data_7HCE
# 
_entry.id   7HCE 
# 
_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   7HCE         pdb_00007hce 10.2210/pdb7hce/pdb 
WWPDB D_1001407296 ?            ?                   
# 
_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                        7HCE 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                                                   
18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                         
78.133    1   ?                      ? ? ?                                                                                    
3 non-polymer syn '1-[(1R,6S,8R)-8lambda~4~-thia-7,9-diazatetracyclo[4.3.0.0~1,8~.0~6,8~]nona-2,4-diene-2-sulfonyl]-L-proline' 
315.369   1   ?                      ? ? ?                                                                                    
4 water       nat water                                                                                                        
18.015    433 ?                      ? ? ?                                                                                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                                                         DMS   
3 '1-[(1R,6S,8R)-8lambda~4~-thia-7,9-diazatetracyclo[4.3.0.0~1,8~.0~6,8~]nona-2,4-diene-2-sulfonyl]-L-proline' A1A47 
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 
A1A47 non-polymer         . 
'1-[(1R,6S,8R)-8lambda~4~-thia-7,9-diazatetracyclo[4.3.0.0~1,8~.0~6,8~]nona-2,4-diene-2-sulfonyl]-L-proline' ? 'C11 H13 N3 O4 S2' 
315.369 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'        78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301 301  DMS   DMS A . 
D 3 A1A47 1   302 201  A1A47 LA1 A . 
E 4 HOH   1   401 196  HOH   HOH A . 
E 4 HOH   2   402 292  HOH   HOH A . 
E 4 HOH   3   403 1301 HOH   HOH A . 
E 4 HOH   4   404 229  HOH   HOH A . 
E 4 HOH   5   405 662  HOH   HOH A . 
E 4 HOH   6   406 625  HOH   HOH A . 
E 4 HOH   7   407 209  HOH   HOH A . 
E 4 HOH   8   408 493  HOH   HOH A . 
E 4 HOH   9   409 153  HOH   HOH A . 
E 4 HOH   10  410 18   HOH   HOH A . 
E 4 HOH   11  411 148  HOH   HOH A . 
E 4 HOH   12  412 93   HOH   HOH A . 
E 4 HOH   13  413 76   HOH   HOH A . 
E 4 HOH   14  414 247  HOH   HOH A . 
E 4 HOH   15  415 109  HOH   HOH A . 
E 4 HOH   16  416 236  HOH   HOH A . 
E 4 HOH   17  417 18   HOH   HOH A . 
E 4 HOH   18  418 1283 HOH   HOH A . 
E 4 HOH   19  419 225  HOH   HOH A . 
E 4 HOH   20  420 57   HOH   HOH A . 
E 4 HOH   21  421 15   HOH   HOH A . 
E 4 HOH   22  422 136  HOH   HOH A . 
E 4 HOH   23  423 124  HOH   HOH A . 
E 4 HOH   24  424 151  HOH   HOH A . 
E 4 HOH   25  425 1295 HOH   HOH A . 
E 4 HOH   26  426 409  HOH   HOH A . 
E 4 HOH   27  427 964  HOH   HOH A . 
E 4 HOH   28  428 140  HOH   HOH A . 
E 4 HOH   29  429 192  HOH   HOH A . 
E 4 HOH   30  430 469  HOH   HOH A . 
E 4 HOH   31  431 1300 HOH   HOH A . 
E 4 HOH   32  432 17   HOH   HOH A . 
E 4 HOH   33  433 337  HOH   HOH A . 
E 4 HOH   34  434 1275 HOH   HOH A . 
E 4 HOH   35  435 241  HOH   HOH A . 
E 4 HOH   36  436 630  HOH   HOH A . 
E 4 HOH   37  437 105  HOH   HOH A . 
E 4 HOH   38  438 393  HOH   HOH A . 
E 4 HOH   39  439 9    HOH   HOH A . 
E 4 HOH   40  440 24   HOH   HOH A . 
E 4 HOH   41  441 164  HOH   HOH A . 
E 4 HOH   42  442 36   HOH   HOH A . 
E 4 HOH   43  443 354  HOH   HOH A . 
E 4 HOH   44  444 281  HOH   HOH A . 
E 4 HOH   45  445 381  HOH   HOH A . 
E 4 HOH   46  446 39   HOH   HOH A . 
E 4 HOH   47  447 661  HOH   HOH A . 
E 4 HOH   48  448 165  HOH   HOH A . 
E 4 HOH   49  449 138  HOH   HOH A . 
E 4 HOH   50  450 139  HOH   HOH A . 
E 4 HOH   51  451 66   HOH   HOH A . 
E 4 HOH   52  452 33   HOH   HOH A . 
E 4 HOH   53  453 102  HOH   HOH A . 
E 4 HOH   54  454 81   HOH   HOH A . 
E 4 HOH   55  455 78   HOH   HOH A . 
E 4 HOH   56  456 396  HOH   HOH A . 
E 4 HOH   57  457 42   HOH   HOH A . 
E 4 HOH   58  458 92   HOH   HOH A . 
E 4 HOH   59  459 1290 HOH   HOH A . 
E 4 HOH   60  460 155  HOH   HOH A . 
E 4 HOH   61  461 169  HOH   HOH A . 
E 4 HOH   62  462 1310 HOH   HOH A . 
E 4 HOH   63  463 6    HOH   HOH A . 
E 4 HOH   64  464 23   HOH   HOH A . 
E 4 HOH   65  465 19   HOH   HOH A . 
E 4 HOH   66  466 2    HOH   HOH A . 
E 4 HOH   67  467 320  HOH   HOH A . 
E 4 HOH   68  468 45   HOH   HOH A . 
E 4 HOH   69  469 56   HOH   HOH A . 
E 4 HOH   70  470 162  HOH   HOH A . 
E 4 HOH   71  471 939  HOH   HOH A . 
E 4 HOH   72  472 5    HOH   HOH A . 
E 4 HOH   73  473 19   HOH   HOH A . 
E 4 HOH   74  474 49   HOH   HOH A . 
E 4 HOH   75  475 132  HOH   HOH A . 
E 4 HOH   76  476 85   HOH   HOH A . 
E 4 HOH   77  477 27   HOH   HOH A . 
E 4 HOH   78  478 1    HOH   HOH A . 
E 4 HOH   79  479 8    HOH   HOH A . 
E 4 HOH   80  480 46   HOH   HOH A . 
E 4 HOH   81  481 96   HOH   HOH A . 
E 4 HOH   82  482 74   HOH   HOH A . 
E 4 HOH   83  483 3    HOH   HOH A . 
E 4 HOH   84  484 7    HOH   HOH A . 
E 4 HOH   85  485 134  HOH   HOH A . 
E 4 HOH   86  486 296  HOH   HOH A . 
E 4 HOH   87  487 34   HOH   HOH A . 
E 4 HOH   88  488 12   HOH   HOH A . 
E 4 HOH   89  489 186  HOH   HOH A . 
E 4 HOH   90  490 86   HOH   HOH A . 
E 4 HOH   91  491 26   HOH   HOH A . 
E 4 HOH   92  492 4    HOH   HOH A . 
E 4 HOH   93  493 35   HOH   HOH A . 
E 4 HOH   94  494 154  HOH   HOH A . 
E 4 HOH   95  495 159  HOH   HOH A . 
E 4 HOH   96  496 195  HOH   HOH A . 
E 4 HOH   97  497 366  HOH   HOH A . 
E 4 HOH   98  498 351  HOH   HOH A . 
E 4 HOH   99  499 1315 HOH   HOH A . 
E 4 HOH   100 500 122  HOH   HOH A . 
E 4 HOH   101 501 1308 HOH   HOH A . 
E 4 HOH   102 502 11   HOH   HOH A . 
E 4 HOH   103 503 6    HOH   HOH A . 
E 4 HOH   104 504 405  HOH   HOH A . 
E 4 HOH   105 505 58   HOH   HOH A . 
E 4 HOH   106 506 1279 HOH   HOH A . 
E 4 HOH   107 507 8    HOH   HOH A . 
E 4 HOH   108 508 461  HOH   HOH A . 
E 4 HOH   109 509 116  HOH   HOH A . 
E 4 HOH   110 510 83   HOH   HOH A . 
E 4 HOH   111 511 218  HOH   HOH A . 
E 4 HOH   112 512 24   HOH   HOH A . 
E 4 HOH   113 513 1289 HOH   HOH A . 
E 4 HOH   114 514 67   HOH   HOH A . 
E 4 HOH   115 515 25   HOH   HOH A . 
E 4 HOH   116 516 21   HOH   HOH A . 
E 4 HOH   117 517 17   HOH   HOH A . 
E 4 HOH   118 518 68   HOH   HOH A . 
E 4 HOH   119 519 121  HOH   HOH A . 
E 4 HOH   120 520 1309 HOH   HOH A . 
E 4 HOH   121 521 199  HOH   HOH A . 
E 4 HOH   122 522 303  HOH   HOH A . 
E 4 HOH   123 523 1189 HOH   HOH A . 
E 4 HOH   124 524 397  HOH   HOH A . 
E 4 HOH   125 525 123  HOH   HOH A . 
E 4 HOH   126 526 95   HOH   HOH A . 
E 4 HOH   127 527 333  HOH   HOH A . 
E 4 HOH   128 528 7    HOH   HOH A . 
E 4 HOH   129 529 1222 HOH   HOH A . 
E 4 HOH   130 530 53   HOH   HOH A . 
E 4 HOH   131 531 22   HOH   HOH A . 
E 4 HOH   132 532 156  HOH   HOH A . 
E 4 HOH   133 533 125  HOH   HOH A . 
E 4 HOH   134 534 278  HOH   HOH A . 
E 4 HOH   135 535 582  HOH   HOH A . 
E 4 HOH   136 536 51   HOH   HOH A . 
E 4 HOH   137 537 1068 HOH   HOH A . 
E 4 HOH   138 538 1313 HOH   HOH A . 
E 4 HOH   139 539 26   HOH   HOH A . 
E 4 HOH   140 540 212  HOH   HOH A . 
E 4 HOH   141 541 1094 HOH   HOH A . 
E 4 HOH   142 542 40   HOH   HOH A . 
E 4 HOH   143 543 952  HOH   HOH A . 
E 4 HOH   144 544 944  HOH   HOH A . 
E 4 HOH   145 545 71   HOH   HOH A . 
E 4 HOH   146 546 1238 HOH   HOH A . 
E 4 HOH   147 547 20   HOH   HOH A . 
E 4 HOH   148 548 70   HOH   HOH A . 
E 4 HOH   149 549 80   HOH   HOH A . 
E 4 HOH   150 550 576  HOH   HOH A . 
E 4 HOH   151 551 1286 HOH   HOH A . 
E 4 HOH   152 552 21   HOH   HOH A . 
E 4 HOH   153 553 94   HOH   HOH A . 
E 4 HOH   154 554 188  HOH   HOH A . 
E 4 HOH   155 555 104  HOH   HOH A . 
E 4 HOH   156 556 16   HOH   HOH A . 
E 4 HOH   157 557 115  HOH   HOH A . 
E 4 HOH   158 558 73   HOH   HOH A . 
E 4 HOH   159 559 97   HOH   HOH A . 
E 4 HOH   160 560 1119 HOH   HOH A . 
E 4 HOH   161 561 330  HOH   HOH A . 
E 4 HOH   162 562 1296 HOH   HOH A . 
E 4 HOH   163 563 16   HOH   HOH A . 
E 4 HOH   164 564 79   HOH   HOH A . 
E 4 HOH   165 565 1134 HOH   HOH A . 
E 4 HOH   166 566 107  HOH   HOH A . 
E 4 HOH   167 567 509  HOH   HOH A . 
E 4 HOH   168 568 726  HOH   HOH A . 
E 4 HOH   169 569 163  HOH   HOH A . 
E 4 HOH   170 570 756  HOH   HOH A . 
E 4 HOH   171 571 361  HOH   HOH A . 
E 4 HOH   172 572 801  HOH   HOH A . 
E 4 HOH   173 573 1276 HOH   HOH A . 
E 4 HOH   174 574 408  HOH   HOH A . 
E 4 HOH   175 575 126  HOH   HOH A . 
E 4 HOH   176 576 556  HOH   HOH A . 
E 4 HOH   177 577 280  HOH   HOH A . 
E 4 HOH   178 578 63   HOH   HOH A . 
E 4 HOH   179 579 319  HOH   HOH A . 
E 4 HOH   180 580 342  HOH   HOH A . 
E 4 HOH   181 581 1307 HOH   HOH A . 
E 4 HOH   182 582 250  HOH   HOH A . 
E 4 HOH   183 583 370  HOH   HOH A . 
E 4 HOH   184 584 1306 HOH   HOH A . 
E 4 HOH   185 585 202  HOH   HOH A . 
E 4 HOH   186 586 224  HOH   HOH A . 
E 4 HOH   187 587 1287 HOH   HOH A . 
E 4 HOH   188 588 695  HOH   HOH A . 
E 4 HOH   189 589 267  HOH   HOH A . 
E 4 HOH   190 590 135  HOH   HOH A . 
E 4 HOH   191 591 13   HOH   HOH A . 
E 4 HOH   192 592 674  HOH   HOH A . 
E 4 HOH   193 593 919  HOH   HOH A . 
E 4 HOH   194 594 1314 HOH   HOH A . 
E 4 HOH   195 595 2    HOH   HOH A . 
E 4 HOH   196 596 309  HOH   HOH A . 
E 4 HOH   197 597 318  HOH   HOH A . 
E 4 HOH   198 598 521  HOH   HOH A . 
E 4 HOH   199 599 711  HOH   HOH A . 
E 4 HOH   200 600 1299 HOH   HOH A . 
E 4 HOH   201 601 263  HOH   HOH A . 
E 4 HOH   202 602 805  HOH   HOH A . 
E 4 HOH   203 603 941  HOH   HOH A . 
E 4 HOH   204 604 152  HOH   HOH A . 
E 4 HOH   205 605 315  HOH   HOH A . 
E 4 HOH   206 606 208  HOH   HOH A . 
E 4 HOH   207 607 331  HOH   HOH A . 
E 4 HOH   208 608 356  HOH   HOH A . 
E 4 HOH   209 609 25   HOH   HOH A . 
E 4 HOH   210 610 4    HOH   HOH A . 
E 4 HOH   211 611 10   HOH   HOH A . 
E 4 HOH   212 612 180  HOH   HOH A . 
E 4 HOH   213 613 5    HOH   HOH A . 
E 4 HOH   214 614 1071 HOH   HOH A . 
E 4 HOH   215 615 350  HOH   HOH A . 
E 4 HOH   216 616 3    HOH   HOH A . 
E 4 HOH   217 617 371  HOH   HOH A . 
E 4 HOH   218 618 363  HOH   HOH A . 
E 4 HOH   219 619 313  HOH   HOH A . 
E 4 HOH   220 620 326  HOH   HOH A . 
E 4 HOH   221 621 1284 HOH   HOH A . 
E 4 HOH   222 622 185  HOH   HOH A . 
E 4 HOH   223 623 429  HOH   HOH A . 
E 4 HOH   224 624 772  HOH   HOH A . 
E 4 HOH   225 625 376  HOH   HOH A . 
E 4 HOH   226 626 1074 HOH   HOH A . 
E 4 HOH   227 627 346  HOH   HOH A . 
E 4 HOH   228 628 14   HOH   HOH A . 
E 4 HOH   229 629 1292 HOH   HOH A . 
E 4 HOH   230 630 12   HOH   HOH A . 
E 4 HOH   231 631 15   HOH   HOH A . 
E 4 HOH   232 632 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 358  HOH   HOH B . 
F 4 HOH   3   203 1249 HOH   HOH B . 
F 4 HOH   4   204 654  HOH   HOH B . 
F 4 HOH   5   205 364  HOH   HOH B . 
F 4 HOH   6   206 900  HOH   HOH B . 
F 4 HOH   7   207 758  HOH   HOH B . 
F 4 HOH   8   208 549  HOH   HOH B . 
F 4 HOH   9   209 531  HOH   HOH B . 
F 4 HOH   10  210 743  HOH   HOH B . 
F 4 HOH   11  211 240  HOH   HOH B . 
F 4 HOH   12  212 120  HOH   HOH B . 
F 4 HOH   13  213 264  HOH   HOH B . 
F 4 HOH   14  214 398  HOH   HOH B . 
F 4 HOH   15  215 353  HOH   HOH B . 
F 4 HOH   16  216 131  HOH   HOH B . 
F 4 HOH   17  217 444  HOH   HOH B . 
F 4 HOH   18  218 343  HOH   HOH B . 
F 4 HOH   19  219 50   HOH   HOH B . 
F 4 HOH   20  220 282  HOH   HOH B . 
F 4 HOH   21  221 332  HOH   HOH B . 
F 4 HOH   22  222 452  HOH   HOH B . 
F 4 HOH   23  223 276  HOH   HOH B . 
F 4 HOH   24  224 54   HOH   HOH B . 
F 4 HOH   25  225 1140 HOH   HOH B . 
F 4 HOH   26  226 1278 HOH   HOH B . 
F 4 HOH   27  227 272  HOH   HOH B . 
F 4 HOH   28  228 205  HOH   HOH B . 
F 4 HOH   29  229 723  HOH   HOH B . 
F 4 HOH   30  230 127  HOH   HOH B . 
F 4 HOH   31  231 1312 HOH   HOH B . 
F 4 HOH   32  232 128  HOH   HOH B . 
F 4 HOH   33  233 110  HOH   HOH B . 
F 4 HOH   34  234 1    HOH   HOH B . 
F 4 HOH   35  235 325  HOH   HOH B . 
F 4 HOH   36  236 82   HOH   HOH B . 
F 4 HOH   37  237 75   HOH   HOH B . 
F 4 HOH   38  238 181  HOH   HOH B . 
F 4 HOH   39  239 9    HOH   HOH B . 
F 4 HOH   40  240 133  HOH   HOH B . 
F 4 HOH   41  241 172  HOH   HOH B . 
F 4 HOH   42  242 300  HOH   HOH B . 
F 4 HOH   43  243 69   HOH   HOH B . 
F 4 HOH   44  244 302  HOH   HOH B . 
F 4 HOH   45  245 72   HOH   HOH B . 
F 4 HOH   46  246 232  HOH   HOH B . 
F 4 HOH   47  247 221  HOH   HOH B . 
F 4 HOH   48  248 347  HOH   HOH B . 
F 4 HOH   49  249 14   HOH   HOH B . 
F 4 HOH   50  250 30   HOH   HOH B . 
F 4 HOH   51  251 231  HOH   HOH B . 
F 4 HOH   52  252 60   HOH   HOH B . 
F 4 HOH   53  253 144  HOH   HOH B . 
F 4 HOH   54  254 166  HOH   HOH B . 
F 4 HOH   55  255 150  HOH   HOH B . 
F 4 HOH   56  256 129  HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 59   HOH   HOH B . 
F 4 HOH   59  259 62   HOH   HOH B . 
F 4 HOH   60  260 391  HOH   HOH B . 
F 4 HOH   61  261 271  HOH   HOH B . 
F 4 HOH   62  262 31   HOH   HOH B . 
F 4 HOH   63  263 41   HOH   HOH B . 
F 4 HOH   64  264 52   HOH   HOH B . 
F 4 HOH   65  265 143  HOH   HOH B . 
F 4 HOH   66  266 10   HOH   HOH B . 
F 4 HOH   67  267 252  HOH   HOH B . 
F 4 HOH   68  268 117  HOH   HOH B . 
F 4 HOH   69  269 61   HOH   HOH B . 
F 4 HOH   70  270 103  HOH   HOH B . 
F 4 HOH   71  271 11   HOH   HOH B . 
F 4 HOH   72  272 20   HOH   HOH B . 
F 4 HOH   73  273 77   HOH   HOH B . 
F 4 HOH   74  274 1277 HOH   HOH B . 
F 4 HOH   75  275 84   HOH   HOH B . 
F 4 HOH   76  276 242  HOH   HOH B . 
F 4 HOH   77  277 43   HOH   HOH B . 
F 4 HOH   78  278 175  HOH   HOH B . 
F 4 HOH   79  279 387  HOH   HOH B . 
F 4 HOH   80  280 114  HOH   HOH B . 
F 4 HOH   81  281 220  HOH   HOH B . 
F 4 HOH   82  282 22   HOH   HOH B . 
F 4 HOH   83  283 147  HOH   HOH B . 
F 4 HOH   84  284 1305 HOH   HOH B . 
F 4 HOH   85  285 235  HOH   HOH B . 
F 4 HOH   86  286 1066 HOH   HOH B . 
F 4 HOH   87  287 287  HOH   HOH B . 
F 4 HOH   88  288 243  HOH   HOH B . 
F 4 HOH   89  289 89   HOH   HOH B . 
F 4 HOH   90  290 704  HOH   HOH B . 
F 4 HOH   91  291 137  HOH   HOH B . 
F 4 HOH   92  292 13   HOH   HOH B . 
F 4 HOH   93  293 106  HOH   HOH B . 
F 4 HOH   94  294 216  HOH   HOH B . 
F 4 HOH   95  295 32   HOH   HOH B . 
F 4 HOH   96  296 99   HOH   HOH B . 
F 4 HOH   97  297 1106 HOH   HOH B . 
F 4 HOH   98  298 299  HOH   HOH B . 
F 4 HOH   99  299 341  HOH   HOH B . 
F 4 HOH   100 300 112  HOH   HOH B . 
F 4 HOH   101 301 160  HOH   HOH B . 
F 4 HOH   102 302 88   HOH   HOH B . 
F 4 HOH   103 303 635  HOH   HOH B . 
F 4 HOH   104 304 215  HOH   HOH B . 
F 4 HOH   105 305 142  HOH   HOH B . 
F 4 HOH   106 306 297  HOH   HOH B . 
F 4 HOH   107 307 118  HOH   HOH B . 
F 4 HOH   108 308 37   HOH   HOH B . 
F 4 HOH   109 309 38   HOH   HOH B . 
F 4 HOH   110 310 48   HOH   HOH B . 
F 4 HOH   111 311 316  HOH   HOH B . 
F 4 HOH   112 312 91   HOH   HOH B . 
F 4 HOH   113 313 101  HOH   HOH B . 
F 4 HOH   114 314 1126 HOH   HOH B . 
F 4 HOH   115 315 311  HOH   HOH B . 
F 4 HOH   116 316 1291 HOH   HOH B . 
F 4 HOH   117 317 182  HOH   HOH B . 
F 4 HOH   118 318 1274 HOH   HOH B . 
F 4 HOH   119 319 177  HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 334  HOH   HOH B . 
F 4 HOH   122 322 141  HOH   HOH B . 
F 4 HOH   123 323 170  HOH   HOH B . 
F 4 HOH   124 324 100  HOH   HOH B . 
F 4 HOH   125 325 339  HOH   HOH B . 
F 4 HOH   126 326 28   HOH   HOH B . 
F 4 HOH   127 327 717  HOH   HOH B . 
F 4 HOH   128 328 197  HOH   HOH B . 
F 4 HOH   129 329 44   HOH   HOH B . 
F 4 HOH   130 330 416  HOH   HOH B . 
F 4 HOH   131 331 161  HOH   HOH B . 
F 4 HOH   132 332 29   HOH   HOH B . 
F 4 HOH   133 333 1294 HOH   HOH B . 
F 4 HOH   134 334 362  HOH   HOH B . 
F 4 HOH   135 335 98   HOH   HOH B . 
F 4 HOH   136 336 1285 HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 207  HOH   HOH B . 
F 4 HOH   139 339 55   HOH   HOH B . 
F 4 HOH   140 340 65   HOH   HOH B . 
F 4 HOH   141 341 234  HOH   HOH B . 
F 4 HOH   142 342 1293 HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 960  HOH   HOH B . 
F 4 HOH   146 346 178  HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 1046 HOH   HOH B . 
F 4 HOH   149 349 1304 HOH   HOH B . 
F 4 HOH   150 350 191  HOH   HOH B . 
F 4 HOH   151 351 335  HOH   HOH B . 
F 4 HOH   152 352 623  HOH   HOH B . 
F 4 HOH   153 353 1280 HOH   HOH B . 
F 4 HOH   154 354 203  HOH   HOH B . 
F 4 HOH   155 355 541  HOH   HOH B . 
F 4 HOH   156 356 304  HOH   HOH B . 
F 4 HOH   157 357 87   HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 1077 HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 479  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 898  HOH   HOH B . 
F 4 HOH   166 366 340  HOH   HOH B . 
F 4 HOH   167 367 1316 HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 615  HOH   HOH B . 
F 4 HOH   171 371 310  HOH   HOH B . 
F 4 HOH   172 372 1303 HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 291  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 183  HOH   HOH B . 
F 4 HOH   177 377 149  HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 1163 HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 418  HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 1311 HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 265  HOH   HOH B . 
F 4 HOH   186 386 491  HOH   HOH B . 
F 4 HOH   187 387 470  HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 1298 HOH   HOH B . 
F 4 HOH   190 390 981  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 184  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 792  HOH   HOH B . 
F 4 HOH   196 396 274  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 566  HOH   HOH B . 
F 4 HOH   199 399 157  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 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           7HCE 
_cell.length_a           88.806 
_cell.length_b           88.806 
_cell.length_c           39.673 
_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                         7HCE 
_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          7HCE 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.93 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2022-06-29 
_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                     7HCE 
_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                   156831 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.036 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        21.800 
_reflns.B_iso_Wilson_estimate        10.360 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.039 
_reflns.pdbx_Rpim_I_all              0.015 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1016389 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.020 1.040  ? 42929 7542 ? 0.523 ? ? ? 5.700 ? 2.500  ? ? ? ? ? ? 97.200 0.577 0.237 0.919 ? 
1 2 5.590 44.400 ? 7149  1039 ? 0.023 ? ? ? 6.900 ? 64.300 ? ? ? ? ? ? 99.700 0.024 0.009 0.999 ? 
# 
_refine.entry_id                                 7HCE 
_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                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6600 
_refine.ls_number_reflns_obs                     156778 
_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                          0.1379 
_refine.ls_R_factor_R_work                       0.1374 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1478 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7558 
_refine.ls_number_reflns_R_work                  149220 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.9431 
_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                                50.860 
_refine.B_iso_min                                6.710 
_refine.pdbx_overall_phase_error                 13.6500 
_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         40 
_refine_hist.number_atoms_solvent             433 
_refine_hist.number_atoms_total               3015 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.44 
_refine_hist.pdbx_B_iso_mean_solvent          26.83 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0200 1.0300  30 96.0000  4752 . 0.3148 0.3395 . 190 0.0000 4942 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 5004 . 0.2520 0.2531 . 281 0.0000 5285 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 4878 . 0.2102 0.2134 . 271 0.0000 5149 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 4972 . 0.1921 0.2243 . 283 0.0000 5255 . 'X-RAY DIFFRACTION' . 
1.0700 1.0800  30 100.0000 4922 . 0.1648 0.1959 . 251 0.0000 5173 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 4959 . 0.1533 0.1872 . 234 0.0000 5193 . 'X-RAY DIFFRACTION' . 
1.1000 1.1100  30 100.0000 4958 . 0.1373 0.1593 . 251 0.0000 5209 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5033 . 0.1325 0.1531 . 233 0.0000 5266 . 'X-RAY DIFFRACTION' . 
1.1300 1.1500  30 100.0000 4897 . 0.1255 0.1335 . 235 0.0000 5132 . 'X-RAY DIFFRACTION' . 
1.1500 1.1700  30 100.0000 5029 . 0.1169 0.1283 . 254 0.0000 5283 . 'X-RAY DIFFRACTION' . 
1.1700 1.1900  30 100.0000 4953 . 0.1158 0.1389 . 251 0.0000 5204 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 4889 . 0.1129 0.1410 . 270 0.0000 5159 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 4990 . 0.1137 0.1328 . 235 0.0000 5225 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 4978 . 0.1181 0.1233 . 255 0.0000 5233 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 4926 . 0.1213 0.1285 . 249 0.0000 5175 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 99.0000  4990 . 0.1232 0.1291 . 258 0.0000 5248 . 'X-RAY DIFFRACTION' . 
1.3200 1.3500  30 100.0000 4937 . 0.1286 0.1342 . 260 0.0000 5197 . 'X-RAY DIFFRACTION' . 
1.3500 1.3800  30 100.0000 4963 . 0.1203 0.1430 . 258 0.0000 5221 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 100.0000 5000 . 0.1166 0.1454 . 229 0.0000 5229 . 'X-RAY DIFFRACTION' . 
1.4300 1.4700  30 100.0000 5009 . 0.1159 0.1250 . 268 0.0000 5277 . 'X-RAY DIFFRACTION' . 
1.4700 1.5200  30 100.0000 4978 . 0.1155 0.1306 . 230 0.0000 5208 . 'X-RAY DIFFRACTION' . 
1.5200 1.5800  30 100.0000 5005 . 0.1163 0.1234 . 269 0.0000 5274 . 'X-RAY DIFFRACTION' . 
1.5800 1.6600  30 99.0000  4929 . 0.1154 0.1246 . 257 0.0000 5186 . 'X-RAY DIFFRACTION' . 
1.6600 1.7400  30 100.0000 5058 . 0.1239 0.1398 . 204 0.0000 5262 . 'X-RAY DIFFRACTION' . 
1.7400 1.8500  30 100.0000 4947 . 0.1289 0.1341 . 291 0.0000 5238 . 'X-RAY DIFFRACTION' . 
1.8500 2.0000  30 100.0000 5014 . 0.1330 0.1283 . 252 0.0000 5266 . 'X-RAY DIFFRACTION' . 
2.0000 2.2000  30 100.0000 4976 . 0.1366 0.1313 . 281 0.0000 5257 . 'X-RAY DIFFRACTION' . 
2.2000 2.5200  30 100.0000 5037 . 0.1383 0.1414 . 251 0.0000 5288 . 'X-RAY DIFFRACTION' . 
2.5200 3.1700  30 100.0000 5051 . 0.1504 0.1583 . 253 0.0000 5304 . 'X-RAY DIFFRACTION' . 
3.1700 44.4000 30 100.0000 5186 . 0.1491 0.1716 . 254 0.0000 5440 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCE 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000002' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCE 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 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 7HCE A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCE 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 7HCE SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCE MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCE SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCE 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 
2 1 B,F     
# 
_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 39  ? VAL A 34  ALA A 39  
AA2 2 HIS A 91  ? VAL A 96  ? HIS A 91  VAL A 96  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HCE 
_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    209 
_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    328 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 54.78 -132.93 
2 1 SER A 128 ? B 66.20 -3.84   
3 1 HIS B 86  ? ? 56.86 -128.49 
# 
_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 627 ? 5.92 .    
2 1 O B A HOH 628 ? .    6.00 
3 1 O ? A HOH 629 ? 6.06 .    
4 1 O B A HOH 630 ? .    6.10 
5 1 O B A HOH 631 ? .    6.32 
6 1 O ? A HOH 632 ? 7.57 .    
7 1 O ? B HOH 401 ? 6.28 .    
