H HD2  . PRO   B 1 136 ? 39.359 -36.609 0.498   1.00 21.51 ?  136 PRO   B HD2  1 
ATOM   6202 H HD3  . PRO   B 1 136 ? 40.379 -35.414 0.826   1.00 21.51 ?  136 PRO   B HD3  1 
ATOM   6203 N N    . ILE   B 1 137 ? 36.840 -35.275 -2.022  1.00 15.66 ?  137 ILE   B N    1 
ATOM   6204 C CA   . ILE   B 1 137 ? 35.619 -35.440 -2.809  1.00 16.23 ?  137 ILE   B CA   1 
ATOM   6205 C C    . ILE   B 1 137 ? 34.545 -34.471 -2.333  1.00 15.67 ?  137 ILE   B C    1 
ATOM   6206 O O    . ILE   B 1 137 ? 33.824 -33.865 -3.137  1.00 15.31 ?  137 ILE   B O    1 
ATOM   6207 C CB   . ILE   B 1 137 ? 35.143 -36.907 -2.749  1.00 18.32 ?  137 ILE   B CB   1 
ATOM   6208 C CG1  . ILE   B 1 137 ? 36.142 -37.810 -3.475  1.00 20.35 ?  137 ILE   B CG1  1 
ATOM   6209 C CG2  . ILE   B 1 137 ? 33.748 -37.053 -3.354  1.00 18.96 ?  137 ILE   B CG2  1 
ATOM   6210 C CD1  . ILE   B 1 137 ? 35.875 -39.294 -3.302  1.00 22.37 ?  137 ILE   B CD1  1 
ATOM   6211 H H    . ILE   B 1 137 ? 37.075 -35.974 -1.581  1.00 18.76 ?  137 ILE   B H    1 
ATOM   6212 H HA   . ILE   B 1 137 ? 35.811 -35.236 -3.738  1.00 19.45 ?  137 ILE   B HA   1 
ATOM   6213 H HB   . ILE   B 1 137 ? 35.101 -37.181 -1.822  1.00 21.96 ?  137 ILE   B HB   1 
ATOM   6214 H HG12 . ILE   B 1 137 ? 36.108 -37.617 -4.425  1.00 24.39 ?  137 ILE   B HG12 1 
ATOM   6215 H HG13 . ILE   B 1 137 ? 37.030 -37.632 -3.134  1.00 24.39 ?  137 ILE   B HG13 1 
ATOM   6216 H HG21 . ILE   B 1 137 ? 33.534 -37.997 -3.450  1.00 22.73 ?  137 ILE   B HG21 1 
ATOM   6217 H HG22 . ILE   B 1 137 ? 33.099 -36.638 -2.765  1.00 22.73 ?  137 ILE   B HG22 1 
ATOM   6218 H HG23 . ILE   B 1 137 ? 33.732 -36.625 -4.223  1.00 22.73 ?  137 ILE   B HG23 1 
ATOM   6219 H HD11 . ILE   B 1 137 ? 36.622 -39.787 -3.673  1.00 26.81 ?  137 ILE   B HD11 1 
ATOM   6220 H HD12 . ILE   B 1 137 ? 35.784 -39.492 -2.356  1.00 26.81 ?  137 ILE   B HD12 1 
ATOM   6221 H HD13 . ILE   B 1 137 ? 35.060 -39.531 -3.770  1.00 26.81 ?  137 ILE   B HD13 1 
ATOM   6222 N N    . HIS   B 1 138 ? 34.413 -34.321 -1.018  1.00 15.75 ?  138 HIS   B N    1 
ATOM   6223 C CA   . HIS   B 1 138 ? 33.471 -33.346 -0.485  1.00 16.11 ?  138 HIS   B CA   1 
ATOM   6224 C C    . HIS   B 1 138 ? 33.892 -31.921 -0.820  1.00 15.05 ?  138 HIS   B C    1 
ATOM   6225 O O    . HIS   B 1 138 ? 33.047 -31.079 -1.139  1.00 15.51 ?  138 HIS   B O    1 
ATOM   6226 C CB   . HIS   B 1 138 ? 33.356 -33.512 1.021   1.00 17.36 ?  138 HIS   B CB   1 
ATOM   6227 C CG   . HIS   B 1 138 ? 32.421 -32.533 1.649   1.00 18.66 ?  138 HIS   B CG   1 
ATOM   6228 N ND1  . HIS   B 1 138 ? 31.086 -32.466 1.315   1.00 20.30 ?  138 HIS   B ND1  1 
ATOM   6229 C CD2  . HIS   B 1 138 ? 32.631 -31.557 2.564   1.00 19.34 ?  138 HIS   B CD2  1 
ATOM   6230 C CE1  . HIS   B 1 138 ? 30.508 -31.505 2.011   1.00 20.18 ?  138 HIS   B CE1  1 
ATOM   6231 N NE2  . HIS   B 1 138 ? 31.423 -30.937 2.777   1.00 19.66 ?  138 HIS   B NE2  1 
ATOM   6232 H H    . HIS   B 1 138 ? 34.854 -34.766 -0.425  1.00 18.87 ?  138 HIS   B H    1 
ATOM   6233 H HA   . HIS   B 1 138 ? 32.599 -33.509 -0.877  1.00 19.30 ?  138 HIS   B HA   1 
ATOM   6234 H HB2  . HIS   B 1 138 ? 33.027 -34.404 1.216   1.00 20.81 ?  138 HIS   B HB2  1 
ATOM   6235 H HB3  . HIS   B 1 138 ? 34.230 -33.386 1.419   1.00 20.81 ?  138 HIS   B HB3  1 
ATOM   6236 H HD1  . HIS   B 1 138 ? 30.688 -32.980 0.746   1.00 24.34 ?  138 HIS   B HD1  1 
ATOM   6237 H HD2  . HIS   B 1 138 ? 33.429 -31.353 2.983   1.00 23.18 ?  138 HIS   B HD2  1 
ATOM   6238 H HE1  . HIS   B 1 138 ? 29.603 -31.274 1.969   1.00 24.19 ?  138 HIS   B HE1  1 
ATOM   6239 N N    . SER   B 1 139 ? 35.188 -31.621 -0.743  1.00 14.32 ?  139 SER   B N    1 
ATOM   6240 C CA   . SER   B 1 139 ? 35.630 -30.272 -1.060  1.00 13.74 ?  139 SER   B CA   1 
ATOM   6241 C C    . SER   B 1 139 ? 35.302 -29.921 -2.500  1.00 12.89 ?  139 SER   B C    1 
ATOM   6242 O O    . SER   B 1 139 ? 34.857 -28.805 -2.781  1.00 13.12 ?  139 SER   B O    1 
ATOM   6243 C CB   . SER   B 1 139 ? 37.123 -30.133 -0.787  1.00 14.04 ?  139 SER   B CB   1 
ATOM   6244 O OG   . SER   B 1 139 ? 37.539 -28.797 -1.034  1.00 14.11 ?  139 SER   B OG   1 
ATOM   6245 H H    . SER   B 1 139 ? 35.814 -32.169 -0.531  1.00 17.16 ?  139 SER   B H    1 
ATOM   6246 H HA   . SER   B 1 139 ? 35.153 -29.648 -0.497  1.00 16.47 ?  139 SER   B HA   1 
ATOM   6247 H HB2  . SER   B 1 139 ? 37.293 -30.354 0.141   1.00 16.83 ?  139 SER   B HB2  1 
ATOM   6248 H HB3  . SER   B 1 139 ? 37.615 -30.721 -1.372  1.00 16.83 ?  139 SER   B HB3  1 
ATOM   6249 H HG   . SER   B 1 139 ? 38.362 -28.714 -0.865  1.00 16.91 ?  139 SER   B HG   1 
ATOM   6250 N N    . LEU   B 1 140 ? 35.492 -30.863 -3.422  1.00 12.84 ?  140 LEU   B N    1 
ATOM   6251 C CA   . LEU   B 1 140 ? 35.131 -30.622 -4.812  1.00 13.03 ?  140 LEU   B CA   1 
ATOM   6252 C C    . LEU   B 1 140 ? 33.629 -30.390 -4.950  1.00 13.40 ?  140 LEU   B C    1 
ATOM   6253 O O    . LEU   B 1 140 ? 33.201 -29.506 -5.695  1.00 12.97 ?  140 LEU   B O    1 
ATOM   6254 C CB   . LEU   B 1 140 ? 35.609 -31.784 -5.685  1.00 13.03 ?  140 LEU   B CB   1 
ATOM   6255 C CG   . LEU   B 1 140 ? 35.252 -31.682 -7.158  1.00 13.14 ?  140 LEU   B CG   1 
ATOM   6256 C CD1  . LEU   B 1 140 ? 35.828 -30.410 -7.755  1.00 14.13 ?  140 LEU   B CD1  1 
ATOM   6257 C CD2  . LEU   B 1 140 ? 35.745 -32.911 -7.893  1.00 14.33 ?  140 LEU   B CD2  1 
ATOM   6258 H H    . LEU   B 1 140 ? 35.818 -31.643 -3.273  1.00 15.39 ?  140 LEU   B H    1 
ATOM   6259 H HA   . LEU   B 1 140 ? 35.585 -29.819 -5.119  1.00 15.61 ?  140 LEU   B HA   1 
ATOM   6260 H HB2  . LEU   B 1 140 ? 36.577 -31.839 -5.627  1.00 15.61 ?  140 LEU   B HB2  1 
ATOM   6261 H HB3  . LEU   B 1 140 ? 35.216 -32.604 -5.354  1.00 15.61 ?  140 LEU   B HB3  1 
ATOM   6262 H HG   . LEU   B 1 140 ? 34.291 -31.638 -7.249  1.00 15.74 ?  140 LEU   B HG   1 
ATOM   6263 H HD11 . LEU   B 1 140 ? 35.725 -30.441 -8.717  1.00 16.94 ?  140 LEU   B HD11 1 
ATOM   6264 H HD12 . LEU   B 1 140 ? 35.349 -29.645 -7.395  1.00 16.94 ?  140 LEU   B HD12 1 
ATOM   6265 H HD13 . LEU   B 1 140 ? 36.769 -30.349 -7.523  1.00 16.94 ?  140 LEU   B HD13 1 
ATOM   6266 H HD21 . LEU   B 1 140 ? 35.506 -32.827 -8.830  1.00 17.18 ?  140 LEU   B HD21 1 
ATOM   6267 H HD22 . LEU   B 1 140 ? 36.702 -32.975 -7.795  1.00 17.18 ?  140 LEU   B HD22 1 
ATOM   6268 H HD23 . LEU   B 1 140 ? 35.311 -33.689 -7.510  1.00 17.18 ?  140 LEU   B HD23 1 
ATOM   6269 N N    . ARG   B 1 141 ? 32.821 -31.178 -4.235  1.00 13.65 ?  141 ARG   B N    1 
ATOM   6270 C CA   . ARG   B 1 141 ? 31.371 -31.001 -4.221  1.00 14.44 ?  141 ARG   B CA   1 
ATOM   6271 C C    . ARG   B 1 141 ? 30.998 -29.586 -3.796  1.00 13.94 ?  141 ARG   B C    1 
ATOM   6272 O O    . ARG   B 1 141 ? 30.197 -28.910 -4.458  1.00 14.14 ?  141 ARG   B O    1 
ATOM   6273 C CB   . ARG   B 1 141 ? 30.777 -32.028 -3.247  1.00 16.13 ?  141 ARG   B CB   1 
ATOM   6274 C CG   . ARG   B 1 141 ? 29.312 -31.898 -2.927  1.00 18.38 ?  141 ARG   B CG   1 
ATOM   6275 C CD   . ARG   B 1 141 ? 28.514 -32.525 -4.000  1.00 20.13 ?  141 ARG   B CD   1 
ATOM   6276 N NE   . ARG   B 1 141 ? 28.259 -31.613 -5.104  1.00 20.58 ?  141 ARG   B NE   1 
ATOM   6277 C CZ   . ARG   B 1 141 ? 28.242 -31.967 -6.382  1.00 19.95 ?  141 ARG   B CZ   1 
ATOM   6278 N NH1  . ARG   B 1 141 ? 28.661 -33.160 -6.777  1.00 19.88 ?  141 ARG   B NH1  1 
ATOM   6279 N NH2  . ARG   B 1 141 ? 27.795 -31.101 -7.287  1.00 21.14 ?  141 ARG   B NH2  1 
ATOM   6280 H H    . ARG   B 1 141 ? 33.099 -31.823 -3.746  1.00 16.36 ?  141 ARG   B H    1 
ATOM   6281 H HA   . ARG   B 1 141 ? 31.013 -31.158 -5.104  1.00 17.30 ?  141 ARG   B HA   1 
ATOM   6282 H HB2  . ARG   B 1 141 ? 30.927 -32.911 -3.620  1.00 19.33 ?  141 ARG   B HB2  1 
ATOM   6283 H HB3  . ARG   B 1 141 ? 31.260 -31.957 -2.410  1.00 19.33 ?  141 ARG   B HB3  1 
ATOM   6284 H HG2  . ARG   B 1 141 ? 29.130 -32.349 -2.093  1.00 22.03 ?  141 ARG   B HG2  1 
ATOM   6285 H HG3  . ARG   B 1 141 ? 29.066 -30.957 -2.859  1.00 22.03 ?  141 ARG   B HG3  1 
ATOM   6286 H HD2  . ARG   B 1 141 ? 28.993 -33.300 -4.341  1.00 24.14 ?  141 ARG   B HD2  1 
ATOM   6287 H HD3  . ARG   B 1 141 ? 27.668 -32.804 -3.633  1.00 24.14 ?  141 ARG   B HD3  1 
ATOM   6288 H HE   . ARG   B 1 141 ? 28.124 -30.782 -4.915  1.00 24.67 ?  141 ARG   B HE   1 
ATOM   6289 H HH11 . ARG   B 1 141 ? 28.940 -33.736 -6.205  1.00 23.83 ?  141 ARG   B HH11 1 
ATOM   6290 H HH12 . ARG   B 1 141 ? 28.646 -33.361 -7.611  1.00 23.83 ?  141 ARG   B HH12 1 
ATOM   6291 H HH21 . ARG   B 1 141 ? 27.526 -30.319 -7.044  1.00 25.35 ?  141 ARG   B HH21 1 
ATOM   6292 H HH22 . ARG   B 1 141 ? 27.797 -31.310 -8.122  1.00 25.35 ?  141 ARG   B HH22 1 
ATOM   6293 N N    . VAL   B 1 142 ? 31.540 -29.137 -2.666  1.00 13.66 ?  142 VAL   B N    1 
ATOM   6294 C CA   . VAL   B 1 142 ? 31.205 -27.803 -2.185  1.00 13.14 ?  142 VAL   B CA   1 
ATOM   6295 C C    . VAL   B 1 142 ? 31.691 -26.748 -3.170  1.00 13.31 ?  142 VAL   B C    1 
ATOM   6296 O O    . VAL   B 1 142 ? 31.002 -25.753 -3.426  1.00 13.62 ?  142 VAL   B O    1 
ATOM   6297 C CB   . VAL   B 1 142 ? 31.750 -27.578 -0.762  1.00 13.81 ?  142 VAL   B CB   1 
ATOM   6298 C CG1  . VAL   B 1 142 ? 31.442 -26.164 -0.277  1.00 13.85 ?  142 VAL   B CG1  1 
ATOM   6299 C CG2  . VAL   B 1 142 ? 31.156 -28.607 0.187   1.00 14.54 ?  142 VAL   B CG2  1 
ATOM   6300 H H    . VAL   B 1 142 ? 32.093 -29.571 -2.171  1.00 16.37 ?  142 VAL   B H    1 
ATOM   6301 H HA   . VAL   B 1 142 ? 30.245 -27.725 -2.134  1.00 15.75 ?  142 VAL   B HA   1 
ATOM   6302 H HB   . VAL   B 1 142 ? 32.713 -27.696 -0.762  1.00 16.55 ?  142 VAL   B HB   1 
ATOM   6303 H HG11 . VAL   B 1 142 ? 31.636 -26.108 0.673   1.00 16.60 ?  142 VAL   B HG11 1 
ATOM   6304 H HG12 . VAL   B 1 142 ? 31.999 -25.536 -0.763  1.00 16.60 ?  142 VAL   B HG12 1 
ATOM   6305 H HG13 . VAL   B 1 142 ? 30.506 -25.974 -0.435  1.00 16.60 ?  142 VAL   B HG13 1 
ATOM   6306 H HG21 . VAL   B 1 142 ? 31.457 -28.419 1.087   1.00 17.42 ?  142 VAL   B HG21 1 
ATOM   6307 H HG22 . VAL   B 1 142 ? 30.188 -28.551 0.142   1.00 17.42 ?  142 VAL   B HG22 1 
ATOM   6308 H HG23 . VAL   B 1 142 ? 31.448 -29.492 -0.084  1.00 17.42 ?  142 VAL   B HG23 1 
ATOM   6309 N N    . CYS   B 1 143 ? 32.874 -26.950 -3.751  1.00 12.52 ?  143 CYS   B N    1 
ATOM   6310 C CA   . CYS   B 1 143 ? 33.372 -26.017 -4.757  1.00 12.54 ?  143 CYS   B CA   1 
ATOM   6311 C C    . CYS   B 1 143 ? 32.368 -25.869 -5.897  1.00 12.56 ?  143 CYS   B C    1 
ATOM   6312 O O    . CYS   B 1 143 ? 31.967 -24.756 -6.257  1.00 13.00 ?  143 CYS   B O    1 
ATOM   6313 C CB   . CYS   B 1 143 ? 34.725 -26.510 -5.283  1.00 12.64 ?  143 CYS   B CB   1 
ATOM   6314 S SG   . CYS   B 1 143 ? 35.485 -25.409 -6.501  1.00 12.98 ?  143 CYS   B SG   1 
ATOM   6315 H H    . CYS   B 1 143 ? 33.403 -27.601 -3.577  1.00 15.00 ?  143 CYS   B H    1 
ATOM   6316 H HA   . CYS   B 1 143 ? 33.509 -25.141 -4.354  1.00 15.02 ?  143 CYS   B HA   1 
ATOM   6317 H HB2  . CYS   B 1 143 ? 35.346 -26.595 -4.540  1.00 15.14 ?  143 CYS   B HB2  1 
ATOM   6318 H HB3  . CYS   B 1 143 ? 34.602 -27.374 -5.700  1.00 15.14 ?  143 CYS   B HB3  1 
ATOM   6319 H HG   . CYS   B 1 143 ? 36.559 -25.851 -6.816  1.00 15.56 ?  143 CYS   B HG   1 
ATOM   6320 N N    . VAL   B 1 144 ? 31.963 -26.991 -6.490  1.00 13.28 ?  144 VAL   B N    1 
ATOM   6321 C CA   . VAL   B 1 144 ? 31.059 -26.925 -7.634  1.00 14.60 ?  144 VAL   B CA   1 
ATOM   6322 C C    . VAL   B 1 144 ? 29.717 -26.312 -7.260  1.00 14.48 ?  144 VAL   B C    1 
ATOM   6323 O O    . VAL   B 1 144 ? 29.101 -25.606 -8.069  1.00 15.71 ?  144 VAL   B O    1 
ATOM   6324 C CB   . VAL   B 1 144 ? 30.899 -28.335 -8.210  1.00 16.67 ?  144 VAL   B CB   1 
ATOM   6325 C CG1  . VAL   B 1 144 ? 29.632 -28.454 -9.049  1.00 19.09 ?  144 VAL   B CG1  1 
ATOM   6326 C CG2  . VAL   B 1 144 ? 32.144 -28.733 -8.997  1.00 17.05 ?  144 VAL   B CG2  1 
ATOM   6327 H H    . VAL   B 1 144 ? 32.198 -27.782 -6.258  1.00 15.91 ?  144 VAL   B H    1 
ATOM   6328 H HA   . VAL   B 1 144 ? 31.452 -26.368 -8.323  1.00 17.50 ?  144 VAL   B HA   1 
ATOM   6329 H HB   . VAL   B 1 144 ? 30.814 -28.962 -7.473  1.00 19.98 ?  144 VAL   B HB   1 
ATOM   6330 H HG11 . VAL   B 1 144 ? 29.705 -29.242 -9.617  1.00 22.88 ?  144 VAL   B HG11 1 
ATOM   6331 H HG12 . VAL   B 1 144 ? 28.867 -28.553 -8.460  1.00 22.88 ?  144 VAL   B HG12 1 
ATOM   6332 H HG13 . VAL   B 1 144 ? 29.536 -27.665 -9.599  1.00 22.88 ?  144 VAL   B HG13 1 
ATOM   6333 H HG21 . VAL   B 1 144 ? 32.025 -29.632 -9.347  1.00 20.44 ?  144 VAL   B HG21 1 
ATOM   6334 H HG22 . VAL   B 1 144 ? 32.264 -28.109 -9.732  1.00 20.44 ?  144 VAL   B HG22 1 
ATOM   6335 H HG23 . VAL   B 1 144 ? 32.912 -28.705 -8.409  1.00 20.44 ?  144 VAL   B HG23 1 
ATOM   6336 N N    . ASP   B 1 145 ? 29.249 -26.553 -6.040  1.00 14.60 ?  145 ASP   B N    1 
ATOM   6337 C CA   . ASP   B 1 145 ? 27.942 -26.088 -5.599  1.00 15.52 ?  145 ASP   B CA   1 
ATOM   6338 C C    . ASP   B 1 145 ? 27.974 -24.665 -5.060  1.00 15.07 ?  145 ASP   B C    1 
ATOM   6339 O O    . ASP   B 1 145 ? 26.916 -24.124 -4.719  1.00 16.71 ?  145 ASP   B O    1 
ATOM   6340 C CB   . ASP   B 1 145 ? 27.384 -27.013 -4.509  1.00 17.44 ?  145 ASP   B CB   1 
ATOM   6341 C CG   . ASP   B 1 145 ? 26.991 -28.376 -5.025  1.00 19.12 ?  145 ASP   B CG   1 
ATOM   6342 O OD1  . ASP   B 1 145 ? 26.891 -28.559 -6.255  1.00 19.38 ?  145 ASP   B OD1  1 
ATOM   6343 O OD2  . ASP   B 1 145 ? 26.790 -29.265 -4.178  1.00 21.21 -1 145 ASP   B OD2  1 
ATOM   6344 H H    . ASP   B 1 145 ? 29.689 -26.975 -5.437  1.00 17.49 ?  145 ASP   B H    1 
ATOM   6345 H HA   . ASP   B 1 145 ? 27.335 -26.089 -6.352  1.00 18.61 ?  145 ASP   B HA   1 
ATOM   6346 H HB2  . ASP   B 1 145 ? 28.059 -27.140 -3.833  1.00 20.90 ?  145 ASP   B HB2  1 
ATOM   6347 H HB3  . ASP   B 1 145 ? 26.596 -26.596 -4.126  1.00 20.90 ?  145 ASP   B HB3  1 
ATOM   6348 N N    . THR   B 1 146 ? 29.152 -24.049 -4.963  1.00 13.21 ?  146 THR   B N    1 
ATOM   6349 C CA   . THR   B 1 146 ? 29.292 -22.727 -4.359  1.00 12.62 ?  146 THR   B CA   1 
ATOM   6350 C C    . THR   B 1 146 ? 29.925 -21.703 -5.283  1.00 12.32 ?  146 THR   B C    1 
ATOM   6351 O O    . THR   B 1 146 ? 29.469 -20.542 -5.334  1.00 12.75 ?  146 THR   B O    1 
ATOM   6352 C CB   . THR   B 1 146 ? 30.118 -22.829 -3.072  1.00 12.73 ?  146 THR   B CB   1 
ATOM   6353 O OG1  . THR   B 1 146 ? 29.538 -23.823 -2.216  1.00 13.16 ?  146 THR   B OG1  1 
ATOM   6354 C CG2  . THR   B 1 146 ? 30.192 -21.489 -2.356  1.00 13.10 ?  146 THR   B CG2  1 
ATOM   6355 H H    . THR   B 1 146 ? 29.901 -24.369 -5.250  1.00 15.82 ?  146 THR   B H    1 
ATOM   6356 H HA   . THR   B 1 146 ? 28.418 -22.392 -4.119  1.00 15.12 ?  146 THR   B HA   1 
ATOM   6357 H HB   . THR   B 1 146 ? 31.029 -23.089 -3.299  1.00 15.25 ?  146 THR   B HB   1 
ATOM   6358 H HG1  . THR   B 1 146 ? 29.583 -24.583 -2.594  1.00 15.77 ?  146 THR   B HG1  1 
ATOM   6359 H HG21 . THR   B 1 146 ? 30.543 -21.608 -1.461  1.00 15.69 ?  146 THR   B HG21 1 
ATOM   6360 H HG22 . THR   B 1 146 ? 30.776 -20.881 -2.842  1.00 15.69 ?  146 THR   B HG22 1 
ATOM   6361 H HG23 . THR   B 1 146 ? 29.308 -21.096 -2.299  1.00 15.69 ?  146 THR   B HG23 1 
ATOM   6362 N N    . VAL   B 1 147 ? 30.991 -22.081 -5.977  1.00 12.18 ?  147 VAL   B N    1 
ATOM   6363 C CA   . VAL   B 1 147 ? 31.717 -21.145 -6.820  1.00 11.78 ?  147 VAL   B CA   1 
ATOM   6364 C C    . VAL   B 1 147 ? 30.985 -21.010 -8.142  1.00 12.11 ?  147 VAL   B C    1 
ATOM   6365 O O    . VAL   B 1 147 ? 30.612 -22.011 -8.768  1.00 12.97 ?  147 VAL   B O    1 
ATOM   6366 C CB   . VAL   B 1 147 ? 33.173 -21.601 -7.019  1.00 11.75 ?  147 VAL   B CB   1 
ATOM   6367 C CG1  . VAL   B 1 147 ? 33.936 -20.571 -7.834  1.00 12.14 ?  147 VAL   B CG1  1 
ATOM   6368 C CG2  . VAL   B 1 147 ? 33.845 -21.813 -5.674  1.00 11.97 ?  147 VAL   B CG2  1 
ATOM   6369 H H    . VAL   B 1 147 ? 31.313 -22.878 -5.985  1.00 14.59 ?  147 VAL   B H    1 
ATOM   6370 H HA   . VAL   B 1 147 ? 31.736 -20.274 -6.395  1.00 14.12 ?  147 VAL   B HA   1 
ATOM   6371 H HB   . VAL   B 1 147 ? 33.187 -22.443 -7.506  1.00 14.07 ?  147 VAL   B HB   1 
ATOM   6372 H HG11 . VAL   B 1 147 ? 34.879 -20.794 -7.821  1.00 14.54 ?  147 VAL   B HG11 1 
ATOM   6373 H HG12 . VAL   B 1 147 ? 33.606 -20.579 -8.745  1.00 14.54 ?  147 VAL   B HG12 1 
ATOM   6374 H HG13 . VAL   B 1 147 ? 33.798 -19.696 -7.438  1.00 14.54 ?  147 VAL   B HG13 1 
ATOM   6375 H HG21 . VAL   B 1 147 ? 34.786 -22.003 -5.815  1.00 14.34 ?  147 VAL   B HG21 1 
ATOM   6376 H HG22 . VAL   B 1 147 ? 33.745 -21.008 -5.143  1.00 14.34 ?  147 VAL   B HG22 1 
ATOM   6377 H HG23 . VAL   B 1 147 ? 33.422 -22.562 -5.224  1.00 14.34 ?  147 VAL   B HG23 1 
ATOM   6378 N N    . ARG   B 1 148 ? 30.780 -19.762 -8.564  1.00 11.94 ?  148 ARG   B N    1 
ATOM   6379 C CA   . ARG   B 1 148 ? 30.157 -19.442 -9.837  1.00 12.31 ?  148 ARG   B CA   1 
ATOM   6380 C C    . ARG   B 1 148 ? 31.117 -18.771 -10.806 1.00 12.35 ?  148 ARG   B C    1 
ATOM   6381 O O    . ARG   B 1 148 ? 30.831 -18.747 -12.007 1.00 13.74 ?  148 ARG   B O    1 
ATOM   6382 C CB   . ARG   B 1 148 ? 28.917 -18.554 -9.622  1.00 12.61 ?  148 ARG   B CB   1 
ATOM   6383 C CG   . ARG   B 1 148 ? 27.847 -19.257 -8.802  1.00 13.34 ?  148 ARG   B CG   1 
ATOM   6384 C CD   . ARG   B 1 148 ? 26.636 -18.372 -8.505  1.00 14.43 ?  148 ARG   B CD   1 
ATOM   6385 N NE   . ARG   B 1 148 ? 27.008 -17.165 -7.776  1.00 14.30 ?  148 ARG   B NE   1 
ATOM   6386 C CZ   . ARG   B 1 148 ? 27.322 -17.129 -6.488  1.00 13.50 ?  148 ARG   B CZ   1 
ATOM   6387 N NH1  . ARG   B 1 148 ? 27.271 -18.216 -5.730  1.00 13.64 ?  148 ARG   B NH1  1 
ATOM   6388 N NH2  . ARG   B 1 148 ? 27.714 -15.977 -5.951  1.00 13.51 ?  148 ARG   B NH2  1 
ATOM   6389 H H    . ARG   B 1 148 ? 30.998 -19.061 -8.108  1.00 14.30 ?  148 ARG   B H    1 
ATOM   6390 H HA   . ARG   B 1 148 ? 29.859 -20.262 -10.252 1.00 14.75 ?  148 ARG   B HA   1 
ATOM   6391 H HB2  . ARG   B 1 148 ? 29.180 -17.749 -9.150  1.00 15.11 ?  148 ARG   B HB2  1 
ATOM   6392 H HB3  . ARG   B 1 148 ? 28.537 -18.326 -10.485 1.00 15.11 ?  148 ARG   B HB3  1 
ATOM   6393 H HG2  . ARG   B 1 148 ? 27.535 -20.038 -9.293  1.00 15.98 ?  148 ARG   B HG2  1 
ATOM   6394 H HG3  . ARG   B 1 148 ? 28.228 -19.536 -7.954  1.00 15.98 ?  148 ARG   B HG3  1 
ATOM   6395 H HD2  . ARG   B 1 148 ? 26.224 -18.108 -9.343  1.00 17.29 ?  148 ARG   B HD2  1 
ATOM   6396 H HD3  . ARG   B 1 148 ? 26.001 -18.873 -7.966  1.00 17.29 ?  148 ARG   B HD3  1 
ATOM   6397 H HE   . ARG   B 1 148 ? 27.029 -16.429 -8.214  1.00 17.14 ?  148 ARG   B HE   1 
ATOM   6398 H HH11 . ARG   B 1 148 ? 27.023 -18.970 -6.064  1.00 16.35 ?  148 ARG   B HH11 1 
ATOM   6399 H HH12 . ARG   B 1 148 ? 27.478 -18.169 -4.894  1.00 16.35 ?  148 ARG   B HH12 1 
ATOM   6400 H HH21 . ARG   B 1 148 ? 27.751 -15.269 -6.437  1.00 16.19 ?  148 ARG   B HH21 1 
ATOM   6401 H HH22 . ARG   B 1 148 ? 27.917 -15.938 -5.118  1.00 16.19 ?  148 ARG   B HH22 1 
ATOM   6402 N N    . THR   B 1 149 ? 32.223 -18.216 -10.316 1.00 12.35 ?  149 THR   B N    1 
ATOM   6403 C CA   . THR   B 1 149 ? 33.261 -17.654 -11.166 1.00 12.22 ?  149 THR   B CA   1 
ATOM   6404 C C    . THR   B 1 149 ? 34.144 -18.792 -11.681 1.00 11.92 ?  149 THR   B C    1 
ATOM   6405 O O    . THR   B 1 149 ? 33.945 -19.963 -11.347 1.00 12.24 ?  149 THR   B O    1 
ATOM   6406 C CB   . THR   B 1 149 ? 34.031 -16.600 -10.382 1.00 12.31 ?  149 THR   B CB   1 
ATOM   6407 O OG1  . THR   B 1 149 ? 34.493 -17.202 -9.171  1.00 12.30 ?  149 THR   B OG1  1 
ATOM   6408 C CG2  . THR   B 1 149 ? 33.146 -15.394 -10.074 1.00 12.60 ?  149 THR   B CG2  1 
ATOM   6409 H H    . THR   B 1 149 ? 32.383 -18.138 -9.474  1.00 14.79 ?  149 THR   B H    1 
ATOM   6410 H HA   . THR   B 1 149 ? 32.847 -17.217 -11.927 1.00 14.64 ?  149 THR   B HA   1 
ATOM   6411 H HB   . THR   B 1 149 ? 34.788 -16.306 -10.900 1.00 14.75 ?  149 THR   B HB   1 
ATOM   6412 H HG1  . THR   B 1 149 ? 34.918 -16.636 -8.708  1.00 14.73 ?  149 THR   B HG1  1 
ATOM   6413 H HG21 . THR   B 1 149 ? 33.656 -14.725 -9.585  1.00 15.10 ?  149 THR   B HG21 1 
ATOM   6414 H HG22 . THR   B 1 149 ? 32.824 -14.998 -10.899 1.00 15.10 ?  149 THR   B HG22 1 
ATOM   6415 H HG23 . THR   B 1 149 ? 32.385 -15.661 -9.534  1.00 15.10 ?  149 THR   B HG23 1 
ATOM   6416 N N    . ASN   B 1 150 ? 35.111 -18.470 -12.527 1.00 11.87 ?  150 ASN   B N    1 
ATOM   6417 C CA   . ASN   B 1 150 ? 35.879 -19.494 -13.225 1.00 12.26 ?  150 ASN   B CA   1 
ATOM   6418 C C    . ASN   B 1 150 ? 37.040 -19.947 -12.355 1.00 11.85 ?  150 ASN   B C    1 
ATOM   6419 O O    . ASN   B 1 150 ? 37.977 -19.185 -12.112 1.00 12.43 ?  150 ASN   B O    1 
ATOM   6420 C CB   . ASN   B 1 150 ? 36.350 -18.961 -14.569 1.00 14.30 ?  150 ASN   B CB   1 
ATOM   6421 C CG   . ASN   B 1 150 ? 35.203 -18.753 -15.518 1.00 16.75 ?  150 ASN   B CG   1 
ATOM   6422 O OD1  . ASN   B 1 150 ? 34.306 -19.585 -15.602 1.00 17.55 ?  150 ASN   B OD1  1 
ATOM   6423 N ND2  . ASN   B 1 150 ? 35.196 -17.626 -16.209 1.00 18.79 ?  150 ASN   B ND2  1 
ATOM   6424 H H    . ASN   B 1 150 ? 35.350 -17.662 -12.702 1.00 14.22 ?  150 ASN   B H    1 
ATOM   6425 H HA   . ASN   B 1 150 ? 35.299 -20.260 -13.388 1.00 14.69 ?  150 ASN   B HA   1 
ATOM   6426 H HB2  . ASN   B 1 150 ? 36.787 -18.104 -14.431 1.00 17.14 ?  150 ASN   B HB2  1 
ATOM   6427 H HB3  . ASN   B 1 150 ? 36.965 -19.593 -14.962 1.00 17.14 ?  150 ASN   B HB3  1 
ATOM   6428 H HD21 . ASN   B 1 150 ? 34.559 -17.464 -16.767 1.00 22.53 ?  150 ASN   B HD21 1 
ATOM   6429 H HD22 . ASN   B 1 150 ? 35.836 -17.058 -16.117 1.00 22.53 ?  150 ASN   B HD22 1 
ATOM   6430 N N    . VAL   B 1 151 ? 36.985 -21.189 -11.888 1.00 11.52 ?  151 VAL   B N    1 
ATOM   6431 C CA   . VAL   B 1 151 ? 37.998 -21.724 -10.994 1.00 11.52 ?  151 VAL   B CA   1 
ATOM   6432 C C    . VAL   B 1 151 ? 38.702 -22.893 -11.671 1.00 11.35 ?  151 VAL   B C    1 
ATOM   6433 O O    . VAL   B 1 151 ? 38.059 -23.825 -12.173 1.00 12.70 ?  151 VAL   B O    1 
ATOM   6434 C CB   . VAL   B 1 151 ? 37.440 -22.064 -9.596  1.00 12.71 ?  151 VAL   B CB   1 
ATOM   6435 C CG1  . VAL   B 1 151 ? 36.274 -23.055 -9.668  1.00 13.89 ?  151 VAL   B CG1  1 
ATOM   6436 C CG2  . VAL   B 1 151 ? 38.551 -22.567 -8.688  1.00 13.13 ?  151 VAL   B CG2  1 
ATOM   6437 H H    . VAL   B 1 151 ? 36.357 -21.750 -12.078 1.00 13.80 ?  151 VAL   B H    1 
ATOM   6438 H HA   . VAL   B 1 151 ? 38.666 -21.031 -10.856 1.00 13.79 ?  151 VAL   B HA   1 
ATOM   6439 H HB   . VAL   B 1 151 ? 37.097 -21.248 -9.197  1.00 15.23 ?  151 VAL   B HB   1 
ATOM   6440 H HG11 . VAL   B 1 151 ? 35.959 -23.244 -8.769  1.00 16.65 ?  151 VAL   B HG11 1 
ATOM   6441 H HG12 . VAL   B 1 151 ? 35.555 -22.663 -10.191 1.00 16.65 ?  151 VAL   B HG12 1 
ATOM   6442 H HG13 . VAL   B 1 151 ? 36.578 -23.875 -10.089 1.00 16.65 ?  151 VAL   B HG13 1 
ATOM   6443 H HG21 . VAL   B 1 151 ? 38.206 -22.637 -7.781  1.00 15.73 ?  151 VAL   B HG21 1 
ATOM   6444 H HG22 . VAL   B 1 151 ? 38.842 -23.439 -8.995  1.00 15.73 ?  151 VAL   B HG22 1 
ATOM   6445 H HG23 . VAL   B 1 151 ? 39.288 -21.940 -8.712  1.00 15.73 ?  151 VAL   B HG23 1 
ATOM   6446 N N    . TYR   B 1 152 ? 40.035 -22.805 -11.692 1.00 11.00 ?  152 TYR   B N    1 
ATOM   6447 C CA   . TYR   B 1 152 ? 40.935 -23.792 -12.273 1.00 11.33 ?  152 TYR   B CA   1 
ATOM   6448 C C    . TYR   B 1 152 ? 41.658 -24.471 -11.113 1.00 10.55 ?  152 TYR   B C    1 
ATOM   6449 O O    . TYR   B 1 152 ? 42.508 -23.856 -10.459 1.00 11.27 ?  152 TYR   B O    1 
ATOM   6450 C CB   . TYR   B 1 152 ? 41.909 -23.094 -13.227 1.00 12.08 ?  152 TYR   B CB   1 
ATOM   6451 C CG   . TYR   B 1 152 ? 41.228 -22.631 -14.495 1.00 12.63 ?  152 TYR   B CG   1 
ATOM   6452 C CD1  . TYR   B 1 152 ? 40.572 -21.404 -14.563 1.00 13.04 ?  152 TYR   B CD1  1 
ATOM   6453 C CD2  . TYR   B 1 152 ? 41.222 -23.437 -15.616 1.00 13.84 ?  152 TYR   B CD2  1 
ATOM   6454 C CE1  . TYR   B 1 152 ? 39.933 -21.001 -15.722 1.00 14.49 ?  152 TYR   B CE1  1 
ATOM   6455 C CE2  . TYR   B 1 152 ? 40.588 -23.050 -16.773 1.00 14.66 ?  152 TYR   B CE2  1 
ATOM   6456 C CZ   . TYR   B 1 152 ? 39.946 -21.829 -16.825 1.00 14.85 ?  152 TYR   B CZ   1 
ATOM   6457 O OH   . TYR   B 1 152 ? 39.319 -21.455 -17.987 1.00 17.51 ?  152 TYR   B OH   1 
ATOM   6458 H H    . TYR   B 1 152 ? 40.466 -22.131 -11.352 1.00 13.18 ?  152 TYR   B H    1 
ATOM   6459 H HA   . TYR   B 1 152 ? 40.424 -24.455 -12.761 1.00 13.58 ?  152 TYR   B HA   1 
ATOM   6460 H HB2  . TYR   B 1 152 ? 42.285 -22.316 -12.780 1.00 14.47 ?  152 TYR   B HB2  1 
ATOM   6461 H HB3  . TYR   B 1 152 ? 42.618 -23.711 -13.466 1.00 14.47 ?  152 TYR   B HB3  1 
ATOM   6462 H HD1  . TYR   B 1 152 ? 40.557 -20.847 -13.815 1.00 15.62 ?  152 TYR   B HD1  1 
ATOM   6463 H HD2  . TYR   B 1 152 ? 41.648 -24.268 -15.582 1.00 16.58 ?  152 TYR   B HD2  1 
ATOM   6464 H HE1  . TYR   B 1 152 ? 39.496 -20.181 -15.760 1.00 17.36 ?  152 TYR   B HE1  1 
ATOM   6465 H HE2  . TYR   B 1 152 ? 40.596 -23.610 -17.518 1.00 17.57 ?  152 TYR   B HE2  1 
ATOM   6466 H HH   . TYR   B 1 152 ? 38.965 -20.695 -17.887 1.00 20.99 ?  152 TYR   B HH   1 
ATOM   6467 N N    . LEU   B 1 153 ? 41.286 -25.723 -10.843 1.00 11.06 ?  153 LEU   B N    1 
ATOM   6468 C CA   . LEU   B 1 153 ? 41.790 -26.470 -9.700  1.00 10.82 ?  153 LEU   B CA   1 
ATOM   6469 C C    . LEU   B 1 153 ? 43.022 -27.274 -10.089 1.00 11.12 ?  153 LEU   B C    1 
ATOM   6470 O O    . LEU   B 1 153 ? 43.004 -28.009 -11.079 1.00 12.17 ?  153 LEU   B O    1 
ATOM   6471 C CB   . LEU   B 1 153 ? 40.715 -27.429 -9.186  1.00 11.26 ?  153 LEU   B CB   1 
ATOM   6472 C CG   . LEU   B 1 153 ? 39.462 -26.778 -8.604  1.00 11.82 ?  153 LEU   B CG   1 
ATOM   6473 C CD1  . LEU   B 1 153 ? 38.360 -27.817 -8.433  1.00 12.82 ?  153 LEU   B CD1  1 
ATOM   6474 C CD2  . LEU   B 1 153 ? 39.774 -26.103 -7.280  1.00 12.21 ?  153 LEU   B CD2  1 
ATOM   6475 H H    . LEU   B 1 153 ? 40.724 -26.170 -11.320 1.00 13.25 ?  153 LEU   B H    1 
ATOM   6476 H HA   . LEU   B 1 153 ? 42.020 -25.857 -8.989  1.00 12.96 ?  153 LEU   B HA   1 
ATOM   6477 H HB2  . LEU   B 1 153 ? 40.431 -27.997 -9.921  1.00 13.48 ?  153 LEU   B HB2  1 
ATOM   6478 H HB3  . LEU   B 1 153 ? 41.103 -27.981 -8.487  1.00 13.48 ?  153 LEU   B HB3  1 
ATOM   6479 H HG   . LEU   B 1 153 ? 39.138 -26.097 -9.219  1.00 14.16 ?  153 LEU   B HG   1 
ATOM   6480 H HD11 . LEU   B 1 153 ? 37.553 -27.370 -8.127  1.00 15.36 ?  153 LEU   B HD11 1 
ATOM   6481 H HD12 . LEU   B 1 153 ? 38.200 -28.245 -9.284  1.00 15.36 ?  153 LEU   B HD12 1 
ATOM   6482 H HD13 . LEU   B 1 153 ? 38.647 -28.468 -7.776  1.00 15.36 ?  153 LEU   B HD13 1 
ATOM   6483 H HD21 . LEU   B 1 153 ? 38.959 -25.750 -6.900  1.00 14.63 ?  153 LEU   B HD21 1 
ATOM   6484 H HD22 . LEU   B 1 153 ? 40.166 -26.760 -6.680  1.00 14.63 ?  153 LEU   B HD22 1 
ATOM   6485 H HD23 . LEU   B 1 153 ? 40.409 -25.384 -7.437  1.00 14.63 ?  153 LEU   B HD23 1 
ATOM   6486 N N    . ALA   B 1 154 ? 44.071 -27.168 -9.278  1.00 11.15 ?  154 ALA   B N    1 
ATOM   6487 C CA   . ALA   B 1 154 ? 45.299 -27.930 -9.463  1.00 12.01 ?  154 ALA   B CA   1 
ATOM   6488 C C    . ALA   B 1 154 ? 45.362 -29.011 -8.390  1.00 12.36 ?  154 ALA   B C    1 
ATOM   6489 O O    . ALA   B 1 154 ? 45.291 -28.711 -7.190  1.00 13.77 ?  154 ALA   B O    1 
ATOM   6490 C CB   . ALA   B 1 154 ? 46.524 -27.024 -9.385  1.00 13.06 ?  154 ALA   B CB   1 
ATOM   6491 H H    . ALA   B 1 154 ? 44.092 -26.641 -8.594  1.00 13.35 ?  154 ALA   B H    1 
ATOM   6492 H HA   . ALA   B 1 154 ? 45.289 -28.356 -10.332 1.00 14.39 ?  154 ALA   B HA   1 
ATOM   6493 H HB1  . ALA   B 1 154 ? 47.324 -27.559 -9.510  1.00 15.64 ?  154 ALA   B HB1  1 
ATOM   6494 H HB2  . ALA   B 1 154 ? 46.467 -26.348 -10.079 1.00 15.64 ?  154 ALA   B HB2  1 
ATOM   6495 H HB3  . ALA   B 1 154 ? 46.549 -26.596 -8.512  1.00 15.64 ?  154 ALA   B HB3  1 
ATOM   6496 N N    . VAL   B 1 155 ? 45.480 -30.261 -8.822  1.00 12.03 ?  155 VAL   B N    1 
ATOM   6497 C CA   . VAL   B 1 155 ? 45.583 -31.406 -7.927  1.00 12.80 ?  155 VAL   B CA   1 
ATOM   6498 C C    . VAL   B 1 155 ? 46.921 -32.083 -8.201  1.00 12.55 ?  155 VAL   B C    1 
ATOM   6499 O O    . VAL   B 1 155 ? 47.157 -32.584 -9.308  1.00 14.35 ?  155 VAL   B O    1 
ATOM   6500 C CB   . VAL   B 1 155 ? 44.420 -32.395 -8.125  1.00 14.19 ?  155 VAL   B CB   1 
ATOM   6501 C CG1  . VAL   B 1 155 ? 44.587 -33.590 -7.202  1.00 14.29 ?  155 VAL   B CG1  1 
ATOM   6502 C CG2  . VAL   B 1 155 ? 43.077 -31.695 -7.889  1.00 14.71 ?  155 VAL   B CG2  1 
ATOM   6503 H H    . VAL   B 1 155 ? 45.514 -30.476 -9.656  1.00 14.41 ?  155 VAL   B H    1 
ATOM   6504 H HA   . VAL   B 1 155 ? 45.572 -31.104 -7.007  1.00 15.34 ?  155 VAL   B HA   1 
ATOM   6505 H HB   . VAL   B 1 155 ? 44.432 -32.717 -9.041  1.00 17.01 ?  155 VAL   B HB   1 
ATOM   6506 H HG11 . VAL   B 1 155 ? 43.757 -34.092 -7.178  1.00 17.12 ?  155 VAL   B HG11 1 
ATOM   6507 H HG12 . VAL   B 1 155 ? 45.302 -34.157 -7.538  1.00 17.12 ?  155 VAL   B HG12 1 
ATOM   6508 H HG13 . VAL   B 1 155 ? 44.808 -33.276 -6.311  1.00 17.12 ?  155 VAL   B HG13 1 
ATOM   6509 H HG21 . VAL   B 1 155 ? 42.361 -32.349 -7.971  1.00 17.63 ?  155 VAL   B HG21 1 
ATOM   6510 H HG22 . VAL   B 1 155 ? 43.071 -31.313 -6.998  1.00 17.63 ?  155 VAL   B HG22 1 
ATOM   6511 H HG23 . VAL   B 1 155 ? 42.960 -30.996 -8.551  1.00 17.63 ?  155 VAL   B HG23 1 
ATOM   6512 N N    . PHE   B 1 156 ? 47.784 -32.119 -7.185  1.00 13.26 ?  156 PHE   B N    1 
ATOM   6513 C CA   . PHE   B 1 156 ? 49.161 -32.579 -7.384  1.00 14.13 ?  156 PHE   B CA   1 
ATOM   6514 C C    . PHE   B 1 156 ? 49.255 -34.079 -7.667  1.00 15.27 ?  156 PHE   B C    1 
ATOM   6515 O O    . PHE   B 1 156 ? 49.980 -34.505 -8.576  1.00 17.03 ?  156 PHE   B O    1 
ATOM   6516 C CB   . PHE   B 1 156 ? 49.996 -32.213 -6.160  1.00 13.85 ?  156 PHE   B CB   1 
ATOM   6517 C CG   . PHE   B 1 156 ? 51.422 -32.678 -6.226  1.00 14.57 ?  156 PHE   B CG   1 
ATOM   6518 C CD1  . PHE   B 1 156 ? 52.300 -32.136 -7.143  1.00 16.20 ?  156 PHE   B CD1  1 
ATOM   6519 C CD2  . PHE   B 1 156 ? 51.889 -33.646 -5.356  1.00 15.14 ?  156 PHE   B CD2  1 
ATOM   6520 C CE1  . PHE   B 1 156 ? 53.626 -32.551 -7.194  1.00 16.94 ?  156 PHE   B CE1  1 
ATOM   6521 C CE2  . PHE   B 1 156 ? 53.209 -34.066 -5.405  1.00 16.64 ?  156 PHE   B CE2  1 
ATOM   6522 C CZ   . PHE   B 1 156 ? 54.069 -33.517 -6.328  1.00 17.02 ?  156 PHE   B CZ   1 
ATOM   6523 H H    . PHE   B 1 156 ? 47.597 -31.886 -6.377  1.00 15.89 ?  156 PHE   B H    1 
ATOM   6524 H HA   . PHE   B 1 156 ? 49.530 -32.114 -8.143  1.00 16.93 ?  156 PHE   B HA   1 
ATOM   6525 H HB2  . PHE   B 1 156 ? 50.005 -31.247 -6.071  1.00 16.59 ?  156 PHE   B HB2  1 
ATOM   6526 H HB3  . PHE   B 1 156 ? 49.593 -32.611 -5.373  1.00 16.59 ?  156 PHE   B HB3  1 
ATOM   6527 H HD1  . PHE   B 1 156 ? 52.007 -31.472 -7.731  1.00 19.42 ?  156 PHE   B HD1  1 
ATOM   6528 H HD2  . PHE   B 1 156 ? 51.304 -34.023 -4.736  1.00 18.14 ?  156 PHE   B HD2  1 
ATOM   6529 H HE1  . PHE   B 1 156 ? 54.213 -32.176 -7.817  1.00 20.30 ?  156 PHE   B HE1  1 
ATOM   6530 H HE2  . PHE   B 1 156 ? 53.504 -34.727 -4.819  1.00 19.95 ?  156 PHE   B HE2  1 
ATOM   6531 H HZ   . PHE   B 1 156 ? 54.956 -33.801 -6.362  1.00 20.40 ?  156 PHE   B HZ   1 
ATOM   6532 N N    . ASP   B 1 157 ? 48.594 -34.899 -6.862  1.00 15.91 ?  157 ASP   B N    1 
ATOM   6533 C CA   . ASP   B 1 157 ? 48.740 -36.347 -6.964  1.00 17.17 ?  157 ASP   B CA   1 
ATOM   6534 C C    . ASP   B 1 157 ? 47.824 -36.888 -8.057  1.00 17.52 ?  157 ASP   B C    1 
ATOM   6535 O O    . ASP   B 1 157 ? 46.601 -36.757 -7.960  1.00 16.96 ?  157 ASP   B O    1 
ATOM   6536 C CB   . ASP   B 1 157 ? 48.377 -36.963 -5.618  1.00 18.71 ?  157 ASP   B CB   1 
ATOM   6537 C CG   . ASP   B 1 157 ? 48.513 -38.469 -5.605  1.00 20.73 ?  157 ASP   B CG   1 
ATOM   6538 O OD1  . ASP   B 1 157 ? 48.848 -39.072 -6.654  1.00 21.35 ?  157 ASP   B OD1  1 
ATOM   6539 O OD2  . ASP   B 1 157 ? 48.297 -39.049 -4.523  1.00 22.60 -1 157 ASP   B OD2  1 
ATOM   6540 H H    . ASP   B 1 157 ? 48.058 -34.648 -6.243  1.00 19.07 ?  157 ASP   B H    1 
ATOM   6541 H HA   . ASP   B 1 157 ? 49.659 -36.581 -7.179  1.00 20.58 ?  157 ASP   B HA   1 
ATOM   6542 H HB2  . ASP   B 1 157 ? 48.956 -36.593 -4.935  1.00 22.43 ?  157 ASP   B HB2  1 
ATOM   6543 H HB3  . ASP   B 1 157 ? 47.452 -36.746 -5.414  1.00 22.43 ?  157 ASP   B HB3  1 
ATOM   6544 N N    . LYS   B 1 158 ? 48.415 -37.508 -9.086  1.00 18.57 ?  158 LYS   B N    1 
ATOM   6545 C CA   . LYS   B 1 158 ? 47.633 -38.113 -10.168 1.00 19.84 ?  158 LYS   B CA   1 
ATOM   6546 C C    . LYS   B 1 158 ? 46.569 -39.074 -9.638  1.00 19.82 ?  158 LYS   B C    1 
ATOM   6547 O O    . LYS   B 1 158 ? 45.464 -39.158 -10.190 1.00 19.87 ?  158 LYS   B O    1 
ATOM   6548 C CB   . LYS   B 1 158 ? 48.575 -38.827 -11.149 1.00 21.68 ?  158 LYS   B CB   1 
ATOM   6549 C CG   . LYS   B 1 158 ? 47.890 -39.715 -12.184 1.00 23.80 ?  158 LYS   B CG   1 
ATOM   6550 C CD   . LYS   B 1 158 ? 47.040 -38.915 -13.147 1.00 25.98 ?  158 LYS   B CD   1 
ATOM   6551 C CE   . LYS   B 1 158 ? 46.433 -39.820 -14.206 1.00 27.49 ?  158 LYS   B CE   1 
ATOM   6552 N NZ   . LYS   B 1 158 ? 45.370 -39.133 -14.992 1.00 27.75 ?  158 LYS   B NZ   1 
ATOM   6553 H H    . LYS   B 1 158 ? 49.269 -37.601 -9.177  1.00 22.26 ?  158 LYS   B H    1 
ATOM   6554 H HA   . LYS   B 1 158 ? 47.185 -37.409 -10.662 1.00 23.78 ?  158 LYS   B HA   1 
ATOM   6555 H HB2  . LYS   B 1 158 ? 49.084 -38.158 -11.641 1.00 25.99 ?  158 LYS   B HB2  1 
ATOM   6556 H HB3  . LYS   B 1 158 ? 49.186 -39.387 -10.646 1.00 25.99 ?  158 LYS   B HB3  1 
ATOM   6557 H HG2  . LYS   B 1 158 ? 48.570 -40.175 -12.702 1.00 28.54 ?  158 LYS   B HG2  1 
ATOM   6558 H HG3  . LYS   B 1 158 ? 47.324 -40.368 -11.742 1.00 28.54 ?  158 LYS   B HG3  1 
ATOM   6559 H HD2  . LYS   B 1 158 ? 46.320 -38.483 -12.663 1.00 31.15 ?  158 LYS   B HD2  1 
ATOM   6560 H HD3  . LYS   B 1 158 ? 47.593 -38.253 -13.593 1.00 31.15 ?  158 LYS   B HD3  1 
ATOM   6561 H HE2  . LYS   B 1 158 ? 47.126 -40.102 -14.821 1.00 32.96 ?  158 LYS   B HE2  1 
ATOM   6562 H HE3  . LYS   B 1 158 ? 46.035 -40.592 -13.774 1.00 32.96 ?  158 LYS   B HE3  1 
ATOM   6563 H HZ1  . LYS   B 1 158 ? 45.034 -39.687 -15.600 1.00 33.28 ?  158 LYS   B HZ1  1 
ATOM   6564 H HZ2  . LYS   B 1 158 ? 44.715 -38.866 -14.450 1.00 33.28 ?  158 LYS   B HZ2  1 
ATOM   6565 H HZ3  . LYS   B 1 158 ? 45.710 -38.421 -15.404 1.00 33.28 ?  158 LYS   B HZ3  1 
ATOM   6566 N N    . ASN   B 1 159 ? 46.888 -39.832 -8.588  1.00 20.24 ?  159 ASN   B N    1 
ATOM   6567 C CA   . ASN   B 1 159 ? 45.930 -40.814 -8.083  1.00 20.74 ?  159 ASN   B CA   1 
ATOM   6568 C C    . ASN   B 1 159 ? 44.734 -40.143 -7.406  1.00 19.60 ?  159 ASN   B C    1 
ATOM   6569 O O    . ASN   B 1 159 ? 43.597 -40.629 -7.513  1.00 19.52 ?  159 ASN   B O    1 
ATOM   6570 C CB   . ASN   B 1 159 ? 46.634 -41.791 -7.147  1.00 22.55 ?  159 ASN   B CB   1 
ATOM   6571 C CG   . ASN   B 1 159 ? 47.648 -42.645 -7.867  1.00 25.11 ?  159 ASN   B CG   1 
ATOM   6572 O OD1  . ASN   B 1 159 ? 47.387 -43.136 -8.970  1.00 26.46 ?  159 ASN   B OD1  1 
ATOM   6573 N ND2  . ASN   B 1 159 ? 48.819 -42.822 -7.256  1.00 25.75 ?  159 ASN   B ND2  1 
ATOM   6574 H H    . ASN   B 1 159 ? 47.634 -39.791 -8.166  1.00 24.26 ?  159 ASN   B H    1 
ATOM   6575 H HA   . ASN   B 1 159 ? 45.596 -41.322 -8.841  1.00 24.86 ?  159 ASN   B HA   1 
ATOM   6576 H HB2  . ASN   B 1 159 ? 47.094 -41.295 -6.456  1.00 27.04 ?  159 ASN   B HB2  1 
ATOM   6577 H HB3  . ASN   B 1 159 ? 45.971 -42.380 -6.759  1.00 27.04 ?  159 ASN   B HB3  1 
ATOM   6578 H HD21 . ASN   B 1 159 ? 49.434 -43.305 -7.623  1.00 30.87 ?  159 ASN   B HD21 1 
ATOM   6579 H HD22 . ASN   B 1 159 ? 48.961 -42.470 -6.484  1.00 30.87 ?  159 ASN   B HD22 1 
ATOM   6580 N N    . LEU   B 1 160 ? 44.957 -39.019 -6.718  1.00 18.20 ?  160 LEU   B N    1 
ATOM   6581 C CA   . LEU   B 1 160 ? 43.829 -38.280 -6.164  1.00 17.19 ?  160 LEU   B CA   1 
ATOM   6582 C C    . LEU   B 1 160 ? 43.037 -37.607 -7.271  1.00 16.16 ?  160 LEU   B C    1 
ATOM   6583 O O    . LEU   B 1 160 ? 41.798 -37.604 -7.241  1.00 15.83 ?  160 LEU   B O    1 
ATOM   6584 C CB   . LEU   B 1 160 ? 44.298 -37.251 -5.141  1.00 17.01 ?  160 LEU   B CB   1 
ATOM   6585 C CG   . LEU   B 1 160 ? 43.171 -36.347 -4.624  1.00 16.55 ?  160 LEU   B CG   1 
ATOM   6586 C CD1  . LEU   B 1 160 ? 42.050 -37.178 -4.004  1.00 17.14 ?  160 LEU   B CD1  1 
ATOM   6587 C CD2  . LEU   B 1 160 ? 43.706 -35.332 -3.625  1.00 16.54 ?  160 LEU   B CD2  1 
ATOM   6588 H H    . LEU   B 1 160 ? 45.732 -38.673 -6.572  1.00 21.82 ?  160 LEU   B H    1 
ATOM   6589 H HA   . LEU   B 1 160 ? 43.242 -38.911 -5.723  1.00 20.61 ?  160 LEU   B HA   1 
ATOM   6590 H HB2  . LEU   B 1 160 ? 44.682 -37.724 -4.386  1.00 20.39 ?  160 LEU   B HB2  1 
ATOM   6591 H HB3  . LEU   B 1 160 ? 44.974 -36.690 -5.555  1.00 20.39 ?  160 LEU   B HB3  1 
ATOM   6592 H HG   . LEU   B 1 160 ? 42.796 -35.857 -5.372  1.00 19.83 ?  160 LEU   B HG   1 
ATOM   6593 H HD11 . LEU   B 1 160 ? 41.428 -36.582 -3.565  1.00 20.54 ?  160 LEU   B HD11 1 
ATOM   6594 H HD12 . LEU   B 1 160 ? 41.595 -37.678 -4.701  1.00 20.54 ?  160 LEU   B HD12 1 
ATOM   6595 H HD13 . LEU   B 1 160 ? 42.434 -37.793 -3.356  1.00 20.54 ?  160 LEU   B HD13 1 
ATOM   6596 H HD21 . LEU   B 1 160 ? 42.977 -34.764 -3.341  1.00 19.83 ?  160 LEU   B HD21 1 
ATOM   6597 H HD22 . LEU   B 1 160 ? 44.080 -35.805 -2.867  1.00 19.83 ?  160 LEU   B HD22 1 
ATOM   6598 H HD23 . LEU   B 1 160 ? 44.394 -34.801 -4.058  1.00 19.83 ?  160 LEU   B HD23 1 
ATOM   6599 N N    . TYR   B 1 161 ? 43.735 -37.043 -8.263  1.00 16.54 ?  161 TYR   B N    1 
ATOM   6600 C CA   . TYR   B 1 161 ? 43.064 -36.475 -9.427  1.00 16.28 ?  161 TYR   B CA   1 
ATOM   6601 C C    . TYR   B 1 161 ? 42.114 -37.493 -10.045 1.00 16.21 ?  161 TYR   B C    1 
ATOM   6602 O O    . TYR   B 1 161 ? 40.943 -37.192 -10.300 1.00 15.97 ?  161 TYR   B O    1 
ATOM   6603 C CB   . TYR   B 1 161 ? 44.105 -36.003 -10.453 1.00 17.00 ?  161 TYR   B CB   1 
ATOM   6604 C CG   . TYR   B 1 161 ? 43.522 -35.529 -11.767 1.00 17.60 ?  161 TYR   B CG   1 
ATOM   6605 C CD1  . TYR   B 1 161 ? 43.132 -34.208 -11.936 1.00 17.49 ?  161 TYR   B CD1  1 
ATOM   6606 C CD2  . TYR   B 1 161 ? 43.345 -36.406 -12.834 1.00 18.13 ?  161 TYR   B CD2  1 
ATOM   6607 C CE1  . TYR   B 1 161 ? 42.596 -33.770 -13.122 1.00 18.58 ?  161 TYR   B CE1  1 
ATOM   6608 C CE2  . TYR   B 1 161 ? 42.803 -35.977 -14.026 1.00 19.27 ?  161 TYR   B CE2  1 
ATOM   6609 C CZ   . TYR   B 1 161 ? 42.435 -34.656 -14.166 1.00 19.35 ?  161 TYR   B CZ   1 
ATOM   6610 O OH   . TYR   B 1 161 ? 41.894 -34.217 -15.347 1.00 21.17 ?  161 TYR   B OH   1 
ATOM   6611 H H    . TYR   B 1 161 ? 44.588 -36.986 -8.291  1.00 19.82 ?  161 TYR   B H    1 
ATOM   6612 H HA   . TYR   B 1 161 ? 42.540 -35.707 -9.157  1.00 19.51 ?  161 TYR   B HA   1 
ATOM   6613 H HB2  . TYR   B 1 161 ? 44.601 -35.262 -10.073 1.00 20.38 ?  161 TYR   B HB2  1 
ATOM   6614 H HB3  . TYR   B 1 161 ? 44.707 -36.736 -10.650 1.00 20.38 ?  161 TYR   B HB3  1 
ATOM   6615 H HD1  . TYR   B 1 161 ? 43.244 -33.602 -11.238 1.00 20.96 ?  161 TYR   B HD1  1 
ATOM   6616 H HD2  . TYR   B 1 161 ? 43.589 -37.299 -12.744 1.00 21.73 ?  161 TYR   B HD2  1 
ATOM   6617 H HE1  . TYR   B 1 161 ? 42.346 -32.874 -13.218 1.00 22.28 ?  161 TYR   B HE1  1 
ATOM   6618 H HE2  . TYR   B 1 161 ? 42.688 -36.572 -14.733 1.00 23.10 ?  161 TYR   B HE2  1 
ATOM   6619 H HH   . TYR   B 1 161 ? 41.851 -34.851 -15.896 1.00 25.38 ?  161 TYR   B HH   1 
ATOM   6620 N N    . ASP   B 1 162 ? 42.603 -38.716 -10.274 1.00 16.60 ?  162 ASP   B N    1 
ATOM   6621 C CA   . ASP   B 1 162 ? 41.770 -39.746 -10.888 1.00 17.27 ?  162 ASP   B CA   1 
ATOM   6622 C C    . ASP   B 1 162 ? 40.567 -40.078 -10.014 1.00 16.72 ?  162 ASP   B C    1 
ATOM   6623 O O    . ASP   B 1 162 ? 39.462 -40.291 -10.525 1.00 16.98 ?  162 ASP   B O    1 
ATOM   6624 C CB   . ASP   B 1 162 ? 42.592 -41.012 -11.145 1.00 18.53 ?  162 ASP   B CB   1 
ATOM   6625 C CG   . ASP   B 1 162 ? 43.596 -40.849 -12.270 1.00 19.90 ?  162 ASP   B CG   1 
ATOM   6626 O OD1  . ASP   B 1 162 ? 43.466 -39.914 -13.083 1.00 20.24 ?  162 ASP   B OD1  1 
ATOM   6627 O OD2  . ASP   B 1 162 ? 44.511 -41.693 -12.355 1.00 21.58 -1 162 ASP   B OD2  1 
ATOM   6628 H H    . ASP   B 1 162 ? 43.402 -38.968 -10.086 1.00 19.90 ?  162 ASP   B H    1 
ATOM   6629 H HA   . ASP   B 1 162 ? 41.441 -39.426 -11.741 1.00 20.70 ?  162 ASP   B HA   1 
ATOM   6630 H HB2  . ASP   B 1 162 ? 43.083 -41.243 -10.342 1.00 22.21 ?  162 ASP   B HB2  1 
ATOM   6631 H HB3  . ASP   B 1 162 ? 41.994 -41.736 -11.390 1.00 22.21 ?  162 ASP   B HB3  1 
ATOM   6632 N N    . LYS   B 1 163 ? 40.765 -40.159 -8.698  1.00 16.20 ?  163 LYS   B N    1 
ATOM   6633 C CA   . LYS   B 1 163 ? 39.644 -40.435 -7.805  1.00 16.66 ?  163 LYS   B CA   1 
ATOM   6634 C C    . LYS   B 1 163 ? 38.603 -39.322 -7.862  1.00 15.48 ?  163 LYS   B C    1 
ATOM   6635 O O    . LYS   B 1 163 ? 37.391 -39.586 -7.850  1.00 16.34 ?  163 LYS   B O    1 
ATOM   6636 C CB   . LYS   B 1 163 ? 40.139 -40.618 -6.373  1.00 19.81 ?  163 LYS   B CB   1 
ATOM   6637 C CG   . LYS   B 1 163 ? 39.055 -41.110 -5.441  1.00 25.65 ?  163 LYS   B CG   1 
ATOM   6638 C CD   . LYS   B 1 163 ? 39.550 -41.339 -4.027  1.00 30.64 ?  163 LYS   B CD   1 
ATOM   6639 C CE   . LYS   B 1 163 ? 38.447 -41.962 -3.182  1.00 34.29 ?  163 LYS   B CE   1 
ATOM   6640 N NZ   . LYS   B 1 163 ? 38.515 -41.541 -1.757  1.00 36.57 ?  163 LYS   B NZ   1 
ATOM   6641 H H    . LYS   B 1 163 ? 41.523 -40.065 -8.309  1.00 19.41 ?  163 LYS   B H    1 
ATOM   6642 H HA   . LYS   B 1 163 ? 39.212 -41.259 -8.080  1.00 19.97 ?  163 LYS   B HA   1 
ATOM   6643 H HB2  . LYS   B 1 163 ? 40.859 -41.272 -6.370  1.00 23.75 ?  163 LYS   B HB2  1 
ATOM   6644 H HB3  . LYS   B 1 163 ? 40.462 -39.769 -6.038  1.00 23.75 ?  163 LYS   B HB3  1 
ATOM   6645 H HG2  . LYS   B 1 163 ? 38.344 -40.454 -5.404  1.00 30.75 ?  163 LYS   B HG2  1 
ATOM   6646 H HG3  . LYS   B 1 163 ? 38.708 -41.955 -5.776  1.00 30.75 ?  163 LYS   B HG3  1 
ATOM   6647 H HD2  . LYS   B 1 163 ? 40.306 -41.948 -4.042  1.00 36.74 ?  163 LYS   B HD2  1 
ATOM   6648 H HD3  . LYS   B 1 163 ? 39.802 -40.493 -3.630  1.00 36.74 ?  163 LYS   B HD3  1 
ATOM   6649 H HE2  . LYS   B 1 163 ? 37.584 -41.701 -3.539  1.00 41.12 ?  163 LYS   B HE2  1 
ATOM   6650 H HE3  . LYS   B 1 163 ? 38.535 -42.927 -3.212  1.00 41.12 ?  163 LYS   B HE3  1 
ATOM   6651 H HZ1  . LYS   B 1 163 ? 37.855 -41.922 -1.296  1.00 43.86 ?  163 LYS   B HZ1  1 
ATOM   6652 H HZ2  . LYS   B 1 163 ? 39.294 -41.786 -1.405  1.00 43.86 ?  163 LYS   B HZ2  1 
ATOM   6653 H HZ3  . LYS   B 1 163 ? 38.435 -40.657 -1.697  1.00 43.86 ?  163 LYS   B HZ3  1 
ATOM   6654 N N    . LEU   B 1 164 ? 39.063 -38.069 -7.918  1.00 14.37 ?  164 LEU   B N    1 
ATOM   6655 C CA   . LEU   B 1 164 ? 38.156 -36.927 -7.971  1.00 13.77 ?  164 LEU   B CA   1 
ATOM   6656 C C    . LEU   B 1 164 ? 37.372 -36.906 -9.276  1.00 14.04 ?  164 LEU   B C    1 
ATOM   6657 O O    . LEU   B 1 164 ? 36.148 -36.707 -9.276  1.00 15.52 ?  164 LEU   B O    1 
ATOM   6658 C CB   . LEU   B 1 164 ? 38.959 -35.635 -7.818  1.00 13.52 ?  164 LEU   B CB   1 
ATOM   6659 C CG   . LEU   B 1 164 ? 39.493 -35.351 -6.417  1.00 14.31 ?  164 LEU   B CG   1 
ATOM   6660 C CD1  . LEU   B 1 164 ? 40.576 -34.286 -6.465  1.00 14.51 ?  164 LEU   B CD1  1 
ATOM   6661 C CD2  . LEU   B 1 164 ? 38.374 -34.915 -5.491  1.00 16.03 ?  164 LEU   B CD2  1 
ATOM   6662 H H    . LEU   B 1 164 ? 39.902 -37.857 -7.936  1.00 17.21 ?  164 LEU   B H    1 
ATOM   6663 H HA   . LEU   B 1 164 ? 37.531 -36.983 -7.242  1.00 16.50 ?  164 LEU   B HA   1 
ATOM   6664 H HB2  . LEU   B 1 164 ? 39.726 -35.674 -8.418  1.00 16.20 ?  164 LEU   B HB2  1 
ATOM   6665 H HB3  . LEU   B 1 164 ? 38.395 -34.890 -8.070  1.00 16.20 ?  164 LEU   B HB3  1 
ATOM   6666 H HG   . LEU   B 1 164 ? 39.890 -36.157 -6.058  1.00 17.15 ?  164 LEU   B HG   1 
ATOM   6667 H HD11 . LEU   B 1 164 ? 40.900 -34.116 -5.563  1.00 17.39 ?  164 LEU   B HD11 1 
ATOM   6668 H HD12 . LEU   B 1 164 ? 41.314 -34.601 -7.018  1.00 17.39 ?  164 LEU   B HD12 1 
ATOM   6669 H HD13 . LEU   B 1 164 ? 40.213 -33.470 -6.842  1.00 17.39 ?  164 LEU   B HD13 1 
ATOM   6670 H HD21 . LEU   B 1 164 ? 38.749 -34.678 -4.630  1.00 19.22 ?  164 LEU   B HD21 1 
ATOM   6671 H HD22 . LEU   B 1 164 ? 37.923 -34.148 -5.879  1.00 19.22 ?  164 LEU   B HD22 1 
ATOM   6672 H HD23 . LEU   B 1 164 ? 37.749 -35.650 -5.390  1.00 19.22 ?  164 LEU   B HD23 1 
ATOM   6673 N N    . VAL   B 1 165 ? 38.060 -37.084 -10.404 1.00 15.84 ?  165 VAL   B N    1 
ATOM   6674 C CA   . VAL   B 1 165 ? 37.399 -37.018 -11.702 1.00 17.16 ?  165 VAL   B CA   1 
ATOM   6675 C C    . VAL   B 1 165 ? 36.480 -38.219 -11.888 1.00 19.45 ?  165 VAL   B C    1 
ATOM   6676 O O    . VAL   B 1 165 ? 35.319 -38.082 -12.296 1.00 20.58 ?  165 VAL   B O    1 
ATOM   6677 C CB   . VAL   B 1 165 ? 38.438 -36.928 -12.834 1.00 18.38 ?  165 VAL   B CB   1 
ATOM   6678 C CG1  . VAL   B 1 165 ? 37.762 -37.035 -14.182 1.00 19.52 ?  165 VAL   B CG1  1 
ATOM   6679 C CG2  . VAL   B 1 165 ? 39.229 -35.636 -12.728 1.00 18.24 ?  165 VAL   B CG2  1 
ATOM   6680 H H    . VAL   B 1 165 ? 38.907 -37.246 -10.445 1.00 18.99 ?  165 VAL   B H    1 
ATOM   6681 H HA   . VAL   B 1 165 ? 36.851 -36.222 -11.738 1.00 20.56 ?  165 VAL   B HA   1 
ATOM   6682 H HB   . VAL   B 1 165 ? 39.065 -37.662 -12.749 1.00 22.03 ?  165 VAL   B HB   1 
ATOM   6683 H HG11 . VAL   B 1 165 ? 38.367 -36.713 -14.865 1.00 23.40 ?  165 VAL   B HG11 1 
ATOM   6684 H HG12 . VAL   B 1 165 ? 37.547 -37.967 -14.350 1.00 23.40 ?  165 VAL   B HG12 1 
ATOM   6685 H HG13 . VAL   B 1 165 ? 36.953 -36.504 -14.174 1.00 23.40 ?  165 VAL   B HG13 1 
ATOM   6686 H HG21 . VAL   B 1 165 ? 39.858 -35.586 -13.466 1.00 21.87 ?  165 VAL   B HG21 1 
ATOM   6687 H HG22 . VAL   B 1 165 ? 38.615 -34.883 -12.769 1.00 21.87 ?  165 VAL   B HG22 1 
ATOM   6688 H HG23 . VAL   B 1 165 ? 39.708 -35.621 -11.884 1.00 21.87 ?  165 VAL   B HG23 1 
ATOM   6689 N N    . SER   B 1 166 ? 36.995 -39.421 -11.597 1.00 20.42 ?  166 SER   B N    1 
ATOM   6690 C CA   . SER   B 1 166 ? 36.244 -40.638 -11.878 1.00 21.82 ?  166 SER   B CA   1 
ATOM   6691 C C    . SER   B 1 166 ? 34.977 -40.718 -11.041 1.00 22.20 ?  166 SER   B C    1 
ATOM   6692 O O    . SER   B 1 166 ? 34.002 -41.335 -11.469 1.00 23.48 ?  166 SER   B O    1 
ATOM   6693 C CB   . SER   B 1 166 ? 37.115 -41.890 -11.684 1.00 22.92 ?  166 SER   B CB   1 
ATOM   6694 O OG   . SER   B 1 166 ? 37.451 -42.096 -10.320 1.00 23.16 ?  166 SER   B OG   1 
ATOM   6695 H H    . SER   B 1 166 ? 37.777 -39.553 -11.245 1.00 24.49 ?  166 SER   B H    1 
ATOM   6696 H HA   . SER   B 1 166 ? 35.983 -40.625 -12.809 1.00 26.16 ?  166 SER   B HA   1 
ATOM   6697 H HB2  . SER   B 1 166 ? 36.629 -42.665 -12.007 1.00 27.48 ?  166 SER   B HB2  1 
ATOM   6698 H HB3  . SER   B 1 166 ? 37.938 -41.787 -12.195 1.00 27.48 ?  166 SER   B HB3  1 
ATOM   6699 H HG   . SER   B 1 166 ? 37.880 -41.437 -10.031 1.00 27.76 ?  166 SER   B HG   1 
ATOM   6700 N N    . SER   B 1 167 ? 34.959 -40.106 -9.859  1.00 20.54 ?  167 SER   B N    1 
ATOM   6701 C CA   . SER   B 1 167 ? 33.799 -40.159 -8.976  1.00 20.10 ?  167 SER   B CA   1 
ATOM   6702 C C    . SER   B 1 167 ? 32.888 -38.934 -9.074  1.00 19.44 ?  167 SER   B C    1 
ATOM   6703 O O    . SER   B 1 167 ? 31.808 -38.936 -8.470  1.00 19.72 ?  167 SER   B O    1 
ATOM   6704 C CB   . SER   B 1 167 ? 34.238 -40.345 -7.516  1.00 20.19 ?  167 SER   B CB   1 
ATOM   6705 O OG   . SER   B 1 167 ? 34.907 -39.182 -7.035  1.00 20.19 ?  167 SER   B OG   1 
ATOM   6706 H H    . SER   B 1 167 ? 35.617 -39.661 -9.542  1.00 24.62 ?  167 SER   B H    1 
ATOM   6707 H HA   . SER   B 1 167 ? 33.266 -40.934 -9.219  1.00 24.10 ?  167 SER   B HA   1 
ATOM   6708 H HB2  . SER   B 1 167 ? 33.449 -40.512 -6.973  1.00 24.20 ?  167 SER   B HB2  1 
ATOM   6709 H HB3  . SER   B 1 167 ? 34.832 -41.118 -7.467  1.00 24.20 ?  167 SER   B HB3  1 
ATOM   6710 H HG   . SER   B 1 167 ? 35.600 -39.058 -7.486  1.00 24.20 ?  167 SER   B HG   1 
ATOM   6711 N N    . PHE   B 1 168 ? 33.276 -37.892 -9.815  1.00 19.18 ?  168 PHE   B N    1 
ATOM   6712 C CA   . PHE   B 1 168 ? 32.442 -36.690 -9.878  1.00 18.12 ?  168 PHE   B CA   1 
ATOM   6713 C C    . PHE   B 1 168 ? 31.126 -36.949 -10.607 1.00 15.55 ?  168 PHE   B C    1 
ATOM   6714 O O    . PHE   B 1 168 ? 30.085 -36.357 -10.263 1.00 16.09 ?  168 PHE   B O    1 
ATOM   6715 C CB   . PHE   B 1 168 ? 33.204 -35.552 -10.559 1.00 18.50 ?  168 PHE   B CB   1 
ATOM   6716 C CG   . PHE   B 1 168 ? 32.391 -34.306 -10.721 1.00 18.52 ?  168 PHE   B CG   1 
ATOM   6717 C CD1  . PHE   B 1 168 ? 32.031 -33.557 -9.610  1.00 19.81 ?  168 PHE   B CD1  1 
ATOM   6718 C CD2  . PHE   B 1 168 ? 31.960 -33.897 -11.968 1.00 17.94 ?  168 PHE   B CD2  1 
ATOM   6719 C CE1  . PHE   B 1 168 ? 31.266 -32.413 -9.738  1.00 20.22 ?  168 PHE   B CE1  1 
ATOM   6720 C CE2  . PHE   B 1 168 ? 31.206 -32.736 -12.109 1.00 19.05 ?  168 PHE   B CE2  1 
ATOM   6721 C CZ   . PHE   B 1 168 ? 30.850 -31.997 -10.989 1.00 19.55 ?  168 PHE   B CZ   1 
ATOM   6722 H H    . PHE   B 1 168 ? 34.004 -37.854 -10.273 1.00 22.99 ?  168 PHE   B H    1 
ATOM   6723 H HA   . PHE   B 1 168 ? 32.227 -36.411 -8.979  1.00 21.72 ?  168 PHE   B HA   1 
ATOM   6724 H HB2  . PHE   B 1 168 ? 33.981 -35.333 -10.023 1.00 22.17 ?  168 PHE   B HB2  1 
ATOM   6725 H HB3  . PHE   B 1 168 ? 33.482 -35.841 -11.442 1.00 22.17 ?  168 PHE   B HB3  1 
ATOM   6726 H HD1  . PHE   B 1 168 ? 32.303 -33.835 -8.767  1.00 23.75 ?  168 PHE   B HD1  1 
ATOM   6727 H HD2  . PHE   B 1 168 ? 32.196 -34.383 -12.722 1.00 21.50 ?  168 PHE   B HD2  1 
ATOM   6728 H HE1  . PHE   B 1 168 ? 31.032 -31.924 -8.986  1.00 24.23 ?  168 PHE   B HE1  1 
ATOM   6729 H HE2  . PHE   B 1 168 ? 30.919 -32.464 -12.955 1.00 22.84 ?  168 PHE   B HE2  1 
ATOM   6730 H HZ   . PHE   B 1 168 ? 30.334 -31.228 -11.082 1.00 23.44 ?  168 PHE   B HZ   1 
ATOM   6731 N N    . LEU   B 1 169 ? 31.161 -37.818 -11.615 1.00 15.61 ?  169 LEU   B N    1 
ATOM   6732 C CA   . LEU   B 1 169 ? 29.981 -38.143 -12.409 1.00 18.06 ?  169 LEU   B CA   1 
ATOM   6733 C C    . LEU   B 1 169 ? 29.979 -39.582 -12.899 1.00 20.86 ?  169 LEU   B C    1 
ATOM   6734 O O    . LEU   B 1 169 ? 29.069 -40.011 -13.610 1.00 23.16 ?  169 LEU   B O    1 
ATOM   6735 C CB   . LEU   B 1 169 ? 29.899 -37.218 -13.620 1.00 19.92 ?  169 LEU   B CB   1 
ATOM   6736 C CG   . LEU   B 1 169 ? 28.650 -36.349 -13.736 1.00 22.95 ?  169 LEU   B CG   1 
ATOM   6737 C CD1  . LEU   B 1 169 ? 28.580 -35.776 -15.129 1.00 23.73 ?  169 LEU   B CD1  1 
ATOM   6738 C CD2  . LEU   B 1 169 ? 27.392 -37.133 -13.413 1.00 23.08 ?  169 LEU   B CD2  1 
ATOM   6739 O OXT  . LEU   B 1 169 ? 30.901 -40.336 -12.612 1.00 21.89 -1 169 LEU   B OXT  1 
ATOM   6740 H H    . LEU   B 1 169 ? 31.872 -38.230 -11.877 1.00 18.70 ?  169 LEU   B H    1 
ATOM   6741 H HA   . LEU   B 1 169 ? 29.200 -38.006 -11.857 1.00 21.64 ?  169 LEU   B HA   1 
ATOM   6742 H HB2  . LEU   B 1 169 ? 30.661 -36.620 -13.605 1.00 23.88 ?  169 LEU   B HB2  1 
ATOM   6743 H HB3  . LEU   B 1 169 ? 29.936 -37.763 -14.423 1.00 23.88 ?  169 LEU   B HB3  1 
ATOM   6744 H HG   . LEU   B 1 169 ? 28.714 -35.609 -13.110 1.00 27.51 ?  169 LEU   B HG   1 
ATOM   6745 H HD11 . LEU   B 1 169 ? 27.809 -35.192 -15.191 1.00 28.45 ?  169 LEU   B HD11 1 
ATOM   6746 H HD12 . LEU   B 1 169 ? 29.392 -35.276 -15.302 1.00 28.45 ?  169 LEU   B HD12 1 
ATOM   6747 H HD13 . LEU   B 1 169 ? 28.497 -36.505 -15.762 1.00 28.45 ?  169 LEU   B HD13 1 
ATOM   6748 H HD21 . LEU   B 1 169 ? 26.636 -36.720 -13.854 1.00 27.67 ?  169 LEU   B HD21 1 
ATOM   6749 H HD22 . LEU   B 1 169 ? 27.502 -38.046 -13.730 1.00 27.67 ?  169 LEU   B HD22 1 
ATOM   6750 H HD23 . LEU   B 1 169 ? 27.259 -37.133 -12.453 1.00 27.67 ?  169 LEU   B HD23 1 
HETATM 6751 C C1   T TFA   C 2 .   ? 12.154 -1.396  1.373   0.20 10.77 ?  201 TFA   A C1   1 
HETATM 6752 C C2   T TFA   C 2 .   ? 12.808 -1.798  0.024   0.20 12.75 ?  201 TFA   A C2   1 
HETATM 6753 O O    T TFA   C 2 .   ? 12.895 -1.566  2.350   0.20 10.15 ?  201 TFA   A O    1 
HETATM 6754 F F1   T TFA   C 2 .   ? 12.928 -3.136  -0.080  0.20 13.12 ?  201 TFA   A F1   1 
HETATM 6755 F F2   T TFA   C 2 .   ? 12.079 -1.400  -1.032  0.20 13.17 ?  201 TFA   A F2   1 
HETATM 6756 F F3   T TFA   C 2 .   ? 14.030 -1.286  -0.144  0.20 14.10 ?  201 TFA   A F3   1 
HETATM 6757 O OXT  T TFA   C 2 .   ? 11.000 -0.966  1.292   0.20 9.63  ?  201 TFA   A OXT  1 
HETATM 6758 O O1   B A1A66 D 3 .   ? 15.621 -2.237  -0.017  0.26 10.17 ?  202 A1A66 A O1   1 
HETATM 6759 C C1   B A1A66 D 3 .   ? 15.983 -1.108  0.731   0.26 8.77  ?  202 A1A66 A C1   1 
HETATM 6760 C C2   B A1A66 D 3 .   ? 14.675 -0.297  0.937   0.26 9.50  ?  202 A1A66 A C2   1 
HETATM 6761 C C3   B A1A66 D 3 .   ? 14.184 0.227   -0.425  0.26 10.52 ?  202 A1A66 A C3   1 
HETATM 6762 C C4   B A1A66 D 3 .   ? 14.648 1.663   -0.522  0.26 11.28 ?  202 A1A66 A C4   1 
HETATM 6763 C C5   B A1A66 D 3 .   ? 15.524 2.094   -1.673  0.26 12.75 ?  202 A1A66 A C5   1 
HETATM 6764 C C6   B A1A66 D 3 .   ? 14.097 2.580   -1.589  0.26 12.38 ?  202 A1A66 A C6   1 
HETATM 6765 C C7   B A1A66 D 3 .   ? 14.993 2.100   0.862   0.26 9.80  ?  202 A1A66 A C7   1 
HETATM 6766 C C8   B A1A66 D 3 .   ? 15.083 0.972   3.108   0.26 9.84  ?  202 A1A66 A C8   1 
HETATM 6767 C C10  B A1A66 D 3 .   ? 15.362 2.038   5.259   0.26 10.25 ?  202 A1A66 A C10  1 
HETATM 6768 C C11  B A1A66 D 3 .   ? 15.313 2.174   3.847   0.26 10.01 ?  202 A1A66 A C11  1 
HETATM 6769 C C12  B A1A66 D 3 .   ? 15.535 3.578   3.632   0.26 10.22 ?  202 A1A66 A C12  1 
HETATM 6770 C C13  B A1A66 D 3 .   ? 15.692 4.221   4.849   0.26 10.43 ?  202 A1A66 A C13  1 
HETATM 6771 C C9   B A1A66 D 3 .   ? 15.007 -0.174  5.143   0.26 10.80 ?  202 A1A66 A C9   1 
HETATM 6772 N N1   B A1A66 D 3 .   ? 15.012 0.909   1.725   0.26 9.29  ?  202 A1A66 A N1   1 
HETATM 6773 N N2   B A1A66 D 3 .   ? 14.945 -0.207  3.778   0.26 10.47 ?  202 A1A66 A N2   1 
HETATM 6774 N N3   B A1A66 D 3 .   ? 15.208 0.876   5.930   0.26 10.64 ?  202 A1A66 A N3   1 
HETATM 6775 N N4   B A1A66 D 3 .   ? 15.585 3.264   5.858   0.26 10.29 ?  202 A1A66 A N4   1 
HETATM 6776 H H2   B A1A66 D 3 .   ? 16.443 -2.614  -0.321  0.26 12.18 ?  202 A1A66 A H2   1 
HETATM 6777 H H4   B A1A66 D 3 .   ? 16.443 -1.419  1.691   0.26 10.50 ?  202 A1A66 A H4   1 
HETATM 6778 H H3   B A1A66 D 3 .   ? 16.747 -0.492  0.202   0.26 10.50 ?  202 A1A66 A H3   1 
HETATM 6779 H H1   B A1A66 D 3 .   ? 13.898 -0.971  1.385   0.26 11.38 ?  202 A1A66 A H1   1 
HETATM 6780 H H6   B A1A66 D 3 .   ? 14.557 -0.374  -1.289  0.26 12.61 ?  202 A1A66 A H6   1 
HETATM 6781 H H5   B A1A66 D 3 .   ? 13.085 0.141   -0.552  0.26 12.61 ?  202 A1A66 A H5   1 
HETATM 6782 H H8   B A1A66 D 3 .   ? 16.296 2.814   -1.631  0.26 15.28 ?  202 A1A66 A H8   1 
HETATM 6783 H H7   B A1A66 D 3 .   ? 15.847 1.376   -2.386  0.26 15.28 ?  202 A1A66 A H7   1 
HETATM 6784 H H10  B A1A66 D 3 .   ? 13.904 3.639   -1.383  0.26 14.83 ?  202 A1A66 A H10  1 
HETATM 6785 H H9   B A1A66 D 3 .   ? 13.332 2.260   -2.311  0.26 14.83 ?  202 A1A66 A H9   1 
HETATM 6786 H H12  B A1A66 D 3 .   ? 15.940 2.659   0.859   0.26 11.74 ?  202 A1A66 A H12  1 
HETATM 6787 H H11  B A1A66 D 3 .   ? 14.188 2.750   1.238   0.26 11.74 ?  202 A1A66 A H11  1 