# 
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 
A1A47 N2   N N N 1   
A1A47 C3   C N N 2   
A1A47 C6   C Y N 3   
A1A47 C9   C Y N 4   
A1A47 C1   C N N 5   
A1A47 C10  C Y N 6   
A1A47 C11  C Y N 7   
A1A47 C2   C N S 8   
A1A47 C4   C N N 9   
A1A47 C5   C N N 10  
A1A47 C7   C Y N 11  
A1A47 C8   C Y N 12  
A1A47 N1   N N N 13  
A1A47 N3   N N N 14  
A1A47 O1   O N N 15  
A1A47 O2   O N N 16  
A1A47 O3   O N N 17  
A1A47 O4   O N N 18  
A1A47 S1   S N N 19  
A1A47 S2   S N N 20  
A1A47 H11  H N N 21  
A1A47 H3   H N N 22  
A1A47 H2   H N N 23  
A1A47 H10  H N N 24  
A1A47 H1   H N N 25  
A1A47 H4   H N N 26  
A1A47 H5   H N N 27  
A1A47 H6   H N N 28  
A1A47 H7   H N N 29  
A1A47 H8   H N N 30  
A1A47 H9   H N N 31  
A1A47 H12  H N N 32  
A1A47 H13  H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
CYS   N    N N N 107 
CYS   CA   C N R 108 
CYS   C    C N N 109 
CYS   O    O N N 110 
CYS   CB   C N N 111 
CYS   SG   S N N 112 
CYS   OXT  O N N 113 
CYS   H    H N N 114 
CYS   H2   H N N 115 
CYS   HA   H N N 116 
CYS   HB2  H N N 117 
CYS   HB3  H N N 118 
CYS   HG   H N N 119 
CYS   HXT  H N N 120 
DMS   S    S N N 121 
DMS   O    O N N 122 
DMS   C1   C N N 123 
DMS   C2   C N N 124 
DMS   H11  H N N 125 
DMS   H12  H N N 126 
DMS   H13  H N N 127 
DMS   H21  H N N 128 
DMS   H22  H N N 129 
DMS   H23  H N N 130 
GLN   N    N N N 131 
GLN   CA   C N S 132 
GLN   C    C N N 133 
GLN   O    O N N 134 
GLN   CB   C N N 135 
GLN   CG   C N N 136 
GLN   CD   C N N 137 
GLN   OE1  O N N 138 
GLN   NE2  N N N 139 
GLN   OXT  O N N 140 
GLN   H    H N N 141 
GLN   H2   H N N 142 
GLN   HA   H N N 143 
GLN   HB2  H N N 144 
GLN   HB3  H N N 145 
GLN   HG2  H N N 146 
GLN   HG3  H N N 147 
GLN   HE21 H N N 148 
GLN   HE22 H N N 149 
GLN   HXT  H N N 150 
GLU   N    N N N 151 
GLU   CA   C N S 152 
GLU   C    C N N 153 
GLU   O    O N N 154 
GLU   CB   C N N 155 
GLU   CG   C N N 156 
GLU   CD   C N N 157 
GLU   OE1  O N N 158 
GLU   OE2  O N N 159 
GLU   OXT  O N N 160 
GLU   H    H N N 161 
GLU   H2   H N N 162 
GLU   HA   H N N 163 
GLU   HB2  H N N 164 
GLU   HB3  H N N 165 
GLU   HG2  H N N 166 
GLU   HG3  H N N 167 
GLU   HE2  H N N 168 
GLU   HXT  H N N 169 
GLY   N    N N N 170 
GLY   CA   C N N 171 
GLY   C    C N N 172 
GLY   O    O N N 173 
GLY   OXT  O N N 174 
GLY   H    H N N 175 
GLY   H2   H N N 176 
GLY   HA2  H N N 177 
GLY   HA3  H N N 178 
GLY   HXT  H N N 179 
HIS   N    N N N 180 
HIS   CA   C N S 181 
HIS   C    C N N 182 
HIS   O    O N N 183 
HIS   CB   C N N 184 
HIS   CG   C Y N 185 
HIS   ND1  N Y N 186 
HIS   CD2  C Y N 187 
HIS   CE1  C Y N 188 
HIS   NE2  N Y N 189 
HIS   OXT  O N N 190 
HIS   H    H N N 191 
HIS   H2   H N N 192 
HIS   HA   H N N 193 
HIS   HB2  H N N 194 
HIS   HB3  H N N 195 
HIS   HD1  H N N 196 
HIS   HD2  H N N 197 
HIS   HE1  H N N 198 
HIS   HE2  H N N 199 
HIS   HXT  H N N 200 
HOH   O    O N N 201 
HOH   H1   H N N 202 
HOH   H2   H N N 203 
ILE   N    N N N 204 
ILE   CA   C N S 205 
ILE   C    C N N 206 
ILE   O    O N N 207 
ILE   CB   C N S 208 
ILE   CG1  C N N 209 
ILE   CG2  C N N 210 
ILE   CD1  C N N 211 
ILE   OXT  O N N 212 
ILE   H    H N N 213 
ILE   H2   H N N 214 
ILE   HA   H N N 215 
ILE   HB   H N N 216 
ILE   HG12 H N N 217 
ILE   HG13 H N N 218 
ILE   HG21 H N N 219 
ILE   HG22 H N N 220 
ILE   HG23 H N N 221 
ILE   HD11 H N N 222 
ILE   HD12 H N N 223 
ILE   HD13 H N N 224 
ILE   HXT  H N N 225 
LEU   N    N N N 226 
LEU   CA   C N S 227 
LEU   C    C N N 228 
LEU   O    O N N 229 
LEU   CB   C N N 230 
LEU   CG   C N N 231 
LEU   CD1  C N N 232 
LEU   CD2  C N N 233 
LEU   OXT  O N N 234 
LEU   H    H N N 235 
LEU   H2   H N N 236 
LEU   HA   H N N 237 
LEU   HB2  H N N 238 
LEU   HB3  H N N 239 
LEU   HG   H N N 240 
LEU   HD11 H N N 241 
LEU   HD12 H N N 242 
LEU   HD13 H N N 243 
LEU   HD21 H N N 244 
LEU   HD22 H N N 245 
LEU   HD23 H N N 246 
LEU   HXT  H N N 247 
LYS   N    N N N 248 
LYS   CA   C N S 249 
LYS   C    C N N 250 
LYS   O    O N N 251 
LYS   CB   C N N 252 
LYS   CG   C N N 253 
LYS   CD   C N N 254 
LYS   CE   C N N 255 
LYS   NZ   N N N 256 
LYS   OXT  O N N 257 
LYS   H    H N N 258 
LYS   H2   H N N 259 
LYS   HA   H N N 260 
LYS   HB2  H N N 261 
LYS   HB3  H N N 262 
LYS   HG2  H N N 263 
LYS   HG3  H N N 264 
LYS   HD2  H N N 265 
LYS   HD3  H N N 266 
LYS   HE2  H N N 267 
LYS   HE3  H N N 268 
LYS   HZ1  H N N 269 
LYS   HZ2  H N N 270 
LYS   HZ3  H N N 271 
LYS   HXT  H N N 272 
MET   N    N N N 273 
MET   CA   C N S 274 
MET   C    C N N 275 
MET   O    O N N 276 
MET   CB   C N N 277 
MET   CG   C N N 278 
MET   SD   S N N 279 
MET   CE   C N N 280 
MET   OXT  O N N 281 
MET   H    H N N 282 
MET   H2   H N N 283 
MET   HA   H N N 284 
MET   HB2  H N N 285 
MET   HB3  H N N 286 
MET   HG2  H N N 287 
MET   HG3  H N N 288 
MET   HE1  H N N 289 
MET   HE2  H N N 290 
MET   HE3  H N N 291 
MET   HXT  H N N 292 
PHE   N    N N N 293 
PHE   CA   C N S 294 
PHE   C    C N N 295 
PHE   O    O N N 296 
PHE   CB   C N N 297 
PHE   CG   C Y N 298 
PHE   CD1  C Y N 299 
PHE   CD2  C Y N 300 
PHE   CE1  C Y N 301 
PHE   CE2  C Y N 302 
PHE   CZ   C Y N 303 
PHE   OXT  O N N 304 
PHE   H    H N N 305 
PHE   H2   H N N 306 
PHE   HA   H N N 307 
PHE   HB2  H N N 308 
PHE   HB3  H N N 309 
PHE   HD1  H N N 310 
PHE   HD2  H N N 311 
PHE   HE1  H N N 312 
PHE   HE2  H N N 313 
PHE   HZ   H N N 314 
PHE   HXT  H N N 315 
PRO   N    N N N 316 
PRO   CA   C N S 317 
PRO   C    C N N 318 
PRO   O    O N N 319 
PRO   CB   C N N 320 
PRO   CG   C N N 321 
PRO   CD   C N N 322 
PRO   OXT  O N N 323 
PRO   H    H N N 324 
PRO   HA   H N N 325 
PRO   HB2  H N N 326 
PRO   HB3  H N N 327 
PRO   HG2  H N N 328 
PRO   HG3  H N N 329 
PRO   HD2  H N N 330 
PRO   HD3  H N N 331 
PRO   HXT  H N N 332 
SER   N    N N N 333 
SER   CA   C N S 334 
SER   C    C N N 335 
SER   O    O N N 336 
SER   CB   C N N 337 
SER   OG   O N N 338 
SER   OXT  O N N 339 
SER   H    H N N 340 
SER   H2   H N N 341 
SER   HA   H N N 342 
SER   HB2  H N N 343 
SER   HB3  H N N 344 
SER   HG   H N N 345 
SER   HXT  H N N 346 
THR   N    N N N 347 
THR   CA   C N S 348 
THR   C    C N N 349 
THR   O    O N N 350 
THR   CB   C N R 351 
THR   OG1  O N N 352 
THR   CG2  C N N 353 
THR   OXT  O N N 354 
THR   H    H N N 355 
THR   H2   H N N 356 
THR   HA   H N N 357 
THR   HB   H N N 358 
THR   HG1  H N N 359 
THR   HG21 H N N 360 
THR   HG22 H N N 361 
THR   HG23 H N N 362 
THR   HXT  H N N 363 
TYR   N    N N N 364 
TYR   CA   C N S 365 
TYR   C    C N N 366 
TYR   O    O N N 367 
TYR   CB   C N N 368 
TYR   CG   C Y N 369 
TYR   CD1  C Y N 370 
TYR   CD2  C Y N 371 
TYR   CE1  C Y N 372 
TYR   CE2  C Y N 373 
TYR   CZ   C Y N 374 
TYR   OH   O N N 375 
TYR   OXT  O N N 376 
TYR   H    H N N 377 
TYR   H2   H N N 378 
TYR   HA   H N N 379 
TYR   HB2  H N N 380 
TYR   HB3  H N N 381 
TYR   HD1  H N N 382 
TYR   HD2  H N N 383 
TYR   HE1  H N N 384 
TYR   HE2  H N N 385 
TYR   HH   H N N 386 
TYR   HXT  H N N 387 
VAL   N    N N N 388 
VAL   CA   C N S 389 
VAL   C    C N N 390 
VAL   O    O N N 391 
VAL   CB   C N N 392 
VAL   CG1  C N N 393 
VAL   CG2  C N N 394 
VAL   OXT  O N N 395 
VAL   H    H N N 396 
VAL   H2   H N N 397 
VAL   HA   H N N 398 
VAL   HB   H N N 399 
VAL   HG11 H N N 400 
VAL   HG12 H N N 401 
VAL   HG13 H N N 402 
VAL   HG21 H N N 403 
VAL   HG22 H N N 404 
VAL   HG23 H N N 405 
VAL   HXT  H N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A47 N2  C10  sing N N 1   
A1A47 N2  S2   sing N N 2   
A1A47 C3  C2   sing N N 3   
A1A47 C3  C4   sing N N 4   
A1A47 C6  C11  sing Y N 5   
A1A47 C6  C7   doub Y N 6   
A1A47 C6  S1   sing N N 7   
A1A47 C9  C10  sing Y N 8   
A1A47 C9  C8   doub Y N 9   
A1A47 C1  C2   sing N N 10  
A1A47 C1  O1   doub N N 11  
A1A47 C1  O4   sing N N 12  
A1A47 C10 C11  doub Y N 13  
A1A47 C11 N3   sing N N 14  
A1A47 C2  N1   sing N N 15  
A1A47 C4  C5   sing N N 16  
A1A47 C5  N1   sing N N 17  
A1A47 C7  C8   sing Y N 18  
A1A47 N1  S1   sing N N 19  
A1A47 N3  S2   sing N N 20  
A1A47 O2  S1   doub N N 21  
A1A47 O3  S1   doub N N 22  
A1A47 N2  H11  sing N N 23  
A1A47 C3  H3   sing N N 24  
A1A47 C3  H2   sing N N 25  
A1A47 C9  H10  sing N N 26  
A1A47 C2  H1   sing N N 27  
A1A47 C4  H4   sing N N 28  
A1A47 C4  H5   sing N N 29  
A1A47 C5  H6   sing N N 30  
A1A47 C5  H7   sing N N 31  
A1A47 C7  H8   sing N N 32  
A1A47 C8  H9   sing N N 33  
A1A47 N3  H12  sing N N 34  
A1A47 O4  H13  sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   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                    7HCE 
_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]   0.025206 
_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 
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   ? 19.667 -16.315 22.274  0.50 38.99 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.697 -16.429 22.401  0.50 38.38 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.700 -15.235 22.434  0.50 38.54 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.756 -15.331 22.593  0.50 37.93 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.359 -13.892 22.149  0.50 36.55 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.415 -14.001 22.243  0.50 35.87 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.478 -13.633 22.594  0.50 36.77 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.536 -13.723 22.671  0.50 36.19 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.055 -15.263 23.836  0.50 39.64 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.191 -15.322 24.030  0.50 39.03 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.022 -14.151 23.976  0.50 39.91 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.240 -14.147 24.226  0.50 39.32 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.421 -16.620 24.099  0.50 39.91 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.485 -16.636 24.331  0.50 39.29 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.990 -15.349 21.787  0.50 46.27 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.008 -15.450 21.993  0.50 45.53 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.741 -15.119 24.506  0.50 47.59 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.920 -15.224 24.662  0.50 46.85 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.513 -14.295 24.790  0.50 47.91 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.739 -14.280 25.047  0.50 47.20 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.477 -13.296 24.021  0.50 47.91 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.754 -13.327 24.284  0.50 47.20 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.428 -14.173 23.209  0.50 47.91 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.630 -14.106 23.473  0.50 47.20 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.958 -16.593 24.950  0.50 47.91 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.105 -16.595 25.223  0.50 47.16 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.793 -16.817 23.386  0.50 47.91 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.780 -16.771 23.678  0.50 47.16 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.117 -17.295 24.121  0.50 47.91 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.128 -17.360 24.278  0.50 47.16 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.663 -13.043 21.394  0.50 34.04 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.719 -13.187 21.451  0.50 33.14 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.113 -11.687 21.111  0.50 31.25 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.156 -11.833 21.135  0.50 30.11 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.960 -10.719 21.357  0.50 28.78 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.997 -10.868 21.362  0.50 27.25 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.834 -11.123 21.668  0.50 28.39 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.873 -11.274 21.675  0.50 26.80 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.680 -11.563 19.689  0.50 30.68 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.720 -11.721 19.710  0.50 29.59 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.678 -11.945 18.621  0.50 29.92 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.709 -12.082 18.643  0.50 28.82 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.557 -11.439 18.596  0.50 29.59 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.635 -11.486 18.564  0.50 28.48 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.078 -12.847 17.730  0.50 29.89 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 19.060 -13.043 17.794  0.50 28.69 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.908 -13.237 21.026  0.50 40.87 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.973 -13.403 21.080  0.50 39.79 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.824 -11.463 21.725  0.50 37.52 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.866 -11.589 21.747  0.50 36.15 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.948 -10.642 19.534  0.50 36.83 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.999 -10.805 19.554  0.50 35.52 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.447 -12.149 19.604  0.50 36.83 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.476 -12.319 19.625  0.50 35.52 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.548 -13.097 17.100  0.50 35.89 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.524 -13.281 17.164  0.50 34.45 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.871 -13.178 17.780  0.50 35.89 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.825 -13.431 17.874  0.50 34.45 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.247 -9.426  21.210  0.50 26.34 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.276 -9.576  21.195  0.50 24.39 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.310 -8.369  21.568  0.50 24.25 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.344 -8.527  21.588  0.50 21.93 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.453 -7.898  20.397  0.50 21.93 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.420 -8.068  20.466  0.50 19.37 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.759 -6.885  20.527  0.50 22.56 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.601 -7.172  20.694  0.50 19.49 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.058 -7.176  22.168  0.50 24.88 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.110 -7.328  22.153  0.50 22.51 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 18.999 -6.654  21.248  0.50 25.20 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.959 -6.781  21.163  0.50 22.61 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.990 -9.133  20.893  0.50 31.63 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 19.011 -9.280  20.850  0.50 29.29 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.716 -8.704  22.255  0.50 29.12 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.782 -8.862  22.294  0.50 26.34 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.419 -6.479  22.392  0.50 29.87 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.481 -6.645  22.437  0.50 27.03 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.526 -7.463  22.968  0.50 29.87 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.644 -7.617  22.916  0.50 27.03 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.405 -5.999  21.589  0.50 30.26 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.540 -7.343  20.936  0.50 27.15 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.485 -8.591  19.263  0.50 18.69 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.505 -8.654  19.275  0.50 16.55 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.601 -8.238  18.159  0.50 16.15 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.608 -8.255  18.196  0.50 15.00 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.167 -8.623  18.506  0.50 16.10 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.172 -8.609  18.570  0.50 15.78 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.898 -9.761  18.899  0.50 17.55 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.905 -9.712  19.057  0.50 17.44 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.039 -8.948  16.881  0.50 14.92 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 16.004 -8.953  16.897  0.50 13.95 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.293 -8.381  16.270  0.50 14.25 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.273 -8.423  16.279  0.50 13.41 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.261 -7.174  15.589  0.50 14.26 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.282 -7.208  15.612  0.50 13.41 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.495 -9.060  16.362  0.50 14.83 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.448 -9.151  16.346  0.50 14.14 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.409 -6.651  15.019  0.50 14.36 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.443 -6.722  15.036  0.50 13.54 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.643 -8.544  15.794  0.50 15.08 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.610 -8.671  15.770  0.50 14.32 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.600 -7.340  15.120  0.50 14.83 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.606 -7.458  15.113  0.50 13.96 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.004 -9.258  19.108  0.50 22.45 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 17.051 -9.287  19.074  0.50 19.88 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.634 -7.283  18.011  0.50 19.41 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.664 -7.300  18.063  0.50 18.02 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.203 -9.884  17.084  0.50 17.93 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 16.137 -9.898  17.079  0.50 16.75 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.327 -8.877  16.225  0.50 17.93 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.288 -8.848  16.251  0.50 16.75 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.457 -6.710  15.517  0.50 17.13 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.497 -6.712  15.555  0.50 16.11 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.529 -9.873  16.815  0.50 17.82 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.458 -9.970  16.787  0.50 16.98 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.377 -5.839  14.566  0.50 17.25 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.437 -5.905  14.593  0.50 16.27 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.447 -9.007  15.866  0.50 18.11 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.397 -9.165  15.827  0.50 17.20 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.374 -6.990  14.742  0.50 17.82 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.390 -7.132  14.730  0.50 16.77 ?  6   PHE   A HZ   1 
ATOM   121  N N    . SER   A 1 7   ? 13.243 -7.674  18.353  1.00 15.32 ?  7   SER   A N    1 
ATOM   122  C CA   . SER   A 1 7   ? 11.862 -7.841  18.800  1.00 16.19 ?  7   SER   A CA   1 
ATOM   123  C C    . SER   A 1 7   ? 10.865 -7.515  17.693  1.00 14.54 ?  7   SER   A C    1 
ATOM   124  O O    . SER   A 1 7   ? 11.093 -6.615  16.884  1.00 14.94 ?  7   SER   A O    1 
ATOM   125  C CB   . SER   A 1 7   ? 11.592 -6.930  20.005  1.00 19.02 ?  7   SER   A CB   1 
ATOM   126  O OG   . SER   A 1 7   ? 10.234 -6.982  20.392  1.00 21.48 ?  7   SER   A OG   1 
ATOM   127  H H    A SER   A 1 7   ? 13.393 -6.911  17.982  0.50 18.40 ?  7   SER   A H    1 
ATOM   128  H H    B SER   A 1 7   ? 13.390 -6.928  17.948  0.50 18.40 ?  7   SER   A H    1 
ATOM   129  H HA   . SER   A 1 7   ? 11.714 -8.756  19.076  1.00 19.45 ?  7   SER   A HA   1 
ATOM   130  H HB2  . SER   A 1 7   ? 12.142 -7.222  20.752  1.00 22.84 ?  7   SER   A HB2  1 
ATOM   131  H HB3  . SER   A 1 7   ? 11.818 -6.016  19.771  1.00 22.84 ?  7   SER   A HB3  1 
ATOM   132  H HG   . SER   A 1 7   ? 10.100 -6.480  21.052  1.00 25.80 ?  7   SER   A HG   1 
ATOM   133  N N    A GLY   A 1 8   ? 9.767  -8.273  17.651  0.50 14.15 ?  8   GLY   A N    1 
ATOM   134  N N    B GLY   A 1 8   ? 9.736  -8.222  17.697  0.50 14.05 ?  8   GLY   A N    1 
ATOM   135  C CA   A GLY   A 1 8   ? 8.696  -8.002  16.711  0.50 13.96 ?  8   GLY   A CA   1 
ATOM   136  C CA   B GLY   A 1 8   ? 8.673  -7.934  16.757  0.50 13.69 ?  8   GLY   A CA   1 
ATOM   137  C C    A GLY   A 1 8   ? 8.909  -8.513  15.302  0.50 12.97 ?  8   GLY   A C    1 
ATOM   138  C C    B GLY   A 1 8   ? 8.889  -8.461  15.360  0.50 12.35 ?  8   GLY   A C    1 
ATOM   139  O O    A GLY   A 1 8   ? 8.223  -8.050  14.384  0.50 13.87 ?  8   GLY   A O    1 
ATOM   140  O O    B GLY   A 1 8   ? 8.131  -8.090  14.454  0.50 13.12 ?  8   GLY   A O    1 
ATOM   141  H H    A GLY   A 1 8   ? 9.623  -8.946  18.165  0.50 17.00 ?  8   GLY   A H    1 
ATOM   142  H H    B GLY   A 1 8   ? 9.564  -8.866  18.239  0.50 16.88 ?  8   GLY   A H    1 
ATOM   143  H HA2  A GLY   A 1 8   ? 7.872  -8.388  17.061  0.50 16.77 ?  8   GLY   A HA2  1 
ATOM   144  H HA2  B GLY   A 1 8   ? 7.848  -8.320  17.086  0.50 16.44 ?  8   GLY   A HA2  1 
ATOM   145  H HA3  A GLY   A 1 8   ? 8.565  -7.042  16.652  0.50 16.77 ?  8   GLY   A HA3  1 
ATOM   146  H HA3  B GLY   A 1 8   ? 8.552  -6.971  16.704  0.50 16.44 ?  8   GLY   A HA3  1 
ATOM   147  N N    A TYR   A 1 9   ? 9.835  -9.451  15.096  0.50 12.40 ?  9   TYR   A N    1 
ATOM   148  N N    B TYR   A 1 9   ? 9.888  -9.316  15.152  0.50 11.63 ?  9   TYR   A N    1 
ATOM   149  C CA   A TYR   A 1 9   ? 10.107 -9.994  13.770  0.50 11.56 ?  9   TYR   A CA   1 
ATOM   150  C CA   B TYR   A 1 9   ? 10.123 -9.878  13.833  0.50 10.97 ?  9   TYR   A CA   1 
ATOM   151  C C    A TYR   A 1 9   ? 9.273  -11.241 13.495  0.50 10.97 ?  9   TYR   A C    1 
ATOM   152  C C    B TYR   A 1 9   ? 9.186  -11.046 13.564  0.50 10.41 ?  9   TYR   A C    1 
ATOM   153  O O    A TYR   A 1 9   ? 9.077  -12.089 14.374  0.50 11.52 ?  9   TYR   A O    1 
ATOM   154  O O    B TYR   A 1 9   ? 8.755  -11.765 14.473  0.50 11.33 ?  9   TYR   A O    1 
ATOM   155  C CB   A TYR   A 1 9   ? 11.594 -10.341 13.617  0.50 11.81 ?  9   TYR   A CB   1 
ATOM   156  C CB   B TYR   A 1 9   ? 11.572 -10.357 13.681  0.50 11.22 ?  9   TYR   A CB   1 
ATOM   157  C CG   A TYR   A 1 9   ? 12.487 -9.129  13.443  0.50 11.62 ?  9   TYR   A CG   1 
ATOM   158  C CG   B TYR   A 1 9   ? 12.553 -9.220  13.573  0.50 10.63 ?  9   TYR   A CG   1 
ATOM   159  C CD1  A TYR   A 1 9   ? 12.785 -8.302  14.520  0.50 11.73 ?  9   TYR   A CD1  1 
ATOM   160  C CD1  B TYR   A 1 9   ? 12.898 -8.477  14.691  0.50 10.83 ?  9   TYR   A CD1  1 
ATOM   161  C CD2  A TYR   A 1 9   ? 13.018 -8.804  12.202  0.50 11.46 ?  9   TYR   A CD2  1 
ATOM   162  C CD2  B TYR   A 1 9   ? 13.112 -8.868  12.353  0.50 10.61 ?  9   TYR   A CD2  1 
ATOM   163  C CE1  A TYR   A 1 9   ? 13.584 -7.181  14.368  0.50 11.37 ?  9   TYR   A CE1  1 
ATOM   164  C CE1  B TYR   A 1 9   ? 13.770 -7.418  14.603  0.50 10.84 ?  9   TYR   A CE1  1 
ATOM   165  C CE2  A TYR   A 1 9   ? 13.817 -7.685  12.038  0.50 10.80 ?  9   TYR   A CE2  1 
ATOM   166  C CE2  B TYR   A 1 9   ? 13.985 -7.806  12.252  0.50 10.70 ?  9   TYR   A CE2  1 
ATOM   167  C CZ   A TYR   A 1 9   ? 14.097 -6.878  13.125  0.50 10.54 ?  9   TYR   A CZ   1 
ATOM   168  C CZ   B TYR   A 1 9   ? 14.311 -7.087  13.381  0.50 11.12 ?  9   TYR   A CZ   1 
ATOM   169  O OH   A TYR   A 1 9   ? 14.886 -5.765  12.964  0.50 10.37 ?  9   TYR   A OH   1 
ATOM   170  O OH   B TYR   A 1 9   ? 15.185 -6.036  13.288  0.50 12.20 ?  9   TYR   A OH   1 
ATOM   171  H H    A TYR   A 1 9   ? 10.327 -9.786  15.715  0.50 14.89 ?  9   TYR   A H    1 
ATOM   172  H H    B TYR   A 1 9   ? 10.438 -9.587  15.760  0.50 13.97 ?  9   TYR   A H    1 
ATOM   173  H HA   A TYR   A 1 9   ? 9.885  -9.326  13.102  0.50 13.90 ?  9   TYR   A HA   1 
ATOM   174  H HA   B TYR   A 1 9   ? 9.965  -9.190  13.162  0.50 13.18 ?  9   TYR   A HA   1 
ATOM   175  H HB2  A TYR   A 1 9   ? 11.887 -10.822 14.407  0.50 14.20 ?  9   TYR   A HB2  1 
ATOM   176  H HB2  B TYR   A 1 9   ? 11.816 -10.894 14.450  0.50 13.48 ?  9   TYR   A HB2  1 
ATOM   177  H HB3  A TYR   A 1 9   ? 11.695 -10.902 12.833  0.50 14.20 ?  9   TYR   A HB3  1 
ATOM   178  H HB3  B TYR   A 1 9   ? 11.638 -10.888 12.870  0.50 13.48 ?  9   TYR   A HB3  1 
ATOM   179  H HD1  A TYR   A 1 9   ? 12.429 -8.505  15.358  0.50 14.09 ?  9   TYR   A HD1  1 
ATOM   180  H HD1  B TYR   A 1 9   ? 12.521 -8.699  15.513  0.50 13.02 ?  9   TYR   A HD1  1 
ATOM   181  H HD2  A TYR   A 1 9   ? 12.830 -9.341  11.467  0.50 13.78 ?  9   TYR   A HD2  1 
ATOM   182  H HD2  B TYR   A 1 9   ? 12.892 -9.349  11.587  0.50 12.75 ?  9   TYR   A HD2  1 
ATOM   183  H HE1  A TYR   A 1 9   ? 13.773 -6.641  15.103  0.50 13.66 ?  9   TYR   A HE1  1 
ATOM   184  H HE1  B TYR   A 1 9   ? 13.988 -6.934  15.365  0.50 13.03 ?  9   TYR   A HE1  1 
ATOM   185  H HE2  A TYR   A 1 9   ? 14.176 -7.479  11.203  0.50 12.98 ?  9   TYR   A HE2  1 
ATOM   186  H HE2  B TYR   A 1 9   ? 14.364 -7.580  11.432  0.50 12.86 ?  9   TYR   A HE2  1 
ATOM   187  H HH   A TYR   A 1 9   ? 14.991 -5.373  13.705  0.50 12.46 ?  9   TYR   A HH   1 
ATOM   188  H HH   B TYR   A 1 9   ? 15.290 -5.691  14.048  0.50 14.66 ?  9   TYR   A HH   1 
ATOM   189  N N    A LEU   A 1 10  ? 8.806  -11.353 12.254  0.50 10.46 ?  10  LEU   A N    1 
ATOM   190  N N    B LEU   A 1 10  ? 8.873  -11.223 12.288  0.50 10.36 ?  10  LEU   A N    1 
ATOM   191  C CA   A LEU   A 1 10  ? 8.244  -12.597 11.748  0.50 10.39 ?  10  LEU   A CA   1 
ATOM   192  C CA   B LEU   A 1 10  ? 8.211  -12.421 11.807  0.50 10.02 ?  10  LEU   A CA   1 
ATOM   193  C C    A LEU   A 1 10  ? 9.386  -13.505 11.299  0.50 9.72  ?  10  LEU   A C    1 
ATOM   194  C C    B LEU   A 1 10  ? 9.286  -13.391 11.331  0.50 9.34  ?  10  LEU   A C    1 
ATOM   195  O O    A LEU   A 1 10  ? 10.394 -13.033 10.762  0.50 9.62  ?  10  LEU   A O    1 
ATOM   196  O O    B LEU   A 1 10  ? 10.104 -13.048 10.466  0.50 9.19  ?  10  LEU   A O    1 
ATOM   197  C CB   A LEU   A 1 10  ? 7.332  -12.289 10.559  0.50 11.68 ?  10  LEU   A CB   1 
ATOM   198  C CB   B LEU   A 1 10  ? 7.256  -12.073 10.668  0.50 10.58 ?  10  LEU   A CB   1 
ATOM   199  C CG   A LEU   A 1 10  ? 6.645  -13.467 9.869   0.50 13.63 ?  10  LEU   A CG   1 
ATOM   200  C CG   B LEU   A 1 10  ? 6.476  -13.274 10.138  0.50 11.83 ?  10  LEU   A CG   1 
ATOM   201  C CD1  A LEU   A 1 10  ? 5.546  -14.043 10.744  0.50 14.54 ?  10  LEU   A CD1  1 
ATOM   202  C CD1  B LEU   A 1 10  ? 5.594  -13.866 11.225  0.50 13.38 ?  10  LEU   A CD1  1 
ATOM   203  C CD2  A LEU   A 1 10  ? 6.099  -13.038 8.518   0.50 14.33 ?  10  LEU   A CD2  1 
ATOM   204  C CD2  B LEU   A 1 10  ? 5.658  -12.887 8.925   0.50 13.96 ?  10  LEU   A CD2  1 
ATOM   205  H H    A LEU   A 1 10  ? 8.814  -10.715 11.668  0.50 12.58 ?  10  LEU   A H    1 
ATOM   206  H H    B LEU   A 1 10  ? 9.040  -10.645 11.673  0.50 12.45 ?  10  LEU   A H    1 
ATOM   207  H HA   A LEU   A 1 10  ? 7.725  -13.038 12.444  0.50 12.49 ?  10  LEU   A HA   1 
ATOM   208  H HA   B LEU   A 1 10  ? 7.708  -12.826 12.529  0.50 12.05 ?  10  LEU   A HA   1 
ATOM   209  H HB2  A LEU   A 1 10  ? 6.627  -11.695 10.862  0.50 14.03 ?  10  LEU   A HB2  1 
ATOM   210  H HB2  B LEU   A 1 10  ? 6.609  -11.417 10.982  0.50 12.72 ?  10  LEU   A HB2  1 
ATOM   211  H HB3  A LEU   A 1 10  ? 7.860  -11.838 9.884   0.50 14.03 ?  10  LEU   A HB3  1 
ATOM   212  H HB3  B LEU   A 1 10  ? 7.765  -11.700 9.931   0.50 12.72 ?  10  LEU   A HB3  1 
ATOM   213  H HG   A LEU   A 1 10  ? 7.298  -14.171 9.714   0.50 16.37 ?  10  LEU   A HG   1 
ATOM   214  H HG   B LEU   A 1 10  ? 7.108  -13.960 9.864   0.50 14.21 ?  10  LEU   A HG   1 
ATOM   215  H HD11 A LEU   A 1 10  ? 5.164  -14.821 10.305  0.50 17.47 ?  10  LEU   A HD11 1 
ATOM   216  H HD11 B LEU   A 1 10  ? 4.983  -14.501 10.821  0.50 16.07 ?  10  LEU   A HD11 1 
ATOM   217  H HD12 A LEU   A 1 10  ? 5.924  -14.301 11.600  0.50 17.47 ?  10  LEU   A HD12 1 
ATOM   218  H HD12 B LEU   A 1 10  ? 6.152  -14.318 11.879  0.50 16.07 ?  10  LEU   A HD12 1 
ATOM   219  H HD13 A LEU   A 1 10  ? 4.862  -13.369 10.876  0.50 17.47 ?  10  LEU   A HD13 1 
ATOM   220  H HD13 B LEU   A 1 10  ? 5.096  -13.152 11.651  0.50 16.07 ?  10  LEU   A HD13 1 
ATOM   221  H HD21 A LEU   A 1 10  ? 5.660  -13.796 8.102   0.50 17.21 ?  10  LEU   A HD21 1 
ATOM   222  H HD21 B LEU   A 1 10  ? 5.181  -13.668 8.607   0.50 16.77 ?  10  LEU   A HD21 1 
ATOM   223  H HD22 A LEU   A 1 10  ? 5.465  -12.319 8.652   0.50 17.21 ?  10  LEU   A HD22 1 
ATOM   224  H HD22 B LEU   A 1 10  ? 5.030  -12.194 9.180   0.50 16.77 ?  10  LEU   A HD22 1 