HETATM 6788 H H14  B A1A66 D 3 .   ? 15.564 4.072   2.689   0.26 12.23 ?  202 A1A66 A H14  1 
HETATM 6789 H H15  B A1A66 D 3 .   ? 15.864 5.256   5.091   0.26 12.49 ?  202 A1A66 A H15  1 
HETATM 6790 H H13  B A1A66 D 3 .   ? 14.890 -1.088  5.765   0.26 12.93 ?  202 A1A66 A H13  1 
HETATM 6791 H H16  B A1A66 D 3 .   ? 15.659 3.427   6.872   0.26 12.33 ?  202 A1A66 A H16  1 
HETATM 6792 O O1   C A1A66 E 3 .   ? 15.705 -2.275  -0.106  0.26 11.81 ?  203 A1A66 A O1   1 
HETATM 6793 C C1   C A1A66 E 3 .   ? 16.086 -0.996  0.333   0.26 10.86 ?  203 A1A66 A C1   1 
HETATM 6794 C C2   C A1A66 E 3 .   ? 14.802 -0.357  0.924   0.26 10.19 ?  203 A1A66 A C2   1 
HETATM 6795 C C3   C A1A66 E 3 .   ? 13.848 0.071   -0.212  0.26 10.39 ?  203 A1A66 A C3   1 
HETATM 6796 C C4   C A1A66 E 3 .   ? 13.633 1.542   -0.069  0.26 10.42 ?  203 A1A66 A C4   1 
HETATM 6797 C C5   C A1A66 E 3 .   ? 13.032 2.363   -1.203  0.26 10.63 ?  203 A1A66 A C5   1 
HETATM 6798 C C6   C A1A66 E 3 .   ? 12.208 2.067   0.019   0.26 10.53 ?  203 A1A66 A C6   1 
HETATM 6799 C C7   C A1A66 E 3 .   ? 14.745 2.047   0.818   0.26 9.50  ?  203 A1A66 A C7   1 
HETATM 6800 C C8   C A1A66 E 3 .   ? 15.197 0.961   3.060   0.26 9.33  ?  203 A1A66 A C8   1 
HETATM 6801 C C10  C A1A66 E 3 .   ? 15.361 2.020   5.241   0.26 9.20  ?  203 A1A66 A C10  1 
HETATM 6802 C C11  C A1A66 E 3 .   ? 15.376 2.155   3.817   0.26 9.15  ?  203 A1A66 A C11  1 
HETATM 6803 C C12  C A1A66 E 3 .   ? 15.599 3.558   3.599   0.26 9.03  ?  203 A1A66 A C12  1 
HETATM 6804 C C13  C A1A66 E 3 .   ? 15.690 4.209   4.815   0.26 9.23  ?  203 A1A66 A C13  1 
HETATM 6805 C C9   C A1A66 E 3 .   ? 15.034 -0.187  5.111   0.26 9.81  ?  203 A1A66 A C9   1 
HETATM 6806 N N1   C A1A66 E 3 .   ? 15.188 0.894   1.650   0.26 9.58  ?  203 A1A66 A N1   1 
HETATM 6807 N N2   C A1A66 E 3 .   ? 15.040 -0.213  3.736   0.26 9.39  ?  203 A1A66 A N2   1 
HETATM 6808 N N3   C A1A66 E 3 .   ? 15.187 0.856   5.933   0.26 9.64  ?  203 A1A66 A N3   1 
HETATM 6809 N N4   C A1A66 E 3 .   ? 15.544 3.255   5.829   0.26 9.09  ?  203 A1A66 A N4   1 
HETATM 6810 H H2   C A1A66 E 3 .   ? 16.433 -2.593  -0.626  0.26 14.15 ?  203 A1A66 A H2   1 
HETATM 6811 H H4   C A1A66 E 3 .   ? 16.501 -0.416  -0.519  0.26 13.00 ?  203 A1A66 A H4   1 
HETATM 6812 H H3   C A1A66 E 3 .   ? 16.890 -1.041  1.102   0.26 13.00 ?  203 A1A66 A H3   1 
HETATM 6813 H H1   C A1A66 E 3 .   ? 14.284 -1.127  1.542   0.26 12.21 ?  203 A1A66 A H1   1 
HETATM 6814 H H6   C A1A66 E 3 .   ? 14.242 -0.147  -1.222  0.26 12.45 ?  203 A1A66 A H6   1 
HETATM 6815 H H5   C A1A66 E 3 .   ? 12.886 -0.477  -0.207  0.26 12.45 ?  203 A1A66 A H5   1 
HETATM 6816 H H8   C A1A66 E 3 .   ? 12.746 1.948   -2.168  0.26 12.73 ?  203 A1A66 A H8   1 
HETATM 6817 H H7   C A1A66 E 3 .   ? 13.330 3.404   -1.396  0.26 12.73 ?  203 A1A66 A H7   1 
HETATM 6818 H H10  C A1A66 E 3 .   ? 11.330 1.424   -0.077  0.26 12.61 ?  203 A1A66 A H10  1 
HETATM 6819 H H9   C A1A66 E 3 .   ? 11.917 2.902   0.675   0.26 12.61 ?  203 A1A66 A H9   1 
HETATM 6820 H H12  C A1A66 E 3 .   ? 14.428 2.929   1.389   0.26 11.38 ?  203 A1A66 A H12  1 
HETATM 6821 H H11  C A1A66 E 3 .   ? 15.611 2.335   0.195   0.26 11.38 ?  203 A1A66 A H11  1 
HETATM 6822 H H14  C A1A66 E 3 .   ? 15.662 4.048   2.645   0.26 10.81 ?  203 A1A66 A H14  1 
HETATM 6823 H H15  C A1A66 E 3 .   ? 15.841 5.246   5.053   0.26 11.05 ?  203 A1A66 A H15  1 
HETATM 6824 H H13  C A1A66 E 3 .   ? 14.896 -1.111  5.703   0.26 11.74 ?  203 A1A66 A H13  1 
HETATM 6825 H H16  C A1A66 E 3 .   ? 15.571 3.423   6.838   0.26 10.88 ?  203 A1A66 A H16  1 
HETATM 6826 O O    A HOH   F 4 .   ? 14.782 -4.614  20.383  0.48 31.89 ?  301 HOH   A O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 11.922 -10.880 -10.049 1.00 51.41 ?  302 HOH   A O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 34.360 -1.834  12.556  1.00 38.07 ?  303 HOH   A O    1 
HETATM 6829 O O    . HOH   F 4 .   ? -0.442 -2.984  2.968   1.00 42.71 ?  304 HOH   A O    1 
HETATM 6830 O O    B HOH   F 4 .   ? 10.853 -1.001  1.923   0.52 17.59 ?  305 HOH   A O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 14.863 3.936   17.386  1.00 39.40 ?  306 HOH   A O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 29.021 0.406   -9.758  1.00 20.44 ?  307 HOH   A O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 17.199 -18.087 14.931  1.00 27.55 ?  308 HOH   A O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 14.248 -4.460  -11.954 1.00 41.13 ?  309 HOH   A O    1 
HETATM 6835 O O    A HOH   F 4 .   ? 4.730  3.898   0.555   0.48 19.74 ?  310 HOH   A O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 9.277  -10.149 19.357  1.00 42.07 ?  311 HOH   A O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 10.938 1.658   12.229  1.00 21.97 ?  312 HOH   A O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 9.939  -21.452 5.670   1.00 19.25 ?  313 HOH   A O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 14.673 -13.874 16.707  1.00 25.41 ?  314 HOH   A O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 11.913 0.357   14.566  1.00 32.28 ?  315 HOH   A O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 15.062 -12.243 18.642  1.00 40.51 ?  316 HOH   A O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 8.143  -21.529 4.017   1.00 49.94 ?  317 HOH   A O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 22.522 -11.883 21.874  1.00 51.39 ?  318 HOH   A O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 42.396 10.546  5.086   1.00 19.27 ?  319 HOH   A O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 28.116 -6.219  19.584  1.00 41.56 ?  320 HOH   A O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 0.746  -4.657  -0.009  1.00 34.47 ?  321 HOH   A O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 13.378 -1.479  -6.843  1.00 23.33 ?  322 HOH   A O    1 
HETATM 6848 O O    B HOH   F 4 .   ? 14.879 -3.027  3.228   0.52 11.18 ?  323 HOH   A O    1 
HETATM 6849 O O    A HOH   F 4 .   ? 6.962  -8.178  11.795  0.48 14.27 ?  324 HOH   A O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 30.342 -13.320 -8.502  1.00 20.25 ?  325 HOH   A O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 10.380 -22.176 -1.232  1.00 53.63 ?  326 HOH   A O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 22.216 5.389   18.906  1.00 45.63 ?  327 HOH   A O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 25.826 -0.874  -7.475  1.00 18.22 ?  328 HOH   A O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 36.210 -5.104  -0.470  1.00 31.93 ?  329 HOH   A O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 30.868 6.214   -12.213 1.00 26.30 ?  330 HOH   A O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 7.632  -6.308  -6.706  1.00 41.46 ?  331 HOH   A O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 44.298 7.204   6.464   1.00 26.43 ?  332 HOH   A O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 31.045 -18.111 7.820   1.00 18.80 ?  333 HOH   A O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 38.265 10.327  7.109   1.00 47.43 ?  334 HOH   A O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 7.983  -12.754 -1.080  1.00 22.80 ?  335 HOH   A O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 20.737 -19.767 -5.066  1.00 28.14 ?  336 HOH   A O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 26.551 -19.344 -1.758  1.00 13.62 ?  337 HOH   A O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 18.719 -19.376 13.567  1.00 39.09 ?  338 HOH   A O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 37.498 2.802   10.305  1.00 25.99 ?  339 HOH   A O    1 
HETATM 6865 O O    A HOH   F 4 .   ? 28.290 -0.217  -13.347 0.48 22.05 ?  340 HOH   A O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 20.059 -12.644 -8.807  1.00 24.86 ?  341 HOH   A O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 27.333 13.784  2.866   1.00 28.86 ?  342 HOH   A O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 14.502 -21.239 -4.277  1.00 29.18 ?  343 HOH   A O    1 
HETATM 6869 O O    A HOH   F 4 .   ? 14.298 0.556   6.760   0.48 21.14 ?  344 HOH   A O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 18.988 -21.988 6.849   1.00 34.32 ?  345 HOH   A O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 38.551 5.008   7.081   1.00 14.23 ?  346 HOH   A O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 34.049 -1.040  -8.879  1.00 25.56 ?  347 HOH   A O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 18.519 9.515   8.898   1.00 20.67 ?  348 HOH   A O    1 
HETATM 6874 O O    B HOH   F 4 .   ? 15.261 6.860   7.067   0.52 17.75 ?  349 HOH   A O    1 
HETATM 6875 O O    B HOH   F 4 .   ? 11.205 6.415   8.975   0.52 24.65 ?  350 HOH   A O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 42.549 4.316   5.499   1.00 32.77 ?  351 HOH   A O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 13.617 -15.279 -7.570  1.00 26.72 ?  352 HOH   A O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 26.859 11.417  1.666   1.00 15.31 ?  353 HOH   A O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 22.162 -19.319 11.386  1.00 33.58 ?  354 HOH   A O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 43.347 7.764   2.720   1.00 31.39 ?  355 HOH   A O    1 
HETATM 6881 O O    A HOH   F 4 .   ? 3.617  -9.481  9.670   0.48 22.26 ?  356 HOH   A O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 39.803 -1.043  -5.115  1.00 21.17 ?  357 HOH   A O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 5.340  2.551   4.898   1.00 33.55 ?  358 HOH   A O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 21.350 -2.257  -2.540  1.00 16.09 ?  359 HOH   A O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 17.067 -19.306 4.871   1.00 14.39 ?  360 HOH   A O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 35.818 -12.648 6.871   1.00 14.87 ?  361 HOH   A O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 30.776 3.096   8.305   1.00 11.15 ?  362 HOH   A O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 31.659 8.203   14.900  1.00 24.08 ?  363 HOH   A O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 24.089 -2.133  -2.158  1.00 10.88 ?  364 HOH   A O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 19.377 -11.131 24.109  1.00 78.80 ?  365 HOH   A O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 27.987 0.804   -7.182  1.00 13.63 ?  366 HOH   A O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 31.162 -13.955 -2.431  1.00 12.94 ?  367 HOH   A O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 17.251 -17.879 -5.104  1.00 27.81 ?  368 HOH   A O    1 
HETATM 6894 O O    A HOH   F 4 .   ? 14.667 -3.672  3.059   0.48 18.06 ?  369 HOH   A O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 21.953 -21.917 8.494   1.00 28.36 ?  370 HOH   A O    1 
HETATM 6896 O O    B HOH   F 4 .   ? 13.320 -3.331  -1.082  0.52 17.97 ?  371 HOH   A O    1 
HETATM 6897 O O    A HOH   F 4 .   ? 17.533 -1.732  0.410   0.48 19.02 ?  372 HOH   A O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 22.737 12.472  1.575   1.00 13.88 ?  373 HOH   A O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 33.663 -7.141  4.376   1.00 15.56 ?  374 HOH   A O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 37.279 11.993  4.974   1.00 25.42 ?  375 HOH   A O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 14.427 -24.641 11.570  1.00 38.30 ?  376 HOH   A O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 37.207 -2.902  9.781   1.00 47.96 ?  377 HOH   A O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 27.426 -10.568 14.125  1.00 15.98 ?  378 HOH   A O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 16.598 -22.097 0.974   1.00 28.54 ?  379 HOH   A O    1 
HETATM 6905 O O    T HOH   F 4 .   ? 15.440 -0.440  2.349   0.20 11.35 ?  380 HOH   A O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 18.943 -0.717  -1.782  1.00 18.85 ?  381 HOH   A O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 24.414 3.584   -1.817  1.00 15.38 ?  382 HOH   A O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 27.639 -6.297  -14.012 1.00 36.40 ?  383 HOH   A O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 43.864 8.463   -3.045  1.00 29.44 ?  384 HOH   A O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 21.135 10.145  15.015  1.00 34.27 ?  385 HOH   A O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 24.701 -17.504 12.775  1.00 23.91 ?  386 HOH   A O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 21.376 3.017   -0.282  1.00 12.65 ?  387 HOH   A O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 32.007 -7.355  -9.760  1.00 20.97 ?  388 HOH   A O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 24.170 -7.735  14.449  1.00 15.41 ?  389 HOH   A O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 30.552 1.928   16.753  1.00 20.56 ?  390 HOH   A O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 23.479 11.395  4.043   1.00 11.46 ?  391 HOH   A O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 13.833 -4.858  17.266  1.00 27.05 ?  392 HOH   A O    1 
HETATM 6918 O O    B HOH   F 4 .   ? 4.737  4.231   0.490   0.52 39.44 ?  393 HOH   A O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 20.600 -19.993 2.785   1.00 17.91 ?  394 HOH   A O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 24.016 -15.749 -9.231  1.00 35.90 ?  395 HOH   A O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 14.118 -23.125 7.394   1.00 18.11 ?  396 HOH   A O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 28.675 -10.658 -14.074 1.00 43.76 ?  397 HOH   A O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 15.235 -21.548 14.244  1.00 17.65 ?  398 HOH   A O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 11.685 -10.720 16.946  1.00 23.79 ?  399 HOH   A O    1 
HETATM 6925 O O    A HOH   F 4 .   ? 20.152 4.523   -7.573  0.48 18.18 ?  400 HOH   A O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 37.544 -2.050  5.865   1.00 24.76 ?  401 HOH   A O    1 
HETATM 6927 O O    A HOH   F 4 .   ? 24.635 2.021   -7.004  0.48 15.26 ?  402 HOH   A O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 16.212 16.645  8.604   1.00 39.35 ?  403 HOH   A O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 32.780 -9.254  5.971   1.00 19.94 ?  404 HOH   A O    1 
HETATM 6930 O O    A HOH   F 4 .   ? 15.827 -0.963  5.234   0.48 23.10 ?  405 HOH   A O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 38.116 -1.333  -1.854  1.00 18.32 ?  406 HOH   A O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 14.603 -0.554  -12.325 1.00 37.04 ?  407 HOH   A O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 40.996 -8.310  -6.824  1.00 36.48 ?  408 HOH   A O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 30.038 -10.065 13.067  1.00 22.10 ?  409 HOH   A O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 15.811 2.097   24.650  1.00 55.58 ?  410 HOH   A O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 26.908 -3.204  19.631  1.00 39.54 ?  411 HOH   A O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 27.106 2.367   18.703  1.00 33.97 ?  412 HOH   A O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 6.641  -3.415  12.755  1.00 31.05 ?  413 HOH   A O    1 
HETATM 6939 O O    A HOH   F 4 .   ? 11.101 -0.399  1.887   0.28 15.28 ?  414 HOH   A O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 24.026 3.960   -4.843  1.00 26.94 ?  415 HOH   A O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 35.181 -5.255  -3.053  1.00 17.32 ?  416 HOH   A O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 16.053 6.924   2.795   1.00 16.06 ?  417 HOH   A O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 26.962 4.141   -0.680  1.00 11.94 ?  418 HOH   A O    1 
HETATM 6944 O O    . HOH   F 4 .   ? -0.823 -8.612  1.967   1.00 42.58 ?  419 HOH   A O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 16.241 -14.110 20.186  1.00 51.25 ?  420 HOH   A O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 30.300 -12.875 13.586  1.00 18.87 ?  421 HOH   A O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 15.421 11.787  7.746   1.00 43.45 ?  422 HOH   A O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 15.280 -8.121  -9.896  1.00 28.59 ?  423 HOH   A O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 32.840 -4.393  -9.842  1.00 27.93 ?  424 HOH   A O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 23.992 -20.274 -1.328  1.00 16.34 ?  425 HOH   A O    1 
HETATM 6951 O O    A HOH   F 4 .   ? 6.481  -5.622  11.123  0.48 15.88 ?  426 HOH   A O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 10.472 -13.823 -1.835  1.00 17.53 ?  427 HOH   A O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 36.722 -4.980  5.468   1.00 23.88 ?  428 HOH   A O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 32.580 -10.639 3.269   1.00 31.59 ?  429 HOH   A O    1 
HETATM 6955 O O    A HOH   F 4 .   ? 18.646 -2.485  -16.367 0.48 28.08 ?  430 HOH   A O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 41.589 1.459   5.108   1.00 38.22 ?  431 HOH   A O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 21.876 -13.941 -8.278  1.00 45.80 ?  432 HOH   A O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 45.106 -0.560  2.998   1.00 39.24 ?  433 HOH   A O    1 
HETATM 6959 O O    A HOH   F 4 .   ? 9.009  -12.138 17.140  0.48 36.51 ?  434 HOH   A O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 23.416 -20.938 1.354   1.00 17.73 ?  435 HOH   A O    1 
HETATM 6961 O O    A HOH   F 4 .   ? 18.902 2.015   -0.781  0.48 10.76 ?  436 HOH   A O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 37.844 -8.873  -3.474  1.00 22.30 ?  437 HOH   A O    1 
HETATM 6963 O O    A HOH   F 4 .   ? 18.505 4.821   -15.059 0.48 33.93 ?  438 HOH   A O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 22.554 8.176   18.422  1.00 48.68 ?  439 HOH   A O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 29.879 -1.938  -12.838 1.00 48.58 ?  440 HOH   A O    1 
HETATM 6966 O O    B HOH   F 4 .   ? 7.919  3.865   1.300   0.52 26.02 ?  441 HOH   A O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 23.431 -8.015  17.099  1.00 19.99 ?  442 HOH   A O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 34.367 -8.200  -0.405  1.00 29.42 ?  443 HOH   A O    1 
HETATM 6969 O O    B HOH   F 4 .   ? 7.497  3.648   4.071   0.52 24.93 ?  444 HOH   A O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 9.467  -16.520 -2.129  1.00 51.86 ?  445 HOH   A O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 21.484 -14.737 17.931  1.00 52.04 ?  446 HOH   A O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 18.430 -15.982 16.157  1.00 36.89 ?  447 HOH   A O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 30.573 14.770  2.784   1.00 17.83 ?  448 HOH   A O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 20.509 -17.704 24.852  1.00 58.15 ?  449 HOH   A O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 31.372 -12.811 0.033   1.00 19.22 ?  450 HOH   A O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 21.377 -9.120  21.353  1.00 57.73 ?  451 HOH   A O    1 
HETATM 6977 O O    A HOH   F 4 .   ? 16.299 2.929   -1.477  0.74 23.07 ?  452 HOH   A O    1 
HETATM 6978 O O    . HOH   F 4 .   ? -1.393 -4.983  7.519   1.00 41.45 ?  453 HOH   A O    1 
HETATM 6979 O O    A HOH   F 4 .   ? 14.058 -0.357  3.422   0.28 31.89 ?  454 HOH   A O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 23.219 7.470   -3.288  1.00 34.10 ?  455 HOH   A O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 29.807 -15.984 10.758  1.00 32.94 ?  456 HOH   A O    1 
HETATM 6982 O O    B HOH   F 4 .   ? 18.390 2.000   -0.828  0.52 15.77 ?  457 HOH   A O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 25.458 8.270   -4.829  1.00 30.39 ?  458 HOH   A O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 19.992 -17.409 -5.015  1.00 25.91 ?  459 HOH   A O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 24.774 5.618   20.659  1.00 57.29 ?  460 HOH   A O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 32.406 -15.953 10.982  1.00 29.64 ?  461 HOH   A O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 27.869 7.157   -6.605  1.00 41.30 ?  462 HOH   A O    1 
HETATM 6988 O O    B HOH   F 4 .   ? 12.644 -3.212  1.612   0.52 15.94 ?  463 HOH   A O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 21.955 5.084   -6.048  1.00 40.38 ?  464 HOH   A O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 24.703 14.671  7.704   1.00 35.96 ?  465 HOH   A O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 23.289 -22.408 -3.257  1.00 35.47 ?  466 HOH   A O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 11.931 -13.451 16.192  1.00 57.46 ?  467 HOH   A O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 18.768 10.953  11.144  1.00 29.92 ?  468 HOH   A O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 27.486 -11.416 16.594  1.00 40.00 ?  469 HOH   A O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 23.454 13.712  5.505   1.00 17.72 ?  470 HOH   A O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 39.789 -7.114  -3.484  1.00 41.32 ?  471 HOH   A O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 15.866 -21.603 3.714   1.00 22.84 ?  472 HOH   A O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 26.950 11.618  -1.305  1.00 33.20 ?  473 HOH   A O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 12.279 1.564   17.189  1.00 39.26 ?  474 HOH   A O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 18.237 -16.240 -8.897  1.00 42.27 ?  475 HOH   A O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 11.057 -15.164 -6.168  1.00 35.75 ?  476 HOH   A O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 25.914 10.837  -3.697  1.00 24.70 ?  477 HOH   A O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 35.084 7.469   12.322  1.00 47.39 ?  478 HOH   A O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 28.684 -4.760  -12.270 1.00 42.25 ?  479 HOH   A O    1 
HETATM 7005 O O    B HOH   F 4 .   ? 11.877 8.776   7.379   0.52 30.03 ?  480 HOH   A O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 14.129 -10.400 -10.935 1.00 36.50 ?  481 HOH   A O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 15.858 -17.233 -7.038  1.00 32.91 ?  482 HOH   A O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 17.427 -18.755 19.801  1.00 51.61 ?  483 HOH   A O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 28.833 9.019   17.611  1.00 37.45 ?  484 HOH   A O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 16.865 -20.540 16.186  1.00 29.34 ?  485 HOH   A O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 41.066 -4.011  -0.252  1.00 35.30 ?  486 HOH   A O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 44.424 10.398  -1.693  1.00 36.62 ?  487 HOH   A O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 30.822 0.713   19.159  1.00 40.45 ?  488 HOH   A O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 41.757 9.384   -3.835  1.00 33.15 ?  489 HOH   A O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 39.185 2.425   7.390   1.00 31.98 ?  490 HOH   A O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 23.220 11.930  -4.080  1.00 20.40 ?  491 HOH   A O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 28.863 -8.050  -15.206 1.00 50.86 ?  492 HOH   A O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 31.642 -0.634  -10.484 1.00 26.39 ?  493 HOH   A O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 23.198 -12.874 19.281  1.00 50.19 ?  494 HOH   A O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 18.471 -23.177 1.885   1.00 43.97 ?  495 HOH   A O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 13.796 -25.254 8.883   1.00 35.43 ?  496 HOH   A O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 16.235 -23.417 5.808   1.00 28.19 ?  497 HOH   A O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 40.673 -0.206  -7.688  1.00 31.96 ?  498 HOH   A O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 16.221 -6.853  -11.956 1.00 45.76 ?  499 HOH   A O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 30.804 5.803   -14.701 1.00 34.10 ?  500 HOH   A O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 20.120 -22.357 4.165   1.00 29.34 ?  501 HOH   A O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 25.798 -18.950 -11.806 1.00 38.83 ?  502 HOH   A O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 23.360 -23.810 1.661   1.00 30.60 ?  503 HOH   A O    1 
HETATM 7029 O O    B HOH   F 4 .   ? 14.774 7.956   4.917   0.52 19.01 ?  504 HOH   A O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 20.594 -16.004 -7.472  1.00 29.66 ?  505 HOH   A O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 30.824 -5.893  -11.842 1.00 52.70 ?  506 HOH   A O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 37.420 -6.661  7.597   1.00 23.98 ?  507 HOH   A O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 39.541 -0.040  6.667   1.00 32.95 ?  508 HOH   A O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 37.967 13.968  6.694   1.00 30.92 ?  509 HOH   A O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 28.969 14.472  0.862   1.00 49.94 ?  510 HOH   A O    1 
HETATM 7036 O O    B HOH   F 4 .   ? 10.317 -0.390  -1.378  0.52 27.17 ?  511 HOH   A O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 8.188  -3.041  -5.759  1.00 50.39 ?  512 HOH   A O    1 
HETATM 7038 O O    B HOH   F 4 .   ? 5.796  6.597   1.346   0.52 29.96 ?  513 HOH   A O    1 
HETATM 7039 O O    B HOH   F 4 .   ? 7.442  5.857   5.569   0.52 28.91 ?  514 HOH   A O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 36.515 -6.464  10.204  1.00 44.03 ?  515 HOH   A O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 22.100 -24.053 4.486   1.00 26.30 ?  516 HOH   A O    1 
HETATM 7042 O O    T HOH   F 4 .   ? 11.968 -2.169  -3.698  0.20 12.33 ?  517 HOH   A O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 17.423 -6.570  -14.202 1.00 49.63 ?  518 HOH   A O    1 
HETATM 7044 O O    A HOH   F 4 .   ? 14.876 8.633   4.849   0.48 37.17 ?  519 HOH   A O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 24.115 9.035   -7.174  1.00 40.34 ?  520 HOH   A O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 16.323 -21.100 18.753  1.00 41.68 ?  521 HOH   A O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 15.815 -12.384 27.389  1.00 45.94 ?  522 HOH   A O    1 
HETATM 7048 O O    B HOH   F 4 .   ? 8.307  7.246   2.037   0.52 31.59 ?  523 HOH   A O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 14.704 -22.691 19.906  1.00 36.00 ?  524 HOH   A O    1 
HETATM 7050 O O    . HOH   G 4 .   ? 29.910 -22.440 5.532   1.00 20.55 ?  201 HOH   B O    1 
HETATM 7051 O O    . HOH   G 4 .   ? 41.675 -36.060 -17.068 1.00 33.94 ?  202 HOH   B O    1 
HETATM 7052 O O    . HOH   G 4 .   ? 27.724 -29.135 -1.820  1.00 32.76 ?  203 HOH   B O    1 
HETATM 7053 O O    . HOH   G 4 .   ? 53.047 -13.443 -20.351 1.00 36.71 ?  204 HOH   B O    1 
HETATM 7054 O O    . HOH   G 4 .   ? 49.470 -22.691 -19.720 1.00 49.35 ?  205 HOH   B O    1 
HETATM 7055 O O    . HOH   G 4 .   ? 59.170 -18.732 6.916   1.00 36.06 ?  206 HOH   B O    1 
HETATM 7056 O O    . HOH   G 4 .   ? 30.003 -26.309 4.122   1.00 27.08 ?  207 HOH   B O    1 
HETATM 7057 O O    . HOH   G 4 .   ? 37.960 -39.487 -0.211  1.00 37.09 ?  208 HOH   B O    1 
HETATM 7058 O O    . HOH   G 4 .   ? 54.567 -9.431  -8.659  1.00 18.47 ?  209 HOH   B O    1 
HETATM 7059 O O    . HOH   G 4 .   ? 57.757 -24.562 5.123   1.00 37.98 ?  210 HOH   B O    1 
HETATM 7060 O O    . HOH   G 4 .   ? 27.881 -41.807 -15.122 1.00 38.33 ?  211 HOH   B O    1 
HETATM 7061 O O    . HOH   G 4 .   ? 30.251 -41.014 -8.026  1.00 16.11 ?  212 HOH   B O    1 
HETATM 7062 O O    . HOH   G 4 .   ? 56.758 -30.781 -7.784  1.00 27.15 ?  213 HOH   B O    1 
HETATM 7063 O O    . HOH   G 4 .   ? 47.419 -7.408  -3.813  1.00 40.79 ?  214 HOH   B O    1 
HETATM 7064 O O    . HOH   G 4 .   ? 30.943 -28.758 4.404   1.00 27.49 ?  215 HOH   B O    1 
HETATM 7065 O O    . HOH   G 4 .   ? 41.387 -7.791  5.461   1.00 38.45 ?  216 HOH   B O    1 
HETATM 7066 O O    . HOH   G 4 .   ? 44.588 -7.172  2.074   1.00 34.77 ?  217 HOH   B O    1 
HETATM 7067 O O    . HOH   G 4 .   ? 50.210 -3.403  7.177   1.00 31.52 ?  218 HOH   B O    1 
HETATM 7068 O O    . HOH   G 4 .   ? 58.245 -12.899 8.491   1.00 29.33 ?  219 HOH   B O    1 
HETATM 7069 O O    . HOH   G 4 .   ? 44.981 -43.563 -10.519 1.00 27.56 ?  220 HOH   B O    1 
HETATM 7070 O O    . HOH   G 4 .   ? 37.232 -19.782 -18.104 1.00 40.09 ?  221 HOH   B O    1 
HETATM 7071 O O    . HOH   G 4 .   ? 56.431 -19.720 7.500   1.00 31.14 ?  222 HOH   B O    1 
HETATM 7072 O O    . HOH   G 4 .   ? 48.005 -6.962  15.582  1.00 32.07 ?  223 HOH   B O    1 
HETATM 7073 O O    . HOH   G 4 .   ? 34.925 -24.690 13.878  1.00 37.40 ?  224 HOH   B O    1 
HETATM 7074 O O    . HOH   G 4 .   ? 34.582 -36.400 -7.123  1.00 17.70 ?  225 HOH   B O    1 
HETATM 7075 O O    . HOH   G 4 .   ? 57.420 -16.294 -12.220 1.00 17.32 ?  226 HOH   B O    1 
HETATM 7076 O O    . HOH   G 4 .   ? 41.509 -39.180 -14.801 1.00 21.24 ?  227 HOH   B O    1 
HETATM 7077 O O    . HOH   G 4 .   ? 29.731 -34.079 -0.395  1.00 33.37 ?  228 HOH   B O    1 
HETATM 7078 O O    . HOH   G 4 .   ? 51.702 -6.520  4.420   1.00 19.61 ?  229 HOH   B O    1 
HETATM 7079 O O    . HOH   G 4 .   ? 35.199 -8.035  -2.925  1.00 17.08 ?  230 HOH   B O    1 
HETATM 7080 O O    . HOH   G 4 .   ? 50.729 -6.119  0.242   1.00 25.75 ?  231 HOH   B O    1 
HETATM 7081 O O    . HOH   G 4 .   ? 38.560 -11.076 -2.267  1.00 17.54 ?  232 HOH   B O    1 
HETATM 7082 O O    . HOH   G 4 .   ? 41.438 -9.662  13.087  1.00 20.76 ?  233 HOH   B O    1 
HETATM 7083 O O    . HOH   G 4 .   ? 28.511 -19.668 -13.118 1.00 24.27 ?  234 HOH   B O    1 
HETATM 7084 O O    . HOH   G 4 .   ? 40.666 -16.072 14.149  1.00 21.80 ?  235 HOH   B O    1 
HETATM 7085 O O    . HOH   G 4 .   ? 36.108 -43.384 -8.310  1.00 39.06 ?  236 HOH   B O    1 
HETATM 7086 O O    . HOH   G 4 .   ? 39.345 -10.857 6.143   1.00 23.39 ?  237 HOH   B O    1 
HETATM 7087 O O    . HOH   G 4 .   ? 46.380 -1.602  13.300  1.00 26.76 ?  238 HOH   B O    1 
HETATM 7088 O O    . HOH   G 4 .   ? 48.072 -24.606 -17.729 1.00 28.42 ?  239 HOH   B O    1 
HETATM 7089 O O    . HOH   G 4 .   ? 48.606 -36.582 -15.428 1.00 41.46 ?  240 HOH   B O    1 
HETATM 7090 O O    . HOH   G 4 .   ? 44.576 -27.769 -0.641  1.00 21.17 ?  241 HOH   B O    1 
HETATM 7091 O O    . HOH   G 4 .   ? 55.381 -16.491 -14.259 1.00 32.18 ?  242 HOH   B O    1 
HETATM 7092 O O    . HOH   G 4 .   ? 42.618 -25.385 2.703   1.00 14.40 ?  243 HOH   B O    1 
HETATM 7093 O O    . HOH   G 4 .   ? 43.102 -43.267 -8.116  1.00 28.38 ?  244 HOH   B O    1 
HETATM 7094 O O    . HOH   G 4 .   ? 50.994 -39.968 -8.124  1.00 34.92 ?  245 HOH   B O    1 
HETATM 7095 O O    . HOH   G 4 .   ? 27.154 -31.824 -9.867  1.00 21.98 ?  246 HOH   B O    1 
HETATM 7096 O O    . HOH   G 4 .   ? 50.810 -13.006 -0.396  1.00 11.11 ?  247 HOH   B O    1 
HETATM 7097 O O    . HOH   G 4 .   ? 39.598 -11.156 0.334   1.00 15.81 ?  248 HOH   B O    1 
HETATM 7098 O O    . HOH   G 4 .   ? 57.224 -26.814 -7.613  1.00 42.11 ?  249 HOH   B O    1 
HETATM 7099 O O    . HOH   G 4 .   ? 57.691 -24.403 -3.732  1.00 21.35 ?  250 HOH   B O    1 
HETATM 7100 O O    . HOH   G 4 .   ? 32.832 -43.823 -11.240 1.00 21.28 ?  251 HOH   B O    1 
HETATM 7101 O O    . HOH   G 4 .   ? 41.921 -23.567 9.341   1.00 17.33 ?  252 HOH   B O    1 
HETATM 7102 O O    . HOH   G 4 .   ? 29.769 -25.233 -10.727 1.00 16.76 ?  253 HOH   B O    1 
HETATM 7103 O O    . HOH   G 4 .   ? 25.410 -25.934 -1.234  1.00 31.72 ?  254 HOH   B O    1 
HETATM 7104 O O    . HOH   G 4 .   ? 45.162 -34.963 6.769   1.00 41.96 ?  255 HOH   B O    1 
HETATM 7105 O O    . HOH   G 4 .   ? 32.165 -9.295  -6.550  1.00 22.06 ?  256 HOH   B O    1 
HETATM 7106 O O    . HOH   G 4 .   ? 42.697 -22.892 3.923   1.00 10.94 ?  257 HOH   B O    1 
HETATM 7107 O O    . HOH   G 4 .   ? 33.587 -16.985 8.144   1.00 18.50 ?  258 HOH   B O    1 
HETATM 7108 O O    . HOH   G 4 .   ? 51.579 -13.858 11.062  1.00 25.15 ?  259 HOH   B O    1 
HETATM 7109 O O    . HOH   G 4 .   ? 40.447 -12.786 -11.500 1.00 14.30 ?  260 HOH   B O    1 
HETATM 7110 O O    . HOH   G 4 .   ? 49.757 -0.499  10.229  1.00 27.82 ?  261 HOH   B O    1 
HETATM 7111 O O    . HOH   G 4 .   ? 34.308 -18.402 11.482  1.00 25.44 ?  262 HOH   B O    1 
HETATM 7112 O O    . HOH   G 4 .   ? 56.223 -23.607 -14.651 1.00 27.04 ?  263 HOH   B O    1 
HETATM 7113 O O    . HOH   G 4 .   ? 46.668 -31.289 -4.760  1.00 18.12 ?  264 HOH   B O    1 
HETATM 7114 O O    . HOH   G 4 .   ? 58.254 -10.633 -4.024  1.00 18.88 ?  265 HOH   B O    1 
HETATM 7115 O O    . HOH   G 4 .   ? 31.864 -17.900 -14.464 1.00 28.87 ?  266 HOH   B O    1 
HETATM 7116 O O    . HOH   G 4 .   ? 49.366 -28.742 -6.852  1.00 14.52 ?  267 HOH   B O    1 
HETATM 7117 O O    . HOH   G 4 .   ? 30.909 -15.727 2.732   1.00 13.02 ?  268 HOH   B O    1 
HETATM 7118 O O    . HOH   G 4 .   ? 48.071 -22.787 5.885   1.00 15.98 ?  269 HOH   B O    1 
HETATM 7119 O O    . HOH   G 4 .   ? 57.541 -9.246  1.484   1.00 18.69 ?  270 HOH   B O    1 
HETATM 7120 O O    . HOH   G 4 .   ? 56.981 -8.635  8.469   1.00 18.10 ?  271 HOH   B O    1 
HETATM 7121 O O    . HOH   G 4 .   ? 46.948 -29.563 9.821   1.00 32.53 ?  272 HOH   B O    1 
HETATM 7122 O O    . HOH   G 4 .   ? 42.413 -9.936  9.367   1.00 18.92 ?  273 HOH   B O    1 
HETATM 7123 O O    . HOH   G 4 .   ? 43.217 -32.393 -17.042 1.00 22.93 ?  274 HOH   B O    1 
HETATM 7124 O O    . HOH   G 4 .   ? 30.629 -42.249 -10.557 1.00 30.05 ?  275 HOH   B O    1 
HETATM 7125 O O    . HOH   G 4 .   ? 38.951 -11.937 12.411  1.00 32.79 ?  276 HOH   B O    1 
HETATM 7126 O O    . HOH   G 4 .   ? 28.290 -34.345 -9.311  1.00 21.22 ?  277 HOH   B O    1 
HETATM 7127 O O    . HOH   G 4 .   ? 28.507 -30.853 -14.751 1.00 31.39 ?  278 HOH   B O    1 
HETATM 7128 O O    . HOH   G 4 .   ? 42.426 -34.697 3.813   1.00 27.29 ?  279 HOH   B O    1 
HETATM 7129 O O    . HOH   G 4 .   ? 57.146 -12.124 12.428  1.00 36.77 ?  280 HOH   B O    1 
HETATM 7130 O O    . HOH   G 4 .   ? 34.532 -12.781 2.650   1.00 22.87 ?  281 HOH   B O    1 
HETATM 7131 O O    . HOH   G 4 .   ? 43.476 -15.818 -12.153 1.00 13.27 ?  282 HOH   B O    1 
HETATM 7132 O O    . HOH   G 4 .   ? 48.448 -25.062 3.140   1.00 12.53 ?  283 HOH   B O    1 
HETATM 7133 O O    . HOH   G 4 .   ? 34.976 -33.381 -19.152 1.00 27.39 ?  284 HOH   B O    1 
HETATM 7134 O O    . HOH   G 4 .   ? 50.045 -24.644 5.810   1.00 33.45 ?  285 HOH   B O    1 
HETATM 7135 O O    . HOH   G 4 .   ? 28.013 -22.887 -7.968  1.00 16.65 ?  286 HOH   B O    1 
HETATM 7136 O O    . HOH   G 4 .   ? 52.583 -10.387 13.027  1.00 21.84 ?  287 HOH   B O    1 
HETATM 7137 O O    . HOH   G 4 .   ? 27.660 -26.678 -15.595 1.00 32.07 ?  288 HOH   B O    1 
HETATM 7138 O O    . HOH   G 4 .   ? 48.769 -20.057 5.998   1.00 13.07 ?  289 HOH   B O    1 
HETATM 7139 O O    . HOH   G 4 .   ? 51.701 -5.935  -7.864  1.00 43.13 ?  290 HOH   B O    1 
HETATM 7140 O O    . HOH   G 4 .   ? 48.651 -12.128 -14.467 1.00 25.24 ?  291 HOH   B O    1 
HETATM 7141 O O    . HOH   G 4 .   ? 41.202 -5.522  11.606  1.00 45.44 ?  292 HOH   B O    1 
HETATM 7142 O O    . HOH   G 4 .   ? 47.119 -34.030 -4.547  1.00 16.95 ?  293 HOH   B O    1 
HETATM 7143 O O    . HOH   G 4 .   ? 59.801 -15.308 8.216   1.00 29.22 ?  294 HOH   B O    1 
HETATM 7144 O O    . HOH   G 4 .   ? 33.605 -15.337 -13.933 1.00 20.67 ?  295 HOH   B O    1 
HETATM 7145 O O    . HOH   G 4 .   ? 36.918 -12.775 -1.466  1.00 23.89 ?  296 HOH   B O    1 
HETATM 7146 O O    . HOH   G 4 .   ? 37.551 -17.993 13.142  1.00 31.52 ?  297 HOH   B O    1 
HETATM 7147 O O    . HOH   G 4 .   ? 51.279 -37.630 -9.531  1.00 28.07 ?  298 HOH   B O    1 
HETATM 7148 O O    . HOH   G 4 .   ? 44.687 -27.494 2.070   1.00 14.75 ?  299 HOH   B O    1 
HETATM 7149 O O    . HOH   G 4 .   ? 43.000 -20.209 -20.672 1.00 39.99 ?  300 HOH   B O    1 
HETATM 7150 O O    . HOH   G 4 .   ? 42.914 -12.127 -18.419 1.00 25.06 ?  301 HOH   B O    1 
HETATM 7151 O O    . HOH   G 4 .   ? 45.381 -33.408 -15.891 1.00 23.59 ?  302 HOH   B O    1 
HETATM 7152 O O    . HOH   G 4 .   ? 52.634 -35.703 -8.640  1.00 29.68 ?  303 HOH   B O    1 
HETATM 7153 O O    . HOH   G 4 .   ? 52.972 -15.932 -12.753 1.00 22.84 ?  304 HOH   B O    1 
HETATM 7154 O O    . HOH   G 4 .   ? 26.007 -21.480 -3.460  1.00 16.30 ?  305 HOH   B O    1 
HETATM 7155 O O    . HOH   G 4 .   ? 35.113 -33.556 4.610   1.00 28.56 ?  306 HOH   B O    1 
HETATM 7156 O O    . HOH   G 4 .   ? 53.736 -12.562 -22.157 1.00 35.48 ?  307 HOH   B O    1 
HETATM 7157 O O    . HOH   G 4 .   ? 44.067 -29.396 -4.617  1.00 22.02 ?  308 HOH   B O    1 
HETATM 7158 O O    . HOH   G 4 .   ? 62.764 -13.609 4.812   1.00 26.49 ?  309 HOH   B O    1 
HETATM 7159 O O    . HOH   G 4 .   ? 40.362 -10.876 -9.494  1.00 16.35 ?  310 HOH   B O    1 
HETATM 7160 O O    . HOH   G 4 .   ? 53.471 -30.246 4.626   1.00 17.95 ?  311 HOH   B O    1 
HETATM 7161 O O    . HOH   G 4 .   ? 37.934 -10.266 -10.727 1.00 16.46 ?  312 HOH   B O    1 
HETATM 7162 O O    . HOH   G 4 .   ? 45.903 -40.425 -3.477  1.00 27.81 ?  313 HOH   B O    1 
HETATM 7163 O O    . HOH   G 4 .   ? 43.259 -21.444 10.721  1.00 15.31 ?  314 HOH   B O    1 
HETATM 7164 O O    . HOH   G 4 .   ? 38.437 -9.402  -13.238 1.00 27.01 ?  315 HOH   B O    1 
HETATM 7165 O O    . HOH   G 4 .   ? 32.848 -34.634 -5.833  1.00 16.38 ?  316 HOH   B O    1 
HETATM 7166 O O    . HOH   G 4 .   ? 42.483 -9.809  -14.841 1.00 37.73 ?  317 HOH   B O    1 
HETATM 7167 O O    . HOH   G 4 .   ? 52.602 -29.283 -13.002 1.00 25.31 ?  318 HOH   B O    1 
HETATM 7168 O O    . HOH   G 4 .   ? 38.365 -12.692 8.010   1.00 17.15 ?  319 HOH   B O    1 
HETATM 7169 O O    . HOH   G 4 .   ? 41.837 -8.077  1.421   1.00 23.08 ?  320 HOH   B O    1 
HETATM 7170 O O    . HOH   G 4 .   ? 37.067 -30.613 -20.953 1.00 32.04 ?  321 HOH   B O    1 
HETATM 7171 O O    . HOH   G 4 .   ? 48.225 -32.672 -16.575 1.00 43.03 ?  322 HOH   B O    1 
HETATM 7172 O O    . HOH   G 4 .   ? 45.776 -36.352 -16.055 1.00 36.10 ?  323 HOH   B O    1 
HETATM 7173 O O    . HOH   G 4 .   ? 57.583 -21.964 3.479   1.00 31.56 ?  324 HOH   B O    1 
HETATM 7174 O O    . HOH   G 4 .   ? 26.427 -21.066 -6.204  1.00 15.89 ?  325 HOH   B O    1 
HETATM 7175 O O    . HOH   G 4 .   ? 33.634 -31.119 11.102  1.00 36.30 ?  326 HOH   B O    1 
HETATM 7176 O O    . HOH   G 4 .   ? 62.967 -20.161 -0.698  1.00 36.58 ?  327 HOH   B O    1 
HETATM 7177 O O    . HOH   G 4 .   ? 44.689 -24.625 9.635   1.00 20.80 ?  328 HOH   B O    1 
HETATM 7178 O O    . HOH   G 4 .   ? 51.446 -33.054 -10.791 1.00 40.07 ?  329 HOH   B O    1 
HETATM 7179 O O    . HOH   G 4 .   ? 36.787 -12.415 4.311   1.00 16.58 ?  330 HOH   B O    1 
HETATM 7180 O O    . HOH   G 4 .   ? 37.261 -35.739 7.261   1.00 35.98 ?  331 HOH   B O    1 
HETATM 7181 O O    . HOH   G 4 .   ? 43.145 -34.633 0.155   1.00 20.95 ?  332 HOH   B O    1 
HETATM 7182 O O    . HOH   G 4 .   ? 47.244 -24.509 8.244   1.00 27.04 ?  333 HOH   B O    1 
HETATM 7183 O O    . HOH   G 4 .   ? 44.116 -1.758  7.700   1.00 47.78 ?  334 HOH   B O    1 
HETATM 7184 O O    . HOH   G 4 .   ? 60.020 -17.258 -10.456 1.00 34.96 ?  335 HOH   B O    1 
HETATM 7185 O O    . HOH   G 4 .   ? 27.868 -14.727 -9.429  1.00 36.16 ?  336 HOH   B O    1 
HETATM 7186 O O    . HOH   G 4 .   ? 39.629 -23.384 -20.361 1.00 33.80 ?  337 HOH   B O    1 
HETATM 7187 O O    . HOH   G 4 .   ? 47.524 -27.470 2.078   1.00 14.45 ?  338 HOH   B O    1 
HETATM 7188 O O    . HOH   G 4 .   ? 41.366 -24.518 15.900  1.00 47.38 ?  339 HOH   B O    1 
HETATM 7189 O O    . HOH   G 4 .   ? 42.966 -43.519 -14.361 1.00 44.22 ?  340 HOH   B O    1 
HETATM 7190 O O    . HOH   G 4 .   ? 37.138 -15.189 -16.520 1.00 40.21 ?  341 HOH   B O    1 
HETATM 7191 O O    . HOH   G 4 .   ? 28.892 -42.883 -12.320 1.00 37.43 ?  342 HOH   B O    1 
HETATM 7192 O O    . HOH   G 4 .   ? 43.543 -15.431 18.137  1.00 28.90 ?  343 HOH   B O    1 
HETATM 7193 O O    . HOH   G 4 .   ? 46.849 -19.959 12.316  1.00 27.06 ?  344 HOH   B O    1 
HETATM 7194 O O    . HOH   G 4 .   ? 37.092 -45.254 -9.628  1.00 38.49 ?  345 HOH   B O    1 
HETATM 7195 O O    . HOH   G 4 .   ? 34.515 -10.350 7.747   1.00 22.50 ?  346 HOH   B O    1 
HETATM 7196 O O    . HOH   G 4 .   ? 33.056 -14.707 1.121   1.00 18.26 ?  347 HOH   B O    1 
HETATM 7197 O O    . HOH   G 4 .   ? 38.575 -22.515 15.092  1.00 45.74 ?  348 HOH   B O    1 
HETATM 7198 O O    . HOH   G 4 .   ? 38.524 -12.275 -16.230 1.00 42.71 ?  349 HOH   B O    1 
HETATM 7199 O O    . HOH   G 4 .   ? 40.422 -43.506 -9.020  1.00 25.61 ?  350 HOH   B O    1 
HETATM 7200 O O    . HOH   G 4 .   ? 62.658 -20.074 -4.697  1.00 50.70 ?  351 HOH   B O    1 
HETATM 7201 O O    . HOH   G 4 .   ? 39.933 -44.300 -11.160 1.00 46.27 ?  352 HOH   B O    1 
HETATM 7202 O O    . HOH   G 4 .   ? 23.322 -23.692 6.858   1.00 33.54 ?  353 HOH   B O    1 
HETATM 7203 O O    . HOH   G 4 .   ? 33.927 -9.247  -8.863  1.00 29.62 ?  354 HOH   B O    1 
HETATM 7204 O O    . HOH   G 4 .   ? 44.206 -37.378 -17.725 1.00 31.84 ?  355 HOH   B O    1 
HETATM 7205 O O    . HOH   G 4 .   ? 27.863 -26.640 -0.471  1.00 27.59 ?  356 HOH   B O    1 
HETATM 7206 O O    . HOH   G 4 .   ? 55.744 -8.265  10.872  1.00 24.38 ?  357 HOH   B O    1 
HETATM 7207 O O    . HOH   G 4 .   ? 34.096 -7.836  11.503  1.00 40.51 ?  358 HOH   B O    1 
HETATM 7208 O O    . HOH   G 4 .   ? 56.650 -7.295  3.079   1.00 26.91 ?  359 HOH   B O    1 
HETATM 7209 O O    . HOH   G 4 .   ? 36.270 -8.552  -9.723  1.00 32.25 ?  360 HOH   B O    1 
HETATM 7210 O O    . HOH   G 4 .   ? 61.567 -19.869 1.814   1.00 38.85 ?  361 HOH   B O    1 
HETATM 7211 O O    . HOH   G 4 .   ? 56.902 -21.596 -16.372 1.00 41.34 ?  362 HOH   B O    1 
HETATM 7212 O O    . HOH   G 4 .   ? 27.242 -25.970 -11.303 1.00 34.66 ?  363 HOH   B O    1 
HETATM 7213 O O    . HOH   G 4 .   ? 40.285 -8.859  9.926   1.00 37.04 ?  364 HOH   B O    1 
HETATM 7214 O O    . HOH   G 4 .   ? 43.216 -12.777 -21.161 1.00 33.04 ?  365 HOH   B O    1 
HETATM 7215 O O    . HOH   G 4 .   ? 40.352 -11.380 -13.945 1.00 30.47 ?  366 HOH   B O    1 
HETATM 7216 O O    . HOH   G 4 .   ? 32.611 -23.627 14.015  1.00 40.02 ?  367 HOH   B O    1 
HETATM 7217 O O    . HOH   G 4 .   ? 48.362 -26.510 8.929   1.00 42.26 ?  368 HOH   B O    1 
HETATM 7218 O O    . HOH   G 4 .   ? 36.170 -8.618  9.054   1.00 36.99 ?  369 HOH   B O    1 
HETATM 7219 O O    . HOH   G 4 .   ? 54.320 -5.873  3.020   1.00 34.40 ?  370 HOH   B O    1 
HETATM 7220 O O    . HOH   G 4 .   ? 39.932 -7.071  7.847   1.00 38.76 ?  371 HOH   B O    1 
HETATM 7221 O O    . HOH   G 4 .   ? 58.999 -10.427 9.284   1.00 38.14 ?  372 HOH   B O    1 
HETATM 7222 O O    . HOH   G 4 .   ? 56.130 -7.810  -0.563  1.00 31.94 ?  373 HOH   B O    1 
HETATM 7223 O O    . HOH   G 4 .   ? 41.924 -10.007 -17.397 1.00 55.96 ?  374 HOH   B O    1 
HETATM 7224 O O    . HOH   G 4 .   ? 41.964 -6.786  -4.860  1.00 45.50 ?  375 HOH   B O    1 
HETATM 7225 O O    . HOH   G 4 .   ? 52.060 -12.948 13.407  1.00 25.53 ?  376 HOH   B O    1 
HETATM 7226 O O    . HOH   G 4 .   ? 63.001 -12.333 6.998   1.00 37.15 ?  377 HOH   B O    1 
HETATM 7227 O O    . HOH   G 4 .   ? 36.587 -22.848 13.344  1.00 31.54 ?  378 HOH   B O    1 
HETATM 7228 O O    . HOH   G 4 .   ? 40.216 -7.753  3.188   1.00 37.08 ?  379 HOH   B O    1 
HETATM 7229 O O    . HOH   G 4 .   ? 38.093 -10.537 10.087  1.00 26.55 ?  380 HOH   B O    1 
HETATM 7230 O O    . HOH   G 4 .   ? 42.700 -17.119 -23.164 1.00 41.81 ?  381 HOH   B O    1 
HETATM 7231 O O    . HOH   G 4 .   ? 44.160 -5.621  -3.482  1.00 39.56 ?  382 HOH   B O    1 
HETATM 7232 O O    . HOH   G 4 .   ? 39.663 -14.065 15.642  1.00 39.11 ?  383 HOH   B O    1 
HETATM 7233 O O    . HOH   G 4 .   ? 60.497 -22.368 2.900   1.00 41.69 ?  384 HOH   B O    1 
HETATM 7234 O O    . HOH   G 4 .   ? 46.729 -5.462  2.969   1.00 38.14 ?  385 HOH   B O    1 
HETATM 7235 O O    . HOH   G 4 .   ? 52.911 -29.911 7.281   1.00 22.06 ?  386 HOH   B O    1 
HETATM 7236 O O    . HOH   G 4 .   ? 35.348 -20.347 13.334  1.00 32.40 ?  387 HOH   B O    1 
HETATM 7237 O O    . HOH   G 4 .   ? 24.017 -20.899 -7.679  1.00 27.38 ?  388 HOH   B O    1 
HETATM 7238 O O    . HOH   G 4 .   ? 35.409 -33.728 7.415   1.00 41.23 ?  389 HOH   B O    1 
HETATM 7239 O O    . HOH   G 4 .   ? 40.979 -9.798  15.932  1.00 42.66 ?  390 HOH   B O    1 
HETATM 7240 O O    . HOH   G 4 .   ? 40.828 -6.609  -0.810  1.00 23.55 ?  391 HOH   B O    1 
HETATM 7241 O O    . HOH   G 4 .   ? 44.201 -31.755 -3.742  1.00 35.31 ?  392 HOH   B O    1 
HETATM 7242 O O    . HOH   G 4 .   ? 28.067 -27.109 2.291   1.00 30.94 ?  393 HOH   B O    1 
HETATM 7243 O O    . HOH   G 4 .   ? 26.692 -27.978 -13.413 1.00 35.59 ?  394 HOH   B O    1 
HETATM 7244 O O    . HOH   G 4 .   ? 24.695 -20.609 -10.509 1.00 42.11 ?  395 HOH   B O    1 
HETATM 7245 O O    . HOH   G 4 .   ? 50.695 -30.901 8.803   1.00 28.99 ?  396 HOH   B O    1 
HETATM 7246 O O    . HOH   G 4 .   ? 34.443 -33.534 9.666   1.00 36.70 ?  397 HOH   B O    1 
HETATM 7247 O O    . HOH   G 4 .   ? 26.872 -30.650 -12.541 1.00 29.70 ?  398 HOH   B O    1 
HETATM 7248 O O    . HOH   G 4 .   ? 57.779 -6.604  -2.302  1.00 33.34 ?  399 HOH   B O    1 
HETATM 7249 O O    . HOH   G 4 .   ? 45.762 -20.098 15.287  1.00 42.49 ?  400 HOH   B O    1 
HETATM 7250 O O    . HOH   G 4 .   ? 41.039 -11.768 -22.288 1.00 34.99 ?  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   ? 0.6291 0.6365 0.7260 0.0090  -0.0267 0.0666  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6328 0.6310 0.7279 0.0038  -0.0298 0.0711  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6264 0.6339 0.7159 0.0076  -0.0253 0.0663  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6303 0.6279 0.7156 0.0027  -0.0285 0.0713  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6115 0.6208 0.6824 0.0007  -0.0267 0.0682  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6161 0.6135 0.6811 -0.0042 -0.0299 0.0725  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6146 0.6236 0.6970 0.0021  -0.0291 0.0701  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6192 0.6166 0.6968 -0.0027 -0.0322 0.0740  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6358 0.6421 0.7308 0.0115  -0.0221 0.0646  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6394 0.6366 0.7280 0.0068  -0.0253 0.0702  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6390 0.6447 0.7343 0.0130  -0.0209 0.0640  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6424 0.6393 0.7310 0.0082  -0.0240 0.0699  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6388 0.6448 0.7342 0.0129  -0.0209 0.0642  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6423 0.6394 0.7309 0.0083  -0.0242 0.0700  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.5908 0.6024 0.6245 -0.0085 -0.0240 0.0671  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.5959 0.5931 0.6196 -0.0134 -0.0270 0.0720  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5672 0.5819 0.5579 -0.0188 -0.0200 0.0642  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.5730 0.5707 0.5487 -0.0236 -0.0225 0.0696  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5311 0.5552 0.5217 -0.0328 -0.0079 0.0455  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5376 0.5432 0.5104 -0.0371 -0.0050 0.0535  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5332 0.5569 0.5246 -0.0329 -0.0085 0.0460  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5403 0.5453 0.5119 -0.0369 -0.0057 0.0551  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.5768 0.5859 0.5225 -0.0158 -0.0269 0.0787  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.5822 0.5733 0.5112 -0.0212 -0.0338 0.0828  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.5839 0.5883 0.4889 -0.0137 -0.0326 0.0917  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.5889 0.5744 0.4760 -0.0197 -0.0435 0.0945  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.5869 0.5894 0.4758 -0.0134 -0.0347 0.0962  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.5917 0.5746 0.4621 -0.0196 -0.0474 0.0990  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.5858 0.5888 0.4796 -0.0127 -0.0348 0.0971  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.5906 0.5745 0.4663 -0.0189 -0.0470 0.0999  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.4906 0.5246 0.4779 -0.0477 0.0046  0.0261  5   SER   A N   
60   N N   B SER   A 5   ? 0.4970 0.5115 0.4664 -0.0519 0.0138  0.0363  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4484 0.4924 0.4329 -0.0618 0.0192  0.0083  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4542 0.4780 0.4222 -0.0666 0.0361  0.0206  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4011 0.4535 0.3815 -0.0730 0.0339  0.0011  5   SER   A C   
64   C C   B SER   A 5   ? 0.4038 0.4356 0.3685 -0.0806 0.0616  0.0166  5   SER   A C   
65   O O   A SER   A 5   ? 0.4039 0.4565 0.3806 -0.0725 0.0378  -0.0035 5   SER   A O   
66   O O   B SER   A 5   ? 0.4077 0.4391 0.3643 -0.0793 0.0665  0.0086  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4527 0.4979 0.4423 -0.0642 0.0191  -0.0003 5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4603 0.4851 0.4352 -0.0671 0.0340  0.0119  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4551 0.5008 0.4467 -0.0654 0.0191  -0.0050 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4637 0.4891 0.4405 -0.0673 0.0324  0.0068  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3493 0.4100 0.3234 -0.0833 0.0451  0.0034  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3476 0.3893 0.3102 -0.0952 0.0833  0.0260  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2996 0.3659 0.2711 -0.0899 0.0492  0.0095  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.2931 0.3405 0.2620 -0.1069 0.0939  0.0378  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2858 0.3574 0.2647 -0.0967 0.0619  0.0068  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.2844 0.3383 0.2706 -0.1096 0.1152  0.0339  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2888 0.3606 0.2915 -0.1015 0.0585  0.0062  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.2863 0.3404 0.3018 -0.1140 0.1207  0.0468  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2707 0.3333 0.2324 -0.0819 0.0360  0.0150  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2598 0.3001 0.2199 -0.1008 0.0654  0.0458  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2470 0.3067 0.2103 -0.0707 0.0242  0.0195  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2331 0.2704 0.1955 -0.0865 0.0427  0.0494  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2365 0.2946 0.2014 -0.0643 0.0204  0.0197  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2221 0.2587 0.1870 -0.0770 0.0334  0.0499  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2442 0.2984 0.2168 -0.0596 0.0228  0.0211  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2308 0.2623 0.2047 -0.0731 0.0348  0.0477  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2327 0.2888 0.2049 -0.0599 0.0246  0.0244  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2166 0.2512 0.1910 -0.0733 0.0317  0.0526  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2401 0.2930 0.2231 -0.0547 0.0246  0.0205  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2254 0.2561 0.2117 -0.0673 0.0272  0.0427  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2355 0.2891 0.2147 -0.0557 0.0239  0.0209  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2200 0.2515 0.2017 -0.0688 0.0262  0.0448  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2688 0.3443 0.2376 -0.0960 0.0715  0.0039  7   SER   A N   
122  N N   B SER   A 7   ? 0.2747 0.3323 0.2557 -0.1012 0.1212  0.0183  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2571 0.3336 0.2285 -0.0884 0.0682  -0.0111 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2732 0.3316 0.2740 -0.0829 0.1056  -0.0109 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2311 0.3008 0.1905 -0.0872 0.0734  -0.0104 7   SER   A C   
126  C C   B SER   A 7   ? 0.2525 0.3101 0.2482 -0.0760 0.1071  -0.0127 7   SER   A C   
127  O O   A SER   A 7   ? 0.2375 0.2925 0.1803 -0.0948 0.0820  -0.0075 7   SER   A O   