ATOM   225  H HD23 A LEU   A 1 10  ? 6.835  -12.736 7.965   0.50 17.21 ?  10  LEU   A HD23 1 
ATOM   226  H HD23 B LEU   A 1 10  ? 6.255  -12.557 8.236   0.50 16.77 ?  10  LEU   A HD23 1 
ATOM   227  N N    A LYS   A 1 11  ? 9.222  -14.814 11.508  0.50 9.59  ?  11  LYS   A N    1 
ATOM   228  N N    B LYS   A 1 11  ? 9.297  -14.584 11.912  0.50 9.02  ?  11  LYS   A N    1 
ATOM   229  C CA   A LYS   A 1 11  ? 10.252 -15.804 11.205  0.50 9.45  ?  11  LYS   A CA   1 
ATOM   230  C CA   B LYS   A 1 11  ? 10.225 -15.622 11.495  0.50 9.34  ?  11  LYS   A CA   1 
ATOM   231  C C    A LYS   A 1 11  ? 9.927  -16.443 9.859   0.50 9.64  ?  11  LYS   A C    1 
ATOM   232  C C    B LYS   A 1 11  ? 9.817  -16.131 10.120  0.50 8.72  ?  11  LYS   A C    1 
ATOM   233  O O    A LYS   A 1 11  ? 8.924  -17.148 9.734   0.50 10.78 ?  11  LYS   A O    1 
ATOM   234  O O    B LYS   A 1 11  ? 8.680  -16.580 9.932   0.50 9.29  ?  11  LYS   A O    1 
ATOM   235  C CB   A LYS   A 1 11  ? 10.308 -16.852 12.320  0.50 9.88  ?  11  LYS   A CB   1 
ATOM   236  C CB   B LYS   A 1 11  ? 10.207 -16.749 12.526  0.50 9.97  ?  11  LYS   A CB   1 
ATOM   237  C CG   A LYS   A 1 11  ? 11.326 -17.973 12.123  0.50 10.13 ?  11  LYS   A CG   1 
ATOM   238  C CG   B LYS   A 1 11  ? 11.241 -17.838 12.304  0.50 10.36 ?  11  LYS   A CG   1 
ATOM   239  C CD   A LYS   A 1 11  ? 11.433 -18.813 13.402  0.50 10.63 ?  11  LYS   A CD   1 
ATOM   240  C CD   B LYS   A 1 11  ? 11.281 -18.783 13.506  0.50 10.92 ?  11  LYS   A CD   1 
ATOM   241  C CE   A LYS   A 1 11  ? 12.402 -19.979 13.265  0.50 10.56 ?  11  LYS   A CE   1 
ATOM   242  C CE   B LYS   A 1 11  ? 12.323 -19.883 13.354  0.50 10.62 ?  11  LYS   A CE   1 
ATOM   243  N NZ   A LYS   A 1 11  ? 13.779 -19.546 12.910  0.50 10.37 ?  11  LYS   A NZ   1 
ATOM   244  N NZ   B LYS   A 1 11  ? 13.699 -19.340 13.220  0.50 10.02 ?  11  LYS   A NZ   1 
ATOM   245  H H    A LYS   A 1 11  ? 8.495  -15.161 11.823  0.50 11.52 ?  11  LYS   A H    1 
ATOM   246  H H    B LYS   A 1 11  ? 8.766  -14.813 12.550  0.50 10.84 ?  11  LYS   A H    1 
ATOM   247  H HA   A LYS   A 1 11  ? 11.114 -15.369 11.145  0.50 11.36 ?  11  LYS   A HA   1 
ATOM   248  H HA   B LYS   A 1 11  ? 11.117 -15.252 11.438  0.50 11.23 ?  11  LYS   A HA   1 
ATOM   249  H HB2  A LYS   A 1 11  ? 10.535 -16.401 13.151  0.50 11.88 ?  11  LYS   A HB2  1 
ATOM   250  H HB2  B LYS   A 1 11  ? 10.372 -16.358 13.400  0.50 11.98 ?  11  LYS   A HB2  1 
ATOM   251  H HB3  A LYS   A 1 11  ? 9.435  -17.261 12.404  0.50 11.88 ?  11  LYS   A HB3  1 
ATOM   252  H HB3  B LYS   A 1 11  ? 9.331  -17.159 12.514  0.50 11.98 ?  11  LYS   A HB3  1 
ATOM   253  H HG2  A LYS   A 1 11  ? 11.033 -18.554 11.402  0.50 12.18 ?  11  LYS   A HG2  1 
ATOM   254  H HG2  B LYS   A 1 11  ? 11.000 -18.351 11.516  0.50 12.46 ?  11  LYS   A HG2  1 
ATOM   255  H HG3  A LYS   A 1 11  ? 12.196 -17.599 11.930  0.50 12.18 ?  11  LYS   A HG3  1 
ATOM   256  H HG3  B LYS   A 1 11  ? 12.115 -17.437 12.196  0.50 12.46 ?  11  LYS   A HG3  1 
ATOM   257  H HD2  A LYS   A 1 11  ? 11.741 -18.248 14.126  0.50 12.78 ?  11  LYS   A HD2  1 
ATOM   258  H HD2  B LYS   A 1 11  ? 11.494 -18.272 14.301  0.50 13.13 ?  11  LYS   A HD2  1 
ATOM   259  H HD3  A LYS   A 1 11  ? 10.556 -19.175 13.617  0.50 12.78 ?  11  LYS   A HD3  1 
ATOM   260  H HD3  B LYS   A 1 11  ? 10.411 -19.203 13.605  0.50 13.13 ?  11  LYS   A HD3  1 
ATOM   261  H HE2  A LYS   A 1 11  ? 12.444 -20.453 14.112  0.50 12.69 ?  11  LYS   A HE2  1 
ATOM   262  H HE2  B LYS   A 1 11  ? 12.301 -20.453 14.140  0.50 12.77 ?  11  LYS   A HE2  1 
ATOM   263  H HE3  A LYS   A 1 11  ? 12.082 -20.573 12.569  0.50 12.69 ?  11  LYS   A HE3  1 
ATOM   264  H HE3  B LYS   A 1 11  ? 12.126 -20.404 12.560  0.50 12.77 ?  11  LYS   A HE3  1 
ATOM   265  H HZ1  A LYS   A 1 11  ? 14.313 -20.258 12.848  0.50 12.46 ?  11  LYS   A HZ1  1 
ATOM   266  H HZ1  B LYS   A 1 11  ? 14.276 -20.003 13.084  0.50 12.05 ?  11  LYS   A HZ1  1 
ATOM   267  H HZ2  A LYS   A 1 11  ? 13.772 -19.122 12.129  0.50 12.46 ?  11  LYS   A HZ2  1 
ATOM   268  H HZ2  B LYS   A 1 11  ? 13.738 -18.777 12.531  0.50 12.05 ?  11  LYS   A HZ2  1 
ATOM   269  H HZ3  A LYS   A 1 11  ? 14.098 -19.000 13.535  0.50 12.46 ?  11  LYS   A HZ3  1 
ATOM   270  H HZ3  B LYS   A 1 11  ? 13.928 -18.904 13.961  0.50 12.05 ?  11  LYS   A HZ3  1 
ATOM   271  N N    A LEU   A 1 12  ? 10.775 -16.214 8.855   0.50 8.73  ?  12  LEU   A N    1 
ATOM   272  N N    B LEU   A 1 12  ? 10.721 -16.035 9.146   0.50 8.71  ?  12  LEU   A N    1 
ATOM   273  C CA   A LEU   A 1 12  ? 10.532 -16.809 7.543   0.50 8.92  ?  12  LEU   A CA   1 
ATOM   274  C CA   B LEU   A 1 12  ? 10.465 -16.567 7.812   0.50 9.21  ?  12  LEU   A CA   1 
ATOM   275  C C    A LEU   A 1 12  ? 11.130 -18.205 7.413   0.50 9.28  ?  12  LEU   A C    1 
ATOM   276  C C    B LEU   A 1 12  ? 11.040 -17.960 7.612   0.50 9.33  ?  12  LEU   A C    1 
ATOM   277  O O    A LEU   A 1 12  ? 10.501 -19.092 6.826   0.50 9.88  ?  12  LEU   A O    1 
ATOM   278  O O    B LEU   A 1 12  ? 10.386 -18.815 7.005   0.50 9.43  ?  12  LEU   A O    1 
ATOM   279  C CB   A LEU   A 1 12  ? 11.084 -15.912 6.429   0.50 9.05  ?  12  LEU   A CB   1 
ATOM   280  C CB   B LEU   A 1 12  ? 11.033 -15.630 6.740   0.50 9.61  ?  12  LEU   A CB   1 
ATOM   281  C CG   A LEU   A 1 12  ? 10.423 -14.544 6.250   0.50 10.00 ?  12  LEU   A CG   1 
ATOM   282  C CG   B LEU   A 1 12  ? 10.381 -14.252 6.652   0.50 9.55  ?  12  LEU   A CG   1 
ATOM   283  C CD1  A LEU   A 1 12  ? 11.173 -13.732 5.215   0.50 10.60 ?  12  LEU   A CD1  1 
ATOM   284  C CD1  B LEU   A 1 12  ? 11.042 -13.432 5.560   0.50 10.39 ?  12  LEU   A CD1  1 
ATOM   285  C CD2  A LEU   A 1 12  ? 8.963  -14.697 5.841   0.50 10.71 ?  12  LEU   A CD2  1 
ATOM   286  C CD2  B LEU   A 1 12  ? 8.896  -14.386 6.398   0.50 9.64  ?  12  LEU   A CD2  1 
ATOM   287  H H    A LEU   A 1 12  ? 11.484 -15.723 8.906   0.50 10.50 ?  12  LEU   A H    1 
ATOM   288  H H    B LEU   A 1 12  ? 11.488 -15.646 9.228   0.50 10.48 ?  12  LEU   A H    1 
ATOM   289  H HA   A LEU   A 1 12  ? 9.574  -16.888 7.418   0.50 10.72 ?  12  LEU   A HA   1 
ATOM   290  H HA   B LEU   A 1 12  ? 9.504  -16.621 7.676   0.50 11.08 ?  12  LEU   A HA   1 
ATOM   291  H HB2  A LEU   A 1 12  ? 12.021 -15.758 6.606   0.50 10.87 ?  12  LEU   A HB2  1 
ATOM   292  H HB2  B LEU   A 1 12  ? 11.974 -15.491 6.920   0.50 11.55 ?  12  LEU   A HB2  1 
ATOM   293  H HB3  A LEU   A 1 12  ? 10.988 -16.391 5.591   0.50 10.87 ?  12  LEU   A HB3  1 
ATOM   294  H HB3  B LEU   A 1 12  ? 10.927 -16.053 5.873   0.50 11.55 ?  12  LEU   A HB3  1 
ATOM   295  H HG   A LEU   A 1 12  ? 10.448 -14.065 7.091   0.50 12.02 ?  12  LEU   A HG   1 
ATOM   296  H HG   B LEU   A 1 12  ? 10.501 -13.786 7.494   0.50 11.48 ?  12  LEU   A HG   1 
ATOM   297  H HD11 A LEU   A 1 12  ? 10.738 -12.871 5.115   0.50 12.74 ?  12  LEU   A HD11 1 
ATOM   298  H HD11 B LEU   A 1 12  ? 10.621 -12.559 5.519   0.50 12.48 ?  12  LEU   A HD11 1 
ATOM   299  H HD12 A LEU   A 1 12  ? 12.086 -13.610 5.516   0.50 12.74 ?  12  LEU   A HD12 1 
ATOM   300  H HD12 B LEU   A 1 12  ? 11.985 -13.336 5.766   0.50 12.48 ?  12  LEU   A HD12 1 
ATOM   301  H HD13 A LEU   A 1 12  ? 11.162 -14.210 4.371   0.50 12.74 ?  12  LEU   A HD13 1 
ATOM   302  H HD13 B LEU   A 1 12  ? 10.934 -13.891 4.711   0.50 12.48 ?  12  LEU   A HD13 1 
ATOM   303  H HD21 A LEU   A 1 12  ? 8.589  -13.821 5.660   0.50 12.88 ?  12  LEU   A HD21 1 
ATOM   304  H HD21 B LEU   A 1 12  ? 8.538  -13.527 6.127   0.50 11.58 ?  12  LEU   A HD21 1 
ATOM   305  H HD22 A LEU   A 1 12  ? 8.911  -15.248 5.044   0.50 12.88 ?  12  LEU   A HD22 1 
ATOM   306  H HD22 B LEU   A 1 12  ? 8.753  -15.040 5.694   0.50 11.58 ?  12  LEU   A HD22 1 
ATOM   307  H HD23 A LEU   A 1 12  ? 8.470  -15.121 6.564   0.50 12.88 ?  12  LEU   A HD23 1 
ATOM   308  H HD23 B LEU   A 1 12  ? 8.459  -14.683 7.213   0.50 11.58 ?  12  LEU   A HD23 1 
ATOM   309  N N    A THR   A 1 13  ? 12.336 -18.409 7.935   0.50 9.36  ?  13  THR   A N    1 
ATOM   310  N N    B THR   A 1 13  ? 12.260 -18.191 8.087   0.50 9.54  ?  13  THR   A N    1 
ATOM   311  C CA   A THR   A 1 13  ? 13.036 -19.683 7.834   0.50 9.83  ?  13  THR   A CA   1 
ATOM   312  C CA   B THR   A 1 13  ? 12.921 -19.485 8.000   0.50 9.78  ?  13  THR   A CA   1 
ATOM   313  C C    A THR   A 1 13  ? 13.832 -19.899 9.117   0.50 9.88  ?  13  THR   A C    1 
ATOM   314  C C    B THR   A 1 13  ? 13.672 -19.724 9.303   0.50 10.08 ?  13  THR   A C    1 
ATOM   315  O O    A THR   A 1 13  ? 13.744 -19.117 10.069  0.50 9.65  ?  13  THR   A O    1 
ATOM   316  O O    B THR   A 1 13  ? 13.591 -18.938 10.253  0.50 10.38 ?  13  THR   A O    1 
ATOM   317  C CB   A THR   A 1 13  ? 13.982 -19.718 6.626   0.50 10.59 ?  13  THR   A CB   1 
ATOM   318  C CB   B THR   A 1 13  ? 13.907 -19.546 6.825   0.50 10.58 ?  13  THR   A CB   1 
ATOM   319  O OG1  A THR   A 1 13  ? 15.102 -18.868 6.889   0.50 10.55 ?  13  THR   A OG1  1 
ATOM   320  O OG1  B THR   A 1 13  ? 14.933 -18.575 7.030   0.50 10.20 ?  13  THR   A OG1  1 
ATOM   321  C CG2  A THR   A 1 13  ? 13.292 -19.253 5.351   0.50 12.06 ?  13  THR   A CG2  1 
ATOM   322  C CG2  B THR   A 1 13  ? 13.216 -19.309 5.488   0.50 11.87 ?  13  THR   A CG2  1 
ATOM   323  H H    A THR   A 1 13  ? 12.783 -17.809 8.359   0.50 11.25 ?  13  THR   A H    1 
ATOM   324  H H    B THR   A 1 13  ? 12.740 -17.583 8.459   0.50 11.47 ?  13  THR   A H    1 
ATOM   325  H HA   A THR   A 1 13  ? 12.391 -20.407 7.742   0.50 11.82 ?  13  THR   A HA   1 
ATOM   326  H HA   B THR   A 1 13  ? 12.260 -20.182 7.888   0.50 11.76 ?  13  THR   A HA   1 
ATOM   327  H HB   A THR   A 1 13  ? 14.294 -20.629 6.489   0.50 12.73 ?  13  THR   A HB   1 
ATOM   328  H HB   B THR   A 1 13  ? 14.317 -20.419 6.800   0.50 12.71 ?  13  THR   A HB   1 
ATOM   329  H HG1  A THR   A 1 13  ? 15.634 -18.883 6.234   0.50 12.68 ?  13  THR   A HG1  1 
ATOM   330  H HG1  B THR   A 1 13  ? 15.478 -18.583 6.385   0.50 12.26 ?  13  THR   A HG1  1 
ATOM   331  H HG21 A THR   A 1 13  ? 13.860 -19.442 4.584   0.50 14.49 ?  13  THR   A HG21 1 
ATOM   332  H HG21 B THR   A 1 13  ? 13.864 -19.384 4.765   0.50 14.26 ?  13  THR   A HG21 1 
ATOM   333  H HG22 A THR   A 1 13  ? 12.451 -19.719 5.241   0.50 14.49 ?  13  THR   A HG22 1 
ATOM   334  H HG22 B THR   A 1 13  ? 12.524 -19.975 5.354   0.50 14.26 ?  13  THR   A HG22 1 
ATOM   335  H HG23 A THR   A 1 13  ? 13.127 -18.300 5.393   0.50 14.49 ?  13  THR   A HG23 1 
ATOM   336  H HG23 B THR   A 1 13  ? 12.820 -18.428 5.465   0.50 14.26 ?  13  THR   A HG23 1 
ATOM   337  N N    A ASP   A 1 14  ? 14.654 -20.950 9.121   0.50 10.41 ?  14  ASP   A N    1 
ATOM   338  N N    B ASP   A 1 14  ? 14.449 -20.805 9.325   0.50 10.20 ?  14  ASP   A N    1 
ATOM   339  C CA   A ASP   A 1 14  ? 15.488 -21.243 10.282  0.50 10.82 ?  14  ASP   A CA   1 
ATOM   340  C CA   B ASP   A 1 14  ? 15.319 -21.070 10.461  0.50 11.21 ?  14  ASP   A CA   1 
ATOM   341  C C    A ASP   A 1 14  ? 16.326 -20.042 10.717  0.50 10.37 ?  14  ASP   A C    1 
ATOM   342  C C    B ASP   A 1 14  ? 16.172 -19.856 10.795  0.50 10.54 ?  14  ASP   A C    1 
ATOM   343  O O    A ASP   A 1 14  ? 16.616 -19.890 11.910  0.50 10.42 ?  14  ASP   A O    1 
ATOM   344  O O    B ASP   A 1 14  ? 16.342 -19.523 11.975  0.50 11.14 ?  14  ASP   A O    1 
ATOM   345  C CB   A ASP   A 1 14  ? 16.395 -22.436 9.967   0.50 12.79 ?  14  ASP   A CB   1 
ATOM   346  C CB   B ASP   A 1 14  ? 16.222 -22.265 10.166  0.50 13.31 ?  14  ASP   A CB   1 
ATOM   347  C CG   A ASP   A 1 14  ? 17.226 -22.874 11.159  0.50 15.59 ?  14  ASP   A CG   1 
ATOM   348  C CG   B ASP   A 1 14  ? 17.254 -22.482 11.250  0.50 16.01 ?  14  ASP   A CG   1 
ATOM   349  O OD1  A ASP   A 1 14  ? 16.622 -23.280 12.176  0.50 16.59 ?  14  ASP   A OD1  1 
ATOM   350  O OD1  B ASP   A 1 14  ? 16.865 -22.878 12.366  0.50 17.24 ?  14  ASP   A OD1  1 
ATOM   351  O OD2  A ASP   A 1 14  ? 18.470 -22.839 11.074  0.50 17.29 -1 14  ASP   A OD2  1 
ATOM   352  O OD2  B ASP   A 1 14  ? 18.448 -22.219 10.988  0.50 16.83 -1 14  ASP   A OD2  1 
ATOM   353  H H    A ASP   A 1 14  ? 14.747 -21.503 8.463   0.50 12.52 ?  14  ASP   A H    1 
ATOM   354  H H    B ASP   A 1 14  ? 14.494 -21.379 8.699   0.50 12.26 ?  14  ASP   A H    1 
ATOM   355  H HA   A ASP   A 1 14  ? 14.919 -21.489 11.021  0.50 13.01 ?  14  ASP   A HA   1 
ATOM   356  H HA   B ASP   A 1 14  ? 14.775 -21.275 11.238  0.50 13.47 ?  14  ASP   A HA   1 
ATOM   357  H HB2  A ASP   A 1 14  ? 15.839 -23.201 9.737   0.50 15.37 ?  14  ASP   A HB2  1 
ATOM   358  H HB2  B ASP   A 1 14  ? 15.661 -23.056 10.060  0.50 15.99 ?  14  ASP   A HB2  1 
ATOM   359  H HB3  A ASP   A 1 14  ? 16.969 -22.211 9.219   0.50 15.37 ?  14  ASP   A HB3  1 
ATOM   360  H HB3  B ASP   A 1 14  ? 16.715 -22.099 9.355   0.50 15.99 ?  14  ASP   A HB3  1 
ATOM   361  N N    . ASN   A 1 15  ? 16.717 -19.175 9.774   1.00 10.31 ?  15  ASN   A N    1 
ATOM   362  C CA   . ASN   A 1 15  ? 17.708 -18.133 10.022  1.00 10.71 ?  15  ASN   A CA   1 
ATOM   363  C C    . ASN   A 1 15  ? 17.338 -16.741 9.534   1.00 10.96 ?  15  ASN   A C    1 
ATOM   364  O O    . ASN   A 1 15  ? 18.119 -15.818 9.777   1.00 12.46 ?  15  ASN   A O    1 
ATOM   365  C CB   . ASN   A 1 15  ? 19.076 -18.524 9.429   1.00 10.74 ?  15  ASN   A CB   1 
ATOM   366  C CG   . ASN   A 1 15  ? 19.056 -18.608 7.919   1.00 10.74 ?  15  ASN   A CG   1 
ATOM   367  O OD1  . ASN   A 1 15  ? 18.322 -19.414 7.339   1.00 11.64 ?  15  ASN   A OD1  1 
ATOM   368  N ND2  . ASN   A 1 15  ? 19.852 -17.769 7.269   1.00 11.20 ?  15  ASN   A ND2  1 
ATOM   369  H H    A ASN   A 1 15  ? 16.409 -19.173 8.972   0.50 12.39 ?  15  ASN   A H    1 
ATOM   370  H H    B ASN   A 1 15  ? 16.530 -19.305 8.945   0.50 12.39 ?  15  ASN   A H    1 
ATOM   371  H HA   . ASN   A 1 15  ? 17.838 -18.063 10.978  1.00 12.87 ?  15  ASN   A HA   1 
ATOM   372  H HB2  . ASN   A 1 15  ? 19.735 -17.853 9.686   1.00 12.91 ?  15  ASN   A HB2  1 
ATOM   373  H HB3  . ASN   A 1 15  ? 19.341 -19.390 9.774   1.00 12.91 ?  15  ASN   A HB3  1 
ATOM   374  H HD21 . ASN   A 1 15  ? 19.875 -17.774 6.410   1.00 13.46 ?  15  ASN   A HD21 1 
ATOM   375  H HD22 . ASN   A 1 15  ? 20.353 -17.214 7.705   1.00 13.46 ?  15  ASN   A HD22 1 
ATOM   376  N N    . VAL   A 1 16  ? 16.196 -16.554 8.868   1.00 10.23 ?  16  VAL   A N    1 
ATOM   377  C CA   . VAL   A 1 16  ? 15.805 -15.266 8.306   1.00 10.13 ?  16  VAL   A CA   1 
ATOM   378  C C    . VAL   A 1 16  ? 14.529 -14.772 8.984   1.00 9.55  ?  16  VAL   A C    1 
ATOM   379  O O    . VAL   A 1 16  ? 13.530 -15.502 9.066   1.00 9.78  ?  16  VAL   A O    1 
ATOM   380  C CB   . VAL   A 1 16  ? 15.627 -15.327 6.778   1.00 10.52 ?  16  VAL   A CB   1 
ATOM   381  C CG1  . VAL   A 1 16  ? 15.197 -13.963 6.230   1.00 11.32 ?  16  VAL   A CG1  1 
ATOM   382  C CG2  . VAL   A 1 16  ? 16.903 -15.804 6.093   1.00 11.52 ?  16  VAL   A CG2  1 
ATOM   383  H H    . VAL   A 1 16  ? 15.616 -17.177 8.732   1.00 12.29 ?  16  VAL   A H    1 
ATOM   384  H HA   . VAL   A 1 16  ? 16.507 -14.621 8.491   1.00 12.17 ?  16  VAL   A HA   1 
ATOM   385  H HB   . VAL   A 1 16  ? 14.926 -15.960 6.571   1.00 12.64 ?  16  VAL   A HB   1 
ATOM   386  H HG11 . VAL   A 1 16  ? 15.286 -13.971 5.263   1.00 13.60 ?  16  VAL   A HG11 1 
ATOM   387  H HG12 . VAL   A 1 16  ? 14.270 -13.803 6.471   1.00 13.60 ?  16  VAL   A HG12 1 
ATOM   388  H HG13 . VAL   A 1 16  ? 15.763 -13.275 6.609   1.00 13.60 ?  16  VAL   A HG13 1 
ATOM   389  H HG21 . VAL   A 1 16  ? 16.780 -15.772 5.130   1.00 13.84 ?  16  VAL   A HG21 1 
ATOM   390  H HG22 . VAL   A 1 16  ? 17.640 -15.225 6.348   1.00 13.84 ?  16  VAL   A HG22 1 
ATOM   391  H HG23 . VAL   A 1 16  ? 17.090 -16.714 6.370   1.00 13.84 ?  16  VAL   A HG23 1 
ATOM   392  N N    A TYR   A 1 17  ? 14.573 -13.523 9.424   0.50 9.26  ?  17  TYR   A N    1 
ATOM   393  N N    B TYR   A 1 17  ? 14.561 -13.506 9.429   0.50 9.43  ?  17  TYR   A N    1 
ATOM   394  C CA   A TYR   A 1 17  ? 13.496 -12.857 10.126  0.50 9.02  ?  17  TYR   A CA   1 
ATOM   395  C CA   B TYR   A 1 17  ? 13.485 -12.830 10.150  0.50 9.32  ?  17  TYR   A CA   1 
ATOM   396  C C    A TYR   A 1 17  ? 13.228 -11.535 9.409   0.50 9.35  ?  17  TYR   A C    1 
ATOM   397  C C    B TYR   A 1 17  ? 13.225 -11.479 9.497   0.50 9.48  ?  17  TYR   A C    1 
ATOM   398  O O    A TYR   A 1 17  ? 14.115 -10.999 8.742   0.50 9.38  ?  17  TYR   A O    1 
ATOM   399  O O    B TYR   A 1 17  ? 14.150 -10.860 8.970   0.50 9.63  ?  17  TYR   A O    1 
ATOM   400  C CB   A TYR   A 1 17  ? 13.937 -12.623 11.573  0.50 9.30  ?  17  TYR   A CB   1 
ATOM   401  C CB   B TYR   A 1 17  ? 13.903 -12.563 11.602  0.50 9.87  ?  17  TYR   A CB   1 
ATOM   402  C CG   A TYR   A 1 17  ? 14.203 -13.909 12.342  0.50 10.00 ?  17  TYR   A CG   1 
ATOM   403  C CG   B TYR   A 1 17  ? 13.988 -13.803 12.449  0.50 10.66 ?  17  TYR   A CG   1 
ATOM   404  C CD1  A TYR   A 1 17  ? 15.403 -14.611 12.211  0.50 10.28 ?  17  TYR   A CD1  1 
ATOM   405  C CD1  B TYR   A 1 17  ? 15.101 -14.631 12.394  0.50 11.10 ?  17  TYR   A CD1  1 
ATOM   406  C CD2  A TYR   A 1 17  ? 13.245 -14.428 13.198  0.50 10.21 ?  17  TYR   A CD2  1 
ATOM   407  C CD2  B TYR   A 1 17  ? 12.951 -14.153 13.301  0.50 10.79 ?  17  TYR   A CD2  1 
ATOM   408  C CE1  A TYR   A 1 17  ? 15.625 -15.798 12.916  0.50 10.26 ?  17  TYR   A CE1  1 
ATOM   409  C CE1  B TYR   A 1 17  ? 15.181 -15.780 13.163  0.50 11.48 ?  17  TYR   A CE1  1 
ATOM   410  C CE2  A TYR   A 1 17  ? 13.457 -15.601 13.905  0.50 10.23 ?  17  TYR   A CE2  1 
ATOM   411  C CE2  B TYR   A 1 17  ? 13.017 -15.305 14.075  0.50 11.06 ?  17  TYR   A CE2  1 
ATOM   412  C CZ   A TYR   A 1 17  ? 14.643 -16.283 13.764  0.50 10.06 ?  17  TYR   A CZ   1 
ATOM   413  C CZ   B TYR   A 1 17  ? 14.139 -16.113 14.006  0.50 11.44 ?  17  TYR   A CZ   1 
ATOM   414  O OH   A TYR   A 1 17  ? 14.825 -17.450 14.481  0.50 10.07 ?  17  TYR   A OH   1 
ATOM   415  O OH   B TYR   A 1 17  ? 14.206 -17.257 14.778  0.50 12.20 ?  17  TYR   A OH   1 
ATOM   416  H H    A TYR   A 1 17  ? 15.267 -13.020 9.318   0.50 11.13 ?  17  TYR   A H    1 
ATOM   417  H H    B TYR   A 1 17  ? 15.240 -12.985 9.302   0.50 11.34 ?  17  TYR   A H    1 
ATOM   418  H HA   A TYR   A 1 17  ? 12.701 -13.413 10.105  0.50 10.84 ?  17  TYR   A HA   1 
ATOM   419  H HA   B TYR   A 1 17  ? 12.671 -13.349 10.134  0.50 11.21 ?  17  TYR   A HA   1 
ATOM   420  H HB2  A TYR   A 1 17  ? 14.756 -12.105 11.569  0.50 11.19 ?  17  TYR   A HB2  1 
ATOM   421  H HB2  B TYR   A 1 17  ? 14.780 -12.150 11.606  0.50 11.87 ?  17  TYR   A HB2  1 
ATOM   422  H HB3  A TYR   A 1 17  ? 13.239 -12.144 12.033  0.50 11.19 ?  17  TYR   A HB3  1 
ATOM   423  H HB3  B TYR   A 1 17  ? 13.260 -11.971 12.014  0.50 11.87 ?  17  TYR   A HB3  1 
ATOM   424  H HD1  A TYR   A 1 17  ? 16.068 -14.299 11.641  0.50 12.36 ?  17  TYR   A HD1  1 
ATOM   425  H HD1  B TYR   A 1 17  ? 15.803 -14.412 11.824  0.50 13.34 ?  17  TYR   A HD1  1 
ATOM   426  H HD2  A TYR   A 1 17  ? 12.439 -13.985 13.300  0.50 12.27 ?  17  TYR   A HD2  1 
ATOM   427  H HD2  B TYR   A 1 17  ? 12.195 -13.612 13.351  0.50 12.96 ?  17  TYR   A HD2  1 
ATOM   428  H HE1  A TYR   A 1 17  ? 16.430 -16.265 12.825  0.50 12.33 ?  17  TYR   A HE1  1 
ATOM   429  H HE1  B TYR   A 1 17  ? 15.934 -16.325 13.110  0.50 13.79 ?  17  TYR   A HE1  1 
ATOM   430  H HE2  A TYR   A 1 17  ? 12.799 -15.935 14.474  0.50 12.30 ?  17  TYR   A HE2  1 
ATOM   431  H HE2  B TYR   A 1 17  ? 12.315 -15.526 14.643  0.50 13.29 ?  17  TYR   A HE2  1 
ATOM   432  H HH   A TYR   A 1 17  ? 15.584 -17.778 14.317  0.50 12.10 ?  17  TYR   A HH   1 
ATOM   433  H HH   B TYR   A 1 17  ? 13.445 -17.435 15.081  0.50 14.66 ?  17  TYR   A HH   1 
ATOM   434  N N    A ILE   A 1 18  ? 12.007 -11.002 9.530   0.50 9.47  ?  18  ILE   A N    1 
ATOM   435  N N    B ILE   A 1 18  ? 11.976 -10.998 9.547   0.50 9.09  ?  18  ILE   A N    1 
ATOM   436  C CA   A ILE   A 1 18  ? 11.630 -9.807  8.771   0.50 9.54  ?  18  ILE   A CA   1 
ATOM   437  C CA   B ILE   A 1 18  ? 11.620 -9.727  8.913   0.50 8.57  ?  18  ILE   A CA   1 
ATOM   438  C C    A ILE   A 1 18  ? 10.641 -8.954  9.564   0.50 9.75  ?  18  ILE   A C    1 
ATOM   439  C C    B ILE   A 1 18  ? 10.745 -8.888  9.840   0.50 8.19  ?  18  ILE   A C    1 
ATOM   440  O O    A ILE   A 1 18  ? 9.782  -9.470  10.283  0.50 10.12 ?  18  ILE   A O    1 
ATOM   441  O O    B ILE   A 1 18  ? 9.892  -9.417  10.564  0.50 9.07  ?  18  ILE   A O    1 
ATOM   442  C CB   A ILE   A 1 18  ? 11.096 -10.190 7.367   0.50 9.17  ?  18  ILE   A CB   1 
ATOM   443  C CB   B ILE   A 1 18  ? 10.951 -9.963  7.543   0.50 8.41  ?  18  ILE   A CB   1 
ATOM   444  C CG1  A ILE   A 1 18  ? 11.043 -8.968  6.453   0.50 8.37  ?  18  ILE   A CG1  1 
ATOM   445  C CG1  B ILE   A 1 18  ? 10.782 -8.647  6.780   0.50 9.55  ?  18  ILE   A CG1  1 
ATOM   446  C CG2  A ILE   A 1 18  ? 9.737  -10.878 7.463   0.50 9.65  ?  18  ILE   A CG2  1 
ATOM   447  C CG2  B ILE   A 1 18  ? 9.628  -10.702 7.709   0.50 9.54  ?  18  ILE   A CG2  1 
ATOM   448  C CD1  A ILE   A 1 18  ? 10.769 -9.326  5.010   0.50 9.67  ?  18  ILE   A CD1  1 
ATOM   449  C CD1  B ILE   A 1 18  ? 10.550 -8.849  5.300   0.50 11.18 ?  18  ILE   A CD1  1 
ATOM   450  H H    A ILE   A 1 18  ? 11.398 -11.321 10.042  0.50 11.38 ?  18  ILE   A H    1 
ATOM   451  H H    B ILE   A 1 18  ? 11.315 -11.398 9.927   0.50 10.93 ?  18  ILE   A H    1 
ATOM   452  H HA   A ILE   A 1 18  ? 12.432 -9.281  8.637   0.50 11.47 ?  18  ILE   A HA   1 
ATOM   453  H HA   B ILE   A 1 18  ? 12.434 -9.223  8.758   0.50 10.30 ?  18  ILE   A HA   1 
ATOM   454  H HB   A ILE   A 1 18  ? 11.721 -10.829 6.974   0.50 11.03 ?  18  ILE   A HB   1 
ATOM   455  H HB   B ILE   A 1 18  ? 11.543 -10.524 7.027   0.50 10.11 ?  18  ILE   A HB   1 
ATOM   456  H HG12 A ILE   A 1 18  ? 10.339 -8.383  6.757   0.50 10.06 ?  18  ILE   A HG12 1 
ATOM   457  H HG12 B ILE   A 1 18  ? 10.013 -8.170  7.137   0.50 11.47 ?  18  ILE   A HG12 1 
ATOM   458  H HG13 A ILE   A 1 18  ? 11.900 -8.515  6.488   0.50 10.06 ?  18  ILE   A HG13 1 
ATOM   459  H HG13 B ILE   A 1 18  ? 11.580 -8.109  6.888   0.50 11.47 ?  18  ILE   A HG13 1 
ATOM   460  H HG21 A ILE   A 1 18  ? 9.516  -11.268 6.601   0.50 11.60 ?  18  ILE   A HG21 1 
ATOM   461  H HG21 B ILE   A 1 18  ? 9.284  -10.927 6.831   0.50 11.47 ?  18  ILE   A HG21 1 
ATOM   462  H HG22 A ILE   A 1 18  ? 9.780  -11.576 8.136   0.50 11.60 ?  18  ILE   A HG22 1 
ATOM   463  H HG22 B ILE   A 1 18  ? 9.783  -11.513 8.220   0.50 11.47 ?  18  ILE   A HG22 1 
ATOM   464  H HG23 A ILE   A 1 18  ? 9.068  -10.222 7.710   0.50 11.60 ?  18  ILE   A HG23 1 
ATOM   465  H HG23 B ILE   A 1 18  ? 8.998  -10.133 8.176   0.50 11.47 ?  18  ILE   A HG23 1 
ATOM   466  H HD11 A ILE   A 1 18  ? 10.830 -8.523  4.470   0.50 11.62 ?  18  ILE   A HD11 1 
ATOM   467  H HD11 B ILE   A 1 18  ? 10.474 -7.981  4.870   0.50 13.44 ?  18  ILE   A HD11 1 
ATOM   468  H HD12 A ILE   A 1 18  ? 11.425 -9.976  4.710   0.50 11.62 ?  18  ILE   A HD12 1 
ATOM   469  H HD12 B ILE   A 1 18  ? 11.305 -9.334  4.928   0.50 13.44 ?  18  ILE   A HD12 1 
ATOM   470  H HD13 A ILE   A 1 18  ? 9.877  -9.703  4.940   0.50 11.62 ?  18  ILE   A HD13 1 
ATOM   471  H HD13 B ILE   A 1 18  ? 9.735  -9.356  5.171   0.50 13.44 ?  18  ILE   A HD13 1 
ATOM   472  N N    A LYS   A 1 19  ? 10.749 -7.632  9.401   0.50 9.53  ?  19  LYS   A N    1 
ATOM   473  N N    B LYS   A 1 19  ? 10.952 -7.568  9.804   0.50 8.14  ?  19  LYS   A N    1 
ATOM   474  C CA   A LYS   A 1 19  ? 9.943  -6.678  10.155  0.50 9.69  ?  19  LYS   A CA   1 
ATOM   475  C CA   B LYS   A 1 19  ? 10.187 -6.636  10.620  0.50 8.63  ?  19  LYS   A CA   1 
ATOM   476  C C    A LYS   A 1 19  ? 9.740  -5.413  9.326   0.50 9.69  ?  19  LYS   A C    1 
ATOM   477  C C    B LYS   A 1 19  ? 9.869  -5.396  9.804   0.50 9.46  ?  19  LYS   A C    1 
ATOM   478  O O    A LYS   A 1 19  ? 10.614 -5.023  8.546   0.50 9.67  ?  19  LYS   A O    1 
ATOM   479  O O    B LYS   A 1 19  ? 10.696 -4.925  9.018   0.50 9.40  ?  19  LYS   A O    1 
ATOM   480  C CB   A LYS   A 1 19  ? 10.663 -6.314  11.462  0.50 10.14 ?  19  LYS   A CB   1 
ATOM   481  C CB   B LYS   A 1 19  ? 10.972 -6.232  11.873  0.50 9.30  ?  19  LYS   A CB   1 
ATOM   482  C CG   A LYS   A 1 19  ? 9.908  -5.413  12.435  0.50 11.57 ?  19  LYS   A CG   1 
ATOM   483  C CG   B LYS   A 1 19  ? 10.267 -5.291  12.829  0.50 9.83  ?  19  LYS   A CG   1 
ATOM   484  C CD   A LYS   A 1 19  ? 10.788 -5.117  13.653  0.50 12.62 ?  19  LYS   A CD   1 
ATOM   485  C CD   B LYS   A 1 19  ? 11.205 -4.941  13.974  0.50 10.67 ?  19  LYS   A CD   1 
ATOM   486  C CE   A LYS   A 1 19  ? 10.109 -4.200  14.662  0.50 13.42 ?  19  LYS   A CE   1 
ATOM   487  C CE   B LYS   A 1 19  ? 10.544 -4.097  15.039  0.50 11.35 ?  19  LYS   A CE   1 
ATOM   488  N NZ   A LYS   A 1 19  ? 11.007 -3.854  15.808  0.50 13.56 ?  19  LYS   A NZ   1 
ATOM   489  N NZ   B LYS   A 1 19  ? 11.464 -3.978  16.204  0.50 11.87 ?  19  LYS   A NZ   1 
ATOM   490  H H    A LYS   A 1 19  ? 11.302 -7.267  8.856   0.50 11.45 ?  19  LYS   A H    1 
ATOM   491  H H    B LYS   A 1 19  ? 11.552 -7.174  9.310   0.50 9.79  ?  19  LYS   A H    1 
ATOM   492  H HA   A LYS   A 1 19  ? 9.079  -7.075  10.368  0.50 11.65 ?  19  LYS   A HA   1 
ATOM   493  H HA   B LYS   A 1 19  ? 9.356  -7.046  10.895  0.50 10.37 ?  19  LYS   A HA   1 
ATOM   494  H HB2  A LYS   A 1 19  ? 10.865 -7.135  11.935  0.50 12.19 ?  19  LYS   A HB2  1 
ATOM   495  H HB2  B LYS   A 1 19  ? 11.179 -7.033  12.374  0.50 11.17 ?  19  LYS   A HB2  1 
ATOM   496  H HB3  A LYS   A 1 19  ? 11.489 -5.862  11.232  0.50 12.19 ?  19  LYS   A HB3  1 
ATOM   497  H HB3  B LYS   A 1 19  ? 11.796 -5.798  11.598  0.50 11.17 ?  19  LYS   A HB3  1 
ATOM   498  H HG2  A LYS   A 1 19  ? 9.690  -4.573  12.004  0.50 13.90 ?  19  LYS   A HG2  1 
ATOM   499  H HG2  B LYS   A 1 19  ? 10.020 -4.475  12.368  0.50 11.82 ?  19  LYS   A HG2  1 
ATOM   500  H HG3  A LYS   A 1 19  ? 9.104  -5.860  12.740  0.50 13.90 ?  19  LYS   A HG3  1 
ATOM   501  H HG3  B LYS   A 1 19  ? 9.480  -5.729  13.194  0.50 11.82 ?  19  LYS   A HG3  1 
ATOM   502  H HD2  A LYS   A 1 19  ? 11.002 -5.950  14.105  0.50 15.16 ?  19  LYS   A HD2  1 
ATOM   503  H HD2  B LYS   A 1 19  ? 11.512 -5.762  14.389  0.50 12.83 ?  19  LYS   A HD2  1 
ATOM   504  H HD3  A LYS   A 1 19  ? 11.607 -4.683  13.360  0.50 15.16 ?  19  LYS   A HD3  1 
ATOM   505  H HD3  B LYS   A 1 19  ? 11.959 -4.445  13.620  0.50 12.83 ?  19  LYS   A HD3  1 
ATOM   506  H HE2  A LYS   A 1 19  ? 9.854  -3.375  14.224  0.50 16.12 ?  19  LYS   A HE2  1 
ATOM   507  H HE2  B LYS   A 1 19  ? 10.364 -3.209  14.688  0.50 13.64 ?  19  LYS   A HE2  1 
ATOM   508  H HE3  A LYS   A 1 19  ? 9.327  -4.645  15.022  0.50 16.12 ?  19  LYS   A HE3  1 
ATOM   509  H HE3  B LYS   A 1 19  ? 9.721  -4.522  15.330  0.50 13.64 ?  19  LYS   A HE3  1 
ATOM   510  H HZ1  A LYS   A 1 19  ? 10.571 -3.351  16.399  0.50 16.30 ?  19  LYS   A HZ1  1 
ATOM   511  H HZ1  B LYS   A 1 19  ? 11.087 -3.484  16.839  0.50 14.27 ?  19  LYS   A HZ1  1 
ATOM   512  H HZ2  A LYS   A 1 19  ? 11.287 -4.596  16.214  0.50 16.30 ?  19  LYS   A HZ2  1 
ATOM   513  H HZ2  B LYS   A 1 19  ? 11.643 -4.786  16.531  0.50 14.27 ?  19  LYS   A HZ2  1 
ATOM   514  H HZ3  A LYS   A 1 19  ? 11.717 -3.402  15.515  0.50 16.30 ?  19  LYS   A HZ3  1 
ATOM   515  H HZ3  B LYS   A 1 19  ? 12.226 -3.594  15.949  0.50 14.27 ?  19  LYS   A HZ3  1 
ATOM   516  N N    A ASN   A 1 20  ? 8.577  -4.775  9.495   0.50 10.91 ?  20  ASN   A N    1 
ATOM   517  N N    B ASN   A 1 20  ? 8.660  -4.885  9.992   0.50 10.83 ?  20  ASN   A N    1 
ATOM   518  C CA   A ASN   A 1 20  ? 8.357  -3.434  8.960   0.50 12.40 ?  20  ASN   A CA   1 
ATOM   519  C CA   B ASN   A 1 20  ? 8.246  -3.613  9.421   0.50 11.95 ?  20  ASN   A CA   1 
ATOM   520  C C    A ASN   A 1 20  ? 8.991  -2.451  9.934   0.50 13.61 ?  20  ASN   A C    1 
ATOM   521  C C    B ASN   A 1 20  ? 8.874  -2.524  10.281  0.50 12.03 ?  20  ASN   A C    1 
ATOM   522  O O    A ASN   A 1 20  ? 8.503  -2.272  11.053  0.50 14.76 ?  20  ASN   A O    1 
ATOM   523  O O    B ASN   A 1 20  ? 8.363  -2.193  11.355  0.50 13.29 ?  20  ASN   A O    1 
ATOM   524  C CB   A ASN   A 1 20  ? 6.868  -3.143  8.778   0.50 13.34 ?  20  ASN   A CB   1 
ATOM   525  C CB   B ASN   A 1 20  ? 6.724  -3.555  9.443   0.50 13.42 ?  20  ASN   A CB   1 
ATOM   526  C CG   A ASN   A 1 20  ? 6.581  -1.657  8.514   0.50 13.92 ?  20  ASN   A CG   1 
ATOM   527  C CG   B ASN   A 1 20  ? 6.156  -2.353  8.725   0.50 14.81 ?  20  ASN   A CG   1 
ATOM   528  O OD1  A ASN   A 1 20  ? 5.704  -1.061  9.139   0.50 14.85 ?  20  ASN   A OD1  1 
ATOM   529  O OD1  B ASN   A 1 20  ? 5.093  -1.861  9.101   0.50 16.49 ?  20  ASN   A OD1  1 
ATOM   530  N ND2  A ASN   A 1 20  ? 7.320  -1.063  7.594   0.50 14.54 ?  20  ASN   A ND2  1 