128  O O   B SER   A 7   ? 0.2580 0.3086 0.2477 -0.0810 0.1064  -0.0160 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2739 0.3517 0.2576 -0.0785 0.0616  -0.0149 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2912 0.3483 0.3119 -0.0728 0.0915  -0.0208 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2867 0.3622 0.2726 -0.0720 0.0556  -0.0151 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3050 0.3570 0.3455 -0.0660 0.0793  -0.0225 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2057 0.2755 0.1823 -0.0779 0.0619  -0.0155 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2294 0.2895 0.2316 -0.0664 0.1036  -0.0092 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1862 0.2534 0.1741 -0.0603 0.0607  -0.0092 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2116 0.2679 0.2283 -0.0529 0.0895  -0.0001 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1632 0.2327 0.1661 -0.0436 0.0451  -0.0060 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1856 0.2452 0.2156 -0.0420 0.0758  0.0082  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1631 0.2378 0.1781 -0.0281 0.0471  -0.0135 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1865 0.2455 0.2266 -0.0320 0.0763  0.0060  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1471 0.2075 0.1438 -0.0373 0.0323  0.0005  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1649 0.2225 0.2024 -0.0353 0.0534  0.0188  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1349 0.1851 0.1392 -0.0309 0.0210  0.0076  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1485 0.2033 0.1725 -0.0303 0.0401  0.0339  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1352 0.1669 0.1485 -0.0191 0.0200  0.0185  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1463 0.1831 0.1487 -0.0221 0.0424  0.0399  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1474 0.1796 0.1639 -0.0180 0.0087  0.0194  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1589 0.1997 0.1675 -0.0283 0.0229  0.0483  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1326 0.1835 0.1383 -0.0298 0.0174  -0.0001 9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1435 0.2130 0.1827 -0.0226 0.0272  0.0305  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1354 0.1820 0.1569 -0.0187 0.0336  -0.0104 9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1407 0.2173 0.1788 -0.0171 0.0317  0.0262  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1375 0.1779 0.1711 -0.0215 0.0422  -0.0162 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1477 0.2182 0.1893 -0.0235 0.0347  0.0236  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1361 0.1809 0.1704 -0.0160 0.0297  0.0060  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1348 0.2151 0.1697 -0.0093 0.0286  0.0315  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1436 0.1817 0.1985 -0.0147 0.0382  -0.0143 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1498 0.2143 0.1956 -0.0218 0.0327  0.0212  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1393 0.1791 0.1845 -0.0145 0.0289  0.0023  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1377 0.2140 0.1753 -0.0077 0.0308  0.0316  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1392 0.1821 0.2113 -0.0219 0.0350  -0.0063 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1392 0.2104 0.1965 -0.0188 0.0367  0.0307  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1505 0.1842 0.2381 -0.0297 0.0254  -0.0086 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1407 0.2109 0.2093 -0.0254 0.0404  0.0419  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1406 0.1452 0.1551 -0.0186 0.0226  0.0178  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1483 0.1581 0.1446 -0.0180 0.0401  0.0299  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1331 0.1369 0.1635 -0.0165 0.0226  0.0278  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1406 0.1518 0.1607 -0.0231 0.0306  0.0211  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1262 0.1265 0.1549 -0.0120 0.0249  0.0203  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1367 0.1355 0.1539 -0.0249 0.0192  0.0230  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1294 0.1248 0.1574 -0.0082 0.0368  0.0206  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1391 0.1250 0.1476 -0.0238 0.0388  0.0246  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1387 0.1456 0.2090 -0.0086 0.0118  0.0391  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1424 0.1573 0.1957 -0.0278 0.0219  0.0357  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1691 0.1598 0.2668 -0.0074 -0.0166 0.0487  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1657 0.1680 0.2455 -0.0206 -0.0046 0.0409  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1795 0.1723 0.2865 -0.0037 -0.0191 0.0528  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1743 0.1819 0.2747 -0.0201 -0.0058 0.0425  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1855 0.1703 0.2862 -0.0060 -0.0170 0.0371  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1780 0.1772 0.2619 -0.0271 -0.0100 0.0411  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1268 0.1214 0.1713 -0.0059 0.0263  0.0195  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1432 0.1324 0.1623 -0.0333 0.0127  0.0297  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1285 0.1225 0.1857 -0.0129 0.0228  0.0239  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1455 0.1272 0.1661 -0.0331 0.0096  0.0341  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1250 0.1269 0.1860 -0.0148 0.0317  0.0089  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1360 0.1212 0.1646 -0.0297 0.0058  0.0237  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1283 0.1360 0.2233 -0.0262 0.0396  -0.0039 11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1332 0.1300 0.1795 -0.0319 0.0143  0.0042  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1319 0.1281 0.1929 -0.0165 0.0175  0.0290  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1602 0.1280 0.1744 -0.0337 0.0010  0.0306  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1372 0.1311 0.1973 -0.0186 0.0184  0.0365  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1735 0.1394 0.1678 -0.0332 0.0083  0.0415  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1491 0.1398 0.2003 -0.0145 0.0077  0.0358  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1869 0.1503 0.1682 -0.0299 0.0120  0.0455  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1573 0.1380 0.1908 -0.0044 0.0027  0.0363  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1975 0.1542 0.1572 -0.0282 0.0126  0.0518  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1530 0.1309 0.1972 0.0061  -0.0029 0.0258  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1981 0.1541 0.1702 -0.0230 0.0105  0.0447  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1236 0.1243 0.1607 -0.0201 0.0330  0.0062  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1352 0.1322 0.1593 -0.0190 -0.0002 0.0156  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1319 0.1293 0.1592 -0.0251 0.0145  0.0148  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1338 0.1416 0.1643 -0.0162 0.0016  0.0224  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1317 0.1208 0.1735 -0.0259 0.0107  0.0145  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1309 0.1450 0.1604 -0.0094 0.0037  0.0232  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1311 0.1225 0.1880 -0.0233 0.0206  0.0017  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1362 0.1418 0.1567 0.0040  0.0017  0.0216  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1369 0.1289 0.1546 -0.0196 0.0091  0.0256  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1374 0.1539 0.1952 -0.0140 0.0015  0.0301  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1489 0.1410 0.1796 -0.0124 0.0197  0.0374  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1416 0.1648 0.2303 -0.0097 0.0090  0.0422  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1568 0.1515 0.1901 -0.0030 0.0107  0.0544  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1466 0.1770 0.2458 -0.0028 0.0135  0.0487  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1511 0.1438 0.1939 -0.0083 0.0241  0.0337  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1414 0.1710 0.2409 -0.0052 0.0082  0.0268  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1294 0.1221 0.1761 -0.0240 0.0033  0.0180  13  THR   A N   
320  N N   B THR   A 13  ? 0.1259 0.1406 0.1740 -0.0063 0.0051  0.0161  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1335 0.1298 0.1808 -0.0168 0.0100  0.0222  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1306 0.1397 0.1838 -0.0188 0.0161  0.0175  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1331 0.1313 0.1865 -0.0158 0.0036  0.0335  13  THR   A C   
324  C C   B THR   A 13  ? 0.1266 0.1499 0.1863 -0.0255 0.0211  0.0297  13  THR   A C   
325  O O   A THR   A 13  ? 0.1381 0.1316 0.1833 -0.0114 0.0028  0.0312  13  THR   A O   
326  O O   B THR   A 13  ? 0.1388 0.1576 0.1791 -0.0282 0.0072  0.0335  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1371 0.1384 0.1917 -0.0140 0.0128  0.0269  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1324 0.1438 0.1952 -0.0099 0.0199  0.0274  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1437 0.1311 0.2039 -0.0074 0.0047  0.0262  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1203 0.1454 0.2047 -0.0131 0.0307  0.0373  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1374 0.1583 0.1913 -0.0195 0.0230  0.0191  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1442 0.1643 0.2046 -0.0040 0.0184  0.0125  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1389 0.1372 0.2104 -0.0154 0.0033  0.0462  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1314 0.1535 0.2062 -0.0318 0.0246  0.0457  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1455 0.1477 0.2326 -0.0113 -0.0047 0.0562  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1379 0.1611 0.2302 -0.0322 0.0107  0.0634  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1416 0.1509 0.2021 -0.0137 -0.0101 0.0577  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1395 0.1547 0.2140 -0.0270 -0.0029 0.0630  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1502 0.1568 0.1913 -0.0133 -0.0169 0.0607  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1542 0.1576 0.2258 -0.0315 -0.0105 0.0633  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1689 0.1696 0.2917 -0.0106 0.0016  0.0716  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1604 0.1857 0.2787 -0.0329 0.0088  0.0885  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1883 0.2064 0.3652 -0.0192 0.0111  0.0667  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.1676 0.2288 0.3401 -0.0360 0.0116  0.0884  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2020 0.2293 0.3961 -0.0097 0.0023  0.0653  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.1724 0.2485 0.3639 -0.0238 0.0024  0.0878  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2023 0.2181 0.3985 -0.0273 0.0135  0.0562  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.1764 0.2490 0.3798 -0.0352 0.0090  0.0777  14  ASP   A OD2 
371  N N   . ASN   A 15  ? 0.1295 0.1435 0.2030 -0.0265 -0.0024 0.0590  15  ASN   A N   
372  C CA  . ASN   A 15  ? 0.1352 0.1456 0.2220 -0.0201 -0.0106 0.0411  15  ASN   A CA  
373  C C   . ASN   A 15  ? 0.1294 0.1370 0.2348 -0.0252 -0.0012 0.0497  15  ASN   A C   
374  O O   . ASN   A 15  ? 0.1343 0.1408 0.2841 -0.0229 -0.0256 0.0560  15  ASN   A O   
375  C CB  . ASN   A 15  ? 0.1331 0.1424 0.2204 -0.0164 -0.0042 0.0459  15  ASN   A CB  
376  C CG  . ASN   A 15  ? 0.1300 0.1512 0.2259 -0.0109 0.0054  0.0328  15  ASN   A CG  
377  O OD1 . ASN   A 15  ? 0.1437 0.1563 0.2356 -0.0278 -0.0031 0.0466  15  ASN   A OD1 
378  N ND2 . ASN   A 15  ? 0.1358 0.1562 0.2115 -0.0216 0.0087  0.0278  15  ASN   A ND2 
386  N N   A VAL   A 16  ? 0.1295 0.1332 0.2093 -0.0178 0.0015  0.0475  16  VAL   A N   
387  N N   B VAL   A 16  ? 0.1270 0.1457 0.2230 -0.0155 -0.0014 0.0581  16  VAL   A N   
388  C CA  A VAL   A 16  ? 0.1289 0.1342 0.1994 -0.0207 0.0049  0.0391  16  VAL   A CA  
389  C CA  B VAL   A 16  ? 0.1245 0.1546 0.2077 -0.0153 0.0110  0.0609  16  VAL   A CA  
390  C C   A VAL   A 16  ? 0.1225 0.1250 0.1911 -0.0263 -0.0018 0.0353  16  VAL   A C   
391  C C   B VAL   A 16  ? 0.1203 0.1599 0.1951 -0.0165 0.0057  0.0610  16  VAL   A C   
392  O O   A VAL   A 16  ? 0.1147 0.1218 0.1869 -0.0312 0.0004  0.0277  16  VAL   A O   
393  O O   B VAL   A 16  ? 0.1181 0.1606 0.1824 -0.0180 0.0084  0.0467  16  VAL   A O   
394  C CB  A VAL   A 16  ? 0.1403 0.1467 0.1921 -0.0035 0.0109  0.0390  16  VAL   A CB  
395  C CB  B VAL   A 16  ? 0.1333 0.1594 0.1971 0.0016  0.0219  0.0594  16  VAL   A CB  
396  C CG1 A VAL   A 16  ? 0.1525 0.1586 0.1888 0.0037  0.0113  0.0360  16  VAL   A CG1 
397  C CG1 B VAL   A 16  ? 0.1433 0.1698 0.1938 0.0099  0.0267  0.0539  16  VAL   A CG1 
398  C CG2 A VAL   A 16  ? 0.1434 0.1571 0.1963 -0.0019 0.0171  0.0308  16  VAL   A CG2 
399  C CG2 B VAL   A 16  ? 0.1335 0.1656 0.2098 0.0041  0.0302  0.0539  16  VAL   A CG2 
418  N N   A TYR   A 17  ? 0.1201 0.1142 0.1915 -0.0281 0.0099  0.0438  17  TYR   A N   
419  N N   B TYR   A 17  ? 0.1163 0.1544 0.1985 -0.0150 0.0060  0.0591  17  TYR   A N   
420  C CA  A TYR   A 17  ? 0.1320 0.1214 0.1715 -0.0275 0.0089  0.0399  17  TYR   A CA  
421  C CA  B TYR   A 17  ? 0.1191 0.1565 0.1762 -0.0139 0.0023  0.0518  17  TYR   A CA  
422  C C   A TYR   A 17  ? 0.1301 0.1138 0.1718 -0.0245 0.0070  0.0333  17  TYR   A C   
423  C C   B TYR   A 17  ? 0.1186 0.1512 0.1733 -0.0111 0.0043  0.0497  17  TYR   A C   
424  O O   A TYR   A 17  ? 0.1263 0.1111 0.1547 -0.0223 0.0090  0.0330  17  TYR   A O   
425  O O   B TYR   A 17  ? 0.1151 0.1526 0.1694 -0.0177 0.0013  0.0417  17  TYR   A O   
426  C CB  A TYR   A 17  ? 0.1492 0.1264 0.1727 -0.0370 -0.0016 0.0508  17  TYR   A CB  
427  C CB  B TYR   A 17  ? 0.1301 0.1615 0.1757 -0.0125 -0.0098 0.0449  17  TYR   A CB  
428  C CG  A TYR   A 17  ? 0.1694 0.1393 0.1866 -0.0361 -0.0180 0.0526  17  TYR   A CG  
429  C CG  B TYR   A 17  ? 0.1441 0.1737 0.1798 -0.0103 -0.0171 0.0375  17  TYR   A CG  
430  C CD1 A TYR   A 17  ? 0.1782 0.1471 0.2007 -0.0327 -0.0265 0.0445  17  TYR   A CD1 
431  C CD1 B TYR   A 17  ? 0.1568 0.1822 0.1882 0.0009  -0.0150 0.0417  17  TYR   A CD1 
432  C CD2 A TYR   A 17  ? 0.1776 0.1405 0.1816 -0.0480 -0.0268 0.0619  17  TYR   A CD2 
433  C CD2 B TYR   A 17  ? 0.1519 0.1816 0.1775 -0.0164 -0.0211 0.0350  17  TYR   A CD2 
434  C CE1 A TYR   A 17  ? 0.1872 0.1455 0.2005 -0.0366 -0.0382 0.0459  17  TYR   A CE1 
435  C CE1 B TYR   A 17  ? 0.1772 0.1892 0.1970 0.0038  -0.0176 0.0426  17  TYR   A CE1 
436  C CE2 A TYR   A 17  ? 0.1891 0.1401 0.1947 -0.0537 -0.0377 0.0470  17  TYR   A CE2 
437  C CE2 B TYR   A 17  ? 0.1727 0.1885 0.1799 -0.0132 -0.0255 0.0295  17  TYR   A CE2 
438  C CZ  A TYR   A 17  ? 0.1975 0.1393 0.1922 -0.0480 -0.0449 0.0482  17  TYR   A CZ  
439  C CZ  B TYR   A 17  ? 0.1864 0.1922 0.1904 -0.0026 -0.0259 0.0410  17  TYR   A CZ  
440  O OH  A TYR   A 17  ? 0.2091 0.1338 0.1952 -0.0519 -0.0475 0.0430  17  TYR   A OH  
441  O OH  B TYR   A 17  ? 0.1993 0.1986 0.2083 0.0041  -0.0173 0.0405  17  TYR   A OH  
460  N N   A ILE   A 18  ? 0.1367 0.1203 0.1759 -0.0249 0.0120  0.0387  18  ILE   A N   
461  N N   B ILE   A 18  ? 0.1188 0.1505 0.1736 -0.0128 0.0121  0.0532  18  ILE   A N   
462  C CA  A ILE   A 18  ? 0.1422 0.1249 0.1694 -0.0223 0.0180  0.0346  18  ILE   A CA  
463  C CA  B ILE   A 18  ? 0.1203 0.1469 0.1579 -0.0089 0.0141  0.0425  18  ILE   A CA  
464  C C   A ILE   A 18  ? 0.1410 0.1283 0.1876 -0.0293 0.0230  0.0299  18  ILE   A C   
465  C C   B ILE   A 18  ? 0.1203 0.1572 0.1570 -0.0087 0.0086  0.0384  18  ILE   A C   
466  O O   A ILE   A 18  ? 0.1345 0.1359 0.1837 -0.0414 0.0216  0.0228  18  ILE   A O   
467  O O   B ILE   A 18  ? 0.1192 0.1660 0.1539 -0.0229 0.0222  0.0320  18  ILE   A O   
468  C CB  A ILE   A 18  ? 0.1475 0.1275 0.1515 -0.0141 0.0186  0.0309  18  ILE   A CB  
469  C CB  B ILE   A 18  ? 0.1252 0.1447 0.1425 -0.0039 0.0139  0.0477  18  ILE   A CB  
470  C CG1 A ILE   A 18  ? 0.1526 0.1389 0.1502 -0.0050 0.0087  0.0206  18  ILE   A CG1 
471  C CG1 B ILE   A 18  ? 0.1445 0.1584 0.1516 -0.0036 0.0133  0.0547  18  ILE   A CG1 
472  C CG2 A ILE   A 18  ? 0.1491 0.1299 0.1521 -0.0021 0.0199  0.0154  18  ILE   A CG2 
473  C CG2 B ILE   A 18  ? 0.1309 0.1575 0.1449 -0.0030 0.0022  0.0391  18  ILE   A CG2 
474  C CD1 A ILE   A 18  ? 0.1695 0.1555 0.1696 0.0100  0.0153  0.0178  18  ILE   A CD1 
475  C CD1 B ILE   A 18  ? 0.1702 0.1811 0.1699 0.0061  0.0159  0.0552  18  ILE   A CD1 
498  N N   A LYS   A 19  ? 0.1405 0.1309 0.2039 -0.0265 0.0408  0.0378  19  LYS   A N   
499  N N   B LYS   A 19  ? 0.1279 0.1628 0.1725 0.0012  0.0284  0.0431  19  LYS   A N   
500  C CA  A LYS   A 19  ? 0.1491 0.1448 0.2106 -0.0164 0.0417  0.0386  19  LYS   A CA  
501  C CA  B LYS   A 19  ? 0.1425 0.1804 0.2049 0.0176  0.0317  0.0418  19  LYS   A CA  
502  C C   A LYS   A 19  ? 0.1387 0.1342 0.2073 -0.0123 0.0429  0.0415  19  LYS   A C   
503  C C   B LYS   A 19  ? 0.1286 0.1766 0.2285 0.0151  0.0347  0.0497  19  LYS   A C   
504  O O   A LYS   A 19  ? 0.1278 0.1228 0.1936 -0.0084 0.0374  0.0314  19  LYS   A O   
505  O O   B LYS   A 19  ? 0.1253 0.1736 0.2304 0.0109  0.0260  0.0503  19  LYS   A O   
506  C CB  A LYS   A 19  ? 0.1561 0.1608 0.2154 -0.0205 0.0527  0.0415  19  LYS   A CB  
507  C CB  B LYS   A 19  ? 0.1579 0.1966 0.2061 0.0258  0.0394  0.0340  19  LYS   A CB  
508  C CG  A LYS   A 19  ? 0.1768 0.1791 0.2227 -0.0137 0.0590  0.0425  19  LYS   A CG  
509  C CG  B LYS   A 19  ? 0.1774 0.2184 0.2123 0.0320  0.0449  0.0254  19  LYS   A CG  
510  C CD  A LYS   A 19  ? 0.1969 0.1910 0.2287 -0.0079 0.0663  0.0387  19  LYS   A CD  
511  C CD  B LYS   A 19  ? 0.1994 0.2368 0.2216 0.0337  0.0467  0.0174  19  LYS   A CD  
512  C CE  A LYS   A 19  ? 0.2093 0.1955 0.2390 -0.0093 0.0656  0.0360  19  LYS   A CE  
513  C CE  B LYS   A 19  ? 0.2122 0.2498 0.2267 0.0272  0.0461  0.0134  19  LYS   A CE  
514  N NZ  A LYS   A 19  ? 0.2154 0.1967 0.2461 -0.0152 0.0706  0.0293  19  LYS   A NZ  
515  N NZ  B LYS   A 19  ? 0.2180 0.2555 0.2251 0.0248  0.0479  0.0056  19  LYS   A NZ  
542  N N   A ASN   A 20  ? 0.1476 0.1405 0.2242 -0.0129 0.0474  0.0549  20  ASN   A N   
543  N N   B ASN   A 20  ? 0.1291 0.1820 0.2576 0.0135  0.0343  0.0594  20  ASN   A N   
544  C CA  A ASN   A 20  ? 0.1503 0.1561 0.2397 0.0021  0.0520  0.0555  20  ASN   A CA  
545  C CA  B ASN   A 20  ? 0.1393 0.1938 0.2810 0.0271  0.0484  0.0614  20  ASN   A CA  
546  C C   A ASN   A 20  ? 0.1663 0.1577 0.2362 0.0016  0.0573  0.0484  20  ASN   A C   
547  C C   B ASN   A 20  ? 0.1556 0.1896 0.2702 0.0156  0.0640  0.0536  20  ASN   A C   
548  O O   A ASN   A 20  ? 0.1804 0.1630 0.2343 -0.0031 0.0608  0.0490  20  ASN   A O   
549  O O   B ASN   A 20  ? 0.1791 0.2017 0.2740 0.0084  0.0630  0.0519  20  ASN   A O   
550  C CB  A ASN   A 20  ? 0.1501 0.1713 0.2686 0.0141  0.0494  0.0667  20  ASN   A CB  
551  C CB  B ASN   A 20  ? 0.1467 0.2110 0.3154 0.0434  0.0438  0.0773  20  ASN   A CB  
552  C CG  A ASN   A 20  ? 0.1547 0.1847 0.3044 0.0252  0.0547  0.0832  20  ASN   A CG  
553  C CG  B ASN   A 20  ? 0.1601 0.2276 0.3567 0.0595  0.0438  0.0917  20  ASN   A CG  
554  O OD1 A ASN   A 20  ? 0.1835 0.1966 0.3352 0.0390  0.0708  0.0785  20  ASN   A OD1 
555  O OD1 B ASN   A 20  ? 0.1954 0.2439 0.4008 0.0613  0.0660  0.0768  20  ASN   A OD1 
556  N ND2 A ASN   A 20  ? 0.1490 0.1861 0.3112 0.0184  0.0502  0.0930  20  ASN   A ND2 
557  N ND2 B ASN   A 20  ? 0.1630 0.2282 0.3590 0.0621  0.0286  0.1104  20  ASN   A ND2 
570  N N   A ALA   A 21  ? 0.1703 0.1619 0.2304 0.0012  0.0467  0.0314  21  ALA   A N   
571  N N   B ALA   A 21  ? 0.1548 0.1792 0.2523 0.0042  0.0672  0.0400  21  ALA   A N   
572  C CA  A ALA   A 21  ? 0.1833 0.1668 0.2317 -0.0012 0.0298  0.0350  21  ALA   A CA  
573  C CA  B ALA   A 21  ? 0.1629 0.1699 0.2408 -0.0069 0.0585  0.0425  21  ALA   A CA  
574  C C   A ALA   A 21  ? 0.1789 0.1724 0.2104 0.0027  0.0262  0.0303  21  ALA   A C   
575  C C   B ALA   A 21  ? 0.1463 0.1577 0.2064 -0.0088 0.0534  0.0397  21  ALA   A C   
576  O O   A ALA   A 21  ? 0.1823 0.1816 0.2106 0.0017  0.0302  0.0169  21  ALA   A O   
577  O O   B ALA   A 21  ? 0.1454 0.1465 0.2155 -0.0071 0.0459  0.0175  21  ALA   A O   
578  C CB  A ALA   A 21  ? 0.1994 0.1743 0.2466 -0.0088 0.0174  0.0463  21  ALA   A CB  
579  C CB  B ALA   A 21  ? 0.1851 0.1809 0.2575 -0.0194 0.0502  0.0488  21  ALA   A CB  
590  N N   A ASP   A 22  ? 0.1803 0.1679 0.2085 0.0023  0.0211  0.0332  22  ASP   A N   
591  N N   B ASP   A 22  ? 0.1416 0.1561 0.1880 -0.0062 0.0506  0.0373  22  ASP   A N   
592  C CA  A ASP   A 22  ? 0.1810 0.1657 0.2052 0.0040  0.0089  0.0438  22  ASP   A CA  
593  C CA  B ASP   A 22  ? 0.1405 0.1526 0.1679 -0.0056 0.0415  0.0304  22  ASP   A CA  
594  C C   A ASP   A 22  ? 0.1694 0.1688 0.1667 0.0003  0.0149  0.0429  22  ASP   A C   
595  C C   B ASP   A 22  ? 0.1338 0.1490 0.1406 -0.0124 0.0412  0.0217  22  ASP   A C   
596  O O   A ASP   A 22  ? 0.1700 0.1755 0.1619 0.0005  0.0196  0.0376  22  ASP   A O   
597  O O   B ASP   A 22  ? 0.1369 0.1631 0.1504 -0.0171 0.0410  0.0065  22  ASP   A O   
598  C CB  A ASP   A 22  ? 0.2018 0.1718 0.2388 0.0058  0.0044  0.0364  22  ASP   A CB  
599  C CB  B ASP   A 22  ? 0.1577 0.1552 0.2005 0.0027  0.0392  0.0251  22  ASP   A CB  
600  C CG  A ASP   A 22  ? 0.2181 0.1798 0.2611 -0.0019 -0.0044 0.0378  22  ASP   A CG  
601  C CG  B ASP   A 22  ? 0.1654 0.1550 0.2209 0.0082  0.0378  0.0285  22  ASP   A CG  
602  O OD1 A ASP   A 22  ? 0.2155 0.1811 0.2747 -0.0174 -0.0142 0.0500  22  ASP   A OD1 
603  O OD1 B ASP   A 22  ? 0.1621 0.1525 0.1855 -0.0013 0.0383  0.0271  22  ASP   A OD1 
604  O OD2 A ASP   A 22  ? 0.2345 0.1842 0.2708 0.0003  -0.0076 0.0249  22  ASP   A OD2 
605  O OD2 B ASP   A 22  ? 0.1838 0.1644 0.2664 0.0066  0.0425  0.0290  22  ASP   A OD2 
614  N N   A ILE   A 23  ? 0.1677 0.1650 0.1490 -0.0005 0.0170  0.0351  23  ILE   A N   
615  N N   B ILE   A 23  ? 0.1329 0.1422 0.1360 -0.0101 0.0364  0.0240  23  ILE   A N   
616  C CA  A ILE   A 23  ? 0.1611 0.1563 0.1368 -0.0014 0.0145  0.0274  23  ILE   A CA  
617  C CA  B ILE   A 23  ? 0.1331 0.1461 0.1272 -0.0087 0.0267  0.0147  23  ILE   A CA  
618  C C   A ILE   A 23  ? 0.1546 0.1623 0.1380 -0.0012 0.0245  0.0188  23  ILE   A C   
619  C C   B ILE   A 23  ? 0.1301 0.1541 0.1331 -0.0148 0.0216  0.0108  23  ILE   A C   
620  O O   A ILE   A 23  ? 0.1595 0.1712 0.1475 -0.0016 0.0206  0.0143  23  ILE   A O   
621  O O   B ILE   A 23  ? 0.1361 0.1534 0.1442 -0.0148 0.0091  0.0178  23  ILE   A O   
622  C CB  A ILE   A 23  ? 0.1642 0.1550 0.1293 0.0042  0.0230  0.0217  23  ILE   A CB  
623  C CB  B ILE   A 23  ? 0.1415 0.1397 0.1338 -0.0012 0.0215  0.0106  23  ILE   A CB  
624  C CG1 A ILE   A 23  ? 0.1678 0.1554 0.1338 0.0056  0.0251  0.0111  23  ILE   A CG1 
625  C CG1 B ILE   A 23  ? 0.1517 0.1412 0.1374 -0.0084 0.0128  0.0047  23  ILE   A CG1 
626  C CG2 A ILE   A 23  ? 0.1657 0.1579 0.1393 0.0087  0.0272  0.0268  23  ILE   A CG2 
627  C CG2 B ILE   A 23  ? 0.1385 0.1302 0.1410 0.0077  0.0264  0.0204  23  ILE   A CG2 
628  C CD1 A ILE   A 23  ? 0.1684 0.1547 0.1435 0.0046  0.0198  0.0063  23  ILE   A CD1 
629  C CD1 B ILE   A 23  ? 0.1497 0.1446 0.1370 -0.0046 0.0034  0.0015  23  ILE   A CD1 
652  N N   A VAL   A 24  ? 0.1582 0.1653 0.1527 -0.0073 0.0201  0.0108  24  VAL   A N   
653  N N   B VAL   A 24  ? 0.1411 0.1602 0.1355 -0.0188 0.0200  0.0013  24  VAL   A N   
654  C CA  A VAL   A 24  ? 0.1688 0.1764 0.1728 -0.0106 0.0159  0.0058  24  VAL   A CA  
655  C CA  B VAL   A 24  ? 0.1634 0.1634 0.1561 -0.0259 0.0156  -0.0026 24  VAL   A CA  
656  C C   A VAL   A 24  ? 0.1721 0.1896 0.1765 -0.0197 0.0053  0.0047  24  VAL   A C   
657  C C   B VAL   A 24  ? 0.1746 0.1835 0.1684 -0.0325 0.0199  -0.0057 24  VAL   A C   
658  O O   A VAL   A 24  ? 0.1821 0.1924 0.1799 -0.0222 0.0043  0.0063  24  VAL   A O   
659  O O   B VAL   A 24  ? 0.1920 0.1918 0.1853 -0.0291 0.0255  -0.0002 24  VAL   A O   
660  C CB  A VAL   A 24  ? 0.1757 0.1823 0.1847 -0.0087 0.0264  0.0089  24  VAL   A CB  
661  C CB  B VAL   A 24  ? 0.1719 0.1602 0.1757 -0.0299 0.0197  0.0013  24  VAL   A CB  
662  C CG1 A VAL   A 24  ? 0.1791 0.1934 0.1842 -0.0011 0.0356  -0.0079 24  VAL   A CG1 
663  C CG1 B VAL   A 24  ? 0.1850 0.1723 0.2075 -0.0209 0.0129  -0.0051 24  VAL   A CG1 
664  C CG2 A VAL   A 24  ? 0.1839 0.1836 0.1899 -0.0089 0.0330  0.0166  24  VAL   A CG2 
665  C CG2 B VAL   A 24  ? 0.1743 0.1592 0.1837 -0.0421 0.0273  0.0045  24  VAL   A CG2 
684  N N   A GLU   A 25  ? 0.1720 0.2024 0.1730 -0.0245 0.0120  -0.0043 25  GLU   A N   
685  N N   B GLU   A 25  ? 0.1729 0.2065 0.1706 -0.0312 0.0394  -0.0091 25  GLU   A N   
686  C CA  A GLU   A 25  ? 0.1890 0.2231 0.1861 -0.0154 0.0195  -0.0064 25  GLU   A CA  
687  C CA  B GLU   A 25  ? 0.1843 0.2293 0.1804 -0.0364 0.0437  -0.0101 25  GLU   A CA  
688  C C   A GLU   A 25  ? 0.1771 0.2239 0.1576 -0.0184 0.0274  -0.0069 25  GLU   A C   
689  C C   B GLU   A 25  ? 0.1766 0.2402 0.1673 -0.0324 0.0434  -0.0090 25  GLU   A C   
690  O O   A GLU   A 25  ? 0.1736 0.2340 0.1648 -0.0178 0.0209  -0.0063 25  GLU   A O   
691  O O   B GLU   A 25  ? 0.1830 0.2451 0.1760 -0.0264 0.0465  -0.0107 25  GLU   A O   
692  C CB  A GLU   A 25  ? 0.2136 0.2430 0.2328 -0.0130 0.0148  -0.0060 25  GLU   A CB  
693  C CB  B GLU   A 25  ? 0.2055 0.2423 0.2211 -0.0377 0.0528  -0.0181 25  GLU   A CB  
694  C CG  A GLU   A 25  ? 0.2412 0.2638 0.2907 -0.0194 0.0013  -0.0132 25  GLU   A CG  
695  C CG  B GLU   A 25  ? 0.2395 0.2604 0.2895 -0.0380 0.0483  -0.0294 25  GLU   A CG  
696  C CD  A GLU   A 25  ? 0.2622 0.2834 0.3396 -0.0238 -0.0107 -0.0181 25  GLU   A CD  
697  C CD  B GLU   A 25  ? 0.2675 0.2784 0.3557 -0.0406 0.0394  -0.0357 25  GLU   A CD  
698  O OE1 A GLU   A 25  ? 0.2717 0.2930 0.3466 -0.0226 -0.0222 -0.0268 25  GLU   A OE1 
699  O OE1 B GLU   A 25  ? 0.2789 0.2860 0.3865 -0.0412 0.0347  -0.0403 25  GLU   A OE1 
700  O OE2 A GLU   A 25  ? 0.2696 0.2920 0.3680 -0.0252 -0.0124 -0.0204 25  GLU   A OE2 
701  O OE2 B GLU   A 25  ? 0.2765 0.2857 0.3805 -0.0410 0.0359  -0.0355 25  GLU   A OE2 
714  N N   A GLU   A 26  ? 0.1711 0.2145 0.1474 -0.0351 0.0334  -0.0016 26  GLU   A N   
715  N N   B GLU   A 26  ? 0.1668 0.2406 0.1598 -0.0408 0.0426  -0.0097 26  GLU   A N   
716  C CA  A GLU   A 26  ? 0.1870 0.2184 0.1400 -0.0468 0.0341  0.0102  26  GLU   A CA  
717  C CA  B GLU   A 26  ? 0.1761 0.2412 0.1650 -0.0415 0.0463  -0.0004 26  GLU   A CA  
718  C C   A GLU   A 26  ? 0.1868 0.2158 0.1211 -0.0459 0.0298  0.0108  26  GLU   A C   
719  C C   B GLU   A 26  ? 0.1698 0.2244 0.1420 -0.0344 0.0382  0.0103  26  GLU   A C   
720  O O   A GLU   A 26  ? 0.1939 0.2191 0.1157 -0.0434 0.0230  0.0060  26  GLU   A O   
721  O O   B GLU   A 26  ? 0.1810 0.2233 0.1343 -0.0379 0.0457  0.0117  26  GLU   A O   
722  C CB  A GLU   A 26  ? 0.2058 0.2235 0.1657 -0.0629 0.0388  0.0245  26  GLU   A CB  
723  C CB  B GLU   A 26  ? 0.1917 0.2521 0.2003 -0.0491 0.0379  -0.0029 26  GLU   A CB  
724  C CG  A GLU   A 26  ? 0.2291 0.2435 0.2431 -0.0689 0.0368  0.0178  26  GLU   A CG  
725  C CG  B GLU   A 26  ? 0.2035 0.2651 0.2294 -0.0552 0.0477  -0.0134 26  GLU   A CG  
726  C CD  A GLU   A 26  ? 0.2457 0.2559 0.2910 -0.0780 0.0463  0.0208  26  GLU   A CD  
727  C CD  B GLU   A 26  ? 0.2123 0.2781 0.2405 -0.0622 0.0612  -0.0165 26  GLU   A CD  
728  O OE1 A GLU   A 26  ? 0.2490 0.2743 0.3077 -0.0669 0.0587  0.0016  26  GLU   A OE1 
729  O OE1 B GLU   A 26  ? 0.2172 0.2996 0.2439 -0.0510 0.0888  -0.0217 26  GLU   A OE1 
730  O OE2 A GLU   A 26  ? 0.2583 0.2595 0.3024 -0.0835 0.0464  0.0360  26  GLU   A OE2 
731  O OE2 B GLU   A 26  ? 0.2161 0.2759 0.2077 -0.0684 0.0641  -0.0159 26  GLU   A OE2 
744  N N   A ALA   A 27  ? 0.1767 0.2117 0.1335 -0.0560 0.0352  0.0170  27  ALA   A N   
745  N N   B ALA   A 27  ? 0.1484 0.2068 0.1304 -0.0207 0.0264  0.0246  27  ALA   A N   
746  C CA  A ALA   A 27  ? 0.1814 0.2206 0.1413 -0.0577 0.0330  0.0101  27  ALA   A CA  
747  C CA  B ALA   A 27  ? 0.1506 0.2061 0.1259 0.0012  0.0108  0.0260  27  ALA   A CA  
748  C C   A ALA   A 27  ? 0.1970 0.2366 0.1553 -0.0640 0.0340  0.0028  27  ALA   A C   
749  C C   B ALA   A 27  ? 0.1667 0.2179 0.1266 0.0096  0.0064  0.0126  27  ALA   A C   
750  O O   A ALA   A 27  ? 0.2008 0.2367 0.1617 -0.0677 0.0246  -0.0010 27  ALA   A O   
751  O O   B ALA   A 27  ? 0.1629 0.2152 0.1481 0.0110  0.0056  0.0065  27  ALA   A O   
752  C CB  A ALA   A 27  ? 0.1738 0.2152 0.1511 -0.0624 0.0268  0.0098  27  ALA   A CB  
753  C CB  B ALA   A 27  ? 0.1433 0.1973 0.1278 -0.0037 0.0059  0.0340  27  ALA   A CB  
764  N N   A LYS   A 28  ? 0.2217 0.2631 0.1790 -0.0519 0.0299  -0.0176 28  LYS   A N   
765  N N   B LYS   A 28  ? 0.1994 0.2367 0.1317 0.0267  -0.0041 -0.0078 28  LYS   A N   
766  C CA  A LYS   A 28  ? 0.2550 0.2936 0.2114 -0.0359 0.0258  -0.0274 28  LYS   A CA  
767  C CA  B LYS   A 28  ? 0.2375 0.2691 0.1606 0.0463  -0.0118 -0.0273 28  LYS   A CA  
768  C C   A LYS   A 28  ? 0.2716 0.3174 0.2146 -0.0387 0.0370  -0.0211 28  LYS   A C   
769  C C   B LYS   A 28  ? 0.2594 0.2886 0.1543 0.0497  0.0012  -0.0133 28  LYS   A C   
770  O O   A LYS   A 28  ? 0.2748 0.3228 0.2338 -0.0370 0.0230  -0.0228 28  LYS   A O   
771  O O   B LYS   A 28  ? 0.2709 0.2958 0.1646 0.0494  -0.0142 -0.0145 28  LYS   A O   
772  C CB  A LYS   A 28  ? 0.2716 0.3045 0.2481 -0.0163 0.0151  -0.0347 28  LYS   A CB  
773  C CB  B LYS   A 28  ? 0.2588 0.2869 0.2131 0.0591  -0.0230 -0.0503 28  LYS   A CB  
774  C CG  A LYS   A 28  ? 0.2876 0.3153 0.2887 -0.0012 0.0058  -0.0362 28  LYS   A CG  
775  C CG  B LYS   A 28  ? 0.2773 0.3076 0.2774 0.0653  -0.0327 -0.0563 28  LYS   A CG  
776  C CD  A LYS   A 28  ? 0.3005 0.3282 0.3344 0.0093  -0.0078 -0.0345 28  LYS   A CD  
777  C CD  B LYS   A 28  ? 0.2959 0.3294 0.3445 0.0698  -0.0454 -0.0559 28  LYS   A CD  
778  C CE  A LYS   A 28  ? 0.3092 0.3380 0.3659 0.0153  -0.0193 -0.0344 28  LYS   A CE  
779  C CE  B LYS   A 28  ? 0.3114 0.3449 0.3916 0.0717  -0.0543 -0.0595 28  LYS   A CE  
780  N NZ  A LYS   A 28  ? 0.3144 0.3426 0.3872 0.0198  -0.0229 -0.0371 28  LYS   A NZ  
781  N NZ  B LYS   A 28  ? 0.3187 0.3524 0.4128 0.0730  -0.0624 -0.0624 28  LYS   A NZ  
808  N N   A LYS   A 29  ? 0.2829 0.3356 0.2157 -0.0446 0.0640  -0.0042 29  LYS   A N   
809  N N   B LYS   A 29  ? 0.2654 0.3032 0.1526 0.0494  0.0390  0.0111  29  LYS   A N   
810  C CA  A LYS   A 29  ? 0.3011 0.3554 0.2351 -0.0468 0.0830  0.0061  29  LYS   A CA  
811  C CA  B LYS   A 29  ? 0.2800 0.3237 0.1712 0.0435  0.0633  0.0323  29  LYS   A CA  
812  C C   A LYS   A 29  ? 0.2963 0.3457 0.2093 -0.0585 0.0741  0.0109  29  LYS   A C   
813  C C   B LYS   A 29  ? 0.2768 0.3143 0.1446 0.0305  0.0556  0.0442  29  LYS   A C   
814  O O   A LYS   A 29  ? 0.3072 0.3544 0.2214 -0.0515 0.0696  0.0054  29  LYS   A O   
815  O O   B LYS   A 29  ? 0.2891 0.3242 0.1583 0.0344  0.0482  0.0419  29  LYS   A O   
816  C CB  A LYS   A 29  ? 0.3206 0.3818 0.2861 -0.0366 0.1036  0.0090  29  LYS   A CB  
817  C CB  B LYS   A 29  ? 0.2991 0.3520 0.2228 0.0479  0.0949  0.0346  29  LYS   A CB  
818  C CG  A LYS   A 29  ? 0.3415 0.4052 0.3462 -0.0268 0.1099  0.0117  29  LYS   A CG  
819  C CG  B LYS   A 29  ? 0.3216 0.3780 0.2948 0.0520  0.1089  0.0336  29  LYS   A CG  
820  C CD  A LYS   A 29  ? 0.3598 0.4241 0.4077 -0.0188 0.1085  0.0105  29  LYS   A CD  
821  C CD  B LYS   A 29  ? 0.3413 0.3988 0.3691 0.0557  0.1118  0.0300  29  LYS   A CD  
822  C CE  A LYS   A 29  ? 0.3726 0.4369 0.4489 -0.0134 0.1087  0.0107  29  LYS   A CE  
823  C CE  B LYS   A 29  ? 0.3560 0.4141 0.4215 0.0564  0.1137  0.0269  29  LYS   A CE  
824  N NZ  A LYS   A 29  ? 0.3782 0.4437 0.4755 -0.0094 0.1078  0.0099  29  LYS   A NZ  
825  N NZ  B LYS   A 29  ? 0.3624 0.4220 0.4546 0.0582  0.1127  0.0256  29  LYS   A NZ  
852  N N   A VAL   A 30  ? 0.2794 0.3256 0.1890 -0.0761 0.0632  0.0173  30  VAL   A N   
853  N N   B VAL   A 30  ? 0.2610 0.2951 0.1373 0.0140  0.0517  0.0505  30  VAL   A N   
854  C CA  A VAL   A 30  ? 0.2698 0.3054 0.1717 -0.0888 0.0443  0.0263  30  VAL   A CA  
855  C CA  B VAL   A 30  ? 0.2470 0.2774 0.1427 -0.0044 0.0360  0.0574  30  VAL   A CA  
856  C C   A VAL   A 30  ? 0.2651 0.2871 0.1335 -0.0823 0.0338  0.0364  30  VAL   A C   
857  C C   B VAL   A 30  ? 0.2459 0.2694 0.1276 -0.0059 0.0247  0.0470  30  VAL   A C   
858  O O   A VAL   A 30  ? 0.2722 0.2920 0.1518 -0.0745 0.0257  0.0327  30  VAL   A O   
859  O O   B VAL   A 30  ? 0.2530 0.2705 0.1387 -0.0085 0.0176  0.0496  30  VAL   A O   
860  C CB  A VAL   A 30  ? 0.2684 0.3051 0.2042 -0.1000 0.0278  0.0189  30  VAL   A CB  
861  C CB  B VAL   A 30  ? 0.2398 0.2669 0.1850 -0.0159 0.0214  0.0654  30  VAL   A CB  
862  C CG1 A VAL   A 30  ? 0.2721 0.3046 0.2190 -0.1001 0.0185  0.0142  30  VAL   A CG1 
863  C CG1 B VAL   A 30  ? 0.2433 0.2636 0.2057 -0.0179 0.0102  0.0634  30  VAL   A CG1 
864  C CG2 A VAL   A 30  ? 0.2646 0.3055 0.2195 -0.1079 0.0249  0.0139  30  VAL   A CG2 
865  C CG2 B VAL   A 30  ? 0.2347 0.2631 0.2053 -0.0233 0.0209  0.0720  30  VAL   A CG2 
884  N N   A LYS   A 31  ? 0.2511 0.2641 0.1135 -0.0801 0.0184  0.0379  31  LYS   A N   
885  N N   B LYS   A 31  ? 0.2440 0.2622 0.1436 -0.0066 0.0103  0.0316  31  LYS   A N   
886  C CA  A LYS   A 31  ? 0.2544 0.2563 0.1325 -0.0627 -0.0087 0.0331  31  LYS   A CA  
887  C CA  B LYS   A 31  ? 0.2497 0.2608 0.1665 -0.0035 -0.0063 0.0219  31  LYS   A CA  
888  C C   A LYS   A 31  ? 0.2352 0.2316 0.1010 -0.0480 -0.0187 0.0567  31  LYS   A C   
889  C C   B LYS   A 31  ? 0.2295 0.2458 0.1417 0.0047  -0.0013 0.0338  31  LYS   A C   
890  O O   A LYS   A 31  ? 0.2366 0.2384 0.1066 -0.0354 -0.0285 0.0681  31  LYS   A O   
891  O O   B LYS   A 31  ? 0.2388 0.2500 0.1572 0.0127  -0.0058 0.0270  31  LYS   A O   
892  C CB  A LYS   A 31  ? 0.2848 0.2793 0.2228 -0.0547 -0.0246 0.0111  31  LYS   A CB  
893  C CB  B LYS   A 31  ? 0.2798 0.2792 0.2404 -0.0068 -0.0257 0.0008  31  LYS   A CB  
894  C CG  A LYS   A 31  ? 0.3173 0.3004 0.3187 -0.0411 -0.0335 -0.0002 31  LYS   A CG  
895  C CG  B LYS   A 31  ? 0.3122 0.3028 0.3335 -0.0069 -0.0420 -0.0154 31  LYS   A CG  
896  C CD  A LYS   A 31  ? 0.3439 0.3176 0.3918 -0.0296 -0.0436 -0.0080 31  LYS   A CD  
897  C CD  B LYS   A 31  ? 0.3363 0.3219 0.4078 -0.0067 -0.0572 -0.0297 31  LYS   A CD  
898  C CE  A LYS   A 31  ? 0.3607 0.3299 0.4404 -0.0210 -0.0520 -0.0128 31  LYS   A CE  
899  C CE  B LYS   A 31  ? 0.3543 0.3378 0.4615 -0.0079 -0.0669 -0.0401 31  LYS   A CE  
900  N NZ  A LYS   A 31  ? 0.3689 0.3353 0.4656 -0.0151 -0.0586 -0.0151 31  LYS   A NZ  
901  N NZ  B LYS   A 31  ? 0.3665 0.3483 0.4932 -0.0083 -0.0696 -0.0475 31  LYS   A NZ  
928  N N   A PRO   A 32  ? 0.2155 0.2102 0.0999 -0.0475 -0.0127 0.0459  32  PRO   A N   
929  N N   B PRO   A 32  ? 0.2035 0.2292 0.1198 0.0036  0.0101  0.0358  32  PRO   A N   
930  C CA  A PRO   A 32  ? 0.2091 0.1966 0.1213 -0.0490 -0.0133 0.0503  32  PRO   A CA  
931  C CA  B PRO   A 32  ? 0.1955 0.2199 0.1244 0.0028  0.0087  0.0431  32  PRO   A CA  
932  C C   A PRO   A 32  ? 0.2045 0.1913 0.1235 -0.0388 -0.0147 0.0469  32  PRO   A C   
933  C C   B PRO   A 32  ? 0.1933 0.2163 0.1256 0.0056  0.0009  0.0412  32  PRO   A C   
934  O O   A PRO   A 32  ? 0.1998 0.1831 0.1137 -0.0452 -0.0027 0.0291  32  PRO   A O   
935  O O   B PRO   A 32  ? 0.1915 0.2163 0.1409 0.0048  -0.0030 0.0295  32  PRO   A O   
936  C CB  A PRO   A 32  ? 0.2057 0.2030 0.1338 -0.0501 -0.0131 0.0348  32  PRO   A CB  
937  C CB  B PRO   A 32  ? 0.1895 0.2253 0.1369 0.0043  0.0093  0.0254  32  PRO   A CB  
938  C CG  A PRO   A 32  ? 0.2072 0.2075 0.1110 -0.0481 -0.0222 0.0269  32  PRO   A CG  
939  C CG  B PRO   A 32  ? 0.1914 0.2296 0.1215 0.0055  0.0027  0.0173  32  PRO   A CG  
940  C CD  A PRO   A 32  ? 0.2078 0.2035 0.0955 -0.0480 -0.0176 0.0384  32  PRO   A CD  
941  C CD  B PRO   A 32  ? 0.1923 0.2278 0.1159 0.0058  0.0104  0.0253  32  PRO   A CD  
956  N N   A THR   A 33  ? 0.2062 0.1933 0.1261 -0.0242 -0.0190 0.0507  33  THR   A N   
957  N N   B THR   A 33  ? 0.1923 0.2122 0.1250 0.0064  -0.0039 0.0476  33  THR   A N   
958  C CA  A THR   A 33  ? 0.2039 0.2014 0.1441 -0.0135 -0.0340 0.0425  33  THR   A CA  
959  C CA  B THR   A 33  ? 0.1923 0.2076 0.1204 0.0073  -0.0237 0.0509  33  THR   A CA  
960  C C   A THR   A 33  ? 0.1806 0.1929 0.1358 -0.0139 -0.0335 0.0368  33  THR   A C   
961  C C   B THR   A 33  ? 0.1720 0.1871 0.1212 -0.0044 -0.0239 0.0351  33  THR   A C   
962  O O   A THR   A 33  ? 0.1733 0.1894 0.1395 -0.0102 -0.0417 0.0413  33  THR   A O   
963  O O   B THR   A 33  ? 0.1638 0.1766 0.1334 -0.0068 -0.0153 0.0225  33  THR   A O   
964  C CB  A THR   A 33  ? 0.2246 0.2192 0.1733 -0.0022 -0.0358 0.0474  33  THR   A CB  
965  C CB  B THR   A 33  ? 0.2151 0.2260 0.1401 0.0179  -0.0155 0.0702  33  THR   A CB  
966  O OG1 A THR   A 33  ? 0.2409 0.2291 0.2010 0.0070  -0.0332 0.0492  33  THR   A OG1 
967  O OG1 B THR   A 33  ? 0.2268 0.2429 0.1640 0.0302  -0.0218 0.0839  33  THR   A OG1 
968  C CG2 A THR   A 33  ? 0.2293 0.2277 0.1823 0.0023  -0.0377 0.0458  33  THR   A CG2 
969  C CG2 B THR   A 33  ? 0.2207 0.2302 0.1617 0.0212  -0.0092 0.0634  33  THR   A CG2 
984  N N   . VAL   A 34  ? 0.1632 0.1860 0.1174 -0.0192 -0.0213 0.0346  34  VAL   A N   
985  C CA  . VAL   A 34  ? 0.1549 0.1665 0.1134 -0.0158 -0.0164 0.0360  34  VAL   A CA  
986  C C   . VAL   A 34  ? 0.1464 0.1535 0.1131 -0.0236 -0.0107 0.0274  34  VAL   A C   
987  O O   . VAL   A 34  ? 0.1480 0.1564 0.1334 -0.0264 -0.0066 0.0402  34  VAL   A O   
988  C CB  . VAL   A 34  ? 0.1586 0.1648 0.1365 -0.0224 -0.0052 0.0263  34  VAL   A CB  
989  C CG1 . VAL   A 34  ? 0.1667 0.1708 0.1355 -0.0150 0.0034  0.0183  34  VAL   A CG1 
990  C CG2 . VAL   A 34  ? 0.1701 0.1796 0.1635 -0.0143 -0.0090 0.0252  34  VAL   A CG2 
1001 N N   . VAL   A 35  ? 0.1333 0.1460 0.1145 -0.0294 -0.0165 0.0267  35  VAL   A N   
1002 C CA  . VAL   A 35  ? 0.1220 0.1493 0.1128 -0.0197 -0.0036 0.0241  35  VAL   A CA  
1003 C C   . VAL   A 35  ? 0.1204 0.1369 0.1066 -0.0162 -0.0007 0.0240  35  VAL   A C   
1004 O O   . VAL   A 35  ? 0.1167 0.1500 0.1258 -0.0234 0.0090  0.0198  35  VAL   A O   
1005 C CB  . VAL   A 35  ? 0.1344 0.1493 0.1267 -0.0085 0.0041  0.0104  35  VAL   A CB  
1006 C CG1 . VAL   A 35  ? 0.1475 0.1534 0.1347 -0.0026 0.0014  0.0043  35  VAL   A CG1 
1007 C CG2 . VAL   A 35  ? 0.1409 0.1499 0.1433 -0.0092 0.0061  0.0060  35  VAL   A CG2 
1017 N N   . VAL   A 36  ? 0.1115 0.1318 0.1027 -0.0143 -0.0001 0.0274  36  VAL   A N   
1018 C CA  . VAL   A 36  ? 0.1098 0.1221 0.1037 -0.0094 0.0011  0.0169  36  VAL   A CA  
1019 C C   . VAL   A 36  ? 0.1048 0.1258 0.1142 -0.0125 0.0053  0.0200  36  VAL   A C   
1020 O O   . VAL   A 36  ? 0.1101 0.1225 0.1369 -0.0105 0.0143  0.0202  36  VAL   A O   
1021 C CB  . VAL   A 36  ? 0.1140 0.1163 0.1216 -0.0104 0.0049  0.0237  36  VAL   A CB  
1022 C CG1 . VAL   A 36  ? 0.1159 0.1199 0.1347 -0.0139 0.0058  0.0066  36  VAL   A CG1 
1023 C CG2 . VAL   A 36  ? 0.1228 0.1238 0.1320 -0.0074 -0.0028 0.0257  36  VAL   A CG2 
1033 N N   . ASN   A 37  ? 0.1069 0.1162 0.1074 -0.0042 -0.0001 0.0216  37  ASN   A N   
1034 C CA  . ASN   A 37  ? 0.1044 0.1146 0.1093 -0.0061 0.0024  0.0242  37  ASN   A CA  
1035 C C   . ASN   A 37  ? 0.1053 0.1137 0.1091 -0.0032 0.0100  0.0320  37  ASN   A C   
1036 O O   . ASN   A 37  ? 0.1168 0.1228 0.1111 0.0012  0.0051  0.0164  37  ASN   A O   
1037 C CB  . ASN   A 37  ? 0.1087 0.1131 0.1224 0.0024  0.0060  0.0201  37  ASN   A CB  
1038 C CG  . ASN   A 37  ? 0.1097 0.1105 0.1296 -0.0002 0.0025  0.0157  37  ASN   A CG  
1039 O OD1 . ASN   A 37  ? 0.1092 0.1153 0.1537 -0.0043 0.0031  0.0276  37  ASN   A OD1 
1040 N ND2 . ASN   A 37  ? 0.1149 0.1104 0.1422 -0.0062 0.0029  0.0287  37  ASN   A ND2 
1047 N N   A ALA   A 38  ? 0.1081 0.1207 0.1108 -0.0035 0.0068  0.0178  38  ALA   A N   
1048 N N   B ALA   A 38  ? 0.1061 0.1216 0.1161 -0.0016 0.0046  0.0247  38  ALA   A N   
1049 C CA  A ALA   A 38  ? 0.1176 0.1177 0.1071 -0.0068 0.0017  0.0071  38  ALA   A CA  
1050 C CA  B ALA   A 38  ? 0.1148 0.1259 0.1235 -0.0061 -0.0012 0.0273  38  ALA   A CA  
1051 C C   A ALA   A 38  ? 0.1111 0.1153 0.1164 -0.0023 -0.0028 0.0005  38  ALA   A C   
1052 C C   B ALA   A 38  ? 0.1134 0.1269 0.1261 0.0030  -0.0041 0.0185  38  ALA   A C   
1053 O O   A ALA   A 38  ? 0.1090 0.1026 0.1165 -0.0124 -0.0149 -0.0054 38  ALA   A O   
1054 O O   B ALA   A 38  ? 0.1130 0.1234 0.1304 -0.0003 -0.0057 0.0245  38  ALA   A O   
1055 C CB  A ALA   A 38  ? 0.1204 0.1157 0.0913 -0.0170 -0.0077 0.0101  38  ALA   A CB  
1056 C CB  B ALA   A 38  ? 0.1159 0.1273 0.1378 -0.0118 -0.0116 0.0191  38  ALA   A CB  
1067 N N   A ALA   A 39  ? 0.1112 0.1145 0.1296 -0.0006 0.0057  0.0120  39  ALA   A N   
1068 N N   B ALA   A 39  ? 0.1200 0.1308 0.1341 0.0012  0.0044  0.0309  39  ALA   A N   
1069 C CA  A ALA   A 39  ? 0.1062 0.1078 0.1199 0.0026  0.0022  0.0129  39  ALA   A CA  
1070 C CA  B ALA   A 39  ? 0.1200 0.1305 0.1242 -0.0020 -0.0053 0.0209  39  ALA   A CA  
1071 C C   A ALA   A 39  ? 0.1098 0.1140 0.1247 -0.0012 0.0030  0.0081  39  ALA   A C   
1072 C C   B ALA   A 39  ? 0.1113 0.1208 0.1261 -0.0078 -0.0050 0.0117  39  ALA   A C   
1073 O O   A ALA   A 39  ? 0.1242 0.1159 0.1216 -0.0070 0.0109  0.0135  39  ALA   A O   
1074 O O   B ALA   A 39  ? 0.1283 0.1215 0.1409 -0.0093 -0.0041 0.0104  39  ALA   A O   
1075 C CB  A ALA   A 39  ? 0.1004 0.1036 0.1204 0.0011  -0.0051 0.0106  39  ALA   A CB  
1076 C CB  B ALA   A 39  ? 0.1295 0.1433 0.1322 -0.0048 -0.0065 0.0189  39  ALA   A CB  
1087 N N   A ASN   A 40  ? 0.1096 0.1225 0.1298 -0.0003 0.0068  0.0089  40  ASN   A N   
1088 N N   B ASN   A 40  ? 0.1105 0.1156 0.1112 -0.0051 0.0096  0.0139  40  ASN   A N   
1089 C CA  A ASN   A 40  ? 0.1142 0.1219 0.1231 -0.0023 -0.0006 0.0080  40  ASN   A CA  
1090 C CA  B ASN   A 40  ? 0.1128 0.1104 0.1192 -0.0024 0.0012  0.0155  40  ASN   A CA  
1091 C C   A ASN   A 40  ? 0.1162 0.1113 0.1070 -0.0023 -0.0014 0.0185  40  ASN   A C   
1092 C C   B ASN   A 40  ? 0.1105 0.1026 0.1071 -0.0041 0.0089  0.0207  40  ASN   A C   
1093 O O   A ASN   A 40  ? 0.1182 0.1173 0.1151 -0.0044 -0.0042 0.0185  40  ASN   A O   
1094 O O   B ASN   A 40  ? 0.1046 0.1052 0.1138 -0.0070 0.0047  0.0206  40  ASN   A O   
1095 C CB  A ASN   A 40  ? 0.1245 0.1331 0.1353 -0.0000 -0.0090 0.0051  40  ASN   A CB  
1096 C CB  B ASN   A 40  ? 0.1213 0.1178 0.1215 0.0025  -0.0053 0.0172  40  ASN   A CB  
1097 C CG  A ASN   A 40  ? 0.1450 0.1377 0.1560 -0.0025 -0.0102 0.0066  40  ASN   A CG  
1098 C CG  B ASN   A 40  ? 0.1290 0.1195 0.1235 0.0040  -0.0071 0.0147  40  ASN   A CG  
1099 O OD1 A ASN   A 40  ? 0.1520 0.1321 0.1341 -0.0065 -0.0242 0.0148  40  ASN   A OD1 
1100 O OD1 B ASN   A 40  ? 0.1340 0.1209 0.1306 -0.0008 -0.0013 0.0091  40  ASN   A OD1 
1101 N ND2 A ASN   A 40  ? 0.1549 0.1525 0.1862 0.0056  0.0001  -0.0018 40  ASN   A ND2 
1102 N ND2 B ASN   A 40  ? 0.1288 0.1298 0.1529 0.0056  0.0045  -0.0025 40  ASN   A ND2 
1115 N N   A VAL   A 41  ? 0.1191 0.1158 0.1043 -0.0045 0.0049  0.0251  41  VAL   A N   
1116 N N   B VAL   A 41  ? 0.1178 0.1156 0.1143 -0.0025 0.0042  0.0162  41  VAL   A N   
1117 C CA  A VAL   A 41  ? 0.1142 0.1137 0.1069 -0.0026 0.0096  0.0205  41  VAL   A CA  
1118 C CA  B VAL   A 41  ? 0.1226 0.1226 0.1248 0.0018  0.0122  0.0202  41  VAL   A CA  
1119 C C   A VAL   A 41  ? 0.1112 0.1095 0.1146 0.0047  0.0048  0.0146  41  VAL   A C   
1120 C C   B VAL   A 41  ? 0.1172 0.1203 0.1196 0.0019  0.0118  0.0186  41  VAL   A C   
1121 O O   A VAL   A 41  ? 0.1226 0.1077 0.1263 0.0085  -0.0032 0.0120  41  VAL   A O   
1122 O O   B VAL   A 41  ? 0.1286 0.1166 0.1272 0.0030  0.0012  0.0214  41  VAL   A O   
1123 C CB  A VAL   A 41  ? 0.1199 0.1196 0.0998 -0.0039 0.0158  0.0085  41  VAL   A CB  
1124 C CB  B VAL   A 41  ? 0.1357 0.1372 0.1420 0.0055  0.0178  0.0216  41  VAL   A CB  
1125 C CG1 A VAL   A 41  ? 0.1296 0.1242 0.1175 -0.0009 0.0163  -0.0006 41  VAL   A CG1 
1126 C CG1 B VAL   A 41  ? 0.1610 0.1440 0.1611 0.0040  0.0182  0.0126  41  VAL   A CG1 
1127 C CG2 A VAL   A 41  ? 0.1120 0.1219 0.0854 -0.0039 0.0140  0.0122  41  VAL   A CG2 
1128 C CG2 B VAL   A 41  ? 0.1410 0.1439 0.1479 0.0008  0.0093  0.0190  41  VAL   A CG2 
1147 N N   A TYR   A 42  ? 0.0985 0.1067 0.1483 -0.0001 0.0128  0.0177  42  TYR   A N   
1148 N N   B TYR   A 42  ? 0.1080 0.1185 0.1382 -0.0012 0.0287  0.0254  42  TYR   A N   
1149 C CA  A TYR   A 42  ? 0.1073 0.1099 0.1454 -0.0053 0.0108  0.0190  42  TYR   A CA  
1150 C CA  B TYR   A 42  ? 0.1053 0.1200 0.1402 -0.0026 0.0260  0.0274  42  TYR   A CA  
1151 C C   A TYR   A 42  ? 0.1023 0.1056 0.1404 -0.0053 0.0180  0.0178  42  TYR   A C   
1152 C C   B TYR   A 42  ? 0.1130 0.1220 0.1428 -0.0024 0.0267  0.0308  42  TYR   A C   
1153 O O   A TYR   A 42  ? 0.1042 0.1037 0.1558 -0.0110 0.0127  -0.0007 42  TYR   A O   
1154 O O   B TYR   A 42  ? 0.1118 0.1257 0.1568 -0.0103 0.0232  0.0238  42  TYR   A O   
1155 C CB  A TYR   A 42  ? 0.1196 0.1240 0.1393 -0.0063 0.0304  0.0259  42  TYR   A CB  
1156 C CB  B TYR   A 42  ? 0.1114 0.1224 0.1427 0.0016  0.0264  0.0427  42  TYR   A CB  
1157 C CG  A TYR   A 42  ? 0.1257 0.1329 0.1321 -0.0043 0.0250  0.0249  42  TYR   A CG  
1158 C CG  B TYR   A 42  ? 0.1216 0.1311 0.1440 0.0121  0.0120  0.0426  42  TYR   A CG  
1159 C CD1 A TYR   A 42  ? 0.1295 0.1387 0.1354 -0.0072 0.0167  0.0226  42  TYR   A CD1 
1160 C CD1 B TYR   A 42  ? 0.1216 0.1351 0.1422 0.0042  0.0249  0.0469  42  TYR   A CD1 
1161 C CD2 A TYR   A 42  ? 0.1245 0.1476 0.1436 -0.0003 0.0204  0.0247  42  TYR   A CD2 
1162 C CD2 B TYR   A 42  ? 0.1365 0.1491 0.1663 0.0199  0.0116  0.0361  42  TYR   A CD2 
1163 C CE1 A TYR   A 42  ? 0.1346 0.1464 0.1411 -0.0050 0.0112  0.0156  42  TYR   A CE1 
1164 C CE1 B TYR   A 42  ? 0.1277 0.1465 0.1413 0.0098  0.0329  0.0492  42  TYR   A CE1 
1165 C CE2 A TYR   A 42  ? 0.1247 0.1531 0.1486 -0.0056 0.0096  0.0209  42  TYR   A CE2 
1166 C CE2 B TYR   A 42  ? 0.1460 0.1617 0.1751 0.0170  0.0179  0.0339  42  TYR   A CE2 
1167 C CZ  A TYR   A 42  ? 0.1348 0.1538 0.1382 -0.0042 0.0094  0.0196  42  TYR   A CZ  
1168 C CZ  B TYR   A 42  ? 0.1459 0.1609 0.1574 0.0113  0.0267  0.0367  42  TYR   A CZ  
1169 O OH  A TYR   A 42  ? 0.1431 0.1635 0.1559 0.0032  0.0041  0.0138  42  TYR   A OH  
1170 O OH  B TYR   A 42  ? 0.1544 0.1768 0.1785 0.0057  0.0209  0.0227  42  TYR   A OH  
1189 N N   A LEU   A 43  ? 0.1080 0.1080 0.1229 -0.0118 0.0138  0.0052  43  LEU   A N   
1190 N N   B LEU   A 43  ? 0.1158 0.1195 0.1423 0.0001  0.0120  0.0229  43  LEU   A N   
1191 C CA  A LEU   A 43  ? 0.1025 0.1117 0.1211 -0.0110 0.0110  0.0068  43  LEU   A CA  
1192 C CA  B LEU   A 43  ? 0.1173 0.1176 0.1381 0.0006  0.0087  0.0204  43  LEU   A CA  
1193 C C   A LEU   A 43  ? 0.1057 0.1163 0.1325 -0.0045 0.0084  0.0046  43  LEU   A C   
1194 C C   B LEU   A 43  ? 0.1180 0.1217 0.1392 -0.0008 0.0033  0.0094  43  LEU   A C   
1195 O O   A LEU   A 43  ? 0.1171 0.1138 0.1563 0.0019  0.0076  0.0099  43  LEU   A O   
1196 O O   B LEU   A 43  ? 0.1299 0.1247 0.1482 -0.0000 -0.0086 0.0101  43  LEU   A O   
1197 C CB  A LEU   A 43  ? 0.1134 0.1184 0.1385 -0.0083 0.0029  0.0029  43  LEU   A CB  
1198 C CB  B LEU   A 43  ? 0.1131 0.1086 0.1428 -0.0036 0.0119  0.0225  43  LEU   A CB  
1199 C CG  A LEU   A 43  ? 0.1173 0.1255 0.1467 -0.0082 -0.0013 0.0029  43  LEU   A CG  
1200 C CG  B LEU   A 43  ? 0.1118 0.1084 0.1542 0.0013  0.0149  0.0214  43  LEU   A CG  
1201 C CD1 A LEU   A 43  ? 0.1151 0.1347 0.1517 -0.0041 0.0006  0.0091  43  LEU   A CD1 
1202 C CD1 B LEU   A 43  ? 0.1175 0.1134 0.1714 0.0075  0.0106  0.0288  43  LEU   A CD1 
1203 C CD2 A LEU   A 43  ? 0.1291 0.1316 0.1375 -0.0077 -0.0095 0.0052  43  LEU   A CD2 
1204 C CD2 B LEU   A 43  ? 0.1257 0.1059 0.1429 -0.0029 0.0098  0.0319  43  LEU   A CD2 
1227 N N   A LYS   A 44  ? 0.1201 0.1117 0.1336 -0.0043 0.0127  0.0079  44  LYS   A N   
1228 N N   B LYS   A 44  ? 0.1218 0.1155 0.1297 0.0025  0.0033  0.0124  44  LYS   A N   
1229 C CA  A LYS   A 44  ? 0.1321 0.1165 0.1394 -0.0089 0.0197  0.0232  44  LYS   A CA  
1230 C CA  B LYS   A 44  ? 0.1312 0.1195 0.1249 0.0014  0.0088  0.0231  44  LYS   A CA  
1231 C C   A LYS   A 44  ? 0.1206 0.1140 0.1392 -0.0026 0.0031  0.0146  44  LYS   A C   
1232 C C   B LYS   A 44  ? 0.1193 0.1152 0.1199 0.0077  0.0039  0.0117  44  LYS   A C   
1233 O O   A LYS   A 44  ? 0.1247 0.1245 0.1651 -0.0069 -0.0009 0.0044  44  LYS   A O   
1234 O O   B LYS   A 44  ? 0.1242 0.1286 0.1261 0.0086  0.0090  -0.0089 44  LYS   A O   
1235 C CB  A LYS   A 44  ? 0.1595 0.1279 0.1736 -0.0073 0.0269  0.0290  44  LYS   A CB  
1236 C CB  B LYS   A 44  ? 0.1632 0.1368 0.1798 0.0062  0.0176  0.0242  44  LYS   A CB  
1237 C CG  A LYS   A 44  ? 0.1888 0.1525 0.2205 -0.0118 0.0427  0.0406  44  LYS   A CG  
1238 C CG  B LYS   A 44  ? 0.1904 0.1701 0.2496 0.0025  0.0302  0.0308  44  LYS   A CG  
1239 C CD  A LYS   A 44  ? 0.2222 0.1969 0.3113 -0.0118 0.0350  0.0237  44  LYS   A CD  
1240 C CD  B LYS   A 44  ? 0.2179 0.2151 0.3369 -0.0040 0.0213  0.0240  44  LYS   A CD  
1241 C CE  A LYS   A 44  ? 0.2389 0.2217 0.3668 -0.0082 0.0351  0.0128  44  LYS   A CE  
1242 C CE  B LYS   A 44  ? 0.2312 0.2410 0.3899 -0.0099 0.0129  0.0248  44  LYS   A CE  
1243 N NZ  A LYS   A 44  ? 0.2446 0.2376 0.3911 -0.0089 0.0362  0.0090  44  LYS   A NZ  
1244 N NZ  B LYS   A 44  ? 0.2412 0.2605 0.4214 -0.0224 0.0094  0.0256  44  LYS   A NZ  
1271 N N   . HIS   A 45  ? 0.1116 0.1090 0.1357 -0.0043 0.0029  0.0157  45  HIS   A N   
1272 C CA  . HIS   A 45  ? 0.1156 0.1078 0.1322 -0.0001 0.0025  0.0093  45  HIS   A CA  
1273 C C   . HIS   A 45  ? 0.1181 0.1216 0.1387 0.0043  0.0050  0.0127  45  HIS   A C   
1274 O O   . HIS   A 45  ? 0.1394 0.1412 0.1644 0.0185  -0.0028 -0.0062 45  HIS   A O   
1275 C CB  . HIS   A 45  ? 0.1162 0.1128 0.1245 -0.0038 0.0062  0.0080  45  HIS   A CB  
1276 C CG  . HIS   A 45  ? 0.1115 0.1130 0.1168 -0.0062 0.0031  0.0106  45  HIS   A CG  
1277 N ND1 . HIS   A 45  ? 0.1065 0.1210 0.1405 -0.0062 -0.0043 0.0155  45  HIS   A ND1 
1278 C CD2 . HIS   A 45  ? 0.1101 0.1171 0.1255 -0.0116 -0.0047 0.0173  45  HIS   A CD2 
1279 C CE1 . HIS   A 45  ? 0.1078 0.1228 0.1289 -0.0049 -0.0035 0.0259  45  HIS   A CE1 
1280 N NE2 . HIS   A 45  ? 0.1066 0.1224 0.1316 -0.0023 0.0000  0.0226  45  HIS   A NE2 
1289 N N   . GLY   A 46  ? 0.1341 0.1253 0.1530 0.0079  -0.0175 0.0214  46  GLY   A N   
1290 C CA  . GLY   A 46  ? 0.1414 0.1365 0.1715 0.0144  -0.0150 0.0275  46  GLY   A CA  
1291 C C   . GLY   A 46  ? 0.1406 0.1318 0.1639 0.0206  -0.0214 0.0296  46  GLY   A C   
1292 O O   . GLY   A 46  ? 0.1410 0.1408 0.2129 0.0167  -0.0347 0.0100  46  GLY   A O   
1296 N N   A GLY   A 47  ? 0.1436 0.1347 0.1529 0.0144  -0.0116 0.0202  47  GLY   A N   
1297 N N   B GLY   A 47  ? 0.1393 0.1370 0.1535 0.0166  -0.0100 0.0199  47  GLY   A N   
1298 C CA  A GLY   A 47  ? 0.1444 0.1341 0.1485 0.0163  -0.0237 0.0125  47  GLY   A CA  
1299 C CA  B GLY   A 47  ? 0.1369 0.1386 0.1464 0.0205  -0.0231 0.0171  47  GLY   A CA  
1300 C C   A GLY   A 47  ? 0.1412 0.1248 0.1421 0.0131  -0.0237 0.0034  47  GLY   A C   
1301 C C   B GLY   A 47  ? 0.1306 0.1269 0.1206 0.0199  -0.0192 0.0038  47  GLY   A C   
1302 O O   A GLY   A 47  ? 0.1388 0.1200 0.1523 0.0142  -0.0217 0.0065  47  GLY   A O   
1303 O O   B GLY   A 47  ? 0.1275 0.1235 0.1120 0.0230  -0.0140 0.0164  47  GLY   A O   
1310 N N   A GLY   A 48  ? 0.1328 0.1262 0.1267 0.0156  -0.0232 -0.0090 48  GLY   A N   
1311 N N   B GLY   A 48  ? 0.1237 0.1278 0.1322 0.0177  -0.0196 -0.0077 48  GLY   A N   
1312 C CA  A GLY   A 48  ? 0.1233 0.1210 0.1371 0.0103  -0.0158 -0.0061 48  GLY   A CA  
1313 C CA  B GLY   A 48  ? 0.1155 0.1168 0.1336 0.0205  -0.0150 -0.0093 48  GLY   A CA  
1314 C C   A GLY   A 48  ? 0.1170 0.1205 0.1270 -0.0054 -0.0104 0.0022  48  GLY   A C   
1315 C C   B GLY   A 48  ? 0.1144 0.1171 0.1333 0.0051  -0.0004 -0.0029 48  GLY   A C   
1316 O O   A GLY   A 48  ? 0.1267 0.1266 0.1189 -0.0070 -0.0106 0.0075  48  GLY   A O   
1317 O O   B GLY   A 48  ? 0.1287 0.1202 0.1322 0.0118  0.0079  -0.0066 48  GLY   A O   
1324 N N   A VAL   A 49  ? 0.1202 0.1200 0.1516 -0.0062 -0.0097 0.0101  49  VAL   A N   
1325 N N   B VAL   A 49  ? 0.1066 0.1139 0.1422 -0.0008 -0.0104 -0.0092 49  VAL   A N   
1326 C CA  A VAL   A 49  ? 0.1251 0.1188 0.1551 -0.0057 0.0053  0.0156  49  VAL   A CA  
1327 C CA  B VAL   A 49  ? 0.1013 0.1150 0.1402 -0.0058 -0.0015 0.0110  49  VAL   A CA  
1328 C C   A VAL   A 49  ? 0.1216 0.1093 0.1411 -0.0047 0.0009  0.0280  49  VAL   A C   
1329 C C   B VAL   A 49  ? 0.1104 0.1113 0.1063 -0.0033 0.0030  0.0020  49  VAL   A C   
1330 O O   A VAL   A 49  ? 0.1256 0.1163 0.1443 -0.0081 -0.0011 0.0233  49  VAL   A O   
1331 O O   B VAL   A 49  ? 0.1128 0.1180 0.0872 -0.0072 0.0139  -0.0011 49  VAL   A O   
1332 C CB  A VAL   A 49  ? 0.1301 0.1244 0.1663 -0.0051 0.0129  0.0045  49  VAL   A CB  
1333 C CB  B VAL   A 49  ? 0.0927 0.1084 0.1569 -0.0051 -0.0041 0.0177  49  VAL   A CB  
1334 C CG1 A VAL   A 49  ? 0.1218 0.1187 0.1717 0.0049  0.0160  -0.0044 49  VAL   A CG1 
1335 C CG1 B VAL   A 49  ? 0.0915 0.1076 0.1448 0.0015  -0.0037 0.0155  49  VAL   A CG1 
1336 C CG2 A VAL   A 49  ? 0.1400 0.1336 0.1911 -0.0166 0.0156  0.0012  49  VAL   A CG2 
1337 C CG2 B VAL   A 49  ? 0.0950 0.1092 0.1833 0.0015  0.0014  0.0186  49  VAL   A CG2 
1356 N N   A ALA   A 50  ? 0.1096 0.1053 0.1269 -0.0053 -0.0140 0.0239  50  ALA   A N   
1357 N N   B ALA   A 50  ? 0.1117 0.1083 0.0943 -0.0013 0.0022  0.0009  50  ALA   A N   
1358 C CA  A ALA   A 50  ? 0.1053 0.1036 0.1244 -0.0135 -0.0123 0.0160  50  ALA   A CA  
1359 C CA  B ALA   A 50  ? 0.1103 0.1071 0.0886 -0.0058 0.0004  -0.0029 50  ALA   A CA  
1360 C C   A ALA   A 50  ? 0.0989 0.1026 0.1350 -0.0090 -0.0025 0.0149  50  ALA   A C   
1361 C C   B ALA   A 50  ? 0.1090 0.1119 0.0952 -0.0080 0.0023  -0.0015 50  ALA   A C   
1362 O O   A ALA   A 50  ? 0.1016 0.1021 0.1327 -0.0039 -0.0037 0.0122  50  ALA   A O   
1363 O O   B ALA   A 50  ? 0.1091 0.1140 0.0911 -0.0025 0.0025  -0.0106 50  ALA   A O   
1364 C CB  A ALA   A 50  ? 0.1056 0.1151 0.1232 -0.0186 -0.0207 0.0079  50  ALA   A CB  
1365 C CB  B ALA   A 50  ? 0.1172 0.0989 0.0802 0.0005  0.0012  -0.0119 50  ALA   A CB  
1376 N N   A GLY   A 51  ? 0.1032 0.1012 0.1412 0.0011  -0.0126 0.0131  51  GLY   A N   
1377 N N   B GLY   A 51  ? 0.1181 0.1064 0.1193 0.0008  -0.0126 -0.0032 51  GLY   A N   
1378 C CA  A GLY   A 51  ? 0.1143 0.1001 0.1523 -0.0003 -0.0109 0.0046  51  GLY   A CA  
1379 C CA  B GLY   A 51  ? 0.1303 0.1011 0.1228 -0.0029 -0.0154 -0.0042 51  GLY   A CA  
1380 C C   A GLY   A 51  ? 0.1063 0.1065 0.1492 0.0058  0.0010  -0.0058 51  GLY   A C   
1381 C C   B GLY   A 51  ? 0.1193 0.1034 0.1174 -0.0006 -0.0095 -0.0081 51  GLY   A C   
1382 O O   A GLY   A 51  ? 0.1134 0.1195 0.1522 0.0053  -0.0106 -0.0018 51  GLY   A O   
1383 O O   B GLY   A 51  ? 0.1218 0.1110 0.1229 -0.0058 -0.0083 -0.0092 51  GLY   A O   
1390 N N   A ALA   A 52  ? 0.1032 0.1141 0.1560 0.0015  0.0114  -0.0044 52  ALA   A N   
1391 N N   B ALA   A 52  ? 0.1106 0.1097 0.1131 0.0034  -0.0090 -0.0145 52  ALA   A N   
1392 C CA  A ALA   A 52  ? 0.1053 0.1232 0.1591 -0.0027 0.0086  -0.0078 52  ALA   A CA  
1393 C CA  B ALA   A 52  ? 0.1157 0.1164 0.1251 0.0019  -0.0024 -0.0120 52  ALA   A CA  
1394 C C   A ALA   A 52  ? 0.1052 0.1317 0.1446 -0.0043 0.0137  -0.0017 52  ALA   A C   
1395 C C   B ALA   A 52  ? 0.1176 0.1162 0.1093 -0.0035 0.0018  -0.0151 52  ALA   A C   
1396 O O   A ALA   A 52  ? 0.1111 0.1374 0.1521 -0.0025 0.0121  -0.0046 52  ALA   A O   
1397 O O   B ALA   A 52  ? 0.1261 0.1328 0.1164 -0.0054 0.0020  -0.0164 52  ALA   A O   
1398 C CB  A ALA   A 52  ? 0.1094 0.1313 0.1711 -0.0100 0.0048  -0.0150 52  ALA   A CB  
1399 C CB  B ALA   A 52  ? 0.1215 0.1290 0.1437 0.0049  0.0036  -0.0019 52  ALA   A CB  
1410 N N   A LEU   A 53  ? 0.0997 0.1318 0.1355 -0.0016 0.0091  0.0069  53  LEU   A N   
1411 N N   B LEU   A 53  ? 0.1083 0.1083 0.1114 -0.0043 -0.0017 -0.0093 53  LEU   A N   
1412 C CA  A LEU   A 53  ? 0.1112 0.1334 0.1275 -0.0028 0.0077  0.0110  53  LEU   A CA  
1413 C CA  B LEU   A 53  ? 0.1173 0.1175 0.1013 -0.0008 0.0049  -0.0034 53  LEU   A CA  
1414 C C   A LEU   A 53  ? 0.1138 0.1306 0.1107 0.0019  0.0089  0.0039  53  LEU   A C   
1415 C C   B LEU   A 53  ? 0.1131 0.1202 0.0835 0.0101  0.0033  0.0051  53  LEU   A C   
1416 O O   A LEU   A 53  ? 0.1225 0.1268 0.1224 -0.0057 0.0072  0.0069  53  LEU   A O   
1417 O O   B LEU   A 53  ? 0.1179 0.1179 0.0953 0.0103  -0.0053 0.0094  53  LEU   A O   
1418 C CB  A LEU   A 53  ? 0.1200 0.1353 0.1370 -0.0058 0.0031  0.0237  53  LEU   A CB  
1419 C CB  B LEU   A 53  ? 0.1285 0.1228 0.1171 -0.0033 -0.0020 0.0059  53  LEU   A CB  
1420 C CG  A LEU   A 53  ? 0.1295 0.1405 0.1451 -0.0171 -0.0014 0.0249  53  LEU   A CG  
1421 C CG  B LEU   A 53  ? 0.1373 0.1258 0.1161 -0.0122 -0.0049 0.0072  53  LEU   A CG  
1422 C CD1 A LEU   A 53  ? 0.1300 0.1402 0.1452 -0.0180 -0.0000 0.0245  53  LEU   A CD1 
1423 C CD1 B LEU   A 53  ? 0.1476 0.1293 0.1219 -0.0154 -0.0064 -0.0069 53  LEU   A CD1 
1424 C CD2 A LEU   A 53  ? 0.1367 0.1533 0.1482 -0.0239 -0.0112 0.0224  53  LEU   A CD2 
1425 C CD2 B LEU   A 53  ? 0.1371 0.1318 0.1172 -0.0155 -0.0003 0.0051  53  LEU   A CD2 
1448 N N   A ASN   A 54  ? 0.1099 0.1255 0.1185 -0.0068 -0.0038 0.0044  54  ASN   A N   
1449 N N   B ASN   A 54  ? 0.1090 0.1243 0.0990 0.0001  0.0024  0.0022  54  ASN   A N   
1450 C CA  A ASN   A 54  ? 0.1092 0.1191 0.1340 -0.0068 -0.0067 0.0047  54  ASN   A CA  
1451 C CA  B ASN   A 54  ? 0.1020 0.1238 0.1150 0.0010  -0.0003 0.0006  54  ASN   A CA  
1452 C C   A ASN   A 54  ? 0.1163 0.1208 0.1368 -0.0125 -0.0038 0.0010  54  ASN   A C   
1453 C C   B ASN   A 54  ? 0.1130 0.1232 0.1275 -0.0102 0.0004  -0.0014 54  ASN   A C   
1454 O O   A ASN   A 54  ? 0.1171 0.1285 0.1428 -0.0093 -0.0070 -0.0040 54  ASN   A O   
1455 O O   B ASN   A 54  ? 0.1133 0.1296 0.1309 -0.0084 -0.0006 -0.0059 54  ASN   A O   
1456 C CB  A ASN   A 54  ? 0.1111 0.1110 0.1417 -0.0157 -0.0148 0.0041  54  ASN   A CB  
1457 C CB  B ASN   A 54  ? 0.1019 0.1197 0.1065 0.0027  -0.0039 -0.0024 54  ASN   A CB  
1458 C CG  A ASN   A 54  ? 0.1146 0.1107 0.1558 -0.0143 -0.0134 0.0033  54  ASN   A CG  
1459 C CG  B ASN   A 54  ? 0.1005 0.1191 0.1091 0.0083  0.0021  -0.0094 54  ASN   A CG  
1460 O OD1 A ASN   A 54  ? 0.1157 0.1040 0.1736 -0.0070 -0.0159 0.0202  54  ASN   A OD1 
1461 O OD1 B ASN   A 54  ? 0.0950 0.1197 0.1038 0.0035  -0.0019 -0.0237 54  ASN   A OD1 
1462 N ND2 A ASN   A 54  ? 0.1139 0.1174 0.1640 -0.0125 -0.0202 0.0072  54  ASN   A ND2 
1463 N ND2 B ASN   A 54  ? 0.1077 0.1180 0.1250 0.0093  0.0023  0.0055  54  ASN   A ND2 
1476 N N   . LYS   A 55  ? 0.1187 0.1202 0.1322 -0.0037 -0.0042 0.0007  55  LYS   A N   
1477 C CA  . LYS   A 55  ? 0.1276 0.1317 0.1420 0.0084  -0.0039 -0.0068 55  LYS   A CA  
1478 C C   . LYS   A 55  ? 0.1156 0.1395 0.1420 -0.0008 0.0008  -0.0150 55  LYS   A C   
1479 O O   . LYS   A 55  ? 0.1308 0.1514 0.1461 0.0025  -0.0059 -0.0231 55  LYS   A O   
1480 C CB  . LYS   A 55  ? 0.1381 0.1524 0.1553 0.0197  -0.0051 -0.0133 55  LYS   A CB  
1481 C CG  . LYS   A 55  ? 0.1530 0.1861 0.1760 0.0319  -0.0204 -0.0272 55  LYS   A CG  
1482 C CD  . LYS   A 55  ? 0.1662 0.2222 0.1874 0.0513  -0.0252 -0.0282 55  LYS   A CD  
1483 C CE  . LYS   A 55  ? 0.1875 0.2545 0.2105 0.0653  -0.0312 -0.0351 55  LYS   A CE  
1484 N NZ  . LYS   A 55  ? 0.2022 0.2774 0.2172 0.0699  -0.0366 -0.0287 55  LYS   A NZ  
1499 N N   . ALA   A 56  ? 0.1230 0.1486 0.1398 -0.0074 0.0017  -0.0149 56  ALA   A N   
1500 C CA  . ALA   A 56  ? 0.1284 0.1636 0.1297 -0.0096 0.0131  -0.0139 56  ALA   A CA  
1501 C C   . ALA   A 56  ? 0.1380 0.1753 0.1155 -0.0075 0.0120  -0.0201 56  ALA   A C   
1502 O O   . ALA   A 56  ? 0.1462 0.2069 0.1298 0.0081  0.0097  -0.0094 56  ALA   A O   
1503 C CB  . ALA   A 56  ? 0.1426 0.1835 0.1402 -0.0160 0.0068  0.0009  56  ALA   A CB  
1509 N N   . THR   A 57  ? 0.1239 0.1560 0.1198 -0.0060 0.0088  -0.0113 57  THR   A N   
1510 C CA  . THR   A 57  ? 0.1321 0.1598 0.1186 -0.0082 0.0001  -0.0061 57  THR   A CA  
1511 C C   . THR   A 57  ? 0.1314 0.1593 0.1281 -0.0071 0.0017  -0.0143 57  THR   A C   
1512 O O   . THR   A 57  ? 0.1308 0.1690 0.1430 -0.0111 -0.0135 -0.0236 57  THR   A O   
1513 C CB  . THR   A 57  ? 0.1291 0.1573 0.1205 -0.0107 -0.0019 -0.0023 57  THR   A CB  
1514 O OG1 . THR   A 57  ? 0.1191 0.1442 0.1222 -0.0054 0.0025  -0.0068 57  THR   A OG1 
1515 C CG2 . THR   A 57  ? 0.1328 0.1515 0.1141 -0.0077 -0.0009 0.0075  57  THR   A CG2 
1523 N N   . ASN   A 58  ? 0.1296 0.1548 0.1499 -0.0103 0.0039  -0.0214 58  ASN   A N   
1524 C CA  . ASN   A 58  ? 0.1523 0.1518 0.1695 -0.0129 0.0157  -0.0332 58  ASN   A CA  
1525 C C   . ASN   A 58  ? 0.1285 0.1375 0.1498 -0.0012 0.0000  -0.0206 58  ASN   A C   
1526 O O   . ASN   A 58  ? 0.1350 0.1488 0.1727 -0.0141 -0.0044 -0.0251 58  ASN   A O   
1527 C CB  . ASN   A 58  ? 0.2086 0.1714 0.2014 -0.0267 0.0398  -0.0561 58  ASN   A CB  
1528 C CG  . ASN   A 58  ? 0.2682 0.1985 0.2821 -0.0296 0.0439  -0.0524 58  ASN   A CG  
1529 O OD1 . ASN   A 58  ? 0.2936 0.1926 0.3309 0.0089  0.0839  -0.0352 58  ASN   A OD1 
1530 N ND2 . ASN   A 58  ? 0.2902 0.2165 0.3085 -0.0410 0.0295  -0.0609 58  ASN   A ND2 
1537 N N   . ASN   A 59  ? 0.1184 0.1329 0.1446 -0.0074 -0.0124 -0.0154 59  ASN   A N   
1538 C CA  . ASN   A 59  ? 0.1201 0.1164 0.1387 -0.0052 -0.0067 -0.0104 59  ASN   A CA  
1539 C C   . ASN   A 59  ? 0.1226 0.1232 0.1280 -0.0071 -0.0070 -0.0056 59  ASN   A C   
1540 O O   . ASN   A 59  ? 0.1221 0.1280 0.1358 -0.0075 0.0029  0.0028  59  ASN   A O   
1541 C CB  . ASN   A 59  ? 0.1289 0.1206 0.1460 0.0019  -0.0166 -0.0175 59  ASN   A CB  
1542 C CG  . ASN   A 59  ? 0.1293 0.1229 0.1493 -0.0060 -0.0270 0.0017  59  ASN   A CG  
1543 O OD1 . ASN   A 59  ? 0.1470 0.1327 0.1449 -0.0137 -0.0240 0.0033  59  ASN   A OD1 
1544 N ND2 . ASN   A 59  ? 0.1409 0.1288 0.1569 -0.0188 -0.0179 0.0040  59  ASN   A ND2 
1551 N N   . ALA   A 60  ? 0.1154 0.1308 0.1357 -0.0008 -0.0081 -0.0029 60  ALA   A N   
1552 C CA  . ALA   A 60  ? 0.1145 0.1306 0.1434 -0.0021 -0.0121 0.0012  60  ALA   A CA  
1553 C C   . ALA   A 60  ? 0.1152 0.1267 0.1464 -0.0038 -0.0062 0.0020  60  ALA   A C   
1554 O O   . ALA   A 60  ? 0.1148 0.1234 0.1635 -0.0041 -0.0114 -0.0049 60  ALA   A O   
1555 C CB  . ALA   A 60  ? 0.1256 0.1424 0.1539 -0.0055 -0.0184 -0.0108 60  ALA   A CB  
1561 N N   . MET   A 61  ? 0.1109 0.1176 0.1319 -0.0071 0.0002  -0.0048 61  MET   A N   
1562 C CA  . MET   A 61  ? 0.1053 0.1166 0.1337 -0.0085 -0.0006 0.0019  61  MET   A CA  
1563 C C   . MET   A 61  ? 0.1066 0.1129 0.1392 -0.0071 -0.0045 -0.0036 61  MET   A C   
1564 O O   . MET   A 61  ? 0.1115 0.1192 0.1464 -0.0026 0.0046  0.0079  61  MET   A O   
1565 C CB  . MET   A 61  ? 0.1180 0.1195 0.1301 -0.0058 0.0019  0.0033  61  MET   A CB  
1566 C CG  . MET   A 61  ? 0.1128 0.1246 0.1470 -0.0008 -0.0032 0.0067  61  MET   A CG  
1567 S SD  . MET   A 61  ? 0.1208 0.1274 0.1664 -0.0121 -0.0023 -0.0147 61  MET   A SD  
1568 C CE  . MET   A 61  ? 0.1416 0.1314 0.1843 -0.0162 0.0150  -0.0076 61  MET   A CE  
1578 N N   . GLN   A 62  ? 0.1090 0.1121 0.1384 -0.0095 -0.0017 -0.0030 62  GLN   A N   
1579 C CA  . GLN   A 62  ? 0.1115 0.1132 0.1423 -0.0062 0.0020  0.0065  62  GLN   A CA  
1580 C C   . GLN   A 62  ? 0.1147 0.1065 0.1481 0.0005  0.0079  0.0054  62  GLN   A C   
1581 O O   . GLN   A 62  ? 0.1146 0.1194 0.1463 -0.0042 0.0021  -0.0001 62  GLN   A O   
1582 C CB  . GLN   A 62  ? 0.1124 0.1152 0.1353 -0.0064 0.0060  0.0035  62  GLN   A CB  
1583 C CG  . GLN   A 62  ? 0.1173 0.1113 0.1455 -0.0074 -0.0008 0.0158  62  GLN   A CG  
1584 C CD  . GLN   A 62  ? 0.1227 0.1101 0.1404 -0.0071 0.0068  0.0126  62  GLN   A CD  
1585 O OE1 . GLN   A 62  ? 0.1279 0.1258 0.1460 -0.0096 -0.0004 0.0037  62  GLN   A OE1 
1586 N NE2 . GLN   A 62  ? 0.1258 0.1186 0.1493 -0.0029 0.0026  -0.0013 62  GLN   A NE2 
1595 N N   . VAL   A 63  ? 0.1083 0.1194 0.1573 -0.0082 0.0056  -0.0148 63  VAL   A N   
1596 C CA  . VAL   A 63  ? 0.1105 0.1264 0.1681 -0.0149 -0.0005 -0.0113 63  VAL   A CA  
1597 C C   . VAL   A 63  ? 0.1020 0.1262 0.1604 -0.0163 -0.0070 -0.0115 63  VAL   A C   
1598 O O   . VAL   A 63  ? 0.1066 0.1262 0.1771 -0.0148 -0.0043 -0.0034 63  VAL   A O   
1599 C CB  . VAL   A 63  ? 0.1232 0.1386 0.1982 -0.0128 -0.0012 -0.0369 63  VAL   A CB  
1600 C CG1 . VAL   A 63  ? 0.1378 0.1593 0.2401 -0.0132 -0.0098 -0.0564 63  VAL   A CG1 
1601 C CG2 . VAL   A 63  ? 0.1339 0.1323 0.2139 -0.0064 0.0069  -0.0393 63  VAL   A CG2 
1611 N N   . GLU   A 64  ? 0.1069 0.1289 0.1514 -0.0061 -0.0004 -0.0067 64  GLU   A N   
1612 C CA  . GLU   A 64  ? 0.1108 0.1266 0.1562 -0.0097 -0.0080 -0.0040 64  GLU   A CA  
1613 C C   . GLU   A 64  ? 0.1046 0.1202 0.1608 -0.0058 0.0007  0.0015  64  GLU   A C   
1614 O O   . GLU   A 64  ? 0.1122 0.1257 0.1603 -0.0017 -0.0030 0.0035  64  GLU   A O   
1615 C CB  . GLU   A 64  ? 0.1218 0.1375 0.1601 -0.0106 -0.0026 -0.0017 64  GLU   A CB  
1616 C CG  . GLU   A 64  ? 0.1266 0.1460 0.1736 -0.0132 -0.0031 -0.0015 64  GLU   A CG  
1617 C CD  . GLU   A 64  ? 0.1328 0.1507 0.1789 -0.0174 0.0006  -0.0012 64  GLU   A CD  
1618 O OE1 . GLU   A 64  ? 0.1348 0.1519 0.1971 -0.0247 0.0055  0.0066  64  GLU   A OE1 
1619 O OE2 . GLU   A 64  ? 0.1513 0.1481 0.1795 -0.0199 -0.0038 0.0045  64  GLU   A OE2 
1626 N N   . SER   A 65  ? 0.0981 0.1180 0.1555 -0.0031 0.0039  0.0055  65  SER   A N   
1627 C CA  . SER   A 65  ? 0.1082 0.1159 0.1516 -0.0034 0.0033  -0.0017 65  SER   A CA  
1628 C C   . SER   A 65  ? 0.1075 0.1228 0.1471 -0.0070 -0.0001 -0.0007 65  SER   A C   
1629 O O   . SER   A 65  ? 0.1125 0.1303 0.1687 -0.0052 0.0181  -0.0035 65  SER   A O   
1630 C CB  . SER   A 65  ? 0.1115 0.1156 0.1475 -0.0053 0.0030  0.0068  65  SER   A CB  
1631 O OG  . SER   A 65  ? 0.1130 0.1226 0.1510 -0.0086 0.0035  0.0137  65  SER   A OG  
1637 N N   . ASP   A 66  ? 0.1085 0.1208 0.1490 -0.0041 0.0080  0.0133  66  ASP   A N   
1638 C CA  . ASP   A 66  ? 0.1186 0.1311 0.1658 -0.0052 0.0141  0.0177  66  ASP   A CA  
1639 C C   . ASP   A 66  ? 0.1236 0.1266 0.1702 -0.0093 0.0144  0.0172  66  ASP   A C   
1640 O O   . ASP   A 66  ? 0.1267 0.1375 0.1902 -0.0089 0.0278  0.0250  66  ASP   A O   
1641 C CB  . ASP   A 66  ? 0.1306 0.1410 0.1924 0.0051  0.0169  0.0363  66  ASP   A CB  
1642 C CG  . ASP   A 66  ? 0.1609 0.1556 0.2200 -0.0035 0.0063  0.0515  66  ASP   A CG  
1643 O OD1 . ASP   A 66  ? 0.1574 0.1864 0.2000 -0.0111 -0.0039 0.0453  66  ASP   A OD1 
1644 O OD2 . ASP   A 66  ? 0.1778 0.1700 0.2990 0.0185  -0.0108 0.0330  66  ASP   A OD2 
1649 N N   . ASP   A 67  ? 0.1131 0.1274 0.1828 -0.0046 0.0089  0.0176  67  ASP   A N   
1650 C CA  . ASP   A 67  ? 0.1133 0.1444 0.1996 -0.0082 0.0029  0.0226  67  ASP   A CA  
1651 C C   . ASP   A 67  ? 0.1194 0.1465 0.1918 -0.0002 0.0086  0.0234  67  ASP   A C   
1652 O O   . ASP   A 67  ? 0.1173 0.1521 0.2126 -0.0022 0.0287  0.0272  67  ASP   A O   
1653 C CB  . ASP   A 67  ? 0.1209 0.1488 0.2260 -0.0067 -0.0131 0.0316  67  ASP   A CB  
1654 C CG  . ASP   A 67  ? 0.1220 0.1641 0.2623 -0.0166 -0.0257 0.0413  67  ASP   A CG  
1655 O OD1 . ASP   A 67  ? 0.1327 0.1838 0.3390 -0.0198 -0.0361 0.0575  67  ASP   A OD1 
1656 O OD2 . ASP   A 67  ? 0.1277 0.1672 0.2556 -0.0031 -0.0227 0.0397  67  ASP   A OD2 
1661 N N   . TYR   A 68  ? 0.1197 0.1319 0.1883 0.0028  0.0167  0.0240  68  TYR   A N   
1662 C CA  . TYR   A 68  ? 0.1271 0.1278 0.1850 0.0015  0.0258  0.0249  68  TYR   A CA  
1663 C C   . TYR   A 68  ? 0.1194 0.1295 0.1900 -0.0013 0.0326  0.0169  68  TYR   A C   
1664 O O   . TYR   A 68  ? 0.1281 0.1365 0.1965 0.0046  0.0291  0.0181  68  TYR   A O   
1665 C CB  . TYR   A 68  ? 0.1341 0.1276 0.1927 0.0025  0.0351  0.0240  68  TYR   A CB  
1666 C CG  . TYR   A 68  ? 0.1397 0.1450 0.2163 0.0009  0.0557  0.0303  68  TYR   A CG  
1667 C CD1 . TYR   A 68  ? 0.1432 0.1438 0.2458 -0.0206 0.0470  -0.0052 68  TYR   A CD1 
1668 C CD2 . TYR   A 68  ? 0.1582 0.1483 0.2534 0.0061  0.0549  0.0497  68  TYR   A CD2 
1669 C CE1 . TYR   A 68  ? 0.1556 0.1554 0.2871 -0.0147 0.0426  -0.0038 68  TYR   A CE1 
1670 C CE2 . TYR   A 68  ? 0.1572 0.1546 0.2826 -0.0022 0.0639  0.0298  68  TYR   A CE2 
1671 C CZ  . TYR   A 68  ? 0.1588 0.1536 0.3005 -0.0192 0.0526  -0.0056 68  TYR   A CZ  
1672 O OH  . TYR   A 68  ? 0.1915 0.1529 0.3221 -0.0161 0.0276  -0.0263 68  TYR   A OH  
1682 N N   . ILE   A 69  ? 0.1146 0.1206 0.1782 -0.0024 0.0237  0.0186  69  ILE   A N   
1683 C CA  . ILE   A 69  ? 0.1236 0.1255 0.1790 -0.0001 0.0214  0.0025  69  ILE   A CA  
1684 C C   . ILE   A 69  ? 0.1334 0.1271 0.1696 0.0031  0.0230  0.0125  69  ILE   A C   
1685 O O   . ILE   A 69  ? 0.1394 0.1349 0.1751 -0.0033 0.0327  0.0139  69  ILE   A O   
1686 C CB  . ILE   A 69  ? 0.1341 0.1466 0.1726 0.0059  0.0239  0.0004  69  ILE   A CB  
1687 C CG1 . ILE   A 69  ? 0.1289 0.1544 0.1771 0.0047  0.0164  -0.0125 69  ILE   A CG1 
1688 C CG2 . ILE   A 69  ? 0.1557 0.1700 0.1969 0.0167  0.0117  -0.0083 69  ILE   A CG2 
1689 C CD1 . ILE   A 69  ? 0.1309 0.1651 0.1946 -0.0064 0.0107  -0.0171 69  ILE   A CD1 
1701 N N   . ALA   A 70  ? 0.1389 0.1291 0.1997 -0.0146 0.0284  0.0129  70  ALA   A N   
1702 C CA  . ALA   A 70  ? 0.1378 0.1402 0.2193 -0.0192 0.0448  0.0150  70  ALA   A CA  
1703 C C   . ALA   A 70  ? 0.1334 0.1571 0.2237 -0.0209 0.0394  0.0137  70  ALA   A C   
1704 O O   . ALA   A 70  ? 0.1525 0.1951 0.2461 0.0025  0.0591  0.0321  70  ALA   A O   
1705 C CB  . ALA   A 70  ? 0.1408 0.1380 0.2418 -0.0191 0.0381  0.0113  70  ALA   A CB  
1711 N N   . THR   A 71  ? 0.1277 0.1601 0.2099 -0.0068 0.0253  0.0155  71  THR   A N   
1712 C CA  . THR   A 71  ? 0.1379 0.1735 0.2456 0.0015  0.0234  0.0205  71  THR   A CA  
1713 C C   . THR   A 71  ? 0.1221 0.1677 0.2729 0.0100  0.0329  0.0134  71  THR   A C   
1714 O O   . THR   A 71  ? 0.1336 0.1964 0.3258 0.0085  0.0485  -0.0101 71  THR   A O   
1715 C CB  . THR   A 71  ? 0.1669 0.1984 0.2768 0.0126  -0.0145 0.0248  71  THR   A CB  
1716 O OG1 . THR   A 71  ? 0.1941 0.2175 0.2820 0.0063  -0.0367 0.0214  71  THR   A OG1 
1717 C CG2 . THR   A 71  ? 0.1796 0.2180 0.3078 0.0211  -0.0258 0.0358  71  THR   A CG2 
1725 N N   . ASN   A 72  ? 0.1283 0.1494 0.2359 0.0087  0.0301  0.0190  72  ASN   A N   
1726 C CA  . ASN   A 72  ? 0.1380 0.1477 0.2319 0.0154  0.0380  0.0205  72  ASN   A CA  
1727 C C   . ASN   A 72  ? 0.1487 0.1447 0.2225 0.0079  0.0464  0.0088  72  ASN   A C   
1728 O O   . ASN   A 72  ? 0.1673 0.1440 0.2430 0.0124  0.0471  -0.0021 72  ASN   A O   
1729 C CB  . ASN   A 72  ? 0.1539 0.1553 0.2273 0.0131  0.0435  0.0276  72  ASN   A CB  
1730 C CG  . ASN   A 72  ? 0.1794 0.1684 0.2284 0.0190  0.0420  0.0324  72  ASN   A CG  
1731 O OD1 . ASN   A 72  ? 0.1950 0.1968 0.2512 0.0228  0.0454  0.0335  72  ASN   A OD1 
1732 N ND2 . ASN   A 72  ? 0.1959 0.1658 0.2325 0.0512  0.0254  0.0236  72  ASN   A ND2 
1739 N N   . GLY   A 73  ? 0.1492 0.1387 0.2073 -0.0003 0.0525  -0.0010 73  GLY   A N   
1740 C CA  . GLY   A 73  ? 0.1554 0.1430 0.1983 -0.0036 0.0497  0.0064  73  GLY   A CA  
1741 C C   . GLY   A 73  ? 0.1563 0.1316 0.1822 0.0001  0.0557  0.0195  73  GLY   A C   
1742 O O   . GLY   A 73  ? 0.1529 0.1345 0.1912 0.0051  0.0401  0.0259  73  GLY   A O   
1746 N N   . PRO   A 74  ? 0.1640 0.1330 0.1866 -0.0101 0.0547  0.0097  74  PRO   A N   
1747 C CA  . PRO   A 74  ? 0.1636 0.1332 0.1893 -0.0066 0.0528  0.0173  74  PRO   A CA  
1748 C C   . PRO   A 74  ? 0.1506 0.1190 0.1758 -0.0036 0.0409  0.0109  74  PRO   A C   
1749 O O   . PRO   A 74  ? 0.1590 0.1241 0.2000 0.0008  0.0414  0.0004  74  PRO   A O   
1750 C CB  . PRO   A 74  ? 0.1810 0.1566 0.2105 0.0007  0.0534  0.0296  74  PRO   A CB  
1751 C CG  . PRO   A 74  ? 0.2041 0.1900 0.2538 -0.0164 0.0396  0.0130  74  PRO   A CG  
1752 C CD  . PRO   A 74  ? 0.1817 0.1657 0.2124 -0.0233 0.0439  0.0025  74  PRO   A CD  
1760 N N   . LEU   A 75  ? 0.1490 0.1140 0.1608 0.0007  0.0294  0.0046  75  LEU   A N   
1761 C CA  . LEU   A 75  ? 0.1500 0.1124 0.1427 -0.0019 0.0100  0.0151  75  LEU   A CA  
1762 C C   . LEU   A 75  ? 0.1604 0.1212 0.1323 0.0030  0.0121  0.0148  75  LEU   A C   
1763 O O   . LEU   A 75  ? 0.1930 0.1375 0.1425 0.0107  0.0099  0.0128  75  LEU   A O   
1764 C CB  . LEU   A 75  ? 0.1504 0.1119 0.1319 -0.0065 0.0040  0.0223  75  LEU   A CB  
1765 C CG  . LEU   A 75  ? 0.1710 0.1526 0.1502 -0.0352 0.0079  0.0121  75  LEU   A CG  
1766 C CD1 . LEU   A 75  ? 0.1770 0.2005 0.1616 -0.0324 0.0118  0.0006  75  LEU   A CD1 
1767 C CD2 . LEU   A 75  ? 0.1969 0.1970 0.1986 -0.0131 0.0106  0.0188  75  LEU   A CD2 
1779 N N   . LYS   A 76  ? 0.1657 0.1213 0.1437 -0.0012 0.0070  0.0050  76  LYS   A N   
1780 C CA  . LYS   A 76  ? 0.1616 0.1395 0.1465 -0.0061 0.0034  0.0064  76  LYS   A CA  
1781 C C   . LYS   A 76  ? 0.1579 0.1290 0.1167 -0.0026 0.0090  0.0149  76  LYS   A C   
1782 O O   . LYS   A 76  ? 0.1614 0.1228 0.1309 -0.0048 0.0132  0.0165  76  LYS   A O   
1783 C CB  . LYS   A 76  ? 0.1621 0.1540 0.1729 0.0043  0.0079  -0.0170 76  LYS   A CB  
1784 C CG  . LYS   A 76  ? 0.1682 0.1548 0.2187 0.0059  -0.0010 -0.0187 76  LYS   A CG  
1785 C CD  . LYS   A 76  ? 0.1699 0.1621 0.2594 0.0131  -0.0066 -0.0268 76  LYS   A CD  
1786 C CE  . LYS   A 76  ? 0.1826 0.1847 0.3197 0.0063  0.0029  -0.0319 76  LYS   A CE  
1787 N NZ  . LYS   A 76  ? 0.1789 0.1799 0.3612 -0.0023 0.0057  -0.0451 76  LYS   A NZ  
1801 N N   . VAL   A 77  ? 0.1665 0.1331 0.1330 -0.0063 0.0186  0.0205  77  VAL   A N   
1802 C CA  . VAL   A 77  ? 0.1644 0.1354 0.1367 -0.0006 0.0129  0.0169  77  VAL   A CA  
1803 C C   . VAL   A 77  ? 0.1566 0.1263 0.1333 0.0068  0.0099  0.0072  77  VAL   A C   
1804 O O   . VAL   A 77  ? 0.1659 0.1342 0.1394 0.0076  0.0232  0.0093  77  VAL   A O   
1805 C CB  . VAL   A 77  ? 0.1741 0.1509 0.1409 -0.0046 0.0000  0.0235  77  VAL   A CB  
1806 C CG1 . VAL   A 77  ? 0.1773 0.1635 0.1661 0.0034  -0.0004 0.0121  77  VAL   A CG1 
1807 C CG2 . VAL   A 77  ? 0.1954 0.1645 0.1608 -0.0052 -0.0057 0.0276  77  VAL   A CG2 
1817 N N   . GLY   A 78  ? 0.1497 0.1228 0.1305 0.0018  0.0147  0.0144  78  GLY   A N   
1818 C CA  . GLY   A 78  ? 0.1452 0.1246 0.1418 -0.0035 0.0257  0.0171  78  GLY   A CA  
1819 C C   . GLY   A 78  ? 0.1362 0.1203 0.1446 0.0024  0.0201  0.0156  78  GLY   A C   
1820 O O   . GLY   A 78  ? 0.1350 0.1262 0.1586 0.0005  0.0153  0.0319  78  GLY   A O   
1824 N N   . GLY   A 79  ? 0.1448 0.1142 0.1400 -0.0036 0.0162  0.0189  79  GLY   A N   
1825 C CA  . GLY   A 79  ? 0.1402 0.1201 0.1464 -0.0040 0.0139  0.0173  79  GLY   A CA  
1826 C C   . GLY   A 79  ? 0.1221 0.1146 0.1375 -0.0014 0.0132  0.0055  79  GLY   A C   
1827 O O   . GLY   A 79  ? 0.1300 0.1260 0.1559 0.0103  0.0116  0.0089  79  GLY   A O   
1831 N N   . SER   A 80  ? 0.1177 0.1288 0.1583 -0.0013 0.0101  -0.0017 80  SER   A N   
1832 C CA  . SER   A 80  ? 0.1137 0.1234 0.1483 -0.0020 0.0086  0.0052  80  SER   A CA  
1833 C C   . SER   A 80  ? 0.1111 0.1266 0.1491 -0.0043 0.0102  0.0132  80  SER   A C   
1834 O O   . SER   A 80  ? 0.1112 0.1473 0.1829 0.0057  0.0143  0.0002  80  SER   A O   
1835 C CB  . SER   A 80  ? 0.1299 0.1209 0.1729 -0.0018 0.0071  0.0106  80  SER   A CB  
1836 O OG  . SER   A 80  ? 0.1511 0.1238 0.2131 0.0044  -0.0012 0.0290  80  SER   A OG  
1842 N N   . CYS   A 81  ? 0.1084 0.1238 0.1482 -0.0002 -0.0048 0.0193  81  CYS   A N   
1843 C CA  . CYS   A 81  ? 0.1105 0.1317 0.1462 -0.0030 -0.0066 0.0235  81  CYS   A CA  
1844 C C   . CYS   A 81  ? 0.1070 0.1256 0.1435 -0.0117 0.0010  0.0281  81  CYS   A C   
1845 O O   . CYS   A 81  ? 0.1060 0.1582 0.1570 0.0005  0.0016  0.0298  81  CYS   A O   
1846 C CB  . CYS   A 81  ? 0.1176 0.1372 0.1582 -0.0136 -0.0018 0.0272  81  CYS   A CB  
1847 S SG  . CYS   A 81  ? 0.1308 0.1243 0.1515 -0.0158 -0.0011 0.0150  81  CYS   A SG  
1853 N N   . VAL   A 82  ? 0.1087 0.1356 0.1446 -0.0019 -0.0085 0.0206  82  VAL   A N   
1854 C CA  . VAL   A 82  ? 0.1257 0.1383 0.1454 -0.0010 -0.0109 0.0305  82  VAL   A CA  
1855 C C   . VAL   A 82  ? 0.1215 0.1404 0.1522 -0.0032 -0.0094 0.0244  82  VAL   A C   
1856 O O   . VAL   A 82  ? 0.1142 0.1449 0.1732 -0.0038 -0.0106 0.0048  82  VAL   A O   
1857 C CB  . VAL   A 82  ? 0.1522 0.1505 0.1575 0.0040  -0.0012 0.0349  82  VAL   A CB  
1858 C CG1 . VAL   A 82  ? 0.1759 0.1694 0.1756 0.0065  0.0056  0.0340  82  VAL   A CG1 
1859 C CG2 . VAL   A 82  ? 0.1606 0.1467 0.1851 -0.0014 0.0011  0.0351  82  VAL   A CG2 
1869 N N   . LEU   A 83  ? 0.1164 0.1365 0.1399 -0.0050 -0.0081 0.0182  83  LEU   A N   
1870 C CA  . LEU   A 83  ? 0.1149 0.1391 0.1320 -0.0123 -0.0131 0.0127  83  LEU   A CA  
1871 C C   . LEU   A 83  ? 0.1209 0.1430 0.1337 -0.0143 -0.0160 0.0161  83  LEU   A C   
1872 O O   . LEU   A 83  ? 0.1332 0.1417 0.1441 -0.0141 -0.0108 0.0270  83  LEU   A O   
1873 C CB  . LEU   A 83  ? 0.1259 0.1448 0.1409 -0.0124 -0.0144 0.0192  83  LEU   A CB  
1874 C CG  . LEU   A 83  ? 0.1396 0.1530 0.1474 -0.0156 -0.0014 0.0144  83  LEU   A CG  
1875 C CD1 . LEU   A 83  ? 0.1478 0.1591 0.1548 -0.0235 0.0006  0.0270  83  LEU   A CD1 
1876 C CD2 . LEU   A 83  ? 0.1386 0.1664 0.1653 -0.0138 0.0109  0.0170  83  LEU   A CD2 
1888 N N   . SER   A 84  ? 0.1374 0.1489 0.1458 -0.0123 -0.0128 0.0179  84  SER   A N   
1889 C CA  . SER   A 84  ? 0.1486 0.1500 0.1270 -0.0100 -0.0151 0.0170  84  SER   A CA  
1890 C C   . SER   A 84  ? 0.1518 0.1515 0.1272 -0.0177 -0.0032 0.0128  84  SER   A C   
1891 O O   . SER   A 84  ? 0.1433 0.1632 0.1192 -0.0109 -0.0122 0.0166  84  SER   A O   
1892 C CB  . SER   A 84  ? 0.1531 0.1691 0.1414 -0.0054 -0.0164 0.0032  84  SER   A CB  
1893 O OG  . SER   A 84  ? 0.1599 0.1882 0.1574 -0.0107 -0.0259 -0.0056 84  SER   A OG  
1899 N N   . GLY   A 85  ? 0.1633 0.1652 0.1328 -0.0202 0.0090  0.0143  85  GLY   A N   
1900 C CA  . GLY   A 85  ? 0.1622 0.1712 0.1407 -0.0298 0.0135  0.0014  85  GLY   A CA  
1901 C C   . GLY   A 85  ? 0.1620 0.1805 0.1244 -0.0158 -0.0085 -0.0030 85  GLY   A C   
1902 O O   . GLY   A 85  ? 0.1597 0.1911 0.1396 -0.0262 0.0031  -0.0097 85  GLY   A O   
1906 N N   . HIS   A 86  ? 0.1686 0.1735 0.1272 -0.0073 -0.0138 0.0134  86  HIS   A N   
1907 C CA  . HIS   A 86  ? 0.1828 0.1770 0.1143 -0.0163 -0.0052 0.0109  86  HIS   A CA  
1908 C C   . HIS   A 86  ? 0.2076 0.1910 0.1067 -0.0236 -0.0115 0.0079  86  HIS   A C   
1909 O O   . HIS   A 86  ? 0.2224 0.2107 0.1217 -0.0136 -0.0024 0.0071  86  HIS   A O   
1910 C CB  . HIS   A 86  ? 0.1764 0.1691 0.1254 -0.0137 -0.0085 0.0074  86  HIS   A CB  
1911 C CG  . HIS   A 86  ? 0.1717 0.1677 0.1268 -0.0070 0.0007  0.0092  86  HIS   A CG  
1912 N ND1 . HIS   A 86  ? 0.1829 0.1671 0.1605 -0.0188 -0.0045 0.0085  86  HIS   A ND1 
1913 C CD2 . HIS   A 86  ? 0.1716 0.1637 0.1249 0.0028  -0.0004 0.0083  86  HIS   A CD2 
1914 C CE1 . HIS   A 86  ? 0.1762 0.1638 0.1611 -0.0164 0.0110  0.0142  86  HIS   A CE1 
1915 N NE2 . HIS   A 86  ? 0.1698 0.1610 0.1389 0.0036  0.0070  0.0204  86  HIS   A NE2 
1923 N N   . ASN   A 87  ? 0.2206 0.2014 0.1239 -0.0087 0.0062  -0.0044 87  ASN   A N   
1924 C CA  . ASN   A 87  ? 0.2389 0.2118 0.1196 -0.0007 0.0223  -0.0118 87  ASN   A CA  
1925 C C   . ASN   A 87  ? 0.2326 0.2249 0.1468 -0.0084 0.0463  -0.0011 87  ASN   A C   
1926 O O   . ASN   A 87  ? 0.2641 0.2481 0.1870 -0.0244 0.0828  -0.0124 87  ASN   A O   
1927 C CB  . ASN   A 87  ? 0.2647 0.2185 0.1341 0.0137  0.0284  -0.0126 87  ASN   A CB  
1928 C CG  . ASN   A 87  ? 0.2840 0.2275 0.1337 0.0220  0.0359  -0.0014 87  ASN   A CG  
1929 O OD1 . ASN   A 87  ? 0.3044 0.2270 0.1370 0.0372  0.0372  0.0024  87  ASN   A OD1 
1930 N ND2 . ASN   A 87  ? 0.2902 0.2505 0.1554 0.0204  0.0374  0.0059  87  ASN   A ND2 
1937 N N   A LEU   A 88  ? 0.2073 0.2164 0.1343 -0.0144 0.0255  0.0096  88  LEU   A N   
1938 N N   B LEU   A 88  ? 0.2089 0.2183 0.1333 -0.0111 0.0345  0.0062  88  LEU   A N   
1939 C CA  A LEU   A 88  ? 0.1883 0.2144 0.1512 -0.0205 0.0220  0.0219  88  LEU   A CA  
1940 C CA  B LEU   A 88  ? 0.1913 0.2175 0.1482 -0.0148 0.0387  0.0170  88  LEU   A CA  
1941 C C   A LEU   A 88  ? 0.1746 0.2156 0.1471 -0.0219 0.0258  0.0265  88  LEU   A C   
1942 C C   B LEU   A 88  ? 0.1758 0.2169 0.1414 -0.0176 0.0353  0.0397  88  LEU   A C   
1943 O O   A LEU   A 88  ? 0.1720 0.2182 0.1738 -0.0234 0.0293  0.0287  88  LEU   A O   
1944 O O   B LEU   A 88  ? 0.1730 0.2182 0.1540 -0.0133 0.0399  0.0731  88  LEU   A O   
1945 C CB  A LEU   A 88  ? 0.1853 0.2156 0.1616 -0.0242 -0.0061 0.0384  88  LEU   A CB  
1946 C CB  B LEU   A 88  ? 0.1922 0.2213 0.1606 -0.0151 0.0247  0.0151  88  LEU   A CB  
1947 C CG  A LEU   A 88  ? 0.1956 0.2199 0.1803 -0.0219 -0.0209 0.0470  88  LEU   A CG  
1948 C CG  B LEU   A 88  ? 0.2012 0.2264 0.1765 -0.0108 0.0200  0.0056  88  LEU   A CG  
1949 C CD1 A LEU   A 88  ? 0.2009 0.2217 0.1797 -0.0242 -0.0251 0.0490  88  LEU   A CD1 
1950 C CD1 B LEU   A 88  ? 0.2031 0.2280 0.1734 -0.0120 0.0231  -0.0036 88  LEU   A CD1 
1951 C CD2 A LEU   A 88  ? 0.2076 0.2319 0.2154 -0.0136 -0.0165 0.0375  88  LEU   A CD2 
1952 C CD2 B LEU   A 88  ? 0.2117 0.2360 0.2006 -0.0014 0.0230  0.0002  88  LEU   A CD2 
1975 N N   . ALA   A 89  ? 0.1714 0.2112 0.1371 -0.0132 0.0171  0.0213  89  ALA   A N   
1976 C CA  . ALA   A 89  ? 0.1710 0.2065 0.1219 -0.0060 0.0039  0.0242  89  ALA   A CA  
1977 C C   . ALA   A 89  ? 0.1717 0.2094 0.1321 -0.0050 -0.0060 0.0264  89  ALA   A C   
1978 O O   . ALA   A 89  ? 0.1681 0.2067 0.1736 -0.0190 -0.0087 -0.0031 89  ALA   A O   
1979 C CB  . ALA   A 89  ? 0.1684 0.2035 0.1230 -0.0093 0.0021  0.0188  89  ALA   A CB  
1986 N N   A LYS   A 90  ? 0.1814 0.2211 0.1342 -0.0085 -0.0134 0.0312  90  LYS   A N   
1987 N N   B LYS   A 90  ? 0.1717 0.2164 0.1233 -0.0105 -0.0148 0.0263  90  LYS   A N   
1988 C CA  A LYS   A 90  ? 0.1949 0.2363 0.1509 -0.0085 -0.0270 0.0354  90  LYS   A CA  
1989 C CA  B LYS   A 90  ? 0.1768 0.2282 0.1314 -0.0112 -0.0335 0.0231  90  LYS   A CA  
1990 C C   A LYS   A 90  ? 0.1849 0.2247 0.1499 -0.0137 -0.0270 0.0266  90  LYS   A C   
1991 C C   B LYS   A 90  ? 0.1572 0.2134 0.1264 -0.0190 -0.0334 0.0121  90  LYS   A C   
1992 O O   A LYS   A 90  ? 0.1935 0.2358 0.1738 -0.0148 -0.0326 0.0292  90  LYS   A O   
1993 O O   B LYS   A 90  ? 0.1614 0.2276 0.1563 -0.0270 -0.0379 0.0020  90  LYS   A O   
1994 C CB  A LYS   A 90  ? 0.2156 0.2646 0.1926 -0.0053 -0.0348 0.0512  90  LYS   A CB  
1995 C CB  B LYS   A 90  ? 0.1981 0.2561 0.1714 -0.0067 -0.0463 0.0364  90  LYS   A CB  
1996 C CG  A LYS   A 90  ? 0.2416 0.2911 0.2774 -0.0023 -0.0354 0.0594  90  LYS   A CG  
1997 C CG  B LYS   A 90  ? 0.2274 0.2822 0.2659 -0.0025 -0.0471 0.0421  90  LYS   A CG  
1998 C CD  A LYS   A 90  ? 0.2625 0.3129 0.3539 -0.0030 -0.0283 0.0642  90  LYS   A CD  
1999 C CD  B LYS   A 90  ? 0.2512 0.3036 0.3483 -0.0019 -0.0387 0.0447  90  LYS   A CD  
2000 C CE  A LYS   A 90  ? 0.2802 0.3312 0.4128 -0.0039 -0.0205 0.0631  90  LYS   A CE  
2001 C CE  B LYS   A 90  ? 0.2714 0.3207 0.4100 -0.0014 -0.0304 0.0408  90  LYS   A CE  
2002 N NZ  A LYS   A 90  ? 0.2930 0.3433 0.4532 -0.0061 -0.0127 0.0610  90  LYS   A NZ  
2003 N NZ  B LYS   A 90  ? 0.2850 0.3305 0.4505 -0.0018 -0.0222 0.0367  90  LYS   A NZ  
2030 N N   A HIS   A 91  ? 0.1755 0.2005 0.1361 -0.0159 -0.0251 0.0241  91  HIS   A N   
2031 N N   B HIS   A 91  ? 0.1473 0.1814 0.1037 -0.0161 -0.0319 0.0207  91  HIS   A N   
2032 C CA  A HIS   A 91  ? 0.1652 0.1845 0.1400 -0.0149 -0.0196 0.0223  91  HIS   A CA  
2033 C CA  B HIS   A 91  ? 0.1360 0.1660 0.1085 -0.0068 -0.0287 0.0143  91  HIS   A CA  
2034 C C   A HIS   A 91  ? 0.1425 0.1592 0.1203 -0.0146 -0.0074 0.0226  91  HIS   A C   
2035 C C   B HIS   A 91  ? 0.1282 0.1565 0.1089 -0.0079 -0.0163 0.0117  91  HIS   A C   
2036 O O   A HIS   A 91  ? 0.1339 0.1511 0.1142 -0.0162 0.0043  0.0230  91  HIS   A O   
2037 O O   B HIS   A 91  ? 0.1228 0.1636 0.1225 -0.0095 -0.0112 0.0061  91  HIS   A O   
2038 C CB  A HIS   A 91  ? 0.1876 0.2087 0.1781 -0.0039 -0.0294 0.0202  91  HIS   A CB  
2039 C CB  B HIS   A 91  ? 0.1505 0.1886 0.1528 0.0154  -0.0371 0.0240  91  HIS   A CB  
2040 C CG  A HIS   A 91  ? 0.2230 0.2456 0.2257 0.0055  -0.0492 0.0078  91  HIS   A CG  
2041 C CG  B HIS   A 91  ? 0.1859 0.2309 0.2108 0.0301  -0.0587 0.0173  91  HIS   A CG  
2042 N ND1 A HIS   A 91  ? 0.2341 0.2653 0.2572 0.0089  -0.0588 -0.0071 91  HIS   A ND1 
2043 N ND1 B HIS   A 91  ? 0.1944 0.2554 0.2521 0.0315  -0.0656 -0.0009 91  HIS   A ND1 
2044 C CD2 A HIS   A 91  ? 0.2425 0.2618 0.2434 0.0095  -0.0579 0.0093  91  HIS   A CD2 
2045 C CD2 B HIS   A 91  ? 0.2117 0.2496 0.2302 0.0317  -0.0653 0.0236  91  HIS   A CD2 
2046 C CE1 A HIS   A 91  ? 0.2438 0.2729 0.2662 0.0143  -0.0608 -0.0021 91  HIS   A CE1 
2047 C CE1 B HIS   A 91  ? 0.2077 0.2627 0.2604 0.0355  -0.0620 0.0063  91  HIS   A CE1 
2048 N NE2 A HIS   A 91  ? 0.2519 0.2720 0.2620 0.0153  -0.0636 0.0022  91  HIS   A NE2 
2049 N NE2 B HIS   A 91  ? 0.2196 0.2621 0.2518 0.0370  -0.0660 0.0123  91  HIS   A NE2 
2064 N N   . CYS   A 92  ? 0.1282 0.1531 0.1148 -0.0162 -0.0065 0.0180  92  CYS   A N   
2065 C CA  . CYS   A 92  ? 0.1223 0.1458 0.1231 -0.0134 -0.0006 0.0136  92  CYS   A CA  
2066 C C   . CYS   A 92  ? 0.1202 0.1345 0.1150 -0.0150 0.0019  0.0204  92  CYS   A C   
2067 O O   . CYS   A 92  ? 0.1189 0.1442 0.1459 -0.0134 0.0019  0.0160  92  CYS   A O   
2068 C CB  . CYS   A 92  ? 0.1236 0.1448 0.1342 -0.0091 -0.0098 0.0114  92  CYS   A CB  
2069 S SG  . CYS   A 92  ? 0.1267 0.1313 0.1247 -0.0141 -0.0040 0.0145  92  CYS   A SG  
2076 N N   . LEU   A 93  ? 0.1185 0.1177 0.1243 -0.0113 0.0070  0.0176  93  LEU   A N   
2077 C CA  . LEU   A 93  ? 0.1108 0.1192 0.1270 -0.0057 -0.0026 0.0184  93  LEU   A CA  
2078 C C   . LEU   A 93  ? 0.1090 0.1117 0.1207 0.0017  0.0027  0.0105  93  LEU   A C   
2079 O O   . LEU   A 93  ? 0.1067 0.1200 0.1149 -0.0020 0.0032  0.0149  93  LEU   A O   
2080 C CB  . LEU   A 93  ? 0.1125 0.1199 0.1299 -0.0056 -0.0050 0.0257  93  LEU   A CB  
2081 C CG  . LEU   A 93  ? 0.1281 0.1200 0.1475 -0.0024 0.0008  0.0349  93  LEU   A CG  
2082 C CD1 . LEU   A 93  ? 0.1268 0.1276 0.1678 0.0043  0.0082  0.0220  93  LEU   A CD1 
2083 C CD2 . LEU   A 93  ? 0.1396 0.1185 0.1675 -0.0108 -0.0018 0.0209  93  LEU   A CD2 
2095 N N   . HIS   A 94  ? 0.1069 0.1085 0.1221 -0.0044 0.0043  0.0245  94  HIS   A N   
2096 C CA  . HIS   A 94  ? 0.1095 0.1109 0.1333 -0.0054 0.0007  0.0194  94  HIS   A CA  
2097 C C   . HIS   A 94  ? 0.1066 0.1072 0.1320 -0.0075 -0.0017 0.0129  94  HIS   A C   
2098 O O   . HIS   A 94  ? 0.1039 0.1324 0.1598 -0.0016 -0.0019 -0.0018 94  HIS   A O   
2099 C CB  . HIS   A 94  ? 0.1064 0.1113 0.1309 -0.0087 -0.0032 0.0156  94  HIS   A CB  
2100 C CG  . HIS   A 94  ? 0.1077 0.1123 0.1235 -0.0082 -0.0050 0.0163  94  HIS   A CG  
2101 N ND1 . HIS   A 94  ? 0.1097 0.1109 0.1342 -0.0027 -0.0035 0.0203  94  HIS   A ND1 
2102 C CD2 . HIS   A 94  ? 0.1151 0.1185 0.1370 -0.0066 -0.0089 0.0106  94  HIS   A CD2 
2103 C CE1 . HIS   A 94  ? 0.1150 0.1159 0.1295 -0.0087 -0.0108 0.0117  94  HIS   A CE1 
2104 N NE2 . HIS   A 94  ? 0.1177 0.1183 0.1299 -0.0115 -0.0110 0.0097  94  HIS   A NE2 
2112 N N   . VAL   A 95  ? 0.1033 0.1027 0.1185 -0.0046 0.0045  0.0140  95  VAL   A N   
2113 C CA  . VAL   A 95  ? 0.1121 0.1083 0.1135 -0.0078 0.0048  0.0180  95  VAL   A CA  
2114 C C   . VAL   A 95  ? 0.1139 0.1097 0.1066 -0.0117 0.0003  0.0105  95  VAL   A C   
2115 O O   . VAL   A 95  ? 0.1171 0.1228 0.1256 0.0087  0.0016  0.0144  95  VAL   A O   
2116 C CB  . VAL   A 95  ? 0.1127 0.1115 0.1326 -0.0089 0.0090  0.0099  95  VAL   A CB  
2117 C CG1 . VAL   A 95  ? 0.1323 0.1128 0.1494 -0.0157 0.0018  0.0068  95  VAL   A CG1 
2118 C CG2 . VAL   A 95  ? 0.1196 0.1180 0.1357 -0.0061 0.0128  0.0264  95  VAL   A CG2 
2128 N N   . VAL   A 96  ? 0.1182 0.1114 0.1003 -0.0058 0.0033  0.0195  96  VAL   A N   
2129 C CA  . VAL   A 96  ? 0.1264 0.1130 0.1269 -0.0087 0.0050  0.0240  96  VAL   A CA  
2130 C C   . VAL   A 96  ? 0.1300 0.1200 0.1223 -0.0107 0.0025  0.0177  96  VAL   A C   
2131 O O   . VAL   A 96  ? 0.1363 0.1243 0.1469 -0.0094 0.0137  0.0030  96  VAL   A O   
2132 C CB  . VAL   A 96  ? 0.1332 0.1196 0.1288 -0.0087 0.0140  0.0115  96  VAL   A CB  
2133 C CG1 . VAL   A 96  ? 0.1386 0.1248 0.1285 -0.0044 0.0120  0.0127  96  VAL   A CG1 
2134 C CG2 . VAL   A 96  ? 0.1363 0.1267 0.1429 -0.0132 0.0189  0.0080  96  VAL   A CG2 
2144 N N   A GLY   A 97  ? 0.1310 0.1196 0.1304 -0.0132 0.0010  0.0162  97  GLY   A N   
2145 N N   B GLY   A 97  ? 0.1293 0.1244 0.1160 -0.0101 -0.0016 0.0135  97  GLY   A N   
2146 C CA  A GLY   A 97  ? 0.1380 0.1320 0.1352 -0.0085 -0.0031 0.0200  97  GLY   A CA  
2147 C CA  B GLY   A 97  ? 0.1348 0.1354 0.1177 -0.0043 -0.0018 0.0211  97  GLY   A CA  
2148 C C   A GLY   A 97  ? 0.1442 0.1401 0.1231 -0.0100 -0.0031 0.0147  97  GLY   A C   
2149 C C   B GLY   A 97  ? 0.1385 0.1411 0.1188 -0.0020 0.0000  0.0214  97  GLY   A C   
2150 O O   A GLY   A 97  ? 0.1513 0.1391 0.1256 -0.0092 0.0022  0.0153  97  GLY   A O   
2151 O O   B GLY   A 97  ? 0.1452 0.1375 0.1371 -0.0017 0.0065  0.0241  97  GLY   A O   
2158 N N   A PRO   A 98  ? 0.1487 0.1379 0.1090 -0.0015 -0.0083 0.0121  98  PRO   A N   
2159 N N   B PRO   A 98  ? 0.1458 0.1450 0.1275 0.0062  -0.0015 0.0259  98  PRO   A N   
2160 C CA  A PRO   A 98  ? 0.1542 0.1454 0.1052 -0.0030 -0.0021 0.0063  98  PRO   A CA  
2161 C CA  B PRO   A 98  ? 0.1520 0.1545 0.1373 0.0052  0.0005  0.0162  98  PRO   A CA  
2162 C C   A PRO   A 98  ? 0.1596 0.1564 0.0963 -0.0075 0.0061  0.0132  98  PRO   A C   
2163 C C   B PRO   A 98  ? 0.1687 0.1498 0.1371 0.0027  -0.0016 0.0193  98  PRO   A C   
2164 O O   A PRO   A 98  ? 0.1554 0.1439 0.0944 -0.0004 0.0044  0.0066  98  PRO   A O   
2165 O O   B PRO   A 98  ? 0.1636 0.1481 0.1576 0.0052  0.0034  0.0180  98  PRO   A O   
2166 C CB  A PRO   A 98  ? 0.1590 0.1491 0.1029 0.0107  -0.0083 -0.0065 98  PRO   A CB  
2167 C CB  B PRO   A 98  ? 0.1595 0.1568 0.1317 0.0153  0.0027  0.0194  98  PRO   A CB  
2168 C CG  A PRO   A 98  ? 0.1547 0.1392 0.1060 0.0155  -0.0107 -0.0065 98  PRO   A CG  
2169 C CG  B PRO   A 98  ? 0.1649 0.1574 0.1468 0.0105  0.0033  0.0155  98  PRO   A CG  
2170 C CD  A PRO   A 98  ? 0.1511 0.1349 0.1101 0.0057  -0.0086 0.0065  98  PRO   A CD  
2171 C CD  B PRO   A 98  ? 0.1505 0.1499 0.1381 0.0079  -0.0042 0.0227  98  PRO   A CD  
2186 N N   A ASN   A 99  ? 0.1606 0.1765 0.0991 -0.0116 0.0048  0.0220  99  ASN   A N   
2187 N N   B ASN   A 99  ? 0.1951 0.1517 0.1341 0.0085  -0.0125 0.0291  99  ASN   A N   
2188 C CA  A ASN   A 99  ? 0.1752 0.1965 0.1105 -0.0151 -0.0006 0.0306  99  ASN   A CA  
2189 C CA  B ASN   A 99  ? 0.2250 0.1547 0.1558 0.0162  -0.0170 0.0406  99  ASN   A CA  
2190 C C   A ASN   A 99  ? 0.1905 0.2269 0.0973 -0.0238 0.0040  0.0402  99  ASN   A C   
2191 C C   B ASN   A 99  ? 0.2337 0.1612 0.1457 0.0152  -0.0231 0.0508  99  ASN   A C   
2192 O O   A ASN   A 99  ? 0.1985 0.2457 0.1152 -0.0150 0.0047  0.0271  99  ASN   A O   
2193 O O   B ASN   A 99  ? 0.2336 0.1606 0.1410 0.0196  -0.0223 0.0401  99  ASN   A O   
2194 C CB  A ASN   A 99  ? 0.1825 0.1917 0.1358 -0.0080 -0.0120 0.0343  99  ASN   A CB  
2195 C CB  B ASN   A 99  ? 0.2487 0.1565 0.1973 0.0190  -0.0293 0.0386  99  ASN   A CB  
2196 C CG  A ASN   A 99  ? 0.1890 0.1945 0.1568 -0.0012 -0.0211 0.0319  99  ASN   A CG  
2197 C CG  B ASN   A 99  ? 0.2697 0.1645 0.2236 0.0174  -0.0377 0.0314  99  ASN   A CG  
2198 O OD1 A ASN   A 99  ? 0.1981 0.2011 0.1532 0.0064  -0.0182 0.0193  99  ASN   A OD1 
2199 O OD1 B ASN   A 99  ? 0.2717 0.1668 0.2212 0.0273  -0.0522 0.0375  99  ASN   A OD1 
2200 N ND2 A ASN   A 99  ? 0.1927 0.1928 0.1691 -0.0019 -0.0200 0.0509  99  ASN   A ND2 
2201 N ND2 B ASN   A 99  ? 0.2820 0.1714 0.2577 0.0174  -0.0401 0.0173  99  ASN   A ND2 
2214 N N   A VAL   A 100 ? 0.2022 0.2418 0.1030 -0.0346 -0.0172 0.0379  100 VAL   A N   
2215 N N   B VAL   A 100 ? 0.2506 0.1910 0.1699 0.0105  -0.0243 0.0554  100 VAL   A N   
2216 C CA  A VAL   A 100 ? 0.2212 0.2631 0.1374 -0.0354 -0.0219 0.0422  100 VAL   A CA  
2217 C CA  B VAL   A 100 ? 0.2716 0.2133 0.2071 0.0129  -0.0316 0.0494  100 VAL   A CA  
2218 C C   A VAL   A 100 ? 0.2315 0.2761 0.1462 -0.0347 -0.0247 0.0605  100 VAL   A C   
2219 C C   B VAL   A 100 ? 0.2864 0.2269 0.2112 0.0187  -0.0371 0.0434  100 VAL   A C   
2220 O O   A VAL   A 100 ? 0.2373 0.2812 0.1641 -0.0313 -0.0192 0.0572  100 VAL   A O   
2221 O O   B VAL   A 100 ? 0.2939 0.2328 0.2155 0.0137  -0.0418 0.0310  100 VAL   A O   
2222 C CB  A VAL   A 100 ? 0.2348 0.2703 0.1781 -0.0388 -0.0233 0.0287  100 VAL   A CB  
2223 C CB  B VAL   A 100 ? 0.2755 0.2215 0.2490 0.0085  -0.0225 0.0411  100 VAL   A CB  
2224 C CG1 A VAL   A 100 ? 0.2399 0.2770 0.1908 -0.0393 -0.0211 0.0267  100 VAL   A CG1 
2225 C CG1 B VAL   A 100 ? 0.2793 0.2214 0.2638 0.0021  -0.0158 0.0366  100 VAL   A CG1 
2226 C CG2 A VAL   A 100 ? 0.2407 0.2714 0.1862 -0.0369 -0.0195 0.0242  100 VAL   A CG2 
2227 C CG2 B VAL   A 100 ? 0.2753 0.2290 0.2632 0.0133  -0.0251 0.0417  100 VAL   A CG2 
2246 N N   A ASN   A 101 ? 0.2424 0.2847 0.1622 -0.0372 -0.0261 0.0790  101 ASN   A N   
2247 N N   B ASN   A 101 ? 0.2950 0.2387 0.2077 0.0293  -0.0373 0.0428  101 ASN   A N   
2248 C CA  A ASN   A 101 ? 0.2588 0.2919 0.1770 -0.0366 -0.0228 0.0922  101 ASN   A CA  
2249 C CA  B ASN   A 101 ? 0.3074 0.2554 0.2194 0.0424  -0.0313 0.0522  101 ASN   A CA  
2250 C C   A ASN   A 101 ? 0.2790 0.3104 0.1962 -0.0323 -0.0115 0.1066  101 ASN   A C   
2251 C C   B ASN   A 101 ? 0.3244 0.2695 0.2220 0.0384  -0.0126 0.0628  101 ASN   A C   
2252 O O   A ASN   A 101 ? 0.2887 0.3151 0.2199 -0.0303 -0.0124 0.1005  101 ASN   A O   
2253 O O   B ASN   A 101 ? 0.3313 0.2733 0.2227 0.0359  -0.0116 0.0736  101 ASN   A O   
2254 C CB  A ASN   A 101 ? 0.2560 0.2785 0.1631 -0.0394 -0.0291 0.0853  101 ASN   A CB  
2255 C CB  B ASN   A 101 ? 0.3038 0.2602 0.2386 0.0486  -0.0318 0.0475  101 ASN   A CB  
2256 C CG  A ASN   A 101 ? 0.2566 0.2715 0.1726 -0.0378 -0.0281 0.0521  101 ASN   A CG  
2257 C CG  B ASN   A 101 ? 0.3035 0.2695 0.2650 0.0516  -0.0306 0.0372  101 ASN   A CG  
2258 O OD1 A ASN   A 101 ? 0.2520 0.2695 0.1743 -0.0307 -0.0249 0.0256  101 ASN   A OD1 
2259 O OD1 B ASN   A 101 ? 0.3079 0.2781 0.2854 0.0509  -0.0308 0.0345  101 ASN   A OD1 
2260 N ND2 A ASN   A 101 ? 0.2630 0.2713 0.1881 -0.0393 -0.0302 0.0396  101 ASN   A ND2 
2261 N ND2 B ASN   A 101 ? 0.3012 0.2685 0.2767 0.0549  -0.0228 0.0304  101 ASN   A ND2 
2274 N N   A LYS   A 102 ? 0.2868 0.3269 0.2208 -0.0325 -0.0038 0.1053  102 LYS   A N   
2275 N N   B LYS   A 102 ? 0.3297 0.2801 0.2437 0.0387  0.0017  0.0542  102 LYS   A N   
2276 C CA  A LYS   A 102 ? 0.3008 0.3449 0.2441 -0.0281 -0.0092 0.0887  102 LYS   A CA  
2277 C CA  B LYS   A 102 ? 0.3352 0.2968 0.2487 0.0346  0.0134  0.0471  102 LYS   A CA  
2278 C C   A LYS   A 102 ? 0.3067 0.3606 0.2375 -0.0187 -0.0089 0.0828  102 LYS   A C   
2279 C C   B LYS   A 102 ? 0.3263 0.2952 0.2188 0.0410  0.0138  0.0633  102 LYS   A C   
2280 O O   A LYS   A 102 ? 0.3112 0.3695 0.2457 -0.0145 -0.0090 0.0782  102 LYS   A O   
2281 O O   B LYS   A 102 ? 0.3300 0.3000 0.2350 0.0455  0.0208  0.0673  102 LYS   A O   
2282 C CB  A LYS   A 102 ? 0.3094 0.3476 0.2820 -0.0305 -0.0183 0.0660  102 LYS   A CB  
2283 C CB  B LYS   A 102 ? 0.3492 0.3137 0.2941 0.0264  0.0102  0.0247  102 LYS   A CB  
2284 C CG  A LYS   A 102 ? 0.3177 0.3475 0.3158 -0.0312 -0.0267 0.0452  102 LYS   A CG  
2285 C CG  B LYS   A 102 ? 0.3624 0.3308 0.3409 0.0182  0.0062  0.0102  102 LYS   A CG  
2286 C CD  A LYS   A 102 ? 0.3271 0.3494 0.3524 -0.0305 -0.0356 0.0230  102 LYS   A CD  
2287 C CD  B LYS   A 102 ? 0.3742 0.3464 0.3833 0.0131  -0.0000 0.0006  102 LYS   A CD  
2288 C CE  A LYS   A 102 ? 0.3349 0.3497 0.3810 -0.0297 -0.0401 0.0092  102 LYS   A CE  
2289 C CE  B LYS   A 102 ? 0.3833 0.3580 0.4175 0.0093  -0.0055 -0.0024 102 LYS   A CE  
2290 N NZ  A LYS   A 102 ? 0.3389 0.3501 0.3972 -0.0312 -0.0400 -0.0001 102 LYS   A NZ  
2291 N NZ  B LYS   A 102 ? 0.3888 0.3639 0.4385 0.0080  -0.0094 -0.0049 102 LYS   A NZ  
2318 N N   A GLY   A 103 ? 0.3082 0.3678 0.2471 -0.0115 -0.0096 0.0697  103 GLY   A N   
2319 N N   B GLY   A 103 ? 0.3104 0.2928 0.1733 0.0465  0.0022  0.0605  103 GLY   A N   
2320 C CA  A GLY   A 103 ? 0.3098 0.3722 0.2521 -0.0043 -0.0036 0.0575  103 GLY   A CA  
2321 C CA  B GLY   A 103 ? 0.2962 0.2873 0.1710 0.0500  -0.0102 0.0614  103 GLY   A CA  
2322 C C   A GLY   A 103 ? 0.3095 0.3774 0.2675 -0.0004 0.0048  0.0435  103 GLY   A C   
2323 C C   B GLY   A 103 ? 0.2797 0.2802 0.1677 0.0497  -0.0232 0.0543  103 GLY   A C   
2324 O O   A GLY   A 103 ? 0.3136 0.3835 0.2939 0.0062  0.0037  0.0334  103 GLY   A O   
2325 O O   B GLY   A 103 ? 0.2904 0.2879 0.1786 0.0548  -0.0191 0.0526  103 GLY   A O   
2332 N N   A GLU   A 104 ? 0.3025 0.3747 0.2449 -0.0070 0.0188  0.0382  104 GLU   A N   
2333 N N   B GLU   A 104 ? 0.2496 0.2607 0.1472 0.0387  -0.0314 0.0535  104 GLU   A N   
2334 C CA  A GLU   A 104 ? 0.2961 0.3706 0.2272 -0.0149 0.0265  0.0310  104 GLU   A CA  
2335 C CA  B GLU   A 104 ? 0.2230 0.2417 0.1254 0.0224  -0.0317 0.0436  104 GLU   A CA  
2336 C C   A GLU   A 104 ? 0.3012 0.3755 0.2236 -0.0175 0.0188  0.0109  104 GLU   A C   
2337 C C   B GLU   A 104 ? 0.2184 0.2395 0.1409 0.0232  -0.0277 0.0210  104 GLU   A C   
2338 O O   A GLU   A 104 ? 0.3014 0.3770 0.2274 -0.0184 0.0116  0.0077  104 GLU   A O   
2339 O O   B GLU   A 104 ? 0.2105 0.2340 0.1900 0.0258  -0.0292 0.0173  104 GLU   A O   
2340 C CB  A GLU   A 104 ? 0.2825 0.3612 0.2155 -0.0214 0.0425  0.0465  104 GLU   A CB  
2341 C CB  B GLU   A 104 ? 0.2053 0.2273 0.1198 0.0016  -0.0247 0.0516  104 GLU   A CB  
2342 C CG  A GLU   A 104 ? 0.2728 0.3523 0.2149 -0.0257 0.0518  0.0580  104 GLU   A CG  
2343 C CG  B GLU   A 104 ? 0.1954 0.2258 0.1318 -0.0176 -0.0193 0.0542  104 GLU   A CG  
2344 C CD  A GLU   A 104 ? 0.2630 0.3432 0.2106 -0.0285 0.0585  0.0692  104 GLU   A CD  
2345 C CD  B GLU   A 104 ? 0.1899 0.2265 0.1417 -0.0274 -0.0255 0.0525  104 GLU   A CD  
2346 O OE1 A GLU   A 104 ? 0.2569 0.3374 0.1919 -0.0319 0.0636  0.0806  104 GLU   A OE1 
2347 O OE1 B GLU   A 104 ? 0.1863 0.2257 0.1491 -0.0271 -0.0347 0.0492  104 GLU   A OE1 
2348 O OE2 A GLU   A 104 ? 0.2652 0.3422 0.2223 -0.0267 0.0594  0.0685  104 GLU   A OE2 
2349 O OE2 B GLU   A 104 ? 0.1951 0.2318 0.1586 -0.0350 -0.0030 0.0510  104 GLU   A OE2 
2362 N N   A ASP   A 105 ? 0.3064 0.3796 0.2295 -0.0187 0.0194  -0.0090 105 ASP   A N   
2363 N N   B ASP   A 105 ? 0.2344 0.2386 0.1499 0.0200  -0.0174 0.0118  105 ASP   A N   
2364 C CA  A ASP   A 105 ? 0.3084 0.3836 0.2473 -0.0197 0.0166  -0.0315 105 ASP   A CA  
2365 C CA  B ASP   A 105 ? 0.2488 0.2385 0.1827 0.0215  -0.0116 -0.0125 105 ASP   A CA  
2366 C C   A ASP   A 105 ? 0.2857 0.3760 0.2210 -0.0318 0.0077  -0.0447 105 ASP   A C   
2367 C C   B ASP   A 105 ? 0.2406 0.2210 0.1520 0.0123  -0.0135 -0.0190 105 ASP   A C   
2368 O O   A ASP   A 105 ? 0.2789 0.3773 0.1971 -0.0330 0.0123  -0.0560 105 ASP   A O   
2369 O O   B ASP   A 105 ? 0.2250 0.2033 0.1167 0.0189  -0.0091 -0.0144 105 ASP   A O   
2370 C CB  A ASP   A 105 ? 0.3304 0.3939 0.2987 -0.0091 0.0217  -0.0393 105 ASP   A CB  
2371 C CB  B ASP   A 105 ? 0.2736 0.2579 0.2541 0.0348  0.0041  -0.0391 105 ASP   A CB  
2372 C CG  A ASP   A 105 ? 0.3474 0.4029 0.3441 -0.0021 0.0218  -0.0454 105 ASP   A CG  
2373 C CG  B ASP   A 105 ? 0.2930 0.2726 0.3111 0.0497  0.0205  -0.0687 105 ASP   A CG  
2374 O OD1 A ASP   A 105 ? 0.3525 0.4071 0.3539 -0.0005 0.0186  -0.0531 105 ASP   A OD1 
2375 O OD1 B ASP   A 105 ? 0.3001 0.2761 0.3110 0.0460  0.0162  -0.0843 105 ASP   A OD1 
2376 O OD2 A ASP   A 105 ? 0.3561 0.4058 0.3723 0.0008  0.0259  -0.0405 105 ASP   A OD2 
2377 O OD2 B ASP   A 105 ? 0.3039 0.2825 0.3555 0.0577  0.0309  -0.0691 105 ASP   A OD2 
2386 N N   A ILE   A 106 ? 0.2685 0.3636 0.2259 -0.0441 -0.0131 -0.0491 106 ILE   A N   
2387 N N   B ILE   A 106 ? 0.2439 0.2308 0.1747 0.0001  -0.0280 -0.0185 106 ILE   A N   
2388 C CA  A ILE   A 106 ? 0.2460 0.3491 0.2329 -0.0566 -0.0313 -0.0571 106 ILE   A CA  
2389 C CA  B ILE   A 106 ? 0.2413 0.2402 0.1957 -0.0201 -0.0389 -0.0253 106 ILE   A CA  
2390 C C   A ILE   A 106 ? 0.2338 0.3265 0.2397 -0.0746 -0.0284 -0.0766 106 ILE   A C   
2391 C C   B ILE   A 106 ? 0.2404 0.2323 0.1999 -0.0288 -0.0281 -0.0166 106 ILE   A C   
2392 O O   A ILE   A 106 ? 0.2190 0.3178 0.2335 -0.0828 -0.0167 -0.0831 106 ILE   A O   
2393 O O   B ILE   A 106 ? 0.2301 0.2296 0.1979 -0.0339 -0.0163 -0.0169 106 ILE   A O   
2394 C CB  A ILE   A 106 ? 0.2435 0.3583 0.2575 -0.0452 -0.0455 -0.0328 106 ILE   A CB  
2395 C CB  B ILE   A 106 ? 0.2497 0.2676 0.2405 -0.0224 -0.0496 -0.0205 106 ILE   A CB  
2396 C CG1 A ILE   A 106 ? 0.2349 0.3599 0.2775 -0.0362 -0.0484 -0.0148 106 ILE   A CG1 
2397 C CG1 B ILE   A 106 ? 0.2533 0.2835 0.2749 -0.0179 -0.0446 -0.0055 106 ILE   A CG1 
2398 C CG2 A ILE   A 106 ? 0.2487 0.3611 0.2644 -0.0422 -0.0499 -0.0297 106 ILE   A CG2 
2399 C CG2 B ILE   A 106 ? 0.2546 0.2747 0.2493 -0.0275 -0.0544 -0.0262 106 ILE   A CG2 
2400 C CD1 A ILE   A 106 ? 0.2313 0.3590 0.2888 -0.0286 -0.0487 -0.0063 106 ILE   A CD1 
2401 C CD1 B ILE   A 106 ? 0.2570 0.2894 0.2943 -0.0125 -0.0375 -0.0009 106 ILE   A CD1 
2424 N N   A GLN   A 107 ? 0.2477 0.3149 0.2691 -0.0744 -0.0190 -0.0848 107 GLN   A N   
2425 N N   B GLN   A 107 ? 0.2568 0.2236 0.2213 -0.0270 -0.0161 -0.0103 107 GLN   A N   
2426 C CA  A GLN   A 107 ? 0.2641 0.3045 0.3214 -0.0625 -0.0019 -0.0776 107 GLN   A CA  
2427 C CA  B GLN   A 107 ? 0.2758 0.2262 0.2746 -0.0233 -0.0059 -0.0024 107 GLN   A CA  
2428 C C   A GLN   A 107 ? 0.2366 0.2651 0.3001 -0.0529 0.0200  -0.0602 107 GLN   A C   
2429 C C   B GLN   A 107 ? 0.2487 0.1906 0.2464 -0.0167 0.0113  0.0105  107 GLN   A C   
2430 O O   A GLN   A 107 ? 0.2444 0.2676 0.3425 -0.0491 0.0338  -0.0576 107 GLN   A O   
2431 O O   B GLN   A 107 ? 0.2533 0.1855 0.2609 -0.0139 0.0129  0.0047  107 GLN   A O   
2432 C CB  A GLN   A 107 ? 0.3047 0.3328 0.4021 -0.0641 -0.0098 -0.0770 107 GLN   A CB  
2433 C CB  B GLN   A 107 ? 0.3179 0.2688 0.3583 -0.0306 -0.0196 -0.0003 107 GLN   A CB  
2434 C CG  A GLN   A 107 ? 0.3415 0.3606 0.4858 -0.0609 -0.0164 -0.0677 107 GLN   A CG  
2435 C CG  B GLN   A 107 ? 0.3555 0.3081 0.4463 -0.0321 -0.0336 0.0137  107 GLN   A CG  
2436 C CD  A GLN   A 107 ? 0.3708 0.3809 0.5565 -0.0581 -0.0210 -0.0563 107 GLN   A CD  
2437 C CD  B GLN   A 107 ? 0.3849 0.3404 0.5247 -0.0322 -0.0432 0.0269  107 GLN   A CD  
2438 O OE1 A GLN   A 107 ? 0.3818 0.3893 0.5853 -0.0563 -0.0220 -0.0508 107 GLN   A OE1 
2439 O OE1 B GLN   A 107 ? 0.3945 0.3516 0.5508 -0.0308 -0.0461 0.0336  107 GLN   A OE1 
2440 N NE2 A GLN   A 107 ? 0.3803 0.3874 0.5794 -0.0579 -0.0241 -0.0548 107 GLN   A NE2 
2441 N NE2 B GLN   A 107 ? 0.3941 0.3495 0.5496 -0.0324 -0.0496 0.0310  107 GLN   A NE2 
2458 N N   A LEU   A 108 ? 0.2027 0.2247 0.2405 -0.0463 0.0262  -0.0498 108 LEU   A N   
2459 N N   B LEU   A 108 ? 0.2190 0.1710 0.2101 -0.0184 0.0204  0.0080  108 LEU   A N   
2460 C CA  A LEU   A 108 ? 0.1831 0.1942 0.2009 -0.0255 0.0258  -0.0189 108 LEU   A CA  
2461 C CA  B LEU   A 108 ? 0.1981 0.1594 0.1862 -0.0107 0.0254  0.0110  108 LEU   A CA  
2462 C C   A LEU   A 108 ? 0.1634 0.1610 0.1773 -0.0114 0.0202  0.0058  108 LEU   A C   
2463 C C   B LEU   A 108 ? 0.1710 0.1418 0.1705 -0.0024 0.0227  0.0213  108 LEU   A C   
2464 O O   A LEU   A 108 ? 0.1611 0.1611 0.1837 -0.0094 0.0240  0.0081  108 LEU   A O   
2465 O O   B LEU   A 108 ? 0.1696 0.1412 0.1826 0.0022  0.0341  0.0240  108 LEU   A O   
2466 C CB  A LEU   A 108 ? 0.1835 0.2039 0.1911 -0.0246 0.0328  -0.0134 108 LEU   A CB  
2467 C CB  B LEU   A 108 ? 0.2051 0.1744 0.1841 -0.0181 0.0329  0.0027  108 LEU   A CB  
2468 C CG  A LEU   A 108 ? 0.1934 0.2200 0.2036 -0.0175 0.0405  -0.0120 108 LEU   A CG  
2469 C CG  B LEU   A 108 ? 0.2201 0.1949 0.2032 -0.0165 0.0372  -0.0084 108 LEU   A CG  
2470 C CD1 A LEU   A 108 ? 0.2015 0.2226 0.2104 -0.0207 0.0461  -0.0123 108 LEU   A CD1 
2471 C CD1 B LEU   A 108 ? 0.2272 0.1999 0.2103 -0.0203 0.0438  -0.0095 108 LEU   A CD1 
2472 C CD2 A LEU   A 108 ? 0.1931 0.2331 0.2208 -0.0106 0.0495  -0.0104 108 LEU   A CD2 
2473 C CD2 B LEU   A 108 ? 0.2220 0.2086 0.2217 -0.0150 0.0413  -0.0152 108 LEU   A CD2 
2496 N N   . LEU   A 109 ? 0.1546 0.1434 0.1729 0.0006  0.0156  0.0187  109 LEU   A N   
2497 C CA  . LEU   A 109 ? 0.1495 0.1374 0.1589 -0.0004 0.0001  0.0213  109 LEU   A CA  
2498 C C   . LEU   A 109 ? 0.1354 0.1291 0.1649 -0.0080 0.0063  0.0089  109 LEU   A C   
2499 O O   . LEU   A 109 ? 0.1397 0.1228 0.1724 -0.0068 0.0025  0.0064  109 LEU   A O   
2500 C CB  . LEU   A 109 ? 0.1550 0.1452 0.1784 0.0072  -0.0058 0.0333  109 LEU   A CB  
2501 C CG  . LEU   A 109 ? 0.1469 0.1544 0.1949 0.0056  0.0022  0.0328  109 LEU   A CG  
2502 C CD1 . LEU   A 109 ? 0.1503 0.1472 0.2097 -0.0006 0.0108  0.0162  109 LEU   A CD1 
2503 C CD2 . LEU   A 109 ? 0.1416 0.1732 0.2213 0.0051  -0.0010 0.0386  109 LEU   A CD2 
2516 N N   . LYS   A 110 ? 0.1392 0.1273 0.1590 -0.0045 -0.0034 0.0063  110 LYS   A N   
2517 C CA  . LYS   A 110 ? 0.1342 0.1203 0.1734 -0.0139 -0.0028 0.0139  110 LYS   A CA  
2518 C C   . LYS   A 110 ? 0.1374 0.1139 0.1562 -0.0085 0.0002  0.0043  110 LYS   A C   
2519 O O   . LYS   A 110 ? 0.1299 0.1160 0.1670 -0.0022 0.0058  0.0024  110 LYS   A O   
2520 C CB  . LYS   A 110 ? 0.1424 0.1299 0.1993 -0.0132 -0.0044 0.0003  110 LYS   A CB  
2521 C CG  . LYS   A 110 ? 0.1373 0.1305 0.2041 -0.0067 -0.0047 -0.0014 110 LYS   A CG  
2522 C CD  . LYS   A 110 ? 0.1406 0.1322 0.2216 -0.0067 -0.0006 -0.0078 110 LYS   A CD  
2523 C CE  . LYS   A 110 ? 0.1526 0.1368 0.2351 -0.0095 0.0115  -0.0124 110 LYS   A CE  
2524 N NZ  . LYS   A 110 ? 0.1503 0.1408 0.2398 -0.0152 0.0178  -0.0035 110 LYS   A NZ  
2538 N N   . SER   A 111 ? 0.1359 0.1172 0.1515 -0.0056 -0.0025 0.0009  111 SER   A N   
2539 C CA  . SER   A 111 ? 0.1287 0.1261 0.1624 -0.0072 0.0033  0.0072  111 SER   A CA  
2540 C C   . SER   A 111 ? 0.1176 0.1210 0.1567 -0.0112 0.0054  0.0169  111 SER   A C   
2541 O O   . SER   A 111 ? 0.1341 0.1108 0.1714 -0.0053 0.0078  0.0123  111 SER   A O   
2542 C CB  . SER   A 111 ? 0.1435 0.1457 0.1761 -0.0070 0.0143  -0.0085 111 SER   A CB  
2543 O OG  . SER   A 111 ? 0.1876 0.1645 0.1838 -0.0006 0.0166  -0.0116 111 SER   A OG  
2549 N N   . ALA   A 112 ? 0.1250 0.1148 0.1543 -0.0036 0.0132  0.0133  112 ALA   A N   
2550 C CA  . ALA   A 112 ? 0.1301 0.1116 0.1482 -0.0064 0.0169  0.0054  112 ALA   A CA  
2551 C C   . ALA   A 112 ? 0.1242 0.1045 0.1512 -0.0013 0.0083  0.0067  112 ALA   A C   
2552 O O   . ALA   A 112 ? 0.1212 0.1067 0.1650 -0.0091 0.0116  0.0133  112 ALA   A O   
2553 C CB  . ALA   A 112 ? 0.1413 0.1162 0.1616 -0.0001 0.0097  0.0124  112 ALA   A CB  
2559 N N   . TYR   A 113 ? 0.1123 0.1091 0.1564 -0.0057 0.0076  0.0136  113 TYR   A N   
2560 C CA  . TYR   A 113 ? 0.1114 0.1097 0.1549 -0.0062 0.0069  0.0181  113 TYR   A CA  
2561 C C   . TYR   A 113 ? 0.1088 0.1123 0.1463 -0.0143 0.0064  0.0176  113 TYR   A C   
2562 O O   . TYR   A 113 ? 0.1133 0.1136 0.1573 -0.0062 0.0127  0.0131  113 TYR   A O   
2563 C CB  . TYR   A 113 ? 0.1109 0.1151 0.1617 -0.0049 -0.0034 0.0246  113 TYR   A CB  
2564 C CG  . TYR   A 113 ? 0.1160 0.1211 0.1488 -0.0122 0.0106  0.0262  113 TYR   A CG  
2565 C CD1 . TYR   A 113 ? 0.1162 0.1343 0.1589 0.0010  0.0076  0.0166  113 TYR   A CD1 
2566 C CD2 . TYR   A 113 ? 0.1219 0.1291 0.1559 -0.0121 0.0037  0.0230  113 TYR   A CD2 
2567 C CE1 . TYR   A 113 ? 0.1256 0.1413 0.1670 0.0032  0.0060  0.0176  113 TYR   A CE1 
2568 C CE2 . TYR   A 113 ? 0.1264 0.1402 0.1616 -0.0074 -0.0033 0.0272  113 TYR   A CE2 
2569 C CZ  . TYR   A 113 ? 0.1201 0.1420 0.1698 0.0044  0.0048  0.0243  113 TYR   A CZ  
2570 O OH  . TYR   A 113 ? 0.1256 0.1487 0.2008 0.0133  -0.0060 0.0230  113 TYR   A OH  
2580 N N   . GLU   A 114 ? 0.1101 0.1123 0.1550 -0.0030 0.0160  0.0168  114 GLU   A N   
2581 C CA  . GLU   A 114 ? 0.1158 0.1066 0.1734 0.0015  0.0105  0.0186  114 GLU   A CA  
2582 C C   . GLU   A 114 ? 0.1158 0.1084 0.1652 -0.0013 0.0142  0.0172  114 GLU   A C   
2583 O O   . GLU   A 114 ? 0.1264 0.1101 0.1606 -0.0032 0.0068  0.0185  114 GLU   A O   
2584 C CB  . GLU   A 114 ? 0.1128 0.1095 0.1857 -0.0046 0.0109  0.0151  114 GLU   A CB  
2585 C CG  . GLU   A 114 ? 0.1229 0.1097 0.1859 0.0014  0.0131  0.0058  114 GLU   A CG  
2586 C CD  . GLU   A 114 ? 0.1306 0.1078 0.1924 -0.0007 0.0047  0.0102  114 GLU   A CD  
2587 O OE1 . GLU   A 114 ? 0.1344 0.1186 0.1929 -0.0079 0.0115  -0.0001 114 GLU   A OE1 
2588 O OE2 . GLU   A 114 ? 0.1504 0.1197 0.2089 -0.0088 0.0097  -0.0090 114 GLU   A OE2 
2595 N N   . ASN   A 115 ? 0.1123 0.1143 0.1582 -0.0096 0.0101  0.0112  115 ASN   A N   
2596 C CA  . ASN   A 115 ? 0.1137 0.1154 0.1579 -0.0119 0.0113  0.0117  115 ASN   A CA  
2597 C C   . ASN   A 115 ? 0.1148 0.1115 0.1548 -0.0167 -0.0013 0.0084  115 ASN   A C   
2598 O O   . ASN   A 115 ? 0.1192 0.1227 0.1554 -0.0124 0.0090  0.0162  115 ASN   A O   
2599 C CB  . ASN   A 115 ? 0.1267 0.1227 0.1570 -0.0176 0.0097  0.0148  115 ASN   A CB  
2600 C CG  . ASN   A 115 ? 0.1219 0.1446 0.1655 -0.0170 0.0132  0.0203  115 ASN   A CG  
2601 O OD1 . ASN   A 115 ? 0.1305 0.2373 0.1870 -0.0141 0.0221  0.0339  115 ASN   A OD1 
2602 N ND2 . ASN   A 115 ? 0.1270 0.1251 0.1626 -0.0108 0.0157  0.0288  115 ASN   A ND2 
2609 N N   . PHE   A 116 ? 0.1094 0.1130 0.1599 -0.0046 0.0088  0.0226  116 PHE   A N   
2610 C CA  . PHE   A 116 ? 0.1105 0.1225 0.1510 -0.0016 0.0100  0.0208  116 PHE   A CA  
2611 C C   . PHE   A 116 ? 0.1134 0.1284 0.1580 -0.0086 0.0099  0.0202  116 PHE   A C   
2612 O O   . PHE   A 116 ? 0.1157 0.1282 0.1692 0.0043  0.0137  0.0310  116 PHE   A O   
2613 C CB  . PHE   A 116 ? 0.1184 0.1215 0.1568 -0.0060 0.0141  0.0206  116 PHE   A CB  
2614 C CG  . PHE   A 116 ? 0.1137 0.1134 0.1473 -0.0016 0.0083  0.0186  116 PHE   A CG  
2615 C CD1 . PHE   A 116 ? 0.1147 0.1167 0.1594 -0.0013 0.0102  0.0218  116 PHE   A CD1 
2616 C CD2 . PHE   A 116 ? 0.1235 0.1236 0.1639 0.0016  0.0158  0.0193  116 PHE   A CD2 
2617 C CE1 . PHE   A 116 ? 0.1192 0.1151 0.1672 -0.0136 0.0070  0.0139  116 PHE   A CE1 
2618 C CE2 . PHE   A 116 ? 0.1208 0.1124 0.1702 -0.0023 0.0155  0.0115  116 PHE   A CE2 
2619 C CZ  . PHE   A 116 ? 0.1217 0.1044 0.1637 0.0003  0.0074  0.0196  116 PHE   A CZ  
2629 N N   . ASN   A 117 ? 0.1156 0.1200 0.1660 -0.0072 0.0085  0.0249  117 ASN   A N   
2630 C CA  . ASN   A 117 ? 0.1142 0.1178 0.1781 -0.0040 0.0151  0.0280  117 ASN   A CA  
2631 C C   . ASN   A 117 ? 0.1181 0.1246 0.1844 -0.0011 0.0158  0.0282  117 ASN   A C   
2632 O O   . ASN   A 117 ? 0.1283 0.1346 0.1936 -0.0015 -0.0022 0.0427  117 ASN   A O   
2633 C CB  . ASN   A 117 ? 0.1210 0.1239 0.1695 -0.0028 0.0133  0.0343  117 ASN   A CB  
2634 C CG  . ASN   A 117 ? 0.1185 0.1187 0.1840 0.0014  0.0109  0.0271  117 ASN   A CG  
2635 O OD1 . ASN   A 117 ? 0.1179 0.1419 0.1915 -0.0090 0.0174  0.0195  117 ASN   A OD1 
2636 N ND2 . ASN   A 117 ? 0.1137 0.1132 0.1889 -0.0043 0.0104  0.0276  117 ASN   A ND2 
2643 N N   . GLN   A 118 ? 0.1159 0.1242 0.1875 0.0001  0.0045  0.0344  118 GLN   A N   
2644 C CA  . GLN   A 118 ? 0.1224 0.1361 0.1984 -0.0012 0.0003  0.0256  118 GLN   A CA  
2645 C C   . GLN   A 118 ? 0.1225 0.1471 0.1848 -0.0037 -0.0042 0.0329  118 GLN   A C   
2646 O O   . GLN   A 118 ? 0.1222 0.1723 0.2023 0.0016  -0.0129 0.0103  118 GLN   A O   
2647 C CB  . GLN   A 118 ? 0.1222 0.1355 0.2099 -0.0006 0.0146  0.0268  118 GLN   A CB  
2648 C CG  . GLN   A 118 ? 0.1198 0.1383 0.2040 -0.0027 0.0181  0.0318  118 GLN   A CG  
2649 C CD  . GLN   A 118 ? 0.1153 0.1465 0.2109 -0.0005 0.0095  0.0264  118 GLN   A CD  
2650 O OE1 . GLN   A 118 ? 0.1232 0.1614 0.2214 0.0069  -0.0012 0.0178  118 GLN   A OE1 
2651 N NE2 . GLN   A 118 ? 0.1232 0.1433 0.2058 0.0038  0.0087  0.0267  118 GLN   A NE2 
2660 N N   . HIS   A 119 ? 0.1267 0.1443 0.1737 0.0002  -0.0022 0.0372  119 HIS   A N   
2661 C CA  . HIS   A 119 ? 0.1335 0.1476 0.1648 -0.0028 0.0052  0.0386  119 HIS   A CA  
2662 C C   . HIS   A 119 ? 0.1403 0.1549 0.1670 -0.0048 0.0034  0.0417  119 HIS   A C   
2663 O O   . HIS   A 119 ? 0.1445 0.1589 0.1719 -0.0184 0.0020  0.0395  119 HIS   A O   
2664 C CB  . HIS   A 119 ? 0.1361 0.1439 0.1855 -0.0007 0.0152  0.0342  119 HIS   A CB  
2665 C CG  . HIS   A 119 ? 0.1405 0.1489 0.2270 0.0024  0.0176  0.0486  119 HIS   A CG  
2666 N ND1 . HIS   A 119 ? 0.1522 0.1676 0.2892 -0.0063 0.0120  0.0324  119 HIS   A ND1 
2667 C CD2 . HIS   A 119 ? 0.1538 0.1610 0.2462 0.0191  0.0349  0.0656  119 HIS   A CD2 
2668 C CE1 . HIS   A 119 ? 0.1540 0.1679 0.3009 -0.0114 0.0317  0.0563  119 HIS   A CE1 
2669 N NE2 . HIS   A 119 ? 0.1639 0.1662 0.2850 0.0056  0.0439  0.0802  119 HIS   A NE2 
2677 N N   . GLU   A 120 ? 0.1444 0.1722 0.1700 -0.0036 0.0009  0.0659  120 GLU   A N   
2678 C CA  . GLU   A 120 ? 0.1611 0.2048 0.1993 0.0078  -0.0045 0.0995  120 GLU   A CA  
2679 C C   . GLU   A 120 ? 0.1469 0.1924 0.1737 -0.0055 0.0003  0.0905  120 GLU   A C   
2680 O O   . GLU   A 120 ? 0.1483 0.1863 0.1838 -0.0097 -0.0016 0.0861  120 GLU   A O   
2681 C CB  . GLU   A 120 ? 0.2126 0.2621 0.2572 0.0243  -0.0095 0.1405  120 GLU   A CB  
2682 C CG  . GLU   A 120 ? 0.2864 0.3126 0.3678 0.0427  -0.0071 0.1472  120 GLU   A CG  
2683 C CD  . GLU   A 120 ? 0.3545 0.3565 0.4815 0.0589  0.0038  0.1413  120 GLU   A CD  
2684 O OE1 . GLU   A 120 ? 0.3785 0.3775 0.5129 0.0617  0.0078  0.1360  120 GLU   A OE1 
2685 O OE2 . GLU   A 120 ? 0.3826 0.3697 0.5276 0.0623  0.0082  0.1414  120 GLU   A OE2 