ATOM   531  N ND2  B ASN   A 1 20  ? 6.845  -1.869  7.696   0.50 14.71 ?  20  ASN   A ND2  1 
ATOM   532  H H    A ASN   A 1 20  ? 7.903  -5.099  9.926   0.50 13.11 ?  20  ASN   A H    1 
ATOM   533  H H    B ASN   A 1 20  ? 8.047  -5.270  10.447  0.50 13.02 ?  20  ASN   A H    1 
ATOM   534  H HA   A ASN   A 1 20  ? 8.789  -3.353  8.096   0.50 14.90 ?  20  ASN   A HA   1 
ATOM   535  H HA   B ASN   A 1 20  ? 8.569  -3.539  8.512   0.50 14.36 ?  20  ASN   A HA   1 
ATOM   536  H HB2  A ASN   A 1 20  ? 6.532  -3.655  8.015   0.50 16.03 ?  20  ASN   A HB2  1 
ATOM   537  H HB2  B ASN   A 1 20  ? 6.372  -4.350  9.022   0.50 16.12 ?  20  ASN   A HB2  1 
ATOM   538  H HB3  A ASN   A 1 20  ? 6.388  -3.410  9.579   0.50 16.03 ?  20  ASN   A HB3  1 
ATOM   539  H HB3  B ASN   A 1 20  ? 6.426  -3.511  10.369  0.50 16.12 ?  20  ASN   A HB3  1 
ATOM   540  H HD21 A ASN   A 1 20  ? 7.184  -0.233  7.410   0.50 17.46 ?  20  ASN   A HD21 1 
ATOM   541  H HD21 B ASN   A 1 20  ? 6.552  -1.191  7.263   0.50 17.67 ?  20  ASN   A HD21 1 
ATOM   542  H HD22 A ASN   A 1 20  ? 7.922  -1.505  7.177   0.50 17.46 ?  20  ASN   A HD22 1 
ATOM   543  H HD22 B ASN   A 1 20  ? 7.589  -2.235  7.458   0.50 17.67 ?  20  ASN   A HD22 1 
ATOM   544  N N    A ALA   A 1 21  ? 10.101 -1.843  9.531   0.50 13.74 ?  21  ALA   A N    1 
ATOM   545  N N    B ALA   A 1 21  ? 10.003 -1.978  9.829   0.50 12.09 ?  21  ALA   A N    1 
ATOM   546  C CA   A ALA   A 1 21  ? 10.792 -0.923  10.419  0.50 13.91 ?  21  ALA   A CA   1 
ATOM   547  C CA   B ALA   A 1 21  ? 10.775 -1.078  10.675  0.50 12.88 ?  21  ALA   A CA   1 
ATOM   548  C C    A ALA   A 1 21  ? 11.766 -0.069  9.625   0.50 13.37 ?  21  ALA   A C    1 
ATOM   549  C C    B ALA   A 1 21  ? 11.623 -0.144  9.827   0.50 12.92 ?  21  ALA   A C    1 
ATOM   550  O O    A ALA   A 1 21  ? 12.266 -0.479  8.574   0.50 13.69 ?  21  ALA   A O    1 
ATOM   551  O O    B ALA   A 1 21  ? 11.964 -0.443  8.680   0.50 12.85 ?  21  ALA   A O    1 
ATOM   552  C CB   A ALA   A 1 21  ? 11.551 -1.682  11.510  0.50 14.95 ?  21  ALA   A CB   1 
ATOM   553  C CB   B ALA   A 1 21  ? 11.673 -1.850  11.650  0.50 13.90 ?  21  ALA   A CB   1 
ATOM   554  H H    A ALA   A 1 21  ? 10.472 -1.963  8.766   0.50 16.51 ?  21  ALA   A H    1 
ATOM   555  H H    B ALA   A 1 21  ? 10.339 -2.108  9.042   0.50 14.53 ?  21  ALA   A H    1 
ATOM   556  H HA   A ALA   A 1 21  ? 10.133 -0.349  10.847  0.50 16.71 ?  21  ALA   A HA   1 
ATOM   557  H HA   B ALA   A 1 21  ? 10.165 -0.533  11.192  0.50 15.48 ?  21  ALA   A HA   1 
ATOM   558  H HB1  A ALA   A 1 21  ? 11.938 -1.038  12.118  0.50 17.96 ?  21  ALA   A HB1  1 
ATOM   559  H HB1  B ALA   A 1 21  ? 12.166 -1.213  12.191  0.50 16.70 ?  21  ALA   A HB1  1 
ATOM   560  H HB2  A ALA   A 1 21  ? 10.931 -2.258  11.988  0.50 17.96 ?  21  ALA   A HB2  1 
ATOM   561  H HB2  B ALA   A 1 21  ? 11.113 -2.403  12.218  0.50 16.70 ?  21  ALA   A HB2  1 
ATOM   562  H HB3  A ALA   A 1 21  ? 12.244 -2.217  11.096  0.50 17.96 ?  21  ALA   A HB3  1 
ATOM   563  H HB3  B ALA   A 1 21  ? 12.285 -2.403  11.145  0.50 16.70 ?  21  ALA   A HB3  1 
ATOM   564  N N    A ASP   A 1 22  ? 12.024 1.123   10.153  0.50 13.28 ?  22  ASP   A N    1 
ATOM   565  N N    B ASP   A 1 22  ? 11.942 1.002   10.426  0.50 13.00 ?  22  ASP   A N    1 
ATOM   566  C CA   A ASP   A 1 22  ? 13.078 1.994   9.651   0.50 13.27 ?  22  ASP   A CA   1 
ATOM   567  C CA   B ASP   A 1 22  ? 12.947 1.929   9.923   0.50 12.98 ?  22  ASP   A CA   1 
ATOM   568  C C    A ASP   A 1 22  ? 14.407 1.499   10.214  0.50 12.23 ?  22  ASP   A C    1 
ATOM   569  C C    B ASP   A 1 22  ? 14.312 1.422   10.377  0.50 12.63 ?  22  ASP   A C    1 
ATOM   570  O O    A ASP   A 1 22  ? 14.615 1.528   11.432  0.50 12.89 ?  22  ASP   A O    1 
ATOM   571  O O    B ASP   A 1 22  ? 14.537 1.241   11.578  0.50 12.81 ?  22  ASP   A O    1 
ATOM   572  C CB   A ASP   A 1 22  ? 12.783 3.419   10.120  0.50 15.01 ?  22  ASP   A CB   1 
ATOM   573  C CB   B ASP   A 1 22  ? 12.643 3.299   10.532  0.50 13.80 ?  22  ASP   A CB   1 
ATOM   574  C CG   A ASP   A 1 22  ? 13.838 4.433   9.685   0.50 16.86 ?  22  ASP   A CG   1 
ATOM   575  C CG   B ASP   A 1 22  ? 13.551 4.403   10.024  0.50 14.25 ?  22  ASP   A CG   1 
ATOM   576  O OD1  A ASP   A 1 22  ? 14.733 4.087   8.889   0.50 17.54 ?  22  ASP   A OD1  1 
ATOM   577  O OD1  B ASP   A 1 22  ? 14.743 4.144   9.774   0.50 13.83 ?  22  ASP   A OD1  1 
ATOM   578  O OD2  A ASP   A 1 22  ? 13.769 5.593   10.154  0.50 18.14 -1 22  ASP   A OD2  1 
ATOM   579  O OD2  B ASP   A 1 22  ? 13.064 5.550   9.900   0.50 14.88 -1 22  ASP   A OD2  1 
ATOM   580  H H    A ASP   A 1 22  ? 11.579 1.452   10.815  0.50 15.95 ?  22  ASP   A H    1 
ATOM   581  H H    B ASP   A 1 22  ? 11.566 1.278   11.148  0.50 15.62 ?  22  ASP   A H    1 
ATOM   582  H HA   A ASP   A 1 22  ? 13.100 1.960   8.681   0.50 15.94 ?  22  ASP   A HA   1 
ATOM   583  H HA   B ASP   A 1 22  ? 12.918 1.987   8.955   0.50 15.60 ?  22  ASP   A HA   1 
ATOM   584  H HB2  A ASP   A 1 22  ? 11.916 3.687   9.771   0.50 18.03 ?  22  ASP   A HB2  1 
ATOM   585  H HB2  B ASP   A 1 22  ? 11.729 3.543   10.326  0.50 16.58 ?  22  ASP   A HB2  1 
ATOM   586  H HB3  A ASP   A 1 22  ? 12.762 3.426   11.089  0.50 18.03 ?  22  ASP   A HB3  1 
ATOM   587  H HB3  B ASP   A 1 22  ? 12.761 3.250   11.494  0.50 16.58 ?  22  ASP   A HB3  1 
ATOM   588  N N    A ILE   A 1 23  ? 15.298 1.030   9.334   0.50 11.20 ?  23  ILE   A N    1 
ATOM   589  N N    B ILE   A 1 23  ? 15.215 1.166   9.425   0.50 12.27 ?  23  ILE   A N    1 
ATOM   590  C CA   A ILE   A 1 23  ? 16.542 0.405   9.783   0.50 10.86 ?  23  ILE   A CA   1 
ATOM   591  C CA   B ILE   A 1 23  ? 16.499 0.560   9.775   0.50 11.81 ?  23  ILE   A CA   1 
ATOM   592  C C    A ILE   A 1 23  ? 17.341 1.343   10.678  0.50 11.30 ?  23  ILE   A C    1 
ATOM   593  C C    B ILE   A 1 23  ? 17.321 1.476   10.673  0.50 11.92 ?  23  ILE   A C    1 
ATOM   594  O O    A ILE   A 1 23  ? 18.059 0.890   11.580  0.50 11.52 ?  23  ILE   A O    1 
ATOM   595  O O    B ILE   A 1 23  ? 18.075 0.998   11.530  0.50 12.42 ?  23  ILE   A O    1 
ATOM   596  C CB   A ILE   A 1 23  ? 17.362 -0.115  8.579   0.50 10.41 ?  23  ILE   A CB   1 
ATOM   597  C CB   B ILE   A 1 23  ? 17.274 0.107   8.517   0.50 11.55 ?  23  ILE   A CB   1 
ATOM   598  C CG1  A ILE   A 1 23  ? 18.484 -1.043  9.056   0.50 10.75 ?  23  ILE   A CG1  1 
ATOM   599  C CG1  B ILE   A 1 23  ? 18.440 -0.802  8.918   0.50 11.64 ?  23  ILE   A CG1  1 
ATOM   600  C CG2  A ILE   A 1 23  ? 17.912 1.038   7.747   0.50 10.51 ?  23  ILE   A CG2  1 
ATOM   601  C CG2  B ILE   A 1 23  ? 17.751 1.305   7.704   0.50 12.04 ?  23  ILE   A CG2  1 
ATOM   602  C CD1  A ILE   A 1 23  ? 19.246 -1.723  7.927   0.50 10.73 ?  23  ILE   A CD1  1 
ATOM   603  C CD1  B ILE   A 1 23  ? 19.149 -1.449  7.750   0.50 11.96 ?  23  ILE   A CD1  1 
ATOM   604  H H    A ILE   A 1 23  ? 15.202 1.067   8.485   0.50 13.46 ?  23  ILE   A H    1 
ATOM   605  H H    B ILE   A 1 23  ? 15.108 1.327   8.592   0.50 14.75 ?  23  ILE   A H    1 
ATOM   606  H HA   A ILE   A 1 23  ? 16.313 -0.367  10.323  0.50 13.06 ?  23  ILE   A HA   1 
ATOM   607  H HA   B ILE   A 1 23  ? 16.317 -0.238  10.288  0.50 14.19 ?  23  ILE   A HA   1 
ATOM   608  H HB   A ILE   A 1 23  ? 16.765 -0.635  8.017   0.50 12.51 ?  23  ILE   A HB   1 
ATOM   609  H HB   B ILE   A 1 23  ? 16.668 -0.410  7.964   0.50 13.88 ?  23  ILE   A HB   1 
ATOM   610  H HG12 A ILE   A 1 23  ? 19.121 -0.528  9.571   0.50 12.92 ?  23  ILE   A HG12 1 
ATOM   611  H HG12 B ILE   A 1 23  ? 19.092 -0.281  9.406   0.50 13.98 ?  23  ILE   A HG12 1 
ATOM   612  H HG13 A ILE   A 1 23  ? 18.099 -1.741  9.611   0.50 12.92 ?  23  ILE   A HG13 1 
ATOM   613  H HG13 B ILE   A 1 23  ? 18.099 -1.516  9.483   0.50 13.98 ?  23  ILE   A HG13 1 
ATOM   614  H HG21 A ILE   A 1 23  ? 18.259 0.687   6.912   0.50 12.63 ?  23  ILE   A HG21 1 
ATOM   615  H HG21 B ILE   A 1 23  ? 18.083 0.992   6.847   0.50 14.47 ?  23  ILE   A HG21 1 
ATOM   616  H HG22 A ILE   A 1 23  ? 17.192 1.665   7.566   0.50 12.63 ?  23  ILE   A HG22 1 
ATOM   617  H HG22 B ILE   A 1 23  ? 17.002 1.907   7.566   0.50 14.47 ?  23  ILE   A HG22 1 
ATOM   618  H HG23 A ILE   A 1 23  ? 18.617 1.479   8.242   0.50 12.63 ?  23  ILE   A HG23 1 
ATOM   619  H HG23 B ILE   A 1 23  ? 18.456 1.758   8.189   0.50 14.47 ?  23  ILE   A HG23 1 
ATOM   620  H HD11 A ILE   A 1 23  ? 19.880 -2.352  8.306   0.50 12.89 ?  23  ILE   A HD11 1 
ATOM   621  H HD11 B ILE   A 1 23  ? 19.822 -2.059  8.090   0.50 14.37 ?  23  ILE   A HD11 1 
ATOM   622  H HD12 A ILE   A 1 23  ? 18.615 -2.193  7.358   0.50 12.89 ?  23  ILE   A HD12 1 
ATOM   623  H HD12 B ILE   A 1 23  ? 18.500 -1.935  7.217   0.50 14.37 ?  23  ILE   A HD12 1 
ATOM   624  H HD13 A ILE   A 1 23  ? 19.717 -1.049  7.412   0.50 12.89 ?  23  ILE   A HD13 1 
ATOM   625  H HD13 B ILE   A 1 23  ? 19.566 -0.758  7.215   0.50 14.37 ?  23  ILE   A HD13 1 
ATOM   626  N N    A VAL   A 1 24  ? 17.215 2.654   10.467  0.50 12.03 ?  24  VAL   A N    1 
ATOM   627  N N    B VAL   A 1 24  ? 17.188 2.793   10.510  0.50 12.05 ?  24  VAL   A N    1 
ATOM   628  C CA   A VAL   A 1 24  ? 17.914 3.618   11.314  0.50 13.30 ?  24  VAL   A CA   1 
ATOM   629  C CA   B VAL   A 1 24  ? 17.892 3.715   11.398  0.50 12.77 ?  24  VAL   A CA   1 
ATOM   630  C C    A VAL   A 1 24  ? 17.408 3.530   12.747  0.50 13.87 ?  24  VAL   A C    1 
ATOM   631  C C    B VAL   A 1 24  ? 17.356 3.598   12.819  0.50 13.59 ?  24  VAL   A C    1 
ATOM   632  O O    A VAL   A 1 24  ? 18.195 3.487   13.701  0.50 13.84 ?  24  VAL   A O    1 
ATOM   633  O O    B VAL   A 1 24  ? 18.122 3.457   13.780  0.50 13.66 ?  24  VAL   A O    1 
ATOM   634  C CB   A VAL   A 1 24  ? 17.767 5.039   10.741  0.50 14.48 ?  24  VAL   A CB   1 
ATOM   635  C CB   B VAL   A 1 24  ? 17.798 5.158   10.872  0.50 13.16 ?  24  VAL   A CB   1 
ATOM   636  C CG1  A VAL   A 1 24  ? 18.313 6.078   11.715  0.50 15.75 ?  24  VAL   A CG1  1 
ATOM   637  C CG1  B VAL   A 1 24  ? 18.249 6.152   11.939  0.50 14.27 ?  24  VAL   A CG1  1 
ATOM   638  C CG2  A VAL   A 1 24  ? 18.469 5.138   9.393   0.50 15.23 ?  24  VAL   A CG2  1 
ATOM   639  C CG2  B VAL   A 1 24  ? 18.636 5.314   9.616   0.50 13.77 ?  24  VAL   A CG2  1 
ATOM   640  H H    A VAL   A 1 24  ? 16.733 3.008   9.851   0.50 14.45 ?  24  VAL   A H    1 
ATOM   641  H H    B VAL   A 1 24  ? 16.706 3.172   9.905   0.50 14.48 ?  24  VAL   A H    1 
ATOM   642  H HA   A VAL   A 1 24  ? 18.858 3.401   11.323  0.50 15.98 ?  24  VAL   A HA   1 
ATOM   643  H HA   B VAL   A 1 24  ? 18.829 3.474   11.415  0.50 15.35 ?  24  VAL   A HA   1 
ATOM   644  H HB   A VAL   A 1 24  ? 16.827 5.228   10.600  0.50 17.39 ?  24  VAL   A HB   1 
ATOM   645  H HB   B VAL   A 1 24  ? 16.877 5.358   10.642  0.50 15.81 ?  24  VAL   A HB   1 
ATOM   646  H HG11 A VAL   A 1 24  ? 18.462 6.908   11.236  0.50 18.92 ?  24  VAL   A HG11 1 
ATOM   647  H HG11 B VAL   A 1 24  ? 18.462 6.995   11.511  0.50 17.15 ?  24  VAL   A HG11 1 
ATOM   648  H HG12 A VAL   A 1 24  ? 17.665 6.217   12.423  0.50 18.92 ?  24  VAL   A HG12 1 
ATOM   649  H HG12 B VAL   A 1 24  ? 17.531 6.276   12.576  0.50 17.15 ?  24  VAL   A HG12 1 
ATOM   650  H HG13 A VAL   A 1 24  ? 19.149 5.755   12.084  0.50 18.92 ?  24  VAL   A HG13 1 
ATOM   651  H HG13 B VAL   A 1 24  ? 19.036 5.799   12.382  0.50 17.15 ?  24  VAL   A HG13 1 
ATOM   652  H HG21 A VAL   A 1 24  ? 18.148 5.927   8.929   0.50 18.30 ?  24  VAL   A HG21 1 
ATOM   653  H HG21 B VAL   A 1 24  ? 18.556 6.224   9.292   0.50 16.55 ?  24  VAL   A HG21 1 
ATOM   654  H HG22 A VAL   A 1 24  ? 19.425 5.208   9.539   0.50 18.30 ?  24  VAL   A HG22 1 
ATOM   655  H HG22 B VAL   A 1 24  ? 19.562 5.117   9.828   0.50 16.55 ?  24  VAL   A HG22 1 
ATOM   656  H HG23 A VAL   A 1 24  ? 18.269 4.345   8.869   0.50 18.30 ?  24  VAL   A HG23 1 
ATOM   657  H HG23 B VAL   A 1 24  ? 18.313 4.694   8.942   0.50 16.55 ?  24  VAL   A HG23 1 
ATOM   658  N N    A GLU   A 1 25  ? 16.084 3.499   12.920  0.50 14.79 ?  25  GLU   A N    1 
ATOM   659  N N    B GLU   A 1 25  ? 16.032 3.657   12.971  0.50 14.60 ?  25  GLU   A N    1 
ATOM   660  C CA   A GLU   A 1 25  ? 15.519 3.429   14.264  0.50 16.17 ?  25  GLU   A CA   1 
ATOM   661  C CA   B GLU   A 1 25  ? 15.436 3.552   14.299  0.50 15.85 ?  25  GLU   A CA   1 
ATOM   662  C C    A GLU   A 1 25  ? 15.735 2.052   14.884  0.50 15.44 ?  25  GLU   A C    1 
ATOM   663  C C    B GLU   A 1 25  ? 15.733 2.201   14.932  0.50 14.91 ?  25  GLU   A C    1 
ATOM   664  O O    A GLU   A 1 25  ? 15.992 1.945   16.089  0.50 15.92 ?  25  GLU   A O    1 
ATOM   665  O O    B GLU   A 1 25  ? 15.964 2.110   16.143  0.50 15.53 ?  25  GLU   A O    1 
ATOM   666  C CB   A GLU   A 1 25  ? 14.039 3.813   14.235  0.50 18.25 ?  25  GLU   A CB   1 
ATOM   667  C CB   B GLU   A 1 25  ? 13.928 3.791   14.213  0.50 18.35 ?  25  GLU   A CB   1 
ATOM   668  C CG   A GLU   A 1 25  ? 13.794 5.238   13.741  0.50 20.59 ?  25  GLU   A CG   1 
ATOM   669  C CG   B GLU   A 1 25  ? 13.570 5.247   13.992  0.50 21.13 ?  25  GLU   A CG   1 
ATOM   670  C CD   A GLU   A 1 25  ? 14.589 6.279   14.509  0.50 22.59 ?  25  GLU   A CD   1 
ATOM   671  C CD   B GLU   A 1 25  ? 14.121 6.149   15.079  0.50 23.30 ?  25  GLU   A CD   1 
ATOM   672  O OE1  A GLU   A 1 25  ? 14.693 6.164   15.749  0.50 23.14 ?  25  GLU   A OE1  1 
ATOM   673  O OE1  B GLU   A 1 25  ? 13.963 5.811   16.270  0.50 23.87 ?  25  GLU   A OE1  1 
ATOM   674  O OE2  A GLU   A 1 25  ? 15.127 7.206   13.865  0.50 23.29 -1 25  GLU   A OE2  1 
ATOM   675  O OE2  B GLU   A 1 25  ? 14.738 7.181   14.742  0.50 24.13 -1 25  GLU   A OE2  1 
ATOM   676  H H    A GLU   A 1 25  ? 15.503 3.524   12.285  0.50 17.76 ?  25  GLU   A H    1 
ATOM   677  H H    B GLU   A 1 25  ? 15.467 3.760   12.329  0.50 17.53 ?  25  GLU   A H    1 
ATOM   678  H HA   A GLU   A 1 25  ? 15.977 4.071   14.824  0.50 19.42 ?  25  GLU   A HA   1 
ATOM   679  H HA   B GLU   A 1 25  ? 15.822 4.231   14.869  0.50 19.04 ?  25  GLU   A HA   1 
ATOM   680  H HB2  A GLU   A 1 25  ? 13.564 3.211   13.641  0.50 21.92 ?  25  GLU   A HB2  1 
ATOM   681  H HB2  B GLU   A 1 25  ? 13.566 3.276   13.473  0.50 22.04 ?  25  GLU   A HB2  1 
ATOM   682  H HB3  A GLU   A 1 25  ? 13.676 3.744   15.133  0.50 21.92 ?  25  GLU   A HB3  1 
ATOM   683  H HB3  B GLU   A 1 25  ? 13.515 3.506   15.042  0.50 22.04 ?  25  GLU   A HB3  1 
ATOM   684  H HG2  A GLU   A 1 25  ? 14.073 5.308   12.819  0.50 24.73 ?  25  GLU   A HG2  1 
ATOM   685  H HG2  B GLU   A 1 25  ? 13.942 5.539   13.146  0.50 25.37 ?  25  GLU   A HG2  1 
ATOM   686  H HG3  A GLU   A 1 25  ? 12.845 5.441   13.819  0.50 24.73 ?  25  GLU   A HG3  1 
ATOM   687  H HG3  B GLU   A 1 25  ? 12.606 5.339   13.985  0.50 25.37 ?  25  GLU   A HG3  1 
ATOM   688  N N    A GLU   A 1 26  ? 15.654 0.987   14.081  0.50 15.06 ?  26  GLU   A N    1 
ATOM   689  N N    B GLU   A 1 26  ? 15.748 1.142   14.124  0.50 14.12 ?  26  GLU   A N    1 
ATOM   690  C CA   A GLU   A 1 26  ? 16.013 -0.336  14.584  0.50 14.78 ?  26  GLU   A CA   1 
ATOM   691  C CA   B GLU   A 1 26  ? 15.980 -0.195  14.657  0.50 13.09 ?  26  GLU   A CA   1 
ATOM   692  C C    A GLU   A 1 26  ? 17.437 -0.336  15.119  0.50 13.86 ?  26  GLU   A C    1 
ATOM   693  C C    B GLU   A 1 26  ? 17.434 -0.375  15.090  0.50 13.35 ?  26  GLU   A C    1 
ATOM   694  O O    A GLU   A 1 26  ? 17.695 -0.783  16.243  0.50 14.00 ?  26  GLU   A O    1 
ATOM   695  O O    B GLU   A 1 26  ? 17.709 -1.009  16.115  0.50 14.25 ?  26  GLU   A O    1 
ATOM   696  C CB   A GLU   A 1 26  ? 15.875 -1.381  13.476  0.50 15.71 ?  26  GLU   A CB   1 
ATOM   697  C CB   B GLU   A 1 26  ? 15.572 -1.223  13.605  0.50 12.06 ?  26  GLU   A CB   1 
ATOM   698  C CG   A GLU   A 1 26  ? 14.469 -1.881  13.248  0.50 16.61 ?  26  GLU   A CG   1 
ATOM   699  C CG   B GLU   A 1 26  ? 15.772 -2.664  14.012  0.50 11.43 ?  26  GLU   A CG   1 
ATOM   700  C CD   A GLU   A 1 26  ? 13.927 -2.666  14.427  0.50 17.16 ?  26  GLU   A CD   1 
ATOM   701  C CD   B GLU   A 1 26  ? 14.702 -3.173  14.959  0.50 11.35 ?  26  GLU   A CD   1 
ATOM   702  O OE1  A GLU   A 1 26  ? 14.442 -3.767  14.722  0.50 17.89 ?  26  GLU   A OE1  1 
ATOM   703  O OE1  B GLU   A 1 26  ? 13.763 -2.420  15.299  0.50 11.96 ?  26  GLU   A OE1  1 
ATOM   704  O OE2  A GLU   A 1 26  ? 12.984 -2.168  15.068  0.50 17.60 -1 26  GLU   A OE2  1 
ATOM   705  O OE2  B GLU   A 1 26  ? 14.805 -4.354  15.347  0.50 11.08 -1 26  GLU   A OE2  1 
ATOM   706  H H    A GLU   A 1 26  ? 15.409 1.007   13.258  0.50 18.09 ?  26  GLU   A H    1 
ATOM   707  H H    B GLU   A 1 26  ? 15.637 1.173   13.271  0.50 16.97 ?  26  GLU   A H    1 
ATOM   708  H HA   A GLU   A 1 26  ? 15.416 -0.574  15.310  0.50 17.76 ?  26  GLU   A HA   1 
ATOM   709  H HA   B GLU   A 1 26  ? 15.419 -0.323  15.435  0.50 15.72 ?  26  GLU   A HA   1 
ATOM   710  H HB2  A GLU   A 1 26  ? 16.183 -0.994  12.644  0.50 18.87 ?  26  GLU   A HB2  1 
ATOM   711  H HB2  B GLU   A 1 26  ? 14.626 -1.105  13.408  0.50 14.50 ?  26  GLU   A HB2  1 
ATOM   712  H HB3  A GLU   A 1 26  ? 16.422 -2.148  13.705  0.50 18.87 ?  26  GLU   A HB3  1 
ATOM   713  H HB3  B GLU   A 1 26  ? 16.090 -1.071  12.802  0.50 14.50 ?  26  GLU   A HB3  1 
ATOM   714  H HG2  A GLU   A 1 26  ? 13.888 -1.119  13.102  0.50 19.96 ?  26  GLU   A HG2  1 
ATOM   715  H HG2  B GLU   A 1 26  ? 15.754 -3.220  13.216  0.50 13.74 ?  26  GLU   A HG2  1 
ATOM   716  H HG3  A GLU   A 1 26  ? 14.461 -2.460  12.470  0.50 19.96 ?  26  GLU   A HG3  1 
ATOM   717  H HG3  B GLU   A 1 26  ? 16.630 -2.764  14.454  0.50 13.74 ?  26  GLU   A HG3  1 
ATOM   718  N N    . ALA   A 1 27  ? 18.379 0.179   14.325  1.00 12.94 ?  27  ALA   A N    1 
ATOM   719  C CA   . ALA   A 1 27  ? 19.777 0.149   14.741  1.00 12.81 ?  27  ALA   A CA   1 
ATOM   720  C C    . ALA   A 1 27  ? 19.983 0.939   16.029  1.00 14.18 ?  27  ALA   A C    1 
ATOM   721  O O    . ALA   A 1 27  ? 20.681 0.483   16.943  1.00 14.15 ?  27  ALA   A O    1 
ATOM   722  C CB   . ALA   A 1 27  ? 20.671 0.690   13.622  1.00 12.43 ?  27  ALA   A CB   1 
ATOM   723  H H    A ALA   A 1 27  ? 18.233 0.548   13.560  0.50 15.55 ?  27  ALA   A H    1 
ATOM   724  H H    B ALA   A 1 27  ? 18.234 0.574   13.574  0.50 15.55 ?  27  ALA   A H    1 
ATOM   725  H HA   . ALA   A 1 27  ? 20.033 -0.770  14.907  1.00 15.39 ?  27  ALA   A HA   1 
ATOM   726  H HB1  . ALA   A 1 27  ? 21.596 0.660   13.915  1.00 14.93 ?  27  ALA   A HB1  1 
ATOM   727  H HB2  . ALA   A 1 27  ? 20.559 0.134   12.832  1.00 14.93 ?  27  ALA   A HB2  1 
ATOM   728  H HB3  . ALA   A 1 27  ? 20.415 1.602   13.422  1.00 14.93 ?  27  ALA   A HB3  1 
ATOM   729  N N    A LYS   A 1 28  ? 19.379 2.125   16.126  0.50 15.85 ?  28  LYS   A N    1 
ATOM   730  N N    B LYS   A 1 28  ? 19.371 2.119   16.131  0.50 15.42 ?  28  LYS   A N    1 
ATOM   731  C CA   A LYS   A 1 28  ? 19.553 2.939   17.325  0.50 18.66 ?  28  LYS   A CA   1 
ATOM   732  C CA   B LYS   A 1 28  ? 19.524 2.909   17.348  0.50 17.81 ?  28  LYS   A CA   1 
ATOM   733  C C    A LYS   A 1 28  ? 18.997 2.249   18.565  0.50 19.67 ?  28  LYS   A C    1 
ATOM   734  C C    B LYS   A 1 28  ? 19.026 2.142   18.568  0.50 18.43 ?  28  LYS   A C    1 
ATOM   735  O O    A LYS   A 1 28  ? 19.492 2.478   19.674  0.50 21.28 ?  28  LYS   A O    1 
ATOM   736  O O    B LYS   A 1 28  ? 19.658 2.176   19.630  0.50 19.77 ?  28  LYS   A O    1 
ATOM   737  C CB   A LYS   A 1 28  ? 18.913 4.317   17.133  0.50 20.64 ?  28  LYS   A CB   1 
ATOM   738  C CB   B LYS   A 1 28  ? 18.822 4.260   17.199  0.50 19.80 ?  28  LYS   A CB   1 
ATOM   739  C CG   A LYS   A 1 28  ? 19.730 5.240   16.241  0.50 22.72 ?  28  LYS   A CG   1 
ATOM   740  C CG   B LYS   A 1 28  ? 19.573 5.223   16.287  0.50 21.86 ?  28  LYS   A CG   1 
ATOM   741  C CD   A LYS   A 1 28  ? 19.240 6.678   16.296  0.50 25.22 ?  28  LYS   A CD   1 
ATOM   742  C CD   B LYS   A 1 28  ? 19.115 6.663   16.458  0.50 24.56 ?  28  LYS   A CD   1 
ATOM   743  C CE   A LYS   A 1 28  ? 17.928 6.849   15.555  0.50 26.90 ?  28  LYS   A CE   1 
ATOM   744  C CE   B LYS   A 1 28  ? 17.815 6.929   15.726  0.50 26.35 ?  28  LYS   A CE   1 
ATOM   745  N NZ   A LYS   A 1 28  ? 17.515 8.279   15.499  0.50 28.08 ?  28  LYS   A NZ   1 
ATOM   746  N NZ   B LYS   A 1 28  ? 17.494 8.383   15.700  0.50 27.58 ?  28  LYS   A NZ   1 
ATOM   747  H H    A LYS   A 1 28  ? 18.876 2.473   15.523  0.50 19.04 ?  28  LYS   A H    1 
ATOM   748  H H    B LYS   A 1 28  ? 18.871 2.472   15.530  0.50 18.52 ?  28  LYS   A H    1 
ATOM   749  H HA   A LYS   A 1 28  ? 20.499 3.075   17.471  0.50 22.41 ?  28  LYS   A HA   1 
ATOM   750  H HA   B LYS   A 1 28  ? 20.463 3.084   17.489  0.50 21.39 ?  28  LYS   A HA   1 
ATOM   751  H HB2  A LYS   A 1 28  ? 18.040 4.206   16.727  0.50 24.78 ?  28  LYS   A HB2  1 
ATOM   752  H HB2  B LYS   A 1 28  ? 17.941 4.122   16.820  0.50 23.78 ?  28  LYS   A HB2  1 
ATOM   753  H HB3  A LYS   A 1 28  ? 18.823 4.745   17.999  0.50 24.78 ?  28  LYS   A HB3  1 
ATOM   754  H HB3  B LYS   A 1 28  ? 18.746 4.678   18.071  0.50 23.78 ?  28  LYS   A HB3  1 
ATOM   755  H HG2  A LYS   A 1 28  ? 20.655 5.227   16.531  0.50 27.28 ?  28  LYS   A HG2  1 
ATOM   756  H HG2  B LYS   A 1 28  ? 20.520 5.184   16.493  0.50 26.26 ?  28  LYS   A HG2  1 
ATOM   757  H HG3  A LYS   A 1 28  ? 19.663 4.935   15.323  0.50 27.28 ?  28  LYS   A HG3  1 
ATOM   758  H HG3  B LYS   A 1 28  ? 19.423 4.969   15.363  0.50 26.26 ?  28  LYS   A HG3  1 
ATOM   759  H HD2  A LYS   A 1 28  ? 19.101 6.935   17.221  0.50 30.28 ?  28  LYS   A HD2  1 
ATOM   760  H HD2  B LYS   A 1 28  ? 18.975 6.845   17.401  0.50 29.49 ?  28  LYS   A HD2  1 
ATOM   761  H HD3  A LYS   A 1 28  ? 19.899 7.258   15.883  0.50 30.28 ?  28  LYS   A HD3  1 
ATOM   762  H HD3  B LYS   A 1 28  ? 19.792 7.259   16.101  0.50 29.49 ?  28  LYS   A HD3  1 
ATOM   763  H HE2  A LYS   A 1 28  ? 18.030 6.526   14.646  0.50 32.29 ?  28  LYS   A HE2  1 
ATOM   764  H HE2  B LYS   A 1 28  ? 17.894 6.618   14.811  0.50 31.64 ?  28  LYS   A HE2  1 
ATOM   765  H HE3  A LYS   A 1 28  ? 17.234 6.350   16.013  0.50 32.29 ?  28  LYS   A HE3  1 
ATOM   766  H HE3  B LYS   A 1 28  ? 17.092 6.466   16.177  0.50 31.64 ?  28  LYS   A HE3  1 
ATOM   767  H HZ1  A LYS   A 1 28  ? 16.745 8.357   15.061  0.50 33.72 ?  28  LYS   A HZ1  1 
ATOM   768  H HZ1  B LYS   A 1 28  ? 16.730 8.518   15.266  0.50 33.12 ?  28  LYS   A HZ1  1 
ATOM   769  H HZ2  A LYS   A 1 28  ? 17.413 8.599   16.323  0.50 33.72 ?  28  LYS   A HZ2  1 
ATOM   770  H HZ2  B LYS   A 1 28  ? 17.415 8.691   16.531  0.50 33.12 ?  28  LYS   A HZ2  1 
ATOM   771  H HZ3  A LYS   A 1 28  ? 18.137 8.759   15.079  0.50 33.72 ?  28  LYS   A HZ3  1 
ATOM   772  H HZ3  B LYS   A 1 28  ? 18.144 8.830   15.287  0.50 33.12 ?  28  LYS   A HZ3  1 
ATOM   773  N N    A LYS   A 1 29  ? 17.980 1.402   18.400  0.50 20.02 ?  29  LYS   A N    1 
ATOM   774  N N    B LYS   A 1 29  ? 17.919 1.410   18.424  0.50 18.99 ?  29  LYS   A N    1 
ATOM   775  C CA   A LYS   A 1 29  ? 17.384 0.705   19.537  0.50 21.31 ?  29  LYS   A CA   1 
ATOM   776  C CA   B LYS   A 1 29  ? 17.352 0.682   19.556  0.50 20.67 ?  29  LYS   A CA   1 
ATOM   777  C C    A LYS   A 1 29  ? 18.189 -0.533  19.917  0.50 19.76 ?  29  LYS   A C    1 
ATOM   778  C C    B LYS   A 1 29  ? 18.205 -0.529  19.920  0.50 19.55 ?  29  LYS   A C    1 
ATOM   779  O O    A LYS   A 1 29  ? 18.469 -0.766  21.100  0.50 20.48 ?  29  LYS   A O    1 
ATOM   780  O O    B LYS   A 1 29  ? 18.541 -0.739  21.092  0.50 20.33 ?  29  LYS   A O    1 
ATOM   781  C CB   A LYS   A 1 29  ? 15.947 0.308   19.193  0.50 24.48 ?  29  LYS   A CB   1 
ATOM   782  C CB   B LYS   A 1 29  ? 15.926 0.241   19.220  0.50 24.02 ?  29  LYS   A CB   1 
ATOM   783  C CG   A LYS   A 1 29  ? 15.193 -0.380  20.319  0.50 27.64 ?  29  LYS   A CG   1 
ATOM   784  C CG   B LYS   A 1 29  ? 15.216 -0.501  20.343  0.50 27.34 ?  29  LYS   A CG   1 
ATOM   785  C CD   A LYS   A 1 29  ? 14.820 0.604   21.414  0.50 30.49 ?  29  LYS   A CD   1 
ATOM   786  C CD   B LYS   A 1 29  ? 14.903 0.427   21.503  0.50 30.29 ?  29  LYS   A CD   1 
ATOM   787  C CE   A LYS   A 1 29  ? 13.928 -0.044  22.460  0.50 32.31 ?  29  LYS   A CE   1 
ATOM   788  C CE   B LYS   A 1 29  ? 14.065 -0.268  22.563  0.50 32.18 ?  29  LYS   A CE   1 
ATOM   789  N NZ   A LYS   A 1 29  ? 13.463 0.940   23.474  0.50 33.45 ?  29  LYS   A NZ   1 
ATOM   790  N NZ   B LYS   A 1 29  ? 13.600 0.686   23.608  0.50 33.36 ?  29  LYS   A NZ   1 
ATOM   791  H H    A LYS   A 1 29  ? 17.617 1.218   17.642  0.50 24.04 ?  29  LYS   A H    1 
ATOM   792  H H    B LYS   A 1 29  ? 17.484 1.316   17.686  0.50 22.81 ?  29  LYS   A H    1 
ATOM   793  H HA   A LYS   A 1 29  ? 17.361 1.299   20.301  0.50 25.59 ?  29  LYS   A HA   1 
ATOM   794  H HA   B LYS   A 1 29  ? 17.312 1.265   20.327  0.50 24.83 ?  29  LYS   A HA   1 
ATOM   795  H HB2  A LYS   A 1 29  ? 15.452 1.107   18.955  0.50 29.40 ?  29  LYS   A HB2  1 
ATOM   796  H HB2  B LYS   A 1 29  ? 15.397 1.027   19.011  0.50 28.84 ?  29  LYS   A HB2  1 
ATOM   797  H HB3  A LYS   A 1 29  ? 15.964 -0.301  18.438  0.50 29.40 ?  29  LYS   A HB3  1 
ATOM   798  H HB3  B LYS   A 1 29  ? 15.952 -0.349  18.451  0.50 28.84 ?  29  LYS   A HB3  1 
ATOM   799  H HG2  A LYS   A 1 29  ? 14.375 -0.764  19.966  0.50 33.19 ?  29  LYS   A HG2  1 
ATOM   800  H HG2  B LYS   A 1 29  ? 14.379 -0.860  20.009  0.50 32.83 ?  29  LYS   A HG2  1 
ATOM   801  H HG3  A LYS   A 1 29  ? 15.745 -1.076  20.709  0.50 33.19 ?  29  LYS   A HG3  1 
ATOM   802  H HG3  B LYS   A 1 29  ? 15.779 -1.221  20.670  0.50 32.83 ?  29  LYS   A HG3  1 
ATOM   803  H HD2  A LYS   A 1 29  ? 15.626 0.917   21.852  0.50 36.61 ?  29  LYS   A HD2  1 
ATOM   804  H HD2  B LYS   A 1 29  ? 15.732 0.718   21.914  0.50 36.37 ?  29  LYS   A HD2  1 
ATOM   805  H HD3  A LYS   A 1 29  ? 14.339 1.350   21.023  0.50 36.61 ?  29  LYS   A HD3  1 
ATOM   806  H HD3  B LYS   A 1 29  ? 14.405 1.193   21.175  0.50 36.37 ?  29  LYS   A HD3  1 
ATOM   807  H HE2  A LYS   A 1 29  ? 13.148 -0.423  22.024  0.50 38.79 ?  29  LYS   A HE2  1 
ATOM   808  H HE2  B LYS   A 1 29  ? 13.285 -0.664  22.145  0.50 38.64 ?  29  LYS   A HE2  1 
ATOM   809  H HE3  A LYS   A 1 29  ? 14.426 -0.740  22.917  0.50 38.79 ?  29  LYS   A HE3  1 
ATOM   810  H HE3  B LYS   A 1 29  ? 14.599 -0.954  22.994  0.50 38.64 ?  29  LYS   A HE3  1 
ATOM   811  H HZ1  A LYS   A 1 29  ? 12.944 0.536   24.074  0.50 40.16 ?  29  LYS   A HZ1  1 
ATOM   812  H HZ1  B LYS   A 1 29  ? 13.112 0.257   24.216  0.50 40.05 ?  29  LYS   A HZ1  1 
ATOM   813  H HZ2  A LYS   A 1 29  ? 14.162 1.299   23.892  0.50 40.16 ?  29  LYS   A HZ2  1 
ATOM   814  H HZ2  B LYS   A 1 29  ? 14.300 1.061   24.010  0.50 40.05 ?  29  LYS   A HZ2  1 
ATOM   815  H HZ3  A LYS   A 1 29  ? 12.998 1.588   23.078  0.50 40.16 ?  29  LYS   A HZ3  1 
ATOM   816  H HZ3  B LYS   A 1 29  ? 13.103 1.324   23.237  0.50 40.05 ?  29  LYS   A HZ3  1 
ATOM   817  N N    . VAL   A 1 30  ? 18.550 -1.348  18.927  1.00 18.54 ?  30  VAL   A N    1 
ATOM   818  C CA   . VAL   A 1 30  ? 19.198 -2.625  19.200  1.00 17.48 ?  30  VAL   A CA   1 
ATOM   819  C C    . VAL   A 1 30  ? 20.703 -2.479  19.416  1.00 16.53 ?  30  VAL   A C    1 
ATOM   820  O O    . VAL   A 1 30  ? 21.293 -3.220  20.210  1.00 17.20 ?  30  VAL   A O    1 
ATOM   821  C CB   . VAL   A 1 30  ? 18.877 -3.586  18.042  1.00 17.79 ?  30  VAL   A CB   1 
ATOM   822  C CG1  . VAL   A 1 30  ? 19.615 -4.905  18.208  1.00 18.26 ?  30  VAL   A CG1  1 
ATOM   823  C CG2  . VAL   A 1 30  ? 17.369 -3.809  17.939  1.00 18.63 ?  30  VAL   A CG2  1 
ATOM   824  H H    A VAL   A 1 30  ? 18.421 -1.190  18.090  0.50 22.27 ?  30  VAL   A H    1 
ATOM   825  H H    B VAL   A 1 30  ? 18.415 -1.191  18.090  0.50 22.27 ?  30  VAL   A H    1 
ATOM   826  H HA   . VAL   A 1 30  ? 18.815 -3.002  20.004  1.00 21.00 ?  30  VAL   A HA   1 
ATOM   827  H HB   . VAL   A 1 30  ? 19.172 -3.187  17.207  1.00 21.37 ?  30  VAL   A HB   1 
ATOM   828  H HG11 . VAL   A 1 30  ? 19.232 -5.558  17.599  1.00 21.94 ?  30  VAL   A HG11 1 
ATOM   829  H HG12 . VAL   A 1 30  ? 20.551 -4.773  18.005  1.00 21.94 ?  30  VAL   A HG12 1 
ATOM   830  H HG13 . VAL   A 1 30  ? 19.508 -5.209  19.123  1.00 21.94 ?  30  VAL   A HG13 1 
ATOM   831  H HG21 . VAL   A 1 30  ? 17.192 -4.477  17.257  1.00 22.37 ?  30  VAL   A HG21 1 
ATOM   832  H HG22 . VAL   A 1 30  ? 17.037 -4.119  18.797  1.00 22.37 ?  30  VAL   A HG22 1 
ATOM   833  H HG23 . VAL   A 1 30  ? 16.939 -2.973  17.701  1.00 22.37 ?  30  VAL   A HG23 1 
ATOM   834  N N    . LYS   A 1 31  ? 21.345 -1.535  18.737  1.00 15.66 ?  31  LYS   A N    1 
ATOM   835  C CA   . LYS   A 1 31  ? 22.799 -1.435  18.696  1.00 16.51 ?  31  LYS   A CA   1 
ATOM   836  C C    . LYS   A 1 31  ? 23.399 -2.788  18.302  1.00 14.92 ?  31  LYS   A C    1 