2692 N N   . VAL   A 121 ? 0.1421 0.1903 0.1571 -0.0034 0.0049  0.0701  121 VAL   A N   
2693 C CA  . VAL   A 121 ? 0.1526 0.1973 0.1434 -0.0044 0.0204  0.0698  121 VAL   A CA  
2694 C C   . VAL   A 121 ? 0.1407 0.1743 0.1289 -0.0167 0.0072  0.0520  121 VAL   A C   
2695 O O   . VAL   A 121 ? 0.1432 0.1779 0.1544 -0.0213 -0.0042 0.0381  121 VAL   A O   
2696 C CB  . VAL   A 121 ? 0.1951 0.2340 0.1879 0.0016  0.0316  0.0806  121 VAL   A CB  
2697 C CG1 . VAL   A 121 ? 0.1977 0.2483 0.1900 0.0121  0.0438  0.0857  121 VAL   A CG1 
2698 C CG2 . VAL   A 121 ? 0.2181 0.2529 0.2341 -0.0068 0.0258  0.0648  121 VAL   A CG2 
2708 N N   . LEU   A 122 ? 0.1289 0.1521 0.1423 -0.0158 0.0084  0.0473  122 LEU   A N   
2709 C CA  . LEU   A 122 ? 0.1397 0.1415 0.1415 -0.0197 0.0180  0.0417  122 LEU   A CA  
2710 C C   . LEU   A 122 ? 0.1296 0.1432 0.1343 -0.0178 0.0042  0.0398  122 LEU   A C   
2711 O O   . LEU   A 122 ? 0.1319 0.1448 0.1755 -0.0250 0.0018  0.0406  122 LEU   A O   
2712 C CB  . LEU   A 122 ? 0.1581 0.1415 0.1780 -0.0103 0.0138  0.0450  122 LEU   A CB  
2713 C CG  . LEU   A 122 ? 0.1598 0.1470 0.1693 -0.0074 0.0220  0.0366  122 LEU   A CG  
2714 C CD1 . LEU   A 122 ? 0.1743 0.1501 0.1824 -0.0093 0.0248  0.0337  122 LEU   A CD1 
2715 C CD2 . LEU   A 122 ? 0.1625 0.1399 0.1559 -0.0055 0.0300  0.0251  122 LEU   A CD2 
2727 N N   . LEU   A 123 ? 0.1247 0.1419 0.1329 -0.0187 0.0010  0.0349  123 LEU   A N   
2728 C CA  . LEU   A 123 ? 0.1230 0.1385 0.1299 -0.0161 0.0043  0.0379  123 LEU   A CA  
2729 C C   . LEU   A 123 ? 0.1214 0.1334 0.1194 -0.0095 -0.0004 0.0348  123 LEU   A C   
2730 O O   . LEU   A 123 ? 0.1178 0.1454 0.1416 -0.0266 0.0022  0.0357  123 LEU   A O   
2731 C CB  . LEU   A 123 ? 0.1345 0.1469 0.1279 -0.0180 0.0152  0.0327  123 LEU   A CB  
2732 C CG  . LEU   A 123 ? 0.1405 0.1625 0.1406 -0.0131 0.0153  0.0244  123 LEU   A CG  
2733 C CD1 . LEU   A 123 ? 0.1465 0.1689 0.1540 -0.0058 0.0113  0.0116  123 LEU   A CD1 
2734 C CD2 . LEU   A 123 ? 0.1459 0.1646 0.1556 -0.0112 0.0022  0.0211  123 LEU   A CD2 
2746 N N   A ALA   A 124 ? 0.1229 0.1298 0.1185 -0.0150 0.0014  0.0341  124 ALA   A N   
2747 N N   B ALA   A 124 ? 0.1185 0.1339 0.1153 -0.0064 0.0002  0.0286  124 ALA   A N   
2748 C CA  A ALA   A 124 ? 0.1219 0.1231 0.1275 -0.0173 0.0032  0.0319  124 ALA   A CA  
2749 C CA  B ALA   A 124 ? 0.1144 0.1331 0.1221 -0.0011 -0.0006 0.0269  124 ALA   A CA  
2750 C C   A ALA   A 124 ? 0.1123 0.1176 0.1368 -0.0217 0.0024  0.0269  124 ALA   A C   
2751 C C   B ALA   A 124 ? 0.1067 0.1284 0.1194 -0.0034 0.0041  0.0285  124 ALA   A C   
2752 O O   A ALA   A 124 ? 0.1132 0.1164 0.1565 -0.0238 0.0081  0.0277  124 ALA   A O   
2753 O O   B ALA   A 124 ? 0.1131 0.1408 0.1305 -0.0053 0.0147  0.0361  124 ALA   A O   
2754 C CB  A ALA   A 124 ? 0.1237 0.1234 0.1401 -0.0215 0.0069  0.0331  124 ALA   A CB  
2755 C CB  B ALA   A 124 ? 0.1090 0.1351 0.1402 0.0056  -0.0050 0.0262  124 ALA   A CB  
2766 N N   A PRO   A 125 ? 0.1125 0.1258 0.1385 -0.0135 0.0040  0.0289  125 PRO   A N   
2767 N N   B PRO   A 125 ? 0.1071 0.1207 0.1153 -0.0014 0.0011  0.0347  125 PRO   A N   
2768 C CA  A PRO   A 125 ? 0.1139 0.1211 0.1383 -0.0115 0.0025  0.0195  125 PRO   A CA  
2769 C CA  B PRO   A 125 ? 0.1158 0.1237 0.1292 -0.0034 -0.0015 0.0243  125 PRO   A CA  
2770 C C   A PRO   A 125 ? 0.1041 0.1170 0.1396 -0.0110 0.0049  0.0216  125 PRO   A C   
2771 C C   B PRO   A 125 ? 0.1158 0.1350 0.1434 -0.0048 -0.0039 0.0227  125 PRO   A C   
2772 O O   A PRO   A 125 ? 0.1059 0.1137 0.1561 -0.0075 0.0018  0.0163  125 PRO   A O   
2773 O O   B PRO   A 125 ? 0.1261 0.1353 0.1586 -0.0013 0.0021  0.0186  125 PRO   A O   
2774 C CB  A PRO   A 125 ? 0.1285 0.1248 0.1395 -0.0151 -0.0000 0.0195  125 PRO   A CB  
2775 C CB  B PRO   A 125 ? 0.1261 0.1181 0.1221 -0.0079 -0.0001 0.0268  125 PRO   A CB  
2776 C CG  A PRO   A 125 ? 0.1275 0.1344 0.1462 -0.0174 0.0031  0.0237  125 PRO   A CG  
2777 C CG  B PRO   A 125 ? 0.1207 0.1184 0.1266 -0.0108 0.0025  0.0288  125 PRO   A CG  
2778 C CD  A PRO   A 125 ? 0.1159 0.1354 0.1474 -0.0164 0.0099  0.0255  125 PRO   A CD  
2779 C CD  B PRO   A 125 ? 0.1060 0.1069 0.1141 -0.0090 0.0058  0.0289  125 PRO   A CD  
2794 N N   A LEU   A 126 ? 0.1024 0.1260 0.1409 -0.0070 0.0039  0.0156  126 LEU   A N   
2795 N N   B LEU   A 126 ? 0.1180 0.1538 0.1579 -0.0078 -0.0063 0.0150  126 LEU   A N   
2796 C CA  A LEU   A 126 ? 0.1159 0.1257 0.1535 -0.0101 0.0009  0.0153  126 LEU   A CA  
2797 C CA  B LEU   A 126 ? 0.1299 0.1449 0.1661 -0.0147 -0.0056 0.0209  126 LEU   A CA  
2798 C C   A LEU   A 126 ? 0.1311 0.1223 0.1726 -0.0060 -0.0038 0.0025  126 LEU   A C   
2799 C C   B LEU   A 126 ? 0.1338 0.1289 0.1626 -0.0004 0.0055  0.0155  126 LEU   A C   
2800 O O   A LEU   A 126 ? 0.1417 0.1154 0.1919 -0.0076 0.0065  -0.0101 126 LEU   A O   
2801 O O   B LEU   A 126 ? 0.1532 0.1190 0.1993 -0.0112 0.0419  0.0147  126 LEU   A O   
2802 C CB  A LEU   A 126 ? 0.1273 0.1306 0.1580 -0.0128 -0.0076 0.0135  126 LEU   A CB  
2803 C CB  B LEU   A 126 ? 0.1462 0.1619 0.1822 -0.0241 -0.0084 0.0304  126 LEU   A CB  
2804 C CG  A LEU   A 126 ? 0.1269 0.1489 0.1693 -0.0146 -0.0111 0.0209  126 LEU   A CG  
2805 C CG  B LEU   A 126 ? 0.1488 0.1700 0.1995 -0.0224 -0.0143 0.0453  126 LEU   A CG  
2806 C CD1 A LEU   A 126 ? 0.1274 0.1586 0.1824 -0.0162 -0.0170 0.0283  126 LEU   A CD1 
2807 C CD1 B LEU   A 126 ? 0.1468 0.1796 0.2123 -0.0205 -0.0305 0.0478  126 LEU   A CD1 
2808 C CD2 A LEU   A 126 ? 0.1376 0.1462 0.1588 -0.0206 -0.0133 0.0304  126 LEU   A CD2 
2809 C CD2 B LEU   A 126 ? 0.1587 0.1701 0.2126 -0.0253 -0.0070 0.0455  126 LEU   A CD2 
2832 N N   A LEU   A 127 ? 0.1313 0.1404 0.1714 -0.0050 -0.0005 0.0044  127 LEU   A N   
2833 N N   B LEU   A 127 ? 0.1192 0.1377 0.1373 0.0080  -0.0020 0.0318  127 LEU   A N   
2834 C CA  A LEU   A 127 ? 0.1346 0.1444 0.1557 -0.0055 0.0039  0.0032  127 LEU   A CA  
2835 C CA  B LEU   A 127 ? 0.1221 0.1464 0.1441 0.0044  0.0026  0.0324  127 LEU   A CA  
2836 C C   A LEU   A 127 ? 0.1319 0.1364 0.1393 -0.0091 0.0093  0.0081  127 LEU   A C   
2837 C C   B LEU   A 127 ? 0.1241 0.1499 0.1578 0.0009  -0.0085 0.0335  127 LEU   A C   
2838 O O   A LEU   A 127 ? 0.1377 0.1445 0.1352 -0.0203 0.0198  0.0079  127 LEU   A O   
2839 O O   B LEU   A 127 ? 0.1296 0.1519 0.1640 -0.0133 -0.0144 0.0383  127 LEU   A O   
2840 C CB  A LEU   A 127 ? 0.1361 0.1502 0.1514 0.0017  0.0023  0.0055  127 LEU   A CB  
2841 C CB  B LEU   A 127 ? 0.1177 0.1557 0.1461 0.0013  0.0053  0.0262  127 LEU   A CB  
2842 C CG  A LEU   A 127 ? 0.1432 0.1495 0.1539 0.0037  0.0021  0.0182  127 LEU   A CG  
2843 C CG  B LEU   A 127 ? 0.1235 0.1724 0.1600 0.0015  0.0020  0.0274  127 LEU   A CG  
2844 C CD1 A LEU   A 127 ? 0.1467 0.1469 0.1607 -0.0038 0.0044  0.0185  127 LEU   A CD1 
2845 C CD1 B LEU   A 127 ? 0.1218 0.1802 0.1790 0.0075  0.0052  0.0299  127 LEU   A CD1 
2846 C CD2 A LEU   A 127 ? 0.1489 0.1501 0.1763 0.0072  -0.0058 0.0250  127 LEU   A CD2 
2847 C CD2 B LEU   A 127 ? 0.1409 0.1825 0.1679 0.0011  -0.0125 0.0183  127 LEU   A CD2 
2870 N N   A SER   A 128 ? 0.1363 0.1310 0.1498 -0.0117 0.0044  0.0089  128 SER   A N   
2871 N N   B SER   A 128 ? 0.1360 0.1572 0.1649 0.0043  -0.0087 0.0328  128 SER   A N   
2872 C CA  A SER   A 128 ? 0.1426 0.1392 0.1362 -0.0097 -0.0003 0.0066  128 SER   A CA  
2873 C CA  B SER   A 128 ? 0.1522 0.1767 0.1665 0.0121  -0.0095 0.0258  128 SER   A CA  
2874 C C   A SER   A 128 ? 0.1434 0.1322 0.1280 -0.0057 -0.0049 0.0122  128 SER   A C   
2875 C C   B SER   A 128 ? 0.1730 0.1931 0.1724 0.0145  -0.0163 0.0288  128 SER   A C   
2876 O O   A SER   A 128 ? 0.1523 0.1427 0.1282 0.0048  0.0002  0.0160  128 SER   A O   
2877 O O   B SER   A 128 ? 0.1728 0.1989 0.1733 0.0064  -0.0159 0.0259  128 SER   A O   
2878 C CB  A SER   A 128 ? 0.1478 0.1392 0.1316 -0.0183 -0.0079 0.0115  128 SER   A CB  
2879 C CB  B SER   A 128 ? 0.1479 0.1723 0.1548 0.0073  -0.0135 0.0300  128 SER   A CB  
2880 O OG  A SER   A 128 ? 0.1409 0.1337 0.1354 -0.0142 -0.0064 0.0075  128 SER   A OG  
2881 O OG  B SER   A 128 ? 0.1354 0.1644 0.1543 0.0082  -0.0026 0.0223  128 SER   A OG  
2892 N N   A ALA   A 129 ? 0.1327 0.1310 0.1420 -0.0029 -0.0094 0.0219  129 ALA   A N   
2893 N N   B ALA   A 129 ? 0.1943 0.2135 0.1735 0.0308  -0.0233 0.0458  129 ALA   A N   
2894 C CA  A ALA   A 129 ? 0.1320 0.1267 0.1626 -0.0021 -0.0126 0.0279  129 ALA   A CA  
2895 C CA  B ALA   A 129 ? 0.2249 0.2335 0.1880 0.0317  -0.0308 0.0347  129 ALA   A CA  
2896 C C   A ALA   A 129 ? 0.1345 0.1245 0.1584 0.0029  -0.0152 0.0112  129 ALA   A C   
2897 C C   B ALA   A 129 ? 0.2620 0.2558 0.2119 0.0348  -0.0376 0.0292  129 ALA   A C   
2898 O O   A ALA   A 129 ? 0.1487 0.1282 0.1874 -0.0096 -0.0124 0.0119  129 ALA   A O   
2899 O O   B ALA   A 129 ? 0.2664 0.2593 0.2092 0.0321  -0.0443 0.0280  129 ALA   A O   
2900 C CB  A ALA   A 129 ? 0.1380 0.1406 0.1974 0.0040  -0.0054 0.0441  129 ALA   A CB  
2901 C CB  B ALA   A 129 ? 0.2285 0.2414 0.2036 0.0214  -0.0229 0.0226  129 ALA   A CB  
2912 N N   A GLY   A 130 ? 0.1420 0.1169 0.1601 0.0088  -0.0014 0.0138  130 GLY   A N   
2913 N N   B GLY   A 130 ? 0.2913 0.2729 0.2472 0.0386  -0.0355 0.0159  130 GLY   A N   
2914 C CA  A GLY   A 130 ? 0.1632 0.1197 0.1736 0.0070  -0.0043 0.0187  130 GLY   A CA  
2915 C CA  B GLY   A 130 ? 0.3097 0.2842 0.2654 0.0419  -0.0355 0.0046  130 GLY   A CA  
2916 C C   A GLY   A 130 ? 0.1697 0.1176 0.1768 0.0019  -0.0115 0.0236  130 GLY   A C   
2917 C C   B GLY   A 130 ? 0.3216 0.2927 0.2786 0.0440  -0.0394 -0.0051 130 GLY   A C   
2918 O O   A GLY   A 130 ? 0.1618 0.1148 0.1704 0.0036  -0.0115 0.0239  130 GLY   A O   
2919 O O   B GLY   A 130 ? 0.3278 0.2974 0.2783 0.0468  -0.0390 -0.0111 130 GLY   A O   
2926 N N   A ILE   A 131 ? 0.1862 0.1185 0.1753 -0.0033 -0.0195 0.0292  131 ILE   A N   
2927 N N   B ILE   A 131 ? 0.3253 0.2930 0.2995 0.0438  -0.0432 -0.0086 131 ILE   A N   
2928 C CA  A ILE   A 131 ? 0.1927 0.1186 0.1554 -0.0090 -0.0365 0.0275  131 ILE   A CA  
2929 C CA  B ILE   A 131 ? 0.3233 0.2887 0.3075 0.0418  -0.0475 -0.0041 131 ILE   A CA  
2930 C C   A ILE   A 131 ? 0.1739 0.1285 0.1490 -0.0112 -0.0326 0.0281  131 ILE   A C   
2931 C C   B ILE   A 131 ? 0.3165 0.2847 0.3039 0.0366  -0.0408 0.0136  131 ILE   A C   
2932 O O   A ILE   A 131 ? 0.1674 0.1337 0.1545 -0.0097 -0.0356 0.0198  131 ILE   A O   
2933 O O   B ILE   A 131 ? 0.3263 0.2898 0.3075 0.0329  -0.0313 0.0181  131 ILE   A O   
2934 C CB  A ILE   A 131 ? 0.2162 0.1279 0.1724 -0.0071 -0.0367 0.0065  131 ILE   A CB  
2935 C CB  B ILE   A 131 ? 0.3281 0.2929 0.3209 0.0442  -0.0562 -0.0199 131 ILE   A CB  
2936 C CG1 A ILE   A 131 ? 0.2296 0.1589 0.2000 -0.0148 -0.0424 -0.0083 131 ILE   A CG1 
2937 C CG1 B ILE   A 131 ? 0.3323 0.2978 0.3274 0.0441  -0.0612 -0.0309 131 ILE   A CG1 
2938 C CG2 A ILE   A 131 ? 0.2242 0.1217 0.1908 -0.0007 -0.0250 0.0079  131 ILE   A CG2 
2939 C CG2 B ILE   A 131 ? 0.3288 0.2947 0.3270 0.0452  -0.0551 -0.0196 131 ILE   A CG2 
2940 C CD1 A ILE   A 131 ? 0.2369 0.1679 0.2242 -0.0123 -0.0434 -0.0119 131 ILE   A CD1 
2941 C CD1 B ILE   A 131 ? 0.3366 0.3012 0.3322 0.0414  -0.0611 -0.0387 131 ILE   A CD1 
2964 N N   A PHE   A 132 ? 0.1692 0.1228 0.1563 -0.0118 -0.0281 0.0329  132 PHE   A N   
2965 N N   B PHE   A 132 ? 0.2956 0.2712 0.2885 0.0367  -0.0480 0.0298  132 PHE   A N   
2966 C CA  A PHE   A 132 ? 0.1720 0.1357 0.1605 -0.0150 -0.0233 0.0122  132 PHE   A CA  
2967 C CA  B PHE   A 132 ? 0.2753 0.2652 0.2818 0.0285  -0.0535 0.0397  132 PHE   A CA  
2968 C C   A PHE   A 132 ? 0.1753 0.1493 0.1745 -0.0175 -0.0344 0.0145  132 PHE   A C   
2969 C C   B PHE   A 132 ? 0.2625 0.2551 0.2673 0.0292  -0.0560 0.0477  132 PHE   A C   
2970 O O   A PHE   A 132 ? 0.1869 0.1625 0.1895 -0.0262 -0.0279 0.0174  132 PHE   A O   
2971 O O   B PHE   A 132 ? 0.2676 0.2623 0.2684 0.0286  -0.0494 0.0501  132 PHE   A O   
2972 C CB  A PHE   A 132 ? 0.1684 0.1280 0.1369 -0.0102 -0.0302 0.0184  132 PHE   A CB  
2973 C CB  B PHE   A 132 ? 0.2664 0.2671 0.2813 0.0234  -0.0564 0.0487  132 PHE   A CB  
2974 C CG  A PHE   A 132 ? 0.1622 0.1224 0.1099 -0.0039 -0.0286 0.0125  132 PHE   A CG  
2975 C CG  B PHE   A 132 ? 0.2652 0.2735 0.3002 0.0186  -0.0523 0.0425  132 PHE   A CG  
2976 C CD1 A PHE   A 132 ? 0.1577 0.1262 0.1142 0.0099  -0.0175 0.0043  132 PHE   A CD1 
2977 C CD1 B PHE   A 132 ? 0.2686 0.2794 0.3184 0.0163  -0.0479 0.0354  132 PHE   A CD1 
2978 C CD2 A PHE   A 132 ? 0.1617 0.1343 0.1181 -0.0012 -0.0267 0.0053  132 PHE   A CD2 
2979 C CD2 B PHE   A 132 ? 0.2641 0.2810 0.3155 0.0174  -0.0465 0.0358  132 PHE   A CD2 
2980 C CE1 A PHE   A 132 ? 0.1529 0.1373 0.1143 0.0084  -0.0268 0.0001  132 PHE   A CE1 
2981 C CE1 B PHE   A 132 ? 0.2667 0.2817 0.3313 0.0136  -0.0472 0.0298  132 PHE   A CE1 
2982 C CE2 A PHE   A 132 ? 0.1522 0.1354 0.1158 0.0044  -0.0247 0.0042  132 PHE   A CE2 
2983 C CE2 B PHE   A 132 ? 0.2652 0.2848 0.3343 0.0146  -0.0452 0.0287  132 PHE   A CE2 
2984 C CZ  A PHE   A 132 ? 0.1461 0.1348 0.1070 -0.0003 -0.0236 0.0060  132 PHE   A CZ  
2985 C CZ  B PHE   A 132 ? 0.2653 0.2847 0.3397 0.0126  -0.0480 0.0277  132 PHE   A CZ  
3004 N N   A GLY   A 133 ? 0.1758 0.1590 0.1771 -0.0179 -0.0415 0.0161  133 GLY   A N   
3005 N N   B GLY   A 133 ? 0.2495 0.2394 0.2511 0.0241  -0.0601 0.0498  133 GLY   A N   
3006 C CA  A GLY   A 133 ? 0.1806 0.1768 0.1856 -0.0206 -0.0503 0.0080  133 GLY   A CA  
3007 C CA  B GLY   A 133 ? 0.2413 0.2296 0.2414 0.0155  -0.0665 0.0388  133 GLY   A CA  
3008 C C   A GLY   A 133 ? 0.1803 0.1887 0.1954 -0.0249 -0.0574 -0.0001 133 GLY   A C   
3009 C C   B GLY   A 133 ? 0.2340 0.2219 0.2401 0.0066  -0.0705 0.0188  133 GLY   A C   
3010 O O   A GLY   A 133 ? 0.1861 0.2030 0.2138 -0.0221 -0.0571 -0.0138 133 GLY   A O   
3011 O O   B GLY   A 133 ? 0.2318 0.2319 0.2430 0.0089  -0.0751 -0.0009 133 GLY   A O   
3018 N N   A ALA   A 134 ? 0.1775 0.1834 0.1977 -0.0292 -0.0444 0.0069  134 ALA   A N   
3019 N N   B ALA   A 134 ? 0.2302 0.2015 0.2446 -0.0015 -0.0569 0.0180  134 ALA   A N   
3020 C CA  A ALA   A 134 ? 0.1772 0.1855 0.2207 -0.0272 -0.0397 0.0162  134 ALA   A CA  
3021 C CA  B ALA   A 134 ? 0.2302 0.1889 0.2460 -0.0083 -0.0541 0.0196  134 ALA   A CA  
3022 C C   A ALA   A 134 ? 0.1774 0.1970 0.2348 -0.0293 -0.0345 0.0301  134 ALA   A C   
3023 C C   B ALA   A 134 ? 0.2296 0.1799 0.2448 -0.0146 -0.0479 0.0291  134 ALA   A C   
3024 O O   A ALA   A 134 ? 0.1852 0.2040 0.2592 -0.0300 -0.0215 0.0369  134 ALA   A O   
3025 O O   B ALA   A 134 ? 0.2320 0.1751 0.2630 -0.0273 -0.0355 0.0367  134 ALA   A O   
3026 C CB  A ALA   A 134 ? 0.1831 0.1818 0.2286 -0.0239 -0.0350 0.0131  134 ALA   A CB  
3027 C CB  B ALA   A 134 ? 0.2329 0.1877 0.2547 -0.0073 -0.0576 0.0131  134 ALA   A CB  
3038 N N   A ASP   A 135 ? 0.1803 0.2018 0.2309 -0.0334 -0.0365 0.0416  135 ASP   A N   
3039 N N   B ASP   A 135 ? 0.2329 0.1815 0.2380 -0.0126 -0.0492 0.0337  135 ASP   A N   
3040 C CA  A ASP   A 135 ? 0.1768 0.2084 0.2326 -0.0394 -0.0473 0.0513  135 ASP   A CA  
3041 C CA  B ASP   A 135 ? 0.2295 0.1906 0.2475 -0.0148 -0.0533 0.0320  135 ASP   A CA  
3042 C C   A ASP   A 135 ? 0.1600 0.1948 0.2263 -0.0266 -0.0430 0.0653  135 ASP   A C   
3043 C C   B ASP   A 135 ? 0.2105 0.1836 0.2344 -0.0097 -0.0462 0.0440  135 ASP   A C   
3044 O O   A ASP   A 135 ? 0.1494 0.1895 0.2193 -0.0336 -0.0482 0.0638  135 ASP   A O   
3045 O O   B ASP   A 135 ? 0.2069 0.1777 0.2341 -0.0187 -0.0405 0.0447  135 ASP   A O   
3046 C CB  A ASP   A 135 ? 0.1900 0.2236 0.2479 -0.0528 -0.0561 0.0382  135 ASP   A CB  
3047 C CB  B ASP   A 135 ? 0.2454 0.2083 0.2763 -0.0213 -0.0542 0.0245  135 ASP   A CB  
3048 C CG  A ASP   A 135 ? 0.2003 0.2349 0.2730 -0.0663 -0.0571 0.0216  135 ASP   A CG  
3049 C CG  B ASP   A 135 ? 0.2620 0.2276 0.3149 -0.0224 -0.0486 0.0117  135 ASP   A CG  
3050 O OD1 A ASP   A 135 ? 0.1920 0.2330 0.2789 -0.0729 -0.0718 0.0282  135 ASP   A OD1 
3051 O OD1 B ASP   A 135 ? 0.2684 0.2327 0.3350 -0.0238 -0.0467 0.0046  135 ASP   A OD1 
3052 O OD2 A ASP   A 135 ? 0.2269 0.2468 0.3080 -0.0598 -0.0308 0.0130  135 ASP   A OD2 
3053 O OD2 B ASP   A 135 ? 0.2710 0.2379 0.3376 -0.0228 -0.0449 0.0105  135 ASP   A OD2 
3062 N N   A PRO   A 136 ? 0.1496 0.1877 0.2428 -0.0084 -0.0233 0.0757  136 PRO   A N   
3063 N N   B PRO   A 136 ? 0.1924 0.1788 0.2413 -0.0003 -0.0335 0.0517  136 PRO   A N   
3064 C CA  A PRO   A 136 ? 0.1410 0.1817 0.2478 -0.0058 -0.0151 0.0626  136 PRO   A CA  
3065 C CA  B PRO   A 136 ? 0.1826 0.1829 0.2391 -0.0028 -0.0252 0.0481  136 PRO   A CA  
3066 C C   A PRO   A 136 ? 0.1188 0.1755 0.2389 -0.0056 -0.0131 0.0537  136 PRO   A C   
3067 C C   B PRO   A 136 ? 0.1641 0.1871 0.2293 -0.0040 -0.0258 0.0476  136 PRO   A C   
3068 O O   A PRO   A 136 ? 0.1105 0.1713 0.2333 -0.0095 -0.0058 0.0453  136 PRO   A O   
3069 O O   B PRO   A 136 ? 0.1563 0.1802 0.2139 -0.0013 -0.0209 0.0499  136 PRO   A O   
3070 C CB  A PRO   A 136 ? 0.1578 0.1817 0.2634 -0.0059 -0.0057 0.0636  136 PRO   A CB  
3071 C CB  B PRO   A 136 ? 0.1920 0.1790 0.2452 -0.0002 -0.0254 0.0509  136 PRO   A CB  
3072 C CG  A PRO   A 136 ? 0.1647 0.1852 0.2731 -0.0104 -0.0086 0.0668  136 PRO   A CG  
3073 C CG  B PRO   A 136 ? 0.1975 0.1791 0.2585 -0.0008 -0.0306 0.0477  136 PRO   A CG  
3074 C CD  A PRO   A 136 ? 0.1599 0.1864 0.2581 -0.0053 -0.0159 0.0784  136 PRO   A CD  
3075 C CD  B PRO   A 136 ? 0.1924 0.1756 0.2537 -0.0009 -0.0293 0.0552  136 PRO   A CD  
3090 N N   A ILE   A 137 ? 0.1173 0.1836 0.2375 -0.0095 -0.0201 0.0556  137 ILE   A N   
3091 N N   B ILE   A 137 ? 0.1643 0.1968 0.2366 -0.0147 -0.0271 0.0423  137 ILE   A N   
3092 C CA  A ILE   A 137 ? 0.1196 0.1952 0.2222 -0.0173 -0.0292 0.0610  137 ILE   A CA  
3093 C CA  B ILE   A 137 ? 0.1727 0.2114 0.2418 -0.0183 -0.0345 0.0392  137 ILE   A CA  
3094 C C   A ILE   A 137 ? 0.1213 0.1898 0.1973 -0.0237 -0.0338 0.0581  137 ILE   A C   
3095 C C   B ILE   A 137 ? 0.1669 0.2146 0.2370 -0.0212 -0.0349 0.0303  137 ILE   A C   
3096 O O   A ILE   A 137 ? 0.1236 0.1781 0.1982 -0.0315 -0.0239 0.0451  137 ILE   A O   
3097 O O   B ILE   A 137 ? 0.1635 0.2130 0.2457 -0.0236 -0.0338 0.0252  137 ILE   A O   
3098 C CB  A ILE   A 137 ? 0.1246 0.2137 0.2338 -0.0187 -0.0435 0.0733  137 ILE   A CB  
3099 C CB  B ILE   A 137 ? 0.1895 0.2214 0.2561 -0.0234 -0.0449 0.0493  137 ILE   A CB  
3100 C CG1 A ILE   A 137 ? 0.1403 0.2297 0.2442 -0.0166 -0.0342 0.0830  137 ILE   A CG1 
3101 C CG1 B ILE   A 137 ? 0.2016 0.2357 0.2667 -0.0131 -0.0491 0.0634  137 ILE   A CG1 
3102 C CG2 A ILE   A 137 ? 0.1307 0.2170 0.2472 -0.0146 -0.0479 0.0670  137 ILE   A CG2 
3103 C CG2 B ILE   A 137 ? 0.1998 0.2188 0.2648 -0.0256 -0.0427 0.0448  137 ILE   A CG2 
3104 C CD1 A ILE   A 137 ? 0.1556 0.2384 0.2533 -0.0136 -0.0277 0.0856  137 ILE   A CD1 
3105 C CD1 B ILE   A 137 ? 0.2088 0.2427 0.2808 -0.0120 -0.0452 0.0688  137 ILE   A CD1 
3128 N N   A HIS   A 138 ? 0.1291 0.2011 0.1997 -0.0182 -0.0244 0.0574  138 HIS   A N   
3129 N N   B HIS   A 138 ? 0.1668 0.2242 0.2359 -0.0191 -0.0234 0.0232  138 HIS   A N   
3130 C CA  A HIS   A 138 ? 0.1392 0.2113 0.1949 -0.0190 -0.0207 0.0509  138 HIS   A CA  
3131 C CA  B HIS   A 138 ? 0.1626 0.2260 0.2165 -0.0232 -0.0189 0.0264  138 HIS   A CA  
3132 C C   A HIS   A 138 ? 0.1346 0.2003 0.1938 -0.0162 -0.0142 0.0483  138 HIS   A C   
3133 C C   B HIS   A 138 ? 0.1486 0.2090 0.2047 -0.0177 -0.0127 0.0364  138 HIS   A C   
3134 O O   A HIS   A 138 ? 0.1404 0.1945 0.1943 -0.0181 -0.0093 0.0473  138 HIS   A O   
3135 O O   B HIS   A 138 ? 0.1576 0.2061 0.2052 -0.0188 -0.0064 0.0355  138 HIS   A O   
3136 C CB  A HIS   A 138 ? 0.1590 0.2287 0.1882 -0.0197 -0.0292 0.0431  138 HIS   A CB  
3137 C CB  B HIS   A 138 ? 0.1762 0.2426 0.2066 -0.0287 -0.0271 0.0145  138 HIS   A CB  
3138 C CG  A HIS   A 138 ? 0.1812 0.2376 0.1965 -0.0243 -0.0206 0.0354  138 HIS   A CG  
3139 C CG  B HIS   A 138 ? 0.1906 0.2528 0.2090 -0.0366 -0.0198 0.0012  138 HIS   A CG  
3140 N ND1 A HIS   A 138 ? 0.1940 0.2449 0.2080 -0.0244 -0.0135 0.0225  138 HIS   A ND1 
3141 N ND1 B HIS   A 138 ? 0.1993 0.2601 0.2193 -0.0372 -0.0132 -0.0127 138 HIS   A ND1 
3142 C CD2 A HIS   A 138 ? 0.1906 0.2437 0.1994 -0.0226 -0.0224 0.0319  138 HIS   A CD2 
3143 C CD2 B HIS   A 138 ? 0.1961 0.2581 0.2070 -0.0365 -0.0233 -0.0043 138 HIS   A CD2 
3144 C CE1 A HIS   A 138 ? 0.1997 0.2492 0.2129 -0.0200 -0.0136 0.0199  138 HIS   A CE1 
3145 C CE1 B HIS   A 138 ? 0.2025 0.2622 0.2199 -0.0345 -0.0145 -0.0154 138 HIS   A CE1 
3146 N NE2 A HIS   A 138 ? 0.1952 0.2491 0.2015 -0.0191 -0.0160 0.0256  138 HIS   A NE2 
3147 N NE2 B HIS   A 138 ? 0.1981 0.2626 0.2075 -0.0347 -0.0189 -0.0116 138 HIS   A NE2 
3162 N N   . SER   A 139 ? 0.1282 0.1939 0.1976 -0.0117 -0.0111 0.0444  139 SER   A N   
3163 C CA  . SER   A 139 ? 0.1285 0.1810 0.1969 -0.0136 -0.0082 0.0502  139 SER   A CA  
3164 C C   . SER   A 139 ? 0.1198 0.1600 0.1938 -0.0148 -0.0033 0.0433  139 SER   A C   
3165 O O   . SER   A 139 ? 0.1198 0.1541 0.1946 -0.0054 -0.0069 0.0414  139 SER   A O   
3166 C CB  . SER   A 139 ? 0.1289 0.1759 0.1976 -0.0132 -0.0075 0.0533  139 SER   A CB  
3167 O OG  . SER   A 139 ? 0.1322 0.1683 0.2010 -0.0133 -0.0174 0.0531  139 SER   A OG  
3174 N N   . LEU   A 140 ? 0.1188 0.1674 0.1818 -0.0098 -0.0075 0.0435  140 LEU   A N   
3175 C CA  . LEU   A 140 ? 0.1176 0.1551 0.1884 -0.0088 -0.0074 0.0402  140 LEU   A CA  
3176 C C   . LEU   A 140 ? 0.1163 0.1609 0.1789 -0.0155 -0.0008 0.0369  140 LEU   A C   
3177 O O   . LEU   A 140 ? 0.1201 0.1578 0.1959 -0.0091 -0.0050 0.0374  140 LEU   A O   
3178 C CB  . LEU   A 140 ? 0.1185 0.1611 0.1891 -0.0098 -0.0062 0.0423  140 LEU   A CB  
3179 C CG  . LEU   A 140 ? 0.1206 0.1729 0.1917 -0.0236 0.0002  0.0489  140 LEU   A CG  
3180 C CD1 . LEU   A 140 ? 0.1264 0.1730 0.2067 -0.0188 -0.0029 0.0516  140 LEU   A CD1 
3181 C CD2 . LEU   A 140 ? 0.1343 0.1891 0.1979 -0.0191 0.0047  0.0468  140 LEU   A CD2 
3193 N N   . ARG   A 141 ? 0.1246 0.1668 0.1821 -0.0185 -0.0160 0.0309  141 ARG   A N   
3194 C CA  . ARG   A 141 ? 0.1370 0.1826 0.1997 -0.0310 -0.0177 0.0150  141 ARG   A CA  
3195 C C   . ARG   A 141 ? 0.1374 0.1678 0.1884 -0.0244 -0.0089 0.0175  141 ARG   A C   
3196 O O   . ARG   A 141 ? 0.1342 0.1660 0.2020 -0.0254 -0.0007 0.0157  141 ARG   A O   
3197 C CB  . ARG   A 141 ? 0.1549 0.2161 0.2325 -0.0395 -0.0242 -0.0112 141 ARG   A CB  
3198 C CG  . ARG   A 141 ? 0.1941 0.2529 0.2693 -0.0462 -0.0121 -0.0203 141 ARG   A CG  
3199 C CD  . ARG   A 141 ? 0.2235 0.2872 0.3040 -0.0543 -0.0104 -0.0256 141 ARG   A CD  
3200 N NE  . ARG   A 141 ? 0.2163 0.3154 0.3221 -0.0612 -0.0126 -0.0260 141 ARG   A NE  
3201 C CZ  . ARG   A 141 ? 0.2164 0.3379 0.3326 -0.0722 -0.0000 -0.0174 141 ARG   A CZ  
3202 N NH1 . ARG   A 141 ? 0.2029 0.3369 0.3307 -0.0866 0.0180  -0.0357 141 ARG   A NH1 
3203 N NH2 . ARG   A 141 ? 0.2254 0.3550 0.3452 -0.0661 -0.0113 -0.0080 141 ARG   A NH2 
3217 N N   . VAL   A 142 ? 0.1264 0.1620 0.1821 -0.0136 -0.0095 0.0164  142 VAL   A N   
3218 C CA  . VAL   A 142 ? 0.1287 0.1588 0.1785 -0.0167 0.0094  0.0146  142 VAL   A CA  
3219 C C   . VAL   A 142 ? 0.1192 0.1528 0.1715 -0.0172 0.0016  0.0208  142 VAL   A C   
3220 O O   . VAL   A 142 ? 0.1268 0.1506 0.1861 -0.0104 0.0026  0.0208  142 VAL   A O   
3221 C CB  . VAL   A 142 ? 0.1392 0.1724 0.1843 -0.0130 0.0067  0.0287  142 VAL   A CB  
3222 C CG1 . VAL   A 142 ? 0.1417 0.1588 0.1864 -0.0201 0.0108  0.0216  142 VAL   A CG1 
3223 C CG2 . VAL   A 142 ? 0.1539 0.1854 0.2029 -0.0094 0.0022  0.0268  142 VAL   A CG2 
3233 N N   . CYS   A 143 ? 0.1255 0.1479 0.1669 -0.0182 0.0008  0.0187  143 CYS   A N   
3234 C CA  . CYS   A 143 ? 0.1252 0.1441 0.1838 -0.0133 -0.0041 0.0278  143 CYS   A CA  
3235 C C   . CYS   A 143 ? 0.1244 0.1337 0.1868 -0.0122 -0.0003 0.0294  143 CYS   A C   
3236 O O   . CYS   A 143 ? 0.1198 0.1368 0.1882 -0.0100 -0.0027 0.0304  143 CYS   A O   
3237 C CB  . CYS   A 143 ? 0.1341 0.1446 0.1894 -0.0069 0.0069  0.0333  143 CYS   A CB  
3238 S SG  . CYS   A 143 ? 0.1493 0.1485 0.1807 0.0038  0.0043  0.0186  143 CYS   A SG  
3244 N N   . VAL   A 144 ? 0.1214 0.1370 0.2054 -0.0127 0.0127  0.0292  144 VAL   A N   
3245 C CA  . VAL   A 144 ? 0.1228 0.1493 0.2297 -0.0131 0.0158  0.0329  144 VAL   A CA  
3246 C C   . VAL   A 144 ? 0.1237 0.1393 0.2291 -0.0184 -0.0040 0.0294  144 VAL   A C   
3247 O O   . VAL   A 144 ? 0.1422 0.1425 0.2460 -0.0060 -0.0053 0.0401  144 VAL   A O   
3248 C CB  . VAL   A 144 ? 0.1449 0.1744 0.2622 -0.0053 0.0251  0.0300  144 VAL   A CB  
3249 C CG1 . VAL   A 144 ? 0.1552 0.1859 0.2905 -0.0226 0.0072  0.0275  144 VAL   A CG1 
3250 C CG2 . VAL   A 144 ? 0.1389 0.1801 0.2684 -0.0075 0.0286  0.0397  144 VAL   A CG2 
3260 N N   . ASP   A 145 ? 0.1364 0.1401 0.2430 -0.0184 0.0048  0.0151  145 ASP   A N   
3261 C CA  . ASP   A 145 ? 0.1482 0.1506 0.2511 -0.0215 0.0030  0.0066  145 ASP   A CA  
3262 C C   . ASP   A 145 ? 0.1440 0.1395 0.2473 -0.0180 0.0058  -0.0026 145 ASP   A C   
3263 O O   . ASP   A 145 ? 0.1550 0.1479 0.3063 -0.0243 -0.0016 -0.0350 145 ASP   A O   
3264 C CB  . ASP   A 145 ? 0.1555 0.1814 0.2757 -0.0272 -0.0133 0.0000  145 ASP   A CB  
3265 C CG  . ASP   A 145 ? 0.1719 0.2156 0.3108 -0.0479 -0.0261 0.0034  145 ASP   A CG  
3266 O OD1 . ASP   A 145 ? 0.1697 0.2266 0.3282 -0.0619 -0.0226 0.0147  145 ASP   A OD1 
3267 O OD2 . ASP   A 145 ? 0.1961 0.2355 0.3244 -0.0586 -0.0436 0.0120  145 ASP   A OD2 
3272 N N   . THR   A 146 ? 0.1325 0.1319 0.2106 -0.0137 0.0073  0.0117  146 THR   A N   
3273 C CA  . THR   A 146 ? 0.1245 0.1278 0.1941 -0.0060 0.0066  0.0123  146 THR   A CA  
3274 C C   . THR   A 146 ? 0.1180 0.1250 0.1968 -0.0061 0.0056  0.0195  146 THR   A C   
3275 O O   . THR   A 146 ? 0.1291 0.1391 0.2187 0.0002  -0.0004 0.0215  146 THR   A O   
3276 C CB  . THR   A 146 ? 0.1242 0.1298 0.1895 -0.0052 0.0066  0.0182  146 THR   A CB  
3277 O OG1 . THR   A 146 ? 0.1258 0.1464 0.1928 -0.0053 0.0004  0.0109  146 THR   A OG1 
3278 C CG2 . THR   A 146 ? 0.1244 0.1289 0.2052 -0.0143 0.0049  0.0181  146 THR   A CG2 
3286 N N   . VAL   A 147 ? 0.1190 0.1304 0.1890 -0.0045 0.0096  0.0202  147 VAL   A N   
3287 C CA  . VAL   A 147 ? 0.1137 0.1326 0.1936 -0.0089 0.0217  0.0251  147 VAL   A CA  
3288 C C   . VAL   A 147 ? 0.1216 0.1279 0.2014 -0.0131 0.0178  0.0319  147 VAL   A C   
3289 O O   . VAL   A 147 ? 0.1259 0.1301 0.2207 -0.0123 0.0116  0.0332  147 VAL   A O   
3290 C CB  . VAL   A 147 ? 0.1268 0.1318 0.1935 -0.0109 0.0144  0.0276  147 VAL   A CB  
3291 C CG1 . VAL   A 147 ? 0.1561 0.1372 0.1977 -0.0026 0.0089  0.0402  147 VAL   A CG1 
3292 C CG2 . VAL   A 147 ? 0.1236 0.1262 0.1954 -0.0136 0.0081  0.0277  147 VAL   A CG2 
3302 N N   . ARG   A 148 ? 0.1213 0.1308 0.1988 -0.0130 0.0196  0.0425  148 ARG   A N   
3303 C CA  . ARG   A 148 ? 0.1299 0.1318 0.2060 -0.0113 0.0114  0.0518  148 ARG   A CA  
3304 C C   . ARG   A 148 ? 0.1437 0.1285 0.2084 -0.0138 0.0074  0.0597  148 ARG   A C   
3305 O O   . ARG   A 148 ? 0.1694 0.1447 0.2199 -0.0167 0.0144  0.0571  148 ARG   A O   
3306 C CB  . ARG   A 148 ? 0.1347 0.1345 0.2208 -0.0070 0.0220  0.0459  148 ARG   A CB  
3307 C CG  . ARG   A 148 ? 0.1520 0.1377 0.2517 -0.0093 0.0322  0.0364  148 ARG   A CG  
3308 C CD  . ARG   A 148 ? 0.1704 0.1386 0.2738 -0.0054 0.0405  0.0537  148 ARG   A CD  
3309 N NE  . ARG   A 148 ? 0.1649 0.1409 0.2709 0.0097  0.0438  0.0606  148 ARG   A NE  
3310 C CZ  . ARG   A 148 ? 0.1616 0.1307 0.2535 0.0065  0.0436  0.0516  148 ARG   A CZ  
3311 N NH1 . ARG   A 148 ? 0.1683 0.1323 0.2553 -0.0049 0.0428  0.0243  148 ARG   A NH1 
3312 N NH2 . ARG   A 148 ? 0.1505 0.1510 0.2607 0.0140  0.0440  0.0552  148 ARG   A NH2 
3326 N N   . THR   A 149 ? 0.1353 0.1411 0.1928 -0.0102 0.0030  0.0491  149 THR   A N   
3327 C CA  . THR   A 149 ? 0.1337 0.1508 0.1910 -0.0114 0.0033  0.0504  149 THR   A CA  
3328 C C   . THR   A 149 ? 0.1292 0.1489 0.1842 -0.0162 0.0077  0.0563  149 THR   A C   
3329 O O   . THR   A 149 ? 0.1292 0.1535 0.2088 -0.0214 0.0045  0.0527  149 THR   A O   
3330 C CB  . THR   A 149 ? 0.1371 0.1600 0.1978 -0.0126 0.0081  0.0432  149 THR   A CB  
3331 O OG1 . THR   A 149 ? 0.1419 0.1438 0.2101 -0.0176 0.0023  0.0389  149 THR   A OG1 
3332 C CG2 . THR   A 149 ? 0.1308 0.1720 0.2045 -0.0011 0.0040  0.0411  149 THR   A CG2 
3340 N N   . ASN   A 150 ? 0.1357 0.1498 0.1906 -0.0110 -0.0021 0.0658  150 ASN   A N   
3341 C CA  . ASN   A 150 ? 0.1449 0.1543 0.1897 -0.0116 0.0111  0.0566  150 ASN   A CA  
3342 C C   . ASN   A 150 ? 0.1262 0.1434 0.1887 -0.0148 0.0106  0.0532  150 ASN   A C   
3343 O O   . ASN   A 150 ? 0.1408 0.1547 0.2109 -0.0131 -0.0059 0.0494  150 ASN   A O   
3344 C CB  . ASN   A 150 ? 0.1884 0.1791 0.2162 -0.0194 0.0180  0.0760  150 ASN   A CB  
3345 C CG  . ASN   A 150 ? 0.2421 0.2121 0.2782 -0.0148 0.0069  0.0802  150 ASN   A CG  
3346 O OD1 . ASN   A 150 ? 0.2664 0.2160 0.2936 -0.0243 0.0128  0.0987  150 ASN   A OD1 
3347 N ND2 . ASN   A 150 ? 0.2732 0.2331 0.3152 -0.0093 -0.0031 0.0803  150 ASN   A ND2 
3354 N N   . VAL   A 151 ? 0.1274 0.1380 0.1846 -0.0176 0.0051  0.0477  151 VAL   A N   
3355 C CA  . VAL   A 151 ? 0.1321 0.1406 0.1771 -0.0203 0.0032  0.0451  151 VAL   A CA  
3356 C C   . VAL   A 151 ? 0.1253 0.1344 0.1774 -0.0240 0.0081  0.0501  151 VAL   A C   
3357 O O   . VAL   A 151 ? 0.1302 0.1426 0.2204 -0.0210 0.0071  0.0423  151 VAL   A O   
3358 C CB  . VAL   A 151 ? 0.1539 0.1555 0.1717 -0.0117 0.0038  0.0464  151 VAL   A CB  
3359 C CG1 . VAL   A 151 ? 0.1554 0.1769 0.1999 -0.0184 0.0037  0.0403  151 VAL   A CG1 
3360 C CG2 . VAL   A 151 ? 0.1621 0.1628 0.1764 -0.0089 0.0127  0.0388  151 VAL   A CG2 
3370 N N   . TYR   A 152 ? 0.1264 0.1331 0.1807 -0.0216 0.0003  0.0466  152 TYR   A N   
3371 C CA  . TYR   A 152 ? 0.1222 0.1409 0.1600 -0.0167 0.0032  0.0438  152 TYR   A CA  
3372 C C   . TYR   A 152 ? 0.1222 0.1370 0.1486 -0.0200 0.0091  0.0458  152 TYR   A C   
3373 O O   . TYR   A 152 ? 0.1320 0.1360 0.1504 -0.0265 0.0110  0.0358  152 TYR   A O   
3374 C CB  . TYR   A 152 ? 0.1378 0.1514 0.1729 -0.0143 0.0109  0.0462  152 TYR   A CB  
3375 C CG  . TYR   A 152 ? 0.1502 0.1721 0.1620 -0.0177 0.0193  0.0513  152 TYR   A CG  
3376 C CD1 . TYR   A 152 ? 0.1688 0.1982 0.1822 -0.0008 0.0227  0.0564  152 TYR   A CD1 
3377 C CD2 . TYR   A 152 ? 0.1536 0.1879 0.1583 -0.0262 0.0105  0.0525  152 TYR   A CD2 
3378 C CE1 . TYR   A 152 ? 0.2023 0.2114 0.1929 0.0023  0.0095  0.0720  152 TYR   A CE1 
3379 C CE2 . TYR   A 152 ? 0.1845 0.2045 0.1748 -0.0286 0.0158  0.0598  152 TYR   A CE2 
3380 C CZ  . TYR   A 152 ? 0.2162 0.2077 0.1876 -0.0129 0.0115  0.0852  152 TYR   A CZ  
3381 O OH  . TYR   A 152 ? 0.2521 0.2314 0.2253 -0.0058 0.0172  0.1056  152 TYR   A OH  
3391 N N   . LEU   A 153 ? 0.1239 0.1384 0.1601 -0.0210 0.0090  0.0448  153 LEU   A N   
3392 C CA  . LEU   A 153 ? 0.1136 0.1353 0.1682 -0.0095 0.0113  0.0451  153 LEU   A CA  
3393 C C   . LEU   A 153 ? 0.1195 0.1410 0.1712 -0.0084 0.0196  0.0453  153 LEU   A C   
3394 O O   . LEU   A 153 ? 0.1253 0.1494 0.2043 -0.0104 0.0306  0.0448  153 LEU   A O   
3395 C CB  . LEU   A 153 ? 0.1110 0.1372 0.1761 -0.0080 0.0061  0.0413  153 LEU   A CB  
3396 C CG  . LEU   A 153 ? 0.1213 0.1400 0.1746 -0.0131 0.0080  0.0358  153 LEU   A CG  
3397 C CD1 . LEU   A 153 ? 0.1327 0.1435 0.1815 -0.0137 -0.0019 0.0287  153 LEU   A CD1 
3398 C CD2 . LEU   A 153 ? 0.1316 0.1550 0.1952 -0.0224 0.0195  0.0140  153 LEU   A CD2 
3410 N N   . ALA   A 154 ? 0.1190 0.1319 0.1791 -0.0047 0.0214  0.0482  154 ALA   A N   
3411 C CA  . ALA   A 154 ? 0.1359 0.1379 0.1831 -0.0051 0.0197  0.0456  154 ALA   A CA  
3412 C C   . ALA   A 154 ? 0.1272 0.1327 0.1825 -0.0007 0.0224  0.0494  154 ALA   A C   
3413 O O   . ALA   A 154 ? 0.1325 0.1467 0.1925 -0.0051 0.0176  0.0546  154 ALA   A O   
3414 C CB  . ALA   A 154 ? 0.1439 0.1415 0.1849 0.0071  0.0129  0.0301  154 ALA   A CB  
3420 N N   A VAL   A 155 ? 0.1277 0.1365 0.1615 0.0044  0.0153  0.0478  155 VAL   A N   
3421 N N   B VAL   A 155 ? 0.1158 0.1284 0.1782 -0.0042 0.0242  0.0566  155 VAL   A N   
3422 C CA  A VAL   A 155 ? 0.1354 0.1459 0.1536 0.0095  -0.0037 0.0408  155 VAL   A CA  
3423 C CA  B VAL   A 155 ? 0.1180 0.1282 0.1925 -0.0085 0.0078  0.0604  155 VAL   A CA  
3424 C CA  T VAL   A 155 ? 0.1782 0.1884 0.1992 0.0079  -0.0015 0.0155  155 VAL   A CA  
3425 C C   A VAL   A 155 ? 0.1422 0.1557 0.1471 0.0221  -0.0137 0.0417  155 VAL   A C   
3426 C C   B VAL   A 155 ? 0.1213 0.1350 0.1998 -0.0041 0.0147  0.0638  155 VAL   A C   
3427 C C   T VAL   A 155 ? 0.1758 0.1837 0.1885 0.0081  0.0032  0.0155  155 VAL   A C   
3428 O O   A VAL   A 155 ? 0.1459 0.1620 0.1574 0.0325  -0.0133 0.0360  155 VAL   A O   
3429 O O   B VAL   A 155 ? 0.1201 0.1435 0.2119 0.0085  0.0271  0.0666  155 VAL   A O   
3430 O O   T VAL   A 155 ? 0.1727 0.1841 0.1834 0.0047  0.0012  0.0146  155 VAL   A O   
3431 C CB  A VAL   A 155 ? 0.1333 0.1441 0.1648 0.0106  -0.0140 0.0343  155 VAL   A CB  
3432 C CB  B VAL   A 155 ? 0.1145 0.1272 0.2007 -0.0112 -0.0154 0.0550  155 VAL   A CB  
3433 C CB  T VAL   A 155 ? 0.1804 0.1905 0.2087 0.0091  -0.0017 0.0157  155 VAL   A CB  
3434 C CG1 A VAL   A 155 ? 0.1423 0.1430 0.1700 0.0089  -0.0201 0.0284  155 VAL   A CG1 
3435 C CG1 B VAL   A 155 ? 0.1252 0.1306 0.2091 -0.0178 -0.0297 0.0515  155 VAL   A CG1 
3436 C CG1 T VAL   A 155 ? 0.1820 0.1930 0.2147 0.0094  -0.0042 0.0153  155 VAL   A CG1 
3437 C CG2 A VAL   A 155 ? 0.1360 0.1492 0.1739 0.0138  -0.0200 0.0321  155 VAL   A CG2 
3438 C CG2 B VAL   A 155 ? 0.1296 0.1311 0.2197 -0.0034 -0.0234 0.0465  155 VAL   A CG2 
3439 C CG2 T VAL   A 155 ? 0.1797 0.1906 0.2105 0.0098  -0.0033 0.0171  155 VAL   A CG2 
3465 N N   A PHE   A 156 ? 0.1483 0.1581 0.1507 0.0292  -0.0093 0.0493  156 PHE   A N   
3466 N N   B PHE   A 156 ? 0.1329 0.1278 0.2219 -0.0057 0.0253  0.0546  156 PHE   A N   
3467 N N   T PHE   A 156 ? 0.1741 0.1775 0.1897 0.0130  0.0093  0.0166  156 PHE   A N   
3468 C CA  A PHE   A 156 ? 0.1639 0.1636 0.1753 0.0395  -0.0044 0.0465  156 PHE   A CA  
3469 C CA  B PHE   A 156 ? 0.1454 0.1350 0.2286 -0.0065 0.0113  0.0564  156 PHE   A CA  
3470 C CA  T PHE   A 156 ? 0.1765 0.1741 0.1881 0.0213  0.0120  0.0198  156 PHE   A CA  
3471 C C   A PHE   A 156 ? 0.1548 0.1624 0.1827 0.0453  0.0098  0.0575  156 PHE   A C   
3472 C C   B PHE   A 156 ? 0.1511 0.1481 0.2524 -0.0015 0.0251  0.0654  156 PHE   A C   
3473 C C   T PHE   A 156 ? 0.1686 0.1741 0.1946 0.0207  0.0225  0.0260  156 PHE   A C   
3474 O O   A PHE   A 156 ? 0.1576 0.1657 0.1844 0.0372  0.0324  0.0583  156 PHE   A O   
3475 O O   B PHE   A 156 ? 0.1638 0.1655 0.2742 -0.0053 0.0367  0.0499  156 PHE   A O   
3476 O O   T PHE   A 156 ? 0.1702 0.1741 0.2057 0.0187  0.0281  0.0152  156 PHE   A O   
3477 C CB  A PHE   A 156 ? 0.1858 0.1737 0.1889 0.0387  -0.0150 0.0391  156 PHE   A CB  
3478 C CB  B PHE   A 156 ? 0.1486 0.1220 0.2081 -0.0085 -0.0059 0.0603  156 PHE   A CB  
3479 C CB  T PHE   A 156 ? 0.1844 0.1697 0.1792 0.0295  0.0033  0.0214  156 PHE   A CB  
3480 C CG  A PHE   A 156 ? 0.2079 0.1823 0.2058 0.0403  -0.0237 0.0277  156 PHE   A CG  
3481 C CG  B PHE   A 156 ? 0.1626 0.1363 0.2051 -0.0048 -0.0107 0.0553  156 PHE   A CG  
3482 C CG  T PHE   A 156 ? 0.1928 0.1685 0.1794 0.0400  -0.0040 0.0221  156 PHE   A CG  
3483 C CD1 A PHE   A 156 ? 0.2180 0.1886 0.2172 0.0418  -0.0192 0.0226  156 PHE   A CD1 
3484 C CD1 B PHE   A 156 ? 0.1691 0.1476 0.2185 -0.0009 -0.0048 0.0476  156 PHE   A CD1 
3485 C CD1 T PHE   A 156 ? 0.1965 0.1648 0.1801 0.0490  -0.0070 0.0236  156 PHE   A CD1 
3486 C CD2 A PHE   A 156 ? 0.2195 0.1887 0.2110 0.0411  -0.0299 0.0205  156 PHE   A CD2 
3487 C CD2 B PHE   A 156 ? 0.1807 0.1436 0.2210 -0.0022 -0.0176 0.0499  156 PHE   A CD2 
3488 C CD2 T PHE   A 156 ? 0.1997 0.1712 0.1851 0.0399  -0.0074 0.0234  156 PHE   A CD2 
3489 C CE1 A PHE   A 156 ? 0.2256 0.1914 0.2255 0.0406  -0.0130 0.0146  156 PHE   A CE1 
3490 C CE1 B PHE   A 156 ? 0.1784 0.1556 0.2371 -0.0037 0.0018  0.0371  156 PHE   A CE1 
3491 C CE1 T PHE   A 156 ? 0.2015 0.1664 0.1911 0.0515  -0.0062 0.0201  156 PHE   A CE1 
3492 C CE2 A PHE   A 156 ? 0.2295 0.1937 0.2191 0.0411  -0.0300 0.0128  156 PHE   A CE2 
3493 C CE2 B PHE   A 156 ? 0.1926 0.1516 0.2362 -0.0047 -0.0173 0.0406  156 PHE   A CE2 
3494 C CE2 T PHE   A 156 ? 0.2054 0.1719 0.1906 0.0429  -0.0109 0.0247  156 PHE   A CE2 
3495 C CZ  A PHE   A 156 ? 0.2298 0.1950 0.2271 0.0425  -0.0168 0.0097  156 PHE   A CZ  
3496 C CZ  B PHE   A 156 ? 0.1862 0.1514 0.2464 -0.0096 -0.0038 0.0410  156 PHE   A CZ  
3497 C CZ  T PHE   A 156 ? 0.2058 0.1691 0.1954 0.0456  -0.0097 0.0236  156 PHE   A CZ  
3525 N N   A ASP   A 157 ? 0.1487 0.1695 0.1933 0.0464  0.0001  0.0553  157 ASP   A N   
3526 N N   B ASP   A 157 ? 0.1592 0.1590 0.2748 -0.0105 0.0149  0.0735  157 ASP   A N   
3527 N N   T ASP   A 157 ? 0.1616 0.1811 0.1993 0.0197  0.0174  0.0382  157 ASP   A N   
3528 C CA  A ASP   A 157 ? 0.1534 0.1864 0.2151 0.0405  -0.0100 0.0545  157 ASP   A CA  
3529 C CA  B ASP   A 157 ? 0.1627 0.1703 0.2827 -0.0131 -0.0017 0.0648  157 ASP   A CA  
3530 C CA  T ASP   A 157 ? 0.1628 0.1909 0.2053 0.0209  0.0115  0.0475  157 ASP   A CA  
3531 C C   A ASP   A 157 ? 0.1514 0.1974 0.2236 0.0392  -0.0056 0.0545  157 ASP   A C   
3532 C C   B ASP   A 157 ? 0.1450 0.1713 0.2649 -0.0103 -0.0084 0.0576  157 ASP   A C   
3533 C C   T ASP   A 157 ? 0.1692 0.2030 0.2129 0.0203  0.0138  0.0464  157 ASP   A C   
3534 O O   A ASP   A 157 ? 0.1503 0.1954 0.2199 0.0374  -0.0022 0.0528  157 ASP   A O   
3535 O O   B ASP   A 157 ? 0.1375 0.1612 0.2409 -0.0109 -0.0164 0.0664  157 ASP   A O   
3536 O O   T ASP   A 157 ? 0.1662 0.2013 0.2070 0.0194  0.0176  0.0480  157 ASP   A O   
3537 C CB  A ASP   A 157 ? 0.1605 0.1906 0.2284 0.0388  -0.0245 0.0572  157 ASP   A CB  
3538 C CB  B ASP   A 157 ? 0.1787 0.1786 0.3084 -0.0076 -0.0096 0.0693  157 ASP   A CB  
3539 C CB  T ASP   A 157 ? 0.1616 0.1882 0.2033 0.0257  0.0037  0.0581  157 ASP   A CB  
3540 C CG  A ASP   A 157 ? 0.1725 0.1954 0.2477 0.0392  -0.0335 0.0554  157 ASP   A CG  
3541 C CG  B ASP   A 157 ? 0.1954 0.1885 0.3322 0.0002  -0.0218 0.0655  157 ASP   A CG  
3542 C CG  T ASP   A 157 ? 0.1648 0.1855 0.2031 0.0316  0.0009  0.0647  157 ASP   A CG  
3543 O OD1 A ASP   A 157 ? 0.1806 0.1989 0.2646 0.0300  -0.0355 0.0553  157 ASP   A OD1 
3544 O OD1 B ASP   A 157 ? 0.2073 0.1971 0.3611 0.0029  -0.0321 0.0640  157 ASP   A OD1 
3545 O OD1 T ASP   A 157 ? 0.1682 0.1842 0.2198 0.0299  0.0057  0.0626  157 ASP   A OD1 
3546 O OD2 A ASP   A 157 ? 0.1748 0.1942 0.2482 0.0411  -0.0295 0.0512  157 ASP   A OD2 
3547 O OD2 B ASP   A 157 ? 0.1976 0.1923 0.3284 0.0009  -0.0152 0.0622  157 ASP   A OD2 
3548 O OD2 T ASP   A 157 ? 0.1654 0.1822 0.1856 0.0326  -0.0018 0.0682  157 ASP   A OD2 
3561 N N   A LYS   A 158 ? 0.1562 0.2114 0.2427 0.0389  0.0043  0.0482  158 LYS   A N   
3562 N N   B LYS   A 158 ? 0.1444 0.1842 0.2859 -0.0087 0.0056  0.0442  158 LYS   A N   
3563 N N   T LYS   A 158 ? 0.1832 0.2188 0.2337 0.0208  0.0152  0.0362  158 LYS   A N   
3564 C CA  A LYS   A 158 ? 0.1618 0.2253 0.2649 0.0447  0.0162  0.0422  158 LYS   A CA  
3565 C CA  B LYS   A 158 ? 0.1499 0.2042 0.2999 -0.0032 0.0140  0.0418  158 LYS   A CA  
3566 C CA  T LYS   A 158 ? 0.1991 0.2335 0.2526 0.0259  0.0144  0.0308  158 LYS   A CA  
3567 C C   A LYS   A 158 ? 0.1561 0.2295 0.2587 0.0498  0.0101  0.0421  158 LYS   A C   
3568 C C   B LYS   A 158 ? 0.1352 0.1968 0.2701 0.0004  -0.0111 0.0405  158 LYS   A C   
3569 C C   T LYS   A 158 ? 0.2008 0.2349 0.2455 0.0280  0.0086  0.0300  158 LYS   A C   
3570 O O   A LYS   A 158 ? 0.1542 0.2322 0.2551 0.0473  0.0200  0.0367  158 LYS   A O   
3571 O O   B LYS   A 158 ? 0.1375 0.1976 0.2604 -0.0088 -0.0046 0.0443  158 LYS   A O   
3572 O O   T LYS   A 158 ? 0.1990 0.2353 0.2401 0.0273  0.0103  0.0277  158 LYS   A O   
3573 C CB  A LYS   A 158 ? 0.1778 0.2339 0.2952 0.0408  0.0333  0.0459  158 LYS   A CB  
3574 C CB  B LYS   A 158 ? 0.1691 0.2367 0.3467 0.0018  0.0413  0.0519  158 LYS   A CB  
3575 C CB  T LYS   A 158 ? 0.2156 0.2446 0.2833 0.0268  0.0199  0.0298  158 LYS   A CB  
3576 C CG  A LYS   A 158 ? 0.1973 0.2417 0.3309 0.0361  0.0430  0.0561  158 LYS   A CG  
3577 C CG  B LYS   A 158 ? 0.1947 0.2664 0.3960 0.0057  0.0572  0.0728  158 LYS   A CG  
3578 C CG  T LYS   A 158 ? 0.2325 0.2551 0.3166 0.0268  0.0229  0.0327  158 LYS   A CG  
3579 C CD  A LYS   A 158 ? 0.2131 0.2461 0.3605 0.0330  0.0541  0.0683  158 LYS   A CD  
3580 C CD  B LYS   A 158 ? 0.2146 0.2914 0.4412 0.0080  0.0753  0.0924  158 LYS   A CD  
3581 C CD  T LYS   A 158 ? 0.2474 0.2631 0.3481 0.0287  0.0253  0.0377  158 LYS   A CD  
3582 C CE  A LYS   A 158 ? 0.2210 0.2457 0.3789 0.0321  0.0635  0.0839  158 LYS   A CE  
3583 C CE  B LYS   A 158 ? 0.2232 0.3059 0.4707 0.0121  0.0972  0.1148  158 LYS   A CE  
3584 C CE  T LYS   A 158 ? 0.2566 0.2676 0.3711 0.0306  0.0267  0.0441  158 LYS   A CE  
3585 N NZ  A LYS   A 158 ? 0.2248 0.2451 0.3918 0.0316  0.0711  0.0907  158 LYS   A NZ  
3586 N NZ  B LYS   A 158 ? 0.2209 0.3133 0.4895 0.0123  0.1112  0.1287  158 LYS   A NZ  
3587 N NZ  T LYS   A 158 ? 0.2619 0.2703 0.3847 0.0320  0.0288  0.0475  158 LYS   A NZ  
3627 N N   A ASN   A 159 ? 0.1585 0.2310 0.2647 0.0514  -0.0024 0.0465  159 ASN   A N   
3628 N N   B ASN   A 159 ? 0.1528 0.2050 0.2736 0.0073  -0.0249 0.0342  159 ASN   A N   
3629 N N   T ASN   A 159 ? 0.2062 0.2351 0.2521 0.0270  0.0039  0.0315  159 ASN   A N   
3630 C CA  A ASN   A 159 ? 0.1630 0.2347 0.2691 0.0487  -0.0122 0.0516  159 ASN   A CA  
3631 C CA  B ASN   A 159 ? 0.1630 0.2146 0.2900 0.0166  -0.0415 0.0348  159 ASN   A CA  
3632 C CA  T ASN   A 159 ? 0.2146 0.2359 0.2584 0.0239  0.0012  0.0326  159 ASN   A CA  
3633 C C   A ASN   A 159 ? 0.1535 0.2290 0.2533 0.0446  -0.0074 0.0520  159 ASN   A C   
3634 C C   B ASN   A 159 ? 0.1440 0.2034 0.2750 0.0067  -0.0353 0.0408  159 ASN   A C   
3635 C C   T ASN   A 159 ? 0.2166 0.2311 0.2514 0.0213  0.0078  0.0264  159 ASN   A C   
3636 O O   A ASN   A 159 ? 0.1485 0.2294 0.2553 0.0484  -0.0103 0.0411  159 ASN   A O   
3637 O O   B ASN   A 159 ? 0.1427 0.2138 0.2918 -0.0001 -0.0394 0.0320  159 ASN   A O   
3638 O O   T ASN   A 159 ? 0.2172 0.2306 0.2561 0.0226  0.0095  0.0199  159 ASN   A O   
3639 C CB  A ASN   A 159 ? 0.1792 0.2432 0.3006 0.0461  -0.0164 0.0554  159 ASN   A CB  
3640 C CB  B ASN   A 159 ? 0.2047 0.2378 0.3360 0.0300  -0.0537 0.0253  159 ASN   A CB  
3641 C CB  T ASN   A 159 ? 0.2206 0.2411 0.2810 0.0218  -0.0031 0.0395  159 ASN   A CB  
3642 C CG  A ASN   A 159 ? 0.1976 0.2530 0.3366 0.0409  -0.0112 0.0538  159 ASN   A CG  
3643 C CG  B ASN   A 159 ? 0.2454 0.2603 0.3964 0.0315  -0.0563 0.0056  159 ASN   A CG  
3644 C CG  T ASN   A 159 ? 0.2285 0.2471 0.3073 0.0184  -0.0011 0.0422  159 ASN   A CG  
3645 O OD1 A ASN   A 159 ? 0.2016 0.2580 0.3454 0.0341  -0.0062 0.0565  159 ASN   A OD1 
3646 O OD1 B ASN   A 159 ? 0.2678 0.2628 0.4286 0.0280  -0.0556 0.0014  159 ASN   A OD1 
3647 O OD1 T ASN   A 159 ? 0.2278 0.2503 0.3146 0.0147  0.0038  0.0447  159 ASN   A OD1 
3648 N ND2 A ASN   A 159 ? 0.1991 0.2542 0.3469 0.0459  -0.0132 0.0557  159 ASN   A ND2 
3649 N ND2 B ASN   A 159 ? 0.2538 0.2708 0.4166 0.0293  -0.0584 0.0002  159 ASN   A ND2 
3650 N ND2 T ASN   A 159 ? 0.2298 0.2484 0.3143 0.0200  -0.0034 0.0458  159 ASN   A ND2 
3669 N N   A LEU   A 160 ? 0.1495 0.2188 0.2443 0.0362  -0.0071 0.0661  160 LEU   A N   
3670 N N   B LEU   A 160 ? 0.1339 0.1914 0.2725 0.0019  -0.0267 0.0552  160 LEU   A N   
3671 N N   T LEU   A 160 ? 0.2182 0.2249 0.2459 0.0168  0.0077  0.0282  160 LEU   A N   
3672 C CA  A LEU   A 160 ? 0.1502 0.2123 0.2341 0.0185  0.0056  0.0809  160 LEU   A CA  
3673 C CA  B LEU   A 160 ? 0.1292 0.1841 0.2588 -0.0104 -0.0108 0.0699  160 LEU   A CA  
3674 C CA  T LEU   A 160 ? 0.2212 0.2198 0.2392 0.0102  0.0123  0.0322  160 LEU   A CA  
3675 C C   A LEU   A 160 ? 0.1336 0.2146 0.2293 0.0098  0.0057  0.0907  160 LEU   A C   
3676 C C   B LEU   A 160 ? 0.1146 0.1843 0.2521 -0.0089 0.0021  0.0738  160 LEU   A C   
3677 O O   A LEU   A 160 ? 0.1314 0.2136 0.2282 0.0077  0.0012  0.0962  160 LEU   A O   
3678 O O   B LEU   A 160 ? 0.1249 0.1735 0.2655 -0.0184 -0.0080 0.0683  160 LEU   A O   
3679 C CB  A LEU   A 160 ? 0.1646 0.2112 0.2306 0.0100  0.0161  0.0726  160 LEU   A CB  
3680 C CB  B LEU   A 160 ? 0.1437 0.1808 0.2483 -0.0218 -0.0177 0.0764  160 LEU   A CB  
3681 C CB  T LEU   A 160 ? 0.2242 0.2181 0.2335 0.0041  0.0172  0.0314  160 LEU   A CB  
3682 C CG  A LEU   A 160 ? 0.1750 0.2117 0.2375 0.0028  0.0251  0.0603  160 LEU   A CG  
3683 C CG  B LEU   A 160 ? 0.1508 0.1871 0.2543 -0.0309 -0.0218 0.0705  160 LEU   A CG  
3684 C CG  T LEU   A 160 ? 0.2265 0.2179 0.2342 -0.0010 0.0219  0.0281  160 LEU   A CG  
3685 C CD1 A LEU   A 160 ? 0.1802 0.2113 0.2436 0.0023  0.0239  0.0524  160 LEU   A CD1 
3686 C CD1 B LEU   A 160 ? 0.1593 0.1996 0.2686 -0.0297 -0.0189 0.0674  160 LEU   A CD1 
3687 C CD1 T LEU   A 160 ? 0.2287 0.2176 0.2365 -0.0014 0.0214  0.0249  160 LEU   A CD1 
3688 C CD2 A LEU   A 160 ? 0.1772 0.2146 0.2408 0.0005  0.0324  0.0528  160 LEU   A CD2 
3689 C CD2 B LEU   A 160 ? 0.1567 0.1798 0.2632 -0.0350 -0.0229 0.0640  160 LEU   A CD2 
3690 C CD2 T LEU   A 160 ? 0.2269 0.2187 0.2351 -0.0032 0.0259  0.0247  160 LEU   A CD2 
3723 N N   A TYR   A 161 ? 0.1347 0.2239 0.2549 0.0029  0.0047  0.0828  161 TYR   A N   
3724 N N   B TYR   A 161 ? 0.1185 0.2006 0.2633 0.0030  0.0217  0.0787  161 TYR   A N   
3725 C CA  A TYR   A 161 ? 0.1295 0.2263 0.2562 -0.0059 0.0030  0.0845  161 TYR   A CA  
3726 C CA  B TYR   A 161 ? 0.1302 0.2121 0.2631 0.0069  0.0202  0.0956  161 TYR   A CA  
3727 C C   A TYR   A 161 ? 0.1229 0.2447 0.2692 -0.0109 -0.0022 0.0879  161 TYR   A C   
3728 C C   B TYR   A 161 ? 0.1409 0.2369 0.2846 0.0057  0.0130  0.0958  161 TYR   A C   
3729 O O   A TYR   A 161 ? 0.1142 0.2525 0.2644 -0.0130 -0.0001 0.0907  161 TYR   A O   
3730 O O   B TYR   A 161 ? 0.1382 0.2405 0.2807 0.0061  0.0154  0.0981  161 TYR   A O   
3731 C CB  A TYR   A 161 ? 0.1356 0.2109 0.2629 -0.0125 0.0015  0.0710  161 TYR   A CB  
3732 C CB  B TYR   A 161 ? 0.1348 0.2021 0.2679 0.0122  0.0306  0.0885  161 TYR   A CB  
3733 C CG  A TYR   A 161 ? 0.1386 0.1959 0.2599 -0.0169 -0.0150 0.0589  161 TYR   A CG  
3734 C CG  B TYR   A 161 ? 0.1393 0.1979 0.2760 0.0145  0.0304  0.0730  161 TYR   A CG  
3735 C CD1 A TYR   A 161 ? 0.1366 0.1882 0.2626 -0.0186 -0.0236 0.0480  161 TYR   A CD1 
3736 C CD1 B TYR   A 161 ? 0.1409 0.1972 0.2882 0.0172  0.0273  0.0570  161 TYR   A CD1 
3737 C CD2 A TYR   A 161 ? 0.1429 0.1921 0.2511 -0.0119 -0.0303 0.0604  161 TYR   A CD2 
3738 C CD2 B TYR   A 161 ? 0.1446 0.1963 0.2778 0.0222  0.0265  0.0729  161 TYR   A CD2 
3739 C CE1 A TYR   A 161 ? 0.1459 0.1759 0.2542 -0.0179 -0.0267 0.0498  161 TYR   A CE1 
3740 C CE1 B TYR   A 161 ? 0.1544 0.1940 0.2927 0.0191  0.0235  0.0553  161 TYR   A CE1 
3741 C CE2 A TYR   A 161 ? 0.1524 0.1821 0.2453 -0.0113 -0.0374 0.0613  161 TYR   A CE2 
3742 C CE2 B TYR   A 161 ? 0.1569 0.1914 0.2876 0.0214  0.0272  0.0701  161 TYR   A CE2 
3743 C CZ  A TYR   A 161 ? 0.1587 0.1707 0.2436 -0.0152 -0.0377 0.0605  161 TYR   A CZ  
3744 C CZ  B TYR   A 161 ? 0.1685 0.1899 0.2999 0.0176  0.0261  0.0611  161 TYR   A CZ  
3745 O OH  A TYR   A 161 ? 0.1723 0.1570 0.2335 -0.0146 -0.0437 0.0744  161 TYR   A OH  
3746 O OH  B TYR   A 161 ? 0.1846 0.1851 0.3194 0.0163  0.0267  0.0537  161 TYR   A OH  
3765 N N   A ASP   A 162 ? 0.1175 0.2555 0.2873 -0.0109 -0.0011 0.0879  162 ASP   A N   
3766 N N   B ASP   A 162 ? 0.1504 0.2619 0.3180 0.0049  0.0127  0.0876  162 ASP   A N   
3767 C CA  A ASP   A 162 ? 0.1063 0.2703 0.2982 -0.0153 0.0066  0.0766  162 ASP   A CA  
3768 C CA  B ASP   A 162 ? 0.1571 0.2865 0.3307 -0.0008 0.0177  0.0771  162 ASP   A CA  
3769 C C   A ASP   A 162 ? 0.0960 0.2834 0.2799 -0.0208 0.0061  0.0824  162 ASP   A C   
3770 C C   B ASP   A 162 ? 0.1663 0.3011 0.3154 -0.0116 0.0178  0.0751  162 ASP   A C   
3771 O O   A ASP   A 162 ? 0.0969 0.2816 0.2857 -0.0283 0.0140  0.0688  162 ASP   A O   
3772 O O   B ASP   A 162 ? 0.1697 0.3012 0.3172 -0.0129 0.0272  0.0676  162 ASP   A O   
3773 C CB  A ASP   A 162 ? 0.1180 0.2719 0.3324 -0.0147 0.0122  0.0589  162 ASP   A CB  
3774 C CB  B ASP   A 162 ? 0.1578 0.2961 0.3627 0.0002  0.0209  0.0667  162 ASP   A CB  
3775 C CG  A ASP   A 162 ? 0.1320 0.2755 0.3621 -0.0091 0.0127  0.0401  162 ASP   A CG  
3776 C CG  B ASP   A 162 ? 0.1655 0.3073 0.3962 0.0012  0.0188  0.0549  162 ASP   A CG  
3777 O OD1 A ASP   A 162 ? 0.1367 0.2765 0.3723 -0.0128 0.0170  0.0282  162 ASP   A OD1 
3778 O OD1 B ASP   A 162 ? 0.1677 0.3100 0.4039 0.0031  0.0216  0.0543  162 ASP   A OD1 
3779 O OD2 A ASP   A 162 ? 0.1441 0.2759 0.3745 -0.0060 0.0115  0.0351  162 ASP   A OD2 
3780 O OD2 B ASP   A 162 ? 0.1809 0.3135 0.4178 0.0076  0.0162  0.0463  162 ASP   A OD2 
3789 N N   A LYS   A 163 ? 0.1104 0.3030 0.2777 -0.0121 -0.0209 0.0866  163 LYS   A N   
3790 N N   B LYS   A 163 ? 0.1858 0.3153 0.3192 -0.0179 -0.0055 0.0702  163 LYS   A N   
3791 C CA  A LYS   A 163 ? 0.1282 0.3183 0.2695 -0.0149 -0.0146 0.0927  163 LYS   A CA  
3792 C CA  B LYS   A 163 ? 0.2028 0.3245 0.3126 -0.0328 -0.0137 0.0666  163 LYS   A CA  
3793 C C   A LYS   A 163 ? 0.1233 0.3084 0.2469 -0.0177 -0.0007 0.0904  163 LYS   A C   
3794 C C   B LYS   A 163 ? 0.1898 0.3035 0.2790 -0.0435 -0.0032 0.0574  163 LYS   A C   
3795 O O   A LYS   A 163 ? 0.1124 0.3187 0.2452 -0.0278 0.0070  0.0948  163 LYS   A O   
3796 O O   B LYS   A 163 ? 0.1912 0.3081 0.2769 -0.0448 0.0049  0.0573  163 LYS   A O   
3797 C CB  A LYS   A 163 ? 0.1631 0.3422 0.3074 -0.0096 -0.0264 0.0892  163 LYS   A CB  
3798 C CB  B LYS   A 163 ? 0.2338 0.3525 0.3548 -0.0369 -0.0240 0.0673  163 LYS   A CB  
3799 C CG  A LYS   A 163 ? 0.2026 0.3631 0.3594 -0.0104 -0.0163 0.0862  163 LYS   A CG  
3800 C CG  B LYS   A 163 ? 0.2621 0.3781 0.4017 -0.0404 -0.0225 0.0712  163 LYS   A CG  
3801 C CD  A LYS   A 163 ? 0.2393 0.3797 0.4087 -0.0123 -0.0108 0.0810  163 LYS   A CD  
3802 C CD  B LYS   A 163 ? 0.2853 0.3983 0.4457 -0.0457 -0.0236 0.0737  163 LYS   A CD  
3803 C CE  A LYS   A 163 ? 0.2696 0.3908 0.4459 -0.0146 -0.0092 0.0784  163 LYS   A CE  
3804 C CE  B LYS   A 163 ? 0.3035 0.4124 0.4803 -0.0486 -0.0226 0.0752  163 LYS   A CE  
3805 N NZ  A LYS   A 163 ? 0.2777 0.3978 0.4691 -0.0151 -0.0079 0.0763  163 LYS   A NZ  
3806 N NZ  B LYS   A 163 ? 0.3085 0.4203 0.4983 -0.0497 -0.0217 0.0739  163 LYS   A NZ  
3833 N N   A LEU   A 164 ? 0.1157 0.2851 0.2299 -0.0203 -0.0073 0.0814  164 LEU   A N   
3834 N N   B LEU   A 164 ? 0.1766 0.2805 0.2513 -0.0490 -0.0102 0.0525  164 LEU   A N   
3835 C CA  A LEU   A 164 ? 0.1171 0.2629 0.2138 -0.0231 0.0057  0.0678  164 LEU   A CA  
3836 C CA  B LEU   A 164 ? 0.1740 0.2615 0.2316 -0.0478 0.0036  0.0513  164 LEU   A CA  
3837 C C   A LEU   A 164 ? 0.1183 0.2512 0.2272 -0.0305 0.0126  0.0662  164 LEU   A C   
3838 C C   B LEU   A 164 ? 0.1800 0.2702 0.2266 -0.0429 0.0072  0.0575  164 LEU   A C   
3839 O O   A LEU   A 164 ? 0.1170 0.2568 0.2388 -0.0402 0.0343  0.0632  164 LEU   A O   
3840 O O   B LEU   A 164 ? 0.1832 0.2720 0.2210 -0.0401 0.0172  0.0547  164 LEU   A O   
3841 C CB  A LEU   A 164 ? 0.1251 0.2537 0.1835 -0.0173 0.0134  0.0542  164 LEU   A CB  
3842 C CB  B LEU   A 164 ? 0.1704 0.2394 0.2126 -0.0507 0.0176  0.0473  164 LEU   A CB  
3843 C CG  A LEU   A 164 ? 0.1347 0.2457 0.1692 -0.0140 0.0056  0.0402  164 LEU   A CG  
3844 C CG  B LEU   A 164 ? 0.1689 0.2303 0.1968 -0.0433 0.0266  0.0392  164 LEU   A CG  
3845 C CD1 A LEU   A 164 ? 0.1313 0.2406 0.1547 -0.0081 0.0013  0.0337  164 LEU   A CD1 
3846 C CD1 B LEU   A 164 ? 0.1639 0.2283 0.1883 -0.0398 0.0144  0.0350  164 LEU   A CD1 
3847 C CD2 A LEU   A 164 ? 0.1453 0.2411 0.1679 -0.0205 0.0063  0.0317  164 LEU   A CD2 
3848 C CD2 B LEU   A 164 ? 0.1822 0.2341 0.1997 -0.0343 0.0277  0.0358  164 LEU   A CD2 
3871 N N   A VAL   A 165 ? 0.1206 0.2379 0.2228 -0.0340 0.0159  0.0639  165 VAL   A N   
3872 N N   B VAL   A 165 ? 0.1840 0.2853 0.2300 -0.0383 0.0151  0.0618  165 VAL   A N   
3873 C CA  A VAL   A 165 ? 0.1331 0.2255 0.2169 -0.0446 0.0297  0.0584  165 VAL   A CA  
3874 C CA  B VAL   A 165 ? 0.1945 0.3008 0.2350 -0.0373 0.0195  0.0597  165 VAL   A CA  
3875 C C   A VAL   A 165 ? 0.1242 0.2310 0.2239 -0.0423 0.0358  0.0548  165 VAL   A C   
3876 C C   B VAL   A 165 ? 0.2012 0.3227 0.2572 -0.0299 0.0187  0.0536  165 VAL   A C   
3877 O O   A VAL   A 165 ? 0.1250 0.2276 0.2304 -0.0353 0.0344  0.0553  165 VAL   A O   
3878 O O   B VAL   A 165 ? 0.1944 0.3260 0.2587 -0.0209 0.0260  0.0449  165 VAL   A O   
3879 C CB  A VAL   A 165 ? 0.1497 0.2180 0.2187 -0.0490 0.0364  0.0482  165 VAL   A CB  
3880 C CB  B VAL   A 165 ? 0.2001 0.2968 0.2348 -0.0372 0.0262  0.0568  165 VAL   A CB  
3881 C CG1 A VAL   A 165 ? 0.1584 0.2183 0.2291 -0.0472 0.0324  0.0406  165 VAL   A CG1 
3882 C CG1 B VAL   A 165 ? 0.2026 0.2966 0.2359 -0.0373 0.0304  0.0525  165 VAL   A CG1 
3883 C CG2 A VAL   A 165 ? 0.1562 0.2156 0.2129 -0.0455 0.0302  0.0543  165 VAL   A CG2 
3884 C CG2 B VAL   A 165 ? 0.2030 0.2987 0.2391 -0.0334 0.0178  0.0547  165 VAL   A CG2 
3903 N N   A SER   A 166 ? 0.1153 0.2464 0.2344 -0.0408 0.0320  0.0424  166 SER   A N   
3904 N N   B SER   A 166 ? 0.2166 0.3409 0.2934 -0.0288 0.0043  0.0513  166 SER   A N   
3905 C CA  A SER   A 166 ? 0.1271 0.2726 0.2598 -0.0449 0.0198  0.0332  166 SER   A CA  
3906 C CA  B SER   A 166 ? 0.2304 0.3585 0.3138 -0.0353 -0.0015 0.0501  166 SER   A CA  
3907 C C   A SER   A 166 ? 0.1282 0.2965 0.2621 -0.0430 0.0075  0.0261  166 SER   A C   
3908 C C   B SER   A 166 ? 0.2487 0.3736 0.3177 -0.0376 -0.0016 0.0421  166 SER   A C   
3909 O O   A SER   A 166 ? 0.1423 0.3043 0.2829 -0.0505 0.0091  0.0034  166 SER   A O   
3910 O O   B SER   A 166 ? 0.2580 0.3780 0.3317 -0.0421 0.0041  0.0319  166 SER   A O   
3911 C CB  A SER   A 166 ? 0.1516 0.2805 0.2772 -0.0399 0.0199  0.0298  166 SER   A CB  
3912 C CB  B SER   A 166 ? 0.2265 0.3609 0.3355 -0.0327 -0.0125 0.0526  166 SER   A CB  
3913 O OG  A SER   A 166 ? 0.1824 0.2889 0.3104 -0.0388 0.0211  0.0348  166 SER   A OG  
3914 O OG  B SER   A 166 ? 0.2185 0.3628 0.3561 -0.0312 -0.0234 0.0573  166 SER   A OG  
3925 N N   A SER   A 167 ? 0.1296 0.3108 0.2423 -0.0208 -0.0088 0.0309  167 SER   A N   
3926 N N   B SER   A 167 ? 0.2655 0.3857 0.3172 -0.0301 -0.0093 0.0420  167 SER   A N   
3927 C CA  A SER   A 167 ? 0.1506 0.3216 0.2367 -0.0057 -0.0215 0.0233  167 SER   A CA  
3928 C CA  B SER   A 167 ? 0.2788 0.3953 0.3219 -0.0262 -0.0137 0.0369  167 SER   A CA  
3929 C C   A SER   A 167 ? 0.1618 0.3234 0.2373 0.0090  -0.0210 0.0086  167 SER   A C   
3930 C C   B SER   A 167 ? 0.2888 0.4022 0.3262 -0.0263 -0.0142 0.0318  167 SER   A C   
3931 O O   A SER   A 167 ? 0.1646 0.3268 0.2286 0.0130  -0.0133 0.0004  167 SER   A O   
3932 O O   B SER   A 167 ? 0.2891 0.4037 0.3294 -0.0280 -0.0184 0.0262  167 SER   A O   
3933 C CB  A SER   A 167 ? 0.1579 0.3302 0.2333 0.0001  -0.0130 0.0284  167 SER   A CB  
3934 C CB  B SER   A 167 ? 0.2852 0.3999 0.3328 -0.0222 -0.0134 0.0360  167 SER   A CB  
3935 O OG  A SER   A 167 ? 0.1573 0.3361 0.2268 0.0008  -0.0001 0.0333  167 SER   A OG  
3936 O OG  B SER   A 167 ? 0.2877 0.4025 0.3414 -0.0182 -0.0129 0.0361  167 SER   A OG  
3947 N N   A PHE   A 168 ? 0.1730 0.3220 0.2439 0.0208  -0.0217 0.0090  168 PHE   A N   
3948 N N   B PHE   A 168 ? 0.2980 0.4081 0.3355 -0.0236 -0.0155 0.0381  168 PHE   A N   