ATOM   837  O O    . LYS   A 1 31  ? 24.188 -3.370  19.052  1.00 15.75 ?  31  LYS   A O    1 
ATOM   838  C CB   . LYS   A 1 31  ? 23.380 -0.934  20.010  1.00 21.76 ?  31  LYS   A CB   1 
ATOM   839  C CG   . LYS   A 1 31  ? 22.695 0.320   20.536  1.00 29.27 ?  31  LYS   A CG   1 
ATOM   840  C CD   . LYS   A 1 31  ? 23.696 1.357   21.026  1.00 35.07 ?  31  LYS   A CD   1 
ATOM   841  C CE   . LYS   A 1 31  ? 23.023 2.428   21.876  1.00 38.43 ?  31  LYS   A CE   1 
ATOM   842  N NZ   . LYS   A 1 31  ? 21.946 3.161   21.153  1.00 40.67 ?  31  LYS   A NZ   1 
ATOM   843  H H    . LYS   A 1 31  ? 20.950 -0.920  18.289  1.00 18.81 ?  31  LYS   A H    1 
ATOM   844  H HA   . LYS   A 1 31  ? 23.042 -0.799  18.012  1.00 19.83 ?  31  LYS   A HA   1 
ATOM   845  H HB2  . LYS   A 1 31  ? 23.294 -1.627  20.681  1.00 26.13 ?  31  LYS   A HB2  1 
ATOM   846  H HB3  . LYS   A 1 31  ? 24.321 -0.723  19.876  1.00 26.13 ?  31  LYS   A HB3  1 
ATOM   847  H HG2  . LYS   A 1 31  ? 22.171 0.719   19.824  1.00 35.14 ?  31  LYS   A HG2  1 
ATOM   848  H HG3  . LYS   A 1 31  ? 22.121 0.080   21.280  1.00 35.14 ?  31  LYS   A HG3  1 
ATOM   849  H HD2  . LYS   A 1 31  ? 24.372 0.919   21.567  1.00 42.10 ?  31  LYS   A HD2  1 
ATOM   850  H HD3  . LYS   A 1 31  ? 24.108 1.790   20.261  1.00 42.10 ?  31  LYS   A HD3  1 
ATOM   851  H HE2  . LYS   A 1 31  ? 22.626 2.008   22.655  1.00 46.14 ?  31  LYS   A HE2  1 
ATOM   852  H HE3  . LYS   A 1 31  ? 23.689 3.076   22.153  1.00 46.14 ?  31  LYS   A HE3  1 
ATOM   853  H HZ1  . LYS   A 1 31  ? 21.585 3.776   21.687  1.00 48.82 ?  31  LYS   A HZ1  1 
ATOM   854  H HZ2  . LYS   A 1 31  ? 22.281 3.565   20.434  1.00 48.82 ?  31  LYS   A HZ2  1 
ATOM   855  H HZ3  . LYS   A 1 31  ? 21.310 2.594   20.896  1.00 48.82 ?  31  LYS   A HZ3  1 
ATOM   856  N N    . PRO   A 1 32  ? 23.031 -3.310  17.140  1.00 13.06 ?  32  PRO   A N    1 
ATOM   857  C CA   . PRO   A 1 32  ? 23.498 -4.637  16.748  1.00 13.25 ?  32  PRO   A CA   1 
ATOM   858  C C    . PRO   A 1 32  ? 24.999 -4.647  16.534  1.00 13.28 ?  32  PRO   A C    1 
ATOM   859  O O    . PRO   A 1 32  ? 25.636 -3.615  16.314  1.00 13.26 ?  32  PRO   A O    1 
ATOM   860  C CB   . PRO   A 1 32  ? 22.756 -4.887  15.431  1.00 13.93 ?  32  PRO   A CB   1 
ATOM   861  C CG   . PRO   A 1 32  ? 22.571 -3.504  14.868  1.00 12.51 ?  32  PRO   A CG   1 
ATOM   862  C CD   . PRO   A 1 32  ? 22.279 -2.649  16.061  1.00 12.19 ?  32  PRO   A CD   1 
ATOM   863  H HA   . PRO   A 1 32  ? 23.253 -5.308  17.402  1.00 15.92 ?  32  PRO   A HA   1 
ATOM   864  H HB2  . PRO   A 1 32  ? 23.295 -5.438  14.839  1.00 16.74 ?  32  PRO   A HB2  1 
ATOM   865  H HB3  . PRO   A 1 32  ? 21.899 -5.312  15.609  1.00 16.74 ?  32  PRO   A HB3  1 
ATOM   866  H HG2  . PRO   A 1 32  ? 23.380 -3.226  14.421  1.00 15.03 ?  32  PRO   A HG2  1 
ATOM   867  H HG3  . PRO   A 1 32  ? 21.818 -3.508  14.249  1.00 15.03 ?  32  PRO   A HG3  1 
ATOM   868  H HD2  . PRO   A 1 32  ? 22.613 -1.751  15.909  1.00 14.65 ?  32  PRO   A HD2  1 
ATOM   869  H HD3  . PRO   A 1 32  ? 21.332 -2.654  16.255  1.00 14.65 ?  32  PRO   A HD3  1 
ATOM   870  N N    . THR   A 1 33  ? 25.561 -5.852  16.578  1.00 13.48 ?  33  THR   A N    1 
ATOM   871  C CA   . THR   A 1 33  ? 26.969 -6.013  16.240  1.00 13.69 ?  33  THR   A CA   1 
ATOM   872  C C    . THR   A 1 33  ? 27.250 -5.537  14.821  1.00 12.21 ?  33  THR   A C    1 
ATOM   873  O O    . THR   A 1 33  ? 28.280 -4.897  14.567  1.00 12.26 ?  33  THR   A O    1 
ATOM   874  C CB   . THR   A 1 33  ? 27.375 -7.476  16.423  1.00 15.26 ?  33  THR   A CB   1 
ATOM   875  O OG1  . THR   A 1 33  ? 27.027 -7.890  17.747  1.00 17.33 ?  33  THR   A OG1  1 
ATOM   876  C CG2  . THR   A 1 33  ? 28.874 -7.663  16.212  1.00 16.41 ?  33  THR   A CG2  1 
ATOM   877  H H    . THR   A 1 33  ? 25.156 -6.584  16.789  1.00 16.20 ?  33  THR   A H    1 
ATOM   878  H HA   . THR   A 1 33  ? 27.505 -5.486  16.849  1.00 16.45 ?  33  THR   A HA   1 
ATOM   879  H HB   . THR   A 1 33  ? 26.907 -8.037  15.779  1.00 18.33 ?  33  THR   A HB   1 
ATOM   880  H HG1  . THR   A 1 33  ? 27.442 -7.427  18.314  1.00 20.81 ?  33  THR   A HG1  1 
ATOM   881  H HG21 . THR   A 1 33  ? 29.135 -8.570  16.450  1.00 19.71 ?  33  THR   A HG21 1 
ATOM   882  H HG22 . THR   A 1 33  ? 29.103 -7.507  15.284  1.00 19.71 ?  33  THR   A HG22 1 
ATOM   883  H HG23 . THR   A 1 33  ? 29.365 -7.041  16.770  1.00 19.71 ?  33  THR   A HG23 1 
ATOM   884  N N    . VAL   A 1 34  ? 26.347 -5.838  13.888  1.00 10.80 ?  34  VAL   A N    1 
ATOM   885  C CA   . VAL   A 1 34  ? 26.525 -5.485  12.483  1.00 9.92  ?  34  VAL   A CA   1 
ATOM   886  C C    . VAL   A 1 34  ? 25.221 -4.920  11.935  1.00 9.01  ?  34  VAL   A C    1 
ATOM   887  O O    . VAL   A 1 34  ? 24.182 -5.589  11.983  1.00 9.81  ?  34  VAL   A O    1 
ATOM   888  C CB   . VAL   A 1 34  ? 26.966 -6.685  11.625  1.00 10.51 ?  34  VAL   A CB   1 
ATOM   889  C CG1  . VAL   A 1 34  ? 27.135 -6.263  10.169  1.00 11.03 ?  34  VAL   A CG1  1 
ATOM   890  C CG2  . VAL   A 1 34  ? 28.250 -7.315  12.172  1.00 11.96 ?  34  VAL   A CG2  1 
ATOM   891  H H    . VAL   A 1 34  ? 25.614 -6.260  14.046  1.00 12.97 ?  34  VAL   A H    1 
ATOM   892  H HA   . VAL   A 1 34  ? 27.210 -4.796  12.410  1.00 11.92 ?  34  VAL   A HA   1 
ATOM   893  H HB   . VAL   A 1 34  ? 26.273 -7.359  11.656  1.00 12.63 ?  34  VAL   A HB   1 
ATOM   894  H HG11 . VAL   A 1 34  ? 27.633 -6.949  9.696   1.00 13.25 ?  34  VAL   A HG11 1 
ATOM   895  H HG12 . VAL   A 1 34  ? 26.263 -6.150  9.765   1.00 13.25 ?  34  VAL   A HG12 1 
ATOM   896  H HG13 . VAL   A 1 34  ? 27.627 -5.424  10.138  1.00 13.25 ?  34  VAL   A HG13 1 
ATOM   897  H HG21 . VAL   A 1 34  ? 28.518 -8.044  11.588  1.00 14.37 ?  34  VAL   A HG21 1 
ATOM   898  H HG22 . VAL   A 1 34  ? 28.948 -6.643  12.201  1.00 14.37 ?  34  VAL   A HG22 1 
ATOM   899  H HG23 . VAL   A 1 34  ? 28.080 -7.655  13.065  1.00 14.37 ?  34  VAL   A HG23 1 
ATOM   900  N N    . VAL   A 1 35  ? 25.285 -3.713  11.371  1.00 8.71  ?  35  VAL   A N    1 
ATOM   901  C CA   . VAL   A 1 35  ? 24.241 -3.194  10.496  1.00 8.52  ?  35  VAL   A CA   1 
ATOM   902  C C    . VAL   A 1 35  ? 24.784 -3.186  9.076   1.00 7.94  ?  35  VAL   A C    1 
ATOM   903  O O    . VAL   A 1 35  ? 25.926 -2.774  8.844   1.00 8.59  ?  35  VAL   A O    1 
ATOM   904  C CB   . VAL   A 1 35  ? 23.709 -1.805  10.923  1.00 9.01  ?  35  VAL   A CB   1 
ATOM   905  C CG1  . VAL   A 1 35  ? 24.771 -0.695  10.791  1.00 9.63  ?  35  VAL   A CG1  1 
ATOM   906  C CG2  . VAL   A 1 35  ? 22.454 -1.452  10.123  1.00 9.75  ?  35  VAL   A CG2  1 
ATOM   907  H H    . VAL   A 1 35  ? 25.938 -3.161  11.483  1.00 10.47 ?  35  VAL   A H    1 
ATOM   908  H HA   . VAL   A 1 35  ? 23.486 -3.805  10.518  1.00 10.24 ?  35  VAL   A HA   1 
ATOM   909  H HB   . VAL   A 1 35  ? 23.442 -1.843  11.855  1.00 10.84 ?  35  VAL   A HB   1 
ATOM   910  H HG11 . VAL   A 1 35  ? 24.420 0.131   11.167  1.00 11.58 ?  35  VAL   A HG11 1 
ATOM   911  H HG12 . VAL   A 1 35  ? 25.567 -0.964  11.268  1.00 11.58 ?  35  VAL   A HG12 1 
ATOM   912  H HG13 . VAL   A 1 35  ? 24.977 -0.561  9.849   1.00 11.58 ?  35  VAL   A HG13 1 
ATOM   913  H HG21 . VAL   A 1 35  ? 22.095 -0.608  10.437  1.00 11.72 ?  35  VAL   A HG21 1 
ATOM   914  H HG22 . VAL   A 1 35  ? 22.687 -1.376  9.180   1.00 11.72 ?  35  VAL   A HG22 1 
ATOM   915  H HG23 . VAL   A 1 35  ? 21.792 -2.155  10.237  1.00 11.72 ?  35  VAL   A HG23 1 
ATOM   916  N N    . VAL   A 1 36  ? 23.961 -3.626  8.128   1.00 7.97  ?  36  VAL   A N    1 
ATOM   917  C CA   . VAL   A 1 36  ? 24.328 -3.629  6.718   1.00 7.53  ?  36  VAL   A CA   1 
ATOM   918  C C    . VAL   A 1 36  ? 23.873 -2.331  6.065   1.00 7.58  ?  36  VAL   A C    1 
ATOM   919  O O    . VAL   A 1 36  ? 22.714 -1.914  6.211   1.00 8.33  ?  36  VAL   A O    1 
ATOM   920  C CB   . VAL   A 1 36  ? 23.715 -4.841  5.996   1.00 7.68  ?  36  VAL   A CB   1 
ATOM   921  C CG1  . VAL   A 1 36  ? 23.977 -4.756  4.508   1.00 8.20  ?  36  VAL   A CG1  1 
ATOM   922  C CG2  . VAL   A 1 36  ? 24.259 -6.142  6.566   1.00 8.37  ?  36  VAL   A CG2  1 
ATOM   923  H H    . VAL   A 1 36  ? 23.169 -3.945  8.279   1.00 9.58  ?  36  VAL   A H    1 
ATOM   924  H HA   . VAL   A 1 36  ? 25.296 -3.690  6.644   1.00 9.05  ?  36  VAL   A HA   1 
ATOM   925  H HB   . VAL   A 1 36  ? 22.758 -4.831  6.131   1.00 9.23  ?  36  VAL   A HB   1 
ATOM   926  H HG11 . VAL   A 1 36  ? 23.841 -5.628  4.110   1.00 9.85  ?  36  VAL   A HG11 1 
ATOM   927  H HG12 . VAL   A 1 36  ? 23.363 -4.114  4.109   1.00 9.85  ?  36  VAL   A HG12 1 
ATOM   928  H HG13 . VAL   A 1 36  ? 24.893 -4.466  4.360   1.00 9.85  ?  36  VAL   A HG13 1 
ATOM   929  H HG21 . VAL   A 1 36  ? 23.869 -6.888  6.085   1.00 10.06 ?  36  VAL   A HG21 1 
ATOM   930  H HG22 . VAL   A 1 36  ? 25.226 -6.155  6.469   1.00 10.06 ?  36  VAL   A HG22 1 
ATOM   931  H HG23 . VAL   A 1 36  ? 24.025 -6.199  7.508   1.00 10.06 ?  36  VAL   A HG23 1 
ATOM   932  N N    . ASN   A 1 37  ? 24.789 -1.708  5.323   1.00 7.49  ?  37  ASN   A N    1 
ATOM   933  C CA   . ASN   A 1 37  ? 24.469 -0.582  4.459   1.00 7.12  ?  37  ASN   A CA   1 
ATOM   934  C C    . ASN   A 1 37  ? 24.336 -1.034  3.013   1.00 7.31  ?  37  ASN   A C    1 
ATOM   935  O O    . ASN   A 1 37  ? 25.110 -1.875  2.534   1.00 7.98  ?  37  ASN   A O    1 
ATOM   936  C CB   . ASN   A 1 37  ? 25.557 0.481   4.550   1.00 7.46  ?  37  ASN   A CB   1 
ATOM   937  C CG   . ASN   A 1 37  ? 25.240 1.700   3.710   1.00 7.51  ?  37  ASN   A CG   1 
ATOM   938  O OD1  . ASN   A 1 37  ? 24.068 2.056   3.535   1.00 8.21  ?  37  ASN   A OD1  1 
ATOM   939  N ND2  . ASN   A 1 37  ? 26.277 2.342   3.190   1.00 7.94  ?  37  ASN   A ND2  1 
ATOM   940  H H    . ASN   A 1 37  ? 25.623 -1.926  5.307   1.00 9.01  ?  37  ASN   A H    1 
ATOM   941  H HA   . ASN   A 1 37  ? 23.633 -0.188  4.743   1.00 8.57  ?  37  ASN   A HA   1 
ATOM   942  H HB2  . ASN   A 1 37  ? 25.646 0.774   5.473   1.00 8.98  ?  37  ASN   A HB2  1 
ATOM   943  H HB3  . ASN   A 1 37  ? 26.400 0.110   4.241   1.00 8.98  ?  37  ASN   A HB3  1 
ATOM   944  H HD21 . ASN   A 1 37  ? 26.146 3.038   2.698   1.00 9.54  ?  37  ASN   A HD21 1 
ATOM   945  H HD22 . ASN   A 1 37  ? 27.071 2.067   3.330   1.00 9.54  ?  37  ASN   A HD22 1 
ATOM   946  N N    A ALA   A 1 38  ? 23.339 -0.458  2.329   0.50 7.38  ?  38  ALA   A N    1 
ATOM   947  N N    B ALA   A 1 38  ? 23.343 -0.473  2.321   0.50 7.79  ?  38  ALA   A N    1 
ATOM   948  C CA   A ALA   A 1 38  ? 23.129 -0.594  0.887   0.50 7.77  ?  38  ALA   A CA   1 
ATOM   949  C CA   B ALA   A 1 38  ? 23.179 -0.640  0.877   0.50 8.60  ?  38  ALA   A CA   1 
ATOM   950  C C    A ALA   A 1 38  ? 24.076 0.368   0.174   0.50 7.76  ?  38  ALA   A C    1 
ATOM   951  C C    B ALA   A 1 38  ? 24.072 0.385   0.177   0.50 8.38  ?  38  ALA   A C    1 
ATOM   952  O O    A ALA   A 1 38  ? 23.696 1.461   -0.258  0.50 8.41  ?  38  ALA   A O    1 
ATOM   953  O O    B ALA   A 1 38  ? 23.640 1.480   -0.197  0.50 8.60  ?  38  ALA   A O    1 
ATOM   954  C CB   A ALA   A 1 38  ? 21.676 -0.280  0.539   0.50 8.69  ?  38  ALA   A CB   1 
ATOM   955  C CB   B ALA   A 1 38  ? 21.716 -0.449  0.494   0.50 10.11 ?  38  ALA   A CB   1 
ATOM   956  H H    A ALA   A 1 38  ? 22.757 0.056   2.699   0.50 8.87  ?  38  ALA   A H    1 
ATOM   957  H H    B ALA   A 1 38  ? 22.742 0.030   2.680   0.50 9.37  ?  38  ALA   A H    1 
ATOM   958  H HA   A ALA   A 1 38  ? 23.327 -1.498  0.607   0.50 9.34  ?  38  ALA   A HA   1 
ATOM   959  H HA   B ALA   A 1 38  ? 23.454 -1.534  0.617   0.50 10.34 ?  38  ALA   A HA   1 
ATOM   960  H HB1  A ALA   A 1 38  ? 21.550 -0.377  -0.419  0.50 10.45 ?  38  ALA   A HB1  1 
ATOM   961  H HB1  B ALA   A 1 38  ? 21.618 -0.585  -0.460  0.50 12.15 ?  38  ALA   A HB1  1 
ATOM   962  H HB2  A ALA   A 1 38  ? 21.098 -0.900  1.011   0.50 10.45 ?  38  ALA   A HB2  1 
ATOM   963  H HB2  B ALA   A 1 38  ? 21.171 -1.091  0.978   0.50 12.15 ?  38  ALA   A HB2  1 
ATOM   964  H HB3  A ALA   A 1 38  ? 21.473 0.630   0.807   0.50 10.45 ?  38  ALA   A HB3  1 
ATOM   965  H HB3  B ALA   A 1 38  ? 21.444 0.454   0.728   0.50 12.15 ?  38  ALA   A HB3  1 
ATOM   966  N N    A ALA   A 1 39  ? 25.333 -0.044  0.062   0.50 7.62  ?  39  ALA   A N    1 
ATOM   967  N N    B ALA   A 1 39  ? 25.345 0.027   0.009   0.50 8.24  ?  39  ALA   A N    1 
ATOM   968  C CA   A ALA   A 1 39  ? 26.397 0.813   -0.431  0.50 7.38  ?  39  ALA   A CA   1 
ATOM   969  C CA   B ALA   A 1 39  ? 26.357 0.956   -0.469  0.50 8.75  ?  39  ALA   A CA   1 
ATOM   970  C C    A ALA   A 1 39  ? 26.477 0.790   -1.954  0.50 7.57  ?  39  ALA   A C    1 
ATOM   971  C C    B ALA   A 1 39  ? 26.547 0.859   -1.982  0.50 8.42  ?  39  ALA   A C    1 
ATOM   972  O O    A ALA   A 1 39  ? 25.953 -0.106  -2.620  0.50 7.92  ?  39  ALA   A O    1 
ATOM   973  O O    B ALA   A 1 39  ? 26.125 -0.098  -2.636  0.50 8.32  ?  39  ALA   A O    1 
ATOM   974  C CB   A ALA   A 1 39  ? 27.733 0.354   0.156   0.50 7.03  ?  39  ALA   A CB   1 
ATOM   975  C CB   B ALA   A 1 39  ? 27.689 0.676   0.229   0.50 10.01 ?  39  ALA   A CB   1 
ATOM   976  H H    A ALA   A 1 39  ? 25.593 -0.841  0.269   0.50 9.16  ?  39  ALA   A H    1 
ATOM   977  H H    B ALA   A 1 39  ? 25.649 -0.767  0.170   0.50 9.91  ?  39  ALA   A H    1 
ATOM   978  H HA   A ALA   A 1 39  ? 26.225 1.721   -0.145  0.50 8.88  ?  39  ALA   A HA   1 
ATOM   979  H HA   B ALA   A 1 39  ? 26.083 1.862   -0.252  0.50 10.52 ?  39  ALA   A HA   1 
ATOM   980  H HB1  A ALA   A 1 39  ? 28.433 0.938   -0.176  0.50 8.46  ?  39  ALA   A HB1  1 
ATOM   981  H HB1  B ALA   A 1 39  ? 28.352 1.306   -0.099  0.50 12.03 ?  39  ALA   A HB1  1 
ATOM   982  H HB2  A ALA   A 1 39  ? 27.684 0.415   1.124   0.50 8.46  ?  39  ALA   A HB2  1 
ATOM   983  H HB2  B ALA   A 1 39  ? 27.577 0.787   1.187   0.50 12.03 ?  39  ALA   A HB2  1 
ATOM   984  H HB3  A ALA   A 1 39  ? 27.900 -0.558  -0.113  0.50 8.46  ?  39  ALA   A HB3  1 
ATOM   985  H HB3  B ALA   A 1 39  ? 27.967 -0.230  0.030   0.50 12.03 ?  39  ALA   A HB3  1 
ATOM   986  N N    A ASN   A 1 40  ? 27.159 1.794   -2.502  0.50 8.39  ?  40  ASN   A N    1 
ATOM   987  N N    B ASN   A 1 40  ? 27.213 1.871   -2.534  0.50 8.66  ?  40  ASN   A N    1 
ATOM   988  C CA   A ASN   A 1 40  ? 27.643 1.765   -3.875  0.50 8.62  ?  40  ASN   A CA   1 
ATOM   989  C CA   B ASN   A 1 40  ? 27.775 1.807   -3.876  0.50 8.50  ?  40  ASN   A CA   1 
ATOM   990  C C    A ASN   A 1 40  ? 29.167 1.667   -3.859  0.50 8.24  ?  40  ASN   A C    1 
ATOM   991  C C    B ASN   A 1 40  ? 29.295 1.669   -3.790  0.50 7.84  ?  40  ASN   A C    1 
ATOM   992  O O    A ASN   A 1 40  ? 29.803 1.767   -2.808  0.50 8.43  ?  40  ASN   A O    1 
ATOM   993  O O    B ASN   A 1 40  ? 29.889 1.738   -2.711  0.50 7.74  ?  40  ASN   A O    1 
ATOM   994  C CB   A ASN   A 1 40  ? 27.141 2.975   -4.680  0.50 9.17  ?  40  ASN   A CB   1 
ATOM   995  C CB   B ASN   A 1 40  ? 27.327 2.999   -4.740  0.50 9.14  ?  40  ASN   A CB   1 
ATOM   996  C CG   A ASN   A 1 40  ? 27.496 4.303   -4.040  0.50 9.88  ?  40  ASN   A CG   1 
ATOM   997  C CG   B ASN   A 1 40  ? 27.741 4.342   -4.171  0.50 9.68  ?  40  ASN   A CG   1 
ATOM   998  O OD1  A ASN   A 1 40  ? 28.652 4.551   -3.686  0.50 11.60 ?  40  ASN   A OD1  1 
ATOM   999  O OD1  B ASN   A 1 40  ? 28.917 4.573   -3.874  0.50 10.03 ?  40  ASN   A OD1  1 
ATOM   1000 N ND2  A ASN   A 1 40  ? 26.495 5.164   -3.883  0.50 9.96  ?  40  ASN   A ND2  1 
ATOM   1001 N ND2  B ASN   A 1 40  ? 26.769 5.247   -4.029  0.50 10.75 ?  40  ASN   A ND2  1 
ATOM   1002 H H    A ASN   A 1 40  ? 27.369 2.515   -2.083  0.50 10.09 ?  40  ASN   A H    1 
ATOM   1003 H H    B ASN   A 1 40  ? 27.353 2.617   -2.136  0.50 10.41 ?  40  ASN   A H    1 
ATOM   1004 H HA   A ASN   A 1 40  ? 27.301 0.966   -4.310  0.50 10.36 ?  40  ASN   A HA   1 
ATOM   1005 H HA   B ASN   A 1 40  ? 27.445 1.004   -4.306  0.50 10.21 ?  40  ASN   A HA   1 
ATOM   1006 H HB2  A ASN   A 1 40  ? 27.535 2.946   -5.570  0.50 11.02 ?  40  ASN   A HB2  1 
ATOM   1007 H HB2  B ASN   A 1 40  ? 27.721 2.911   -5.622  0.50 10.98 ?  40  ASN   A HB2  1 
ATOM   1008 H HB3  A ASN   A 1 40  ? 26.174 2.922   -4.754  0.50 11.02 ?  40  ASN   A HB3  1 
ATOM   1009 H HB3  B ASN   A 1 40  ? 26.359 2.986   -4.809  0.50 10.98 ?  40  ASN   A HB3  1 
ATOM   1010 H HD21 A ASN   A 1 40  ? 26.645 5.935   -3.537  0.50 11.97 ?  40  ASN   A HD21 1 
ATOM   1011 H HD21 B ASN   A 1 40  ? 26.950 6.027   -3.715  0.50 12.92 ?  40  ASN   A HD21 1 
ATOM   1012 H HD22 A ASN   A 1 40  ? 25.700 4.950   -4.134  0.50 11.97 ?  40  ASN   A HD22 1 
ATOM   1013 H HD22 B ASN   A 1 40  ? 25.961 5.051   -4.251  0.50 12.92 ?  40  ASN   A HD22 1 
ATOM   1014 N N    A VAL   A 1 41  ? 29.761 1.433   -5.032  0.50 8.78  ?  41  VAL   A N    1 
ATOM   1015 N N    B VAL   A 1 41  ? 29.922 1.429   -4.946  0.50 8.08  ?  41  VAL   A N    1 
ATOM   1016 C CA   A VAL   A 1 41  ? 31.193 1.129   -5.074  0.50 9.26  ?  41  VAL   A CA   1 
ATOM   1017 C CA   B VAL   A 1 41  ? 31.348 1.103   -4.978  0.50 8.80  ?  41  VAL   A CA   1 
ATOM   1018 C C    A VAL   A 1 41  ? 32.061 2.281   -4.593  0.50 9.16  ?  41  VAL   A C    1 
ATOM   1019 C C    B VAL   A 1 41  ? 32.219 2.250   -4.501  0.50 8.69  ?  41  VAL   A C    1 
ATOM   1020 O O    A VAL   A 1 41  ? 33.219 2.058   -4.221  0.50 9.59  ?  41  VAL   A O    1 
ATOM   1021 O O    B VAL   A 1 41  ? 33.347 2.017   -4.051  0.50 9.30  ?  41  VAL   A O    1 
ATOM   1022 C CB   A VAL   A 1 41  ? 31.675 0.644   -6.460  0.50 10.51 ?  41  VAL   A CB   1 
ATOM   1023 C CB   B VAL   A 1 41  ? 31.805 0.618   -6.375  0.50 9.80  ?  41  VAL   A CB   1 
ATOM   1024 C CG1  A VAL   A 1 41  ? 31.031 -0.685  -6.816  0.50 11.11 ?  41  VAL   A CG1  1 
ATOM   1025 C CG1  B VAL   A 1 41  ? 31.053 -0.641  -6.777  0.50 10.29 ?  41  VAL   A CG1  1 
ATOM   1026 C CG2  A VAL   A 1 41  ? 31.440 1.703   -7.536  0.50 11.06 ?  41  VAL   A CG2  1 
ATOM   1027 C CG2  B VAL   A 1 41  ? 31.661 1.716   -7.429  0.50 10.18 ?  41  VAL   A CG2  1 
ATOM   1028 H H    A VAL   A 1 41  ? 29.366 1.440   -5.799  0.50 10.55 ?  41  VAL   A H    1 
ATOM   1029 H H    B VAL   A 1 41  ? 29.550 1.446   -5.718  0.50 9.71  ?  41  VAL   A H    1 
ATOM   1030 H HA   A VAL   A 1 41  ? 31.345 0.397   -4.460  0.50 11.13 ?  41  VAL   A HA   1 
ATOM   1031 H HA   B VAL   A 1 41  ? 31.508 0.374   -4.364  0.50 10.58 ?  41  VAL   A HA   1 
ATOM   1032 H HB   A VAL   A 1 41  ? 32.631 0.491   -6.407  0.50 12.63 ?  41  VAL   A HB   1 
ATOM   1033 H HB   B VAL   A 1 41  ? 32.747 0.387   -6.329  0.50 11.78 ?  41  VAL   A HB   1 
ATOM   1034 H HG11 A VAL   A 1 41  ? 31.379 -0.985  -7.669  0.50 13.35 ?  41  VAL   A HG11 1 
ATOM   1035 H HG11 B VAL   A 1 41  ? 31.378 -0.946  -7.638  0.50 12.37 ?  41  VAL   A HG11 1 
ATOM   1036 H HG12 A VAL   A 1 41  ? 31.245 -1.334  -6.125  0.50 13.35 ?  41  VAL   A HG12 1 
ATOM   1037 H HG12 B VAL   A 1 41  ? 31.201 -1.328  -6.106  0.50 12.37 ?  41  VAL   A HG12 1 
ATOM   1038 H HG13 A VAL   A 1 41  ? 30.071 -0.566  -6.871  0.50 13.35 ?  41  VAL   A HG13 1 
ATOM   1039 H HG13 B VAL   A 1 41  ? 30.105 -0.438  -6.836  0.50 12.37 ?  41  VAL   A HG13 1 
ATOM   1040 H HG21 A VAL   A 1 41  ? 31.717 1.345   -8.394  0.50 13.29 ?  41  VAL   A HG21 1 
ATOM   1041 H HG21 B VAL   A 1 41  ? 31.855 1.342   -8.304  0.50 12.23 ?  41  VAL   A HG21 1 
ATOM   1042 H HG22 A VAL   A 1 41  ? 30.500 1.930   -7.558  0.50 13.29 ?  41  VAL   A HG22 1 
ATOM   1043 H HG22 B VAL   A 1 41  ? 30.751 2.054   -7.410  0.50 12.23 ?  41  VAL   A HG22 1 
ATOM   1044 H HG23 A VAL   A 1 41  ? 31.968 2.490   -7.322  0.50 13.29 ?  41  VAL   A HG23 1 
ATOM   1045 H HG23 B VAL   A 1 41  ? 32.283 2.432   -7.230  0.50 12.23 ?  41  VAL   A HG23 1 
ATOM   1046 N N    A TYR   A 1 42  ? 31.546 3.512   -4.613  0.50 9.22  ?  42  TYR   A N    1 
ATOM   1047 N N    B TYR   A 1 42  ? 31.730 3.487   -4.597  0.50 9.00  ?  42  TYR   A N    1 
ATOM   1048 C CA   A TYR   A 1 42  ? 32.300 4.688   -4.193  0.50 8.98  ?  42  TYR   A CA   1 
ATOM   1049 C CA   B TYR   A 1 42  ? 32.467 4.664   -4.162  0.50 9.13  ?  42  TYR   A CA   1 
ATOM   1050 C C    A TYR   A 1 42  ? 32.058 5.059   -2.738  0.50 8.91  ?  42  TYR   A C    1 
ATOM   1051 C C    B TYR   A 1 42  ? 32.172 5.037   -2.716  0.50 8.88  ?  42  TYR   A C    1 
ATOM   1052 O O    A TYR   A 1 42  ? 32.602 6.068   -2.268  0.50 9.37  ?  42  TYR   A O    1 
ATOM   1053 O O    B TYR   A 1 42  ? 32.757 6.000   -2.203  0.50 9.48  ?  42  TYR   A O    1 
ATOM   1054 C CB   A TYR   A 1 42  ? 31.955 5.880   -5.100  0.50 9.67  ?  42  TYR   A CB   1 
ATOM   1055 C CB   B TYR   A 1 42  ? 32.155 5.858   -5.085  0.50 10.43 ?  42  TYR   A CB   1 
ATOM   1056 C CG   A TYR   A 1 42  ? 32.203 5.568   -6.554  0.50 10.68 ?  42  TYR   A CG   1 
ATOM   1057 C CG   B TYR   A 1 42  ? 32.239 5.543   -6.569  0.50 11.46 ?  42  TYR   A CG   1 
ATOM   1058 C CD1  A TYR   A 1 42  ? 33.493 5.391   -7.028  0.50 11.29 ?  42  TYR   A CD1  1 
ATOM   1059 C CD1  B TYR   A 1 42  ? 33.460 5.305   -7.182  0.50 12.01 ?  42  TYR   A CD1  1 
ATOM   1060 C CD2  A TYR   A 1 42  ? 31.151 5.404   -7.443  0.50 11.89 ?  42  TYR   A CD2  1 
ATOM   1061 C CD2  B TYR   A 1 42  ? 31.095 5.482   -7.355  0.50 12.60 ?  42  TYR   A CD2  1 
ATOM   1062 C CE1  A TYR   A 1 42  ? 33.732 5.078   -8.351  0.50 12.08 ?  42  TYR   A CE1  1 
ATOM   1063 C CE1  B TYR   A 1 42  ? 33.541 5.010   -8.535  0.50 12.61 ?  42  TYR   A CE1  1 
ATOM   1064 C CE2  A TYR   A 1 42  ? 31.380 5.097   -8.771  0.50 12.75 ?  42  TYR   A CE2  1 
ATOM   1065 C CE2  B TYR   A 1 42  ? 31.166 5.196   -8.711  0.50 13.34 ?  42  TYR   A CE2  1 
ATOM   1066 C CZ   A TYR   A 1 42  ? 32.673 4.933   -9.218  0.50 12.95 ?  42  TYR   A CZ   1 
ATOM   1067 C CZ   B TYR   A 1 42  ? 32.394 4.959   -9.294  0.50 13.42 ?  42  TYR   A CZ   1 
ATOM   1068 O OH   A TYR   A 1 42  ? 32.902 4.622   -10.539 0.50 14.40 ?  42  TYR   A OH   1 
ATOM   1069 O OH   B TYR   A 1 42  ? 32.478 4.670   -10.640 0.50 14.30 ?  42  TYR   A OH   1 
ATOM   1070 H H    A TYR   A 1 42  ? 30.748 3.697   -4.882  0.50 11.08 ?  42  TYR   A H    1 
ATOM   1071 H H    B TYR   A 1 42  ? 30.954 3.673   -4.916  0.50 10.82 ?  42  TYR   A H    1 
ATOM   1072 H HA   A TYR   A 1 42  ? 33.244 4.508   -4.309  0.50 10.80 ?  42  TYR   A HA   1 
ATOM   1073 H HA   B TYR   A 1 42  ? 33.416 4.490   -4.221  0.50 10.97 ?  42  TYR   A HA   1 
ATOM   1074 H HB2  A TYR   A 1 42  ? 31.016 6.106   -4.992  0.50 11.62 ?  42  TYR   A HB2  1 
ATOM   1075 H HB2  B TYR   A 1 42  ? 31.257 6.171   -4.904  0.50 12.54 ?  42  TYR   A HB2  1 
ATOM   1076 H HB3  A TYR   A 1 42  ? 32.508 6.643   -4.854  0.50 11.62 ?  42  TYR   A HB3  1 
ATOM   1077 H HB3  B TYR   A 1 42  ? 32.792 6.570   -4.904  0.50 12.54 ?  42  TYR   A HB3  1 
ATOM   1078 H HD1  A TYR   A 1 42  ? 34.212 5.488   -6.443  0.50 13.57 ?  42  TYR   A HD1  1 
ATOM   1079 H HD1  B TYR   A 1 42  ? 34.240 5.335   -6.677  0.50 14.44 ?  42  TYR   A HD1  1 
ATOM   1080 H HD2  A TYR   A 1 42  ? 30.276 5.515   -7.142  0.50 14.28 ?  42  TYR   A HD2  1 
ATOM   1081 H HD2  B TYR   A 1 42  ? 30.266 5.641   -6.967  0.50 15.14 ?  42  TYR   A HD2  1 
ATOM   1082 H HE1  A TYR   A 1 42  ? 34.605 4.970   -8.653  0.50 14.51 ?  42  TYR   A HE1  1 
ATOM   1083 H HE1  B TYR   A 1 42  ? 34.368 4.852   -8.932  0.50 15.15 ?  42  TYR   A HE1  1 
ATOM   1084 H HE2  A TYR   A 1 42  ? 30.666 4.996   -9.358  0.50 15.32 ?  42  TYR   A HE2  1 
ATOM   1085 H HE2  B TYR   A 1 42  ? 30.389 5.157   -9.225  0.50 16.02 ?  42  TYR   A HE2  1 
ATOM   1086 H HH   A TYR   A 1 42  ? 33.724 4.509   -10.668 0.50 17.30 ?  42  TYR   A HH   1 
ATOM   1087 H HH   B TYR   A 1 42  ? 33.281 4.547   -10.860 0.50 17.18 ?  42  TYR   A HH   1 
ATOM   1088 N N    A LEU   A 1 43  ? 31.254 4.272   -2.023  0.50 8.51  ?  43  LEU   A N    1 
ATOM   1089 N N    B LEU   A 1 43  ? 31.282 4.297   -2.052  0.50 8.66  ?  43  LEU   A N    1 
ATOM   1090 C CA   A LEU   A 1 43  ? 30.812 4.604   -0.667  0.50 8.36  ?  43  LEU   A CA   1 
ATOM   1091 C CA   B LEU   A 1 43  ? 30.826 4.622   -0.699  0.50 8.74  ?  43  LEU   A CA   1 
ATOM   1092 C C    A LEU   A 1 43  ? 30.304 6.041   -0.574  0.50 8.22  ?  43  LEU   A C    1 
ATOM   1093 C C    B LEU   A 1 43  ? 30.395 6.085   -0.587  0.50 8.92  ?  43  LEU   A C    1 
ATOM   1094 O O    A LEU   A 1 43  ? 30.506 6.732   0.428   0.50 8.64  ?  43  LEU   A O    1 
ATOM   1095 O O    B LEU   A 1 43  ? 30.753 6.796   0.355   0.50 9.69  ?  43  LEU   A O    1 
ATOM   1096 C CB   A LEU   A 1 43  ? 31.875 4.312   0.392   0.50 8.50  ?  43  LEU   A CB   1 
ATOM   1097 C CB   B LEU   A 1 43  ? 31.869 4.272   0.361   0.50 8.92  ?  43  LEU   A CB   1 
ATOM   1098 C CG   A LEU   A 1 43  ? 32.341 2.858   0.522   0.50 8.95  ?  43  LEU   A CG   1 
ATOM   1099 C CG   B LEU   A 1 43  ? 32.365 2.824   0.390   0.50 9.16  ?  43  LEU   A CG   1 
ATOM   1100 C CD1  A LEU   A 1 43  ? 33.357 2.735   1.654   0.50 9.37  ?  43  LEU   A CD1  1 
ATOM   1101 C CD1  B LEU   A 1 43  ? 33.475 2.684   1.421   0.50 9.62  ?  43  LEU   A CD1  1 
ATOM   1102 C CD2  A LEU   A 1 43  ? 31.176 1.899   0.739   0.50 9.27  ?  43  LEU   A CD2  1 
ATOM   1103 C CD2  B LEU   A 1 43  ? 31.240 1.839   0.678   0.50 9.28  ?  43  LEU   A CD2  1 
ATOM   1104 H H    A LEU   A 1 43  ? 30.933 3.525   -2.309  0.50 10.23 ?  43  LEU   A H    1 
ATOM   1105 H H    B LEU   A 1 43  ? 30.916 3.581   -2.368  0.50 10.41 ?  43  LEU   A H    1 
ATOM   1106 H HA   A LEU   A 1 43  ? 30.054 4.040   -0.463  0.50 10.05 ?  43  LEU   A HA   1 
ATOM   1107 H HA   B LEU   A 1 43  ? 30.045 4.075   -0.509  0.50 10.50 ?  43  LEU   A HA   1 
ATOM   1108 H HB2  A LEU   A 1 43  ? 32.659 4.846   0.202   0.50 10.22 ?  43  LEU   A HB2  1 
ATOM   1109 H HB2  B LEU   A 1 43  ? 32.642 4.836   0.223   0.50 10.73 ?  43  LEU   A HB2  1 
ATOM   1110 H HB3  A LEU   A 1 43  ? 31.513 4.566   1.256   0.50 10.22 ?  43  LEU   A HB3  1 
ATOM   1111 H HB3  B LEU   A 1 43  ? 31.486 4.458   1.234   0.50 10.73 ?  43  LEU   A HB3  1 
ATOM   1112 H HG   A LEU   A 1 43  ? 32.785 2.597   -0.298  0.50 10.76 ?  43  LEU   A HG   1 
ATOM   1113 H HG   B LEU   A 1 43  ? 32.736 2.601   -0.477  0.50 11.01 ?  43  LEU   A HG   1 
ATOM   1114 H HD11 A LEU   A 1 43  ? 33.645 1.811   1.724   0.50 11.26 ?  43  LEU   A HD11 1 
ATOM   1115 H HD11 B LEU   A 1 43  ? 33.783 1.764   1.433   0.50 11.56 ?  43  LEU   A HD11 1 
ATOM   1116 H HD12 A LEU   A 1 43  ? 34.118 3.304   1.457   0.50 11.26 ?  43  LEU   A HD12 1 
ATOM   1117 H HD12 B LEU   A 1 43  ? 34.205 3.275   1.180   0.50 11.56 ?  43  LEU   A HD12 1 
ATOM   1118 H HD13 A LEU   A 1 43  ? 32.942 3.016   2.485   0.50 11.26 ?  43  LEU   A HD13 1 
ATOM   1119 H HD13 B LEU   A 1 43  ? 33.128 2.928   2.294   0.50 11.56 ?  43  LEU   A HD13 1 
ATOM   1120 H HD21 A LEU   A 1 43  ? 31.527 1.015   0.938   0.50 11.14 ?  43  LEU   A HD21 1 
ATOM   1121 H HD21 B LEU   A 1 43  ? 31.613 0.946   0.754   0.50 11.15 ?  43  LEU   A HD21 1 
ATOM   1122 H HD22 A LEU   A 1 43  ? 30.641 2.216   1.483   0.50 11.14 ?  43  LEU   A HD22 1 
ATOM   1123 H HD22 B LEU   A 1 43  ? 30.810 2.087   1.513   0.50 11.15 ?  43  LEU   A HD22 1 
ATOM   1124 H HD23 A LEU   A 1 43  ? 30.639 1.867   -0.067  0.50 11.14 ?  43  LEU   A HD23 1 
ATOM   1125 H HD23 B LEU   A 1 43  ? 30.598 1.870   -0.047  0.50 11.15 ?  43  LEU   A HD23 1 
ATOM   1126 N N    A LYS   A 1 44  ? 29.616 6.489   -1.627  0.50 8.04  ?  44  LYS   A N    1 
ATOM   1127 N N    B LYS   A 1 44  ? 29.613 6.539   -1.567  0.50 9.13  ?  44  LYS   A N    1 
ATOM   1128 C CA   A LYS   A 1 44  ? 28.945 7.785   -1.633  0.50 8.48  ?  44  LYS   A CA   1 
ATOM   1129 C CA   B LYS   A 1 44  ? 29.017 7.874   -1.544  0.50 10.02 ?  44  LYS   A CA   1 
ATOM   1130 C C    A LYS   A 1 44  ? 27.526 7.571   -1.126  0.50 8.06  ?  44  LYS   A C    1 
ATOM   1131 C C    B LYS   A 1 44  ? 27.587 7.720   -1.042  0.50 9.13  ?  44  LYS   A C    1 
ATOM   1132 O O    A LYS   A 1 44  ? 26.676 7.018   -1.835  0.50 8.61  ?  44  LYS   A O    1 
ATOM   1133 O O    B LYS   A 1 44  ? 26.699 7.279   -1.777  0.50 9.69  ?  44  LYS   A O    1 
ATOM   1134 C CB   A LYS   A 1 44  ? 28.954 8.410   -3.026  0.50 10.45 ?  44  LYS   A CB   1 
ATOM   1135 C CB   B LYS   A 1 44  ? 29.072 8.525   -2.923  0.50 12.27 ?  44  LYS   A CB   1 
ATOM   1136 C CG   A LYS   A 1 44  ? 30.308 8.948   -3.461  0.50 13.71 ?  44  LYS   A CG   1 
ATOM   1137 C CG   B LYS   A 1 44  ? 30.477 8.885   -3.390  0.50 15.11 ?  44  LYS   A CG   1 
ATOM   1138 C CD   A LYS   A 1 44  ? 30.958 9.826   -2.395  0.50 18.44 ?  44  LYS   A CD   1 
ATOM   1139 C CD   B LYS   A 1 44  ? 31.214 9.765   -2.386  0.50 18.86 ?  44  LYS   A CD   1 
ATOM   1140 C CE   A LYS   A 1 44  ? 32.275 10.402  -2.886  0.50 20.93 ?  44  LYS   A CE   1 
ATOM   1141 C CE   B LYS   A 1 44  ? 32.640 10.034  -2.824  0.50 21.00 ?  44  LYS   A CE   1 
ATOM   1142 N NZ   A LYS   A 1 44  ? 33.058 11.056  -1.802  0.50 22.43 ?  44  LYS   A NZ   1 
ATOM   1143 N NZ   B LYS   A 1 44  ? 33.423 10.702  -1.753  0.50 21.59 ?  44  LYS   A NZ   1 
ATOM   1144 H H    A LYS   A 1 44  ? 29.521 6.048   -2.360  0.50 9.67  ?  44  LYS   A H    1 
ATOM   1145 H H    B LYS   A 1 44  ? 29.420 6.090   -2.275  0.50 10.98 ?  44  LYS   A H    1 
ATOM   1146 H HA   A LYS   A 1 44  ? 29.380 8.379   -1.007  0.50 10.20 ?  44  LYS   A HA   1 
ATOM   1147 H HA   B LYS   A 1 44  ? 29.490 8.432   -0.906  0.50 12.04 ?  44  LYS   A HA   1 
ATOM   1148 H HB2  A LYS   A 1 44  ? 28.681 7.738   -3.673  0.50 12.56 ?  44  LYS   A HB2  1 
ATOM   1149 H HB2  B LYS   A 1 44  ? 28.692 7.910   -3.571  0.50 14.75 ?  44  LYS   A HB2  1 
ATOM   1150 H HB3  A LYS   A 1 44  ? 28.325 9.150   -3.042  0.50 12.56 ?  44  LYS   A HB3  1 
ATOM   1151 H HB3  B LYS   A 1 44  ? 28.548 9.342   -2.903  0.50 14.75 ?  44  LYS   A HB3  1 
ATOM   1152 H HG2  A LYS   A 1 44  ? 30.902 8.203   -3.644  0.50 16.47 ?  44  LYS   A HG2  1 
ATOM   1153 H HG2  B LYS   A 1 44  ? 30.987 8.070   -3.514  0.50 18.15 ?  44  LYS   A HG2  1 
ATOM   1154 H HG3  A LYS   A 1 44  ? 30.195 9.486   -4.263  0.50 16.47 ?  44  LYS   A HG3  1 
ATOM   1155 H HG3  B LYS   A 1 44  ? 30.414 9.370   -4.230  0.50 18.15 ?  44  LYS   A HG3  1 
ATOM   1156 H HD2  A LYS   A 1 44  ? 30.357 10.552  -2.169  0.50 22.15 ?  44  LYS   A HD2  1 
ATOM   1157 H HD2  B LYS   A 1 44  ? 30.740 10.609  -2.300  0.50 22.65 ?  44  LYS   A HD2  1 
ATOM   1158 H HD3  A LYS   A 1 44  ? 31.149 9.287   -1.609  0.50 22.15 ?  44  LYS   A HD3  1 
ATOM   1159 H HD3  B LYS   A 1 44  ? 31.250 9.314   -1.528  0.50 22.65 ?  44  LYS   A HD3  1 
ATOM   1160 H HE2  A LYS   A 1 44  ? 32.815 9.681   -3.252  0.50 25.13 ?  44  LYS   A HE2  1 
ATOM   1161 H HE2  B LYS   A 1 44  ? 33.069 9.192   -3.036  0.50 25.22 ?  44  LYS   A HE2  1 
ATOM   1162 H HE3  A LYS   A 1 44  ? 32.095 11.061  -3.568  0.50 25.13 ?  44  LYS   A HE3  1 
ATOM   1163 H HE3  B LYS   A 1 44  ? 32.626 10.612  -3.601  0.50 25.22 ?  44  LYS   A HE3  1 
ATOM   1164 H HZ1  A LYS   A 1 44  ? 33.821 11.378  -2.132  0.50 26.94 ?  44  LYS   A HZ1  1 
ATOM   1165 H HZ1  B LYS   A 1 44  ? 34.253 10.852  -2.033  0.50 25.93 ?  44  LYS   A HZ1  1 
ATOM   1166 H HZ2  A LYS   A 1 44  ? 32.591 11.726  -1.450  0.50 26.94 ?  44  LYS   A HZ2  1 
ATOM   1167 H HZ2  B LYS   A 1 44  ? 33.044 11.482  -1.541  0.50 25.93 ?  44  LYS   A HZ2  1 
ATOM   1168 H HZ3  A LYS   A 1 44  ? 33.248 10.467  -1.162  0.50 26.94 ?  44  LYS   A HZ3  1 
ATOM   1169 H HZ3  B LYS   A 1 44  ? 33.448 10.189  -1.027  0.50 25.93 ?  44  LYS   A HZ3  1 
ATOM   1170 N N    A HIS   A 1 45  ? 27.278 7.989   0.109   0.50 7.74  ?  45  HIS   A N    1 
ATOM   1171 N N    B HIS   A 1 45  ? 27.366 8.080   0.222   0.50 8.97  ?  45  HIS   A N    1 
ATOM   1172 C CA   A HIS   A 1 45  ? 26.059 7.620   0.824   0.50 7.60  ?  45  HIS   A CA   1 
ATOM   1173 C CA   B HIS   A 1 45  ? 26.107 7.771   0.901   0.50 9.38  ?  45  HIS   A CA   1 
ATOM   1174 C C    A HIS   A 1 45  ? 25.003 8.716   0.662   0.50 7.92  ?  45  HIS   A C    1 
ATOM   1175 C C    B HIS   A 1 45  ? 25.155 8.954   0.745   0.50 10.29 ?  45  HIS   A C    1 
ATOM   1176 O O    A HIS   A 1 45  ? 24.659 9.445   1.592   0.50 8.51  ?  45  HIS   A O    1 
ATOM   1177 O O    B HIS   A 1 45  ? 24.941 9.748   1.662   0.50 11.24 ?  45  HIS   A O    1 
ATOM   1178 C CB   A HIS   A 1 45  ? 26.385 7.357   2.287   0.50 7.39  ?  45  HIS   A CB   1 
ATOM   1179 C CB   B HIS   A 1 45  ? 26.359 7.476   2.370   0.50 8.91  ?  45  HIS   A CB   1 
ATOM   1180 C CG   A HIS   A 1 45  ? 27.489 6.369   2.485   0.50 7.04  ?  45  HIS   A CG   1 
ATOM   1181 C CG   B HIS   A 1 45  ? 27.481 6.521   2.615   0.50 8.43  ?  45  HIS   A CG   1 
ATOM   1182 N ND1  A HIS   A 1 45  ? 27.455 5.095   1.953   0.50 6.94  ?  45  HIS   A ND1  1 
ATOM   1183 N ND1  B HIS   A 1 45  ? 27.486 5.231   2.128   0.50 9.07  ?  45  HIS   A ND1  1 
ATOM   1184 C CD2  A HIS   A 1 45  ? 28.665 6.475   3.150   0.50 7.85  ?  45  HIS   A CD2  1 
ATOM   1185 C CD2  B HIS   A 1 45  ? 28.635 6.672   3.307   0.50 7.82  ?  45  HIS   A CD2  1 
ATOM   1186 C CE1  A HIS   A 1 45  ? 28.566 4.462   2.287   0.50 7.50  ?  45  HIS   A CE1  1 
ATOM   1187 C CE1  B HIS   A 1 45  ? 28.603 4.632   2.505   0.50 7.86  ?  45  HIS   A CE1  1 
ATOM   1188 N NE2  A HIS   A 1 45  ? 29.315 5.274   3.014   0.50 8.16  ?  45  HIS   A NE2  1 
ATOM   1189 N NE2  B HIS   A 1 45  ? 29.316 5.484   3.222   0.50 7.47  ?  45  HIS   A NE2  1 
ATOM   1190 H H    A HIS   A 1 45  ? 27.806 8.487   0.569   0.50 9.31  ?  45  HIS   A H    1 
ATOM   1191 H H    B HIS   A 1 45  ? 27.928 8.517   0.708   0.50 10.79 ?  45  HIS   A H    1 
ATOM   1192 H HA   A HIS   A 1 45  ? 25.699 6.803   0.447   0.50 9.14  ?  45  HIS   A HA   1 
ATOM   1193 H HA   B HIS   A 1 45  ? 25.702 6.992   0.491   0.50 11.28 ?  45  HIS   A HA   1 
ATOM   1194 H HB2  A HIS   A 1 45  ? 26.648 8.187   2.709   0.50 8.88  ?  45  HIS   A HB2  1 
ATOM   1195 H HB2  B HIS   A 1 45  ? 26.569 8.306   2.823   0.50 10.71 ?  45  HIS   A HB2  1 
ATOM   1196 H HB3  A HIS   A 1 45  ? 25.592 7.002   2.729   0.50 8.88  ?  45  HIS   A HB3  1 
ATOM   1197 H HB3  B HIS   A 1 45  ? 25.553 7.089   2.749   0.50 10.71 ?  45  HIS   A HB3  1 
ATOM   1198 H HD2  A HIS   A 1 45  ? 28.980 7.218   3.614   0.50 9.44  ?  45  HIS   A HD2  1 
ATOM   1199 H HD2  B HIS   A 1 45  ? 28.918 7.438   3.752   0.50 9.40  ?  45  HIS   A HD2  1 
ATOM   1200 H HE1  A HIS   A 1 45  ? 28.782 3.582   2.061   0.50 9.01  ?  45  HIS   A HE1  1 
ATOM   1201 H HE1  B HIS   A 1 45  ? 28.840 3.755   2.304   0.50 9.46  ?  45  HIS   A HE1  1 
ATOM   1202 H HE2  A HIS   A 1 45  ? 30.088 5.076   3.347   0.50 9.82  ?  45  HIS   A HE2  1 
ATOM   1203 H HE2  B HIS   A 1 45  ? 30.080 5.316   3.578   0.50 8.98  ?  45  HIS   A HE2  1 
ATOM   1204 N N    A GLY   A 1 46  ? 24.456 8.792   -0.547  0.50 8.90  ?  46  GLY   A N    1 
ATOM   1205 N N    B GLY   A 1 46  ? 24.562 9.066   -0.438  0.50 10.73 ?  46  GLY   A N    1 
ATOM   1206 C CA   A GLY   A 1 46  ? 23.628 9.922   -0.925  0.50 9.82  ?  46  GLY   A CA   1 
ATOM   1207 C CA   B GLY   A 1 46  ? 23.759 10.237  -0.729  0.50 10.54 ?  46  GLY   A CA   1 
ATOM   1208 C C    A GLY   A 1 46  ? 22.147 9.803   -0.629  0.50 10.22 ?  46  GLY   A C    1 
ATOM   1209 C C    B GLY   A 1 46  ? 22.275 10.079  -0.457  0.50 9.70  ?  46  GLY   A C    1 
ATOM   1210 O O    A GLY   A 1 46  ? 21.492 10.812  -0.343  0.50 11.03 ?  46  GLY   A O    1 
ATOM   1211 O O    B GLY   A 1 46  ? 21.603 11.040  -0.063  0.50 10.40 ?  46  GLY   A O    1 
ATOM   1212 H H    A GLY   A 1 46  ? 24.544 8.200   -1.157  0.50 10.70 ?  46  GLY   A H    1 
ATOM   1213 H H    B GLY   A 1 46  ? 24.598 8.483   -1.074  0.50 12.90 ?  46  GLY   A H    1 
ATOM   1214 H HA2  A GLY   A 1 46  ? 23.939 10.709  -0.460  0.50 11.80 ?  46  GLY   A HA2  1 
ATOM   1215 H HA2  B GLY   A 1 46  ? 24.086 10.983  -0.200  0.50 12.67 ?  46  GLY   A HA2  1 
ATOM   1216 H HA3  A GLY   A 1 46  ? 23.726 10.072  -1.875  0.50 11.80 ?  46  GLY   A HA3  1 
ATOM   1217 H HA3  B GLY   A 1 46  ? 23.864 10.466  -1.663  0.50 12.67 ?  46  GLY   A HA3  1 
ATOM   1218 N N    A GLY   A 1 47  ? 21.599 8.593   -0.712  0.50 10.33 ?  47  GLY   A N    1 
ATOM   1219 N N    B GLY   A 1 47  ? 21.749 8.880   -0.684  0.50 9.43  ?  47  GLY   A N    1 
ATOM   1220 C CA   A GLY   A 1 47  ? 20.163 8.419   -0.602  0.50 10.45 ?  47  GLY   A CA   1 
ATOM   1221 C CA   B GLY   A 1 47  ? 20.322 8.631   -0.612  0.50 10.28 ?  47  GLY   A CA   1 
ATOM   1222 C C    A GLY   A 1 47  ? 19.816 6.995   -0.238  0.50 9.12  ?  47  GLY   A C    1 
ATOM   1223 C C    B GLY   A 1 47  ? 20.060 7.169   -0.309  0.50 9.73  ?  47  GLY   A C    1 
ATOM   1224 O O    A GLY   A 1 47  ? 20.690 6.155   -0.014  0.50 8.63  ?  47  GLY   A O    1 
ATOM   1225 O O    B GLY   A 1 47  ? 20.982 6.373   -0.120  0.50 9.60  ?  47  GLY   A O    1 
ATOM   1226 H H    A GLY   A 1 47  ? 22.034 7.857   -0.826  0.50 12.42 ?  47  GLY   A H    1 
ATOM   1227 H H    B GLY   A 1 47  ? 22.210 8.189   -0.876  0.50 11.33 ?  47  GLY   A H    1 
ATOM   1228 H HA2  A GLY   A 1 47  ? 19.813 9.002   0.083   0.50 12.56 ?  47  GLY   A HA2  1 
ATOM   1229 H HA2  B GLY   A 1 47  ? 19.921 9.174   0.083   0.50 12.36 ?  47  GLY   A HA2  1 
ATOM   1230 H HA3  A GLY   A 1 47  ? 19.740 8.630   -1.447  0.50 12.56 ?  47  GLY   A HA3  1 
ATOM   1231 H HA3  B GLY   A 1 47  ? 19.911 8.862   -1.464  0.50 12.36 ?  47  GLY   A HA3  1 
ATOM   1232 N N    A GLY   A 1 48  ? 18.514 6.725   -0.197  0.50 9.30  ?  48  GLY   A N    1 
ATOM   1233 N N    B GLY   A 1 48  ? 18.781 6.814   -0.279  0.50 9.79  ?  48  GLY   A N    1 
ATOM   1234 C CA   A GLY   A 1 48  ? 18.065 5.417   0.213   0.50 8.84  ?  48  GLY   A CA   1 
ATOM   1235 C CA   B GLY   A 1 48  ? 18.401 5.460   0.085   0.50 9.56  ?  48  GLY   A CA   1 
ATOM   1236 C C    A GLY   A 1 48  ? 18.564 5.094   1.606   0.50 8.27  ?  48  GLY   A C    1 
ATOM   1237 C C    B GLY   A 1 48  ? 18.826 5.110   1.503   0.50 8.76  ?  48  GLY   A C    1 
ATOM   1238 O O    A GLY   A 1 48  ? 18.707 5.973   2.464   0.50 9.05  ?  48  GLY   A O    1 
ATOM   1239 O O    B GLY   A 1 48  ? 18.997 5.980   2.365   0.50 9.12  ?  48  GLY   A O    1 
ATOM   1240 H H    A GLY   A 1 48  ? 17.882 7.277   -0.392  0.50 11.18 ?  48  GLY   A H    1 
ATOM   1241 H H    B GLY   A 1 48  ? 18.127 7.331   -0.478  0.50 11.77 ?  48  GLY   A H    1 
ATOM   1242 H HA2  A GLY   A 1 48  ? 17.095 5.377   0.211   0.50 10.63 ?  48  GLY   A HA2  1 
ATOM   1243 H HA2  B GLY   A 1 48  ? 17.438 5.367   0.010   0.50 11.49 ?  48  GLY   A HA2  1 
ATOM   1244 H HA3  A GLY   A 1 48  ? 18.404 4.742   -0.398  0.50 10.63 ?  48  GLY   A HA3  1 
ATOM   1245 H HA3  B GLY   A 1 48  ? 18.818 4.826   -0.524  0.50 11.49 ?  48  GLY   A HA3  1 
ATOM   1246 N N    A VAL   A 1 49  ? 18.833 3.811   1.840   0.50 7.93  ?  49  VAL   A N    1 
ATOM   1247 N N    B VAL   A 1 49  ? 19.008 3.808   1.745   0.50 8.72  ?  49  VAL   A N    1 
ATOM   1248 C CA   A VAL   A 1 49  ? 19.328 3.395   3.148   0.50 8.25  ?  49  VAL   A CA   1 
ATOM   1249 C CA   B VAL   A 1 49  ? 19.497 3.336   3.041   0.50 8.34  ?  49  VAL   A CA   1 
ATOM   1250 C C    A VAL   A 1 49  ? 20.645 4.098   3.471   0.50 7.85  ?  49  VAL   A C    1 
ATOM   1251 C C    B VAL   A 1 49  ? 20.783 4.054   3.431   0.50 7.32  ?  49  VAL   A C    1 
ATOM   1252 O O    A VAL   A 1 49  ? 20.844 4.593   4.586   0.50 8.41  ?  49  VAL   A O    1 
ATOM   1253 O O    B VAL   A 1 49  ? 20.985 4.402   4.600   0.50 7.34  ?  49  VAL   A O    1 
ATOM   1254 C CB   A VAL   A 1 49  ? 19.456 1.863   3.211   0.50 9.49  ?  49  VAL   A CB   1 
ATOM   1255 C CB   B VAL   A 1 49  ? 19.702 1.807   3.011   0.50 8.55  ?  49  VAL   A CB   1 
ATOM   1256 C CG1  A VAL   A 1 49  ? 20.147 1.440   4.497   0.50 10.32 ?  49  VAL   A CG1  1 
ATOM   1257 C CG1  B VAL   A 1 49  ? 20.520 1.334   4.222   0.50 7.69  ?  49  VAL   A CG1  1 
ATOM   1258 C CG2  A VAL   A 1 49  ? 18.080 1.214   3.094   0.50 11.15 ?  49  VAL   A CG2  1 
ATOM   1259 C CG2  B VAL   A 1 49  ? 18.368 1.079   2.941   0.50 9.68  ?  49  VAL   A CG2  1 
ATOM   1260 H H    A VAL   A 1 49  ? 18.741 3.169   1.268   0.50 9.54  ?  49  VAL   A H    1 
ATOM   1261 H H    B VAL   A 1 49  ? 18.861 3.184   1.178   0.50 10.49 ?  49  VAL   A H    1 
ATOM   1262 H HA   A VAL   A 1 49  ? 18.683 3.658   3.818   0.50 9.92  ?  49  VAL   A HA   1 
ATOM   1263 H HA   B VAL   A 1 49  ? 18.836 3.533   3.723   0.50 10.03 ?  49  VAL   A HA   1 
ATOM   1264 H HB   A VAL   A 1 49  ? 19.998 1.554   2.467   0.50 11.41 ?  49  VAL   A HB   1 
ATOM   1265 H HB   B VAL   A 1 49  ? 20.204 1.577   2.217   0.50 10.28 ?  49  VAL   A HB   1 
ATOM   1266 H HG11 A VAL   A 1 49  ? 19.987 0.497   4.644   0.50 12.40 ?  49  VAL   A HG11 1 
ATOM   1267 H HG11 B VAL   A 1 49  ? 20.381 0.381   4.345   0.50 9.25  ?  49  VAL   A HG11 1 
ATOM   1268 H HG12 A VAL   A 1 49  ? 21.097 1.609   4.417   0.50 12.40 ?  49  VAL   A HG12 1 
ATOM   1269 H HG12 B VAL   A 1 49  ? 21.461 1.508   4.061   0.50 9.25  ?  49  VAL   A HG12 1 
ATOM   1270 H HG13 A VAL   A 1 49  ? 19.777 1.957   5.233   0.50 12.40 ?  49  VAL   A HG13 1 
ATOM   1271 H HG13 B VAL   A 1 49  ? 20.223 1.811   5.012   0.50 9.25  ?  49  VAL   A HG13 1 
ATOM   1272 H HG21 A VAL   A 1 49  ? 18.176 0.251   3.158   0.50 13.40 ?  49  VAL   A HG21 1 
ATOM   1273 H HG21 B VAL   A 1 49  ? 18.528 0.121   2.915   0.50 11.64 ?  49  VAL   A HG21 1 
ATOM   1274 H HG22 A VAL   A 1 49  ? 17.516 1.538   3.814   0.50 13.40 ?  49  VAL   A HG22 1 
ATOM   1275 H HG22 B VAL   A 1 49  ? 17.841 1.302   3.726   0.50 11.64 ?  49  VAL   A HG22 1 
ATOM   1276 H HG23 A VAL   A 1 49  ? 17.691 1.452   2.237   0.50 13.40 ?  49  VAL   A HG23 1 
ATOM   1277 H HG23 B VAL   A 1 49  ? 17.898 1.356   2.139   0.50 11.64 ?  49  VAL   A HG23 1 
ATOM   1278 N N    A ALA   A 1 50  ? 21.567 4.138   2.503   0.50 7.78  ?  50  ALA   A N    1 
ATOM   1279 N N    B ALA   A 1 50  ? 21.695 4.235   2.473   0.50 7.14  ?  50  ALA   A N    1 
ATOM   1280 C CA   A ALA   A 1 50  ? 22.886 4.709   2.761   0.50 7.63  ?  50  ALA   A CA   1 
ATOM   1281 C CA   B ALA   A 1 50  ? 23.004 4.794   2.797   0.50 7.15  ?  50  ALA   A CA   1 
ATOM   1282 C C    A ALA   A 1 50  ? 22.788 6.167   3.180   0.50 7.30  ?  50  ALA   A C    1 
ATOM   1283 C C    B ALA   A 1 50  ? 22.885 6.239   3.253   0.50 7.19  ?  50  ALA   A C    1 
ATOM   1284 O O    A ALA   A 1 50  ? 23.444 6.595   4.135   0.50 7.94  ?  50  ALA   A O    1 
ATOM   1285 O O    B ALA   A 1 50  ? 23.502 6.640   4.247   0.50 7.60  ?  50  ALA   A O    1 
ATOM   1286 C CB   A ALA   A 1 50  ? 23.765 4.586   1.520   0.50 7.74  ?  50  ALA   A CB   1 
ATOM   1287 C CB   B ALA   A 1 50  ? 23.937 4.680   1.593   0.50 7.02  ?  50  ALA   A CB   1 
ATOM   1288 H H    A ALA   A 1 50  ? 21.454 3.838   1.703   0.50 9.36  ?  50  ALA   A H    1 
ATOM   1289 H H    B ALA   A 1 50  ? 21.577 4.049   1.642   0.50 8.59  ?  50  ALA   A H    1 
ATOM   1290 H HA   A ALA   A 1 50  ? 23.306 4.225   3.486   0.50 9.18  ?  50  ALA   A HA   1 
ATOM   1291 H HA   B ALA   A 1 50  ? 23.390 4.294   3.527   0.50 8.60  ?  50  ALA   A HA   1 
ATOM   1292 H HB1  A ALA   A 1 50  ? 24.633 4.976   1.714   0.50 9.31  ?  50  ALA   A HB1  1 
ATOM   1293 H HB1  B ALA   A 1 50  ? 24.801 5.055   1.827   0.50 8.44  ?  50  ALA   A HB1  1 
ATOM   1294 H HB2  A ALA   A 1 50  ? 23.862 3.651   1.297   0.50 9.31  ?  50  ALA   A HB2  1 
ATOM   1295 H HB2  B ALA   A 1 50  ? 24.036 3.744   1.360   0.50 8.44  ?  50  ALA   A HB2  1 
ATOM   1296 H HB3  A ALA   A 1 50  ? 23.343 5.064   0.789   0.50 9.31  ?  50  ALA   A HB3  1 
ATOM   1297 H HB3  B ALA   A 1 50  ? 23.556 5.168   0.847   0.50 8.44  ?  50  ALA   A HB3  1 
ATOM   1298 N N    A GLY   A 1 51  ? 21.988 6.953   2.463   0.50 7.56  ?  51  GLY   A N    1 
ATOM   1299 N N    B GLY   A 1 51  ? 22.107 7.044   2.529   0.50 7.85  ?  51  GLY   A N    1 
ATOM   1300 C CA   A GLY   A 1 51  ? 21.859 8.354   2.818   0.50 8.28  ?  51  GLY   A CA   1 
ATOM   1301 C CA   B GLY   A 1 51  ? 21.887 8.410   2.967   0.50 8.40  ?  51  GLY   A CA   1 
ATOM   1302 C C    A GLY   A 1 51  ? 21.273 8.538   4.202   0.50 7.63  ?  51  GLY   A C    1 
ATOM   1303 C C    B GLY   A 1 51  ? 21.265 8.471   4.348   0.50 8.43  ?  51  GLY   A C    1 
ATOM   1304 O O    A GLY   A 1 51  ? 21.684 9.433   4.946   0.50 8.13  ?  51  GLY   A O    1 
ATOM   1305 O O    B GLY   A 1 51  ? 21.617 9.331   5.161   0.50 9.19  ?  51  GLY   A O    1 
ATOM   1306 H H    A GLY   A 1 51  ? 21.525 6.707   1.782   0.50 9.09  ?  51  GLY   A H    1 
ATOM   1307 H H    B GLY   A 1 51  ? 21.711 6.829   1.791   0.50 9.43  ?  51  GLY   A H    1 
ATOM   1308 H HA2  A GLY   A 1 51  ? 22.729 8.778   2.796   0.50 9.96  ?  51  GLY   A HA2  1 
ATOM   1309 H HA2  B GLY   A 1 51  ? 22.731 8.886   2.982   0.50 10.09 ?  51  GLY   A HA2  1 
ATOM   1310 H HA3  A GLY   A 1 51  ? 21.281 8.802   2.178   0.50 9.96  ?  51  GLY   A HA3  1 
ATOM   1311 H HA3  B GLY   A 1 51  ? 21.295 8.859   2.337   0.50 10.09 ?  51  GLY   A HA3  1 
ATOM   1312 N N    A ALA   A 1 52  ? 20.299 7.697   4.561   0.50 7.57  ?  52  ALA   A N    1 
ATOM   1313 N N    B ALA   A 1 52  ? 20.334 7.554   4.632   0.50 8.64  ?  52  ALA   A N    1 
ATOM   1314 C CA   A ALA   A 1 52  ? 19.666 7.792   5.872   0.50 8.07  ?  52  ALA   A CA   1 
ATOM   1315 C CA   B ALA   A 1 52  ? 19.676 7.535   5.933   0.50 8.79  ?  52  ALA   A CA   1 
ATOM   1316 C C    A ALA   A 1 52  ? 20.611 7.346   6.985   0.50 7.76  ?  52  ALA   A C    1 
ATOM   1317 C C    B ALA   A 1 52  ? 20.653 7.162   7.042   0.50 8.50  ?  52  ALA   A C    1 
ATOM   1318 O O    A ALA   A 1 52  ? 20.710 8.008   8.024   0.50 8.52  ?  52  ALA   A O    1 
ATOM   1319 O O    B ALA   A 1 52  ? 20.720 7.839   8.074   0.50 9.05  ?  52  ALA   A O    1 
ATOM   1320 C CB   A ALA   A 1 52  ? 18.372 6.976   5.885   0.50 8.94  ?  52  ALA   A CB   1 
ATOM   1321 C CB   B ALA   A 1 52  ? 18.489 6.571   5.902   0.50 9.55  ?  52  ALA   A CB   1 
ATOM   1322 H H    A ALA   A 1 52  ? 19.997 7.062   4.065   0.50 9.10  ?  52  ALA   A H    1 
ATOM   1323 H H    B ALA   A 1 52  ? 20.079 6.930   4.094   0.50 10.39 ?  52  ALA   A H    1 
ATOM   1324 H HA   A ALA   A 1 52  ? 19.433 8.714   6.036   0.50 9.70  ?  52  ALA   A HA   1 
ATOM   1325 H HA   B ALA   A 1 52  ? 19.339 8.419   6.126   0.50 10.57 ?  52  ALA   A HA   1 
ATOM   1326 H HB1  A ALA   A 1 52  ? 17.960 7.048   6.761   0.50 10.74 ?  52  ALA   A HB1  1 
ATOM   1327 H HB1  B ALA   A 1 52  ? 18.060 6.572   6.773   0.50 11.48 ?  52  ALA   A HB1  1 
ATOM   1328 H HB2  A ALA   A 1 52  ? 17.769 7.328   5.208   0.50 10.74 ?  52  ALA   A HB2  1 
ATOM   1329 H HB2  B ALA   A 1 52  ? 17.861 6.871   5.225   0.50 11.48 ?  52  ALA   A HB2  1 
ATOM   1330 H HB3  A ALA   A 1 52  ? 18.576 6.047   5.691   0.50 10.74 ?  52  ALA   A HB3  1 
ATOM   1331 H HB3  B ALA   A 1 52  ? 18.807 5.682   5.689   0.50 11.48 ?  52  ALA   A HB3  1 
ATOM   1332 N N    A LEU   A 1 53  ? 21.309 6.222   6.793   0.50 7.46  ?  53  LEU   A N    1 
ATOM   1333 N N    B LEU   A 1 53  ? 21.414 6.080   6.858   0.50 8.24  ?  53  LEU   A N    1 
ATOM   1334 C CA   A LEU   A 1 53  ? 22.245 5.758   7.816   0.50 8.09  ?  53  LEU   A CA   1 
ATOM   1335 C CA   B LEU   A 1 53  ? 22.416 5.722   7.860   0.50 7.88  ?  53  LEU   A CA   1 
ATOM   1336 C C    A LEU   A 1 53  ? 23.340 6.784   8.041   0.50 8.40  ?  53  LEU   A C    1 
ATOM   1337 C C    B LEU   A 1 53  ? 23.423 6.854   8.040   0.50 7.50  ?  53  LEU   A C    1 
ATOM   1338 O O    A LEU   A 1 53  ? 23.715 7.069   9.184   0.50 9.30  ?  53  LEU   A O    1 
ATOM   1339 O O    B LEU   A 1 53  ? 23.713 7.271   9.167   0.50 7.82  ?  53  LEU   A O    1 
ATOM   1340 C CB   A LEU   A 1 53  ? 22.870 4.420   7.414   0.50 8.60  ?  53  LEU   A CB   1 
ATOM   1341 C CB   B LEU   A 1 53  ? 23.125 4.416   7.483   0.50 7.65  ?  53  LEU   A CB   1 
ATOM   1342 C CG   A LEU   A 1 53  ? 21.972 3.182   7.477   0.50 8.79  ?  53  LEU   A CG   1 
ATOM   1343 C CG   B LEU   A 1 53  ? 22.314 3.115   7.504   0.50 8.32  ?  53  LEU   A CG   1 
ATOM   1344 C CD1  A LEU   A 1 53  ? 22.710 1.972   6.925   0.50 8.80  ?  53  LEU   A CD1  1 
ATOM   1345 C CD1  B LEU   A 1 53  ? 23.141 1.977   6.913   0.50 8.75  ?  53  LEU   A CD1  1 
ATOM   1346 C CD2  A LEU   A 1 53  ? 21.496 2.908   8.895   0.50 10.10 ?  53  LEU   A CD2  1 
ATOM   1347 C CD2  B LEU   A 1 53  ? 21.855 2.756   8.911   0.50 9.08  ?  53  LEU   A CD2  1 
ATOM   1348 H H    A LEU   A 1 53  ? 21.272 5.725   6.095   0.50 8.97  ?  53  LEU   A H    1 
ATOM   1349 H H    B LEU   A 1 53  ? 21.364 5.539   6.182   0.50 9.91  ?  53  LEU   A H    1 
ATOM   1350 H HA   A LEU   A 1 53  ? 21.778 5.637   8.656   0.50 9.73  ?  53  LEU   A HA   1 
ATOM   1351 H HA   B LEU   A 1 53  ? 21.970 5.579   8.708   0.50 9.47  ?  53  LEU   A HA   1 
ATOM   1352 H HB2  A LEU   A 1 53  ? 23.183 4.496   6.500   0.50 10.34 ?  53  LEU   A HB2  1 
ATOM   1353 H HB2  B LEU   A 1 53  ? 23.473 4.510   6.585   0.50 9.20  ?  53  LEU   A HB2  1 
ATOM   1354 H HB3  A LEU   A 1 53  ? 23.626 4.247   7.996   0.50 10.34 ?  53  LEU   A HB3  1 
ATOM   1355 H HB3  B LEU   A 1 53  ? 23.864 4.290   8.098   0.50 9.20  ?  53  LEU   A HB3  1 
ATOM   1356 H HG   A LEU   A 1 53  ? 21.191 3.331   6.920   0.50 10.56 ?  53  LEU   A HG   1 
ATOM   1357 H HG   B LEU   A 1 53  ? 21.527 3.221   6.949   0.50 10.00 ?  53  LEU   A HG   1 
ATOM   1358 H HD11 A LEU   A 1 53  ? 22.128 1.198   6.970   0.50 10.57 ?  53  LEU   A HD11 1 
ATOM   1359 H HD11 B LEU   A 1 53  ? 22.618 1.158   6.932   0.50 10.52 ?  53  LEU   A HD11 1 
ATOM   1360 H HD12 A LEU   A 1 53  ? 22.961 2.145   6.004   0.50 10.57 ?  53  LEU   A HD12 1 
ATOM   1361 H HD12 B LEU   A 1 53  ? 23.372 2.196   5.995   0.50 10.52 ?  53  LEU   A HD12 1 
ATOM   1362 H HD13 A LEU   A 1 53  ? 23.507 1.818   7.459   0.50 10.57 ?  53  LEU   A HD13 1 
ATOM   1363 H HD13 B LEU   A 1 53  ? 23.949 1.863   7.438   0.50 10.52 ?  53  LEU   A HD13 1 
ATOM   1364 H HD21 A LEU   A 1 53  ? 21.008 2.071   8.905   0.50 12.13 ?  53  LEU   A HD21 1 
ATOM   1365 H HD21 B LEU   A 1 53  ? 21.375 1.909   8.884   0.50 10.91 ?  53  LEU   A HD21 1 
ATOM   1366 H HD22 A LEU   A 1 53  ? 22.270 2.848   9.477   0.50 12.13 ?  53  LEU   A HD22 1 
ATOM   1367 H HD22 B LEU   A 1 53  ? 22.625 2.681   9.491   0.50 10.91 ?  53  LEU   A HD22 1 
ATOM   1368 H HD23 A LEU   A 1 53  ? 20.922 3.632   9.180   0.50 12.13 ?  53  LEU   A HD23 1 
ATOM   1369 H HD23 B LEU   A 1 53  ? 21.261 3.455   9.235   0.50 10.91 ?  53  LEU   A HD23 1 
ATOM   1370 N N    A ASN   A 1 54  ? 23.865 7.355   6.961   0.50 8.02  ?  54  ASN   A N    1 
ATOM   1371 N N    B ASN   A 1 54  ? 23.950 7.384   6.935   0.50 7.43  ?  54  ASN   A N    1 
ATOM   1372 C CA   A ASN   A 1 54  ? 24.931 8.332   7.119   0.50 7.91  ?  54  ASN   A CA   1 
ATOM   1373 C CA   B ASN   A 1 54  ? 24.991 8.400   7.046   0.50 7.54  ?  54  ASN   A CA   1 
ATOM   1374 C C    A ASN   A 1 54  ? 24.428 9.576   7.847   0.50 8.20  ?  54  ASN   A C    1 
ATOM   1375 C C    B ASN   A 1 54  ? 24.479 9.648   7.764   0.50 8.12  ?  54  ASN   A C    1 
ATOM   1376 O O    A ASN   A 1 54  ? 25.103 10.093  8.748   0.50 8.05  ?  54  ASN   A O    1 
ATOM   1377 O O    B ASN   A 1 54  ? 25.196 10.237  8.583   0.50 8.59  ?  54  ASN   A O    1 
ATOM   1378 C CB   A ASN   A 1 54  ? 25.509 8.708   5.764   0.50 7.87  ?  54  ASN   A CB   1 
ATOM   1379 C CB   B ASN   A 1 54  ? 25.556 8.757   5.674   0.50 8.22  ?  54  ASN   A CB   1 
ATOM   1380 C CG   A ASN   A 1 54  ? 26.547 9.794   5.888   0.50 7.53  ?  54  ASN   A CG   1 
ATOM   1381 C CG   B ASN   A 1 54  ? 26.548 9.892   5.752   0.50 9.13  ?  54  ASN   A CG   1 
ATOM   1382 O OD1  A ASN   A 1 54  ? 27.523 9.648   6.625   0.50 6.71  ?  54  ASN   A OD1  1 
ATOM   1383 O OD1  B ASN   A 1 54  ? 27.592 9.761   6.384   0.50 9.58  ?  54  ASN   A OD1  1 
ATOM   1384 N ND2  A ASN   A 1 54  ? 26.337 10.898  5.197   0.50 8.48  ?  54  ASN   A ND2  1 
ATOM   1385 N ND2  B ASN   A 1 54  ? 26.226 11.018  5.135   0.50 9.93  ?  54  ASN   A ND2  1 
ATOM   1386 H H    A ASN   A 1 54  ? 23.624 7.196   6.149   0.50 9.64  ?  54  ASN   A H    1 
ATOM   1387 H H    B ASN   A 1 54  ? 23.727 7.175   6.130   0.50 8.94  ?  54  ASN   A H    1 
ATOM   1388 H HA   A ASN   A 1 54  ? 25.642 7.937   7.644   0.50 9.51  ?  54  ASN   A HA   1 
ATOM   1389 H HA   B ASN   A 1 54  ? 25.713 8.038   7.578   0.50 9.07  ?  54  ASN   A HA   1 
ATOM   1390 H HB2  A ASN   A 1 54  ? 25.926 7.919   5.366   0.50 9.46  ?  54  ASN   A HB2  1 
ATOM   1391 H HB2  B ASN   A 1 54  ? 26.018 7.979   5.314   0.50 9.89  ?  54  ASN   A HB2  1 
ATOM   1392 H HB3  A ASN   A 1 54  ? 24.797 9.027   5.188   0.50 9.46  ?  54  ASN   A HB3  1 
ATOM   1393 H HB3  B ASN   A 1 54  ? 24.836 9.020   5.088   0.50 9.89  ?  54  ASN   A HB3  1 
ATOM   1394 H HD21 A ASN   A 1 54  ? 26.905 11.537  5.244   0.50 10.19 ?  54  ASN   A HD21 1 
ATOM   1395 H HD21 B ASN   A 1 54  ? 26.759 11.692  5.167   0.50 11.93 ?  54  ASN   A HD21 1 
ATOM   1396 H HD22 A ASN   A 1 54  ? 25.639 10.969  4.704   0.50 10.19 ?  54  ASN   A HD22 1 
ATOM   1397 H HD22 B ASN   A 1 54  ? 25.490 11.069  4.700   0.50 11.93 ?  54  ASN   A HD22 1 
ATOM   1398 N N    . LYS   A 1 55  ? 23.241 10.067  7.473   1.00 8.49  ?  55  LYS   A N    1 
ATOM   1399 C CA   . LYS   A 1 55  ? 22.669 11.227  8.148   1.00 9.01  ?  55  LYS   A CA   1 
ATOM   1400 C C    . LYS   A 1 55  ? 22.570 10.981  9.648   1.00 9.18  ?  55  LYS   A C    1 
ATOM   1401 O O    . LYS   A 1 55  ? 22.848 11.876  10.454  1.00 10.18 ?  55  LYS   A O    1 
ATOM   1402 C CB   . LYS   A 1 55  ? 21.300 11.541  7.535   1.00 9.97  ?  55  LYS   A CB   1 
ATOM   1403 C CG   . LYS   A 1 55  ? 20.556 12.701  8.177   1.00 11.56 ?  55  LYS   A CG   1 
ATOM   1404 C CD   . LYS   A 1 55  ? 19.237 12.956  7.448   1.00 12.87 ?  55  LYS   A CD   1 
ATOM   1405 C CE   . LYS   A 1 55  ? 18.434 14.088  8.063   1.00 15.41 ?  55  LYS   A CE   1 
ATOM   1406 N NZ   . LYS   A 1 55  ? 17.105 14.248  7.400   1.00 15.88 ?  55  LYS   A NZ   1 
ATOM   1407 H H    A LYS   A 1 55  ? 22.753 9.742   6.841   0.50 10.21 ?  55  LYS   A H    1 
ATOM   1408 H H    B LYS   A 1 55  ? 22.716 9.686   6.904   0.50 10.21 ?  55  LYS   A H    1 
ATOM   1409 H HA   . LYS   A 1 55  ? 23.247 11.988  8.009   1.00 10.83 ?  55  LYS   A HA   1 
ATOM   1410 H HB2  . LYS   A 1 55  ? 21.428 11.761  6.601   1.00 11.98 ?  55  LYS   A HB2  1 
ATOM   1411 H HB3  . LYS   A 1 55  ? 20.740 10.754  7.612   1.00 11.98 ?  55  LYS   A HB3  1 
ATOM   1412 H HG2  . LYS   A 1 55  ? 20.352 12.481  9.102   1.00 13.90 ?  55  LYS   A HG2  1 
ATOM   1413 H HG3  . LYS   A 1 55  ? 21.094 13.501  8.127   1.00 13.90 ?  55  LYS   A HG3  1 
ATOM   1414 H HD2  . LYS   A 1 55  ? 19.428 13.186  6.526   1.00 15.47 ?  55  LYS   A HD2  1 
ATOM   1415 H HD3  . LYS   A 1 55  ? 18.696 12.148  7.482   1.00 15.47 ?  55  LYS   A HD3  1 
ATOM   1416 H HE2  . LYS   A 1 55  ? 18.286 13.896  9.004   1.00 18.51 ?  55  LYS   A HE2  1 
ATOM   1417 H HE3  . LYS   A 1 55  ? 18.927 14.915  7.963   1.00 18.51 ?  55  LYS   A HE3  1 
ATOM   1418 H HZ1  . LYS   A 1 55  ? 16.572 14.746  7.911   1.00 19.08 ?  55  LYS   A HZ1  1 
ATOM   1419 H HZ2  . LYS   A 1 55  ? 17.203 14.645  6.612   1.00 19.08 ?  55  LYS   A HZ2  1 
ATOM   1420 H HZ3  . LYS   A 1 55  ? 16.725 13.451  7.282   1.00 19.08 ?  55  LYS   A HZ3  1 
ATOM   1421 N N    . ALA   A 1 56  ? 22.177 9.765   10.042  1.00 9.39  ?  56  ALA   A N    1 
ATOM   1422 C CA   . ALA   A 1 56  ? 22.057 9.432   11.455  1.00 10.44 ?  56  ALA   A CA   1 
ATOM   1423 C C    . ALA   A 1 56  ? 23.397 9.457   12.183  1.00 10.36 ?  56  ALA   A C    1 
ATOM   1424 O O    . ALA   A 1 56  ? 23.419 9.644   13.402  1.00 11.86 ?  56  ALA   A O    1 
ATOM   1425 C CB   . ALA   A 1 56  ? 21.373 8.071   11.620  1.00 11.47 ?  56  ALA   A CB   1 
ATOM   1426 H H    . ALA   A 1 56  ? 21.981 9.120   9.506   1.00 11.29 ?  56  ALA   A H    1 
ATOM   1427 H HA   . ALA   A 1 56  ? 21.488 10.086  11.876  1.00 12.55 ?  56  ALA   A HA   1 
ATOM   1428 H HB1  . ALA   A 1 56  ? 21.296 7.866   12.568  1.00 13.79 ?  56  ALA   A HB1  1 
ATOM   1429 H HB2  . ALA   A 1 56  ? 20.486 8.110   11.223  1.00 13.79 ?  56  ALA   A HB2  1 
ATOM   1430 H HB3  . ALA   A 1 56  ? 21.900 7.387   11.178  1.00 13.79 ?  56  ALA   A HB3  1 
ATOM   1431 N N    . THR   A 1 57  ? 24.509 9.278   11.467  1.00 9.23  ?  57  THR   A N    1 
ATOM   1432 C CA   . THR   A 1 57  ? 25.851 9.399   12.041  1.00 9.52  ?  57  THR   A CA   1 
ATOM   1433 C C    . THR   A 1 57  ? 26.404 10.820  11.967  1.00 9.63  ?  57  THR   A C    1 
ATOM   1434 O O    . THR   A 1 57  ? 27.588 11.031  12.268  1.00 10.20 ?  57  THR   A O    1 
ATOM   1435 C CB   . THR   A 1 57  ? 26.859 8.451   11.361  1.00 9.31  ?  57  THR   A CB   1 
ATOM   1436 O OG1  . THR   A 1 57  ? 27.249 8.958   10.074  1.00 9.03  ?  57  THR   A OG1  1 
ATOM   1437 C CG2  . THR   A 1 57  ? 26.325 7.043   11.240  1.00 9.26  ?  57  THR   A CG2  1 
ATOM   1438 H H    . THR   A 1 57  ? 24.512 9.071   10.625  1.00 11.09 ?  57  THR   A H    1 
ATOM   1439 H HA   . THR   A 1 57  ? 25.801 9.141   12.977  1.00 11.44 ?  57  THR   A HA   1 
ATOM   1440 H HB   . THR   A 1 57  ? 27.650 8.399   11.924  1.00 11.19 ?  57  THR   A HB   1 
ATOM   1441 H HG1  . THR   A 1 57  ? 26.577 9.029   9.582   1.00 10.86 ?  57  THR   A HG1  1 
ATOM   1442 H HG21 . THR   A 1 57  ? 26.996 6.456   10.858  1.00 11.13 ?  57  THR   A HG21 1 
ATOM   1443 H HG22 . THR   A 1 57  ? 26.070 6.700   12.114  1.00 11.13 ?  57  THR   A HG22 1 
ATOM   1444 H HG23 . THR   A 1 57  ? 25.540 7.029   10.666  1.00 11.13 ?  57  THR   A HG23 1 
ATOM   1445 N N    . ASN   A 1 58  ? 25.589 11.795  11.564  1.00 10.13 ?  58  ASN   A N    1 
ATOM   1446 C CA   . ASN   A 1 58  ? 26.056 13.175  11.468  1.00 11.22 ?  58  ASN   A CA   1 
ATOM   1447 C C    . ASN   A 1 58  ? 27.205 13.300  10.463  1.00 10.16 ?  58  ASN   A C    1 
ATOM   1448 O O    . ASN   A 1 58  ? 28.103 14.132  10.623  1.00 10.92 ?  58  ASN   A O    1 