3949 C CA  A PHE   A 168 ? 0.1922 0.3217 0.2744 0.0192  -0.0195 0.0042  168 PHE   A CA  
3950 C CA  B PHE   A 168 ? 0.3120 0.4139 0.3576 -0.0253 -0.0178 0.0415  168 PHE   A CA  
3951 C C   A PHE   A 168 ? 0.2344 0.3470 0.3501 0.0056  -0.0003 -0.0009 168 PHE   A C   
3952 C C   B PHE   A 168 ? 0.3543 0.4397 0.4310 -0.0172 -0.0230 0.0386  168 PHE   A C   
3953 O O   A PHE   A 168 ? 0.2389 0.3513 0.3760 0.0052  0.0018  0.0074  168 PHE   A O   
3954 O O   B PHE   A 168 ? 0.3573 0.4419 0.4536 -0.0184 -0.0140 0.0402  168 PHE   A O   
3955 C CB  A PHE   A 168 ? 0.1824 0.3014 0.2400 0.0163  -0.0338 0.0114  168 PHE   A CB  
3956 C CB  B PHE   A 168 ? 0.2859 0.3940 0.3095 -0.0343 -0.0170 0.0474  168 PHE   A CB  
3957 C CG  A PHE   A 168 ? 0.1727 0.2816 0.2111 0.0091  -0.0359 0.0179  168 PHE   A CG  
3958 C CG  B PHE   A 168 ? 0.2615 0.3758 0.2681 -0.0459 -0.0153 0.0524  168 PHE   A CG  
3959 C CD1 A PHE   A 168 ? 0.1666 0.2761 0.2002 0.0057  -0.0455 0.0304  168 PHE   A CD1 
3960 C CD1 B PHE   A 168 ? 0.2487 0.3677 0.2524 -0.0521 -0.0214 0.0568  168 PHE   A CD1 
3961 C CD2 A PHE   A 168 ? 0.1669 0.2699 0.1976 0.0061  -0.0154 0.0109  168 PHE   A CD2 
3962 C CD2 B PHE   A 168 ? 0.2516 0.3676 0.2481 -0.0519 -0.0060 0.0539  168 PHE   A CD2 
3963 C CE1 A PHE   A 168 ? 0.1581 0.2705 0.1910 0.0015  -0.0433 0.0342  168 PHE   A CE1 
3964 C CE1 B PHE   A 168 ? 0.2387 0.3616 0.2379 -0.0590 -0.0208 0.0589  168 PHE   A CE1 
3965 C CE2 A PHE   A 168 ? 0.1645 0.2630 0.1939 0.0010  -0.0105 0.0194  168 PHE   A CE2 
3966 C CE2 B PHE   A 168 ? 0.2457 0.3611 0.2341 -0.0583 -0.0033 0.0605  168 PHE   A CE2 
3967 C CZ  A PHE   A 168 ? 0.1615 0.2668 0.1985 -0.0023 -0.0202 0.0295  168 PHE   A CZ  
3968 C CZ  B PHE   A 168 ? 0.2395 0.3606 0.2351 -0.0596 -0.0099 0.0609  168 PHE   A CZ  
3987 N N   A LEU   A 169 ? 0.2770 0.3659 0.3959 -0.0062 0.0094  -0.0171 169 LEU   A N   
3988 N N   B LEU   A 169 ? 0.3920 0.4616 0.4730 -0.0107 -0.0401 0.0339  169 LEU   A N   
3989 C CA  A LEU   A 169 ? 0.3249 0.3873 0.4461 -0.0136 0.0117  -0.0256 169 LEU   A CA  
3990 C CA  B LEU   A 169 ? 0.4246 0.4837 0.5106 -0.0013 -0.0560 0.0335  169 LEU   A CA  
3991 C C   A LEU   A 169 ? 0.3420 0.3938 0.4710 -0.0207 0.0154  -0.0178 169 LEU   A C   
3992 C C   B LEU   A 169 ? 0.4351 0.4897 0.5253 0.0014  -0.0595 0.0337  169 LEU   A C   
3993 O O   A LEU   A 169 ? 0.3493 0.3981 0.4805 -0.0236 0.0198  -0.0130 169 LEU   A O   
3994 O O   B LEU   A 169 ? 0.4384 0.4913 0.5296 0.0034  -0.0588 0.0341  169 LEU   A O   
3995 C CB  A LEU   A 169 ? 0.3498 0.3993 0.4573 -0.0143 0.0107  -0.0393 169 LEU   A CB  
3996 C CB  B LEU   A 169 ? 0.4409 0.4969 0.5270 0.0042  -0.0679 0.0341  169 LEU   A CB  
3997 C CG  A LEU   A 169 ? 0.3699 0.4084 0.4661 -0.0143 0.0077  -0.0543 169 LEU   A CG  
3998 C CG  B LEU   A 169 ? 0.4520 0.5065 0.5390 0.0069  -0.0773 0.0363  169 LEU   A CG  
3999 C CD1 A LEU   A 169 ? 0.3767 0.4113 0.4731 -0.0134 0.0060  -0.0587 169 LEU   A CD1 
4000 C CD1 B LEU   A 169 ? 0.4550 0.5098 0.5410 0.0079  -0.0811 0.0370  169 LEU   A CD1 
4001 C CD2 A LEU   A 169 ? 0.3765 0.4120 0.4650 -0.0145 0.0080  -0.0599 169 LEU   A CD2 
4002 C CD2 B LEU   A 169 ? 0.4558 0.5095 0.5422 0.0079  -0.0810 0.0370  169 LEU   A CD2 
4003 O OXT A LEU   A 169 ? 0.3405 0.3923 0.4708 -0.0237 0.0176  -0.0180 169 LEU   A OXT 
4004 O OXT B LEU   A 169 ? 0.4394 0.4920 0.5301 -0.0006 -0.0641 0.0337  169 LEU   A OXT 
4027 N N   A SER   B 1   ? 0.3578 0.3347 0.3424 -0.1105 -0.0812 0.0134  1   SER   B N   
4028 N N   B SER   B 1   ? 0.3203 0.3149 0.3326 -0.1220 -0.0693 0.0084  1   SER   B N   
4029 C CA  A SER   B 1   ? 0.3522 0.3388 0.3456 -0.1122 -0.0868 0.0138  1   SER   B CA  
4030 C CA  B SER   B 1   ? 0.3093 0.3226 0.3331 -0.1277 -0.0787 0.0034  1   SER   B CA  
4031 C C   A SER   B 1   ? 0.3360 0.3398 0.3286 -0.1148 -0.0891 0.0381  1   SER   B C   
4032 C C   B SER   B 1   ? 0.2881 0.3284 0.3070 -0.1312 -0.0909 0.0176  1   SER   B C   
4033 O O   A SER   B 1   ? 0.3434 0.3445 0.3209 -0.1098 -0.0844 0.0394  1   SER   B O   
4034 O O   B SER   B 1   ? 0.2951 0.3343 0.3041 -0.1267 -0.0862 0.0092  1   SER   B O   
4035 C CB  A SER   B 1   ? 0.3607 0.3390 0.3624 -0.1105 -0.0829 -0.0041 1   SER   B CB  
4036 C CB  B SER   B 1   ? 0.3174 0.3216 0.3608 -0.1272 -0.0686 -0.0116 1   SER   B CB  
4037 O OG  A SER   B 1   ? 0.3700 0.3446 0.3934 -0.1066 -0.0753 -0.0120 1   SER   B OG  
4038 O OG  B SER   B 1   ? 0.3266 0.3279 0.3974 -0.1244 -0.0617 -0.0147 1   SER   B OG  
4053 N N   A MET   B 2   ? 0.3158 0.3359 0.3212 -0.1182 -0.0862 0.0741  2   MET   B N   
4054 N N   B MET   B 2   ? 0.2702 0.3300 0.2860 -0.1286 -0.0931 0.0569  2   MET   B N   
4055 C CA  A MET   B 2   ? 0.3003 0.3333 0.3305 -0.1125 -0.0852 0.0988  2   MET   B CA  
4056 C CA  B MET   B 2   ? 0.2638 0.3338 0.2861 -0.1122 -0.0921 0.0893  2   MET   B CA  
4057 C C   A MET   B 2   ? 0.2613 0.3059 0.2902 -0.1082 -0.1031 0.1270  2   MET   B C   
4058 C C   B MET   B 2   ? 0.2470 0.3187 0.2739 -0.0992 -0.0945 0.1228  2   MET   B C   
4059 O O   A MET   B 2   ? 0.2514 0.2973 0.2848 -0.1147 -0.1210 0.1356  2   MET   B O   
4060 O O   B MET   B 2   ? 0.2466 0.3357 0.2820 -0.0863 -0.0941 0.1275  2   MET   B O   
4061 C CB  A MET   B 2   ? 0.3281 0.3627 0.4035 -0.1009 -0.0609 0.0790  2   MET   B CB  
4062 C CB  B MET   B 2   ? 0.2812 0.3581 0.3250 -0.0968 -0.0760 0.0801  2   MET   B CB  
4063 C CG  A MET   B 2   ? 0.3553 0.3893 0.4735 -0.0868 -0.0389 0.0657  2   MET   B CG  
4064 C CG  B MET   B 2   ? 0.2983 0.3799 0.3517 -0.0784 -0.0619 0.0845  2   MET   B CG  
4065 S SD  A MET   B 2   ? 0.3812 0.4140 0.5411 -0.0716 -0.0234 0.0552  2   MET   B SD  
4066 S SD  B MET   B 2   ? 0.3162 0.4021 0.3695 -0.0592 -0.0568 0.0915  2   MET   B SD  
4067 C CE  A MET   B 2   ? 0.3865 0.4191 0.5500 -0.0713 -0.0144 0.0541  2   MET   B CE  
4068 C CE  B MET   B 2   ? 0.3187 0.4076 0.3955 -0.0611 -0.0488 0.0818  2   MET   B CE  
4087 N N   . VAL   B 3   ? 0.2278 0.2789 0.2641 -0.1068 -0.0974 0.1406  3   VAL   B N   
4088 C CA  . VAL   B 3   ? 0.2098 0.2338 0.2694 -0.0869 -0.0848 0.1250  3   VAL   B CA  
4089 C C   . VAL   B 3   ? 0.1911 0.2293 0.2294 -0.0711 -0.0711 0.1014  3   VAL   B C   
4090 O O   . VAL   B 3   ? 0.1925 0.2480 0.2281 -0.0692 -0.0701 0.1042  3   VAL   B O   
4091 C CB  . VAL   B 3   ? 0.2202 0.2247 0.3350 -0.0752 -0.0792 0.1002  3   VAL   B CB  
4092 C CG1 . VAL   B 3   ? 0.2286 0.2162 0.3562 -0.0804 -0.0745 0.1042  3   VAL   B CG1 
4093 C CG2 . VAL   B 3   ? 0.2212 0.2266 0.3559 -0.0663 -0.0615 0.1055  3   VAL   B CG2 
4104 N N   . ASN   B 4   ? 0.1730 0.2010 0.1971 -0.0633 -0.0588 0.0790  4   ASN   B N   
4105 C CA  . ASN   B 4   ? 0.1742 0.2000 0.1656 -0.0554 -0.0466 0.0434  4   ASN   B CA  
4106 C C   . ASN   B 4   ? 0.1760 0.2078 0.1701 -0.0554 -0.0401 0.0323  4   ASN   B C   
4107 O O   . ASN   B 4   ? 0.1751 0.2162 0.1906 -0.0497 -0.0399 0.0063  4   ASN   B O   
4108 C CB  . ASN   B 4   ? 0.1738 0.1973 0.1505 -0.0507 -0.0537 0.0296  4   ASN   B CB  
4109 C CG  . ASN   B 4   ? 0.1750 0.1775 0.1457 -0.0463 -0.0480 0.0283  4   ASN   B CG  
4110 O OD1 . ASN   B 4   ? 0.1765 0.1661 0.1564 -0.0437 -0.0491 0.0280  4   ASN   B OD1 
4111 N ND2 . ASN   B 4   ? 0.1949 0.1863 0.1566 -0.0308 -0.0322 0.0233  4   ASN   B ND2 
4118 N N   . SER   B 5   ? 0.1884 0.2198 0.1750 -0.0585 -0.0353 0.0296  5   SER   B N   
4119 C CA  . SER   B 5   ? 0.2126 0.2564 0.1959 -0.0544 -0.0230 0.0304  5   SER   B CA  
4120 C C   . SER   B 5   ? 0.2377 0.2639 0.2294 -0.0762 0.0014  0.0350  5   SER   B C   
4121 O O   . SER   B 5   ? 0.2587 0.2539 0.2880 -0.0654 0.0341  0.0261  5   SER   B O   
4122 C CB  . SER   B 5   ? 0.2240 0.2770 0.2299 -0.0435 -0.0078 0.0437  5   SER   B CB  
4123 O OG  . SER   B 5   ? 0.2510 0.3081 0.2970 -0.0283 -0.0031 0.0468  5   SER   B OG  
4129 N N   . PHE   B 6   ? 0.2634 0.2973 0.2227 -0.0846 0.0175  0.0489  6   PHE   B N   
4130 C CA  . PHE   B 6   ? 0.2840 0.3146 0.1848 -0.1044 0.0283  0.0353  6   PHE   B CA  
4131 C C   . PHE   B 6   ? 0.3456 0.3652 0.2361 -0.1134 0.0656  0.0119  6   PHE   B C   
4132 O O   . PHE   B 6   ? 0.3583 0.3964 0.2732 -0.1047 0.0545  -0.0064 6   PHE   B O   
4133 C CB  . PHE   B 6   ? 0.2507 0.2902 0.1666 -0.0970 0.0068  0.0342  6   PHE   B CB  
4134 C CG  . PHE   B 6   ? 0.2149 0.2570 0.1694 -0.0868 -0.0081 0.0342  6   PHE   B CG  
4135 C CD1 . PHE   B 6   ? 0.2092 0.2293 0.1503 -0.0809 -0.0180 0.0292  6   PHE   B CD1 
4136 C CD2 . PHE   B 6   ? 0.1891 0.2512 0.1771 -0.0717 -0.0176 0.0517  6   PHE   B CD2 
4137 C CE1 . PHE   B 6   ? 0.2012 0.2023 0.1607 -0.0678 -0.0275 0.0217  6   PHE   B CE1 
4138 C CE2 . PHE   B 6   ? 0.1864 0.2300 0.2020 -0.0589 -0.0045 0.0526  6   PHE   B CE2 
4139 C CZ  . PHE   B 6   ? 0.1879 0.2100 0.1883 -0.0574 -0.0192 0.0285  6   PHE   B CZ  
4149 N N   . SER   B 7   ? 0.3949 0.3692 0.2679 -0.1380 0.1120  0.0019  7   SER   B N   
4150 C CA  . SER   B 7   ? 0.4446 0.3971 0.3361 -0.1433 0.1465  -0.0051 7   SER   B CA  
4151 C C   . SER   B 7   ? 0.4413 0.3620 0.3048 -0.1483 0.1539  -0.0364 7   SER   B C   
4152 O O   . SER   B 7   ? 0.4489 0.3536 0.3244 -0.1532 0.1469  -0.0456 7   SER   B O   
4153 C CB  . SER   B 7   ? 0.4783 0.4417 0.4325 -0.1438 0.1736  0.0152  7   SER   B CB  
4154 O OG  . SER   B 7   ? 0.4860 0.4646 0.5066 -0.1432 0.1826  0.0251  7   SER   B OG  
4160 N N   . GLY   B 8   ? 0.4353 0.3389 0.2907 -0.1345 0.1529  -0.0599 8   GLY   B N   
4161 C CA  . GLY   B 8   ? 0.4198 0.3127 0.2806 -0.1242 0.1518  -0.0695 8   GLY   B CA  
4162 C C   . GLY   B 8   ? 0.3970 0.2793 0.2668 -0.1172 0.1490  -0.0684 8   GLY   B C   
4163 O O   . GLY   B 8   ? 0.4053 0.2827 0.3042 -0.1115 0.1513  -0.0698 8   GLY   B O   
4167 N N   . TYR   B 9   ? 0.3759 0.2519 0.2393 -0.1033 0.1181  -0.0816 9   TYR   B N   
4168 C CA  . TYR   B 9   ? 0.3516 0.2174 0.2171 -0.0925 0.0877  -0.0618 9   TYR   B CA  
4169 C C   . TYR   B 9   ? 0.3415 0.2171 0.2132 -0.0854 0.0583  -0.0462 9   TYR   B C   
4170 O O   . TYR   B 9   ? 0.3484 0.2356 0.2523 -0.0865 0.0583  -0.0302 9   TYR   B O   
4171 C CB  . TYR   B 9   ? 0.3442 0.1913 0.2242 -0.0840 0.0796  -0.0522 9   TYR   B CB  
4172 C CG  . TYR   B 9   ? 0.3325 0.1718 0.2295 -0.0866 0.0704  -0.0498 9   TYR   B CG  
4173 C CD1 . TYR   B 9   ? 0.3323 0.1686 0.2402 -0.0961 0.0740  -0.0452 9   TYR   B CD1 
4174 C CD2 . TYR   B 9   ? 0.3163 0.1688 0.2157 -0.0784 0.0634  -0.0471 9   TYR   B CD2 
4175 C CE1 . TYR   B 9   ? 0.3253 0.1792 0.2323 -0.0972 0.0782  -0.0599 9   TYR   B CE1 
4176 C CE2 . TYR   B 9   ? 0.3152 0.1701 0.2236 -0.0772 0.0675  -0.0428 9   TYR   B CE2 
4177 C CZ  . TYR   B 9   ? 0.3178 0.1821 0.2319 -0.0906 0.0727  -0.0618 9   TYR   B CZ  
4178 O OH  . TYR   B 9   ? 0.3159 0.1975 0.2457 -0.1016 0.0742  -0.0739 9   TYR   B OH  
4188 N N   . LEU   B 10  ? 0.3223 0.1884 0.1948 -0.0864 0.0315  -0.0431 10  LEU   B N   
4189 C CA  . LEU   B 10  ? 0.3171 0.1829 0.1885 -0.0914 -0.0054 -0.0320 10  LEU   B CA  
4190 C C   . LEU   B 10  ? 0.3036 0.1847 0.1929 -0.0836 -0.0252 -0.0302 10  LEU   B C   
4191 O O   . LEU   B 10  ? 0.2857 0.1865 0.1960 -0.0751 -0.0219 -0.0207 10  LEU   B O   
4192 C CB  . LEU   B 10  ? 0.3322 0.1844 0.2023 -0.0927 -0.0256 -0.0160 10  LEU   B CB  
4193 C CG  . LEU   B 10  ? 0.3456 0.1986 0.2346 -0.0888 -0.0518 -0.0058 10  LEU   B CG  
4194 C CD1 . LEU   B 10  ? 0.3536 0.2024 0.2553 -0.0868 -0.0526 -0.0109 10  LEU   B CD1 
4195 C CD2 . LEU   B 10  ? 0.3514 0.2094 0.2541 -0.0886 -0.0490 0.0161  10  LEU   B CD2 
4207 N N   . LYS   B 11  ? 0.3159 0.2088 0.1962 -0.0792 -0.0364 -0.0194 11  LYS   B N   
4208 C CA  . LYS   B 11  ? 0.3306 0.2358 0.2410 -0.0680 -0.0510 -0.0320 11  LYS   B CA  
4209 C C   . LYS   B 11  ? 0.3070 0.2131 0.2390 -0.0857 -0.0461 -0.0398 11  LYS   B C   
4210 O O   . LYS   B 11  ? 0.3204 0.2296 0.2669 -0.0988 -0.0437 -0.0706 11  LYS   B O   
4211 C CB  . LYS   B 11  ? 0.3685 0.2887 0.3218 -0.0404 -0.0567 -0.0348 11  LYS   B CB  
4212 C CG  . LYS   B 11  ? 0.3986 0.3250 0.4078 -0.0241 -0.0590 -0.0395 11  LYS   B CG  
4213 C CD  . LYS   B 11  ? 0.4227 0.3510 0.4860 -0.0142 -0.0580 -0.0429 11  LYS   B CD  
4214 C CE  . LYS   B 11  ? 0.4387 0.3683 0.5440 -0.0101 -0.0592 -0.0463 11  LYS   B CE  
4215 N NZ  . LYS   B 11  ? 0.4467 0.3775 0.5740 -0.0082 -0.0604 -0.0474 11  LYS   B NZ  
4229 N N   . LEU   B 12  ? 0.2682 0.1896 0.2357 -0.0789 -0.0502 -0.0376 12  LEU   B N   
4230 C CA  . LEU   B 12  ? 0.2471 0.1711 0.2483 -0.0669 -0.0401 -0.0262 12  LEU   B CA  
4231 C C   . LEU   B 12  ? 0.2286 0.1743 0.2571 -0.0636 -0.0484 -0.0211 12  LEU   B C   
4232 O O   . LEU   B 12  ? 0.2211 0.1767 0.2818 -0.0675 -0.0585 -0.0141 12  LEU   B O   
4233 C CB  . LEU   B 12  ? 0.2467 0.1542 0.2461 -0.0528 -0.0340 -0.0191 12  LEU   B CB  
4234 C CG  . LEU   B 12  ? 0.2469 0.1506 0.2428 -0.0498 -0.0237 -0.0152 12  LEU   B CG  
4235 C CD1 . LEU   B 12  ? 0.2541 0.1535 0.2373 -0.0372 -0.0256 0.0041  12  LEU   B CD1 
4236 C CD2 . LEU   B 12  ? 0.2541 0.1608 0.2537 -0.0512 -0.0182 -0.0234 12  LEU   B CD2 
4248 N N   . THR   B 13  ? 0.2178 0.1781 0.2605 -0.0636 -0.0543 -0.0295 13  THR   B N   
4249 C CA  . THR   B 13  ? 0.2176 0.1875 0.2479 -0.0714 -0.0687 -0.0153 13  THR   B CA  
4250 C C   . THR   B 13  ? 0.2581 0.2059 0.2653 -0.0777 -0.0891 -0.0110 13  THR   B C   
4251 O O   . THR   B 13  ? 0.2787 0.2108 0.2838 -0.0743 -0.0591 -0.0133 13  THR   B O   
4252 C CB  . THR   B 13  ? 0.1966 0.1901 0.2435 -0.0673 -0.0656 -0.0107 13  THR   B CB  
4253 O OG1 . THR   B 13  ? 0.1856 0.1835 0.2504 -0.0581 -0.0455 -0.0069 13  THR   B OG1 
4254 C CG2 . THR   B 13  ? 0.2039 0.2013 0.2558 -0.0610 -0.0495 -0.0012 13  THR   B CG2 
4262 N N   A ASP   B 14  ? 0.2691 0.2174 0.2810 -0.0827 -0.1037 -0.0002 14  ASP   B N   
4263 N N   B ASP   B 14  ? 0.2696 0.2174 0.2749 -0.0816 -0.1040 0.0061  14  ASP   B N   
4264 C CA  A ASP   B 14  ? 0.2796 0.2315 0.3032 -0.0833 -0.1086 0.0095  14  ASP   B CA  
4265 C CA  B ASP   B 14  ? 0.2808 0.2324 0.2925 -0.0804 -0.1083 0.0212  14  ASP   B CA  
4266 C C   A ASP   B 14  ? 0.2701 0.2164 0.2634 -0.0818 -0.0983 0.0158  14  ASP   B C   
4267 C C   B ASP   B 14  ? 0.2704 0.2161 0.2573 -0.0813 -0.1004 0.0233  14  ASP   B C   
4268 O O   A ASP   B 14  ? 0.2906 0.2299 0.2693 -0.0815 -0.0893 0.0231  14  ASP   B O   
4269 O O   B ASP   B 14  ? 0.2918 0.2281 0.2645 -0.0826 -0.0939 0.0321  14  ASP   B O   
4270 C CB  A ASP   B 14  ? 0.2989 0.2659 0.3750 -0.0793 -0.1164 0.0054  14  ASP   B CB  
4271 C CB  B ASP   B 14  ? 0.3020 0.2697 0.3578 -0.0716 -0.1112 0.0241  14  ASP   B CB  
4272 C CG  A ASP   B 14  ? 0.3165 0.2961 0.4450 -0.0753 -0.1133 -0.0069 14  ASP   B CG  
4273 C CG  B ASP   B 14  ? 0.3219 0.3040 0.4236 -0.0625 -0.1023 0.0155  14  ASP   B CG  
4274 O OD1 A ASP   B 14  ? 0.3228 0.3019 0.4625 -0.0826 -0.1135 -0.0159 14  ASP   B OD1 
4275 O OD1 B ASP   B 14  ? 0.3320 0.3158 0.4390 -0.0616 -0.0948 0.0094  14  ASP   B OD1 
4276 O OD2 A ASP   B 14  ? 0.3220 0.3117 0.4771 -0.0716 -0.1108 -0.0088 14  ASP   B OD2 
4277 O OD2 B ASP   B 14  ? 0.3273 0.3192 0.4546 -0.0604 -0.1011 0.0134  14  ASP   B OD2 
4286 N N   . ASN   B 15  ? 0.2403 0.1937 0.2346 -0.0681 -0.0953 0.0202  15  ASN   B N   
4287 C CA  . ASN   B 15  ? 0.1940 0.1629 0.2185 -0.0465 -0.0688 0.0073  15  ASN   B CA  
4288 C C   . ASN   B 15  ? 0.1706 0.1445 0.2059 -0.0323 -0.0562 0.0018  15  ASN   B C   
4289 O O   . ASN   B 15  ? 0.1632 0.1383 0.2218 -0.0292 -0.0525 -0.0045 15  ASN   B O   
4290 C CB  . ASN   B 15  ? 0.1793 0.1530 0.2311 -0.0239 -0.0662 0.0134  15  ASN   B CB  
4291 C CG  . ASN   B 15  ? 0.1601 0.1523 0.2507 -0.0284 -0.0465 0.0124  15  ASN   B CG  
4292 O OD1 . ASN   B 15  ? 0.1641 0.1845 0.2815 -0.0462 -0.0489 0.0156  15  ASN   B OD1 
4293 N ND2 . ASN   B 15  ? 0.1587 0.1389 0.2344 -0.0160 -0.0173 -0.0086 15  ASN   B ND2 
4301 N N   . VAL   B 16  ? 0.1723 0.1392 0.2099 -0.0389 -0.0624 -0.0021 16  VAL   B N   
4302 C CA  . VAL   B 16  ? 0.1737 0.1388 0.1921 -0.0341 -0.0494 -0.0165 16  VAL   B CA  
4303 C C   . VAL   B 16  ? 0.1746 0.1517 0.1878 -0.0432 -0.0484 -0.0087 16  VAL   B C   
4304 O O   . VAL   B 16  ? 0.1810 0.1586 0.2121 -0.0355 -0.0435 -0.0161 16  VAL   B O   
4305 C CB  . VAL   B 16  ? 0.1698 0.1374 0.2078 -0.0188 -0.0342 -0.0165 16  VAL   B CB  
4306 C CG1 . VAL   B 16  ? 0.1767 0.1373 0.2094 -0.0050 -0.0240 -0.0096 16  VAL   B CG1 
4307 C CG2 . VAL   B 16  ? 0.1712 0.1405 0.2336 -0.0121 -0.0376 -0.0148 16  VAL   B CG2 
4317 N N   . TYR   B 17  ? 0.1861 0.1589 0.1812 -0.0425 -0.0413 -0.0088 17  TYR   B N   
4318 C CA  . TYR   B 17  ? 0.1968 0.1780 0.1770 -0.0535 -0.0395 0.0115  17  TYR   B CA  
4319 C C   . TYR   B 17  ? 0.1856 0.1477 0.1724 -0.0515 -0.0235 -0.0001 17  TYR   B C   
4320 O O   . TYR   B 17  ? 0.1764 0.1559 0.1761 -0.0399 -0.0275 -0.0271 17  TYR   B O   
4321 C CB  . TYR   B 17  ? 0.2323 0.2261 0.2036 -0.0456 -0.0487 0.0441  17  TYR   B CB  
4322 C CG  . TYR   B 17  ? 0.2608 0.2785 0.2533 -0.0405 -0.0706 0.0652  17  TYR   B CG  
4323 C CD1 . TYR   B 17  ? 0.2790 0.2985 0.2846 -0.0380 -0.0809 0.0820  17  TYR   B CD1 
4324 C CD2 . TYR   B 17  ? 0.2826 0.3083 0.2880 -0.0287 -0.0835 0.0709  17  TYR   B CD2 
4325 C CE1 . TYR   B 17  ? 0.2972 0.3268 0.3100 -0.0278 -0.0920 0.0843  17  TYR   B CE1 
4326 C CE2 . TYR   B 17  ? 0.2983 0.3315 0.3116 -0.0159 -0.0983 0.0802  17  TYR   B CE2 
4327 C CZ  . TYR   B 17  ? 0.3091 0.3414 0.3216 -0.0187 -0.1027 0.0837  17  TYR   B CZ  
4328 O OH  . TYR   B 17  ? 0.3218 0.3545 0.3405 -0.0118 -0.1125 0.0784  17  TYR   B OH  
4338 N N   . ILE   B 18  ? 0.1945 0.1514 0.1667 -0.0464 -0.0148 -0.0114 18  ILE   B N   
4339 C CA  . ILE   B 18  ? 0.1977 0.1437 0.1681 -0.0439 -0.0072 -0.0234 18  ILE   B CA  
4340 C C   . ILE   B 18  ? 0.2104 0.1499 0.1623 -0.0563 -0.0040 -0.0294 18  ILE   B C   
4341 O O   . ILE   B 18  ? 0.2317 0.1679 0.1771 -0.0534 0.0025  -0.0337 18  ILE   B O   
4342 C CB  . ILE   B 18  ? 0.1991 0.1486 0.1839 -0.0507 -0.0129 -0.0146 18  ILE   B CB  
4343 C CG1 . ILE   B 18  ? 0.2020 0.1517 0.1906 -0.0546 -0.0091 -0.0096 18  ILE   B CG1 
4344 C CG2 . ILE   B 18  ? 0.2018 0.1565 0.1910 -0.0500 -0.0188 -0.0149 18  ILE   B CG2 
4345 C CD1 . ILE   B 18  ? 0.2050 0.1776 0.2154 -0.0522 -0.0246 0.0165  18  ILE   B CD1 
4357 N N   . LYS   B 19  ? 0.2095 0.1487 0.1776 -0.0366 0.0352  -0.0359 19  LYS   B N   
4358 C CA  . LYS   B 19  ? 0.2217 0.1569 0.1982 -0.0418 0.0303  -0.0459 19  LYS   B CA  
4359 C C   . LYS   B 19  ? 0.2009 0.1518 0.2180 -0.0364 0.0346  -0.0561 19  LYS   B C   
4360 O O   . LYS   B 19  ? 0.1912 0.1557 0.2028 -0.0268 0.0284  -0.0490 19  LYS   B O   
4361 C CB  . LYS   B 19  ? 0.2504 0.1767 0.2105 -0.0488 0.0443  -0.0356 19  LYS   B CB  
4362 C CG  . LYS   B 19  ? 0.2810 0.1997 0.2303 -0.0520 0.0565  -0.0402 19  LYS   B CG  
4363 C CD  . LYS   B 19  ? 0.3085 0.2242 0.2383 -0.0568 0.0717  -0.0343 19  LYS   B CD  
4364 C CE  . LYS   B 19  ? 0.3348 0.2421 0.2594 -0.0620 0.0653  -0.0318 19  LYS   B CE  
4365 N NZ  . LYS   B 19  ? 0.3519 0.2530 0.2601 -0.0642 0.0652  -0.0269 19  LYS   B NZ  
4379 N N   . ASN   B 20  ? 0.1944 0.1691 0.2453 -0.0336 0.0399  -0.0710 20  ASN   B N   
4380 C CA  . ASN   B 20  ? 0.1948 0.1850 0.2717 -0.0247 0.0458  -0.0885 20  ASN   B CA  
4381 C C   . ASN   B 20  ? 0.1935 0.2053 0.2697 -0.0255 0.0578  -0.0929 20  ASN   B C   
4382 O O   . ASN   B 20  ? 0.2090 0.2385 0.2915 -0.0377 0.0550  -0.0917 20  ASN   B O   
4383 C CB  . ASN   B 20  ? 0.2205 0.1923 0.3053 0.0006  0.0347  -0.0904 20  ASN   B CB  
4384 C CG  . ASN   B 20  ? 0.2462 0.1942 0.3309 0.0295  0.0289  -0.0982 20  ASN   B CG  
4385 O OD1 . ASN   B 20  ? 0.2780 0.2205 0.3541 0.0433  0.0262  -0.0969 20  ASN   B OD1 
4386 N ND2 . ASN   B 20  ? 0.2350 0.1909 0.3296 0.0298  0.0174  -0.0868 20  ASN   B ND2 
4393 N N   . ALA   B 21  ? 0.1922 0.1902 0.2625 -0.0328 0.0602  -0.0751 21  ALA   B N   
4394 C CA  . ALA   B 21  ? 0.1989 0.1924 0.2708 -0.0371 0.0505  -0.0587 21  ALA   B CA  
4395 C C   . ALA   B 21  ? 0.1983 0.1662 0.2532 -0.0268 0.0466  -0.0365 21  ALA   B C   
4396 O O   . ALA   B 21  ? 0.2076 0.1557 0.2338 -0.0353 0.0390  -0.0314 21  ALA   B O   
4397 C CB  . ALA   B 21  ? 0.2142 0.2191 0.2931 -0.0535 0.0471  -0.0443 21  ALA   B CB  
4403 N N   . ASP   B 22  ? 0.1883 0.1549 0.2467 -0.0252 0.0373  -0.0338 22  ASP   B N   
4404 C CA  . ASP   B 22  ? 0.1824 0.1492 0.2365 -0.0097 0.0296  -0.0260 22  ASP   B CA  
4405 C C   . ASP   B 22  ? 0.1720 0.1418 0.1914 -0.0204 0.0191  -0.0107 22  ASP   B C   
4406 O O   . ASP   B 22  ? 0.1796 0.1508 0.1910 -0.0130 0.0131  -0.0065 22  ASP   B O   
4407 C CB  . ASP   B 22  ? 0.1883 0.1499 0.2794 0.0028  0.0337  -0.0167 22  ASP   B CB  
4408 C CG  . ASP   B 22  ? 0.1890 0.1705 0.3319 0.0042  0.0099  -0.0143 22  ASP   B CG  
4409 O OD1 . ASP   B 22  ? 0.1960 0.1585 0.3253 0.0024  -0.0165 -0.0048 22  ASP   B OD1 
4410 O OD2 . ASP   B 22  ? 0.1971 0.2021 0.4010 0.0109  -0.0061 -0.0249 22  ASP   B OD2 
4415 N N   . ILE   B 23  ? 0.1777 0.1390 0.1694 -0.0144 0.0074  0.0098  23  ILE   B N   
4416 C CA  . ILE   B 23  ? 0.1664 0.1306 0.1625 -0.0133 0.0011  0.0038  23  ILE   B CA  
4417 C C   . ILE   B 23  ? 0.1583 0.1317 0.1597 -0.0100 -0.0120 0.0041  23  ILE   B C   
4418 O O   . ILE   B 23  ? 0.1495 0.1315 0.1518 -0.0110 -0.0105 0.0010  23  ILE   B O   
4419 C CB  . ILE   B 23  ? 0.1591 0.1384 0.1725 -0.0278 0.0013  0.0151  23  ILE   B CB  
4420 C CG1 . ILE   B 23  ? 0.1606 0.1467 0.1818 -0.0142 0.0068  0.0239  23  ILE   B CG1 
4421 C CG2 . ILE   B 23  ? 0.1720 0.1654 0.1730 -0.0206 -0.0005 0.0091  23  ILE   B CG2 
4422 C CD1 . ILE   B 23  ? 0.1697 0.1582 0.1877 -0.0080 0.0081  0.0253  23  ILE   B CD1 
4434 N N   . VAL   B 24  ? 0.1618 0.1353 0.1577 -0.0119 -0.0118 0.0070  24  VAL   B N   
4435 C CA  . VAL   B 24  ? 0.1546 0.1428 0.1830 -0.0101 -0.0173 0.0019  24  VAL   B CA  
4436 C C   . VAL   B 24  ? 0.1499 0.1429 0.1823 -0.0143 -0.0106 0.0029  24  VAL   B C   
4437 O O   . VAL   B 24  ? 0.1481 0.1552 0.2016 -0.0191 -0.0059 0.0131  24  VAL   B O   
4438 C CB  . VAL   B 24  ? 0.1610 0.1607 0.1859 0.0006  -0.0195 -0.0015 24  VAL   B CB  
4439 C CG1 . VAL   B 24  ? 0.1623 0.1648 0.2051 -0.0143 -0.0231 -0.0094 24  VAL   B CG1 
4440 C CG2 . VAL   B 24  ? 0.1674 0.1889 0.1863 0.0028  -0.0194 -0.0072 24  VAL   B CG2 
4450 N N   . GLU   B 25  ? 0.1709 0.1574 0.1897 -0.0142 0.0043  0.0060  25  GLU   B N   
4451 C CA  . GLU   B 25  ? 0.1812 0.1870 0.2127 -0.0031 0.0199  0.0000  25  GLU   B CA  
4452 C C   . GLU   B 25  ? 0.1769 0.1784 0.1823 -0.0160 0.0199  0.0003  25  GLU   B C   
4453 O O   . GLU   B 25  ? 0.1851 0.1924 0.1966 -0.0181 0.0245  0.0046  25  GLU   B O   
4454 C CB  . GLU   B 25  ? 0.2218 0.2396 0.2864 0.0233  0.0350  -0.0034 25  GLU   B CB  
4455 C CG  . GLU   B 25  ? 0.2613 0.3133 0.4070 0.0302  0.0333  -0.0075 25  GLU   B CG  
4456 C CD  . GLU   B 25  ? 0.2995 0.3740 0.5024 0.0280  0.0306  -0.0091 25  GLU   B CD  
4457 O OE1 . GLU   B 25  ? 0.3226 0.3945 0.5345 0.0311  0.0339  -0.0094 25  GLU   B OE1 
4458 O OE2 . GLU   B 25  ? 0.3141 0.3914 0.5320 0.0275  0.0260  -0.0128 25  GLU   B OE2 
4465 N N   . GLU   B 26  ? 0.1694 0.1643 0.1630 -0.0310 0.0170  -0.0012 26  GLU   B N   
4466 C CA  . GLU   B 26  ? 0.1756 0.1837 0.1698 -0.0384 -0.0023 0.0042  26  GLU   B CA  
4467 C C   . GLU   B 26  ? 0.1595 0.1797 0.1543 -0.0309 0.0089  0.0231  26  GLU   B C   
4468 O O   . GLU   B 26  ? 0.1824 0.1952 0.1674 -0.0254 0.0023  0.0221  26  GLU   B O   
4469 C CB  . GLU   B 26  ? 0.2076 0.2000 0.1799 -0.0496 0.0090  0.0150  26  GLU   B CB  
4470 C CG  . GLU   B 26  ? 0.2509 0.2373 0.2495 -0.0598 0.0198  -0.0097 26  GLU   B CG  
4471 C CD  . GLU   B 26  ? 0.2751 0.2584 0.2598 -0.0845 0.0323  -0.0457 26  GLU   B CD  
4472 O OE1 . GLU   B 26  ? 0.2975 0.2455 0.2764 -0.0962 0.0743  -0.0423 26  GLU   B OE1 
4473 O OE2 . GLU   B 26  ? 0.2831 0.2976 0.3126 -0.0742 0.0255  -0.0362 26  GLU   B OE2 
4480 N N   . ALA   B 27  ? 0.1464 0.1583 0.1555 -0.0279 0.0069  0.0180  27  ALA   B N   
4481 C CA  . ALA   B 27  ? 0.1505 0.1577 0.1700 -0.0195 -0.0005 0.0299  27  ALA   B CA  
4482 C C   . ALA   B 27  ? 0.1509 0.1693 0.1971 -0.0186 0.0046  0.0412  27  ALA   B C   
4483 O O   . ALA   B 27  ? 0.1544 0.1760 0.2085 -0.0044 0.0070  0.0512  27  ALA   B O   
4484 C CB  . ALA   B 27  ? 0.1656 0.1437 0.1761 -0.0217 0.0038  0.0265  27  ALA   B CB  
4490 N N   . LYS   B 28  ? 0.1422 0.1867 0.2326 -0.0206 0.0160  0.0650  28  LYS   B N   
4491 C CA  . LYS   B 28  ? 0.1643 0.2288 0.2584 -0.0093 0.0519  0.0940  28  LYS   B CA  
4492 C C   . LYS   B 28  ? 0.1880 0.2388 0.2368 -0.0009 0.0636  0.0766  28  LYS   B C   
4493 O O   . LYS   B 28  ? 0.2124 0.2413 0.2485 0.0002  0.0670  0.0677  28  LYS   B O   
4494 C CB  . LYS   B 28  ? 0.1883 0.2743 0.3315 0.0035  0.0773  0.1275  28  LYS   B CB  
4495 C CG  . LYS   B 28  ? 0.2192 0.3358 0.3887 0.0141  0.0887  0.1570  28  LYS   B CG  
4496 C CD  . LYS   B 28  ? 0.2688 0.4066 0.4529 0.0211  0.1050  0.1732  28  LYS   B CD  
4497 C CE  . LYS   B 28  ? 0.3260 0.4574 0.5127 0.0306  0.1012  0.1818  28  LYS   B CE  
4498 N NZ  . LYS   B 28  ? 0.3651 0.4808 0.5390 0.0378  0.0954  0.1898  28  LYS   B NZ  
4512 N N   . LYS   B 29  ? 0.2022 0.2607 0.2360 0.0152  0.0633  0.0627  29  LYS   B N   
4513 C CA  . LYS   B 29  ? 0.2484 0.2916 0.2649 0.0166  0.0562  0.0602  29  LYS   B CA  
4514 C C   . LYS   B 29  ? 0.2384 0.2842 0.2270 0.0103  0.0364  0.0670  29  LYS   B C   
4515 O O   . LYS   B 29  ? 0.2565 0.3061 0.2339 0.0198  0.0328  0.0749  29  LYS   B O   
4516 C CB  . LYS   B 29  ? 0.3080 0.3326 0.3549 0.0185  0.0624  0.0469  29  LYS   B CB  
4517 C CG  . LYS   B 29  ? 0.3580 0.3686 0.4479 0.0192  0.0746  0.0382  29  LYS   B CG  
4518 C CD  . LYS   B 29  ? 0.4015 0.3948 0.5204 0.0179  0.0912  0.0283  29  LYS   B CD  
4519 C CE  . LYS   B 29  ? 0.4324 0.4123 0.5666 0.0164  0.1073  0.0211  29  LYS   B CE  
4520 N NZ  . LYS   B 29  ? 0.4461 0.4225 0.5938 0.0154  0.1139  0.0167  29  LYS   B NZ  
4534 N N   . VAL   B 30  ? 0.2055 0.2559 0.2099 -0.0098 0.0194  0.0610  30  VAL   B N   
4535 C CA  . VAL   B 30  ? 0.1969 0.2423 0.2393 -0.0226 -0.0131 0.0588  30  VAL   B CA  
4536 C C   . VAL   B 30  ? 0.1714 0.2295 0.2196 -0.0233 -0.0104 0.0669  30  VAL   B C   
4537 O O   . VAL   B 30  ? 0.1837 0.2440 0.2099 -0.0206 -0.0089 0.0734  30  VAL   B O   
4538 C CB  . VAL   B 30  ? 0.2106 0.2414 0.3012 -0.0364 -0.0299 0.0681  30  VAL   B CB  
4539 C CG1 . VAL   B 30  ? 0.2239 0.2547 0.3071 -0.0319 -0.0209 0.0608  30  VAL   B CG1 
4540 C CG2 . VAL   B 30  ? 0.2225 0.2399 0.3238 -0.0415 -0.0368 0.0572  30  VAL   B CG2 
4550 N N   A LYS   B 31  ? 0.1659 0.2066 0.2341 -0.0320 -0.0066 0.0765  31  LYS   B N   
4551 N N   B LYS   B 31  ? 0.1638 0.2046 0.2324 -0.0340 -0.0061 0.0750  31  LYS   B N   
4552 C CA  A LYS   B 31  ? 0.1624 0.2082 0.2591 -0.0355 -0.0098 0.0760  31  LYS   B CA  
4553 C CA  B LYS   B 31  ? 0.1589 0.2070 0.2568 -0.0383 -0.0102 0.0717  31  LYS   B CA  
4554 C C   A LYS   B 31  ? 0.1548 0.1756 0.2248 -0.0357 -0.0259 0.0685  31  LYS   B C   
4555 C C   B LYS   B 31  ? 0.1521 0.1746 0.2236 -0.0374 -0.0263 0.0658  31  LYS   B C   
4556 O O   A LYS   B 31  ? 0.1546 0.1820 0.2318 -0.0285 -0.0217 0.0787  31  LYS   B O   
4557 O O   B LYS   B 31  ? 0.1518 0.1816 0.2304 -0.0296 -0.0225 0.0746  31  LYS   B O   
4558 C CB  A LYS   B 31  ? 0.1747 0.2466 0.3026 -0.0353 0.0091  0.0847  31  LYS   B CB  
4559 C CB  B LYS   B 31  ? 0.1706 0.2470 0.2964 -0.0385 0.0077  0.0759  31  LYS   B CB  
4560 C CG  A LYS   B 31  ? 0.1962 0.2825 0.3490 -0.0370 0.0178  0.0821  31  LYS   B CG  
4561 C CG  B LYS   B 31  ? 0.1930 0.2849 0.3400 -0.0403 0.0130  0.0680  31  LYS   B CG  
4562 C CD  A LYS   B 31  ? 0.2184 0.3202 0.3946 -0.0345 0.0154  0.0740  31  LYS   B CD  
4563 C CD  B LYS   B 31  ? 0.2158 0.3242 0.3863 -0.0398 0.0078  0.0588  31  LYS   B CD  
4564 C CE  A LYS   B 31  ? 0.2345 0.3466 0.4333 -0.0331 0.0088  0.0645  31  LYS   B CE  
4565 C CE  B LYS   B 31  ? 0.2310 0.3504 0.4275 -0.0402 -0.0004 0.0493  31  LYS   B CE  
4566 N NZ  A LYS   B 31  ? 0.2470 0.3583 0.4511 -0.0265 0.0007  0.0553  31  LYS   B NZ  
4567 N NZ  B LYS   B 31  ? 0.2429 0.3615 0.4454 -0.0338 -0.0118 0.0399  31  LYS   B NZ  
4594 N N   . PRO   B 32  ? 0.1594 0.1475 0.1892 -0.0384 -0.0423 0.0459  32  PRO   B N   
4595 C CA  . PRO   B 32  ? 0.1703 0.1416 0.1484 -0.0320 -0.0440 0.0249  32  PRO   B CA  
4596 C C   . PRO   B 32  ? 0.1795 0.1350 0.1503 -0.0383 -0.0530 0.0295  32  PRO   B C   
4597 O O   . PRO   B 32  ? 0.1901 0.1355 0.1880 -0.0372 -0.0660 0.0291  32  PRO   B O   
4598 C CB  . PRO   B 32  ? 0.1899 0.1396 0.1534 -0.0386 -0.0324 0.0085  32  PRO   B CB  
4599 C CG  . PRO   B 32  ? 0.2034 0.1326 0.1537 -0.0262 -0.0484 0.0227  32  PRO   B CG  
4600 C CD  . PRO   B 32  ? 0.1858 0.1402 0.1746 -0.0220 -0.0547 0.0251  32  PRO   B CD  
4608 N N   . THR   B 33  ? 0.1869 0.1240 0.1453 -0.0349 -0.0491 0.0222  33  THR   B N   
4609 C CA  . THR   B 33  ? 0.1991 0.1302 0.1410 -0.0393 -0.0446 0.0285  33  THR   B CA  
4610 C C   . THR   B 33  ? 0.1961 0.1235 0.1368 -0.0379 -0.0507 0.0173  33  THR   B C   
4611 O O   . THR   B 33  ? 0.2174 0.1301 0.1498 -0.0498 -0.0551 0.0200  33  THR   B O   
4612 C CB  . THR   B 33  ? 0.2062 0.1415 0.1401 -0.0251 -0.0465 0.0292  33  THR   B CB  
4613 O OG1 . THR   B 33  ? 0.1891 0.1482 0.1510 -0.0286 -0.0422 0.0322  33  THR   B OG1 
4614 C CG2 . THR   B 33  ? 0.2337 0.1497 0.1607 -0.0173 -0.0418 0.0223  33  THR   B CG2 
4622 N N   . VAL   B 34  ? 0.1758 0.1250 0.1323 -0.0342 -0.0444 0.0172  34  VAL   B N   
4623 C CA  . VAL   B 34  ? 0.1622 0.1271 0.1301 -0.0318 -0.0394 0.0098  34  VAL   B CA  
4624 C C   . VAL   B 34  ? 0.1455 0.1215 0.1168 -0.0352 -0.0232 0.0100  34  VAL   B C   
4625 O O   . VAL   B 34  ? 0.1672 0.1259 0.1128 -0.0320 -0.0350 0.0117  34  VAL   B O   
4626 C CB  . VAL   B 34  ? 0.1671 0.1315 0.1561 -0.0140 -0.0234 0.0066  34  VAL   B CB  
4627 C CG1 . VAL   B 34  ? 0.1559 0.1457 0.1633 -0.0106 -0.0126 -0.0008 34  VAL   B CG1 
4628 C CG2 . VAL   B 34  ? 0.1740 0.1344 0.1782 -0.0134 -0.0224 0.0083  34  VAL   B CG2 
4638 N N   . VAL   B 35  ? 0.1424 0.1144 0.0998 -0.0310 -0.0202 0.0117  35  VAL   B N   
4639 C CA  . VAL   B 35  ? 0.1370 0.1144 0.1033 -0.0218 -0.0153 0.0094  35  VAL   B CA  
4640 C C   . VAL   B 35  ? 0.1239 0.1108 0.1135 -0.0192 -0.0145 0.0086  35  VAL   B C   
4641 O O   . VAL   B 35  ? 0.1308 0.1195 0.1102 -0.0276 -0.0028 -0.0039 35  VAL   B O   
4642 C CB  . VAL   B 35  ? 0.1369 0.1366 0.1110 -0.0201 0.0038  0.0067  35  VAL   B CB  
4643 C CG1 . VAL   B 35  ? 0.1284 0.1463 0.1313 -0.0291 0.0004  0.0036  35  VAL   B CG1 
4644 C CG2 . VAL   B 35  ? 0.1412 0.1337 0.1311 -0.0084 0.0002  0.0046  35  VAL   B CG2 
4654 N N   . VAL   B 36  ? 0.1277 0.1142 0.1094 -0.0220 -0.0190 0.0150  36  VAL   B N   
4655 C CA  . VAL   B 36  ? 0.1251 0.1094 0.1109 -0.0169 -0.0071 0.0100  36  VAL   B CA  
4656 C C   . VAL   B 36  ? 0.1196 0.1139 0.0908 -0.0082 -0.0041 0.0060  36  VAL   B C   
4657 O O   . VAL   B 36  ? 0.1294 0.1201 0.1225 -0.0113 -0.0056 -0.0054 36  VAL   B O   
4658 C CB  . VAL   B 36  ? 0.1205 0.1224 0.1164 -0.0187 -0.0030 0.0062  36  VAL   B CB  
4659 C CG1 . VAL   B 36  ? 0.1197 0.1358 0.1253 -0.0163 -0.0076 0.0069  36  VAL   B CG1 
4660 C CG2 . VAL   B 36  ? 0.1267 0.1296 0.1276 -0.0162 -0.0147 0.0149  36  VAL   B CG2 
4670 N N   . ASN   B 37  ? 0.1222 0.1163 0.0960 -0.0039 -0.0063 0.0050  37  ASN   B N   
4671 C CA  . ASN   B 37  ? 0.1259 0.1159 0.1055 0.0017  -0.0092 0.0086  37  ASN   B CA  
4672 C C   . ASN   B 37  ? 0.1260 0.1214 0.1117 0.0054  -0.0058 0.0001  37  ASN   B C   
4673 O O   . ASN   B 37  ? 0.1317 0.1281 0.1136 0.0025  0.0052  0.0117  37  ASN   B O   
4674 C CB  . ASN   B 37  ? 0.1219 0.1149 0.1077 0.0001  -0.0138 0.0058  37  ASN   B CB  
4675 C CG  . ASN   B 37  ? 0.1242 0.1174 0.1167 -0.0005 -0.0097 0.0036  37  ASN   B CG  
4676 O OD1 . ASN   B 37  ? 0.1359 0.1229 0.1382 0.0057  -0.0197 0.0001  37  ASN   B OD1 
4677 N ND2 . ASN   B 37  ? 0.1317 0.1191 0.1145 0.0012  -0.0174 0.0072  37  ASN   B ND2 
4684 N N   . ALA   B 38  ? 0.1351 0.1150 0.1116 0.0062  0.0048  0.0082  38  ALA   B N   
4685 C CA  . ALA   B 38  ? 0.1419 0.1210 0.1103 -0.0013 0.0051  0.0082  38  ALA   B CA  
4686 C C   . ALA   B 38  ? 0.1356 0.1145 0.1139 0.0036  0.0039  0.0123  38  ALA   B C   
4687 O O   . ALA   B 38  ? 0.1505 0.1279 0.1286 0.0099  0.0016  0.0112  38  ALA   B O   
4688 C CB  . ALA   B 38  ? 0.1660 0.1338 0.1211 -0.0077 0.0013  0.0025  38  ALA   B CB  
4694 N N   . ALA   B 39  ? 0.1400 0.1206 0.1068 0.0093  0.0018  0.0084  39  ALA   B N   
4695 C CA  . ALA   B 39  ? 0.1468 0.1284 0.1133 0.0101  -0.0073 0.0019  39  ALA   B CA  
4696 C C   . ALA   B 39  ? 0.1537 0.1312 0.0905 0.0110  -0.0072 0.0040  39  ALA   B C   
4697 O O   . ALA   B 39  ? 0.1517 0.1412 0.1273 0.0016  -0.0016 0.0084  39  ALA   B O   
4698 C CB  . ALA   B 39  ? 0.1426 0.1301 0.1307 -0.0026 -0.0007 -0.0007 39  ALA   B CB  
4704 N N   . ASN   B 40  ? 0.1517 0.1554 0.0992 0.0032  0.0014  -0.0037 40  ASN   B N   
4705 C CA  . ASN   B 40  ? 0.1623 0.1600 0.1144 0.0052  -0.0047 -0.0039 40  ASN   B CA  
4706 C C   . ASN   B 40  ? 0.1642 0.1567 0.0949 0.0152  -0.0024 0.0007  40  ASN   B C   
4707 O O   . ASN   B 40  ? 0.1617 0.1445 0.1084 0.0176  -0.0130 -0.0027 40  ASN   B O   
4708 C CB  . ASN   B 40  ? 0.1701 0.1576 0.1291 0.0218  -0.0128 0.0130  40  ASN   B CB  
4709 C CG  . ASN   B 40  ? 0.1780 0.1636 0.1642 0.0135  -0.0184 0.0197  40  ASN   B CG  
4710 O OD1 . ASN   B 40  ? 0.1735 0.1594 0.2469 0.0028  -0.0377 0.0228  40  ASN   B OD1 
4711 N ND2 . ASN   B 40  ? 0.1791 0.1618 0.1712 0.0158  -0.0124 0.0169  40  ASN   B ND2 
4718 N N   . VAL   B 41  ? 0.1760 0.1575 0.1030 0.0230  0.0042  -0.0023 41  VAL   B N   
4719 C CA  . VAL   B 41  ? 0.1791 0.1681 0.1075 0.0175  -0.0012 -0.0087 41  VAL   B CA  
4720 C C   . VAL   B 41  ? 0.1783 0.1681 0.1084 0.0229  -0.0101 -0.0049 41  VAL   B C   
4721 O O   . VAL   B 41  ? 0.1702 0.1658 0.1212 0.0196  -0.0124 -0.0084 41  VAL   B O   
4722 C CB  . VAL   B 41  ? 0.1941 0.1895 0.1427 0.0038  0.0194  -0.0165 41  VAL   B CB  
4723 C CG1 . VAL   B 41  ? 0.1871 0.1902 0.1593 0.0016  0.0294  -0.0236 41  VAL   B CG1 
4724 C CG2 . VAL   B 41  ? 0.2033 0.2045 0.1454 -0.0058 0.0257  -0.0149 41  VAL   B CG2 
4734 N N   . TYR   B 42  ? 0.1895 0.1649 0.1153 0.0235  -0.0177 -0.0004 42  TYR   B N   
4735 C CA  . TYR   B 42  ? 0.1919 0.1666 0.1113 0.0243  -0.0276 -0.0122 42  TYR   B CA  
4736 C C   . TYR   B 42  ? 0.1707 0.1576 0.1219 0.0285  -0.0254 -0.0114 42  TYR   B C   
4737 O O   . TYR   B 42  ? 0.1722 0.1697 0.1548 0.0265  -0.0379 -0.0196 42  TYR   B O   
4738 C CB  . TYR   B 42  ? 0.2108 0.1969 0.1367 0.0148  -0.0346 0.0027  42  TYR   B CB  
4739 C CG  . TYR   B 42  ? 0.2061 0.2077 0.1182 -0.0023 -0.0315 0.0122  42  TYR   B CG  
4740 C CD1 . TYR   B 42  ? 0.1987 0.2075 0.0869 -0.0108 -0.0165 0.0091  42  TYR   B CD1 
4741 C CD2 . TYR   B 42  ? 0.2144 0.2137 0.1523 -0.0027 -0.0237 0.0149  42  TYR   B CD2 
4742 C CE1 . TYR   B 42  ? 0.2076 0.2141 0.0906 -0.0102 -0.0151 0.0072  42  TYR   B CE1 
4743 C CE2 . TYR   B 42  ? 0.2142 0.2211 0.1417 -0.0016 0.0041  0.0254  42  TYR   B CE2 
4744 C CZ  . TYR   B 42  ? 0.2221 0.2280 0.1137 0.0084  0.0066  0.0147  42  TYR   B CZ  
4745 O OH  . TYR   B 42  ? 0.2473 0.2385 0.1561 0.0220  0.0002  0.0119  42  TYR   B OH  
4755 N N   . LEU   B 43  ? 0.1553 0.1450 0.1107 0.0165  -0.0130 -0.0121 43  LEU   B N   
4756 C CA  . LEU   B 43  ? 0.1543 0.1446 0.1102 0.0057  -0.0187 -0.0025 43  LEU   B CA  
4757 C C   . LEU   B 43  ? 0.1581 0.1448 0.1152 0.0055  -0.0186 0.0007  43  LEU   B C   
4758 O O   . LEU   B 43  ? 0.1581 0.1431 0.1424 0.0101  -0.0204 0.0020  43  LEU   B O   
4759 C CB  . LEU   B 43  ? 0.1527 0.1350 0.1331 0.0007  -0.0215 -0.0048 43  LEU   B CB  
4760 C CG  . LEU   B 43  ? 0.1594 0.1340 0.1339 0.0049  -0.0319 -0.0065 43  LEU   B CG  
4761 C CD1 . LEU   B 43  ? 0.1707 0.1406 0.1736 -0.0007 -0.0456 -0.0056 43  LEU   B CD1 
4762 C CD2 . LEU   B 43  ? 0.1566 0.1397 0.1461 -0.0027 -0.0274 -0.0058 43  LEU   B CD2 
4774 N N   . LYS   B 44  ? 0.1590 0.1428 0.1224 0.0075  -0.0157 -0.0027 44  LYS   B N   
4775 C CA  . LYS   B 44  ? 0.1741 0.1526 0.1194 0.0167  -0.0138 0.0046  44  LYS   B CA  
4776 C C   . LYS   B 44  ? 0.1725 0.1455 0.1138 0.0123  -0.0158 0.0028  44  LYS   B C   
4777 O O   . LYS   B 44  ? 0.1905 0.1426 0.1458 0.0095  -0.0052 0.0039  44  LYS   B O   
4778 C CB  . LYS   B 44  ? 0.1980 0.1702 0.1388 0.0262  -0.0225 -0.0058 44  LYS   B CB  
4779 C CG  . LYS   B 44  ? 0.2321 0.1969 0.1911 0.0173  -0.0525 0.0025  44  LYS   B CG  
4780 C CD  . LYS   B 44  ? 0.2729 0.2175 0.2699 0.0060  -0.0557 -0.0001 44  LYS   B CD  
4781 C CE  . LYS   B 44  ? 0.3084 0.2438 0.3235 0.0025  -0.0614 0.0136  44  LYS   B CE  
4782 N NZ  . LYS   B 44  ? 0.3175 0.2509 0.3395 0.0043  -0.0722 0.0314  44  LYS   B NZ  
4796 N N   . HIS   B 45  ? 0.1580 0.1448 0.1138 0.0077  -0.0115 0.0053  45  HIS   B N   
4797 C CA  . HIS   B 45  ? 0.1593 0.1440 0.1225 0.0168  -0.0117 -0.0085 45  HIS   B CA  
4798 C C   . HIS   B 45  ? 0.1841 0.1641 0.1603 0.0255  -0.0207 -0.0090 45  HIS   B C   
4799 O O   . HIS   B 45  ? 0.1995 0.1986 0.2039 0.0509  0.0019  -0.0087 45  HIS   B O   
4800 C CB  . HIS   B 45  ? 0.1503 0.1531 0.1139 0.0062  -0.0113 -0.0017 45  HIS   B CB  
4801 C CG  . HIS   B 45  ? 0.1513 0.1496 0.1143 -0.0003 -0.0086 -0.0004 45  HIS   B CG  
4802 N ND1 . HIS   B 45  ? 0.1555 0.1367 0.1327 0.0047  -0.0186 -0.0068 45  HIS   B ND1 
4803 C CD2 . HIS   B 45  ? 0.1633 0.1479 0.1417 -0.0064 -0.0146 0.0014  45  HIS   B CD2 
4804 C CE1 . HIS   B 45  ? 0.1651 0.1302 0.1205 0.0008  -0.0270 -0.0087 45  HIS   B CE1 
4805 N NE2 . HIS   B 45  ? 0.1717 0.1348 0.1330 0.0006  -0.0231 -0.0052 45  HIS   B NE2 
4813 N N   A GLY   B 46  ? 0.1944 0.1614 0.1964 0.0275  -0.0394 0.0025  46  GLY   B N   
4814 N N   B GLY   B 46  ? 0.1962 0.1632 0.1882 0.0286  -0.0407 0.0092  46  GLY   B N   
4815 C CA  A GLY   B 46  ? 0.2056 0.1759 0.2427 0.0233  -0.0469 -0.0004 46  GLY   B CA  
4816 C CA  B GLY   B 46  ? 0.2088 0.1797 0.2263 0.0238  -0.0498 0.0098  46  GLY   B CA  
4817 C C   A GLY   B 46  ? 0.2056 0.1941 0.2871 0.0248  -0.0406 -0.0057 46  GLY   B C   
4818 C C   B GLY   B 46  ? 0.2106 0.2003 0.2692 0.0244  -0.0424 0.0079  46  GLY   B C   
4819 O O   A GLY   B 46  ? 0.2107 0.2049 0.3609 0.0283  -0.0258 -0.0265 46  GLY   B O   
4820 O O   B GLY   B 46  ? 0.2206 0.2164 0.3231 0.0256  -0.0282 0.0062  46  GLY   B O   
4827 N N   . GLY   B 47  ? 0.2052 0.2063 0.2567 0.0130  -0.0302 -0.0050 47  GLY   B N   
4828 C CA  . GLY   B 47  ? 0.1919 0.1766 0.2100 0.0030  -0.0258 -0.0047 47  GLY   B CA  
4829 C C   . GLY   B 47  ? 0.1747 0.1526 0.1731 -0.0001 -0.0073 0.0023  47  GLY   B C   
4830 O O   . GLY   B 47  ? 0.1859 0.1437 0.1810 0.0035  -0.0166 0.0059  47  GLY   B O   
4835 N N   . GLY   B 48  ? 0.1525 0.1410 0.1763 0.0070  -0.0148 0.0094  48  GLY   B N   
4836 C CA  . GLY   B 48  ? 0.1492 0.1358 0.1779 -0.0019 -0.0013 0.0072  48  GLY   B CA  
4837 C C   . GLY   B 48  ? 0.1463 0.1372 0.1600 0.0030  0.0033  0.0007  48  GLY   B C   
4838 O O   . GLY   B 48  ? 0.1366 0.1408 0.1798 0.0064  -0.0087 0.0075  48  GLY   B O   
4842 N N   . VAL   B 49  ? 0.1470 0.1367 0.1521 0.0123  0.0002  0.0036  49  VAL   B N   
4843 C CA  . VAL   B 49  ? 0.1435 0.1446 0.1457 0.0168  -0.0099 -0.0073 49  VAL   B CA  
4844 C C   . VAL   B 49  ? 0.1316 0.1350 0.1284 0.0166  -0.0030 -0.0012 49  VAL   B C   
4845 O O   . VAL   B 49  ? 0.1460 0.1435 0.1414 0.0060  -0.0048 -0.0007 49  VAL   B O   
4846 C CB  . VAL   B 49  ? 0.1475 0.1643 0.1611 0.0053  -0.0243 -0.0064 49  VAL   B CB  
4847 C CG1 . VAL   B 49  ? 0.1456 0.1801 0.1606 0.0079  -0.0267 0.0028  49  VAL   B CG1 
4848 C CG2 . VAL   B 49  ? 0.1657 0.1839 0.1795 -0.0024 -0.0336 -0.0105 49  VAL   B CG2 
4858 N N   . ALA   B 50  ? 0.1341 0.1309 0.1275 -0.0000 0.0027  0.0045  50  ALA   B N   
4859 C CA  . ALA   B 50  ? 0.1362 0.1215 0.1357 0.0051  -0.0017 0.0056  50  ALA   B CA  
4860 C C   . ALA   B 50  ? 0.1409 0.1306 0.1311 0.0059  -0.0009 0.0054  50  ALA   B C   
4861 O O   . ALA   B 50  ? 0.1434 0.1311 0.1273 0.0098  -0.0012 -0.0041 50  ALA   B O   
4862 C CB  . ALA   B 50  ? 0.1420 0.1262 0.1350 -0.0002 -0.0045 0.0065  50  ALA   B CB  
4868 N N   . GLY   B 51  ? 0.1426 0.1397 0.1415 0.0129  -0.0121 0.0093  51  GLY   B N   
4869 C CA  . GLY   B 51  ? 0.1428 0.1522 0.1561 0.0167  -0.0184 0.0066  51  GLY   B CA  
4870 C C   . GLY   B 51  ? 0.1423 0.1447 0.1556 0.0218  -0.0131 0.0012  51  GLY   B C   
4871 O O   . GLY   B 51  ? 0.1412 0.1549 0.1800 0.0165  -0.0136 -0.0060 51  GLY   B O   
4875 N N   . ALA   B 52  ? 0.1371 0.1412 0.1413 0.0182  -0.0096 0.0002  52  ALA   B N   
4876 C CA  . ALA   B 52  ? 0.1439 0.1431 0.1494 0.0215  0.0011  -0.0097 52  ALA   B CA  
4877 C C   . ALA   B 52  ? 0.1355 0.1460 0.1419 0.0120  0.0030  -0.0078 52  ALA   B C   
4878 O O   . ALA   B 52  ? 0.1349 0.1494 0.1643 0.0088  -0.0029 -0.0050 52  ALA   B O   
4879 C CB  . ALA   B 52  ? 0.1582 0.1440 0.1632 0.0091  0.0027  -0.0104 52  ALA   B CB  
4885 N N   . LEU   B 53  ? 0.1305 0.1463 0.1340 0.0147  -0.0036 0.0009  53  LEU   B N   
4886 C CA  . LEU   B 53  ? 0.1325 0.1504 0.1272 0.0127  -0.0065 -0.0037 53  LEU   B CA  
4887 C C   . LEU   B 53  ? 0.1372 0.1408 0.1311 0.0127  -0.0032 -0.0019 53  LEU   B C   
4888 O O   . LEU   B 53  ? 0.1418 0.1481 0.1498 0.0037  0.0073  0.0044  53  LEU   B O   
4889 C CB  . LEU   B 53  ? 0.1333 0.1510 0.1443 0.0104  0.0015  0.0076  53  LEU   B CB  
4890 C CG  . LEU   B 53  ? 0.1286 0.1572 0.1431 0.0042  -0.0021 0.0146  53  LEU   B CG  
4891 C CD1 . LEU   B 53  ? 0.1423 0.1802 0.1666 0.0167  -0.0037 -0.0010 53  LEU   B CD1 
4892 C CD2 . LEU   B 53  ? 0.1421 0.1893 0.1700 -0.0073 -0.0106 -0.0132 53  LEU   B CD2 
4904 N N   . ASN   B 54  ? 0.1373 0.1313 0.1332 0.0048  -0.0110 -0.0003 54  ASN   B N   
4905 C CA  . ASN   B 54  ? 0.1382 0.1481 0.1368 0.0071  -0.0105 -0.0042 54  ASN   B CA  
4906 C C   . ASN   B 54  ? 0.1351 0.1489 0.1584 0.0039  0.0000  -0.0015 54  ASN   B C   
4907 O O   . ASN   B 54  ? 0.1302 0.1504 0.1689 0.0007  0.0002  -0.0020 54  ASN   B O   
4908 C CB  . ASN   B 54  ? 0.1421 0.1555 0.1508 0.0045  -0.0012 -0.0015 54  ASN   B CB  
4909 C CG  . ASN   B 54  ? 0.1434 0.1581 0.1497 0.0049  -0.0093 -0.0016 54  ASN   B CG  
4910 O OD1 . ASN   B 54  ? 0.1396 0.1584 0.1587 0.0016  -0.0141 -0.0191 54  ASN   B OD1 
4911 N ND2 . ASN   B 54  ? 0.1573 0.1792 0.1818 -0.0026 -0.0254 0.0124  54  ASN   B ND2 
4918 N N   . LYS   B 55  ? 0.1341 0.1537 0.1750 0.0114  0.0002  -0.0023 55  LYS   B N   
4919 C CA  . LYS   B 55  ? 0.1430 0.1710 0.1913 0.0224  -0.0048 -0.0052 55  LYS   B CA  
4920 C C   . LYS   B 55  ? 0.1367 0.1696 0.1883 0.0152  0.0037  -0.0165 55  LYS   B C   
4921 O O   . LYS   B 55  ? 0.1347 0.1787 0.2039 0.0106  0.0003  -0.0117 55  LYS   B O   
4922 C CB  . LYS   B 55  ? 0.1572 0.1808 0.2359 0.0343  0.0103  0.0064  55  LYS   B CB  
4923 C CG  . LYS   B 55  ? 0.1909 0.2056 0.3178 0.0418  0.0293  0.0203  55  LYS   B CG  
4924 C CD  . LYS   B 55  ? 0.2295 0.2318 0.3952 0.0524  0.0440  0.0328  55  LYS   B CD  
4925 C CE  . LYS   B 55  ? 0.2529 0.2512 0.4639 0.0556  0.0565  0.0365  55  LYS   B CE  
4926 N NZ  . LYS   B 55  ? 0.2608 0.2676 0.5012 0.0539  0.0435  0.0484  55  LYS   B NZ  
4940 N N   . ALA   B 56  ? 0.1361 0.1758 0.1587 0.0123  -0.0001 -0.0161 56  ALA   B N   
4941 C CA  . ALA   B 56  ? 0.1491 0.1921 0.1644 0.0057  0.0018  -0.0128 56  ALA   B CA  
4942 C C   . ALA   B 56  ? 0.1486 0.1873 0.1591 0.0040  0.0119  -0.0081 56  ALA   B C   
4943 O O   . ALA   B 56  ? 0.1579 0.1935 0.1812 0.0048  0.0238  -0.0044 56  ALA   B O   
4944 C CB  . ALA   B 56  ? 0.1613 0.2082 0.1623 -0.0105 0.0033  -0.0175 56  ALA   B CB  
4950 N N   . THR   B 57  ? 0.1431 0.1739 0.1686 0.0052  0.0197  -0.0039 57  THR   B N   
4951 C CA  . THR   B 57  ? 0.1492 0.1725 0.1610 0.0009  0.0226  0.0005  57  THR   B CA  
4952 C C   . THR   B 57  ? 0.1497 0.1779 0.1834 -0.0026 0.0251  -0.0020 57  THR   B C   
4953 O O   . THR   B 57  ? 0.1554 0.1766 0.1901 -0.0221 0.0137  -0.0054 57  THR   B O   
4954 C CB  . THR   B 57  ? 0.1535 0.1556 0.1435 -0.0033 0.0136  0.0123  57  THR   B CB  
4955 O OG1 . THR   B 57  ? 0.1479 0.1486 0.1695 -0.0057 0.0097  0.0027  57  THR   B OG1 
4956 C CG2 . THR   B 57  ? 0.1531 0.1566 0.1466 -0.0010 0.0126  0.0121  57  THR   B CG2 
4964 N N   . ASN   B 58  ? 0.1398 0.1981 0.2200 -0.0146 0.0108  -0.0249 58  ASN   B N   
4965 C CA  . ASN   B 58  ? 0.1551 0.2361 0.2639 -0.0260 0.0300  -0.0244 58  ASN   B CA  
4966 C C   . ASN   B 58  ? 0.1363 0.2150 0.2143 -0.0131 -0.0017 -0.0187 58  ASN   B C   
4967 O O   . ASN   B 58  ? 0.1442 0.2225 0.2185 -0.0158 -0.0016 -0.0238 58  ASN   B O   
4968 C CB  . ASN   B 58  ? 0.2306 0.3010 0.3811 -0.0446 0.0813  -0.0150 58  ASN   B CB  
4969 C CG  . ASN   B 58  ? 0.3301 0.3656 0.5241 -0.0501 0.1105  0.0129  58  ASN   B CG  
4970 O OD1 . ASN   B 58  ? 0.3534 0.3883 0.5805 -0.0496 0.1118  0.0179  58  ASN   B OD1 
4971 N ND2 . ASN   B 58  ? 0.4097 0.4097 0.5731 -0.0547 0.1240  0.0217  58  ASN   B ND2 
4978 N N   . ASN   B 59  ? 0.1365 0.1981 0.1867 -0.0088 -0.0078 -0.0048 59  ASN   B N   
4979 C CA  . ASN   B 59  ? 0.1429 0.1971 0.1762 -0.0077 -0.0182 0.0035  59  ASN   B CA  
4980 C C   . ASN   B 59  ? 0.1373 0.1868 0.1645 -0.0123 -0.0198 -0.0101 59  ASN   B C   
4981 O O   . ASN   B 59  ? 0.1377 0.1888 0.1691 -0.0120 -0.0112 -0.0088 59  ASN   B O   
4982 C CB  . ASN   B 59  ? 0.1531 0.2154 0.1863 -0.0024 -0.0245 0.0012  59  ASN   B CB  
4983 C CG  . ASN   B 59  ? 0.1621 0.2304 0.1972 0.0077  -0.0306 0.0027  59  ASN   B CG  
4984 O OD1 . ASN   B 59  ? 0.1624 0.2337 0.1959 0.0093  -0.0197 0.0188  59  ASN   B OD1 
4985 N ND2 . ASN   B 59  ? 0.1699 0.2432 0.2006 0.0017  -0.0322 -0.0018 59  ASN   B ND2 
4992 N N   . ALA   B 60  ? 0.1385 0.1775 0.1700 -0.0131 -0.0087 -0.0078 60  ALA   B N   
4993 C CA  . ALA   B 60  ? 0.1453 0.1686 0.1688 -0.0204 -0.0032 -0.0020 60  ALA   B CA  
4994 C C   . ALA   B 60  ? 0.1465 0.1544 0.1502 -0.0091 -0.0087 0.0005  60  ALA   B C   
4995 O O   . ALA   B 60  ? 0.1541 0.1634 0.1707 -0.0143 -0.0054 -0.0135 60  ALA   B O   
4996 C CB  . ALA   B 60  ? 0.1601 0.1744 0.1910 -0.0237 -0.0006 -0.0009 60  ALA   B CB  
5002 N N   . MET   B 61  ? 0.1370 0.1480 0.1483 -0.0064 -0.0048 0.0021  61  MET   B N   
5003 C CA  . MET   B 61  ? 0.1349 0.1442 0.1344 -0.0036 -0.0165 0.0038  61  MET   B CA  
5004 C C   . MET   B 61  ? 0.1355 0.1412 0.1428 -0.0097 -0.0122 0.0005  61  MET   B C   
5005 O O   . MET   B 61  ? 0.1386 0.1414 0.1346 -0.0008 -0.0107 -0.0131 61  MET   B O   
5006 C CB  . MET   B 61  ? 0.1302 0.1419 0.1417 0.0008  -0.0131 -0.0019 61  MET   B CB  
5007 C CG  . MET   B 61  ? 0.1281 0.1431 0.1378 0.0014  -0.0095 -0.0000 61  MET   B CG  
5008 S SD  . MET   B 61  ? 0.1327 0.1456 0.1563 -0.0015 -0.0074 -0.0095 61  MET   B SD  
5009 C CE  . MET   B 61  ? 0.1341 0.1644 0.1713 0.0029  -0.0149 -0.0210 61  MET   B CE  
5019 N N   . GLN   B 62  ? 0.1350 0.1451 0.1324 -0.0053 -0.0243 0.0075  62  GLN   B N   
5020 C CA  . GLN   B 62  ? 0.1402 0.1522 0.1374 0.0050  -0.0214 -0.0018 62  GLN   B CA  
5021 C C   . GLN   B 62  ? 0.1424 0.1595 0.1352 -0.0025 -0.0231 -0.0048 62  GLN   B C   
5022 O O   . GLN   B 62  ? 0.1534 0.1596 0.1438 -0.0010 -0.0303 -0.0072 62  GLN   B O   
5023 C CB  . GLN   B 62  ? 0.1427 0.1515 0.1489 0.0063  -0.0159 0.0006  62  GLN   B CB  
5024 C CG  . GLN   B 62  ? 0.1472 0.1568 0.1443 0.0117  -0.0273 -0.0034 62  GLN   B CG  
5025 C CD  . GLN   B 62  ? 0.1494 0.1527 0.1304 0.0113  -0.0255 0.0026  62  GLN   B CD  
5026 O OE1 . GLN   B 62  ? 0.1537 0.1495 0.1557 0.0082  -0.0281 -0.0041 62  GLN   B OE1 
5027 N NE2 . GLN   B 62  ? 0.1554 0.1592 0.1363 0.0130  -0.0179 -0.0065 62  GLN   B NE2 
5036 N N   . VAL   B 63  ? 0.1388 0.1641 0.1497 -0.0081 -0.0210 -0.0163 63  VAL   B N   
5037 C CA  . VAL   B 63  ? 0.1487 0.1644 0.1659 -0.0119 -0.0286 -0.0107 63  VAL   B CA  
5038 C C   . VAL   B 63  ? 0.1496 0.1537 0.1528 -0.0137 -0.0341 -0.0202 63  VAL   B C   
5039 O O   . VAL   B 63  ? 0.1620 0.1540 0.1699 -0.0095 -0.0419 -0.0167 63  VAL   B O   
5040 C CB  . VAL   B 63  ? 0.1552 0.1754 0.2011 -0.0129 -0.0330 -0.0138 63  VAL   B CB  
5041 C CG1 . VAL   B 63  ? 0.1623 0.1771 0.2137 -0.0259 -0.0168 -0.0104 63  VAL   B CG1 
5042 C CG2 . VAL   B 63  ? 0.1518 0.1950 0.2130 -0.0057 -0.0331 -0.0151 63  VAL   B CG2 
5052 N N   . GLU   B 64  ? 0.1467 0.1416 0.1487 -0.0029 -0.0299 -0.0120 64  GLU   B N   
5053 C CA  . GLU   B 64  ? 0.1471 0.1389 0.1488 -0.0116 -0.0310 -0.0078 64  GLU   B CA  
5054 C C   . GLU   B 64  ? 0.1444 0.1388 0.1371 -0.0010 -0.0346 -0.0177 64  GLU   B C   
5055 O O   . GLU   B 64  ? 0.1577 0.1499 0.1351 -0.0057 -0.0289 -0.0171 64  GLU   B O   
5056 C CB  . GLU   B 64  ? 0.1443 0.1461 0.1459 -0.0127 -0.0264 0.0011  64  GLU   B CB  
5057 C CG  . GLU   B 64  ? 0.1560 0.1490 0.1528 -0.0239 -0.0274 -0.0061 64  GLU   B CG  
5058 C CD  . GLU   B 64  ? 0.1609 0.1604 0.1568 -0.0302 -0.0293 -0.0052 64  GLU   B CD  
5059 O OE1 . GLU   B 64  ? 0.1640 0.1771 0.1635 -0.0277 -0.0212 -0.0261 64  GLU   B OE1 
5060 O OE2 . GLU   B 64  ? 0.1807 0.1709 0.1623 -0.0349 -0.0396 -0.0111 64  GLU   B OE2 
5067 N N   . SER   B 65  ? 0.1473 0.1336 0.1364 -0.0067 -0.0219 -0.0208 65  SER   B N   
5068 C CA  . SER   B 65  ? 0.1449 0.1333 0.1368 0.0039  -0.0187 -0.0149 65  SER   B CA  
5069 C C   . SER   B 65  ? 0.1465 0.1303 0.1422 0.0091  -0.0304 -0.0149 65  SER   B C   
5070 O O   . SER   B 65  ? 0.1483 0.1404 0.1441 0.0052  -0.0236 -0.0218 65  SER   B O   
5071 C CB  . SER   B 65  ? 0.1468 0.1460 0.1345 -0.0045 -0.0160 -0.0127 65  SER   B CB  
5072 O OG  . SER   B 65  ? 0.1496 0.1414 0.1339 -0.0066 -0.0151 -0.0226 65  SER   B OG  
5078 N N   . ASP   B 66  ? 0.1594 0.1392 0.1349 0.0041  -0.0366 -0.0188 66  ASP   B N   
5079 C CA  . ASP   B 66  ? 0.1679 0.1469 0.1365 0.0076  -0.0330 -0.0057 66  ASP   B CA  
5080 C C   . ASP   B 66  ? 0.1671 0.1513 0.1309 -0.0002 -0.0293 -0.0132 66  ASP   B C   
5081 O O   . ASP   B 66  ? 0.1707 0.1566 0.1435 0.0056  -0.0317 -0.0216 66  ASP   B O   
5082 C CB  . ASP   B 66  ? 0.1781 0.1611 0.1544 0.0129  -0.0437 -0.0158 66  ASP   B CB  
5083 C CG  . ASP   B 66  ? 0.2023 0.1767 0.1828 0.0206  -0.0534 -0.0051 66  ASP   B CG  
5084 O OD1 . ASP   B 66  ? 0.2246 0.1704 0.1899 0.0159  -0.0506 -0.0011 66  ASP   B OD1 
5085 O OD2 . ASP   B 66  ? 0.2179 0.2060 0.2437 0.0407  -0.0521 -0.0038 66  ASP   B OD2 
5090 N N   . ASP   B 67  ? 0.1611 0.1441 0.1365 -0.0032 -0.0290 -0.0243 67  ASP   B N   
5091 C CA  . ASP   B 67  ? 0.1773 0.1446 0.1433 -0.0084 -0.0286 -0.0111 67  ASP   B CA  
5092 C C   . ASP   B 67  ? 0.1770 0.1428 0.1510 -0.0003 -0.0277 -0.0144 67  ASP   B C   
5093 O O   . ASP   B 67  ? 0.1830 0.1508 0.1630 0.0020  -0.0181 -0.0237 67  ASP   B O   
5094 C CB  . ASP   B 67  ? 0.1951 0.1532 0.1619 -0.0163 -0.0461 -0.0065 67  ASP   B CB  
5095 C CG  . ASP   B 67  ? 0.2309 0.1557 0.1705 -0.0085 -0.0639 -0.0113 67  ASP   B CG  
5096 O OD1 . ASP   B 67  ? 0.2489 0.1625 0.1939 -0.0084 -0.0589 -0.0131 67  ASP   B OD1 
5097 O OD2 . ASP   B 67  ? 0.2490 0.1628 0.1882 0.0088  -0.0669 -0.0115 67  ASP   B OD2 
5102 N N   . TYR   B 68  ? 0.1681 0.1470 0.1419 0.0065  -0.0410 -0.0199 68  TYR   B N   
5103 C CA  . TYR   B 68  ? 0.1663 0.1579 0.1659 0.0121  -0.0403 -0.0308 68  TYR   B CA  
5104 C C   . TYR   B 68  ? 0.1571 0.1502 0.1596 0.0077  -0.0349 -0.0408 68  TYR   B C   
5105 O O   . TYR   B 68  ? 0.1625 0.1637 0.1684 0.0129  -0.0338 -0.0362 68  TYR   B O   
5106 C CB  . TYR   B 68  ? 0.1675 0.1778 0.1689 0.0117  -0.0440 -0.0422 68  TYR   B CB  
5107 C CG  . TYR   B 68  ? 0.1794 0.1920 0.1762 0.0190  -0.0424 -0.0625 68  TYR   B CG  
5108 C CD1 . TYR   B 68  ? 0.1794 0.1943 0.1982 0.0028  -0.0415 -0.0606 68  TYR   B CD1 
5109 C CD2 . TYR   B 68  ? 0.1877 0.2132 0.1887 0.0219  -0.0554 -0.0508 68  TYR   B CD2 
5110 C CE1 . TYR   B 68  ? 0.1903 0.2151 0.2160 0.0006  -0.0327 -0.0613 68  TYR   B CE1 
5111 C CE2 . TYR   B 68  ? 0.1879 0.2154 0.1910 0.0225  -0.0440 -0.0634 68  TYR   B CE2 
5112 C CZ  . TYR   B 68  ? 0.1820 0.2203 0.2105 0.0068  -0.0368 -0.0618 68  TYR   B CZ  
5113 O OH  . TYR   B 68  ? 0.1754 0.2351 0.2389 0.0057  -0.0287 -0.0365 68  TYR   B OH  
5123 N N   . ILE   B 69  ? 0.1510 0.1441 0.1648 0.0048  -0.0362 -0.0379 69  ILE   B N   
5124 C CA  . ILE   B 69  ? 0.1575 0.1554 0.1508 0.0001  -0.0228 -0.0369 69  ILE   B CA  
5125 C C   . ILE   B 69  ? 0.1588 0.1542 0.1483 0.0047  -0.0267 -0.0187 69  ILE   B C   
5126 O O   . ILE   B 69  ? 0.1645 0.1575 0.1469 0.0023  -0.0236 -0.0259 69  ILE   B O   
5127 C CB  . ILE   B 69  ? 0.1656 0.1568 0.1741 0.0022  -0.0086 -0.0292 69  ILE   B CB  
5128 C CG1 . ILE   B 69  ? 0.1687 0.1621 0.1897 -0.0040 -0.0029 -0.0268 69  ILE   B CG1 
5129 C CG2 . ILE   B 69  ? 0.1774 0.1662 0.1859 0.0059  -0.0083 -0.0182 69  ILE   B CG2 
5130 C CD1 . ILE   B 69  ? 0.1626 0.1645 0.2034 -0.0124 -0.0101 -0.0367 69  ILE   B CD1 
5142 N N   . ALA   B 70  ? 0.1542 0.1546 0.1478 0.0063  -0.0296 -0.0206 70  ALA   B N   
5143 C CA  . ALA   B 70  ? 0.1603 0.1566 0.1314 0.0010  -0.0326 -0.0209 70  ALA   B CA  
5144 C C   . ALA   B 70  ? 0.1695 0.1526 0.1451 -0.0039 -0.0379 -0.0312 70  ALA   B C   
5145 O O   . ALA   B 70  ? 0.1747 0.1563 0.1565 -0.0011 -0.0345 -0.0335 70  ALA   B O   
5146 C CB  . ALA   B 70  ? 0.1635 0.1702 0.1398 0.0014  -0.0270 -0.0257 70  ALA   B CB  
5152 N N   . THR   B 71  ? 0.1770 0.1538 0.1510 0.0044  -0.0491 -0.0301 71  THR   B N   
5153 C CA  . THR   B 71  ? 0.1916 0.1554 0.1802 0.0122  -0.0620 -0.0283 71  THR   B CA  
5154 C C   . THR   B 71  ? 0.1878 0.1603 0.2022 0.0300  -0.0622 -0.0425 71  THR   B C   
5155 O O   . THR   B 71  ? 0.1994 0.1689 0.2396 0.0308  -0.0521 -0.0554 71  THR   B O   
5156 C CB  . THR   B 71  ? 0.2152 0.1779 0.2047 0.0060  -0.0711 -0.0086 71  THR   B CB  
5157 O OG1 . THR   B 71  ? 0.2299 0.2023 0.2368 -0.0122 -0.0662 0.0130  71  THR   B OG1 
5158 C CG2 . THR   B 71  ? 0.2336 0.1805 0.2239 0.0068  -0.0649 -0.0005 71  THR   B CG2 
5166 N N   . ASN   B 72  ? 0.1746 0.1651 0.1961 0.0227  -0.0583 -0.0644 72  ASN   B N   
5167 C CA  . ASN   B 72  ? 0.1712 0.1793 0.2062 0.0205  -0.0411 -0.0716 72  ASN   B CA  
5168 C C   . ASN   B 72  ? 0.1683 0.1894 0.2085 0.0077  -0.0224 -0.0672 72  ASN   B C   
5169 O O   . ASN   B 72  ? 0.1694 0.2057 0.2427 0.0081  -0.0082 -0.0650 72  ASN   B O   
5170 C CB  . ASN   B 72  ? 0.1755 0.1941 0.2143 0.0116  -0.0595 -0.0637 72  ASN   B CB  
5171 C CG  . ASN   B 72  ? 0.1915 0.2091 0.2286 0.0320  -0.0645 -0.0378 72  ASN   B CG  
5172 O OD1 . ASN   B 72  ? 0.2134 0.2290 0.2346 0.0180  -0.0432 -0.0376 72  ASN   B OD1 
5173 N ND2 . ASN   B 72  ? 0.2058 0.2157 0.2767 0.0484  -0.0546 -0.0119 72  ASN   B ND2 
5180 N N   . GLY   B 73  ? 0.1709 0.1898 0.1843 0.0061  -0.0277 -0.0688 73  GLY   B N   
5181 C CA  . GLY   B 73  ? 0.1645 0.1999 0.1610 0.0046  -0.0181 -0.0553 73  GLY   B CA  
5182 C C   . GLY   B 73  ? 0.1602 0.1936 0.1166 0.0089  -0.0229 -0.0454 73  GLY   B C   
5183 O O   . GLY   B 73  ? 0.1653 0.1790 0.1433 0.0125  -0.0203 -0.0327 73  GLY   B O   
5187 N N   . PRO   B 74  ? 0.1644 0.2052 0.1259 0.0098  -0.0200 -0.0289 74  PRO   B N   
5188 C CA  . PRO   B 74  ? 0.1610 0.2043 0.1055 0.0096  -0.0116 -0.0190 74  PRO   B CA  
5189 C C   . PRO   B 74  ? 0.1470 0.1862 0.1109 0.0110  -0.0151 -0.0137 74  PRO   B C   
5190 O O   . PRO   B 74  ? 0.1505 0.1919 0.1607 0.0133  -0.0129 -0.0308 74  PRO   B O   
5191 C CB  . PRO   B 74  ? 0.1730 0.2242 0.1111 0.0074  -0.0112 -0.0118 74  PRO   B CB  