ATOM   1449 C CB   . ASN   A 1 58  ? 26.441 13.705  12.864  1.00 13.84 ?  58  ASN   A CB   1 
ATOM   1450 C CG   . ASN   A 1 58  ? 26.849 15.162  12.867  1.00 17.66 ?  58  ASN   A CG   1 
ATOM   1451 O OD1  . ASN   A 1 58  ? 26.217 15.984  12.219  1.00 19.18 ?  58  ASN   A OD1  1 
ATOM   1452 N ND2  . ASN   A 1 58  ? 27.905 15.489  13.614  1.00 19.18 ?  58  ASN   A ND2  1 
ATOM   1453 H H    . ASN   A 1 58  ? 24.769 11.674  11.331  1.00 12.17 ?  58  ASN   A H    1 
ATOM   1454 H HA   . ASN   A 1 58  ? 25.321 13.715  11.144  1.00 13.49 ?  58  ASN   A HA   1 
ATOM   1455 H HB2  . ASN   A 1 58  ? 25.672 13.600  13.457  1.00 16.63 ?  58  ASN   A HB2  1 
ATOM   1456 H HB3  . ASN   A 1 58  ? 27.185 13.192  13.204  1.00 16.63 ?  58  ASN   A HB3  1 
ATOM   1457 H HD21 . ASN   A 1 58  ? 28.163 16.307  13.653  1.00 23.04 ?  58  ASN   A HD21 1 
ATOM   1458 H HD22 . ASN   A 1 58  ? 28.317 14.882  14.056  1.00 23.04 ?  58  ASN   A HD22 1 
ATOM   1459 N N    . ASN   A 1 59  ? 27.180 12.481  9.408   1.00 9.22  ?  59  ASN   A N    1 
ATOM   1460 C CA   . ASN   A 1 59  ? 28.159 12.471  8.312   1.00 9.00  ?  59  ASN   A CA   1 
ATOM   1461 C C    . ASN   A 1 59  ? 29.478 11.789  8.694   1.00 9.00  ?  59  ASN   A C    1 
ATOM   1462 O O    . ASN   A 1 59  ? 30.395 11.748  7.867   1.00 9.06  ?  59  ASN   A O    1 
ATOM   1463 C CB   . ASN   A 1 59  ? 28.441 13.861  7.716   1.00 9.58  ?  59  ASN   A CB   1 
ATOM   1464 C CG   . ASN   A 1 59  ? 28.804 13.800  6.246   1.00 9.66  ?  59  ASN   A CG   1 
ATOM   1465 O OD1  . ASN   A 1 59  ? 28.091 13.189  5.444   1.00 10.24 ?  59  ASN   A OD1  1 
ATOM   1466 N ND2  . ASN   A 1 59  ? 29.894 14.461  5.876   1.00 10.32 ?  59  ASN   A ND2  1 
ATOM   1467 H H    . ASN   A 1 59  ? 26.565 11.891  9.293   1.00 11.08 ?  59  ASN   A H    1 
ATOM   1468 H HA   . ASN   A 1 59  ? 27.782 11.941  7.596   1.00 10.82 ?  59  ASN   A HA   1 
ATOM   1469 H HB2  . ASN   A 1 59  ? 27.646 14.412  7.801   1.00 11.51 ?  59  ASN   A HB2  1 
ATOM   1470 H HB3  . ASN   A 1 59  ? 29.181 14.270  8.189   1.00 11.51 ?  59  ASN   A HB3  1 
ATOM   1471 H HD21 . ASN   A 1 59  ? 30.146 14.458  5.055   1.00 12.41 ?  59  ASN   A HD21 1 
ATOM   1472 H HD22 . ASN   A 1 59  ? 30.371 14.879  6.465   1.00 12.41 ?  59  ASN   A HD22 1 
ATOM   1473 N N    . ALA   A 1 60  ? 29.603 11.237  9.903   1.00 8.86  ?  60  ALA   A N    1 
ATOM   1474 C CA   . ALA   A 1 60  ? 30.841 10.549  10.261  1.00 9.15  ?  60  ALA   A CA   1 
ATOM   1475 C C    . ALA   A 1 60  ? 31.065 9.312   9.396   1.00 9.08  ?  60  ALA   A C    1 
ATOM   1476 O O    . ALA   A 1 60  ? 32.209 8.990   9.061   1.00 9.26  ?  60  ALA   A O    1 
ATOM   1477 C CB   . ALA   A 1 60  ? 30.836 10.174  11.740  1.00 9.91  ?  60  ALA   A CB   1 
ATOM   1478 H H    . ALA   A 1 60  ? 29.001 11.239  10.516  1.00 10.65 ?  60  ALA   A H    1 
ATOM   1479 H HA   . ALA   A 1 60  ? 31.587 11.150  10.107  1.00 11.00 ?  60  ALA   A HA   1 
ATOM   1480 H HB1  . ALA   A 1 60  ? 31.669 9.723   11.955  1.00 11.91 ?  60  ALA   A HB1  1 
ATOM   1481 H HB2  . ALA   A 1 60  ? 30.759 10.987  12.268  1.00 11.91 ?  60  ALA   A HB2  1 
ATOM   1482 H HB3  . ALA   A 1 60  ? 30.086 9.591   11.918  1.00 11.91 ?  60  ALA   A HB3  1 
ATOM   1483 N N    . MET   A 1 61  ? 29.991 8.623   9.005   1.00 8.54  ?  61  MET   A N    1 
ATOM   1484 C CA   . MET   A 1 61  ? 30.136 7.492   8.094   1.00 8.53  ?  61  MET   A CA   1 
ATOM   1485 C C    . MET   A 1 61  ? 30.768 7.929   6.773   1.00 8.20  ?  61  MET   A C    1 
ATOM   1486 O O    . MET   A 1 61  ? 31.656 7.246   6.249   1.00 8.64  ?  61  MET   A O    1 
ATOM   1487 C CB   . MET   A 1 61  ? 28.774 6.829   7.875   1.00 8.49  ?  61  MET   A CB   1 
ATOM   1488 C CG   . MET   A 1 61  ? 28.772 5.679   6.877   1.00 8.75  ?  61  MET   A CG   1 
ATOM   1489 S SD   . MET   A 1 61  ? 27.147 4.939   6.657   1.00 9.76  ?  61  MET   A SD   1 
ATOM   1490 C CE   . MET   A 1 61  ? 27.002 4.020   8.187   1.00 11.03 ?  61  MET   A CE   1 
ATOM   1491 H H    . MET   A 1 61  ? 29.182 8.795   9.240   1.00 10.27 ?  61  MET   A H    1 
ATOM   1492 H HA   . MET   A 1 61  ? 30.718 6.838   8.509   1.00 10.25 ?  61  MET   A HA   1 
ATOM   1493 H HB2  . MET   A 1 61  ? 28.469 6.476   8.724   1.00 10.21 ?  61  MET   A HB2  1 
ATOM   1494 H HB3  . MET   A 1 61  ? 28.154 7.496   7.554   1.00 10.21 ?  61  MET   A HB3  1 
ATOM   1495 H HG2  . MET   A 1 61  ? 29.064 6.004   6.010   1.00 10.52 ?  61  MET   A HG2  1 
ATOM   1496 H HG3  . MET   A 1 61  ? 29.371 4.983   7.187   1.00 10.52 ?  61  MET   A HG3  1 
ATOM   1497 H HE1  . MET   A 1 61  ? 26.161 3.535   8.188   1.00 13.26 ?  61  MET   A HE1  1 
ATOM   1498 H HE2  . MET   A 1 61  ? 27.743 3.392   8.246   1.00 13.26 ?  61  MET   A HE2  1 
ATOM   1499 H HE3  . MET   A 1 61  ? 27.031 4.635   8.934   1.00 13.26 ?  61  MET   A HE3  1 
ATOM   1500 N N    . GLN   A 1 62  ? 30.322 9.061   6.218   1.00 8.16  ?  62  GLN   A N    1 
ATOM   1501 C CA   . GLN   A 1 62  ? 30.884 9.541   4.961   1.00 8.29  ?  62  GLN   A CA   1 
ATOM   1502 C C    . GLN   A 1 62  ? 32.356 9.912   5.109   1.00 8.60  ?  62  GLN   A C    1 
ATOM   1503 O O    . GLN   A 1 62  ? 33.163 9.611   4.225   1.00 9.27  ?  62  GLN   A O    1 
ATOM   1504 C CB   . GLN   A 1 62  ? 30.082 10.731  4.433   1.00 8.46  ?  62  GLN   A CB   1 
ATOM   1505 C CG   . GLN   A 1 62  ? 30.465 11.106  3.011   1.00 8.67  ?  62  GLN   A CG   1 
ATOM   1506 C CD   . GLN   A 1 62  ? 30.138 9.981   2.055   1.00 8.96  ?  62  GLN   A CD   1 
ATOM   1507 O OE1  . GLN   A 1 62  ? 28.962 9.681   1.838   1.00 9.72  ?  62  GLN   A OE1  1 
ATOM   1508 N NE2  . GLN   A 1 62  ? 31.151 9.307   1.534   1.00 9.53  ?  62  GLN   A NE2  1 
ATOM   1509 H H    . GLN   A 1 62  ? 29.703 9.557   6.549   1.00 9.81  ?  62  GLN   A H    1 
ATOM   1510 H HA   . GLN   A 1 62  ? 30.827 8.824   4.308   1.00 9.96  ?  62  GLN   A HA   1 
ATOM   1511 H HB2  . GLN   A 1 62  ? 29.141 10.508  4.445   1.00 10.17 ?  62  GLN   A HB2  1 
ATOM   1512 H HB3  . GLN   A 1 62  ? 30.252 11.498  5.002   1.00 10.17 ?  62  GLN   A HB3  1 
ATOM   1513 H HG2  . GLN   A 1 62  ? 29.959 11.891  2.741   1.00 10.42 ?  62  GLN   A HG2  1 
ATOM   1514 H HG3  . GLN   A 1 62  ? 31.415 11.285  2.962   1.00 10.42 ?  62  GLN   A HG3  1 
ATOM   1515 H HE21 . GLN   A 1 62  ? 31.958 9.532   1.718   1.00 11.46 ?  62  GLN   A HE21 1 
ATOM   1516 H HE22 . GLN   A 1 62  ? 31.000 8.654   0.992   1.00 11.46 ?  62  GLN   A HE22 1 
ATOM   1517 N N    . VAL   A 1 63  ? 32.721 10.589  6.204   1.00 9.02  ?  63  VAL   A N    1 
ATOM   1518 C CA   . VAL   A 1 63  ? 34.115 10.972  6.425   1.00 9.98  ?  63  VAL   A CA   1 
ATOM   1519 C C    . VAL   A 1 63  ? 35.010 9.736   6.474   1.00 9.32  ?  63  VAL   A C    1 
ATOM   1520 O O    . VAL   A 1 63  ? 36.061 9.677   5.821   1.00 9.95  ?  63  VAL   A O    1 
ATOM   1521 C CB   . VAL   A 1 63  ? 34.228 11.837  7.695   1.00 11.58 ?  63  VAL   A CB   1 
ATOM   1522 C CG1  . VAL   A 1 63  ? 35.679 12.057  8.075   1.00 13.34 ?  63  VAL   A CG1  1 
ATOM   1523 C CG2  . VAL   A 1 63  ? 33.503 13.174  7.482   1.00 12.06 ?  63  VAL   A CG2  1 
ATOM   1524 H H    . VAL   A 1 63  ? 32.172 10.844  6.825   1.00 10.84 ?  63  VAL   A H    1 
ATOM   1525 H HA   . VAL   A 1 63  ? 34.397 11.516  5.677   1.00 11.99 ?  63  VAL   A HA   1 
ATOM   1526 H HB   . VAL   A 1 63  ? 33.790 11.378  8.430   1.00 13.92 ?  63  VAL   A HB   1 
ATOM   1527 H HG11 . VAL   A 1 63  ? 35.730 12.786  8.711   1.00 16.02 ?  63  VAL   A HG11 1 
ATOM   1528 H HG12 . VAL   A 1 63  ? 36.029 11.245  8.472   1.00 16.02 ?  63  VAL   A HG12 1 
ATOM   1529 H HG13 . VAL   A 1 63  ? 36.181 12.281  7.275   1.00 16.02 ?  63  VAL   A HG13 1 
ATOM   1530 H HG21 . VAL   A 1 63  ? 33.597 13.718  8.281   1.00 14.49 ?  63  VAL   A HG21 1 
ATOM   1531 H HG22 . VAL   A 1 63  ? 33.896 13.633  6.723   1.00 14.49 ?  63  VAL   A HG22 1 
ATOM   1532 H HG23 . VAL   A 1 63  ? 32.561 13.005  7.311   1.00 14.49 ?  63  VAL   A HG23 1 
ATOM   1533 N N    . GLU   A 1 64  ? 34.593 8.722   7.236   1.00 9.11  ?  64  GLU   A N    1 
ATOM   1534 C CA   . GLU   A 1 64  ? 35.349 7.479   7.320   1.00 9.38  ?  64  GLU   A CA   1 
ATOM   1535 C C    . GLU   A 1 64  ? 35.435 6.801   5.956   1.00 8.93  ?  64  GLU   A C    1 
ATOM   1536 O O    . GLU   A 1 64  ? 36.484 6.260   5.575   1.00 9.48  ?  64  GLU   A O    1 
ATOM   1537 C CB   . GLU   A 1 64  ? 34.656 6.569   8.333   1.00 9.54  ?  64  GLU   A CB   1 
ATOM   1538 C CG   . GLU   A 1 64  ? 35.320 5.223   8.511   1.00 10.76 ?  64  GLU   A CG   1 
ATOM   1539 C CD   . GLU   A 1 64  ? 34.431 4.221   9.227   1.00 11.31 ?  64  GLU   A CD   1 
ATOM   1540 O OE1  . GLU   A 1 64  ? 33.190 4.326   9.100   1.00 12.01 ?  64  GLU   A OE1  1 
ATOM   1541 O OE2  . GLU   A 1 64  ? 34.976 3.315   9.903   1.00 11.70 -1 64  GLU   A OE2  1 
ATOM   1542 H H    . GLU   A 1 64  ? 33.867 8.728   7.701   1.00 10.95 ?  64  GLU   A H    1 
ATOM   1543 H HA   . GLU   A 1 64  ? 36.248 7.674   7.632   1.00 11.27 ?  64  GLU   A HA   1 
ATOM   1544 H HB2  . GLU   A 1 64  ? 34.654 7.018   9.198   1.00 11.46 ?  64  GLU   A HB2  1 
ATOM   1545 H HB3  . GLU   A 1 64  ? 33.745 6.424   8.040   1.00 11.46 ?  64  GLU   A HB3  1 
ATOM   1546 H HG2  . GLU   A 1 64  ? 35.548 4.853   7.642   1.00 12.93 ?  64  GLU   A HG2  1 
ATOM   1547 H HG3  . GLU   A 1 64  ? 36.126 5.334   9.041   1.00 12.93 ?  64  GLU   A HG3  1 
ATOM   1548 N N    . SER   A 1 65  ? 34.319 6.805   5.219   1.00 8.64  ?  65  SER   A N    1 
ATOM   1549 C CA   . SER   A 1 65  ? 34.261 6.155   3.914   1.00 8.59  ?  65  SER   A CA   1 
ATOM   1550 C C    . SER   A 1 65  ? 35.182 6.831   2.907   1.00 8.93  ?  65  SER   A C    1 
ATOM   1551 O O    . SER   A 1 65  ? 35.829 6.157   2.097   1.00 9.73  ?  65  SER   A O    1 
ATOM   1552 C CB   . SER   A 1 65  ? 32.827 6.174   3.383   1.00 8.49  ?  65  SER   A CB   1 
ATOM   1553 O OG   . SER   A 1 65  ? 31.971 5.350   4.164   1.00 9.23  ?  65  SER   A OG   1 
ATOM   1554 H H    . SER   A 1 65  ? 33.582 7.179   5.459   1.00 10.38 ?  65  SER   A H    1 
ATOM   1555 H HA   . SER   A 1 65  ? 34.536 5.232   4.006   1.00 10.32 ?  65  SER   A HA   1 
ATOM   1556 H HB2  . SER   A 1 65  ? 32.492 7.084   3.404   1.00 10.21 ?  65  SER   A HB2  1 
ATOM   1557 H HB3  . SER   A 1 65  ? 32.829 5.846   2.470   1.00 10.21 ?  65  SER   A HB3  1 
ATOM   1558 H HG   . SER   A 1 65  ? 31.962 5.629   4.962   1.00 11.10 ?  65  SER   A HG   1 
ATOM   1559 N N    . ASP   A 1 66  ? 35.258 8.163   2.936   1.00 9.12  ?  66  ASP   A N    1 
ATOM   1560 C CA   . ASP   A 1 66  ? 36.120 8.864   1.991   1.00 10.14 ?  66  ASP   A CA   1 
ATOM   1561 C C    . ASP   A 1 66  ? 37.585 8.505   2.222   1.00 10.04 ?  66  ASP   A C    1 
ATOM   1562 O O    . ASP   A 1 66  ? 38.351 8.340   1.265   1.00 10.90 ?  66  ASP   A O    1 
ATOM   1563 C CB   . ASP   A 1 66  ? 35.901 10.371  2.107   1.00 11.34 ?  66  ASP   A CB   1 
ATOM   1564 C CG   . ASP   A 1 66  ? 34.568 10.835  1.505   1.00 13.13 ?  66  ASP   A CG   1 
ATOM   1565 O OD1  . ASP   A 1 66  ? 33.852 10.042  0.855   1.00 13.44 ?  66  ASP   A OD1  1 
ATOM   1566 O OD2  . ASP   A 1 66  ? 34.257 12.031  1.670   1.00 16.42 -1 66  ASP   A OD2  1 
ATOM   1567 H H    . ASP   A 1 66  ? 34.812 8.675   3.470   1.00 10.96 ?  66  ASP   A H    1 
ATOM   1568 H HA   . ASP   A 1 66  ? 35.882 8.601   1.088   1.00 12.19 ?  66  ASP   A HA   1 
ATOM   1569 H HB2  . ASP   A 1 66  ? 35.903 10.620  3.045   1.00 13.62 ?  66  ASP   A HB2  1 
ATOM   1570 H HB3  . ASP   A 1 66  ? 36.623 10.830  1.644   1.00 13.62 ?  66  ASP   A HB3  1 
ATOM   1571 N N    . ASP   A 1 67  ? 37.991 8.372   3.485   1.00 10.29 ?  67  ASP   A N    1 
ATOM   1572 C CA   . ASP   A 1 67  ? 39.343 7.916   3.782   1.00 10.75 ?  67  ASP   A CA   1 
ATOM   1573 C C    . ASP   A 1 67  ? 39.559 6.483   3.303   1.00 10.47 ?  67  ASP   A C    1 
ATOM   1574 O O    . ASP   A 1 67  ? 40.617 6.158   2.752   1.00 11.15 ?  67  ASP   A O    1 
ATOM   1575 C CB   . ASP   A 1 67  ? 39.610 8.034   5.279   1.00 12.40 ?  67  ASP   A CB   1 
ATOM   1576 C CG   . ASP   A 1 67  ? 40.914 7.379   5.689   1.00 13.20 ?  67  ASP   A CG   1 
ATOM   1577 O OD1  . ASP   A 1 67  ? 41.986 8.009   5.554   1.00 15.85 ?  67  ASP   A OD1  1 
ATOM   1578 O OD2  . ASP   A 1 67  ? 40.862 6.215   6.140   1.00 12.94 -1 67  ASP   A OD2  1 
ATOM   1579 H H    . ASP   A 1 67  ? 37.505 8.534   4.176   1.00 12.36 ?  67  ASP   A H    1 
ATOM   1580 H HA   . ASP   A 1 67  ? 39.973 8.479   3.312   1.00 12.92 ?  67  ASP   A HA   1 
ATOM   1581 H HB2  . ASP   A 1 67  ? 39.654 8.972   5.510   1.00 14.90 ?  67  ASP   A HB2  1 
ATOM   1582 H HB3  . ASP   A 1 67  ? 38.886 7.603   5.762   1.00 14.90 ?  67  ASP   A HB3  1 
ATOM   1583 N N    . TYR   A 1 68  ? 38.564 5.609   3.495   1.00 9.85  ?  68  TYR   A N    1 
ATOM   1584 C CA   . TYR   A 1 68  ? 38.678 4.232   3.014   1.00 10.09 ?  68  TYR   A CA   1 
ATOM   1585 C C    . TYR   A 1 68  ? 38.919 4.190   1.506   1.00 9.94  ?  68  TYR   A C    1 
ATOM   1586 O O    . TYR   A 1 68  ? 39.798 3.464   1.026   1.00 10.44 ?  68  TYR   A O    1 
ATOM   1587 C CB   . TYR   A 1 68  ? 37.431 3.407   3.394   1.00 10.45 ?  68  TYR   A CB   1 
ATOM   1588 C CG   . TYR   A 1 68  ? 37.452 2.017   2.761   1.00 12.17 ?  68  TYR   A CG   1 
ATOM   1589 C CD1  . TYR   A 1 68  ? 36.995 1.827   1.459   1.00 13.47 ?  68  TYR   A CD1  1 
ATOM   1590 C CD2  . TYR   A 1 68  ? 37.984 0.928   3.428   1.00 13.56 ?  68  TYR   A CD2  1 
ATOM   1591 C CE1  . TYR   A 1 68  ? 37.062 0.609   0.837   1.00 14.82 ?  68  TYR   A CE1  1 
ATOM   1592 C CE2  . TYR   A 1 68  ? 38.046 -0.332  2.806   1.00 14.11 ?  68  TYR   A CE2  1 
ATOM   1593 C CZ   . TYR   A 1 68  ? 37.586 -0.462  1.510   1.00 14.99 ?  68  TYR   A CZ   1 
ATOM   1594 O OH   . TYR   A 1 68  ? 37.661 -1.670  0.875   1.00 16.30 ?  68  TYR   A OH   1 
ATOM   1595 H H    . TYR   A 1 68  ? 37.812 5.785   3.889   1.00 11.83 ?  68  TYR   A H    1 
ATOM   1596 H HA   . TYR   A 1 68  ? 39.438 3.819   3.444   1.00 12.12 ?  68  TYR   A HA   1 
ATOM   1597 H HB2  . TYR   A 1 68  ? 37.403 3.296   4.358   1.00 12.55 ?  68  TYR   A HB2  1 
ATOM   1598 H HB3  . TYR   A 1 68  ? 36.634 3.867   3.087   1.00 12.55 ?  68  TYR   A HB3  1 
ATOM   1599 H HD1  . TYR   A 1 68  ? 36.653 2.560   0.992   1.00 16.18 ?  68  TYR   A HD1  1 
ATOM   1600 H HD2  . TYR   A 1 68  ? 38.315 1.031   4.288   1.00 16.29 ?  68  TYR   A HD2  1 
ATOM   1601 H HE1  . TYR   A 1 68  ? 36.743 0.516   -0.032  1.00 17.80 ?  68  TYR   A HE1  1 
ATOM   1602 H HE2  . TYR   A 1 68  ? 38.408 -1.064  3.244   1.00 16.95 ?  68  TYR   A HE2  1 
ATOM   1603 H HH   . TYR   A 1 68  ? 37.986 -2.245  1.398   1.00 19.58 ?  68  TYR   A HH   1 
ATOM   1604 N N    . ILE   A 1 69  ? 38.129 4.949   0.739   1.00 9.86  ?  69  ILE   A N    1 
ATOM   1605 C CA   . ILE   A 1 69  ? 38.261 4.935   -0.718  1.00 9.85  ?  69  ILE   A CA   1 
ATOM   1606 C C    . ILE   A 1 69  ? 39.590 5.550   -1.152  1.00 9.82  ?  69  ILE   A C    1 
ATOM   1607 O O    . ILE   A 1 69  ? 40.234 5.069   -2.091  1.00 10.22 ?  69  ILE   A O    1 
ATOM   1608 C CB   . ILE   A 1 69  ? 37.062 5.643   -1.380  1.00 10.73 ?  69  ILE   A CB   1 
ATOM   1609 C CG1  . ILE   A 1 69  ? 35.751 4.904   -1.099  1.00 11.32 ?  69  ILE   A CG1  1 
ATOM   1610 C CG2  . ILE   A 1 69  ? 37.302 5.834   -2.883  1.00 12.42 ?  69  ILE   A CG2  1 
ATOM   1611 C CD1  . ILE   A 1 69  ? 35.591 3.612   -1.863  1.00 12.09 ?  69  ILE   A CD1  1 
ATOM   1612 H H    . ILE   A 1 69  ? 37.522 5.481   1.036   1.00 11.86 ?  69  ILE   A H    1 
ATOM   1613 H HA   . ILE   A 1 69  ? 38.259 4.011   -1.015  1.00 11.85 ?  69  ILE   A HA   1 
ATOM   1614 H HB   . ILE   A 1 69  ? 36.990 6.520   -0.983  1.00 12.90 ?  69  ILE   A HB   1 
ATOM   1615 H HG12 . ILE   A 1 69  ? 35.711 4.691   -0.152  1.00 13.60 ?  69  ILE   A HG12 1 
ATOM   1616 H HG13 . ILE   A 1 69  ? 35.013 5.482   -1.337  1.00 13.60 ?  69  ILE   A HG13 1 
ATOM   1617 H HG21 . ILE   A 1 69  ? 36.455 6.033   -3.315  1.00 14.92 ?  69  ILE   A HG21 1 
ATOM   1618 H HG22 . ILE   A 1 69  ? 37.915 6.580   -3.014  1.00 14.92 ?  69  ILE   A HG22 1 
ATOM   1619 H HG23 . ILE   A 1 69  ? 37.681 5.026   -3.255  1.00 14.92 ?  69  ILE   A HG23 1 
ATOM   1620 H HD11 . ILE   A 1 69  ? 34.787 3.163   -1.555  1.00 14.53 ?  69  ILE   A HD11 1 
ATOM   1621 H HD12 . ILE   A 1 69  ? 35.512 3.810   -2.810  1.00 14.53 ?  69  ILE   A HD12 1 
ATOM   1622 H HD13 . ILE   A 1 69  ? 36.363 3.047   -1.705  1.00 14.53 ?  69  ILE   A HD13 1 
ATOM   1623 N N    . ALA   A 1 70  ? 40.012 6.631   -0.495  1.00 10.18 ?  70  ALA   A N    1 
ATOM   1624 C CA   . ALA   A 1 70  ? 41.288 7.242   -0.857  1.00 11.14 ?  70  ALA   A CA   1 
ATOM   1625 C C    . ALA   A 1 70  ? 42.439 6.259   -0.684  1.00 11.12 ?  70  ALA   A C    1 
ATOM   1626 O O    . ALA   A 1 70  ? 43.400 6.285   -1.456  1.00 13.14 ?  70  ALA   A O    1 
ATOM   1627 C CB   . ALA   A 1 70  ? 41.528 8.499   -0.023  1.00 11.68 ?  70  ALA   A CB   1 
ATOM   1628 H H    . ALA   A 1 70  ? 39.589 7.019   0.141   1.00 12.23 ?  70  ALA   A H    1 
ATOM   1629 H HA   . ALA   A 1 70  ? 41.257 7.507   -1.789  1.00 13.38 ?  70  ALA   A HA   1 
ATOM   1630 H HB1  . ALA   A 1 70  ? 42.386 8.886   -0.281  1.00 14.03 ?  70  ALA   A HB1  1 
ATOM   1631 H HB2  . ALA   A 1 70  ? 40.819 9.134   -0.191  1.00 14.03 ?  70  ALA   A HB2  1 
ATOM   1632 H HB3  . ALA   A 1 70  ? 41.550 8.258   0.915   1.00 14.03 ?  70  ALA   A HB3  1 
ATOM   1633 N N    . THR   A 1 71  ? 42.342 5.361   0.296   1.00 10.64 ?  71  THR   A N    1 
ATOM   1634 C CA   . THR   A 1 71  ? 43.399 4.385   0.542   1.00 12.16 ?  71  THR   A CA   1 
ATOM   1635 C C    . THR   A 1 71  ? 43.279 3.162   -0.356  1.00 12.29 ?  71  THR   A C    1 
ATOM   1636 O O    . THR   A 1 71  ? 44.289 2.663   -0.871  1.00 14.22 ?  71  THR   A O    1 
ATOM   1637 C CB   . THR   A 1 71  ? 43.338 3.939   1.999   1.00 14.02 ?  71  THR   A CB   1 
ATOM   1638 O OG1  . THR   A 1 71  ? 43.601 5.067   2.839   1.00 15.23 ?  71  THR   A OG1  1 
ATOM   1639 C CG2  . THR   A 1 71  ? 44.345 2.828   2.281   1.00 15.60 ?  71  THR   A CG2  1 
ATOM   1640 H H    . THR   A 1 71  ? 41.673 5.294   0.829   1.00 12.79 ?  71  THR   A H    1 
ATOM   1641 H HA   . THR   A 1 71  ? 44.261 4.791   0.378   1.00 14.61 ?  71  THR   A HA   1 
ATOM   1642 H HB   . THR   A 1 71  ? 42.451 3.590   2.188   1.00 16.85 ?  71  THR   A HB   1 
ATOM   1643 H HG1  . THR   A 1 71  ? 43.018 5.655   2.709   1.00 18.30 ?  71  THR   A HG1  1 
ATOM   1644 H HG21 . THR   A 1 71  ? 44.489 2.746   3.238   1.00 18.74 ?  71  THR   A HG21 1 
ATOM   1645 H HG22 . THR   A 1 71  ? 44.025 1.979   1.939   1.00 18.74 ?  71  THR   A HG22 1 
ATOM   1646 H HG23 . THR   A 1 71  ? 45.197 3.036   1.858   1.00 18.74 ?  71  THR   A HG23 1 
ATOM   1647 N N    . ASN   A 1 72  ? 42.056 2.653   -0.535  1.00 11.20 ?  72  ASN   A N    1 
ATOM   1648 C CA   . ASN   A 1 72  ? 41.837 1.329   -1.103  1.00 11.65 ?  72  ASN   A CA   1 
ATOM   1649 C C    . ASN   A 1 72  ? 41.214 1.321   -2.487  1.00 11.65 ?  72  ASN   A C    1 
ATOM   1650 O O    . ASN   A 1 72  ? 41.230 0.269   -3.141  1.00 13.10 ?  72  ASN   A O    1 
ATOM   1651 C CB   . ASN   A 1 72  ? 40.950 0.502   -0.165  1.00 12.26 ?  72  ASN   A CB   1 
ATOM   1652 C CG   . ASN   A 1 72  ? 41.563 0.349   1.197   1.00 13.24 ?  72  ASN   A CG   1 
ATOM   1653 O OD1  . ASN   A 1 72  ? 41.109 0.951   2.168   1.00 14.93 ?  72  ASN   A OD1  1 
ATOM   1654 N ND2  . ASN   A 1 72  ? 42.619 -0.432  1.278   1.00 13.86 ?  72  ASN   A ND2  1 
ATOM   1655 H H    . ASN   A 1 72  ? 41.324 3.063   -0.332  1.00 13.46 ?  72  ASN   A H    1 
ATOM   1656 H HA   . ASN   A 1 72  ? 42.691 0.877   -1.173  1.00 14.00 ?  72  ASN   A HA   1 
ATOM   1657 H HB2  . ASN   A 1 72  ? 40.094 0.943   -0.065  1.00 14.73 ?  72  ASN   A HB2  1 
ATOM   1658 H HB3  . ASN   A 1 72  ? 40.830 -0.385  -0.541  1.00 14.73 ?  72  ASN   A HB3  1 
ATOM   1659 H HD21 . ASN   A 1 72  ? 43.014 -0.544  2.036   1.00 16.65 ?  72  ASN   A HD21 1 
ATOM   1660 H HD22 . ASN   A 1 72  ? 42.915 -0.833  0.578   1.00 16.65 ?  72  ASN   A HD22 1 
ATOM   1661 N N    . GLY   A 1 73  ? 40.663 2.437   -2.946  1.00 11.29 ?  73  GLY   A N    1 
ATOM   1662 C CA   . GLY   A 1 73  ? 39.925 2.455   -4.183  1.00 11.30 ?  73  GLY   A CA   1 
ATOM   1663 C C    . GLY   A 1 73  ? 38.532 1.874   -4.020  1.00 10.43 ?  73  GLY   A C    1 
ATOM   1664 O O    . GLY   A 1 73  ? 38.140 1.413   -2.943  1.00 10.85 ?  73  GLY   A O    1 
ATOM   1665 H H    . GLY   A 1 73  ? 40.711 3.206   -2.556  1.00 13.56 ?  73  GLY   A H    1 
ATOM   1666 H HA2  . GLY   A 1 73  ? 39.850 3.371   -4.499  1.00 13.58 ?  73  GLY   A HA2  1 
ATOM   1667 H HA3  . GLY   A 1 73  ? 40.404 1.940   -4.855  1.00 13.58 ?  73  GLY   A HA3  1 
ATOM   1668 N N    . PRO   A 1 74  ? 37.761 1.891   -5.105  1.00 10.62 ?  74  PRO   A N    1 
ATOM   1669 C CA   . PRO   A 1 74  ? 36.365 1.461   -5.031  1.00 10.84 ?  74  PRO   A CA   1 
ATOM   1670 C C    . PRO   A 1 74  ? 36.211 -0.022  -4.725  1.00 10.12 ?  74  PRO   A C    1 
ATOM   1671 O O    . PRO   A 1 74  ? 37.074 -0.854  -5.021  1.00 11.36 ?  74  PRO   A O    1 
ATOM   1672 C CB   . PRO   A 1 74  ? 35.821 1.781   -6.430  1.00 12.57 ?  74  PRO   A CB   1 
ATOM   1673 C CG   . PRO   A 1 74  ? 36.789 2.760   -7.027  1.00 15.31 ?  74  PRO   A CG   1 
ATOM   1674 C CD   . PRO   A 1 74  ? 38.116 2.408   -6.438  1.00 12.83 ?  74  PRO   A CD   1 
ATOM   1675 H HA   . PRO   A 1 74  ? 35.887 1.984   -4.369  1.00 13.03 ?  74  PRO   A HA   1 
ATOM   1676 H HB2  . PRO   A 1 74  ? 35.784 0.970   -6.958  1.00 15.11 ?  74  PRO   A HB2  1 
ATOM   1677 H HB3  . PRO   A 1 74  ? 34.940 2.181   -6.352  1.00 15.11 ?  74  PRO   A HB3  1 
ATOM   1678 H HG2  . PRO   A 1 74  ? 36.810 2.659   -7.991  1.00 18.39 ?  74  PRO   A HG2  1 
ATOM   1679 H HG3  . PRO   A 1 74  ? 36.542 3.663   -6.780  1.00 18.39 ?  74  PRO   A HG3  1 
ATOM   1680 H HD2  . PRO   A 1 74  ? 38.558 1.718   -6.967  1.00 15.42 ?  74  PRO   A HD2  1 
ATOM   1681 H HD3  . PRO   A 1 74  ? 38.676 3.202   -6.369  1.00 15.42 ?  74  PRO   A HD3  1 
ATOM   1682 N N    . LEU   A 1 75  ? 35.063 -0.342  -4.137  1.00 9.42  ?  75  LEU   A N    1 
ATOM   1683 C CA   . LEU   A 1 75  ? 34.648 -1.728  -3.989  1.00 9.43  ?  75  LEU   A CA   1 
ATOM   1684 C C    . LEU   A 1 75  ? 34.262 -2.303  -5.349  1.00 9.95  ?  75  LEU   A C    1 
ATOM   1685 O O    . LEU   A 1 75  ? 34.160 -1.590  -6.351  1.00 11.18 ?  75  LEU   A O    1 
ATOM   1686 C CB   . LEU   A 1 75  ? 33.456 -1.842  -3.035  1.00 9.48  ?  75  LEU   A CB   1 
ATOM   1687 C CG   . LEU   A 1 75  ? 33.677 -1.434  -1.579  1.00 11.46 ?  75  LEU   A CG   1 
ATOM   1688 C CD1  . LEU   A 1 75  ? 32.388 -1.600  -0.768  1.00 13.43 ?  75  LEU   A CD1  1 
ATOM   1689 C CD2  . LEU   A 1 75  ? 34.811 -2.180  -0.936  1.00 14.64 ?  75  LEU   A CD2  1 
ATOM   1690 H H    . LEU   A 1 75  ? 34.500 0.230   -3.822  1.00 11.33 ?  75  LEU   A H    1 
ATOM   1691 H HA   . LEU   A 1 75  ? 35.384 -2.244  -3.636  1.00 11.34 ?  75  LEU   A HA   1 
ATOM   1692 H HB2  . LEU   A 1 75  ? 32.740 -1.292  -3.378  1.00 11.40 ?  75  LEU   A HB2  1 
ATOM   1693 H HB3  . LEU   A 1 75  ? 33.171 -2.771  -3.028  1.00 11.40 ?  75  LEU   A HB3  1 
ATOM   1694 H HG   . LEU   A 1 75  ? 33.915 -0.494  -1.563  1.00 13.77 ?  75  LEU   A HG   1 
ATOM   1695 H HD11 . LEU   A 1 75  ? 32.558 -1.329  0.149   1.00 16.13 ?  75  LEU   A HD11 1 
ATOM   1696 H HD12 . LEU   A 1 75  ? 31.702 -1.033  -1.157  1.00 16.13 ?  75  LEU   A HD12 1 
ATOM   1697 H HD13 . LEU   A 1 75  ? 32.113 -2.525  -0.797  1.00 16.13 ?  75  LEU   A HD13 1 
ATOM   1698 H HD21 . LEU   A 1 75  ? 34.865 -1.929  -0.000  1.00 17.59 ?  75  LEU   A HD21 1 
ATOM   1699 H HD22 . LEU   A 1 75  ? 34.651 -3.131  -1.016  1.00 17.59 ?  75  LEU   A HD22 1 
ATOM   1700 H HD23 . LEU   A 1 75  ? 35.643 -1.946  -1.385  1.00 17.59 ?  75  LEU   A HD23 1 
ATOM   1701 N N    . LYS   A 1 76  ? 34.060 -3.621  -5.369  1.00 10.29 ?  76  LYS   A N    1 
ATOM   1702 C CA   . LYS   A 1 76  ? 33.451 -4.330  -6.489  1.00 10.89 ?  76  LYS   A CA   1 
ATOM   1703 C C    . LYS   A 1 76  ? 31.939 -4.418  -6.291  1.00 9.50  ?  76  LYS   A C    1 
ATOM   1704 O O    . LYS   A 1 76  ? 31.463 -4.552  -5.168  1.00 9.43  ?  76  LYS   A O    1 
ATOM   1705 C CB   . LYS   A 1 76  ? 33.996 -5.768  -6.556  1.00 13.02 ?  76  LYS   A CB   1 
ATOM   1706 C CG   . LYS   A 1 76  ? 35.510 -5.884  -6.732  1.00 14.78 ?  76  LYS   A CG   1 
ATOM   1707 C CD   . LYS   A 1 76  ? 36.025 -7.301  -6.559  1.00 16.06 ?  76  LYS   A CD   1 
ATOM   1708 C CE   . LYS   A 1 76  ? 37.520 -7.377  -6.774  1.00 18.57 ?  76  LYS   A CE   1 
ATOM   1709 N NZ   . LYS   A 1 76  ? 38.017 -8.745  -6.561  1.00 19.47 ?  76  LYS   A NZ   1 
ATOM   1710 H H    . LYS   A 1 76  ? 34.278 -4.139  -4.717  1.00 12.37 ?  76  LYS   A H    1 
ATOM   1711 H HA   . LYS   A 1 76  ? 33.645 -3.873  -7.322  1.00 13.09 ?  76  LYS   A HA   1 
ATOM   1712 H HB2  . LYS   A 1 76  ? 33.763 -6.224  -5.735  1.00 15.65 ?  76  LYS   A HB2  1 
ATOM   1713 H HB3  . LYS   A 1 76  ? 33.582 -6.215  -7.310  1.00 15.65 ?  76  LYS   A HB3  1 
ATOM   1714 H HG2  . LYS   A 1 76  ? 35.749 -5.583  -7.623  1.00 17.75 ?  76  LYS   A HG2  1 
ATOM   1715 H HG3  . LYS   A 1 76  ? 35.948 -5.324  -6.068  1.00 17.75 ?  76  LYS   A HG3  1 
ATOM   1716 H HD2  . LYS   A 1 76  ? 35.829 -7.605  -5.659  1.00 19.29 ?  76  LYS   A HD2  1 
ATOM   1717 H HD3  . LYS   A 1 76  ? 35.593 -7.878  -7.209  1.00 19.29 ?  76  LYS   A HD3  1 
ATOM   1718 H HE2  . LYS   A 1 76  ? 37.726 -7.112  -7.683  1.00 22.30 ?  76  LYS   A HE2  1 
ATOM   1719 H HE3  . LYS   A 1 76  ? 37.963 -6.790  -6.141  1.00 22.30 ?  76  LYS   A HE3  1 
ATOM   1720 H HZ1  . LYS   A 1 76  ? 38.895 -8.779  -6.691  1.00 23.38 ?  76  LYS   A HZ1  1 
ATOM   1721 H HZ2  . LYS   A 1 76  ? 37.836 -9.015  -5.731  1.00 23.38 ?  76  LYS   A HZ2  1 
ATOM   1722 H HZ3  . LYS   A 1 76  ? 37.621 -9.308  -7.133  1.00 23.38 ?  76  LYS   A HZ3  1 
ATOM   1723 N N    . VAL   A 1 77  ? 31.181 -4.382  -7.393  1.00 10.02 ?  77  VAL   A N    1 
ATOM   1724 C CA   . VAL   A 1 77  ? 29.774 -4.768  -7.310  1.00 9.89  ?  77  VAL   A CA   1 
ATOM   1725 C C    . VAL   A 1 77  ? 29.708 -6.222  -6.867  1.00 9.07  ?  77  VAL   A C    1 
ATOM   1726 O O    . VAL   A 1 77  ? 30.371 -7.093  -7.445  1.00 9.77  ?  77  VAL   A O    1 
ATOM   1727 C CB   . VAL   A 1 77  ? 29.048 -4.541  -8.645  1.00 10.83 ?  77  VAL   A CB   1 
ATOM   1728 C CG1  . VAL   A 1 77  ? 27.590 -4.977  -8.532  1.00 11.68 ?  77  VAL   A CG1  1 
ATOM   1729 C CG2  . VAL   A 1 77  ? 29.128 -3.080  -9.054  1.00 12.60 ?  77  VAL   A CG2  1 
ATOM   1730 H H    . VAL   A 1 77  ? 31.461 -4.145  -8.170  1.00 12.04 ?  77  VAL   A H    1 
ATOM   1731 H HA   . VAL   A 1 77  ? 29.343 -4.224  -6.633  1.00 11.89 ?  77  VAL   A HA   1 
ATOM   1732 H HB   . VAL   A 1 77  ? 29.481 -5.070  -9.336  1.00 13.02 ?  77  VAL   A HB   1 
ATOM   1733 H HG11 . VAL   A 1 77  ? 27.116 -4.679  -9.323  1.00 14.04 ?  77  VAL   A HG11 1 
ATOM   1734 H HG12 . VAL   A 1 77  ? 27.554 -5.942  -8.465  1.00 14.04 ?  77  VAL   A HG12 1 
ATOM   1735 H HG13 . VAL   A 1 77  ? 27.205 -4.571  -7.741  1.00 14.04 ?  77  VAL   A HG13 1 
ATOM   1736 H HG21 . VAL   A 1 77  ? 28.627 -2.957  -9.873  1.00 15.14 ?  77  VAL   A HG21 1 
ATOM   1737 H HG22 . VAL   A 1 77  ? 28.750 -2.536  -8.346  1.00 15.14 ?  77  VAL   A HG22 1 
ATOM   1738 H HG23 . VAL   A 1 77  ? 30.058 -2.839  -9.194  1.00 15.14 ?  77  VAL   A HG23 1 
ATOM   1739 N N    . GLY   A 1 78  ? 28.914 -6.492  -5.830  1.00 9.11  ?  78  GLY   A N    1 
ATOM   1740 C CA   . GLY   A 1 78  ? 28.883 -7.779  -5.170  1.00 9.33  ?  78  GLY   A CA   1 
ATOM   1741 C C    . GLY   A 1 78  ? 29.811 -7.884  -3.980  1.00 8.84  ?  78  GLY   A C    1 
ATOM   1742 O O    . GLY   A 1 78  ? 29.758 -8.891  -3.262  1.00 9.46  ?  78  GLY   A O    1 
ATOM   1743 H H    . GLY   A 1 78  ? 28.359 -5.920  -5.497  1.00 10.95 ?  78  GLY   A H    1 
ATOM   1744 H HA2  . GLY   A 1 78  ? 27.980 -7.955  -4.867  1.00 11.21 ?  78  GLY   A HA2  1 
ATOM   1745 H HA3  . GLY   A 1 78  ? 29.129 -8.465  -5.809  1.00 11.21 ?  78  GLY   A HA3  1 
ATOM   1746 N N    . GLY   A 1 79  ? 30.670 -6.888  -3.757  1.00 8.79  ?  79  GLY   A N    1 
ATOM   1747 C CA   . GLY   A 1 79  ? 31.634 -6.913  -2.682  1.00 9.10  ?  79  GLY   A CA   1 
ATOM   1748 C C    . GLY   A 1 79  ? 31.193 -6.112  -1.469  1.00 8.58  ?  79  GLY   A C    1 
ATOM   1749 O O    . GLY   A 1 79  ? 30.072 -5.603  -1.386  1.00 9.10  ?  79  GLY   A O    1 
ATOM   1750 H H    . GLY   A 1 79  ? 30.712 -6.171  -4.235  1.00 10.57 ?  79  GLY   A H    1 
ATOM   1751 H HA2  . GLY   A 1 79  ? 31.779 -7.838  -2.409  1.00 10.95 ?  79  GLY   A HA2  1 
ATOM   1752 H HA3  . GLY   A 1 79  ? 32.478 -6.559  -2.999  1.00 10.95 ?  79  GLY   A HA3  1 
ATOM   1753 N N    . SER   A 1 80  ? 32.106 -6.018  -0.502  1.00 9.41  ?  80  SER   A N    1 
ATOM   1754 C CA   . SER   A 1 80  ? 31.790 -5.391  0.772   1.00 8.86  ?  80  SER   A CA   1 