5192 C CG  . PRO   B 74  ? 0.1962 0.2349 0.1408 0.0026  -0.0099 -0.0034 74  PRO   B CG  
5193 C CD  . PRO   B 74  ? 0.1902 0.2246 0.1301 0.0099  -0.0112 -0.0176 74  PRO   B CD  
5201 N N   . LEU   B 75  ? 0.1490 0.1741 0.1066 0.0139  -0.0169 -0.0125 75  LEU   B N   
5202 C CA  . LEU   B 75  ? 0.1556 0.1752 0.1083 0.0097  -0.0169 0.0004  75  LEU   B CA  
5203 C C   . LEU   B 75  ? 0.1610 0.1862 0.1158 0.0142  -0.0051 -0.0005 75  LEU   B C   
5204 O O   . LEU   B 75  ? 0.1748 0.1987 0.1316 0.0048  -0.0041 0.0044  75  LEU   B O   
5205 C CB  . LEU   B 75  ? 0.1584 0.1716 0.1008 -0.0029 -0.0201 0.0115  75  LEU   B CB  
5206 C CG  . LEU   B 75  ? 0.1901 0.1906 0.1254 -0.0228 -0.0092 0.0031  75  LEU   B CG  
5207 C CD1 . LEU   B 75  ? 0.2222 0.2090 0.1279 -0.0341 0.0172  -0.0062 75  LEU   B CD1 
5208 C CD2 . LEU   B 75  ? 0.2322 0.2125 0.1985 -0.0105 0.0051  0.0121  75  LEU   B CD2 
5220 N N   . LYS   B 76  ? 0.1590 0.2041 0.1493 0.0100  0.0056  0.0097  76  LYS   B N   
5221 C CA  . LYS   B 76  ? 0.1670 0.2135 0.1706 0.0002  0.0216  0.0092  76  LYS   B CA  
5222 C C   . LYS   B 76  ? 0.1635 0.2003 0.1425 0.0040  0.0152  0.0265  76  LYS   B C   
5223 O O   . LYS   B 76  ? 0.1663 0.1773 0.1427 0.0003  0.0093  0.0169  76  LYS   B O   
5224 C CB  . LYS   B 76  ? 0.1848 0.2237 0.2267 -0.0006 0.0411  -0.0223 76  LYS   B CB  
5225 C CG  . LYS   B 76  ? 0.1944 0.2437 0.2743 0.0059  0.0314  -0.0296 76  LYS   B CG  
5226 C CD  . LYS   B 76  ? 0.1953 0.2520 0.3073 0.0102  0.0256  -0.0478 76  LYS   B CD  
5227 C CE  . LYS   B 76  ? 0.2014 0.2647 0.3528 0.0137  0.0122  -0.0607 76  LYS   B CE  
5228 N NZ  . LYS   B 76  ? 0.1969 0.2687 0.3624 0.0100  0.0005  -0.0832 76  LYS   B NZ  
5242 N N   . VAL   B 77  ? 0.1732 0.2142 0.1502 0.0060  0.0137  0.0293  77  VAL   B N   
5243 C CA  . VAL   B 77  ? 0.1759 0.2069 0.1650 0.0149  0.0176  0.0566  77  VAL   B CA  
5244 C C   . VAL   B 77  ? 0.1610 0.1818 0.1586 0.0173  0.0286  0.0407  77  VAL   B C   
5245 O O   . VAL   B 77  ? 0.1640 0.1794 0.1606 0.0204  0.0348  0.0349  77  VAL   B O   
5246 C CB  . VAL   B 77  ? 0.1934 0.2190 0.2102 0.0091  0.0264  0.0769  77  VAL   B CB  
5247 C CG1 . VAL   B 77  ? 0.1915 0.2125 0.2341 0.0067  0.0271  0.0934  77  VAL   B CG1 
5248 C CG2 . VAL   B 77  ? 0.2079 0.2297 0.2230 0.0106  0.0099  0.0812  77  VAL   B CG2 
5258 N N   . GLY   B 78  ? 0.1537 0.1605 0.1638 0.0135  0.0194  0.0296  78  GLY   B N   
5259 C CA  . GLY   B 78  ? 0.1509 0.1562 0.1535 0.0181  0.0242  0.0196  78  GLY   B CA  
5260 C C   . GLY   B 78  ? 0.1483 0.1505 0.1395 0.0114  0.0196  0.0239  78  GLY   B C   
5261 O O   . GLY   B 78  ? 0.1471 0.1497 0.1547 0.0197  0.0195  0.0274  78  GLY   B O   
5265 N N   . GLY   B 79  ? 0.1397 0.1559 0.1466 0.0162  0.0158  0.0201  79  GLY   B N   
5266 C CA  . GLY   B 79  ? 0.1423 0.1452 0.1478 0.0153  0.0072  0.0241  79  GLY   B CA  
5267 C C   . GLY   B 79  ? 0.1314 0.1393 0.1373 0.0181  0.0118  0.0093  79  GLY   B C   
5268 O O   . GLY   B 79  ? 0.1405 0.1379 0.1486 0.0145  0.0125  0.0205  79  GLY   B O   
5272 N N   . SER   B 80  ? 0.1342 0.1337 0.1415 0.0084  0.0196  0.0086  80  SER   B N   
5273 C CA  . SER   B 80  ? 0.1275 0.1329 0.1318 0.0022  0.0080  0.0099  80  SER   B CA  
5274 C C   . SER   B 80  ? 0.1294 0.1271 0.1290 0.0084  -0.0094 0.0032  80  SER   B C   
5275 O O   . SER   B 80  ? 0.1443 0.1330 0.1665 0.0124  0.0028  -0.0040 80  SER   B O   
5276 C CB  . SER   B 80  ? 0.1334 0.1371 0.1370 -0.0009 -0.0033 0.0149  80  SER   B CB  
5277 O OG  . SER   B 80  ? 0.1378 0.1523 0.1693 -0.0006 -0.0168 0.0121  80  SER   B OG  
5283 N N   . CYS   B 81  ? 0.1292 0.1169 0.1378 0.0078  -0.0070 -0.0021 81  CYS   B N   
5284 C CA  . CYS   B 81  ? 0.1333 0.1177 0.1378 0.0034  -0.0150 0.0048  81  CYS   B CA  
5285 C C   . CYS   B 81  ? 0.1290 0.1173 0.1177 0.0013  -0.0182 0.0038  81  CYS   B C   
5286 O O   . CYS   B 81  ? 0.1532 0.1192 0.1356 0.0093  -0.0053 -0.0046 81  CYS   B O   
5287 C CB  . CYS   B 81  ? 0.1445 0.1294 0.1507 -0.0032 -0.0171 -0.0031 81  CYS   B CB  
5288 S SG  . CYS   B 81  ? 0.1503 0.1462 0.1366 -0.0029 -0.0249 -0.0069 81  CYS   B SG  
5294 N N   . VAL   B 82  ? 0.1386 0.1175 0.1361 0.0025  -0.0155 -0.0018 82  VAL   B N   
5295 C CA  . VAL   B 82  ? 0.1408 0.1186 0.1346 -0.0017 -0.0118 0.0073  82  VAL   B CA  
5296 C C   . VAL   B 82  ? 0.1463 0.1099 0.1398 -0.0059 -0.0155 0.0044  82  VAL   B C   
5297 O O   . VAL   B 82  ? 0.1540 0.1133 0.1681 -0.0022 -0.0133 -0.0154 82  VAL   B O   
5298 C CB  . VAL   B 82  ? 0.1459 0.1384 0.1517 -0.0039 -0.0138 0.0088  82  VAL   B CB  
5299 C CG1 . VAL   B 82  ? 0.1558 0.1598 0.1593 0.0036  -0.0121 0.0195  82  VAL   B CG1 
5300 C CG2 . VAL   B 82  ? 0.1504 0.1525 0.1688 -0.0013 -0.0309 0.0187  82  VAL   B CG2 
5310 N N   . LEU   B 83  ? 0.1390 0.1114 0.1358 -0.0155 -0.0246 -0.0010 83  LEU   B N   
5311 C CA  . LEU   B 83  ? 0.1425 0.1232 0.1199 -0.0134 -0.0234 -0.0044 83  LEU   B CA  
5312 C C   . LEU   B 83  ? 0.1381 0.1198 0.1210 -0.0154 -0.0282 -0.0022 83  LEU   B C   
5313 O O   . LEU   B 83  ? 0.1417 0.1285 0.1091 -0.0231 -0.0139 0.0011  83  LEU   B O   
5314 C CB  . LEU   B 83  ? 0.1444 0.1366 0.1179 -0.0125 -0.0272 -0.0081 83  LEU   B CB  
5315 C CG  . LEU   B 83  ? 0.1628 0.1548 0.1301 -0.0183 -0.0208 -0.0039 83  LEU   B CG  
5316 C CD1 . LEU   B 83  ? 0.1775 0.1623 0.1309 -0.0183 -0.0220 -0.0016 83  LEU   B CD1 
5317 C CD2 . LEU   B 83  ? 0.1812 0.1548 0.1566 -0.0087 -0.0210 -0.0175 83  LEU   B CD2 
5329 N N   . SER   B 84  ? 0.1419 0.1302 0.1436 -0.0197 -0.0249 0.0021  84  SER   B N   
5330 C CA  . SER   B 84  ? 0.1430 0.1493 0.1316 -0.0274 -0.0176 0.0176  84  SER   B CA  
5331 C C   . SER   B 84  ? 0.1346 0.1660 0.0969 -0.0202 -0.0210 0.0217  84  SER   B C   
5332 O O   . SER   B 84  ? 0.1480 0.1528 0.0981 -0.0177 -0.0132 0.0045  84  SER   B O   
5333 C CB  . SER   B 84  ? 0.1602 0.1568 0.1767 -0.0231 0.0049  0.0085  84  SER   B CB  
5334 O OG  . SER   B 84  ? 0.1612 0.1699 0.2081 -0.0410 0.0015  0.0201  84  SER   B OG  
5340 N N   . GLY   B 85  ? 0.1397 0.1829 0.1161 -0.0201 -0.0217 0.0248  85  GLY   B N   
5341 C CA  . GLY   B 85  ? 0.1423 0.1905 0.1330 -0.0351 -0.0012 -0.0077 85  GLY   B CA  
5342 C C   . GLY   B 85  ? 0.1388 0.1786 0.1185 -0.0437 -0.0122 0.0042  85  GLY   B C   
5343 O O   . GLY   B 85  ? 0.1533 0.1794 0.1325 -0.0597 0.0159  -0.0072 85  GLY   B O   
5347 N N   . HIS   B 86  ? 0.1355 0.1659 0.1370 -0.0310 -0.0153 0.0131  86  HIS   B N   
5348 C CA  . HIS   B 86  ? 0.1423 0.1629 0.1223 -0.0374 -0.0172 0.0164  86  HIS   B CA  
5349 C C   . HIS   B 86  ? 0.1443 0.1781 0.1172 -0.0458 -0.0075 0.0289  86  HIS   B C   
5350 O O   . HIS   B 86  ? 0.1602 0.1861 0.1265 -0.0369 0.0067  0.0250  86  HIS   B O   
5351 C CB  . HIS   B 86  ? 0.1535 0.1685 0.1353 -0.0231 -0.0193 0.0050  86  HIS   B CB  
5352 C CG  . HIS   B 86  ? 0.1491 0.1687 0.1350 -0.0129 -0.0234 0.0134  86  HIS   B CG  
5353 N ND1 . HIS   B 86  ? 0.1621 0.1875 0.1589 -0.0184 -0.0266 -0.0035 86  HIS   B ND1 
5354 C CD2 . HIS   B 86  ? 0.1570 0.1716 0.1345 -0.0096 -0.0161 0.0098  86  HIS   B CD2 
5355 C CE1 . HIS   B 86  ? 0.1680 0.1854 0.1452 -0.0127 -0.0040 -0.0155 86  HIS   B CE1 
5356 N NE2 . HIS   B 86  ? 0.1631 0.1766 0.1323 -0.0026 -0.0050 0.0057  86  HIS   B NE2 
5364 N N   . ASN   B 87  ? 0.1474 0.1738 0.1400 -0.0400 -0.0033 0.0199  87  ASN   B N   
5365 C CA  . ASN   B 87  ? 0.1584 0.1891 0.1453 -0.0355 0.0249  0.0163  87  ASN   B CA  
5366 C C   . ASN   B 87  ? 0.1751 0.1823 0.1293 -0.0334 0.0313  0.0145  87  ASN   B C   
5367 O O   . ASN   B 87  ? 0.2010 0.1857 0.1630 -0.0289 0.0459  0.0068  87  ASN   B O   
5368 C CB  . ASN   B 87  ? 0.1570 0.2187 0.1756 -0.0317 0.0307  0.0132  87  ASN   B CB  
5369 C CG  . ASN   B 87  ? 0.1682 0.2355 0.1852 -0.0041 0.0329  0.0275  87  ASN   B CG  
5370 O OD1 . ASN   B 87  ? 0.1630 0.2204 0.1718 0.0060  0.0452  0.0402  87  ASN   B OD1 
5371 N ND2 . ASN   B 87  ? 0.2034 0.2495 0.2248 0.0082  0.0442  0.0246  87  ASN   B ND2 
5378 N N   . LEU   B 88  ? 0.1591 0.1685 0.1184 -0.0373 0.0184  0.0112  88  LEU   B N   
5379 C CA  . LEU   B 88  ? 0.1746 0.1624 0.1256 -0.0383 0.0091  -0.0006 88  LEU   B CA  
5380 C C   . LEU   B 88  ? 0.1735 0.1515 0.1203 -0.0423 -0.0028 -0.0019 88  LEU   B C   
5381 O O   . LEU   B 88  ? 0.1926 0.1579 0.1603 -0.0238 -0.0267 -0.0091 88  LEU   B O   
5382 C CB  . LEU   B 88  ? 0.1890 0.1713 0.1362 -0.0469 -0.0051 0.0067  88  LEU   B CB  
5383 C CG  . LEU   B 88  ? 0.2288 0.1989 0.1630 -0.0423 -0.0254 0.0249  88  LEU   B CG  
5384 C CD1 . LEU   B 88  ? 0.2383 0.2297 0.1780 -0.0526 -0.0232 0.0445  88  LEU   B CD1 
5385 C CD2 . LEU   B 88  ? 0.2659 0.2264 0.2259 -0.0066 -0.0411 0.0097  88  LEU   B CD2 
5397 N N   . ALA   B 89  ? 0.1535 0.1530 0.1125 -0.0432 0.0164  -0.0025 89  ALA   B N   
5398 C CA  . ALA   B 89  ? 0.1529 0.1460 0.1068 -0.0422 0.0029  0.0072  89  ALA   B CA  
5399 C C   . ALA   B 89  ? 0.1619 0.1443 0.1076 -0.0482 0.0122  0.0039  89  ALA   B C   
5400 O O   . ALA   B 89  ? 0.1427 0.1550 0.1400 -0.0422 0.0114  -0.0319 89  ALA   B O   
5401 C CB  . ALA   B 89  ? 0.1427 0.1444 0.1244 -0.0403 0.0085  0.0153  89  ALA   B CB  
5407 N N   . LYS   B 90  ? 0.1983 0.1320 0.1232 -0.0515 -0.0117 0.0152  90  LYS   B N   
5408 C CA  . LYS   B 90  ? 0.2109 0.1318 0.1198 -0.0476 -0.0135 0.0086  90  LYS   B CA  
5409 C C   . LYS   B 90  ? 0.1896 0.1246 0.1288 -0.0434 -0.0126 0.0000  90  LYS   B C   
5410 O O   . LYS   B 90  ? 0.1956 0.1405 0.1395 -0.0561 -0.0022 -0.0001 90  LYS   B O   
5411 C CB  . LYS   B 90  ? 0.2281 0.1410 0.1442 -0.0393 -0.0053 0.0125  90  LYS   B CB  
5412 C CG  . LYS   B 90  ? 0.2278 0.1520 0.1543 -0.0319 0.0238  0.0076  90  LYS   B CG  
5413 C CD  . LYS   B 90  ? 0.2425 0.1659 0.1962 -0.0224 0.0471  -0.0092 90  LYS   B CD  
5414 C CE  . LYS   B 90  ? 0.2597 0.1806 0.2474 -0.0222 0.0648  -0.0214 90  LYS   B CE  
5415 N NZ  . LYS   B 90  ? 0.2810 0.1751 0.2473 -0.0303 0.0816  -0.0201 90  LYS   B NZ  
5429 N N   . HIS   B 91  ? 0.1612 0.1174 0.1142 -0.0322 -0.0180 0.0100  91  HIS   B N   
5430 C CA  . HIS   B 91  ? 0.1509 0.1221 0.1185 -0.0220 -0.0220 0.0058  91  HIS   B CA  
5431 C C   . HIS   B 91  ? 0.1412 0.1233 0.1015 -0.0263 -0.0123 0.0004  91  HIS   B C   
5432 O O   . HIS   B 91  ? 0.1566 0.1268 0.1058 -0.0284 -0.0188 0.0034  91  HIS   B O   
5433 C CB  . HIS   B 91  ? 0.1690 0.1196 0.1586 -0.0120 -0.0183 0.0145  91  HIS   B CB  
5434 C CG  . HIS   B 91  ? 0.2035 0.1378 0.2291 -0.0026 0.0216  0.0307  91  HIS   B CG  
5435 N ND1 . HIS   B 91  ? 0.2340 0.1428 0.2898 -0.0048 0.0319  0.0079  91  HIS   B ND1 
5436 C CD2 . HIS   B 91  ? 0.2142 0.1689 0.2789 0.0157  0.0110  0.0586  91  HIS   B CD2 
5437 C CE1 . HIS   B 91  ? 0.2370 0.1602 0.3124 0.0098  0.0303  0.0181  91  HIS   B CE1 
5438 N NE2 . HIS   B 91  ? 0.2321 0.1787 0.3101 0.0205  0.0222  0.0589  91  HIS   B NE2 
5446 N N   . CYS   B 92  ? 0.1341 0.1209 0.1045 -0.0292 -0.0137 -0.0023 92  CYS   B N   
5447 C CA  . CYS   B 92  ? 0.1344 0.1197 0.1092 -0.0242 -0.0075 -0.0031 92  CYS   B CA  
5448 C C   . CYS   B 92  ? 0.1272 0.1151 0.1027 -0.0097 -0.0093 0.0059  92  CYS   B C   
5449 O O   . CYS   B 92  ? 0.1376 0.1203 0.1264 -0.0161 -0.0086 0.0004  92  CYS   B O   
5450 C CB  . CYS   B 92  ? 0.1332 0.1283 0.1094 -0.0142 -0.0155 0.0017  92  CYS   B CB  
5451 S SG  . CYS   B 92  ? 0.1332 0.1291 0.1152 -0.0128 -0.0118 0.0053  92  CYS   B SG  
5457 N N   . LEU   B 93  ? 0.1224 0.1213 0.1076 -0.0153 -0.0116 0.0007  93  LEU   B N   
5458 C CA  . LEU   B 93  ? 0.1257 0.1164 0.1111 -0.0031 -0.0146 0.0046  93  LEU   B CA  
5459 C C   . LEU   B 93  ? 0.1189 0.1118 0.1011 -0.0001 -0.0071 0.0099  93  LEU   B C   
5460 O O   . LEU   B 93  ? 0.1263 0.1108 0.1244 -0.0068 -0.0061 0.0016  93  LEU   B O   
5461 C CB  . LEU   B 93  ? 0.1291 0.1133 0.1209 0.0011  -0.0162 0.0054  93  LEU   B CB  
5462 C CG  . LEU   B 93  ? 0.1235 0.1257 0.1404 -0.0054 -0.0142 0.0160  93  LEU   B CG  
5463 C CD1 . LEU   B 93  ? 0.1283 0.1392 0.1398 0.0045  -0.0115 -0.0032 93  LEU   B CD1 
5464 C CD2 . LEU   B 93  ? 0.1306 0.1278 0.1439 -0.0021 -0.0158 0.0097  93  LEU   B CD2 
5476 N N   . HIS   B 94  ? 0.1248 0.1139 0.1025 -0.0020 -0.0102 0.0070  94  HIS   B N   
5477 C CA  . HIS   B 94  ? 0.1276 0.1123 0.0979 0.0002  -0.0039 0.0058  94  HIS   B CA  
5478 C C   . HIS   B 94  ? 0.1204 0.1132 0.1214 0.0017  -0.0046 0.0094  94  HIS   B C   
5479 O O   . HIS   B 94  ? 0.1174 0.1239 0.1581 -0.0021 0.0109  -0.0075 94  HIS   B O   
5480 C CB  . HIS   B 94  ? 0.1257 0.1173 0.1169 0.0032  -0.0124 0.0022  94  HIS   B CB  
5481 C CG  . HIS   B 94  ? 0.1260 0.1171 0.1144 -0.0030 -0.0210 0.0030  94  HIS   B CG  
5482 N ND1 . HIS   B 94  ? 0.1314 0.1219 0.1078 -0.0062 -0.0208 0.0005  94  HIS   B ND1 
5483 C CD2 . HIS   B 94  ? 0.1320 0.1190 0.1209 -0.0016 -0.0128 0.0026  94  HIS   B CD2 
5484 C CE1 . HIS   B 94  ? 0.1353 0.1197 0.1063 -0.0098 -0.0182 0.0006  94  HIS   B CE1 
5485 N NE2 . HIS   B 94  ? 0.1242 0.1248 0.1264 -0.0108 -0.0156 0.0022  94  HIS   B NE2 
5493 N N   . VAL   B 95  ? 0.1166 0.1085 0.1290 -0.0009 -0.0026 0.0086  95  VAL   B N   
5494 C CA  . VAL   B 95  ? 0.1186 0.1197 0.1222 0.0011  0.0001  0.0145  95  VAL   B CA  
5495 C C   . VAL   B 95  ? 0.1277 0.1190 0.1129 -0.0016 0.0059  0.0108  95  VAL   B C   
5496 O O   . VAL   B 95  ? 0.1315 0.1151 0.1408 0.0097  0.0050  0.0199  95  VAL   B O   
5497 C CB  . VAL   B 95  ? 0.1302 0.1200 0.1251 -0.0040 -0.0074 0.0118  95  VAL   B CB  
5498 C CG1 . VAL   B 95  ? 0.1368 0.1362 0.1474 -0.0042 -0.0027 0.0171  95  VAL   B CG1 
5499 C CG2 . VAL   B 95  ? 0.1327 0.1175 0.1284 -0.0012 -0.0144 0.0077  95  VAL   B CG2 
5509 N N   . VAL   B 96  ? 0.1377 0.1235 0.1212 0.0072  0.0021  0.0153  96  VAL   B N   
5510 C CA  . VAL   B 96  ? 0.1476 0.1350 0.1121 0.0076  0.0028  0.0232  96  VAL   B CA  
5511 C C   . VAL   B 96  ? 0.1510 0.1359 0.1277 0.0049  0.0157  0.0264  96  VAL   B C   
5512 O O   . VAL   B 96  ? 0.1502 0.1455 0.1538 0.0024  0.0185  0.0099  96  VAL   B O   
5513 C CB  . VAL   B 96  ? 0.1557 0.1596 0.1088 0.0090  0.0070  0.0157  96  VAL   B CB  
5514 C CG1 . VAL   B 96  ? 0.1474 0.1736 0.1235 0.0138  0.0066  0.0105  96  VAL   B CG1 
5515 C CG2 . VAL   B 96  ? 0.1655 0.1645 0.1151 0.0083  0.0082  0.0020  96  VAL   B CG2 
5525 N N   . GLY   B 97  ? 0.1562 0.1368 0.1259 0.0037  0.0043  0.0249  97  GLY   B N   
5526 C CA  . GLY   B 97  ? 0.1792 0.1428 0.1399 0.0064  0.0114  0.0253  97  GLY   B CA  
5527 C C   . GLY   B 97  ? 0.1988 0.1489 0.1440 0.0147  0.0075  0.0203  97  GLY   B C   
5528 O O   . GLY   B 97  ? 0.2181 0.1569 0.1435 0.0038  0.0036  0.0180  97  GLY   B O   
5532 N N   . PRO   B 98  ? 0.2149 0.1624 0.1653 0.0196  0.0359  0.0424  98  PRO   B N   
5533 C CA  . PRO   B 98  ? 0.2291 0.1832 0.1692 0.0319  0.0524  0.0383  98  PRO   B CA  
5534 C C   . PRO   B 98  ? 0.2434 0.1849 0.1454 0.0538  0.0575  0.0577  98  PRO   B C   
5535 O O   . PRO   B 98  ? 0.2333 0.1820 0.1717 0.0456  0.0593  0.0559  98  PRO   B O   
5536 C CB  . PRO   B 98  ? 0.2177 0.1883 0.1893 0.0256  0.0592  0.0371  98  PRO   B CB  
5537 C CG  . PRO   B 98  ? 0.2129 0.1788 0.1909 0.0184  0.0496  0.0558  98  PRO   B CG  
5538 C CD  . PRO   B 98  ? 0.1980 0.1645 0.1826 0.0201  0.0481  0.0560  98  PRO   B CD  
5546 N N   . ASN   B 99  ? 0.2603 0.2055 0.1563 0.0696  0.0568  0.0406  99  ASN   B N   
5547 C CA  . ASN   B 99  ? 0.2843 0.2148 0.1659 0.0768  0.0489  0.0699  99  ASN   B CA  
5548 C C   . ASN   B 99  ? 0.3139 0.2516 0.2121 0.0705  0.0771  0.0992  99  ASN   B C   
5549 O O   . ASN   B 99  ? 0.3260 0.2583 0.2146 0.0690  0.0738  0.0954  99  ASN   B O   
5550 C CB  . ASN   B 99  ? 0.2894 0.2091 0.1703 0.0747  0.0395  0.0559  99  ASN   B CB  
5551 C CG  . ASN   B 99  ? 0.2917 0.2138 0.1910 0.0696  0.0324  0.0500  99  ASN   B CG  
5552 O OD1 . ASN   B 99  ? 0.2943 0.2169 0.2180 0.0716  0.0394  0.0549  99  ASN   B OD1 
5553 N ND2 . ASN   B 99  ? 0.2909 0.2138 0.2046 0.0641  0.0061  0.0440  99  ASN   B ND2 
5560 N N   A VAL   B 100 ? 0.3330 0.2686 0.2620 0.0598  0.0783  0.1196  100 VAL   B N   
5561 N N   B VAL   B 100 ? 0.3313 0.2669 0.2631 0.0579  0.0801  0.1222  100 VAL   B N   
5562 C CA  A VAL   B 100 ? 0.3572 0.2872 0.3124 0.0474  0.0713  0.1350  100 VAL   B CA  
5563 C CA  B VAL   B 100 ? 0.3542 0.2840 0.3143 0.0438  0.0744  0.1394  100 VAL   B CA  
5564 C C   A VAL   B 100 ? 0.3760 0.2929 0.3085 0.0494  0.0688  0.1513  100 VAL   B C   
5565 C C   B VAL   B 100 ? 0.3740 0.2892 0.3059 0.0469  0.0713  0.1547  100 VAL   B C   
5566 O O   A VAL   B 100 ? 0.3807 0.3028 0.3161 0.0482  0.0760  0.1421  100 VAL   B O   
5567 O O   B VAL   B 100 ? 0.3780 0.2963 0.3074 0.0450  0.0794  0.1456  100 VAL   B O   
5568 C CB  A VAL   B 100 ? 0.3635 0.2976 0.3628 0.0305  0.0664  0.1415  100 VAL   B CB  
5569 C CB  B VAL   B 100 ? 0.3587 0.2932 0.3677 0.0239  0.0720  0.1502  100 VAL   B CB  
5570 C CG1 A VAL   B 100 ? 0.3672 0.3024 0.3823 0.0265  0.0644  0.1419  100 VAL   B CG1 
5571 C CG1 B VAL   B 100 ? 0.3621 0.2979 0.3890 0.0195  0.0703  0.1518  100 VAL   B CG1 
5572 C CG2 A VAL   B 100 ? 0.3648 0.3009 0.3776 0.0243  0.0645  0.1460  100 VAL   B CG2 
5573 C CG2 B VAL   B 100 ? 0.3592 0.2956 0.3828 0.0161  0.0707  0.1570  100 VAL   B CG2 
5592 N N   . ASN   B 101 ? 0.3900 0.2938 0.3059 0.0559  0.0548  0.1624  101 ASN   B N   
5593 C CA  . ASN   B 101 ? 0.4270 0.3101 0.3172 0.0619  0.0223  0.1700  101 ASN   B CA  
5594 C C   . ASN   B 101 ? 0.4723 0.3523 0.3214 0.0583  0.0057  0.1804  101 ASN   B C   
5595 O O   . ASN   B 101 ? 0.4774 0.3664 0.3506 0.0615  0.0084  0.1479  101 ASN   B O   
5596 C CB  . ASN   B 101 ? 0.4213 0.2909 0.3315 0.0611  0.0177  0.1507  101 ASN   B CB  
5597 C CG  . ASN   B 101 ? 0.4143 0.2732 0.3379 0.0602  0.0180  0.1386  101 ASN   B CG  
5598 O OD1 . ASN   B 101 ? 0.4157 0.2733 0.3535 0.0510  0.0347  0.1311  101 ASN   B OD1 
5599 N ND2 . ASN   B 101 ? 0.4085 0.2662 0.3329 0.0625  0.0136  0.1232  101 ASN   B ND2 
5607 N N   . LYS   B 102 ? 0.5107 0.3939 0.3429 0.0440  0.0058  0.1762  102 LYS   B N   
5608 C CA  . LYS   B 102 ? 0.5466 0.4429 0.3697 0.0262  0.0094  0.1476  102 LYS   B CA  
5609 C C   . LYS   B 102 ? 0.5425 0.4465 0.3506 0.0229  0.0128  0.1582  102 LYS   B C   
5610 O O   . LYS   B 102 ? 0.5501 0.4500 0.3554 0.0232  -0.0045 0.1598  102 LYS   B O   
5611 C CB  . LYS   B 102 ? 0.5810 0.4858 0.4273 0.0125  0.0211  0.0953  102 LYS   B CB  
5612 C CG  . LYS   B 102 ? 0.6089 0.5223 0.4883 0.0013  0.0330  0.0448  102 LYS   B CG  
5613 C CD  . LYS   B 102 ? 0.6327 0.5528 0.5540 -0.0070 0.0447  0.0047  102 LYS   B CD  
5614 C CE  . LYS   B 102 ? 0.6498 0.5746 0.6063 -0.0133 0.0527  -0.0234 102 LYS   B CE  
5615 N NZ  . LYS   B 102 ? 0.6585 0.5861 0.6396 -0.0160 0.0554  -0.0394 102 LYS   B NZ  
5629 N N   . GLY   B 103 ? 0.5260 0.4428 0.3522 0.0195  0.0370  0.1526  103 GLY   B N   
5630 C CA  . GLY   B 103 ? 0.5063 0.4362 0.3684 0.0190  0.0600  0.1293  103 GLY   B CA  
5631 C C   . GLY   B 103 ? 0.4826 0.4245 0.3684 0.0177  0.0814  0.1043  103 GLY   B C   
5632 O O   . GLY   B 103 ? 0.4860 0.4298 0.3665 0.0174  0.0891  0.1088  103 GLY   B O   
5636 N N   A GLU   B 104 ? 0.4686 0.4152 0.3639 0.0199  0.0869  0.0858  104 GLU   B N   
5637 N N   B GLU   B 104 ? 0.4666 0.4124 0.3609 0.0153  0.0862  0.0875  104 GLU   B N   
5638 C CA  A GLU   B 104 ? 0.4532 0.4051 0.3557 0.0238  0.0886  0.0628  104 GLU   B CA  
5639 C CA  B GLU   B 104 ? 0.4493 0.3996 0.3502 0.0148  0.0867  0.0662  104 GLU   B CA  
5640 C C   A GLU   B 104 ? 0.4506 0.4025 0.3631 0.0120  0.1189  0.0637  104 GLU   B C   
5641 C C   B GLU   B 104 ? 0.4449 0.3960 0.3566 0.0039  0.1181  0.0708  104 GLU   B C   
5642 O O   A GLU   B 104 ? 0.4512 0.4048 0.3745 0.0100  0.1200  0.0643  104 GLU   B O   
5643 O O   B GLU   B 104 ? 0.4454 0.3976 0.3706 0.0021  0.1190  0.0697  104 GLU   B O   
5644 C CB  A GLU   B 104 ? 0.4415 0.3958 0.3425 0.0398  0.0576  0.0330  104 GLU   B CB  
5645 C CB  B GLU   B 104 ? 0.4377 0.3885 0.3356 0.0255  0.0527  0.0342  104 GLU   B CB  
5646 C CG  A GLU   B 104 ? 0.4300 0.3872 0.3253 0.0557  0.0249  0.0012  104 GLU   B CG  
5647 C CG  B GLU   B 104 ? 0.4265 0.3783 0.3164 0.0365  0.0174  0.0004  104 GLU   B CG  
5648 C CD  A GLU   B 104 ? 0.4200 0.3789 0.3056 0.0694  -0.0029 -0.0231 104 GLU   B CD  
5649 C CD  B GLU   B 104 ? 0.4171 0.3682 0.2943 0.0453  -0.0120 -0.0252 104 GLU   B CD  
5650 O OE1 A GLU   B 104 ? 0.4131 0.3715 0.2784 0.0764  -0.0052 -0.0323 104 GLU   B OE1 
5651 O OE1 B GLU   B 104 ? 0.4104 0.3605 0.2689 0.0498  -0.0149 -0.0345 104 GLU   B OE1 
5652 O OE2 A GLU   B 104 ? 0.4173 0.3789 0.2962 0.0736  -0.0216 -0.0368 104 GLU   B OE2 
5653 O OE2 B GLU   B 104 ? 0.4141 0.3670 0.2798 0.0478  -0.0322 -0.0392 104 GLU   B OE2 
5666 N N   A ASP   B 105 ? 0.4449 0.3969 0.3529 0.0033  0.1460  0.0606  105 ASP   B N   
5667 N N   B ASP   B 105 ? 0.4370 0.3897 0.3397 -0.0045 0.1470  0.0725  105 ASP   B N   
5668 C CA  A ASP   B 105 ? 0.4419 0.3921 0.3648 -0.0037 0.1631  0.0438  105 ASP   B CA  
5669 C CA  B ASP   B 105 ? 0.4314 0.3846 0.3480 -0.0110 0.1651  0.0586  105 ASP   B CA  
5670 C C   A ASP   B 105 ? 0.4262 0.3703 0.3245 -0.0140 0.1746  0.0379  105 ASP   B C   
5671 C C   B ASP   B 105 ? 0.4148 0.3629 0.3090 -0.0233 0.1754  0.0524  105 ASP   B C   
5672 O O   A ASP   B 105 ? 0.4220 0.3663 0.3040 -0.0132 0.1887  0.0434  105 ASP   B O   
5673 O O   B ASP   B 105 ? 0.4050 0.3574 0.2894 -0.0252 0.1838  0.0598  105 ASP   B O   
5674 C CB  A ASP   B 105 ? 0.4522 0.4067 0.4258 0.0016  0.1646  0.0282  105 ASP   B CB  
5675 C CB  B ASP   B 105 ? 0.4416 0.3989 0.4051 -0.0037 0.1646  0.0450  105 ASP   B CB  
5676 C CG  A ASP   B 105 ? 0.4600 0.4179 0.4845 0.0037  0.1679  0.0170  105 ASP   B CG  
5677 C CG  B ASP   B 105 ? 0.4485 0.4095 0.4574 -0.0009 0.1683  0.0377  105 ASP   B CG  
5678 O OD1 A ASP   B 105 ? 0.4603 0.4210 0.4972 0.0014  0.1754  0.0191  105 ASP   B OD1 
5679 O OD1 B ASP   B 105 ? 0.4485 0.4129 0.4705 -0.0038 0.1733  0.0406  105 ASP   B OD1 
5680 O OD2 A ASP   B 105 ? 0.4645 0.4230 0.5155 0.0072  0.1624  0.0083  105 ASP   B OD2 
5681 O OD2 B ASP   B 105 ? 0.4504 0.4141 0.4782 0.0012  0.1695  0.0333  105 ASP   B OD2 
5690 N N   A ILE   B 106 ? 0.4129 0.3508 0.3244 -0.0230 0.1658  0.0299  106 ILE   B N   
5691 N N   B ILE   B 106 ? 0.4044 0.3452 0.3102 -0.0310 0.1685  0.0400  106 ILE   B N   
5692 C CA  A ILE   B 106 ? 0.3942 0.3305 0.3305 -0.0327 0.1647  0.0202  106 ILE   B CA  
5693 C CA  B ILE   B 106 ? 0.3886 0.3274 0.3194 -0.0400 0.1681  0.0259  106 ILE   B CA  
5694 C C   A ILE   B 106 ? 0.3676 0.3218 0.3243 -0.0277 0.1621  0.0117  106 ILE   B C   
5695 C C   B ILE   B 106 ? 0.3616 0.3201 0.3115 -0.0350 0.1676  0.0137  106 ILE   B C   
5696 O O   A ILE   B 106 ? 0.3635 0.3104 0.3181 -0.0320 0.1642  0.0142  106 ILE   B O   
5697 O O   B ILE   B 106 ? 0.3564 0.3079 0.3010 -0.0426 0.1701  0.0172  106 ILE   B O   
5698 C CB  A ILE   B 106 ? 0.4022 0.3219 0.3422 -0.0439 0.1649  0.0170  106 ILE   B CB  
5699 C CB  B ILE   B 106 ? 0.3989 0.3212 0.3334 -0.0496 0.1677  0.0211  106 ILE   B CB  
5700 C CG1 A ILE   B 106 ? 0.4048 0.3183 0.3392 -0.0446 0.1608  0.0106  106 ILE   B CG1 
5701 C CG1 B ILE   B 106 ? 0.4038 0.3199 0.3342 -0.0476 0.1611  0.0136  106 ILE   B CG1 
5702 C CG2 A ILE   B 106 ? 0.4056 0.3223 0.3578 -0.0481 0.1669  0.0173  106 ILE   B CG2 
5703 C CG2 B ILE   B 106 ? 0.4025 0.3224 0.3502 -0.0543 0.1699  0.0205  106 ILE   B CG2 
5704 C CD1 A ILE   B 106 ? 0.4058 0.3167 0.3338 -0.0439 0.1587  0.0088  106 ILE   B CD1 
5705 C CD1 B ILE   B 106 ? 0.4062 0.3192 0.3334 -0.0452 0.1568  0.0115  106 ILE   B CD1 
5728 N N   A GLN   B 107 ? 0.3479 0.3262 0.3368 -0.0232 0.1504  0.0105  107 GLN   B N   
5729 N N   B GLN   B 107 ? 0.3433 0.3259 0.3276 -0.0274 0.1559  0.0095  107 GLN   B N   
5730 C CA  A GLN   B 107 ? 0.3286 0.3310 0.3520 -0.0163 0.1319  0.0093  107 GLN   B CA  
5731 C CA  B GLN   B 107 ? 0.3254 0.3325 0.3458 -0.0181 0.1388  0.0078  107 GLN   B CA  
5732 C C   A GLN   B 107 ? 0.2959 0.3067 0.3134 -0.0043 0.1214  0.0023  107 GLN   B C   
5733 C C   B GLN   B 107 ? 0.2939 0.3081 0.3091 -0.0055 0.1271  0.0006  107 GLN   B C   
5734 O O   A GLN   B 107 ? 0.2896 0.3089 0.3325 0.0009  0.1056  -0.0159 107 GLN   B O   
5735 O O   B GLN   B 107 ? 0.2878 0.3120 0.3304 0.0002  0.1113  -0.0204 107 GLN   B O   
5736 C CB  A GLN   B 107 ? 0.3510 0.3612 0.4221 -0.0161 0.1062  0.0136  107 GLN   B CB  
5737 C CB  B GLN   B 107 ? 0.3498 0.3645 0.4190 -0.0158 0.1118  0.0119  107 GLN   B CB  
5738 C CG  A GLN   B 107 ? 0.3733 0.3874 0.4873 -0.0131 0.0772  0.0167  107 GLN   B CG  
5739 C CG  B GLN   B 107 ? 0.3746 0.3924 0.4875 -0.0108 0.0803  0.0147  107 GLN   B CG  
5740 C CD  A GLN   B 107 ? 0.3896 0.4073 0.5394 -0.0129 0.0566  0.0218  107 GLN   B CD  
5741 C CD  B GLN   B 107 ? 0.3932 0.4137 0.5421 -0.0090 0.0571  0.0190  107 GLN   B CD  
5742 O OE1 A GLN   B 107 ? 0.3953 0.4144 0.5586 -0.0123 0.0529  0.0219  107 GLN   B OE1 
5743 O OE1 B GLN   B 107 ? 0.4001 0.4216 0.5617 -0.0083 0.0529  0.0196  107 GLN   B OE1 
5744 N NE2 A GLN   B 107 ? 0.3959 0.4138 0.5571 -0.0116 0.0478  0.0253  107 GLN   B NE2 
5745 N NE2 B GLN   B 107 ? 0.4001 0.4207 0.5605 -0.0072 0.0478  0.0218  107 GLN   B NE2 
5762 N N   . LEU   B 108 ? 0.2711 0.2822 0.2779 0.0106  0.1135  0.0080  108 LEU   B N   
5763 C CA  . LEU   B 108 ? 0.2400 0.2446 0.2294 0.0290  0.0865  0.0281  108 LEU   B CA  
5764 C C   . LEU   B 108 ? 0.1952 0.1929 0.2155 0.0281  0.0532  0.0307  108 LEU   B C   
5765 O O   . LEU   B 108 ? 0.1849 0.1758 0.2035 0.0212  0.0428  0.0232  108 LEU   B O   
5766 C CB  . LEU   B 108 ? 0.2572 0.2647 0.2080 0.0350  0.0889  0.0353  108 LEU   B CB  
5767 C CG  . LEU   B 108 ? 0.2749 0.2962 0.2275 0.0362  0.0774  0.0203  108 LEU   B CG  
5768 C CD1 . LEU   B 108 ? 0.2880 0.3113 0.2204 0.0290  0.0720  0.0220  108 LEU   B CD1 
5769 C CD2 . LEU   B 108 ? 0.2813 0.3051 0.2327 0.0414  0.0687  0.0018  108 LEU   B CD2 
5782 N N   . LEU   B 109 ? 0.1748 0.1674 0.2065 0.0160  0.0443  0.0318  109 LEU   B N   
5783 C CA  . LEU   B 109 ? 0.1474 0.1414 0.2249 0.0081  0.0414  0.0342  109 LEU   B CA  
5784 C C   . LEU   B 109 ? 0.1410 0.1262 0.2255 0.0043  0.0362  0.0251  109 LEU   B C   
5785 O O   . LEU   B 109 ? 0.1402 0.1248 0.2067 0.0036  0.0358  0.0352  109 LEU   B O   
5786 C CB  . LEU   B 109 ? 0.1557 0.1336 0.2360 0.0049  0.0314  0.0421  109 LEU   B CB  
5787 C CG  . LEU   B 109 ? 0.1562 0.1329 0.2213 0.0049  0.0231  0.0286  109 LEU   B CG  
5788 C CD1 . LEU   B 109 ? 0.1577 0.1466 0.2048 0.0143  0.0288  0.0289  109 LEU   B CD1 
5789 C CD2 . LEU   B 109 ? 0.1696 0.1399 0.2288 0.0058  0.0132  0.0302  109 LEU   B CD2 
5801 N N   . LYS   B 110 ? 0.1376 0.1272 0.2107 -0.0032 0.0342  0.0185  110 LYS   B N   
5802 C CA  . LYS   B 110 ? 0.1365 0.1212 0.2136 -0.0015 0.0304  0.0189  110 LYS   B CA  
5803 C C   . LYS   B 110 ? 0.1356 0.1231 0.2085 -0.0004 0.0311  0.0162  110 LYS   B C   
5804 O O   . LYS   B 110 ? 0.1284 0.1281 0.2029 -0.0087 0.0216  0.0154  110 LYS   B O   
5805 C CB  . LYS   B 110 ? 0.1382 0.1259 0.2394 -0.0059 0.0311  0.0191  110 LYS   B CB  
5806 C CG  . LYS   B 110 ? 0.1383 0.1317 0.2397 -0.0056 0.0220  0.0272  110 LYS   B CG  
5807 C CD  . LYS   B 110 ? 0.1428 0.1279 0.2463 -0.0041 0.0230  0.0204  110 LYS   B CD  
5808 C CE  . LYS   B 110 ? 0.1410 0.1484 0.2739 -0.0037 0.0230  0.0122  110 LYS   B CE  
5809 N NZ  . LYS   B 110 ? 0.1466 0.1625 0.2646 0.0035  0.0164  0.0098  110 LYS   B NZ  
5823 N N   . SER   B 111 ? 0.1413 0.1254 0.2122 0.0012  0.0306  0.0174  111 SER   B N   
5824 C CA  . SER   B 111 ? 0.1459 0.1296 0.1964 0.0053  0.0253  0.0240  111 SER   B CA  
5825 C C   . SER   B 111 ? 0.1375 0.1224 0.1777 -0.0016 0.0187  0.0128  111 SER   B C   
5826 O O   . SER   B 111 ? 0.1335 0.1335 0.1927 -0.0006 0.0161  0.0127  111 SER   B O   
5827 C CB  . SER   B 111 ? 0.1596 0.1521 0.2095 0.0144  0.0405  0.0335  111 SER   B CB  
5828 O OG  . SER   B 111 ? 0.1732 0.1817 0.2220 0.0150  0.0508  0.0329  111 SER   B OG  
5834 N N   . ALA   B 112 ? 0.1307 0.1305 0.1878 0.0085  0.0308  0.0192  112 ALA   B N   
5835 C CA  . ALA   B 112 ? 0.1336 0.1332 0.1711 0.0044  0.0107  0.0092  112 ALA   B CA  
5836 C C   . ALA   B 112 ? 0.1256 0.1247 0.1719 0.0021  0.0160  0.0103  112 ALA   B C   
5837 O O   . ALA   B 112 ? 0.1255 0.1204 0.1729 -0.0053 0.0147  0.0065  112 ALA   B O   
5838 C CB  . ALA   B 112 ? 0.1404 0.1374 0.1802 0.0051  0.0145  0.0190  112 ALA   B CB  
5844 N N   . TYR   B 113 ? 0.1207 0.1166 0.1883 -0.0043 0.0132  0.0210  113 TYR   B N   
5845 C CA  . TYR   B 113 ? 0.1202 0.1117 0.1816 -0.0033 0.0141  0.0090  113 TYR   B CA  
5846 C C   . TYR   B 113 ? 0.1217 0.1062 0.1756 -0.0062 0.0085  0.0093  113 TYR   B C   
5847 O O   . TYR   B 113 ? 0.1254 0.1093 0.1725 -0.0066 0.0036  0.0034  113 TYR   B O   
5848 C CB  . TYR   B 113 ? 0.1246 0.1077 0.1864 0.0022  0.0183  0.0148  113 TYR   B CB  
5849 C CG  . TYR   B 113 ? 0.1261 0.1115 0.1989 -0.0043 0.0123  0.0129  113 TYR   B CG  
5850 C CD1 . TYR   B 113 ? 0.1322 0.1129 0.2078 -0.0033 0.0213  0.0208  113 TYR   B CD1 
5851 C CD2 . TYR   B 113 ? 0.1311 0.1121 0.1980 -0.0080 0.0080  0.0128  113 TYR   B CD2 
5852 C CE1 . TYR   B 113 ? 0.1296 0.1206 0.1992 -0.0062 0.0246  0.0092  113 TYR   B CE1 
5853 C CE2 . TYR   B 113 ? 0.1352 0.1071 0.2080 -0.0000 0.0115  0.0181  113 TYR   B CE2 
5854 C CZ  . TYR   B 113 ? 0.1313 0.1156 0.2129 0.0033  0.0146  0.0139  113 TYR   B CZ  
5855 O OH  . TYR   B 113 ? 0.1416 0.1117 0.2347 0.0086  0.0191  0.0115  113 TYR   B OH  
5865 N N   . GLU   B 114 ? 0.1139 0.1035 0.1872 -0.0077 0.0136  0.0049  114 GLU   B N   
5866 C CA  . GLU   B 114 ? 0.1161 0.1027 0.1810 -0.0003 0.0059  0.0094  114 GLU   B CA  
5867 C C   . GLU   B 114 ? 0.1165 0.1045 0.1762 0.0014  0.0076  0.0057  114 GLU   B C   
5868 O O   . GLU   B 114 ? 0.1181 0.1132 0.1843 0.0016  -0.0021 0.0122  114 GLU   B O   
5869 C CB  . GLU   B 114 ? 0.1182 0.1138 0.1887 -0.0027 0.0123  0.0012  114 GLU   B CB  
5870 C CG  . GLU   B 114 ? 0.1270 0.1117 0.1924 -0.0076 0.0111  0.0094  114 GLU   B CG  
5871 C CD  . GLU   B 114 ? 0.1220 0.1170 0.2003 -0.0067 0.0110  0.0152  114 GLU   B CD  
5872 O OE1 . GLU   B 114 ? 0.1158 0.1321 0.2015 -0.0055 0.0189  0.0139  114 GLU   B OE1 
5873 O OE2 . GLU   B 114 ? 0.1232 0.1359 0.2181 -0.0176 0.0110  0.0129  114 GLU   B OE2 
5880 N N   . ASN   B 115 ? 0.1178 0.1020 0.1747 -0.0040 0.0002  0.0090  115 ASN   B N   
5881 C CA  . ASN   B 115 ? 0.1191 0.1115 0.1612 -0.0109 0.0038  0.0067  115 ASN   B CA  
5882 C C   . ASN   B 115 ? 0.1135 0.1070 0.1670 -0.0086 -0.0063 0.0031  115 ASN   B C   
5883 O O   . ASN   B 115 ? 0.1270 0.1142 0.1701 -0.0097 -0.0035 0.0065  115 ASN   B O   
5884 C CB  . ASN   B 115 ? 0.1322 0.1252 0.1624 -0.0107 0.0043  0.0048  115 ASN   B CB  
5885 C CG  . ASN   B 115 ? 0.1371 0.1274 0.1575 0.0021  0.0012  0.0046  115 ASN   B CG  
5886 O OD1 . ASN   B 115 ? 0.1815 0.1394 0.1849 -0.0017 0.0117  -0.0057 115 ASN   B OD1 
5887 N ND2 . ASN   B 115 ? 0.1351 0.1401 0.1564 -0.0021 0.0023  0.0113  115 ASN   B ND2 
5894 N N   . PHE   B 116 ? 0.1186 0.1111 0.1555 -0.0079 0.0009  0.0047  116 PHE   B N   
5895 C CA  . PHE   B 116 ? 0.1177 0.1137 0.1527 -0.0125 -0.0008 0.0074  116 PHE   B CA  
5896 C C   . PHE   B 116 ? 0.1226 0.1002 0.1559 -0.0138 -0.0049 0.0052  116 PHE   B C   
5897 O O   . PHE   B 116 ? 0.1241 0.1148 0.1648 -0.0062 -0.0082 0.0081  116 PHE   B O   
5898 C CB  . PHE   B 116 ? 0.1138 0.1140 0.1433 -0.0052 -0.0028 0.0045  116 PHE   B CB  
5899 C CG  . PHE   B 116 ? 0.1117 0.1143 0.1514 -0.0096 0.0008  0.0046  116 PHE   B CG  
5900 C CD1 . PHE   B 116 ? 0.1220 0.1177 0.1671 -0.0008 -0.0041 0.0067  116 PHE   B CD1 
5901 C CD2 . PHE   B 116 ? 0.1190 0.1250 0.1495 -0.0068 0.0056  0.0032  116 PHE   B CD2 
5902 C CE1 . PHE   B 116 ? 0.1285 0.1223 0.1695 -0.0047 -0.0070 0.0104  116 PHE   B CE1 
5903 C CE2 . PHE   B 116 ? 0.1170 0.1214 0.1513 -0.0003 0.0032  0.0045  116 PHE   B CE2 
5904 C CZ  . PHE   B 116 ? 0.1118 0.1199 0.1598 -0.0047 -0.0091 0.0081  116 PHE   B CZ  
5914 N N   . ASN   B 117 ? 0.1220 0.1041 0.1722 -0.0062 -0.0081 0.0106  117 ASN   B N   
5915 C CA  . ASN   B 117 ? 0.1297 0.1098 0.1729 -0.0028 -0.0130 0.0069  117 ASN   B CA  
5916 C C   . ASN   B 117 ? 0.1344 0.1093 0.1814 -0.0048 -0.0156 0.0110  117 ASN   B C   
5917 O O   . ASN   B 117 ? 0.1399 0.1137 0.2070 -0.0094 -0.0324 0.0123  117 ASN   B O   
5918 C CB  . ASN   B 117 ? 0.1295 0.1122 0.1755 -0.0029 -0.0121 -0.0030 117 ASN   B CB  
5919 C CG  . ASN   B 117 ? 0.1236 0.1188 0.1847 0.0019  -0.0046 0.0005  117 ASN   B CG  
5920 O OD1 . ASN   B 117 ? 0.1423 0.1178 0.2028 -0.0119 0.0005  -0.0029 117 ASN   B OD1 
5921 N ND2 . ASN   B 117 ? 0.1275 0.1201 0.1765 -0.0037 0.0001  -0.0027 117 ASN   B ND2 
5928 N N   . GLN   B 118 ? 0.1341 0.1050 0.1663 -0.0106 -0.0169 0.0029  118 GLN   B N   
5929 C CA  . GLN   B 118 ? 0.1381 0.1130 0.1803 -0.0030 -0.0159 -0.0013 118 GLN   B CA  
5930 C C   . GLN   B 118 ? 0.1393 0.1066 0.1840 -0.0033 -0.0078 0.0003  118 GLN   B C   
5931 O O   . GLN   B 118 ? 0.1566 0.1095 0.2226 -0.0051 -0.0025 0.0052  118 GLN   B O   
5932 C CB  . GLN   B 118 ? 0.1398 0.1204 0.1915 0.0032  -0.0185 0.0042  118 GLN   B CB  
5933 C CG  . GLN   B 118 ? 0.1486 0.1202 0.1867 0.0064  -0.0146 -0.0037 118 GLN   B CG  
5934 C CD  . GLN   B 118 ? 0.1523 0.1107 0.1909 0.0045  -0.0139 -0.0045 118 GLN   B CD  
5935 O OE1 . GLN   B 118 ? 0.1570 0.1129 0.2102 0.0012  0.0023  0.0101  118 GLN   B OE1 
5936 N NE2 . GLN   B 118 ? 0.1654 0.1152 0.1859 0.0028  -0.0183 0.0028  118 GLN   B NE2 
5945 N N   . HIS   B 119 ? 0.1418 0.1099 0.1540 -0.0107 -0.0093 0.0150  119 HIS   B N   
5946 C CA  . HIS   B 119 ? 0.1526 0.1196 0.1438 -0.0088 -0.0176 0.0119  119 HIS   B CA  
5947 C C   . HIS   B 119 ? 0.1512 0.1258 0.1356 -0.0077 -0.0298 0.0139  119 HIS   B C   
5948 O O   . HIS   B 119 ? 0.1567 0.1280 0.1680 -0.0266 -0.0218 0.0133  119 HIS   B O   
5949 C CB  . HIS   B 119 ? 0.1550 0.1376 0.1459 -0.0004 -0.0241 0.0032  119 HIS   B CB  
5950 C CG  . HIS   B 119 ? 0.1549 0.1637 0.1642 0.0052  -0.0402 -0.0128 119 HIS   B CG  
5951 N ND1 . HIS   B 119 ? 0.1624 0.1816 0.2094 -0.0055 -0.0445 -0.0341 119 HIS   B ND1 
5952 C CD2 . HIS   B 119 ? 0.1744 0.1885 0.1653 0.0360  -0.0468 -0.0184 119 HIS   B CD2 
5953 C CE1 . HIS   B 119 ? 0.1798 0.2021 0.2111 0.0136  -0.0550 -0.0394 119 HIS   B CE1 
5954 N NE2 . HIS   B 119 ? 0.1892 0.2089 0.1869 0.0340  -0.0511 -0.0299 119 HIS   B NE2 
5962 N N   . GLU   B 120 ? 0.1694 0.1306 0.1501 -0.0125 -0.0411 0.0147  120 GLU   B N   
5963 C CA  . GLU   B 120 ? 0.1948 0.1404 0.1545 -0.0077 -0.0546 0.0262  120 GLU   B CA  
5964 C C   . GLU   B 120 ? 0.1729 0.1283 0.1475 -0.0167 -0.0418 0.0197  120 GLU   B C   
5965 O O   . GLU   B 120 ? 0.1683 0.1459 0.1597 -0.0151 -0.0435 0.0119  120 GLU   B O   
5966 C CB  . GLU   B 120 ? 0.2584 0.1760 0.2314 0.0103  -0.0784 0.0513  120 GLU   B CB  
5967 C CG  . GLU   B 120 ? 0.3176 0.2495 0.3379 0.0193  -0.0974 0.0700  120 GLU   B CG  
5968 C CD  . GLU   B 120 ? 0.3597 0.3114 0.4427 0.0222  -0.1082 0.0907  120 GLU   B CD  
5969 O OE1 . GLU   B 120 ? 0.3791 0.3314 0.4728 0.0171  -0.1027 0.1076  120 GLU   B OE1 
5970 O OE2 . GLU   B 120 ? 0.3784 0.3370 0.4986 0.0212  -0.1111 0.0857  120 GLU   B OE2 
5977 N N   . VAL   B 121 ? 0.1655 0.1293 0.1466 -0.0252 -0.0310 0.0234  121 VAL   B N   
5978 C CA  . VAL   B 121 ? 0.1602 0.1387 0.1211 -0.0194 -0.0319 0.0181  121 VAL   B CA  
5979 C C   . VAL   B 121 ? 0.1555 0.1318 0.1289 -0.0291 -0.0206 0.0126  121 VAL   B C   
5980 O O   . VAL   B 121 ? 0.1624 0.1309 0.1504 -0.0380 -0.0292 0.0141  121 VAL   B O   
5981 C CB  . VAL   B 121 ? 0.1809 0.1750 0.1427 -0.0106 -0.0379 0.0199  121 VAL   B CB  
5982 C CG1 . VAL   B 121 ? 0.1914 0.1870 0.1780 -0.0177 -0.0254 0.0226  121 VAL   B CG1 
5983 C CG2 . VAL   B 121 ? 0.2028 0.1991 0.1597 -0.0001 -0.0297 0.0113  121 VAL   B CG2 
5993 N N   . LEU   B 122 ? 0.1443 0.1274 0.1313 -0.0264 -0.0283 0.0137  122 LEU   B N   
5994 C CA  . LEU   B 122 ? 0.1376 0.1343 0.1166 -0.0249 -0.0241 0.0117  122 LEU   B CA  
5995 C C   . LEU   B 122 ? 0.1344 0.1227 0.1256 -0.0287 -0.0195 0.0144  122 LEU   B C   
5996 O O   . LEU   B 122 ? 0.1445 0.1226 0.1597 -0.0344 -0.0301 0.0111  122 LEU   B O   
5997 C CB  . LEU   B 122 ? 0.1583 0.1476 0.1539 -0.0057 -0.0231 0.0171  122 LEU   B CB  
5998 C CG  . LEU   B 122 ? 0.1455 0.1540 0.1615 -0.0190 -0.0091 0.0123  122 LEU   B CG  
5999 C CD1 . LEU   B 122 ? 0.1520 0.1725 0.1504 -0.0307 -0.0142 0.0085  122 LEU   B CD1 
6000 C CD2 . LEU   B 122 ? 0.1454 0.1504 0.1444 -0.0162 -0.0204 0.0025  122 LEU   B CD2 
6012 N N   . LEU   B 123 ? 0.1354 0.1155 0.1140 -0.0248 -0.0226 0.0079  123 LEU   B N   
6013 C CA  . LEU   B 123 ? 0.1377 0.1194 0.1257 -0.0226 -0.0184 0.0039  123 LEU   B CA  
6014 C C   . LEU   B 123 ? 0.1328 0.1137 0.1232 -0.0257 -0.0160 0.0033  123 LEU   B C   
6015 O O   . LEU   B 123 ? 0.1398 0.1195 0.1234 -0.0326 -0.0115 0.0033  123 LEU   B O   
6016 C CB  . LEU   B 123 ? 0.1424 0.1223 0.1318 -0.0215 -0.0120 0.0013  123 LEU   B CB  
6017 C CG  . LEU   B 123 ? 0.1413 0.1255 0.1404 -0.0173 -0.0112 0.0106  123 LEU   B CG  
6018 C CD1 . LEU   B 123 ? 0.1500 0.1295 0.1585 -0.0186 -0.0049 -0.0038 123 LEU   B CD1 
6019 C CD2 . LEU   B 123 ? 0.1510 0.1366 0.1596 -0.0217 -0.0022 0.0169  123 LEU   B CD2 
6031 N N   . ALA   B 124 ? 0.1302 0.1100 0.1202 -0.0222 -0.0102 0.0017  124 ALA   B N   
6032 C CA  . ALA   B 124 ? 0.1262 0.1134 0.1328 -0.0161 -0.0102 -0.0039 124 ALA   B CA  
6033 C C   . ALA   B 124 ? 0.1186 0.1110 0.1297 -0.0204 -0.0074 0.0010  124 ALA   B C   
6034 O O   . ALA   B 124 ? 0.1318 0.1129 0.1395 -0.0190 -0.0122 0.0007  124 ALA   B O   
6035 C CB  . ALA   B 124 ? 0.1321 0.1144 0.1424 -0.0107 0.0065  -0.0007 124 ALA   B CB  
6041 N N   . PRO   B 125 ? 0.1317 0.1144 0.1236 -0.0185 -0.0170 0.0142  125 PRO   B N   
6042 C CA  . PRO   B 125 ? 0.1400 0.1179 0.1432 -0.0175 -0.0165 0.0199  125 PRO   B CA  
6043 C C   . PRO   B 125 ? 0.1345 0.1135 0.1557 -0.0135 -0.0108 0.0088  125 PRO   B C   
6044 O O   . PRO   B 125 ? 0.1338 0.1137 0.1678 -0.0087 -0.0025 0.0160  125 PRO   B O   
6045 C CB  . PRO   B 125 ? 0.1436 0.1450 0.1595 -0.0207 -0.0232 0.0346  125 PRO   B CB  
6046 C CG  . PRO   B 125 ? 0.1513 0.1507 0.1373 -0.0276 -0.0220 0.0234  125 PRO   B CG  
6047 C CD  . PRO   B 125 ? 0.1438 0.1270 0.1348 -0.0357 -0.0093 0.0148  125 PRO   B CD  
6055 N N   . LEU   B 126 ? 0.1422 0.1084 0.1766 -0.0169 0.0116  0.0210  126 LEU   B N   
6056 C CA  . LEU   B 126 ? 0.1485 0.1203 0.1809 -0.0098 0.0197  0.0205  126 LEU   B CA  
6057 C C   . LEU   B 126 ? 0.1407 0.1300 0.1847 0.0008  0.0247  0.0284  126 LEU   B C   
6058 O O   . LEU   B 126 ? 0.1597 0.1586 0.2157 0.0241  0.0018  0.0018  126 LEU   B O   
6059 C CB  . LEU   B 126 ? 0.1642 0.1270 0.2111 -0.0170 0.0245  0.0117  126 LEU   B CB  
6060 C CG  . LEU   B 126 ? 0.1782 0.1335 0.2245 -0.0245 0.0214  -0.0033 126 LEU   B CG  
6061 C CD1 . LEU   B 126 ? 0.1861 0.1383 0.2721 -0.0161 0.0176  -0.0090 126 LEU   B CD1 
6062 C CD2 . LEU   B 126 ? 0.1799 0.1415 0.2188 -0.0404 0.0183  -0.0071 126 LEU   B CD2 
6074 N N   . LEU   B 127 ? 0.1368 0.1169 0.2005 0.0045  0.0295  0.0177  127 LEU   B N   
6075 C CA  . LEU   B 127 ? 0.1410 0.1288 0.2036 0.0008  0.0312  0.0253  127 LEU   B CA  
6076 C C   . LEU   B 127 ? 0.1356 0.1250 0.1956 -0.0020 0.0283  0.0280  127 LEU   B C   
6077 O O   . LEU   B 127 ? 0.1427 0.1260 0.2048 -0.0166 0.0203  0.0253  127 LEU   B O   
6078 C CB  . LEU   B 127 ? 0.1579 0.1255 0.2109 -0.0022 0.0265  0.0200  127 LEU   B CB  
6079 C CG  . LEU   B 127 ? 0.1649 0.1228 0.2211 0.0050  0.0267  0.0143  127 LEU   B CG  
6080 C CD1 . LEU   B 127 ? 0.1722 0.1291 0.2246 0.0131  0.0195  0.0121  127 LEU   B CD1 
6081 C CD2 . LEU   B 127 ? 0.1673 0.1333 0.2292 -0.0098 0.0281  0.0254  127 LEU   B CD2 
6093 N N   . SER   B 128 ? 0.1417 0.1217 0.1972 0.0048  0.0031  0.0192  128 SER   B N   
6094 C CA  . SER   B 128 ? 0.1509 0.1298 0.2027 0.0118  0.0005  0.0294  128 SER   B CA  
6095 C C   . SER   B 128 ? 0.1680 0.1351 0.2318 0.0127  -0.0195 0.0295  128 SER   B C   
6096 O O   . SER   B 128 ? 0.1831 0.1371 0.2732 0.0120  -0.0146 0.0431  128 SER   B O   
6097 C CB  . SER   B 128 ? 0.1629 0.1337 0.1984 0.0066  0.0070  0.0380  128 SER   B CB  
6098 O OG  . SER   B 128 ? 0.1724 0.1488 0.2023 0.0119  0.0068  0.0363  128 SER   B OG  
6104 N N   . ALA   B 129 ? 0.1782 0.1414 0.2568 0.0271  -0.0078 0.0118  129 ALA   B N   
6105 C CA  . ALA   B 129 ? 0.1942 0.1494 0.2673 0.0317  -0.0053 0.0024  129 ALA   B CA  
6106 C C   . ALA   B 129 ? 0.1822 0.1438 0.2477 0.0180  0.0128  0.0070  129 ALA   B C   
6107 O O   . ALA   B 129 ? 0.1708 0.1470 0.2355 0.0184  0.0017  0.0127  129 ALA   B O   
6108 C CB  . ALA   B 129 ? 0.2131 0.1720 0.3097 0.0351  0.0089  -0.0013 129 ALA   B CB  
6114 N N   . GLY   B 130 ? 0.1821 0.1401 0.2598 0.0273  0.0154  -0.0017 130 GLY   B N   
6115 C CA  . GLY   B 130 ? 0.1867 0.1473 0.2685 0.0237  0.0305  -0.0001 130 GLY   B CA  
6116 C C   . GLY   B 130 ? 0.1925 0.1536 0.2593 0.0186  0.0200  0.0098  130 GLY   B C   
6117 O O   . GLY   B 130 ? 0.1999 0.1676 0.2687 0.0192  0.0099  0.0156  130 GLY   B O   
6121 N N   . ILE   B 131 ? 0.1887 0.1730 0.2631 0.0319  0.0207  0.0047  131 ILE   B N   
6122 C CA  . ILE   B 131 ? 0.2091 0.1902 0.2719 0.0347  0.0110  0.0199  131 ILE   B CA  
6123 C C   . ILE   B 131 ? 0.2215 0.1807 0.2325 0.0271  0.0079  0.0285  131 ILE   B C   
6124 O O   . ILE   B 131 ? 0.2489 0.1978 0.2370 0.0297  -0.0089 0.0321  131 ILE   B O   
6125 C CB  . ILE   B 131 ? 0.2095 0.2193 0.3143 0.0305  -0.0010 0.0254  131 ILE   B CB  
6126 C CG1 . ILE   B 131 ? 0.2107 0.2388 0.3323 0.0019  0.0011  0.0319  131 ILE   B CG1 
6127 C CG2 . ILE   B 131 ? 0.2077 0.2322 0.3285 0.0399  -0.0025 0.0188  131 ILE   B CG2 
6128 C CD1 . ILE   B 131 ? 0.2136 0.2584 0.3492 -0.0165 -0.0052 0.0331  131 ILE   B CD1 
6140 N N   . PHE   B 132 ? 0.2064 0.1624 0.2152 0.0185  0.0256  0.0312  132 PHE   B N   
6141 C CA  . PHE   B 132 ? 0.2166 0.1649 0.2206 0.0090  0.0489  0.0237  132 PHE   B CA  
6142 C C   . PHE   B 132 ? 0.2315 0.1768 0.2392 0.0125  0.0571  0.0214  132 PHE   B C   
6143 O O   . PHE   B 132 ? 0.2467 0.1967 0.2529 0.0132  0.0632  0.0260  132 PHE   B O   
6144 C CB  . PHE   B 132 ? 0.2024 0.1605 0.1973 0.0144  0.0453  0.0297  132 PHE   B CB  
6145 C CG  . PHE   B 132 ? 0.1900 0.1588 0.1878 0.0183  0.0282  0.0279  132 PHE   B CG  
6146 C CD1 . PHE   B 132 ? 0.1949 0.1624 0.2285 0.0103  0.0246  0.0200  132 PHE   B CD1 
6147 C CD2 . PHE   B 132 ? 0.1939 0.1648 0.1592 0.0316  0.0214  0.0321  132 PHE   B CD2 
6148 C CE1 . PHE   B 132 ? 0.1974 0.1684 0.2337 0.0066  0.0182  0.0187  132 PHE   B CE1 
6149 C CE2 . PHE   B 132 ? 0.2009 0.1713 0.1657 0.0221  0.0105  0.0249  132 PHE   B CE2 
6150 C CZ  . PHE   B 132 ? 0.2014 0.1732 0.2090 0.0146  0.0059  0.0320  132 PHE   B CZ  
6160 N N   . GLY   B 133 ? 0.2276 0.1642 0.2432 0.0035  0.0372  0.0438  133 GLY   B N   
6161 C CA  . GLY   B 133 ? 0.2353 0.1754 0.2663 -0.0132 0.0310  0.0562  133 GLY   B CA  
6162 C C   . GLY   B 133 ? 0.2364 0.1820 0.2772 -0.0263 0.0399  0.0647  133 GLY   B C   
6163 O O   . GLY   B 133 ? 0.2512 0.1980 0.3182 -0.0432 0.0439  0.0725  133 GLY   B O   
6167 N N   . ALA   B 134 ? 0.2223 0.1805 0.2585 -0.0252 0.0423  0.0460  134 ALA   B N   
6168 C CA  . ALA   B 134 ? 0.2202 0.1763 0.2588 -0.0239 0.0466  0.0297  134 ALA   B CA  
6169 C C   . ALA   B 134 ? 0.2279 0.1656 0.2473 -0.0158 0.0430  0.0389  134 ALA   B C   
6170 O O   . ALA   B 134 ? 0.2290 0.1900 0.2556 0.0005  0.0364  0.0312  134 ALA   B O   
6171 C CB  . ALA   B 134 ? 0.2185 0.1775 0.2834 -0.0209 0.0314  0.0241  134 ALA   B CB  
6177 N N   . ASP   B 135 ? 0.2386 0.1615 0.2573 -0.0095 0.0220  0.0466  135 ASP   B N   
6178 C CA  . ASP   B 135 ? 0.2526 0.1545 0.2755 -0.0034 0.0070  0.0478  135 ASP   B CA  
6179 C C   . ASP   B 135 ? 0.2288 0.1417 0.2540 0.0010  0.0100  0.0421  135 ASP   B C   
6180 O O   . ASP   B 135 ? 0.2175 0.1404 0.2647 -0.0031 0.0155  0.0429  135 ASP   B O   
6181 C CB  . ASP   B 135 ? 0.2821 0.1617 0.3097 -0.0283 0.0054  0.0476  135 ASP   B CB  
6182 C CG  . ASP   B 135 ? 0.3039 0.1646 0.3535 -0.0504 0.0034  0.0430  135 ASP   B CG  
6183 O OD1 . ASP   B 135 ? 0.3085 0.1533 0.3495 -0.0340 -0.0057 0.0433  135 ASP   B OD1 
6184 O OD2 . ASP   B 135 ? 0.3224 0.1963 0.4142 -0.0719 0.0055  0.0195  135 ASP   B OD2 
6189 N N   . PRO   B 136 ? 0.2205 0.1461 0.2662 0.0211  -0.0059 0.0343  136 PRO   B N   
6190 C CA  . PRO   B 136 ? 0.2005 0.1383 0.2679 0.0138  -0.0026 0.0198  136 PRO   B CA  
6191 C C   . PRO   B 136 ? 0.1792 0.1248 0.2713 0.0178  0.0070  0.0165  136 PRO   B C   
6192 O O   . PRO   B 136 ? 0.1605 0.1223 0.2616 0.0098  0.0069  0.0150  136 PRO   B O   
6193 C CB  . PRO   B 136 ? 0.2067 0.1632 0.2806 0.0263  -0.0018 0.0070  136 PRO   B CB  
6194 C CG  . PRO   B 136 ? 0.2267 0.1670 0.2960 0.0272  0.0019  0.0109  136 PRO   B CG  
6195 C CD  . PRO   B 136 ? 0.2298 0.1608 0.2913 0.0349  0.0012  0.0221  136 PRO   B CD  
6203 N N   . ILE   B 137 ? 0.1932 0.1198 0.2819 0.0170  0.0047  0.0112  137 ILE   B N   
6204 C CA  . ILE   B 137 ? 0.2002 0.1172 0.2991 0.0022  0.0039  0.0046  137 ILE   B CA  
6205 C C   . ILE   B 137 ? 0.1860 0.1228 0.2868 -0.0037 0.0142  0.0106  137 ILE   B C   
6206 O O   . ILE   B 137 ? 0.1759 0.1247 0.2810 -0.0027 0.0121  0.0153  137 ILE   B O   
6207 C CB  . ILE   B 137 ? 0.2282 0.1240 0.3439 0.0023  0.0076  0.0114  137 ILE   B CB  
6208 C CG1 . ILE   B 137 ? 0.2493 0.1438 0.3800 0.0101  0.0079  -0.0019 137 ILE   B CG1 
6209 C CG2 . ILE   B 137 ? 0.2347 0.1284 0.3574 -0.0249 0.0122  0.0204  137 ILE   B CG2 
6210 C CD1 . ILE   B 137 ? 0.2666 0.1675 0.4156 0.0207  -0.0012 0.0005  137 ILE   B CD1 
6222 N N   . HIS   B 138 ? 0.1954 0.1211 0.2818 -0.0059 0.0234  0.0124  138 HIS   B N   
6223 C CA  . HIS   B 138 ? 0.2032 0.1331 0.2755 -0.0015 0.0418  0.0222  138 HIS   B CA  
6224 C C   . HIS   B 138 ? 0.1786 0.1327 0.2603 -0.0037 0.0354  0.0282  138 HIS   B C   
6225 O O   . HIS   B 138 ? 0.1692 0.1387 0.2814 0.0013  0.0377  0.0390  138 HIS   B O   
6226 C CB  . HIS   B 138 ? 0.2322 0.1403 0.2872 -0.0063 0.0600  0.0317  138 HIS   B CB  
6227 C CG  . HIS   B 138 ? 0.2528 0.1584 0.2979 -0.0104 0.0784  0.0450  138 HIS   B CG  
6228 N ND1 . HIS   B 138 ? 0.2620 0.1817 0.3277 -0.0100 0.0925  0.0382  138 HIS   B ND1 
6229 C CD2 . HIS   B 138 ? 0.2665 0.1660 0.3023 -0.0152 0.0857  0.0380  138 HIS   B CD2 
6230 C CE1 . HIS   B 138 ? 0.2671 0.1750 0.3245 -0.0080 0.0943  0.0371  138 HIS   B CE1 
6231 N NE2 . HIS   B 138 ? 0.2749 0.1651 0.3069 -0.0023 0.0890  0.0248  138 HIS   B NE2 
6239 N N   . SER   B 139 ? 0.1721 0.1178 0.2542 0.0056  0.0315  0.0178  139 SER   B N   
6240 C CA  . SER   B 139 ? 0.1709 0.1111 0.2402 -0.0017 0.0297  0.0105  139 SER   B CA  
6241 C C   . SER   B 139 ? 0.1486 0.1067 0.2347 -0.0072 0.0233  0.0073  139 SER   B C   
6242 O O   . SER   B 139 ? 0.1486 0.1119 0.2379 -0.0031 0.0093  0.0095  139 SER   B O   
6243 C CB  . SER   B 139 ? 0.1766 0.1141 0.2428 -0.0021 0.0167  0.0116  139 SER   B CB  
6244 O OG  . SER   B 139 ? 0.1784 0.1137 0.2439 0.0009  -0.0043 0.0172  139 SER   B OG  
6250 N N   . LEU   B 140 ? 0.1473 0.1057 0.2350 -0.0059 0.0285  0.0020  140 LEU   B N   
6251 C CA  . LEU   B 140 ? 0.1497 0.1093 0.2361 -0.0028 0.0228  0.0132  140 LEU   B CA  
6252 C C   . LEU   B 140 ? 0.1481 0.1124 0.2485 -0.0030 0.0141  0.0061  140 LEU   B C   
6253 O O   . LEU   B 140 ? 0.1409 0.1152 0.2368 -0.0045 0.0070  0.0102  140 LEU   B O   
6254 C CB  . LEU   B 140 ? 0.1449 0.1111 0.2389 -0.0144 0.0206  0.0013  140 LEU   B CB  
6255 C CG  . LEU   B 140 ? 0.1505 0.1129 0.2357 -0.0132 0.0022  0.0098  140 LEU   B CG  
6256 C CD1 . LEU   B 140 ? 0.1610 0.1267 0.2494 -0.0103 0.0100  -0.0005 140 LEU   B CD1 
6257 C CD2 . LEU   B 140 ? 0.1688 0.1242 0.2516 -0.0121 0.0033  -0.0050 140 LEU   B CD2 
6269 N N   . ARG   B 141 ? 0.1400 0.1128 0.2659 -0.0092 0.0148  0.0072  141 ARG   B N   
6270 C CA  . ARG   B 141 ? 0.1403 0.1102 0.2982 -0.0158 0.0321  -0.0020 141 ARG   B CA  
6271 C C   . ARG   B 141 ? 0.1261 0.1152 0.2884 -0.0142 0.0203  -0.0009 141 ARG   B C   
6272 O O   . ARG   B 141 ? 0.1371 0.1170 0.2829 -0.0123 0.0084  -0.0121 141 ARG   B O   
6273 C CB  . ARG   B 141 ? 0.1623 0.1286 0.3219 -0.0197 0.0467  -0.0054 141 ARG   B CB  
6274 C CG  . ARG   B 141 ? 0.2043 0.1596 0.3343 -0.0254 0.0443  -0.0069 141 ARG   B CG  
6275 C CD  . ARG   B 141 ? 0.2559 0.1778 0.3312 -0.0255 0.0346  -0.0179 141 ARG   B CD  
6276 N NE  . ARG   B 141 ? 0.2848 0.1783 0.3187 -0.0432 0.0425  -0.0195 141 ARG   B NE  
6277 C CZ  . ARG   B 141 ? 0.3080 0.1597 0.2902 -0.0464 0.0502  -0.0347 141 ARG   B CZ  
6278 N NH1 . ARG   B 141 ? 0.3243 0.1534 0.2777 -0.0402 0.0529  -0.0306 141 ARG   B NH1 
6279 N NH2 . ARG   B 141 ? 0.3234 0.1762 0.3038 -0.0293 0.0372  -0.0206 141 ARG   B NH2 
6293 N N   . VAL   B 142 ? 0.1376 0.1071 0.2744 -0.0102 0.0237  -0.0008 142 VAL   B N   
6294 C CA  . VAL   B 142 ? 0.1307 0.1151 0.2536 -0.0035 0.0249  0.0033  142 VAL   B CA  
6295 C C   . VAL   B 142 ? 0.1338 0.1160 0.2559 -0.0040 0.0130  -0.0000 142 VAL   B C   
6296 O O   . VAL   B 142 ? 0.1345 0.1134 0.2698 -0.0000 0.0152  0.0030  142 VAL   B O   
6297 C CB  . VAL   B 142 ? 0.1451 0.1270 0.2526 0.0018  0.0273  0.0185  142 VAL   B CB  
6298 C CG1 . VAL   B 142 ? 0.1446 0.1262 0.2555 0.0047  0.0291  0.0095  142 VAL   B CG1 
6299 C CG2 . VAL   B 142 ? 0.1670 0.1259 0.2596 0.0023  0.0260  0.0201  142 VAL   B CG2 
6309 N N   . CYS   B 143 ? 0.1295 0.1151 0.2311 -0.0008 0.0056  0.0106  143 CYS   B N   
6310 C CA  . CYS   B 143 ? 0.1255 0.1111 0.2398 -0.0066 0.0095  0.0047  143 CYS   B CA  
6311 C C   . CYS   B 143 ? 0.1217 0.1134 0.2422 -0.0094 0.0069  -0.0022 143 CYS   B C   
6312 O O   . CYS   B 143 ? 0.1285 0.1202 0.2451 -0.0027 -0.0055 -0.0007 143 CYS   B O   
6313 C CB  . CYS   B 143 ? 0.1284 0.1199 0.2318 -0.0082 0.0013  0.0111  143 CYS   B CB  
6314 S SG  . CYS   B 143 ? 0.1376 0.1356 0.2202 -0.0060 0.0056  0.0075  143 CYS   B SG  
6320 N N   . VAL   B 144 ? 0.1287 0.1162 0.2596 -0.0075 -0.0026 -0.0104 144 VAL   B N   
6321 C CA  . VAL   B 144 ? 0.1414 0.1285 0.2850 -0.0171 -0.0110 -0.0234 144 VAL   B CA  
6322 C C   . VAL   B 144 ? 0.1307 0.1268 0.2928 -0.0111 -0.0084 0.0002  144 VAL   B C   
6323 O O   . VAL   B 144 ? 0.1387 0.1489 0.3092 -0.0013 -0.0083 0.0241  144 VAL   B O   
6324 C CB  . VAL   B 144 ? 0.1634 0.1379 0.3320 -0.0173 -0.0202 -0.0345 144 VAL   B CB  
6325 C CG1 . VAL   B 144 ? 0.1895 0.1783 0.3575 -0.0061 -0.0296 -0.0303 144 VAL   B CG1 
6326 C CG2 . VAL   B 144 ? 0.1800 0.1381 0.3298 -0.0019 -0.0362 -0.0442 144 VAL   B CG2 
6336 N N   . ASP   B 145 ? 0.1286 0.1210 0.3050 -0.0102 -0.0024 -0.0097 145 ASP   B N   
6337 C CA  . ASP   B 145 ? 0.1310 0.1245 0.3344 -0.0051 0.0107  -0.0033 145 ASP   B CA  
6338 C C   . ASP   B 145 ? 0.1289 0.1273 0.3162 -0.0125 0.0046  -0.0019 145 ASP   B C   
6339 O O   . ASP   B 145 ? 0.1276 0.1358 0.3714 -0.0140 0.0105  -0.0176 145 ASP   B O   
6340 C CB  . ASP   B 145 ? 0.1457 0.1340 0.3828 -0.0141 0.0278  0.0058  145 ASP   B CB  
6341 C CG  . ASP   B 145 ? 0.1591 0.1348 0.4325 -0.0241 0.0320  -0.0018 145 ASP   B CG  
6342 O OD1 . ASP   B 145 ? 0.1631 0.1360 0.4371 -0.0227 -0.0042 -0.0084 145 ASP   B OD1 
6343 O OD2 . ASP   B 145 ? 0.1899 0.1458 0.4702 -0.0366 0.0487  0.0057  145 ASP   B OD2 
6348 N N   . THR   B 146 ? 0.1242 0.1197 0.2578 -0.0103 -0.0008 0.0053  146 THR   B N   
6349 C CA  . THR   B 146 ? 0.1301 0.1168 0.2326 -0.0067 0.0087  0.0023  146 THR   B CA  
6350 C C   . THR   B 146 ? 0.1302 0.1155 0.2225 -0.0088 0.0041  0.0042  146 THR   B C   
6351 O O   . THR   B 146 ? 0.1354 0.1137 0.2355 -0.0080 0.0033  0.0070  146 THR   B O   
6352 C CB  . THR   B 146 ? 0.1327 0.1166 0.2343 -0.0016 0.0224  0.0051  146 THR   B CB  
6353 O OG1 . THR   B 146 ? 0.1371 0.1169 0.2462 -0.0049 0.0236  0.0126  146 THR   B OG1 
6354 C CG2 . THR   B 146 ? 0.1430 0.1253 0.2294 -0.0074 0.0161  -0.0015 146 THR   B CG2 
6362 N N   . VAL   B 147 ? 0.1360 0.1225 0.2041 -0.0031 0.0150  0.0043  147 VAL   B N   
6363 C CA  . VAL   B 147 ? 0.1313 0.1139 0.2024 -0.0127 0.0002  0.0011  147 VAL   B CA  
6364 C C   . VAL   B 147 ? 0.1299 0.1145 0.2156 -0.0198 -0.0073 -0.0007 147 VAL   B C   
6365 O O   . VAL   B 147 ? 0.1439 0.1239 0.2252 -0.0214 -0.0353 -0.0025 147 VAL   B O   
6366 C CB  . VAL   B 147 ? 0.1330 0.1266 0.1868 -0.0064 -0.0050 0.0046  147 VAL   B CB  
6367 C CG1 . VAL   B 147 ? 0.1356 0.1400 0.1856 -0.0084 -0.0058 0.0037  147 VAL   B CG1 
6368 C CG2 . VAL   B 147 ? 0.1362 0.1198 0.1989 -0.0124 -0.0029 0.0015  147 VAL   B CG2 
6378 N N   . ARG   B 148 ? 0.1325 0.1201 0.2010 -0.0145 -0.0170 -0.0085 148 ARG   B N   
6379 C CA  . ARG   B 148 ? 0.1348 0.1248 0.2081 -0.0121 -0.0324 -0.0093 148 ARG   B CA  
6380 C C   . ARG   B 148 ? 0.1392 0.1335 0.1967 -0.0108 -0.0376 -0.0031 148 ARG   B C   
6381 O O   . ARG   B 148 ? 0.1572 0.1600 0.2050 -0.0280 -0.0417 0.0055  148 ARG   B O   
6382 C CB  . ARG   B 148 ? 0.1399 0.1300 0.2094 -0.0067 -0.0310 -0.0182 148 ARG   B CB  
6383 C CG  . ARG   B 148 ? 0.1417 0.1491 0.2160 -0.0075 -0.0288 -0.0353 148 ARG   B CG  
6384 C CD  . ARG   B 148 ? 0.1496 0.1704 0.2283 0.0045  -0.0259 -0.0351 148 ARG   B CD  
6385 N NE  . ARG   B 148 ? 0.1521 0.1702 0.2212 0.0221  -0.0310 -0.0360 148 ARG   B NE  
6386 C CZ  . ARG   B 148 ? 0.1428 0.1614 0.2088 0.0129  -0.0221 -0.0237 148 ARG   B CZ  
6387 N NH1 . ARG   B 148 ? 0.1383 0.1643 0.2157 -0.0045 -0.0117 -0.0248 148 ARG   B NH1 
6388 N NH2 . ARG   B 148 ? 0.1603 0.1488 0.2042 0.0146  -0.0225 -0.0205 148 ARG   B NH2 
6402 N N   . THR   B 149 ? 0.1412 0.1286 0.1994 -0.0120 -0.0377 0.0019  149 THR   B N   
6403 C CA  . THR   B 149 ? 0.1507 0.1286 0.1852 -0.0186 -0.0321 0.0106  149 THR   B CA  
6404 C C   . THR   B 149 ? 0.1473 0.1268 0.1789 -0.0197 -0.0329 0.0069  149 THR   B C   
6405 O O   . THR   B 149 ? 0.1515 0.1266 0.1871 -0.0254 -0.0170 0.0081  149 THR   B O   
6406 C CB  . THR   B 149 ? 0.1522 0.1295 0.1861 -0.0195 -0.0322 0.0057  149 THR   B CB  
6407 O OG1 . THR   B 149 ? 0.1480 0.1375 0.1818 -0.0232 -0.0360 0.0081  149 THR   B OG1 
6408 C CG2 . THR   B 149 ? 0.1611 0.1312 0.1865 -0.0088 -0.0177 0.0015  149 THR   B CG2 
6416 N N   . ASN   B 150 ? 0.1549 0.1272 0.1690 -0.0215 -0.0357 0.0067  150 ASN   B N   
6417 C CA  . ASN   B 150 ? 0.1646 0.1469 0.1545 -0.0241 -0.0376 0.0002  150 ASN   B CA  
6418 C C   . ASN   B 150 ? 0.1515 0.1402 0.1588 -0.0221 -0.0331 -0.0020 150 ASN   B C   
6419 O O   . ASN   B 150 ? 0.1579 0.1319 0.1824 -0.0305 -0.0419 0.0021  150 ASN   B O   
6420 C CB  . ASN   B 150 ? 0.1913 0.1826 0.1696 -0.0255 -0.0479 0.0131  150 ASN   B CB  
6421 C CG  . ASN   B 150 ? 0.2128 0.2221 0.2016 -0.0260 -0.0529 0.0280  150 ASN   B CG  
6422 O OD1 . ASN   B 150 ? 0.2161 0.2373 0.2136 -0.0335 -0.0688 0.0276  150 ASN   B OD1 
6423 N ND2 . ASN   B 150 ? 0.2301 0.2443 0.2396 -0.0143 -0.0514 0.0656  150 ASN   B ND2 
6430 N N   . VAL   B 151 ? 0.1444 0.1359 0.1575 -0.0257 -0.0365 0.0076  151 VAL   B N   
6431 C CA  . VAL   B 151 ? 0.1463 0.1326 0.1586 -0.0248 -0.0251 0.0044  151 VAL   B CA  
6432 C C   . VAL   B 151 ? 0.1501 0.1271 0.1541 -0.0343 -0.0287 0.0025  151 VAL   B C   
6433 O O   . VAL   B 151 ? 0.1584 0.1395 0.1847 -0.0310 -0.0255 -0.0062 151 VAL   B O   
6434 C CB  . VAL   B 151 ? 0.1640 0.1432 0.1759 -0.0155 -0.0248 0.0017  151 VAL   B CB  
6435 C CG1 . VAL   B 151 ? 0.1743 0.1531 0.2004 -0.0177 -0.0129 -0.0058 151 VAL   B CG1 
6436 C CG2 . VAL   B 151 ? 0.1736 0.1600 0.1651 -0.0034 -0.0252 0.0116  151 VAL   B CG2 
6446 N N   . TYR   B 152 ? 0.1464 0.1149 0.1568 -0.0256 -0.0274 -0.0028 152 TYR   B N   
6447 C CA  . TYR   B 152 ? 0.1487 0.1361 0.1458 -0.0314 -0.0207 -0.0073 152 TYR   B CA  
6448 C C   . TYR   B 152 ? 0.1439 0.1202 0.1367 -0.0244 -0.0145 -0.0050 152 TYR   B C   
6449 O O   . TYR   B 152 ? 0.1556 0.1195 0.1531 -0.0302 -0.0190 0.0018  152 TYR   B O   
6450 C CB  . TYR   B 152 ? 0.1554 0.1525 0.1509 -0.0372 -0.0065 0.0054  152 TYR   B CB  
6451 C CG  . TYR   B 152 ? 0.1742 0.1650 0.1405 -0.0454 -0.0190 0.0026  152 TYR   B CG  
6452 C CD1 . TYR   B 152 ? 0.1838 0.1745 0.1372 -0.0368 -0.0282 0.0099  152 TYR   B CD1 
6453 C CD2 . TYR   B 152 ? 0.1988 0.1833 0.1437 -0.0445 -0.0133 0.0032  152 TYR   B CD2 
6454 C CE1 . TYR   B 152 ? 0.2048 0.1946 0.1511 -0.0372 -0.0334 0.0209  152 TYR   B CE1 
6455 C CE2 . TYR   B 152 ? 0.2086 0.2039 0.1446 -0.0441 -0.0208 0.0025  152 TYR   B CE2 
6456 C CZ  . TYR   B 152 ? 0.2129 0.2161 0.1352 -0.0418 -0.0448 0.0245  152 TYR   B CZ  
6457 O OH  . TYR   B 152 ? 0.2374 0.2467 0.1813 -0.0336 -0.0483 0.0316  152 TYR   B OH  
6467 N N   . LEU   B 153 ? 0.1524 0.1198 0.1482 -0.0323 -0.0119 -0.0008 153 LEU   B N   
6468 C CA  . LEU   B 153 ? 0.1529 0.1143 0.1439 -0.0216 -0.0075 -0.0046 153 LEU   B CA  
6469 C C   . LEU   B 153 ? 0.1530 0.1158 0.1537 -0.0299 -0.0082 -0.0137 153 LEU   B C   
6470 O O   . LEU   B 153 ? 0.1586 0.1359 0.1681 -0.0184 -0.0107 -0.0297 153 LEU   B O   
6471 C CB  . LEU   B 153 ? 0.1516 0.1186 0.1575 -0.0292 0.0004  -0.0031 153 LEU   B CB  
6472 C CG  . LEU   B 153 ? 0.1435 0.1282 0.1774 -0.0224 -0.0008 -0.0025 153 LEU   B CG  
6473 C CD1 . LEU   B 153 ? 0.1508 0.1431 0.1932 -0.0282 -0.0025 0.0087  153 LEU   B CD1 
6474 C CD2 . LEU   B 153 ? 0.1483 0.1373 0.1784 -0.0231 0.0094  0.0068  153 LEU   B CD2 
6486 N N   . ALA   B 154 ? 0.1434 0.1201 0.1600 -0.0103 -0.0104 -0.0109 154 ALA   B N   
6487 C CA  . ALA   B 154 ? 0.1549 0.1324 0.1692 -0.0054 -0.0119 -0.0240 154 ALA   B CA  
6488 C C   . ALA   B 154 ? 0.1638 0.1338 0.1720 -0.0023 -0.0163 -0.0258 154 ALA   B C   
6489 O O   . ALA   B 154 ? 0.1909 0.1381 0.1944 0.0040  -0.0126 -0.0035 154 ALA   B O   
6490 C CB  . ALA   B 154 ? 0.1572 0.1493 0.1896 -0.0102 -0.0070 -0.0286 154 ALA   B CB  
6496 N N   . VAL   B 155 ? 0.1366 0.1240 0.1963 -0.0077 -0.0017 -0.0174 155 VAL   B N   
6497 C CA  . VAL   B 155 ? 0.1371 0.1258 0.2234 -0.0075 -0.0113 -0.0090 155 VAL   B CA  
6498 C C   . VAL   B 155 ? 0.1356 0.1215 0.2196 -0.0049 -0.0099 -0.0234 155 VAL   B C   
6499 O O   . VAL   B 155 ? 0.1521 0.1404 0.2529 0.0043  -0.0015 -0.0400 155 VAL   B O   
6500 C CB  . VAL   B 155 ? 0.1442 0.1415 0.2536 -0.0041 -0.0177 0.0014  155 VAL   B CB  
6501 C CG1 . VAL   B 155 ? 0.1488 0.1415 0.2526 -0.0058 -0.0088 -0.0042 155 VAL   B CG1 
6502 C CG2 . VAL   B 155 ? 0.1345 0.1539 0.2705 -0.0065 -0.0148 0.0300  155 VAL   B CG2 
6512 N N   . PHE   B 156 ? 0.1261 0.1357 0.2419 -0.0031 -0.0079 -0.0192 156 PHE   B N   
6513 C CA  . PHE   B 156 ? 0.1338 0.1425 0.2605 0.0031  -0.0035 -0.0231 156 PHE   B CA  
6514 C C   . PHE   B 156 ? 0.1306 0.1482 0.3014 0.0137  -0.0078 -0.0362 156 PHE   B C   
6515 O O   . PHE   B 156 ? 0.1524 0.1679 0.3269 0.0209  0.0023  -0.0489 156 PHE   B O   
6516 C CB  . PHE   B 156 ? 0.1396 0.1377 0.2488 -0.0016 -0.0054 -0.0153 156 PHE   B CB  
6517 C CG  . PHE   B 156 ? 0.1383 0.1451 0.2703 -0.0001 -0.0101 0.0027  156 PHE   B CG  
6518 C CD1 . PHE   B 156 ? 0.1431 0.1727 0.2998 0.0050  0.0026  0.0290  156 PHE   B CD1 
6519 C CD2 . PHE   B 156 ? 0.1481 0.1568 0.2704 0.0126  -0.0102 0.0095  156 PHE   B CD2 
6520 C CE1 . PHE   B 156 ? 0.1455 0.1863 0.3117 -0.0006 0.0001  0.0290  156 PHE   B CE1 
6521 C CE2 . PHE   B 156 ? 0.1536 0.1842 0.2946 0.0135  -0.0162 0.0140  156 PHE   B CE2 
6522 C CZ  . PHE   B 156 ? 0.1441 0.1888 0.3139 0.0110  -0.0214 0.0193  156 PHE   B CZ  
6532 N N   . ASP   B 157 ? 0.1347 0.1387 0.3310 0.0143  -0.0226 -0.0217 157 ASP   B N   
6533 C CA  . ASP   B 157 ? 0.1487 0.1413 0.3626 0.0106  -0.0280 -0.0313 157 ASP   B CA  
6534 C C   . ASP   B 157 ? 0.1463 0.1451 0.3743 0.0112  -0.0210 -0.0512 157 ASP   B C   
6535 O O   . ASP   B 157 ? 0.1327 0.1470 0.3649 0.0106  -0.0244 -0.0398 157 ASP   B O   
6536 C CB  . ASP   B 157 ? 0.1781 0.1576 0.3751 0.0115  -0.0543 -0.0122 157 ASP   B CB  
6537 C CG  . ASP   B 157 ? 0.2175 0.1679 0.4021 0.0039  -0.0485 -0.0184 157 ASP   B CG  
6538 O OD1 . ASP   B 157 ? 0.2264 0.1656 0.4191 0.0078  -0.0351 -0.0159 157 ASP   B OD1 
6539 O OD2 . ASP   B 157 ? 0.2480 0.1867 0.4240 -0.0008 -0.0352 -0.0192 157 ASP   B OD2 
6544 N N   . LYS   B 158 ? 0.1506 0.1746 0.3804 0.0111  -0.0092 -0.0854 158 LYS   B N   
6545 C CA  . LYS   B 158 ? 0.1704 0.1976 0.3857 0.0083  0.0008  -0.1043 158 LYS   B CA  
6546 C C   . LYS   B 158 ? 0.1671 0.1833 0.4028 0.0124  -0.0067 -0.0948 158 LYS   B C   
6547 O O   . LYS   B 158 ? 0.1690 0.1791 0.4068 0.0037  -0.0138 -0.1003 158 LYS   B O   
6548 C CB  . LYS   B 158 ? 0.2013 0.2411 0.3813 0.0070  0.0127  -0.1287 158 LYS   B CB  
6549 C CG  . LYS   B 158 ? 0.2343 0.2882 0.3819 0.0047  0.0162  -0.1419 158 LYS   B CG  
6550 C CD  . LYS   B 158 ? 0.2587 0.3374 0.3910 0.0003  0.0230  -0.1363 158 LYS   B CD  
6551 C CE  . LYS   B 158 ? 0.2777 0.3688 0.3979 0.0019  0.0279  -0.1297 158 LYS   B CE  
6552 N NZ  . LYS   B 158 ? 0.2759 0.3845 0.3940 -0.0003 0.0337  -0.1285 158 LYS   B NZ  
6566 N N   . ASN   B 159 ? 0.1687 0.1718 0.4283 0.0077  -0.0208 -0.0782 159 ASN   B N   
6567 C CA  . ASN   B 159 ? 0.1808 0.1616 0.4456 0.0270  -0.0381 -0.0636 159 ASN   B CA  
6568 C C   . ASN   B 159 ? 0.1680 0.1466 0.4302 0.0181  -0.0484 -0.0492 159 ASN   B C   
6569 O O   . ASN   B 159 ? 0.1651 0.1384 0.4381 0.0023  -0.0605 -0.0338 159 ASN   B O   
6570 C CB  . ASN   B 159 ? 0.2048 0.1762 0.4757 0.0502  -0.0500 -0.0620 159 ASN   B CB  
6571 C CG  . ASN   B 159 ? 0.2391 0.2111 0.5039 0.0525  -0.0634 -0.0627 159 ASN   B CG  
6572 O OD1 . ASN   B 159 ? 0.2614 0.2303 0.5135 0.0566  -0.0623 -0.0697 159 ASN   B OD1 
6573 N ND2 . ASN   B 159 ? 0.2387 0.2231 0.5166 0.0587  -0.0763 -0.0556 159 ASN   B ND2 
6580 N N   . LEU   B 160 ? 0.1520 0.1409 0.3988 0.0078  -0.0505 -0.0392 160 LEU   B N   
6581 C CA  . LEU   B 160 ? 0.1487 0.1440 0.3605 0.0111  -0.0418 -0.0223 160 LEU   B CA  
6582 C C   . LEU   B 160 ? 0.1411 0.1311 0.3419 0.0012  -0.0288 -0.0337 160 LEU   B C   
6583 O O   . LEU   B 160 ? 0.1324 0.1384 0.3304 -0.0010 -0.0341 -0.0150 160 LEU   B O   
6584 C CB  . LEU   B 160 ? 0.1489 0.1571 0.3403 0.0131  -0.0405 -0.0088 160 LEU   B CB  
6585 C CG  . LEU   B 160 ? 0.1491 0.1689 0.3108 0.0114  -0.0338 -0.0033 160 LEU   B CG  
6586 C CD1 . LEU   B 160 ? 0.1625 0.1856 0.3030 -0.0010 -0.0143 -0.0124 160 LEU   B CD1 
6587 C CD2 . LEU   B 160 ? 0.1539 0.1709 0.3038 0.0243  -0.0359 -0.0084 160 LEU   B CD2 
6599 N N   . TYR   B 161 ? 0.1473 0.1389 0.3421 -0.0065 -0.0030 -0.0439 161 TYR   B N   
6600 C CA  . TYR   B 161 ? 0.1531 0.1386 0.3269 -0.0175 0.0190  -0.0453 161 TYR   B CA  
6601 C C   . TYR   B 161 ? 0.1570 0.1407 0.3181 -0.0108 0.0257  -0.0345 161 TYR   B C   
6602 O O   . TYR   B 161 ? 0.1571 0.1447 0.3048 -0.0155 0.0173  -0.0290 161 TYR   B O   
6603 C CB  . TYR   B 161 ? 0.1685 0.1498 0.3278 -0.0257 0.0370  -0.0544 161 TYR   B CB  
6604 C CG  . TYR   B 161 ? 0.1940 0.1513 0.3234 -0.0342 0.0476  -0.0535 161 TYR   B CG  
6605 C CD1 . TYR   B 161 ? 0.2027 0.1493 0.3124 -0.0463 0.0541  -0.0524 161 TYR   B CD1 
6606 C CD2 . TYR   B 161 ? 0.2148 0.1605 0.3134 -0.0267 0.0490  -0.0556 161 TYR   B CD2 
6607 C CE1 . TYR   B 161 ? 0.2219 0.1721 0.3121 -0.0428 0.0548  -0.0563 161 TYR   B CE1 
6608 C CE2 . TYR   B 161 ? 0.2345 0.1806 0.3169 -0.0320 0.0526  -0.0549 161 TYR   B CE2 
6609 C CZ  . TYR   B 161 ? 0.2390 0.1821 0.3138 -0.0481 0.0430  -0.0509 161 TYR   B CZ  
6610 O OH  . TYR   B 161 ? 0.2681 0.2024 0.3339 -0.0544 0.0387  -0.0456 161 TYR   B OH  
6620 N N   . ASP   B 162 ? 0.1595 0.1381 0.3331 -0.0098 0.0102  -0.0534 162 ASP   B N   
6621 C CA  . ASP   B 162 ? 0.1684 0.1485 0.3392 -0.0054 0.0029  -0.0507 162 ASP   B CA  
6622 C C   . ASP   B 162 ? 0.1673 0.1406 0.3272 -0.0101 -0.0022 -0.0385 162 ASP   B C   
6623 O O   . ASP   B 162 ? 0.1696 0.1466 0.3288 -0.0175 -0.0249 -0.0296 162 ASP   B O   
6624 C CB  . ASP   B 162 ? 0.1833 0.1616 0.3590 -0.0039 -0.0089 -0.0726 162 ASP   B CB  
6625 C CG  . ASP   B 162 ? 0.1903 0.1860 0.3798 0.0039  -0.0058 -0.0861 162 ASP   B CG  
6626 O OD1 . ASP   B 162 ? 0.1941 0.2043 0.3705 -0.0105 0.0094  -0.0839 162 ASP   B OD1 
6627 O OD2 . ASP   B 162 ? 0.1986 0.2173 0.4040 0.0222  -0.0071 -0.0783 162 ASP   B OD2 
6632 N N   . LYS   B 163 ? 0.1633 0.1290 0.3231 -0.0060 -0.0192 -0.0283 163 LYS   B N   
6633 C CA  . LYS   B 163 ? 0.1698 0.1387 0.3245 -0.0152 -0.0180 -0.0068 163 LYS   B CA  
6634 C C   . LYS   B 163 ? 0.1436 0.1338 0.3110 -0.0160 -0.0194 0.0043  163 LYS   B C   
6635 O O   . LYS   B 163 ? 0.1457 0.1431 0.3321 -0.0214 -0.0235 0.0123  163 LYS   B O   
6636 C CB  . LYS   B 163 ? 0.2164 0.1724 0.3640 -0.0120 -0.0177 0.0125  163 LYS   B CB  
6637 C CG  . LYS   B 163 ? 0.2963 0.2524 0.4257 -0.0157 -0.0008 0.0170  163 LYS   B CG  
6638 C CD  . LYS   B 163 ? 0.3620 0.3190 0.4831 -0.0243 0.0074  0.0149  163 LYS   B CD  
6639 C CE  . LYS   B 163 ? 0.4146 0.3681 0.5201 -0.0327 0.0167  0.0146  163 LYS   B CE  
6640 N NZ  . LYS   B 163 ? 0.4475 0.3983 0.5437 -0.0374 0.0218  0.0104  163 LYS   B NZ  
6654 N N   . LEU   B 164 ? 0.1369 0.1269 0.2820 -0.0166 -0.0154 0.0027  164 LEU   B N   
6655 C CA  . LEU   B 164 ? 0.1383 0.1269 0.2580 -0.0179 -0.0252 0.0042  164 LEU   B CA  
6656 C C   . LEU   B 164 ? 0.1453 0.1265 0.2616 -0.0249 -0.0312 0.0079  164 LEU   B C   
6657 O O   . LEU   B 164 ? 0.1545 0.1519 0.2832 -0.0240 -0.0324 0.0143  164 LEU   B O   
6658 C CB  . LEU   B 164 ? 0.1305 0.1289 0.2542 -0.0101 -0.0194 -0.0006 164 LEU   B CB  
6659 C CG  . LEU   B 164 ? 0.1426 0.1407 0.2604 -0.0166 -0.0123 0.0073  164 LEU   B CG  
6660 C CD1 . LEU   B 164 ? 0.1513 0.1427 0.2573 -0.0189 -0.0219 -0.0036 164 LEU   B CD1 
6661 C CD2 . LEU   B 164 ? 0.1569 0.1689 0.2835 -0.0182 -0.0061 -0.0000 164 LEU   B CD2 
6673 N N   . VAL   B 165 ? 0.1763 0.1393 0.2863 -0.0254 -0.0413 0.0034  165 VAL   B N   
6674 C CA  . VAL   B 165 ? 0.2134 0.1452 0.2932 -0.0415 -0.0650 0.0046  165 VAL   B CA  
6675 C C   . VAL   B 165 ? 0.2459 0.1604 0.3326 -0.0451 -0.0879 0.0095  165 VAL   B C   
6676 O O   . VAL   B 165 ? 0.2627 0.1788 0.3405 -0.0488 -0.0954 0.0124  165 VAL   B O   
6677 C CB  . VAL   B 165 ? 0.2359 0.1621 0.3002 -0.0226 -0.0327 -0.0026 165 VAL   B CB  
6678 C CG1 . VAL   B 165 ? 0.2502 0.1699 0.3217 -0.0198 -0.0230 0.0064  165 VAL   B CG1 
6679 C CG2 . VAL   B 165 ? 0.2305 0.1683 0.2944 -0.0152 -0.0175 -0.0052 165 VAL   B CG2 
6689 N N   . SER   B 166 ? 0.2556 0.1458 0.3747 -0.0472 -0.1037 -0.0156 166 SER   B N   
6690 C CA  . SER   B 166 ? 0.2472 0.1496 0.4321 -0.0424 -0.0904 -0.0262 166 SER   B CA  
6691 C C   . SER   B 166 ? 0.2334 0.1635 0.4467 -0.0483 -0.0844 0.0026  166 SER   B C   
6692 O O   . SER   B 166 ? 0.2351 0.1859 0.4711 -0.0608 -0.0954 -0.0194 166 SER   B O   
6693 C CB  . SER   B 166 ? 0.2448 0.1581 0.4678 -0.0376 -0.0833 -0.0339 166 SER   B CB  
6694 O OG  . SER   B 166 ? 0.2342 0.1556 0.4902 -0.0332 -0.0842 -0.0180 166 SER   B OG  
6700 N N   . SER   B 167 ? 0.2119 0.1524 0.4160 -0.0516 -0.0874 0.0412  167 SER   B N   
6701 C CA  . SER   B 167 ? 0.2021 0.1625 0.3991 -0.0443 -0.0690 0.0460  167 SER   B CA  
6702 C C   . SER   B 167 ? 0.1926 0.1732 0.3727 -0.0589 -0.0663 0.0571  167 SER   B C   
6703 O O   . SER   B 167 ? 0.1934 0.1868 0.3690 -0.0585 -0.0606 0.0533  167 SER   B O   
6704 C CB  . SER   B 167 ? 0.1908 0.1646 0.4117 -0.0398 -0.0368 0.0432  167 SER   B CB  
6705 O OG  . SER   B 167 ? 0.1874 0.1770 0.4027 -0.0233 -0.0159 0.0375  167 SER   B OG  
6711 N N   . PHE   B 168 ? 0.1965 0.1747 0.3573 -0.0512 -0.0477 0.0654  168 PHE   B N   
6712 C CA  . PHE   B 168 ? 0.1990 0.1744 0.3152 -0.0484 -0.0391 0.0395  168 PHE   B CA  
6713 C C   . PHE   B 168 ? 0.1724 0.1581 0.2603 -0.0295 -0.0229 0.0196  168 PHE   B C   
6714 O O   . PHE   B 168 ? 0.2063 0.1482 0.2570 0.0025  -0.0136 0.0011  168 PHE   B O   
6715 C CB  . PHE   B 168 ? 0.2125 0.1773 0.3131 -0.0606 -0.0491 0.0503  168 PHE   B CB  
6716 C CG  . PHE   B 168 ? 0.2409 0.1602 0.3027 -0.0589 -0.0501 0.0200  168 PHE   B CG  
6717 C CD1 . PHE   B 168 ? 0.2702 0.1642 0.3184 -0.0508 -0.0519 0.0152  168 PHE   B CD1 
6718 C CD2 . PHE   B 168 ? 0.2330 0.1476 0.3010 -0.0506 -0.0449 0.0264  168 PHE   B CD2 
6719 C CE1 . PHE   B 168 ? 0.2801 0.1729 0.3151 -0.0395 -0.0418 0.0208  168 PHE   B CE1 
6720 C CE2 . PHE   B 168 ? 0.2591 0.1595 0.3054 -0.0311 -0.0491 0.0198  168 PHE   B CE2 
6721 C CZ  . PHE   B 168 ? 0.2719 0.1571 0.3140 -0.0263 -0.0502 0.0359  168 PHE   B CZ  
6731 N N   . LEU   B 169 ? 0.1767 0.1644 0.2518 -0.0093 -0.0064 0.0054  169 LEU   B N   
6732 C CA  . LEU   B 169 ? 0.2046 0.1966 0.2849 -0.0114 0.0048  -0.0283 169 LEU   B CA  
6733 C C   . LEU   B 169 ? 0.2324 0.2203 0.3400 0.0041  -0.0005 -0.0566 169 LEU   B C   
6734 O O   . LEU   B 169 ? 0.2473 0.2369 0.3958 0.0018  -0.0056 -0.0791 169 LEU   B O   
6735 C CB  . LEU   B 169 ? 0.2215 0.2355 0.2999 -0.0146 0.0013  -0.0044 169 LEU   B CB  
6736 C CG  . LEU   B 169 ? 0.2565 0.2747 0.3406 -0.0023 0.0049  0.0024  169 LEU   B CG  
6737 C CD1 . LEU   B 169 ? 0.2683 0.2900 0.3433 -0.0038 0.0028  0.0163  169 LEU   B CD1 
6738 C CD2 . LEU   B 169 ? 0.2509 0.2815 0.3446 0.0127  0.0217  -0.0084 169 LEU   B CD2 
6739 O OXT . LEU   B 169 ? 0.2507 0.2375 0.3434 0.0334  0.0091  -0.0530 169 LEU   B OXT 
6751 C C1  T TFA   C .   ? 0.1375 0.1577 0.1140 -0.0269 0.0193  0.0171  201 TFA   A C1  
6752 C C2  T TFA   C .   ? 0.1533 0.1730 0.1580 -0.0344 0.0017  0.0149  201 TFA   A C2  
6753 O O   T TFA   C .   ? 0.1296 0.1472 0.1088 -0.0248 0.0286  0.0191  201 TFA   A O   
6754 F F1  T TFA   C .   ? 0.1469 0.1704 0.1812 -0.0421 -0.0199 0.0104  201 TFA   A F1  
6755 F F2  T TFA   C .   ? 0.1595 0.1800 0.1609 -0.0351 -0.0009 0.0134  201 TFA   A F2  
6756 F F3  T TFA   C .   ? 0.1699 0.1841 0.1817 -0.0380 0.0130  0.0162  201 TFA   A F3  
6757 O OXT T TFA   C .   ? 0.1273 0.1501 0.0886 -0.0198 0.0351  0.0128  201 TFA   A OXT 
6758 O O1  B A1A66 D .   ? 0.1263 0.1331 0.1268 -0.0114 0.0047  0.0139  202 A1A66 A O1  
6759 C C1  B A1A66 D .   ? 0.1195 0.1173 0.0963 -0.0128 0.0149  0.0242  202 A1A66 A C1  
6760 C C2  B A1A66 D .   ? 0.1254 0.1203 0.1153 -0.0116 0.0085  0.0245  202 A1A66 A C2  
6761 C C3  B A1A66 D .   ? 0.1391 0.1319 0.1289 -0.0108 0.0030  0.0248  202 A1A66 A C3  
6762 C C4  B A1A66 D .   ? 0.1576 0.1327 0.1385 -0.0073 -0.0004 0.0376  202 A1A66 A C4  
6763 C C5  B A1A66 D .   ? 0.1777 0.1493 0.1575 -0.0119 0.0032  0.0312  202 A1A66 A C5  
6764 C C6  B A1A66 D .   ? 0.1762 0.1416 0.1527 -0.0094 -0.0075 0.0342  202 A1A66 A C6  
6765 C C7  B A1A66 D .   ? 0.1321 0.1120 0.1284 -0.0092 0.0104  0.0400  202 A1A66 A C7  
6766 C C8  B A1A66 D .   ? 0.1209 0.1219 0.1310 -0.0060 0.0020  0.0306  202 A1A66 A C8  
6767 C C10 B A1A66 D .   ? 0.1236 0.1292 0.1369 -0.0087 0.0006  0.0300  202 A1A66 A C10 
6768 C C11 B A1A66 D .   ? 0.1193 0.1282 0.1329 -0.0091 0.0002  0.0317  202 A1A66 A C11 
6769 C C12 B A1A66 D .   ? 0.1222 0.1352 0.1307 -0.0089 -0.0001 0.0351  202 A1A66 A C12 
6770 C C13 B A1A66 D .   ? 0.1237 0.1328 0.1399 -0.0104 -0.0046 0.0293  202 A1A66 A C13 
6771 C C9  B A1A66 D .   ? 0.1283 0.1370 0.1450 -0.0035 0.0013  0.0392  202 A1A66 A C9  
6772 N N1  B A1A66 D .   ? 0.1183 0.1116 0.1230 -0.0064 0.0050  0.0327  202 A1A66 A N1  
6773 N N2  B A1A66 D .   ? 0.1247 0.1293 0.1439 -0.0048 0.0012  0.0358  202 A1A66 A N2  
6774 N N3  B A1A66 D .   ? 0.1288 0.1341 0.1416 -0.0059 0.0057  0.0412  202 A1A66 A N3  
6775 N N4  B A1A66 D .   ? 0.1258 0.1297 0.1357 -0.0053 -0.0071 0.0292  202 A1A66 A N4  
6792 O O1  C A1A66 E .   ? 0.1335 0.1441 0.1712 0.0086  -0.0226 -0.0005 203 A1A66 A O1  
6793 C C1  C A1A66 E .   ? 0.1245 0.1329 0.1551 0.0097  -0.0174 -0.0012 203 A1A66 A C1  
6794 C C2  C A1A66 E .   ? 0.1180 0.1258 0.1434 0.0023  -0.0191 0.0124  203 A1A66 A C2  
6795 C C3  C A1A66 E .   ? 0.1248 0.1317 0.1383 0.0038  -0.0184 0.0173  203 A1A66 A C3  
6796 C C4  C A1A66 E .   ? 0.1296 0.1256 0.1409 0.0031  -0.0232 0.0172  203 A1A66 A C4  
6797 C C5  C A1A66 E .   ? 0.1379 0.1246 0.1414 0.0053  -0.0264 0.0117  203 A1A66 A C5  
6798 C C6  C A1A66 E .   ? 0.1370 0.1239 0.1392 0.0064  -0.0287 0.0178  203 A1A66 A C6  
6799 C C7  C A1A66 E .   ? 0.1152 0.1096 0.1362 0.0024  -0.0212 0.0255  203 A1A66 A C7  
6800 C C8  C A1A66 E .   ? 0.1052 0.1151 0.1341 -0.0069 -0.0023 0.0264  203 A1A66 A C8  
6801 C C10 C A1A66 E .   ? 0.1020 0.1118 0.1357 -0.0099 -0.0017 0.0285  203 A1A66 A C10 
6802 C C11 C A1A66 E .   ? 0.0986 0.1155 0.1334 -0.0091 -0.0019 0.0298  203 A1A66 A C11 
6803 C C12 C A1A66 E .   ? 0.0958 0.1198 0.1274 -0.0074 0.0031  0.0335  203 A1A66 A C12 
6804 C C13 C A1A66 E .   ? 0.0987 0.1143 0.1378 -0.0099 -0.0072 0.0275  203 A1A66 A C13 
6805 C C9  C A1A66 E .   ? 0.1064 0.1242 0.1419 -0.0073 0.0023  0.0387  203 A1A66 A C9  
6806 N N1  C A1A66 E .   ? 0.1099 0.1131 0.1410 -0.0044 -0.0177 0.0234  203 A1A66 A N1  
6807 N N2  C A1A66 E .   ? 0.0998 0.1181 0.1387 -0.0095 0.0033  0.0341  203 A1A66 A N2  
6808 N N3  C A1A66 E .   ? 0.1073 0.1182 0.1408 -0.0092 0.0066  0.0411  203 A1A66 A N3  
6809 N N4  C A1A66 E .   ? 0.1033 0.1101 0.1320 -0.0032 -0.0142 0.0282  203 A1A66 A N4  
6826 O O   A HOH   F .   ? 0.3167 0.5667 0.3283 -0.0754 0.0107  0.1403  301 HOH   A O   
6827 O O   . HOH   F .   ? 0.6186 0.7376 0.5973 -0.1086 -0.1250 -0.1132 302 HOH   A O   
6828 O O   . HOH   F .   ? 0.6593 0.4824 0.3047 0.2394  -0.1092 0.0301  303 HOH   A O   
6829 O O   . HOH   F .   ? 0.3191 0.6818 0.6219 0.0316  0.0853  0.0966  304 HOH   A O   
6830 O O   B HOH   F .   ? 0.2068 0.1862 0.2753 0.0077  0.0090  0.0804  305 HOH   A O   
6831 O O   . HOH   F .   ? 0.4690 0.6030 0.4252 0.2592  0.0392  -0.1078 306 HOH   A O   
6832 O O   . HOH   F .   ? 0.2930 0.3044 0.1791 -0.0369 0.0477  0.0542  307 HOH   A O   
6833 O O   . HOH   F .   ? 0.2931 0.2504 0.5032 -0.0400 -0.1342 0.1407  308 HOH   A O   
6834 O O   . HOH   F .   ? 0.5595 0.4564 0.5467 -0.1326 -0.0803 0.0094  309 HOH   A O   
6835 O O   A HOH   F .   ? 0.2111 0.1684 0.3706 -0.0144 -0.0754 0.0316  310 HOH   A O   
6836 O O   . HOH   F .   ? 0.5626 0.4715 0.5646 -0.0840 0.1860  0.2182  311 HOH   A O   
6837 O O   . HOH   F .   ? 0.2327 0.2858 0.3164 -0.0229 0.0822  -0.0221 312 HOH   A O   
6838 O O   . HOH   F .   ? 0.2734 0.2115 0.2467 -0.0428 0.0211  -0.0153 313 HOH   A O   
6839 O O   . HOH   F .   ? 0.3322 0.3326 0.3006 -0.1303 -0.0121 0.1085  314 HOH   A O   
6840 O O   . HOH   F .   ? 0.4408 0.3521 0.4336 0.0223  0.1641  0.0509  315 HOH   A O   
6841 O O   . HOH   F .   ? 0.5415 0.4307 0.5669 -0.0338 0.1578  0.1839  316 HOH   A O   
6842 O O   . HOH   F .   ? 0.7699 0.5169 0.6108 -0.1001 -0.1309 0.2035  317 HOH   A O   
6843 O O   . HOH   F .   ? 0.5949 0.5416 0.8161 -0.1391 -0.0242 0.1702  318 HOH   A O   
6844 O O   . HOH   F .   ? 0.2042 0.1632 0.3649 -0.0455 0.0129  -0.0075 319 HOH   A O   
6845 O O   . HOH   F .   ? 0.6434 0.5824 0.3534 -0.1153 -0.0846 0.1088  320 HOH   A O   
6846 O O   . HOH   F .   ? 0.2724 0.6769 0.3605 -0.0196 -0.0521 0.0647  321 HOH   A O   
6847 O O   . HOH   F .   ? 0.2418 0.1907 0.4541 0.0106  -0.0864 -0.0255 322 HOH   A O   
6848 O O   B HOH   F .   ? 0.1189 0.1364 0.1693 -0.0004 -0.0102 0.0318  323 HOH   A O   
6849 O O   A HOH   F .   ? 0.1530 0.1768 0.2125 -0.0345 0.0450  0.0554  324 HOH   A O   
6850 O O   . HOH   F .   ? 0.1822 0.3115 0.2758 0.0422  -0.0244 -0.0207 325 HOH   A O   
6851 O O   . HOH   F .   ? 0.7065 0.6850 0.6463 -0.1326 0.1824  -0.0654 326 HOH   A O   
6852 O O   . HOH   F .   ? 0.6118 0.5616 0.5604 0.0363  0.3088  -0.1039 327 HOH   A O   
6853 O O   . HOH   F .   ? 0.2053 0.2583 0.2285 -0.0668 -0.0340 0.1089  328 HOH   A O   
6854 O O   . HOH   F .   ? 0.2913 0.4330 0.4887 -0.1273 0.1735  -0.0792 329 HOH   A O   
6855 O O   . HOH   F .   ? 0.4320 0.2746 0.2929 -0.1194 0.0495  0.0380  330 HOH   A O   
6856 O O   . HOH   F .   ? 0.3448 0.5892 0.6413 -0.0794 -0.1092 0.2204  331 HOH   A O   
6857 O O   . HOH   F .   ? 0.2315 0.4096 0.3631 0.1002  -0.0721 -0.0301 332 HOH   A O   
6858 O O   . HOH   F .   ? 0.2390 0.2080 0.2672 0.0518  0.0320  0.0496  333 HOH   A O   
6859 O O   . HOH   F .   ? 0.6463 0.7453 0.4105 0.2252  -0.0458 -0.0683 334 HOH   A O   
6860 O O   . HOH   F .   ? 0.1590 0.4377 0.2698 -0.0195 0.0184  0.0691  335 HOH   A O   
6861 O O   . HOH   F .   ? 0.3147 0.3699 0.3844 -0.1217 -0.0895 -0.0144 336 HOH   A O   
6862 O O   . HOH   F .   ? 0.1510 0.1472 0.2191 -0.0287 0.0058  0.0119  337 HOH   A O   
6863 O O   . HOH   F .   ? 0.5598 0.4528 0.4726 -0.1585 -0.0608 0.2431  338 HOH   A O   
6864 O O   . HOH   F .   ? 0.2001 0.4142 0.3731 -0.0388 -0.0611 0.1776  339 HOH   A O   
6865 O O   A HOH   F .   ? 0.2932 0.3244 0.2202 -0.1055 0.0325  0.0426  340 HOH   A O   
6866 O O   . HOH   F .   ? 0.1970 0.3122 0.4354 -0.0392 0.0421  -0.0844 341 HOH   A O   
6867 O O   . HOH   F .   ? 0.5527 0.1710 0.3729 0.0068  -0.1393 0.0429  342 HOH   A O   
6868 O O   . HOH   F .   ? 0.3264 0.3239 0.4586 -0.0482 -0.1200 -0.0757 343 HOH   A O   
6869 O O   A HOH   F .   ? 0.1958 0.3592 0.2484 0.0628  -0.0308 -0.0194 344 HOH   A O   
6870 O O   . HOH   F .   ? 0.5409 0.1963 0.5666 0.0957  -0.0910 -0.0133 345 HOH   A O   
6871 O O   . HOH   F .   ? 0.1375 0.2028 0.2004 -0.0012 -0.0139 0.0464  346 HOH   A O   
6872 O O   . HOH   F .   ? 0.3266 0.4259 0.2185 -0.0101 0.0696  0.0404  347 HOH   A O   
6873 O O   . HOH   F .   ? 0.1751 0.2342 0.3762 0.0173  0.0730  -0.0528 348 HOH   A O   
6874 O O   B HOH   F .   ? 0.2227 0.2085 0.2434 -0.0415 -0.0004 0.0523  349 HOH   A O   
6875 O O   B HOH   F .   ? 0.2217 0.2931 0.4218 0.0340  0.0585  0.0104  350 HOH   A O   
6876 O O   . HOH   F .   ? 0.3677 0.4520 0.4256 0.2111  0.0980  0.0980  351 HOH   A O   
6877 O O   . HOH   F .   ? 0.3631 0.3099 0.3420 -0.0831 -0.0183 -0.0054 352 HOH   A O   
6878 O O   . HOH   F .   ? 0.1949 0.1584 0.2284 0.0277  -0.0290 0.0045  353 HOH   A O   
6879 O O   . HOH   F .   ? 0.6028 0.3407 0.3324 0.0986  0.0898  0.1180  354 HOH   A O   
6880 O O   . HOH   F .   ? 0.3294 0.5284 0.3348 0.0546  -0.0402 0.0875  355 HOH   A O   
6881 O O   A HOH   F .   ? 0.2755 0.2656 0.3048 -0.0287 0.0920  0.1195  356 HOH   A O   
6882 O O   . HOH   F .   ? 0.1980 0.1816 0.4249 0.0152  0.1171  -0.0129 357 HOH   A O   
6883 O O   . HOH   F .   ? 0.3092 0.3410 0.6245 0.0928  0.1303  -0.0099 358 HOH   A O   
6884 O O   . HOH   F .   ? 0.1579 0.1791 0.2746 -0.0002 -0.0208 -0.0248 359 HOH   A O   
6885 O O   . HOH   F .   ? 0.1656 0.1623 0.2187 -0.0224 0.0063  0.0384  360 HOH   A O   
6886 O O   . HOH   F .   ? 0.1374 0.1839 0.2439 0.0087  -0.0014 0.0017  361 HOH   A O   
6887 O O   . HOH   F .   ? 0.1323 0.1442 0.1471 -0.0065 -0.0169 -0.0034 362 HOH   A O   
6888 O O   . HOH   F .   ? 0.3280 0.3866 0.2002 -0.1067 -0.0309 -0.0751 363 HOH   A O   
6889 O O   . HOH   F .   ? 0.1286 0.1239 0.1610 -0.0016 0.0092  0.0158  364 HOH   A O   
6890 O O   . HOH   F .   ? 1.1213 1.0399 0.8327 -0.0710 -0.1092 -0.0237 365 HOH   A O   
6891 O O   . HOH   F .   ? 0.1981 0.1562 0.1637 -0.0078 0.0193  0.0225  366 HOH   A O   
6892 O O   . HOH   F .   ? 0.1510 0.1238 0.2167 -0.0057 0.0141  -0.0066 367 HOH   A O   
6893 O O   . HOH   F .   ? 0.2661 0.4468 0.3437 -0.0768 0.0501  -0.0096 368 HOH   A O   
6894 O O   A HOH   F .   ? 0.1666 0.3354 0.1841 0.0993  0.0228  0.0269  369 HOH   A O   
6895 O O   . HOH   F .   ? 0.4008 0.2259 0.4506 -0.1180 0.1011  0.0248  370 HOH   A O   
6896 O O   B HOH   F .   ? 0.2551 0.1900 0.2378 -0.0647 0.0213  0.0473  371 HOH   A O   
6897 O O   A HOH   F .   ? 0.3263 0.1396 0.2570 0.0241  0.0235  -0.0090 372 HOH   A O   
6898 O O   . HOH   F .   ? 0.1603 0.1546 0.2125 0.0094  -0.0249 0.0219  373 HOH   A O   
6899 O O   . HOH   F .   ? 0.1739 0.1861 0.2313 -0.0322 0.0080  0.0278  374 HOH   A O   
6900 O O   . HOH   F .   ? 0.3898 0.2193 0.3567 -0.1177 0.1562  -0.0350 375 HOH   A O   
6901 O O   . HOH   F .   ? 0.3878 0.4484 0.6189 0.1491  0.0871  -0.1497 376 HOH   A O   
6902 O O   . HOH   F .   ? 0.4091 0.7862 0.6271 -0.0909 -0.1477 -0.0465 377 HOH   A O   
6903 O O   . HOH   F .   ? 0.1791 0.2097 0.2184 -0.0190 -0.0428 0.0479  378 HOH   A O   
6904 O O   . HOH   F .   ? 0.3427 0.2340 0.5078 -0.0733 -0.0317 -0.0000 379 HOH   A O   
6905 O O   T HOH   F .   ? 0.1084 0.1110 0.2118 -0.0392 -0.0184 0.0510  380 HOH   A O   
6906 O O   . HOH   F .   ? 0.1859 0.2261 0.3041 0.0200  -0.0586 -0.0280 381 HOH   A O   
6907 O O   . HOH   F .   ? 0.2007 0.2037 0.1801 -0.0231 0.0156  0.0134  382 HOH   A O   
6908 O O   . HOH   F .   ? 0.3381 0.6828 0.3621 -0.0648 -0.0058 0.1337  383 HOH   A O   
6909 O O   . HOH   F .   ? 0.2792 0.5068 0.3327 0.0878  0.0947  0.2169  384 HOH   A O   
6910 O O   . HOH   F .   ? 0.3287 0.6703 0.3031 0.1335  0.0727  -0.0483 385 HOH   A O   
6911 O O   . HOH   F .   ? 0.3072 0.2633 0.3379 -0.0074 -0.0339 0.1105  386 HOH   A O   
6912 O O   . HOH   F .   ? 0.1438 0.1633 0.1734 0.0180  -0.0246 -0.0226 387 HOH   A O   
6913 O O   . HOH   F .   ? 0.3123 0.2711 0.2136 0.0359  0.0700  0.0289  388 HOH   A O   
6914 O O   . HOH   F .   ? 0.2296 0.1832 0.1726 -0.0524 0.0119  0.0384  389 HOH   A O   
6915 O O   . HOH   F .   ? 0.2906 0.2467 0.2437 -0.0682 -0.1056 0.0418  390 HOH   A O   
6916 O O   . HOH   F .   ? 0.1265 0.1317 0.1771 -0.0064 -0.0160 0.0081  391 HOH   A O   
6917 O O   . HOH   F .   ? 0.3032 0.3499 0.3747 -0.1314 0.1242  -0.0037 392 HOH   A O   
6918 O O   B HOH   F .   ? 0.4413 0.6284 0.4287 0.0624  -0.0327 -0.0044 393 HOH   A O   
6919 O O   . HOH   F .   ? 0.2042 0.1569 0.3195 0.0044  -0.0370 -0.0001 394 HOH   A O   
6920 O O   . HOH   F .   ? 0.5383 0.3048 0.5211 0.1055  -0.1094 0.0064  395 HOH   A O   
6921 O O   . HOH   F .   ? 0.2553 0.1843 0.2488 -0.0093 0.0060  0.0309  396 HOH   A O   
6922 O O   . HOH   F .   ? 0.4861 0.7336 0.4429 0.2276  -0.0717 -0.0319 397 HOH   A O   
6923 O O   . HOH   F .   ? 0.1903 0.2061 0.2743 -0.0111 -0.0228 0.0880  398 HOH   A O   
6924 O O   . HOH   F .   ? 0.3609 0.3038 0.2390 -0.0557 -0.0260 0.0298  399 HOH   A O   
6925 O O   A HOH   F .   ? 0.2156 0.2052 0.2699 0.0241  -0.0380 0.0685  400 HOH   A O   
6926 O O   . HOH   F .   ? 0.2239 0.3878 0.3290 -0.0409 0.0808  -0.0713 401 HOH   A O   
6927 O O   A HOH   F .   ? 0.1775 0.1605 0.2418 0.0083  -0.0664 0.0200  402 HOH   A O   
6928 O O   . HOH   F .   ? 0.4849 0.5790 0.4310 0.1442  -0.1160 -0.1611 403 HOH   A O   
6929 O O   . HOH   F .   ? 0.1739 0.1786 0.4051 0.0389  0.1122  0.1085  404 HOH   A O   
6930 O O   A HOH   F .   ? 0.2197 0.3499 0.3082 -0.0608 0.0122  0.0198  405 HOH   A O   
6931 O O   . HOH   F .   ? 0.2437 0.2029 0.2494 -0.0536 0.0028  0.0565  406 HOH   A O   
6932 O O   . HOH   F .   ? 0.4876 0.6571 0.2626 -0.1412 -0.0835 -0.0287 407 HOH   A O   
6933 O O   . HOH   F .   ? 0.2465 0.3702 0.7695 -0.0539 0.0790  -0.0437 408 HOH   A O   
6934 O O   . HOH   F .   ? 0.1625 0.2548 0.4224 0.0024  -0.0104 0.0552  409 HOH   A O   
6935 O O   . HOH   F .   ? 0.7611 0.7098 0.6409 0.1079  0.1844  0.0476  410 HOH   A O   
6936 O O   . HOH   F .   ? 0.6144 0.4621 0.4259 -0.0538 -0.1533 0.0033  411 HOH   A O   
6937 O O   . HOH   F .   ? 0.4967 0.5945 0.1996 -0.0770 -0.0036 -0.0285 412 HOH   A O   
6938 O O   . HOH   F .   ? 0.2950 0.3674 0.5172 -0.0226 0.1129  -0.0199 413 HOH   A O   
6939 O O   A HOH   F .   ? 0.2248 0.1426 0.2131 0.0200  0.0470  0.0801  414 HOH   A O   
6940 O O   . HOH   F .   ? 0.2131 0.2716 0.5388 -0.0011 -0.0937 -0.0242 415 HOH   A O   
6941 O O   . HOH   F .   ? 0.3442 0.1256 0.1884 -0.0084 -0.0613 0.0114  416 HOH   A O   
6942 O O   . HOH   F .   ? 0.1841 0.1755 0.2508 0.0235  -0.0486 0.0150  417 HOH   A O   
6943 O O   . HOH   F .   ? 0.1607 0.1292 0.1636 -0.0235 0.0201  0.0047  418 HOH   A O   
6944 O O   . HOH   F .   ? 0.6170 0.4561 0.5449 0.0180  -0.0983 -0.0373 419 HOH   A O   
6945 O O   . HOH   F .   ? 0.6215 0.6688 0.6572 0.0067  -0.0880 -0.0307 420 HOH   A O   
6946 O O   . HOH   F .   ? 0.1960 0.2703 0.2507 -0.0010 -0.0521 0.0588  421 HOH   A O   
6947 O O   . HOH   F .   ? 0.3968 0.6262 0.6280 0.0582  -0.0841 0.1991  422 HOH   A O   
6948 O O   . HOH   F .   ? 0.4591 0.3196 0.3074 -0.0038 -0.0915 -0.0343 423 HOH   A O   
6949 O O   . HOH   F .   ? 0.2687 0.6071 0.1855 -0.0348 0.0596  0.0001  424 HOH   A O   
6950 O O   . HOH   F .   ? 0.1502 0.1591 0.3113 -0.0050 0.0045  0.0222  425 HOH   A O   
6951 O O   A HOH   F .   ? 0.1182 0.2162 0.2691 0.0042  0.0626  0.0890  426 HOH   A O   
6952 O O   . HOH   F .   ? 0.1678 0.2158 0.2826 -0.0275 -0.0137 0.0501  427 HOH   A O   
6953 O O   . HOH   F .   ? 0.2251 0.4022 0.2800 0.1524  0.0094  0.0298  428 HOH   A O   
6954 O O   . HOH   F .   ? 0.4010 0.2248 0.5746 -0.0707 -0.2327 0.1097  429 HOH   A O   
6955 O O   A HOH   F .   ? 0.4596 0.3368 0.2704 -0.1474 -0.0248 0.0799  430 HOH   A O   
6956 O O   . HOH   F .   ? 0.4399 0.6839 0.3283 -0.1052 -0.0306 0.1150  431 HOH   A O   
6957 O O   . HOH   F .   ? 0.4984 0.6311 0.6106 0.2805  0.1840  0.0386  432 HOH   A O   
6958 O O   . HOH   F .   ? 0.6802 0.3930 0.4177 0.1776  -0.0970 0.0978  433 HOH   A O   
6959 O O   A HOH   F .   ? 0.5678 0.4582 0.3613 -0.0886 0.0057  0.1154  434 HOH   A O   
6960 O O   . HOH   F .   ? 0.2242 0.1549 0.2948 0.0134  0.0076  0.0177  435 HOH   A O   
6961 O O   A HOH   F .   ? 0.1326 0.1559 0.1205 0.0114  -0.0128 -0.0228 436 HOH   A O   
6962 O O   . HOH   F .   ? 0.1885 0.1994 0.4594 -0.0217 -0.0870 0.0614  437 HOH   A O   
6963 O O   A HOH   F .   ? 0.4205 0.5604 0.3081 0.0622  -0.1046 0.1400  438 HOH   A O   
6964 O O   . HOH   F .   ? 0.6529 0.7343 0.4623 0.1141  0.2856  -0.0322 439 HOH   A O   
6965 O O   . HOH   F .   ? 0.6417 0.7129 0.4913 -0.1101 0.1266  0.1352  440 HOH   A O   
6966 O O   B HOH   F .   ? 0.4363 0.2293 0.3231 0.0362  -0.1013 0.0342  441 HOH   A O   
6967 O O   . HOH   F .   ? 0.3387 0.2548 0.1659 -0.0767 0.0216  0.0469  442 HOH   A O   
6968 O O   . HOH   F .   ? 0.4377 0.4024 0.2776 0.2463  -0.0591 -0.0338 443 HOH   A O   
6969 O O   B HOH   F .   ? 0.3312 0.1917 0.4242 -0.0869 -0.0342 0.0595  444 HOH   A O   
6970 O O   . HOH   F .   ? 0.6261 0.7786 0.5659 0.0567  0.0838  -0.1252 445 HOH   A O   
6971 O O   . HOH   F .   ? 0.5881 0.5976 0.7916 0.0828  -0.1156 0.1532  446 HOH   A O   
6972 O O   . HOH   F .   ? 0.4006 0.4963 0.5047 -0.0392 -0.0929 -0.1356 447 HOH   A O   
6973 O O   . HOH   F .   ? 0.2188 0.2048 0.2539 0.0022  0.0147  0.0366  448 HOH   A O   
6974 O O   . HOH   F .   ? 0.7654 0.6799 0.7642 0.0392  -0.0255 0.0024  449 HOH   A O   
6975 O O   . HOH   F .   ? 0.2032 0.2685 0.2584 -0.0082 -0.0113 -0.0531 450 HOH   A O   
6976 O O   . HOH   F .   ? 0.7416 0.7476 0.7043 -0.1391 0.0503  -0.1289 451 HOH   A O   
6977 O O   A HOH   F .   ? 0.3942 0.1924 0.2899 -0.0839 0.0127  -0.0052 452 HOH   A O   
6978 O O   . HOH   F .   ? 0.5275 0.4619 0.5854 0.0281  0.1249  0.2128  453 HOH   A O   
6979 O O   A HOH   F .   ? 0.5375 0.3624 0.3119 -0.0071 0.0754  0.0530  454 HOH   A O   
6980 O O   . HOH   F .   ? 0.2622 0.4102 0.6231 0.0066  0.0962  -0.2003 455 HOH   A O   
6981 O O   . HOH   F .   ? 0.4843 0.3542 0.4131 0.1548  0.1979  0.1086  456 HOH   A O   
6982 O O   B HOH   F .   ? 0.2148 0.1329 0.2513 -0.0654 0.1106  -0.0446 457 HOH   A O   
6983 O O   . HOH   F .   ? 0.4029 0.3740 0.3777 0.1991  -0.0753 -0.0105 458 HOH   A O   
6984 O O   . HOH   F .   ? 0.2871 0.2932 0.4041 -0.0563 0.0327  -0.1051 459 HOH   A O   
6985 O O   . HOH   F .   ? 0.8083 0.8581 0.5105 -0.0516 -0.1131 -0.0165 460 HOH   A O   
6986 O O   . HOH   F .   ? 0.4177 0.3475 0.3612 0.0231  0.0774  0.0133  461 HOH   A O   
6987 O O   . HOH   F .   ? 0.4350 0.6522 0.4821 -0.0226 0.0070  0.1498  462 HOH   A O   
6988 O O   B HOH   F .   ? 0.1554 0.1421 0.3082 -0.0224 -0.0353 0.0632  463 HOH   A O   
6989 O O   . HOH   F .   ? 0.4326 0.3415 0.7600 0.0196  -0.0451 -0.0547 464 HOH   A O   
6990 O O   . HOH   F .   ? 0.3165 0.5285 0.5213 0.0681  -0.0955 0.1940  465 HOH   A O   
6991 O O   . HOH   F .   ? 0.3293 0.5124 0.5061 -0.1795 0.0779  -0.1336 466 HOH   A O   
6992 O O   . HOH   F .   ? 0.8198 0.7062 0.6571 0.1520  0.2265  0.2604  467 HOH   A O   
6993 O O   . HOH   F .   ? 0.2523 0.4443 0.4402 0.0611  -0.0152 -0.1883 468 HOH   A O   
6994 O O   . HOH   F .   ? 0.3755 0.6710 0.4733 -0.0507 -0.0777 0.2844  469 HOH   A O   
6995 O O   . HOH   F .   ? 0.2612 0.1699 0.2424 0.0348  -0.0888 -0.0363 470 HOH   A O   
6996 O O   . HOH   F .   ? 0.5244 0.3243 0.7214 0.1133  0.1143  0.2107  471 HOH   A O   
6997 O O   . HOH   F .   ? 0.2793 0.2621 0.3264 -0.1019 0.0286  -0.0067 472 HOH   A O   
6998 O O   . HOH   F .   ? 0.3405 0.5177 0.4033 -0.1181 0.0333  -0.0174 473 HOH   A O   
6999 O O   . HOH   F .   ? 0.5205 0.4345 0.5366 -0.0049 0.1326  0.0101  474 HOH   A O   
7000 O O   . HOH   F .   ? 0.5256 0.6326 0.4478 0.1188  -0.0446 -0.0288 475 HOH   A O   
7001 O O   . HOH   F .   ? 0.4445 0.5218 0.3921 0.0464  -0.0986 -0.1080 476 HOH   A O   
7002 O O   . HOH   F .   ? 0.3050 0.3083 0.3252 0.0326  0.0703  0.0234  477 HOH   A O   
7003 O O   . HOH   F .   ? 0.4936 0.6506 0.6565 -0.1542 -0.1296 -0.0456 478 HOH   A O   
7004 O O   . HOH   F .   ? 0.7164 0.4043 0.4844 0.0047  0.0675  0.0628  479 HOH   A O   
7005 O O   B HOH   F .   ? 0.3635 0.4516 0.3258 0.1264  -0.1657 -0.0235 480 HOH   A O   
7006 O O   . HOH   F .   ? 0.5535 0.5028 0.3304 -0.0605 -0.0625 0.0015  481 HOH   A O   
7007 O O   . HOH   F .   ? 0.4554 0.5132 0.2819 -0.0333 -0.0183 0.0371  482 HOH   A O   
7008 O O   . HOH   F .   ? 0.6388 0.5604 0.7616 -0.1180 0.0821  -0.0733 483 HOH   A O   
7009 O O   . HOH   F .   ? 0.4485 0.3967 0.5777 -0.1647 -0.0500 -0.0407 484 HOH   A O   
7010 O O   . HOH   F .   ? 0.4952 0.2749 0.3446 -0.0472 -0.1354 0.0804  485 HOH   A O   
7011 O O   . HOH   F .   ? 0.5270 0.3713 0.4429 0.0071  -0.0255 -0.0949 486 HOH   A O   
7012 O O   . HOH   F .   ? 0.4828 0.4158 0.4928 0.0104  0.2375  0.1288  487 HOH   A O   
7013 O O   . HOH   F .   ? 0.8350 0.3653 0.3366 -0.0166 -0.1378 0.0069  488 HOH   A O   
7014 O O   . HOH   F .   ? 0.2557 0.5513 0.4525 0.1022  0.1059  0.2726  489 HOH   A O   
7015 O O   . HOH   F .   ? 0.2481 0.2222 0.7449 0.0061  -0.1521 0.0079  490 HOH   A O   
7016 O O   . HOH   F .   ? 0.2682 0.2554 0.2515 0.0515  -0.0028 0.0075  491 HOH   A O   
7017 O O   . HOH   F .   ? 0.5987 0.5679 0.7657 0.0724  0.2257  -0.1172 492 HOH   A O   
7018 O O   . HOH   F .   ? 0.4162 0.3328 0.2537 -0.0869 0.1380  -0.0465 493 HOH   A O   
7019 O O   . HOH   F .   ? 0.7455 0.6844 0.4771 -0.1036 0.1858  0.1401  494 HOH   A O   
7020 O O   . HOH   F .   ? 0.5367 0.6163 0.5177 -0.0289 -0.0809 0.0122  495 HOH   A O   
7021 O O   . HOH   F .   ? 0.5084 0.3660 0.4716 -0.0836 0.1075  0.1441  496 HOH   A O   
7022 O O   . HOH   F .   ? 0.2677 0.2571 0.5464 0.0029  0.0857  -0.0499 497 HOH   A O   
7023 O O   . HOH   F .   ? 0.3996 0.3110 0.5036 0.0004  0.2397  0.0581  498 HOH   A O   
7024 O O   . HOH   F .   ? 0.6084 0.5355 0.5946 -0.1266 -0.0910 -0.0781 499 HOH   A O   
7025 O O   . HOH   F .   ? 0.6803 0.2491 0.3664 -0.0666 0.0833  0.0293  500 HOH   A O   
7026 O O   . HOH   F .   ? 0.2809 0.1934 0.6405 0.0094  0.0787  0.0711  501 HOH   A O   
7027 O O   . HOH   F .   ? 0.5727 0.4630 0.4396 0.0162  -0.0860 -0.0320 502 HOH   A O   
7028 O O   . HOH   F .   ? 0.4732 0.2333 0.4561 -0.1328 0.0225  0.0023  503 HOH   A O   
7029 O O   B HOH   F .   ? 0.1809 0.2923 0.2493 0.0549  0.0444  0.0521  504 HOH   A O   
7030 O O   . HOH   F .   ? 0.3125 0.4975 0.3171 -0.0209 -0.0560 -0.0442 505 HOH   A O   
7031 O O   . HOH   F .   ? 0.4333 0.9609 0.6080 -0.1022 -0.0659 0.2079  506 HOH   A O   
7032 O O   . HOH   F .   ? 0.2400 0.3540 0.3170 0.0717  -0.0429 0.0774  507 HOH   A O   
7033 O O   . HOH   F .   ? 0.2635 0.4490 0.5393 0.0213  -0.1052 -0.0003 508 HOH   A O   
7034 O O   . HOH   F .   ? 0.5385 0.2280 0.4082 0.0908  -0.1314 -0.0084 509 HOH   A O   
7035 O O   . HOH   F .   ? 0.6538 0.7373 0.5066 0.1594  -0.0215 0.0472  510 HOH   A O   
7036 O O   B HOH   F .   ? 0.4874 0.2888 0.2564 -0.0848 0.0283  -0.0436 511 HOH   A O   
7037 O O   . HOH   F .   ? 0.6231 0.7152 0.5763 0.1529  -0.1489 0.0253  512 HOH   A O   
7038 O O   B HOH   F .   ? 0.4287 0.3269 0.3828 0.1281  0.0768  0.1285  513 HOH   A O   
7039 O O   B HOH   F .   ? 0.5049 0.2164 0.3772 -0.0219 0.1744  -0.0224 514 HOH   A O   
7040 O O   . HOH   F .   ? 0.4966 0.6824 0.4938 0.3106  -0.0253 0.1166  515 HOH   A O   
7041 O O   . HOH   F .   ? 0.2856 0.2130 0.5007 0.0014  0.0407  0.0641  516 HOH   A O   
7042 O O   T HOH   F .   ? 0.1166 0.1827 0.1691 -0.0417 -0.0196 0.0975  517 HOH   A O   
7043 O O   . HOH   F .   ? 0.6441 0.7590 0.4825 -0.1199 -0.1051 -0.1414 518 HOH   A O   
7044 O O   A HOH   F .   ? 0.3927 0.6875 0.3319 0.1800  -0.0858 0.0017  519 HOH   A O   
7045 O O   . HOH   F .   ? 0.3120 0.7703 0.4503 0.1071  0.0328  -0.0889 520 HOH   A O   
7046 O O   . HOH   F .   ? 0.5684 0.4058 0.6095 0.0676  0.1318  0.0300  521 HOH   A O   
7047 O O   . HOH   F .   ? 0.5342 0.6905 0.5209 -0.0026 -0.0466 0.0847  522 HOH   A O   
7048 O O   B HOH   F .   ? 0.3267 0.4429 0.4307 0.1031  -0.0395 0.0335  523 HOH   A O   
7049 O O   . HOH   F .   ? 0.3152 0.5080 0.5445 -0.0771 -0.0873 0.2944  524 HOH   A O   
7050 O O   . HOH   G .   ? 0.2395 0.2184 0.3228 0.0244  0.1067  0.0282  201 HOH   B O   
7051 O O   . HOH   G .   ? 0.4753 0.3738 0.4404 -0.0178 -0.0284 -0.1855 202 HOH   B O   
7052 O O   . HOH   G .   ? 0.3114 0.3090 0.6244 -0.0398 0.0215  0.0343  203 HOH   B O   
7053 O O   . HOH   G .   ? 0.3754 0.4462 0.5735 -0.1179 -0.0125 -0.1458 204 HOH   B O   
7054 O O   . HOH   G .   ? 0.6672 0.6261 0.5817 0.2727  0.0539  0.0282  205 HOH   B O   
7055 O O   . HOH   G .   ? 0.3078 0.6925 0.3697 0.0417  0.0173  0.2695  206 HOH   B O   
7056 O O   . HOH   G .   ? 0.3078 0.2001 0.5208 0.0246  0.1946  0.0872  207 HOH   B O   
7057 O O   . HOH   G .   ? 0.6423 0.3334 0.4335 0.0694  0.1222  0.0229  208 HOH   B O   
7058 O O   . HOH   G .   ? 0.1927 0.2169 0.2920 -0.0029 0.0325  -0.0385 209 HOH   B O   
7059 O O   . HOH   G .   ? 0.3574 0.5518 0.5340 0.2447  0.0369  -0.0513 210 HOH   B O   
7060 O O   . HOH   G .   ? 0.2898 0.6345 0.5320 0.0377  0.1559  -0.1509 211 HOH   B O   
7061 O O   . HOH   G .   ? 0.1567 0.1922 0.2634 -0.0270 -0.0121 0.0017  212 HOH   B O   
7062 O O   . HOH   G .   ? 0.3491 0.2767 0.4059 0.0397  -0.0321 -0.0091 213 HOH   B O   
7063 O O   . HOH   G .   ? 0.5692 0.3718 0.6090 0.0660  -0.0864 0.2420  214 HOH   B O   
7064 O O   . HOH   G .   ? 0.3294 0.2154 0.4999 -0.0095 0.2035  0.0077  215 HOH   B O   
7065 O O   . HOH   G .   ? 0.4830 0.6000 0.3780 0.3011  -0.0847 -0.0171 216 HOH   B O   
7066 O O   . HOH   G .   ? 0.4985 0.4281 0.3946 0.0777  0.0701  -0.1785 217 HOH   B O   
7067 O O   . HOH   G .   ? 0.3619 0.4702 0.3654 0.1622  -0.0287 -0.0087 218 HOH   B O   
7068 O O   . HOH   G .   ? 0.3959 0.4108 0.3078 -0.0034 -0.1147 0.0677  219 HOH   B O   
7069 O O   . HOH   G .   ? 0.3554 0.2545 0.4374 0.0740  -0.0079 -0.0406 220 HOH   B O   
7070 O O   . HOH   G .   ? 0.4869 0.6483 0.3881 0.2739  0.0420  0.0733  221 HOH   B O   
7071 O O   . HOH   G .   ? 0.3137 0.2645 0.6050 0.0817  -0.0988 0.0596  222 HOH   B O   
7072 O O   . HOH   G .   ? 0.4715 0.5028 0.2443 -0.0003 -0.0993 -0.1377 223 HOH   B O   
7073 O O   . HOH   G .   ? 0.7254 0.4113 0.2843 -0.0630 0.0804  0.0591  224 HOH   B O   
7074 O O   . HOH   G .   ? 0.1691 0.2001 0.3032 -0.0249 0.0211  -0.0249 225 HOH   B O   
7075 O O   . HOH   G .   ? 0.2352 0.1610 0.2617 -0.0290 0.0985  -0.0083 226 HOH   B O   
7076 O O   . HOH   G .   ? 0.2134 0.2111 0.3826 -0.0370 0.0064  -0.0598 227 HOH   B O   
7077 O O   . HOH   G .   ? 0.3793 0.3728 0.5158 -0.1498 0.0040  0.0706  228 HOH   B O   
7078 O O   . HOH   G .   ? 0.3905 0.1710 0.1835 0.0318  -0.0987 -0.0158 229 HOH   B O   
7079 O O   . HOH   G .   ? 0.2046 0.1252 0.3192 0.0066  -0.0568 -0.0076 230 HOH   B O   
7080 O O   . HOH   G .   ? 0.4819 0.2012 0.2953 0.0087  -0.0894 -0.0001 231 HOH   B O   
7081 O O   . HOH   G .   ? 0.2376 0.1987 0.2300 0.0824  -0.0813 -0.0605 232 HOH   B O   
7082 O O   . HOH   G .   ? 0.2640 0.2459 0.2788 0.0302  0.0300  -0.0666 233 HOH   B O   
7083 O O   . HOH   G .   ? 0.2208 0.3743 0.3270 -0.0573 -0.0739 -0.0573 234 HOH   B O   
7084 O O   . HOH   G .   ? 0.3387 0.2936 0.1959 0.0202  0.0549  0.0203  235 HOH   B O   
7085 O O   . HOH   G .   ? 0.3201 0.4601 0.7040 0.0431  0.1411  0.0018  236 HOH   B O   
7086 O O   . HOH   G .   ? 0.2667 0.3443 0.2777 -0.0863 0.0456  -0.0664 237 HOH   B O   
7087 O O   . HOH   G .   ? 0.3358 0.2516 0.4292 0.0466  -0.1015 -0.1378 238 HOH   B O   
7088 O O   . HOH   G .   ? 0.4691 0.3154 0.2952 -0.1206 0.0762  -0.0552 239 HOH   B O   
7089 O O   . HOH   G .   ? 0.6831 0.4262 0.4660 0.1476  -0.0026 -0.1027 240 HOH   B O   
7090 O O   . HOH   G .   ? 0.2107 0.3724 0.2214 -0.0457 -0.0183 0.0698  241 HOH   B O   
7091 O O   . HOH   G .   ? 0.5250 0.2735 0.4240 -0.1700 -0.0475 0.0635  242 HOH   B O   
7092 O O   . HOH   G .   ? 0.1514 0.1428 0.2528 -0.0056 0.0092  -0.0044 243 HOH   B O   
7093 O O   . HOH   G .   ? 0.2870 0.1684 0.6231 -0.0070 -0.1021 -0.0304 244 HOH   B O   
7094 O O   . HOH   G .   ? 0.2365 0.5472 0.5432 0.1517  -0.0393 -0.1064 245 HOH   B O   
7095 O O   . HOH   G .   ? 0.1991 0.1895 0.4465 0.0060  -0.0619 -0.0413 246 HOH   B O   
7096 O O   . HOH   G .   ? 0.1438 0.1377 0.1408 -0.0100 -0.0094 -0.0011 247 HOH   B O   
7097 O O   . HOH   G .   ? 0.2147 0.1793 0.2068 -0.0341 -0.0466 0.0194  248 HOH   B O   
7098 O O   . HOH   G .   ? 0.4571 0.4546 0.6882 0.1347  -0.1528 -0.0870 249 HOH   B O   
7099 O O   . HOH   G .   ? 0.2878 0.2423 0.2812 0.0915  0.0825  0.0100  250 HOH   B O   
7100 O O   . HOH   G .   ? 0.2383 0.2428 0.3275 -0.0763 0.0207  -0.0390 251 HOH   B O   
7101 O O   . HOH   G .   ? 0.2665 0.2112 0.1806 0.0046  -0.0074 -0.0021 252 HOH   B O   
7102 O O   . HOH   G .   ? 0.1555 0.1658 0.3155 -0.0296 -0.0158 0.0167  253 HOH   B O   
7103 O O   . HOH   G .   ? 0.5200 0.3068 0.3784 -0.2191 0.0221  0.0217  254 HOH   B O   
7104 O O   . HOH   G .   ? 0.6229 0.6315 0.3400 0.0113  0.0382  0.0486  255 HOH   B O   
7105 O O   . HOH   G .   ? 0.4141 0.2046 0.2193 0.1302  0.0522  0.0316  256 HOH   B O   
7106 O O   . HOH   G .   ? 0.1425 0.1237 0.1496 -0.0023 -0.0046 0.0060  257 HOH   B O   
7107 O O   . HOH   G .   ? 0.1783 0.2548 0.2698 0.0391  0.0376  0.0953  258 HOH   B O   
7108 O O   . HOH   G .   ? 0.2730 0.4142 0.2685 -0.0684 -0.0548 -0.0752 259 HOH   B O   
7109 O O   . HOH   G .   ? 0.1965 0.1459 0.2009 -0.0316 -0.0360 0.0303  260 HOH   B O   
7110 O O   . HOH   G .   ? 0.3952 0.2673 0.3946 -0.0189 -0.0922 -0.0411 261 HOH   B O   
7111 O O   . HOH   G .   ? 0.3825 0.3694 0.2146 0.0211  0.1006  0.0140  262 HOH   B O   
7112 O O   . HOH   G .   ? 0.2509 0.4205 0.3561 0.0130  0.1254  -0.0153 263 HOH   B O   
7113 O O   . HOH   G .   ? 0.2156 0.2527 0.2200 0.0663  -0.0209 -0.0126 264 HOH   B O   
7114 O O   . HOH   G .   ? 0.2212 0.2936 0.2027 -0.0518 0.0326  0.0381  265 HOH   B O   
7115 O O   . HOH   G .   ? 0.3296 0.4498 0.3175 -0.0352 -0.1159 0.0689  266 HOH   B O   
7116 O O   . HOH   G .   ? 0.2017 0.1440 0.2061 -0.0290 -0.0118 0.0159  267 HOH   B O   
7117 O O   . HOH   G .   ? 0.1273 0.1546 0.2129 -0.0048 0.0039  0.0147  268 HOH   B O   
7118 O O   . HOH   G .   ? 0.2296 0.2079 0.1695 0.0238  0.0018  -0.0011 269 HOH   B O   
7119 O O   . HOH   G .   ? 0.2448 0.1968 0.2685 -0.0661 0.0038  -0.0021 270 HOH   B O   
7120 O O   . HOH   G .   ? 0.2211 0.2626 0.2041 -0.0344 -0.0622 -0.0536 271 HOH   B O   
7121 O O   . HOH   G .   ? 0.4041 0.3595 0.4723 0.1628  -0.0728 -0.0916 272 HOH   B O   
7122 O O   . HOH   G .   ? 0.2383 0.2615 0.2190 -0.0290 -0.0723 0.0181  273 HOH   B O   
7123 O O   . HOH   G .   ? 0.3265 0.2492 0.2957 -0.0547 0.0294  -0.0582 274 HOH   B O   
7124 O O   . HOH   G .   ? 0.4694 0.3689 0.3035 0.0023  0.0029  -0.1117 275 HOH   B O   
7125 O O   . HOH   G .   ? 0.2473 0.4063 0.5923 0.0376  0.0310  -0.0894 276 HOH   B O   
7126 O O   . HOH   G .   ? 0.1724 0.1362 0.4977 -0.0057 -0.0417 -0.0194 277 HOH   B O   
7127 O O   . HOH   G .   ? 0.2269 0.5033 0.4625 -0.0789 -0.0526 -0.1131 278 HOH   B O   
7128 O O   . HOH   G .   ? 0.2917 0.2002 0.5451 0.0144  0.0528  0.0417  279 HOH   B O   
7129 O O   . HOH   G .   ? 0.4700 0.4387 0.4884 0.0173  -0.1664 0.0657  280 HOH   B O   
7130 O O   . HOH   G .   ? 0.2225 0.3431 0.3034 -0.0404 0.0305  -0.1321 281 HOH   B O   
7131 O O   . HOH   G .   ? 0.1837 0.1695 0.1509 -0.0481 -0.0458 0.0109  282 HOH   B O   
7132 O O   . HOH   G .   ? 0.1624 0.1472 0.1666 0.0042  0.0076  0.0020  283 HOH   B O   
7133 O O   . HOH   G .   ? 0.3585 0.2776 0.4045 -0.0376 -0.0528 -0.0180 284 HOH   B O   
7134 O O   . HOH   G .   ? 0.5612 0.3929 0.3168 0.2577  0.1515  0.1123  285 HOH   B O   
7135 O O   . HOH   G .   ? 0.1562 0.1475 0.3289 -0.0179 -0.0045 -0.0001 286 HOH   B O   
7136 O O   . HOH   G .   ? 0.3864 0.2374 0.2060 0.0330  -0.0933 0.0090  287 HOH   B O   
7137 O O   . HOH   G .   ? 0.2694 0.4471 0.5019 -0.1133 -0.1262 0.0655  288 HOH   B O   
7138 O O   . HOH   G .   ? 0.1557 0.1932 0.1478 -0.0092 -0.0181 0.0076  289 HOH   B O   
7139 O O   . HOH   G .   ? 0.6181 0.5447 0.4760 0.2877  -0.0627 -0.0045 290 HOH   B O   
7140 O O   . HOH   G .   ? 0.2222 0.2168 0.5200 -0.0492 0.0012  0.1272  291 HOH   B O   
7141 O O   . HOH   G .   ? 0.2837 0.7545 0.6884 0.1670  -0.0765 -0.1292 292 HOH   B O   
7142 O O   . HOH   G .   ? 0.1661 0.1945 0.2834 0.0199  -0.0087 0.0019  293 HOH   B O   
7143 O O   . HOH   G .   ? 0.2509 0.6686 0.1907 0.0835  -0.0240 -0.0434 294 HOH   B O   
7144 O O   . HOH   G .   ? 0.2561 0.2613 0.2681 0.0136  -0.0771 0.0145  295 HOH   B O   
7145 O O   . HOH   G .   ? 0.3565 0.1927 0.3585 -0.0840 -0.1871 0.0713  296 HOH   B O   
7146 O O   . HOH   G .   ? 0.4438 0.5160 0.2376 0.0028  0.0931  0.1310  297 HOH   B O   
7147 O O   . HOH   G .   ? 0.1709 0.3159 0.5798 0.0318  -0.0189 -0.1506 298 HOH   B O   
7148 O O   . HOH   G .   ? 0.1748 0.1542 0.2314 0.0131  0.0067  0.0211  299 HOH   B O   
7149 O O   . HOH   G .   ? 0.5410 0.7517 0.2268 -0.0625 -0.0991 0.0341  300 HOH   B O   
7150 O O   . HOH   G .   ? 0.4031 0.3300 0.2192 0.0962  -0.0556 0.0638  301 HOH   B O   
7151 O O   . HOH   G .   ? 0.3258 0.2863 0.2842 -0.0498 0.0233  -0.1381 302 HOH   B O   
7152 O O   . HOH   G .   ? 0.2110 0.3237 0.5930 0.0720  -0.0725 -0.1734 303 HOH   B O   
7153 O O   . HOH   G .   ? 0.3884 0.2639 0.2155 -0.1482 0.0460  -0.0215 304 HOH   B O   
7154 O O   . HOH   G .   ? 0.1562 0.1373 0.3257 -0.0005 -0.0002 0.0038  305 HOH   B O   
7155 O O   . HOH   G .   ? 0.3255 0.3260 0.4335 -0.1237 0.1407  -0.0512 306 HOH   B O   
7156 O O   . HOH   G .   ? 0.2064 0.6754 0.4664 -0.0962 -0.0054 -0.0071 307 HOH   B O   
7157 O O   . HOH   G .   ? 0.3274 0.1818 0.3275 0.0685  0.1217  0.0560  308 HOH   B O   
7158 O O   . HOH   G .   ? 0.2075 0.3351 0.4640 -0.0182 -0.0661 -0.0383 309 HOH   B O   
7159 O O   . HOH   G .   ? 0.2035 0.1702 0.2475 -0.0423 -0.0130 -0.0148 310 HOH   B O   
7160 O O   . HOH   G .   ? 0.2033 0.1523 0.3265 0.0365  -0.0960 0.0005  311 HOH   B O   
7161 O O   . HOH   G .   ? 0.2334 0.1438 0.2483 -0.0227 -0.0240 0.0292  312 HOH   B O   
7162 O O   . HOH   G .   ? 0.3108 0.2638 0.4822 -0.0145 -0.0315 0.1165  313 HOH   B O   
7163 O O   . HOH   G .   ? 0.2166 0.1872 0.1782 -0.0044 0.0152  0.0262  314 HOH   B O   
7164 O O   . HOH   G .   ? 0.4601 0.2586 0.3075 0.0533  0.0644  0.0996  315 HOH   B O   
7165 O O   . HOH   G .   ? 0.1549 0.1797 0.2878 -0.0273 -0.0072 0.0104  316 HOH   B O   
7166 O O   . HOH   G .   ? 0.4057 0.6894 0.3385 0.2154  -0.0622 0.0810  317 HOH   B O   
7167 O O   . HOH   G .   ? 0.2844 0.3192 0.3582 -0.0622 0.1355  -0.1211 318 HOH   B O   
7168 O O   . HOH   G .   ? 0.1613 0.2759 0.2146 -0.0125 -0.0215 0.0640  319 HOH   B O   
7169 O O   . HOH   G .   ? 0.4021 0.2100 0.2648 0.1424  0.0834  0.0282  320 HOH   B O   
7170 O O   . HOH   G .   ? 0.5343 0.4036 0.2795 0.0295  -0.0376 -0.0755 321 HOH   B O   
7171 O O   . HOH   G .   ? 0.6371 0.4500 0.5479 0.1355  0.2305  0.0479  322 HOH   B O   
7172 O O   . HOH   G .   ? 0.5667 0.3789 0.4259 0.0575  0.0974  -0.1602 323 HOH   B O   
7173 O O   . HOH   G .   ? 0.2909 0.3245 0.5838 -0.0661 -0.1780 0.1975  324 HOH   B O   
7174 O O   . HOH   G .   ? 0.1518 0.1692 0.2829 -0.0210 -0.0039 -0.0148 325 HOH   B O   
7175 O O   . HOH   G .   ? 0.6153 0.3585 0.4054 0.0476  0.1668  0.1642  326 HOH   B O   
7176 O O   . HOH   G .   ? 0.4776 0.4028 0.5093 0.0475  0.0208  0.0106  327 HOH   B O   
7177 O O   . HOH   G .   ? 0.3426 0.2175 0.2302 0.0346  -0.0224 0.0441  328 HOH   B O   
7178 O O   . HOH   G .   ? 0.3475 0.3732 0.8018 -0.0212 -0.0905 0.2253  329 HOH   B O   
7179 O O   . HOH   G .   ? 0.1737 0.1807 0.2755 0.0239  0.0412  0.0104  330 HOH   B O   
7180 O O   . HOH   G .   ? 0.4217 0.4887 0.4569 -0.0524 0.0025  0.1665  331 HOH   B O   
7181 O O   . HOH   G .   ? 0.1761 0.2855 0.3343 0.0333  -0.0164 -0.0816 332 HOH   B O   
7182 O O   . HOH   G .   ? 0.2644 0.1904 0.5727 0.0080  -0.0106 0.0485  333 HOH   B O   
7183 O O   . HOH   G .   ? 0.5816 0.5156 0.7184 0.1574  -0.0814 0.2278  334 HOH   B O   
7184 O O   . HOH   G .   ? 0.4656 0.3335 0.5294 0.1524  0.2441  0.1922  335 HOH   B O   
7185 O O   . HOH   G .   ? 0.8080 0.2205 0.3453 0.0091  -0.1056 -0.0170 336 HOH   B O   
7186 O O   . HOH   G .   ? 0.4819 0.4620 0.3402 0.0177  -0.1130 0.0381  337 HOH   B O   
7187 O O   . HOH   G .   ? 0.1770 0.1458 0.2262 0.0145  -0.0199 0.0071  338 HOH   B O   
7188 O O   . HOH   G .   ? 0.6041 0.6191 0.5768 -0.0798 -0.0745 0.2346  339 HOH   B O   
7189 O O   . HOH   G .   ? 0.5857 0.4245 0.6700 -0.1129 -0.1297 -0.0773 340 HOH   B O   
7190 O O   . HOH   G .   ? 0.3693 0.7540 0.4044 -0.0670 -0.0774 0.2230  341 HOH   B O   
7191 O O   . HOH   G .   ? 0.2765 0.4945 0.6511 -0.0194 -0.0257 0.0302  342 HOH   B O   
7192 O O   . HOH   G .   ? 0.4720 0.4128 0.2135 0.1541  -0.1169 -0.0427 343 HOH   B O   
7193 O O   . HOH   G .   ? 0.4549 0.2871 0.2860 0.0712  -0.1200 -0.0727 344 HOH   B O   
7194 O O   . HOH   G .   ? 0.4226 0.6479 0.3918 -0.1056 -0.1032 -0.0841 345 HOH   B O   
7195 O O   . HOH   G .   ? 0.2723 0.1738 0.4088 0.0369  -0.1210 -0.0518 346 HOH   B O   
7196 O O   . HOH   G .   ? 0.2020 0.1935 0.2983 -0.0014 0.0635  0.0060  347 HOH   B O   
7197 O O   . HOH   G .   ? 0.6194 0.5434 0.5751 -0.1407 0.0929  0.0818  348 HOH   B O   
7198 O O   . HOH   G .   ? 0.7461 0.5572 0.3196 0.0754  -0.0507 0.1461  349 HOH   B O   
7199 O O   . HOH   G .   ? 0.2696 0.2191 0.4845 -0.0323 -0.0876 -0.0416 350 HOH   B O   
7200 O O   . HOH   G .   ? 0.4630 0.6946 0.7686 0.0664  0.0765  -0.0105 351 HOH   B O   
7201 O O   . HOH   G .   ? 0.4263 0.6856 0.6461 -0.0458 -0.1040 0.2081  352 HOH   B O   
7202 O O   . HOH   G .   ? 0.5022 0.2457 0.5265 -0.0617 0.1705  0.0499  353 HOH   B O   
7203 O O   . HOH   G .   ? 0.2232 0.5594 0.3427 0.1413  -0.0535 -0.1463 354 HOH   B O   
7204 O O   . HOH   G .   ? 0.3198 0.4441 0.4458 -0.1498 0.0345  -0.0563 355 HOH   B O   
7205 O O   . HOH   G .   ? 0.2245 0.3634 0.4603 0.0259  0.0153  -0.0042 356 HOH   B O   
7206 O O   . HOH   G .   ? 0.3947 0.2026 0.3292 -0.0775 0.0602  -0.0867 357 HOH   B O   
7207 O O   . HOH   G .   ? 0.5134 0.5092 0.5164 0.2267  -0.1316 0.1235  358 HOH   B O   
7208 O O   . HOH   G .   ? 0.3703 0.2876 0.3646 -0.0993 -0.0109 -0.0620 359 HOH   B O   
7209 O O   . HOH   G .   ? 0.4596 0.3695 0.3963 -0.0064 0.1072  -0.0620 360 HOH   B O   
7210 O O   . HOH   G .   ? 0.6145 0.3572 0.5046 0.0293  -0.1608 -0.0944 361 HOH   B O   
7211 O O   . HOH   G .   ? 0.5406 0.4071 0.6230 0.0450  0.1186  0.1565  362 HOH   B O   
7212 O O   . HOH   G .   ? 0.2286 0.4588 0.6293 -0.1110 -0.0534 -0.0906 363 HOH   B O   
7213 O O   . HOH   G .   ? 0.3956 0.7151 0.2966 0.2085  -0.0257 0.0421  364 HOH   B O   
7214 O O   . HOH   G .   ? 0.4724 0.3382 0.4448 0.0221  0.0238  0.0270  365 HOH   B O   
7215 O O   . HOH   G .   ? 0.6068 0.2317 0.3191 -0.0112 -0.0476 0.0789  366 HOH   B O   
7216 O O   . HOH   G .   ? 0.6455 0.4708 0.4041 0.1232  0.0058  0.0585  367 HOH   B O   
7217 O O   . HOH   G .   ? 0.4843 0.6113 0.5102 -0.0394 -0.0289 -0.1212 368 HOH   B O   
7218 O O   . HOH   G .   ? 0.4166 0.4133 0.5754 0.1560  -0.1596 -0.0159 369 HOH   B O   
7219 O O   . HOH   G .   ? 0.4923 0.3095 0.5053 -0.1358 -0.0507 0.0103  370 HOH   B O   
7220 O O   . HOH   G .   ? 0.4001 0.5779 0.4947 0.2625  0.0937  0.1338  371 HOH   B O   
7221 O O   . HOH   G .   ? 0.4481 0.6918 0.3091 0.1933  -0.0845 0.0955  372 HOH   B O   
7222 O O   . HOH   G .   ? 0.5769 0.3622 0.2746 -0.1005 -0.0923 -0.0453 373 HOH   B O   
7223 O O   . HOH   G .   ? 0.8186 0.7560 0.5516 0.2649  -0.1160 -0.0199 374 HOH   B O   
7224 O O   . HOH   G .   ? 0.4698 0.6704 0.5888 0.1288  -0.0143 0.2717  375 HOH   B O   
7225 O O   . HOH   G .   ? 0.3117 0.3573 0.3008 0.0911  -0.0694 -0.0706 376 HOH   B O   
7226 O O   . HOH   G .   ? 0.4497 0.4844 0.4776 -0.1044 -0.0470 0.0522  377 HOH   B O   
7227 O O   . HOH   G .   ? 0.3169 0.6658 0.2155 -0.0499 0.0117  0.0444  378 HOH   B O   
7228 O O   . HOH   G .   ? 0.3399 0.4955 0.5735 0.0816  -0.0605 -0.0225 379 HOH   B O   
7229 O O   . HOH   G .   ? 0.2307 0.3756 0.4024 0.0265  -0.0700 -0.0488 380 HOH   B O   
7230 O O   . HOH   G .   ? 0.5269 0.7015 0.3601 -0.1370 0.0067  -0.1552 381 HOH   B O   
7231 O O   . HOH   G .   ? 0.7318 0.3208 0.4506 -0.0590 -0.0828 -0.0378 382 HOH   B O   
7232 O O   . HOH   G .   ? 0.3870 0.6206 0.4784 0.0404  0.1364  0.1112  383 HOH   B O   
7233 O O   . HOH   G .   ? 0.3429 0.7639 0.4773 0.0805  0.1170  0.0972  384 HOH   B O   
7234 O O   . HOH   G .   ? 0.7493 0.3077 0.3922 0.0631  0.0395  -0.0671 385 HOH   B O   
7235 O O   . HOH   G .   ? 0.2906 0.2640 0.2835 0.0107  0.0017  0.0076  386 HOH   B O   
7236 O O   . HOH   G .   ? 0.5237 0.3607 0.3465 0.0370  0.1109  -0.0376 387 HOH   B O   
7237 O O   . HOH   G .   ? 0.2113 0.4115 0.4177 -0.0639 -0.0911 0.0070  388 HOH   B O   
7238 O O   . HOH   G .   ? 0.6600 0.4094 0.4970 -0.0918 0.0701  0.0054  389 HOH   B O   
7239 O O   . HOH   G .   ? 0.6987 0.4823 0.4400 0.1614  -0.0327 0.0724  390 HOH   B O   
7240 O O   . HOH   G .   ? 0.3846 0.2187 0.2915 0.0812  -0.0346 0.0082  391 HOH   B O   
7241 O O   . HOH   G .   ? 0.5030 0.4498 0.3889 0.0351  0.0109  0.0507  392 HOH   B O   
7242 O O   . HOH   G .   ? 0.4570 0.2011 0.5176 -0.0530 0.1121  0.0677  393 HOH   B O   
7243 O O   . HOH   G .   ? 0.2471 0.4275 0.6776 -0.1196 -0.0821 -0.0173 394 HOH   B O   
7244 O O   . HOH   G .   ? 0.4013 0.7547 0.4438 0.0841  0.0286  -0.1107 395 HOH   B O   
7245 O O   . HOH   G .   ? 0.3274 0.4240 0.3501 -0.0057 0.0264  -0.1076 396 HOH   B O   
7246 O O   . HOH   G .   ? 0.5501 0.4170 0.4273 0.0791  0.1181  0.0675  397 HOH   B O   
7247 O O   . HOH   G .   ? 0.2157 0.2758 0.6369 -0.0603 -0.0832 0.0453  398 HOH   B O   
7248 O O   . HOH   G .   ? 0.5998 0.3735 0.2934 -0.1913 -0.0637 0.0703  399 HOH   B O   
7249 O O   . HOH   G .   ? 0.5546 0.5696 0.4902 -0.0041 -0.1123 0.2940  400 HOH   B O   
7250 O O   . HOH   G .   ? 0.5179 0.4909 0.3207 0.1193  0.0190  -0.0170 401 HOH   B O   
# 