ATOM   1755 C C    . SER   A 1 80  ? 33.062 -4.946  1.477   1.00 8.88  ?  80  SER   A C    1 
ATOM   1756 O O    . SER   A 1 80  ? 34.176 -5.371  1.144   1.00 10.38 ?  80  SER   A O    1 
ATOM   1757 C CB   . SER   A 1 80  ? 31.018 -6.354  1.684   1.00 9.87  ?  80  SER   A CB   1 
ATOM   1758 O OG   . SER   A 1 80  ? 31.847 -7.405  2.157   1.00 11.46 ?  80  SER   A OG   1 
ATOM   1759 H H    . SER   A 1 80  ? 32.920 -6.297  -0.572  1.00 11.31 ?  80  SER   A H    1 
ATOM   1760 H HA   . SER   A 1 80  ? 31.241 -4.611  0.597   1.00 10.65 ?  80  SER   A HA   1 
ATOM   1761 H HB2  . SER   A 1 80  ? 30.680 -5.857  2.442   1.00 11.87 ?  80  SER   A HB2  1 
ATOM   1762 H HB3  . SER   A 1 80  ? 30.281 -6.736  1.181   1.00 11.87 ?  80  SER   A HB3  1 
ATOM   1763 H HG   . SER   A 1 80  ? 32.150 -7.845  1.501   1.00 13.77 ?  80  SER   A HG   1 
ATOM   1764 N N    . CYS   A 1 81  ? 32.873 -4.099  2.486   1.00 8.44  ?  81  CYS   A N    1 
ATOM   1765 C CA   . CYS   A 1 81  ? 33.925 -3.820  3.450   1.00 8.51  ?  81  CYS   A CA   1 
ATOM   1766 C C    . CYS   A 1 81  ? 33.284 -3.590  4.808   1.00 8.33  ?  81  CYS   A C    1 
ATOM   1767 O O    . CYS   A 1 81  ? 32.118 -3.193  4.902   1.00 9.57  ?  81  CYS   A O    1 
ATOM   1768 C CB   . CYS   A 1 81  ? 34.802 -2.637  3.035   1.00 9.58  ?  81  CYS   A CB   1 
ATOM   1769 S SG   . CYS   A 1 81  ? 33.920 -1.050  3.055   1.00 9.36  ?  81  CYS   A SG   1 
ATOM   1770 H H    . CYS   A 1 81  ? 32.133 -3.674  2.638   1.00 10.15 ?  81  CYS   A H    1 
ATOM   1771 H HA   . CYS   A 1 81  ? 34.494 -4.602  3.518   1.00 10.23 ?  81  CYS   A HA   1 
ATOM   1772 H HB2  . CYS   A 1 81  ? 35.556 -2.576  3.644   1.00 11.52 ?  81  CYS   A HB2  1 
ATOM   1773 H HB3  . CYS   A 1 81  ? 35.128 -2.792  2.130   1.00 11.52 ?  81  CYS   A HB3  1 
ATOM   1774 H HG   . CYS   A 1 81  ? 34.678 -0.178  2.719   1.00 11.25 ?  81  CYS   A HG   1 
ATOM   1775 N N    . VAL   A 1 82  ? 34.055 -3.854  5.856   1.00 8.80  ?  82  VAL   A N    1 
ATOM   1776 C CA   . VAL   A 1 82  ? 33.627 -3.618  7.229   1.00 8.95  ?  82  VAL   A CA   1 
ATOM   1777 C C    . VAL   A 1 82  ? 34.237 -2.311  7.710   1.00 9.36  ?  82  VAL   A C    1 
ATOM   1778 O O    . VAL   A 1 82  ? 35.465 -2.149  7.704   1.00 10.19 ?  82  VAL   A O    1 
ATOM   1779 C CB   . VAL   A 1 82  ? 34.040 -4.769  8.160   1.00 10.64 ?  82  VAL   A CB   1 
ATOM   1780 C CG1  . VAL   A 1 82  ? 33.602 -4.468  9.588   1.00 11.84 ?  82  VAL   A CG1  1 
ATOM   1781 C CG2  . VAL   A 1 82  ? 33.475 -6.095  7.686   1.00 11.95 ?  82  VAL   A CG2  1 
ATOM   1782 H H    . VAL   A 1 82  ? 34.853 -4.186  5.798   1.00 10.58 ?  82  VAL   A H    1 
ATOM   1783 H HA   . VAL   A 1 82  ? 32.661 -3.533  7.254   1.00 10.76 ?  82  VAL   A HA   1 
ATOM   1784 H HB   . VAL   A 1 82  ? 35.003 -4.838  8.161   1.00 12.79 ?  82  VAL   A HB   1 
ATOM   1785 H HG11 . VAL   A 1 82  ? 33.665 -5.279  10.116  1.00 14.23 ?  82  VAL   A HG11 1 
ATOM   1786 H HG12 . VAL   A 1 82  ? 34.180 -3.785  9.966   1.00 14.23 ?  82  VAL   A HG12 1 
ATOM   1787 H HG13 . VAL   A 1 82  ? 32.682 -4.153  9.581   1.00 14.23 ?  82  VAL   A HG13 1 
ATOM   1788 H HG21 . VAL   A 1 82  ? 33.723 -6.787  8.318   1.00 14.36 ?  82  VAL   A HG21 1 
ATOM   1789 H HG22 . VAL   A 1 82  ? 32.507 -6.027  7.636   1.00 14.36 ?  82  VAL   A HG22 1 
ATOM   1790 H HG23 . VAL   A 1 82  ? 33.838 -6.296  6.811   1.00 14.36 ?  82  VAL   A HG23 1 
ATOM   1791 N N    . LEU   A 1 83  ? 33.385 -1.384  8.143   1.00 8.88  ?  83  LEU   A N    1 
ATOM   1792 C CA   . LEU   A 1 83  ? 33.811 -0.125  8.738   1.00 9.23  ?  83  LEU   A CA   1 
ATOM   1793 C C    . LEU   A 1 83  ? 33.096 0.049   10.076  1.00 9.04  ?  83  LEU   A C    1 
ATOM   1794 O O    . LEU   A 1 83  ? 32.375 -0.842  10.537  1.00 9.56  ?  83  LEU   A O    1 
ATOM   1795 C CB   . LEU   A 1 83  ? 33.570 1.038   7.766   1.00 9.51  ?  83  LEU   A CB   1 
ATOM   1796 C CG   . LEU   A 1 83  ? 34.463 1.033   6.518   1.00 10.35 ?  83  LEU   A CG   1 
ATOM   1797 C CD1  . LEU   A 1 83  ? 34.031 2.090   5.520   1.00 11.06 ?  83  LEU   A CD1  1 
ATOM   1798 C CD2  . LEU   A 1 83  ? 35.936 1.231   6.883   1.00 11.29 ?  83  LEU   A CD2  1 
ATOM   1799 H H    . LEU   A 1 83  ? 32.529 -1.463  8.092   1.00 10.67 ?  83  LEU   A H    1 
ATOM   1800 H HA   . LEU   A 1 83  ? 34.763 -0.165  8.912   1.00 11.09 ?  83  LEU   A HA   1 
ATOM   1801 H HB2  . LEU   A 1 83  ? 32.648 1.008   7.463   1.00 11.43 ?  83  LEU   A HB2  1 
ATOM   1802 H HB3  . LEU   A 1 83  ? 33.727 1.875   8.233   1.00 11.43 ?  83  LEU   A HB3  1 
ATOM   1803 H HG   . LEU   A 1 83  ? 34.384 0.169   6.087   1.00 12.44 ?  83  LEU   A HG   1 
ATOM   1804 H HD11 . LEU   A 1 83  ? 34.616 2.046   4.744   1.00 13.30 ?  83  LEU   A HD11 1 
ATOM   1805 H HD12 . LEU   A 1 83  ? 33.117 1.913   5.252   1.00 13.30 ?  83  LEU   A HD12 1 
ATOM   1806 H HD13 . LEU   A 1 83  ? 34.096 2.962   5.934   1.00 13.30 ?  83  LEU   A HD13 1 
ATOM   1807 H HD21 . LEU   A 1 83  ? 36.451 1.366   6.067   1.00 13.57 ?  83  LEU   A HD21 1 
ATOM   1808 H HD22 . LEU   A 1 83  ? 36.022 2.012   7.454   1.00 13.57 ?  83  LEU   A HD22 1 
ATOM   1809 H HD23 . LEU   A 1 83  ? 36.262 0.445   7.348   1.00 13.57 ?  83  LEU   A HD23 1 
ATOM   1810 N N    . SER   A 1 84  ? 33.311 1.192   10.717  1.00 9.66  ?  84  SER   A N    1 
ATOM   1811 C CA   . SER   A 1 84  ? 32.664 1.441   11.993  1.00 9.92  ?  84  SER   A CA   1 
ATOM   1812 C C    . SER   A 1 84  ? 31.148 1.531   11.841  1.00 9.68  ?  84  SER   A C    1 
ATOM   1813 O O    . SER   A 1 84  ? 30.630 2.010   10.833  1.00 9.86  ?  84  SER   A O    1 
ATOM   1814 C CB   . SER   A 1 84  ? 33.163 2.761   12.570  1.00 10.60 ?  84  SER   A CB   1 
ATOM   1815 O OG   . SER   A 1 84  ? 32.537 3.033   13.807  1.00 11.47 ?  84  SER   A OG   1 
ATOM   1816 H H    . SER   A 1 84  ? 33.827 1.831   10.433  1.00 11.61 ?  84  SER   A H    1 
ATOM   1817 H HA   . SER   A 1 84  ? 32.882 0.730   12.609  1.00 11.92 ?  84  SER   A HA   1 
ATOM   1818 H HB2  . SER   A 1 84  ? 34.124 2.711   12.705  1.00 12.74 ?  84  SER   A HB2  1 
ATOM   1819 H HB3  . SER   A 1 84  ? 32.957 3.481   11.948  1.00 12.74 ?  84  SER   A HB3  1 
ATOM   1820 H HG   . SER   A 1 84  ? 32.816 3.763   14.123  1.00 13.78 ?  84  SER   A HG   1 
ATOM   1821 N N    . GLY   A 1 85  ? 30.434 1.106   12.881  1.00 10.31 ?  85  GLY   A N    1 
ATOM   1822 C CA   . GLY   A 1 85  ? 29.013 1.361   12.966  1.00 10.97 ?  85  GLY   A CA   1 
ATOM   1823 C C    . GLY   A 1 85  ? 28.659 2.667   13.632  1.00 10.35 ?  85  GLY   A C    1 
ATOM   1824 O O    . GLY   A 1 85  ? 27.474 2.983   13.764  1.00 10.83 ?  85  GLY   A O    1 
ATOM   1825 H H    . GLY   A 1 85  ? 30.763 0.672   13.547  1.00 12.39 ?  85  GLY   A H    1 
ATOM   1826 H HA2  . GLY   A 1 85  ? 28.642 1.365   12.071  1.00 13.18 ?  85  GLY   A HA2  1 
ATOM   1827 H HA3  . GLY   A 1 85  ? 28.598 0.647   13.465  1.00 13.18 ?  85  GLY   A HA3  1 
ATOM   1828 N N    . HIS   A 1 86  ? 29.653 3.431   14.071  1.00 10.09 ?  86  HIS   A N    1 
ATOM   1829 C CA   . HIS   A 1 86  ? 29.441 4.758   14.662  1.00 10.75 ?  86  HIS   A CA   1 
ATOM   1830 C C    . HIS   A 1 86  ? 28.455 4.629   15.817  1.00 11.44 ?  86  HIS   A C    1 
ATOM   1831 O O    . HIS   A 1 86  ? 28.623 3.741   16.665  1.00 12.42 ?  86  HIS   A O    1 
ATOM   1832 C CB   . HIS   A 1 86  ? 29.065 5.758   13.575  1.00 11.09 ?  86  HIS   A CB   1 
ATOM   1833 C CG   . HIS   A 1 86  ? 30.113 5.867   12.529  1.00 11.08 ?  86  HIS   A CG   1 
ATOM   1834 N ND1  . HIS   A 1 86  ? 31.206 6.695   12.669  1.00 11.86 ?  86  HIS   A ND1  1 
ATOM   1835 C CD2  . HIS   A 1 86  ? 30.292 5.189   11.374  1.00 10.85 ?  86  HIS   A CD2  1 
ATOM   1836 C CE1  . HIS   A 1 86  ? 31.998 6.542   11.623  1.00 11.62 ?  86  HIS   A CE1  1 
ATOM   1837 N NE2  . HIS   A 1 86  ? 31.473 5.628   10.828  1.00 10.93 ?  86  HIS   A NE2  1 
ATOM   1838 H H    . HIS   A 1 86  ? 30.479 3.198   14.055  1.00 12.13 ?  86  HIS   A H    1 
ATOM   1839 H HA   . HIS   A 1 86  ? 30.283 5.058   15.039  1.00 12.92 ?  86  HIS   A HA   1 
ATOM   1840 H HB2  . HIS   A 1 86  ? 28.243 5.482   13.148  1.00 13.33 ?  86  HIS   A HB2  1 
ATOM   1841 H HB3  . HIS   A 1 86  ? 28.953 6.641   13.972  1.00 13.33 ?  86  HIS   A HB3  1 
ATOM   1842 H HD2  . HIS   A 1 86  ? 29.730 4.537   11.019  1.00 13.04 ?  86  HIS   A HD2  1 
ATOM   1843 H HE1  . HIS   A 1 86  ? 32.796 6.999   11.461  1.00 13.97 ?  86  HIS   A HE1  1 
ATOM   1844 H HE2  . HIS   A 1 86  ? 31.809 5.359   10.076  1.00 13.13 ?  86  HIS   A HE2  1 
ATOM   1845 N N    . ASN   A 1 87  ? 27.451 5.490   15.894  1.00 12.06 ?  87  ASN   A N    1 
ATOM   1846 C CA   . ASN   A 1 87  ? 26.461 5.478   16.954  1.00 13.20 ?  87  ASN   A CA   1 
ATOM   1847 C C    . ASN   A 1 87  ? 25.337 4.485   16.707  1.00 14.35 ?  87  ASN   A C    1 
ATOM   1848 O O    . ASN   A 1 87  ? 24.416 4.417   17.525  1.00 16.98 ?  87  ASN   A O    1 
ATOM   1849 C CB   . ASN   A 1 87  ? 25.869 6.883   17.126  1.00 14.16 ?  87  ASN   A CB   1 
ATOM   1850 C CG   . ASN   A 1 87  ? 25.350 7.474   15.816  1.00 14.88 ?  87  ASN   A CG   1 
ATOM   1851 O OD1  . ASN   A 1 87  ? 25.990 7.378   14.768  1.00 15.59 ?  87  ASN   A OD1  1 
ATOM   1852 N ND2  . ASN   A 1 87  ? 24.190 8.101   15.880  1.00 15.95 ?  87  ASN   A ND2  1 
ATOM   1853 H H    . ASN   A 1 87  ? 27.327 6.121   15.329  1.00 14.49 ?  87  ASN   A H    1 
ATOM   1854 H HA   . ASN   A 1 87  ? 26.891 5.231   17.790  1.00 15.86 ?  87  ASN   A HA   1 
ATOM   1855 H HB2  . ASN   A 1 87  ? 25.123 6.832   17.755  1.00 17.01 ?  87  ASN   A HB2  1 
ATOM   1856 H HB3  . ASN   A 1 87  ? 26.552 7.471   17.479  1.00 17.01 ?  87  ASN   A HB3  1 
ATOM   1857 H HD21 . ASN   A 1 87  ? 23.857 8.454   15.175  1.00 19.16 ?  87  ASN   A HD21 1 
ATOM   1858 H HD22 . ASN   A 1 87  ? 23.768 8.156   16.632  1.00 19.16 ?  87  ASN   A HD22 1 
ATOM   1859 N N    . LEU   A 1 88  ? 25.393 3.706   15.626  1.00 13.14 ?  88  LEU   A N    1 
ATOM   1860 C CA   . LEU   A 1 88  ? 24.278 2.847   15.241  1.00 13.47 ?  88  LEU   A CA   1 
ATOM   1861 C C    . LEU   A 1 88  ? 24.495 1.372   15.547  1.00 13.15 ?  88  LEU   A C    1 
ATOM   1862 O O    . LEU   A 1 88  ? 23.518 0.643   15.743  1.00 14.49 ?  88  LEU   A O    1 
ATOM   1863 C CB   . LEU   A 1 88  ? 24.009 2.990   13.742  1.00 14.30 ?  88  LEU   A CB   1 
ATOM   1864 C CG   . LEU   A 1 88  ? 23.732 4.408   13.244  1.00 16.17 ?  88  LEU   A CG   1 
ATOM   1865 C CD1  . LEU   A 1 88  ? 23.533 4.399   11.739  1.00 16.40 ?  88  LEU   A CD1  1 
ATOM   1866 C CD2  . LEU   A 1 88  ? 22.521 5.008   13.948  1.00 17.83 ?  88  LEU   A CD2  1 
ATOM   1867 H H    . LEU   A 1 88  ? 26.077 3.655   15.094  1.00 15.78 ?  88  LEU   A H    1 
ATOM   1868 H HA   . LEU   A 1 88  ? 23.488 3.137   15.715  1.00 16.18 ?  88  LEU   A HA   1 
ATOM   1869 H HB2  . LEU   A 1 88  ? 24.778 2.660   13.255  1.00 17.18 ?  88  LEU   A HB2  1 
ATOM   1870 H HB3  . LEU   A 1 88  ? 23.231 2.453   13.520  1.00 17.18 ?  88  LEU   A HB3  1 
ATOM   1871 H HG   . LEU   A 1 88  ? 24.500 4.968   13.436  1.00 19.43 ?  88  LEU   A HG   1 
ATOM   1872 H HD11 . LEU   A 1 88  ? 23.382 5.306   11.432  1.00 19.69 ?  88  LEU   A HD11 1 
ATOM   1873 H HD12 . LEU   A 1 88  ? 24.330 4.036   11.317  1.00 19.69 ?  88  LEU   A HD12 1 
ATOM   1874 H HD13 . LEU   A 1 88  ? 22.766 3.844   11.525  1.00 19.69 ?  88  LEU   A HD13 1 
ATOM   1875 H HD21 . LEU   A 1 88  ? 22.304 5.857   13.532  1.00 21.42 ?  88  LEU   A HD21 1 
ATOM   1876 H HD22 . LEU   A 1 88  ? 21.775 4.396   13.865  1.00 21.42 ?  88  LEU   A HD22 1 
ATOM   1877 H HD23 . LEU   A 1 88  ? 22.738 5.144   14.883  1.00 21.42 ?  88  LEU   A HD23 1 
ATOM   1878 N N    . ALA   A 1 89  ? 25.741 0.919   15.570  1.00 12.09 ?  89  ALA   A N    1 
ATOM   1879 C CA   . ALA   A 1 89  ? 26.071 -0.496  15.659  1.00 11.29 ?  89  ALA   A CA   1 
ATOM   1880 C C    . ALA   A 1 89  ? 27.558 -0.569  15.960  1.00 11.70 ?  89  ALA   A C    1 
ATOM   1881 O O    . ALA   A 1 89  ? 28.273 0.427   15.839  1.00 12.70 ?  89  ALA   A O    1 
ATOM   1882 C CB   . ALA   A 1 89  ? 25.772 -1.205  14.338  1.00 11.34 ?  89  ALA   A CB   1 
ATOM   1883 H H    . ALA   A 1 89  ? 26.437 1.427   15.524  1.00 14.52 ?  89  ALA   A H    1 
ATOM   1884 H HA   . ALA   A 1 89  ? 25.571 -0.913  16.380  1.00 13.57 ?  89  ALA   A HA   1 
ATOM   1885 H HB1  . ALA   A 1 89  ? 26.022 -2.142  14.420  1.00 13.62 ?  89  ALA   A HB1  1 
ATOM   1886 H HB2  . ALA   A 1 89  ? 24.820 -1.138  14.151  1.00 13.62 ?  89  ALA   A HB2  1 
ATOM   1887 H HB3  . ALA   A 1 89  ? 26.281 -0.788  13.631  1.00 13.62 ?  89  ALA   A HB3  1 
ATOM   1888 N N    . LYS   A 1 90  ? 28.037 -1.753  16.338  1.00 12.55 ?  90  LYS   A N    1 
ATOM   1889 C CA   . LYS   A 1 90  ? 29.481 -1.903  16.484  1.00 13.55 ?  90  LYS   A CA   1 
ATOM   1890 C C    . LYS   A 1 90  ? 30.178 -1.700  15.141  1.00 12.43 ?  90  LYS   A C    1 
ATOM   1891 O O    . LYS   A 1 90  ? 31.111 -0.889  15.019  1.00 13.69 ?  90  LYS   A O    1 
ATOM   1892 C CB   . LYS   A 1 90  ? 29.819 -3.268  17.088  1.00 16.22 ?  90  LYS   A CB   1 
ATOM   1893 C CG   . LYS   A 1 90  ? 31.291 -3.415  17.431  1.00 20.67 ?  90  LYS   A CG   1 
ATOM   1894 C CD   . LYS   A 1 90  ? 31.544 -4.651  18.276  1.00 25.37 ?  90  LYS   A CD   1 
ATOM   1895 C CE   . LYS   A 1 90  ? 32.953 -4.657  18.850  1.00 29.05 ?  90  LYS   A CE   1 
ATOM   1896 N NZ   . LYS   A 1 90  ? 33.992 -4.845  17.802  1.00 31.19 ?  90  LYS   A NZ   1 
ATOM   1897 H H    . LYS   A 1 90  ? 27.566 -2.450  16.512  1.00 15.08 ?  90  LYS   A H    1 
ATOM   1898 H HA   . LYS   A 1 90  ? 29.805 -1.222  17.092  1.00 16.28 ?  90  LYS   A HA   1 
ATOM   1899 H HB2  . LYS   A 1 90  ? 29.304 -3.387  17.905  1.00 19.48 ?  90  LYS   A HB2  1 
ATOM   1900 H HB3  . LYS   A 1 90  ? 29.586 -3.961  16.451  1.00 19.48 ?  90  LYS   A HB3  1 
ATOM   1901 H HG2  . LYS   A 1 90  ? 31.803 -3.496  16.613  1.00 24.82 ?  90  LYS   A HG2  1 
ATOM   1902 H HG3  . LYS   A 1 90  ? 31.581 -2.638  17.935  1.00 24.82 ?  90  LYS   A HG3  1 
ATOM   1903 H HD2  . LYS   A 1 90  ? 30.915 -4.671  19.015  1.00 30.46 ?  90  LYS   A HD2  1 
ATOM   1904 H HD3  . LYS   A 1 90  ? 31.438 -5.444  17.726  1.00 30.46 ?  90  LYS   A HD3  1 
ATOM   1905 H HE2  . LYS   A 1 90  ? 33.120 -3.808  19.290  1.00 34.88 ?  90  LYS   A HE2  1 
ATOM   1906 H HE3  . LYS   A 1 90  ? 33.034 -5.383  19.489  1.00 34.88 ?  90  LYS   A HE3  1 
ATOM   1907 H HZ1  . LYS   A 1 90  ? 34.802 -4.844  18.173  1.00 37.45 ?  90  LYS   A HZ1  1 
ATOM   1908 H HZ2  . LYS   A 1 90  ? 33.867 -5.623  17.387  1.00 37.45 ?  90  LYS   A HZ2  1 
ATOM   1909 H HZ3  . LYS   A 1 90  ? 33.946 -4.187  17.206  1.00 37.45 ?  90  LYS   A HZ3  1 
ATOM   1910 N N    . HIS   A 1 91  ? 29.702 -2.402  14.114  1.00 10.79 ?  91  HIS   A N    1 
ATOM   1911 C CA   . HIS   A 1 91  ? 30.272 -2.377  12.782  1.00 10.12 ?  91  HIS   A CA   1 
ATOM   1912 C C    . HIS   A 1 91  ? 29.182 -2.094  11.765  1.00 9.17  ?  91  HIS   A C    1 
ATOM   1913 O O    . HIS   A 1 91  ? 28.016 -2.449  11.966  1.00 9.65  ?  91  HIS   A O    1 
ATOM   1914 C CB   . HIS   A 1 91  ? 30.865 -3.745  12.411  1.00 12.18 ?  91  HIS   A CB   1 
ATOM   1915 C CG   . HIS   A 1 91  ? 31.855 -4.273  13.400  1.00 16.82 ?  91  HIS   A CG   1 
ATOM   1916 N ND1  . HIS   A 1 91  ? 33.133 -3.774  13.514  1.00 19.09 ?  91  HIS   A ND1  1 
ATOM   1917 C CD2  . HIS   A 1 91  ? 31.761 -5.276  14.306  1.00 18.88 ?  91  HIS   A CD2  1 
ATOM   1918 C CE1  . HIS   A 1 91  ? 33.783 -4.440  14.453  1.00 19.97 ?  91  HIS   A CE1  1 
ATOM   1919 N NE2  . HIS   A 1 91  ? 32.972 -5.357  14.950  1.00 20.17 ?  91  HIS   A NE2  1 
ATOM   1920 H H    . HIS   A 1 91  ? 29.020 -2.937  14.180  1.00 12.97 ?  91  HIS   A H    1 
ATOM   1921 H HA   . HIS   A 1 91  ? 30.959 -1.701  12.723  1.00 12.16 ?  91  HIS   A HA   1 
ATOM   1922 H HB2  . HIS   A 1 91  ? 30.145 -4.395  12.347  1.00 14.63 ?  91  HIS   A HB2  1 
ATOM   1923 H HB3  . HIS   A 1 91  ? 31.316 -3.672  11.558  1.00 14.63 ?  91  HIS   A HB3  1 
ATOM   1924 H HD1  . HIS   A 1 91  ? 33.458 -3.130  13.046  1.00 22.92 ?  91  HIS   A HD1  1 
ATOM   1925 H HD2  . HIS   A 1 91  ? 31.020 -5.810  14.470  1.00 22.68 ?  91  HIS   A HD2  1 
ATOM   1926 H HE1  . HIS   A 1 91  ? 34.664 -4.284  14.720  1.00 23.98 ?  91  HIS   A HE1  1 
ATOM   1927 N N    . CYS   A 1 92  ? 29.587 -1.495  10.649  1.00 8.97  ?  92  CYS   A N    1 
ATOM   1928 C CA   . CYS   A 1 92  ? 28.748 -1.413  9.464   1.00 8.73  ?  92  CYS   A CA   1 
ATOM   1929 C C    . CYS   A 1 92  ? 29.391 -2.233  8.354   1.00 8.26  ?  92  CYS   A C    1 
ATOM   1930 O O    . CYS   A 1 92  ? 30.553 -1.988  7.989   1.00 8.97  ?  92  CYS   A O    1 
ATOM   1931 C CB   . CYS   A 1 92  ? 28.541 0.031   9.007   1.00 9.31  ?  92  CYS   A CB   1 
ATOM   1932 S SG   . CYS   A 1 92  ? 27.524 0.150   7.505   1.00 8.85  ?  92  CYS   A SG   1 
ATOM   1933 H H    . CYS   A 1 92  ? 30.358 -1.124  10.553  1.00 10.78 ?  92  CYS   A H    1 
ATOM   1934 H HA   . CYS   A 1 92  ? 27.879 -1.794  9.660   1.00 10.49 ?  92  CYS   A HA   1 
ATOM   1935 H HB2  . CYS   A 1 92  ? 28.095 0.528   9.713   1.00 11.19 ?  92  CYS   A HB2  1 
ATOM   1936 H HB3  . CYS   A 1 92  ? 29.403 0.431   8.814   1.00 11.19 ?  92  CYS   A HB3  1 
ATOM   1937 H HG   . CYS   A 1 92  ? 27.390 1.302   7.216   1.00 10.64 ?  92  CYS   A HG   1 
ATOM   1938 N N    . LEU   A 1 93  ? 28.645 -3.211  7.843   1.00 8.11  ?  93  LEU   A N    1 
ATOM   1939 C CA   . LEU   A 1 93  ? 29.042 -3.965  6.660   1.00 7.64  ?  93  LEU   A CA   1 
ATOM   1940 C C    . LEU   A 1 93  ? 28.452 -3.259  5.443   1.00 7.26  ?  93  LEU   A C    1 
ATOM   1941 O O    . LEU   A 1 93  ? 27.236 -3.314  5.211   1.00 7.62  ?  93  LEU   A O    1 
ATOM   1942 C CB   . LEU   A 1 93  ? 28.551 -5.408  6.762   1.00 8.08  ?  93  LEU   A CB   1 
ATOM   1943 C CG   . LEU   A 1 93  ? 28.929 -6.306  5.585   1.00 8.59  ?  93  LEU   A CG   1 
ATOM   1944 C CD1  . LEU   A 1 93  ? 30.437 -6.561  5.562   1.00 9.97  ?  93  LEU   A CD1  1 
ATOM   1945 C CD2  . LEU   A 1 93  ? 28.154 -7.629  5.619   1.00 9.30  ?  93  LEU   A CD2  1 
ATOM   1946 H H    . LEU   A 1 93  ? 27.889 -3.454  8.174   1.00 9.75  ?  93  LEU   A H    1 
ATOM   1947 H HA   . LEU   A 1 93  ? 30.007 -3.966  6.588   1.00 9.19  ?  93  LEU   A HA   1 
ATOM   1948 H HB2  . LEU   A 1 93  ? 28.927 -5.804  7.566   1.00 9.71  ?  93  LEU   A HB2  1 
ATOM   1949 H HB3  . LEU   A 1 93  ? 27.585 -5.402  6.825   1.00 9.71  ?  93  LEU   A HB3  1 
ATOM   1950 H HG   . LEU   A 1 93  ? 28.703 -5.856  4.763   1.00 10.32 ?  93  LEU   A HG   1 
ATOM   1951 H HD11 . LEU   A 1 93  ? 30.649 -7.183  4.846   1.00 11.98 ?  93  LEU   A HD11 1 
ATOM   1952 H HD12 . LEU   A 1 93  ? 30.907 -5.726  5.425   1.00 11.98 ?  93  LEU   A HD12 1 
ATOM   1953 H HD13 . LEU   A 1 93  ? 30.711 -6.953  6.416   1.00 11.98 ?  93  LEU   A HD13 1 
ATOM   1954 H HD21 . LEU   A 1 93  ? 28.426 -8.171  4.858   1.00 11.18 ?  93  LEU   A HD21 1 
ATOM   1955 H HD22 . LEU   A 1 93  ? 28.357 -8.097  6.443   1.00 11.18 ?  93  LEU   A HD22 1 
ATOM   1956 H HD23 . LEU   A 1 93  ? 27.206 -7.440  5.567   1.00 11.18 ?  93  LEU   A HD23 1 
ATOM   1957 N N    . HIS   A 1 94  ? 29.308 -2.571  4.689   1.00 7.20  ?  94  HIS   A N    1 
ATOM   1958 C CA   . HIS   A 1 94  ? 28.893 -1.886  3.470   1.00 7.43  ?  94  HIS   A CA   1 
ATOM   1959 C C    . HIS   A 1 94  ? 28.892 -2.912  2.352   1.00 7.32  ?  94  HIS   A C    1 
ATOM   1960 O O    . HIS   A 1 94  ? 29.953 -3.430  2.003   1.00 9.06  ?  94  HIS   A O    1 
ATOM   1961 C CB   . HIS   A 1 94  ? 29.864 -0.753  3.149   1.00 7.66  ?  94  HIS   A CB   1 
ATOM   1962 C CG   . HIS   A 1 94  ? 29.854 0.343   4.161   1.00 7.46  ?  94  HIS   A CG   1 
ATOM   1963 N ND1  . HIS   A 1 94  ? 28.982 1.410   4.100   1.00 7.79  ?  94  HIS   A ND1  1 
ATOM   1964 C CD2  . HIS   A 1 94  ? 30.582 0.500   5.290   1.00 8.41  ?  94  HIS   A CD2  1 
ATOM   1965 C CE1  . HIS   A 1 94  ? 29.192 2.180   5.153   1.00 8.00  ?  94  HIS   A CE1  1 
ATOM   1966 N NE2  . HIS   A 1 94  ? 30.164 1.658   5.883   1.00 8.40  ?  94  HIS   A NE2  1 
ATOM   1967 H H    . HIS   A 1 94  ? 30.149 -2.485  4.864   1.00 8.66  ?  94  HIS   A H    1 
ATOM   1968 H HA   . HIS   A 1 94  ? 27.997 -1.530  3.575   1.00 8.94  ?  94  HIS   A HA   1 
ATOM   1969 H HB2  . HIS   A 1 94  ? 30.759 -1.112  3.106   1.00 9.21  ?  94  HIS   A HB2  1 
ATOM   1970 H HB3  . HIS   A 1 94  ? 29.616 -0.367  2.293   1.00 9.21  ?  94  HIS   A HB3  1 
ATOM   1971 H HD2  . HIS   A 1 94  ? 31.253 -0.059  5.599   1.00 10.11 ?  94  HIS   A HD2  1 
ATOM   1972 H HE1  . HIS   A 1 94  ? 28.730 2.971   5.342   1.00 9.62  ?  94  HIS   A HE1  1 
ATOM   1973 H HE2  . HIS   A 1 94  ? 30.471 1.996   6.614   1.00 10.10 ?  94  HIS   A HE2  1 
ATOM   1974 N N    . VAL   A 1 95  ? 27.718 -3.231  1.807   1.00 6.98  ?  95  VAL   A N    1 
ATOM   1975 C CA   . VAL   A 1 95  ? 27.574 -4.257  0.776   1.00 7.15  ?  95  VAL   A CA   1 
ATOM   1976 C C    . VAL   A 1 95  ? 27.038 -3.608  -0.487  1.00 7.06  ?  95  VAL   A C    1 
ATOM   1977 O O    . VAL   A 1 95  ? 26.045 -2.873  -0.432  1.00 7.87  ?  95  VAL   A O    1 
ATOM   1978 C CB   . VAL   A 1 95  ? 26.631 -5.391  1.220   1.00 7.93  ?  95  VAL   A CB   1 
ATOM   1979 C CG1  . VAL   A 1 95  ? 26.524 -6.435  0.127   1.00 8.90  ?  95  VAL   A CG1  1 
ATOM   1980 C CG2  . VAL   A 1 95  ? 27.116 -6.008  2.514   1.00 8.20  ?  95  VAL   A CG2  1 
ATOM   1981 H H    . VAL   A 1 95  ? 26.970 -2.862  2.023   1.00 8.40  ?  95  VAL   A H    1 
ATOM   1982 H HA   . VAL   A 1 95  ? 28.435 -4.644  0.576   1.00 8.60  ?  95  VAL   A HA   1 
ATOM   1983 H HB   . VAL   A 1 95  ? 25.743 -5.030  1.375   1.00 9.53  ?  95  VAL   A HB   1 
ATOM   1984 H HG11 . VAL   A 1 95  ? 26.112 -7.240  0.492   1.00 10.70 ?  95  VAL   A HG11 1 
ATOM   1985 H HG12 . VAL   A 1 95  ? 25.980 -6.094  -0.599  1.00 10.70 ?  95  VAL   A HG12 1 
ATOM   1986 H HG13 . VAL   A 1 95  ? 27.414 -6.650  -0.198  1.00 10.70 ?  95  VAL   A HG13 1 
ATOM   1987 H HG21 . VAL   A 1 95  ? 26.555 -6.766  2.735   1.00 9.86  ?  95  VAL   A HG21 1 
ATOM   1988 H HG22 . VAL   A 1 95  ? 28.035 -6.295  2.401   1.00 9.86  ?  95  VAL   A HG22 1 
ATOM   1989 H HG23 . VAL   A 1 95  ? 27.063 -5.340  3.219   1.00 9.86  ?  95  VAL   A HG23 1 
ATOM   1990 N N    A VAL   A 1 96  ? 27.673 -3.889  -1.621  0.50 7.11  ?  96  VAL   A N    1 
ATOM   1991 N N    B VAL   A 1 96  ? 27.662 -3.909  -1.624  0.50 7.17  ?  96  VAL   A N    1 
ATOM   1992 C CA   A VAL   A 1 96  ? 27.262 -3.332  -2.905  0.50 7.75  ?  96  VAL   A CA   1 
ATOM   1993 C CA   B VAL   A 1 96  ? 27.276 -3.342  -2.912  0.50 7.80  ?  96  VAL   A CA   1 
ATOM   1994 C C    A VAL   A 1 96  ? 26.448 -4.382  -3.654  0.50 8.16  ?  96  VAL   A C    1 
ATOM   1995 C C    B VAL   A 1 96  ? 26.451 -4.372  -3.678  0.50 7.94  ?  96  VAL   A C    1 
ATOM   1996 O O    A VAL   A 1 96  ? 26.996 -5.339  -4.209  0.50 9.22  ?  96  VAL   A O    1 
ATOM   1997 O O    B VAL   A 1 96  ? 26.996 -5.299  -4.285  0.50 8.57  ?  96  VAL   A O    1 
ATOM   1998 C CB   A VAL   A 1 96  ? 28.452 -2.849  -3.734  0.50 8.08  ?  96  VAL   A CB   1 
ATOM   1999 C CB   B VAL   A 1 96  ? 28.489 -2.891  -3.726  0.50 8.42  ?  96  VAL   A CB   1 
ATOM   2000 C CG1  A VAL   A 1 96  ? 27.944 -2.268  -5.041  0.50 8.09  ?  96  VAL   A CG1  1 
ATOM   2001 C CG1  B VAL   A 1 96  ? 28.015 -2.168  -4.973  0.50 9.08  ?  96  VAL   A CG1  1 
ATOM   2002 C CG2  A VAL   A 1 96  ? 29.269 -1.823  -2.957  0.50 8.51  ?  96  VAL   A CG2  1 
ATOM   2003 C CG2  B VAL   A 1 96  ? 29.409 -2.009  -2.889  0.50 8.63  ?  96  VAL   A CG2  1 
ATOM   2004 H H    A VAL   A 1 96  ? 28.361 -4.404  -1.674  0.50 8.55  ?  96  VAL   A H    1 
ATOM   2005 H H    B VAL   A 1 96  ? 28.334 -4.446  -1.677  0.50 8.62  ?  96  VAL   A H    1 
ATOM   2006 H HA   A VAL   A 1 96  ? 26.688 -2.567  -2.746  0.50 9.32  ?  96  VAL   A HA   1 
ATOM   2007 H HA   B VAL   A 1 96  ? 26.718 -2.564  -2.761  0.50 9.38  ?  96  VAL   A HA   1 
ATOM   2008 H HB   A VAL   A 1 96  ? 29.027 -3.600  -3.941  0.50 9.71  ?  96  VAL   A HB   1 
ATOM   2009 H HB   B VAL   A 1 96  ? 28.993 -3.669  -4.008  0.50 10.12 ?  96  VAL   A HB   1 
ATOM   2010 H HG11 A VAL   A 1 96  ? 28.668 -1.774  -5.464  0.50 9.72  ?  96  VAL   A HG11 1 
ATOM   2011 H HG11 B VAL   A 1 96  ? 28.782 -1.759  -5.408  0.50 10.92 ?  96  VAL   A HG11 1 
ATOM   2012 H HG12 A VAL   A 1 96  ? 27.655 -2.987  -5.619  0.50 9.72  ?  96  VAL   A HG12 1 
ATOM   2013 H HG12 B VAL   A 1 96  ? 27.597 -2.803  -5.571  0.50 10.92 ?  96  VAL   A HG12 1 
ATOM   2014 H HG13 A VAL   A 1 96  ? 27.206 -1.668  -4.854  0.50 9.72  ?  96  VAL   A HG13 1 
ATOM   2015 H HG13 B VAL   A 1 96  ? 27.380 -1.481  -4.716  0.50 10.92 ?  96  VAL   A HG13 1 
ATOM   2016 H HG21 A VAL   A 1 96  ? 29.981 -1.490  -3.523  0.50 10.23 ?  96  VAL   A HG21 1 
ATOM   2017 H HG21 B VAL   A 1 96  ? 30.107 -1.650  -3.457  0.50 10.37 ?  96  VAL   A HG21 1 
ATOM   2018 H HG22 A VAL   A 1 96  ? 28.686 -1.092  -2.692  0.50 10.23 ?  96  VAL   A HG22 1 
ATOM   2019 H HG22 B VAL   A 1 96  ? 28.886 -1.282  -2.510  0.50 10.37 ?  96  VAL   A HG22 1 
ATOM   2020 H HG23 A VAL   A 1 96  ? 29.641 -2.250  -2.169  0.50 10.23 ?  96  VAL   A HG23 1 
ATOM   2021 H HG23 B VAL   A 1 96  ? 29.797 -2.541  -2.179  0.50 10.37 ?  96  VAL   A HG23 1 
ATOM   2022 N N    . GLY   A 1 97  ? 25.131 -4.206  -3.683  1.00 8.24  ?  97  GLY   A N    1 
ATOM   2023 C CA   . GLY   A 1 97  ? 24.296 -4.965  -4.578  1.00 8.32  ?  97  GLY   A CA   1 
ATOM   2024 C C    . GLY   A 1 97  ? 24.312 -4.317  -5.953  1.00 8.58  ?  97  GLY   A C    1 
ATOM   2025 O O    . GLY   A 1 97  ? 24.611 -3.124  -6.100  1.00 9.47  ?  97  GLY   A O    1 
ATOM   2026 H H    A GLY   A 1 97  ? 24.700 -3.641  -3.190  0.50 9.90  ?  97  GLY   A H    1 
ATOM   2027 H H    B GLY   A 1 97  ? 24.701 -3.649  -3.179  0.50 9.90  ?  97  GLY   A H    1 
ATOM   2028 H HA2  . GLY   A 1 97  ? 24.631 -5.873  -4.640  1.00 10.00 ?  97  GLY   A HA2  1 
ATOM   2029 H HA3  . GLY   A 1 97  ? 23.385 -4.988  -4.240  1.00 10.00 ?  97  GLY   A HA3  1 
ATOM   2030 N N    . PRO   A 1 98  ? 23.978 -5.079  -6.990  1.00 8.80  ?  98  PRO   A N    1 
ATOM   2031 C CA   . PRO   A 1 98  ? 23.869 -4.477  -8.321  1.00 10.19 ?  98  PRO   A CA   1 
ATOM   2032 C C    . PRO   A 1 98  ? 22.759 -3.434  -8.373  1.00 10.33 ?  98  PRO   A C    1 
ATOM   2033 O O    . PRO   A 1 98  ? 21.683 -3.608  -7.795  1.00 10.45 ?  98  PRO   A O    1 
ATOM   2034 C CB   . PRO   A 1 98  ? 23.559 -5.676  -9.224  1.00 10.45 ?  98  PRO   A CB   1 
ATOM   2035 C CG   . PRO   A 1 98  ? 22.912 -6.680  -8.314  1.00 10.58 ?  98  PRO   A CG   1 
ATOM   2036 C CD   . PRO   A 1 98  ? 23.647 -6.518  -7.003  1.00 9.35  ?  98  PRO   A CD   1 
ATOM   2037 H HA   . PRO   A 1 98  ? 24.715 -4.078  -8.581  1.00 12.25 ?  98  PRO   A HA   1 
ATOM   2038 H HB2  . PRO   A 1 98  ? 22.946 -5.402  -9.926  1.00 12.56 ?  98  PRO   A HB2  1 
ATOM   2039 H HB3  . PRO   A 1 98  ? 24.380 -6.027  -9.599  1.00 12.56 ?  98  PRO   A HB3  1 
ATOM   2040 H HG2  . PRO   A 1 98  ? 21.973 -6.468  -8.213  1.00 12.72 ?  98  PRO   A HG2  1 
ATOM   2041 H HG3  . PRO   A 1 98  ? 23.035 -7.568  -8.674  1.00 12.72 ?  98  PRO   A HG3  1 
ATOM   2042 H HD2  . PRO   A 1 98  ? 23.063 -6.748  -6.260  1.00 11.24 ?  98  PRO   A HD2  1 
ATOM   2043 H HD3  . PRO   A 1 98  ? 24.455 -7.056  -6.997  1.00 11.24 ?  98  PRO   A HD3  1 
ATOM   2044 N N    A ASN   A 1 99  ? 23.033 -2.325  -9.064  0.50 11.01 ?  99  ASN   A N    1 
ATOM   2045 N N    B ASN   A 1 99  ? 23.040 -2.346  -9.079  0.50 11.65 ?  99  ASN   A N    1 
ATOM   2046 C CA   A ASN   A 1 99  ? 22.061 -1.243  -9.244  0.50 11.68 ?  99  ASN   A CA   1 
ATOM   2047 C CA   B ASN   A 1 99  ? 22.067 -1.298  -9.342  0.50 12.94 ?  99  ASN   A CA   1 
ATOM   2048 C C    A ASN   A 1 99  ? 21.496 -1.358  -10.656 0.50 12.60 ?  99  ASN   A C    1 
ATOM   2049 C C    B ASN   A 1 99  ? 21.473 -1.548  -10.721 0.50 13.58 ?  99  ASN   A C    1 
ATOM   2050 O O    A ASN   A 1 99  ? 22.116 -0.911  -11.629 0.50 12.90 ?  99  ASN   A O    1 
ATOM   2051 O O    B ASN   A 1 99  ? 22.198 -1.561  -11.725 0.50 13.83 ?  99  ASN   A O    1 
ATOM   2052 C CB   A ASN   A 1 99  ? 22.694 0.125   -8.997  0.50 11.97 ?  99  ASN   A CB   1 
ATOM   2053 C CB   B ASN   A 1 99  ? 22.735 0.075   -9.286  0.50 14.18 ?  99  ASN   A CB   1 
ATOM   2054 C CG   A ASN   A 1 99  ? 21.667 1.265   -9.009  0.50 12.68 ?  99  ASN   A CG   1 
ATOM   2055 C CG   B ASN   A 1 99  ? 21.730 1.216   -9.180  0.50 15.34 ?  99  ASN   A CG   1 
ATOM   2056 O OD1  A ASN   A 1 99  ? 20.676 1.221   -9.743  0.50 13.22 ?  99  ASN   A OD1  1 
ATOM   2057 O OD1  B ASN   A 1 99  ? 20.654 1.173   -9.782  0.50 15.53 ?  99  ASN   A OD1  1 
ATOM   2058 N ND2  A ASN   A 1 99  ? 21.914 2.294   -8.200  0.50 13.35 ?  99  ASN   A ND2  1 
ATOM   2059 N ND2  B ASN   A 1 99  ? 22.083 2.244   -8.412  0.50 15.98 ?  99  ASN   A ND2  1 
ATOM   2060 H H    A ASN   A 1 99  ? 23.794 -2.173  -9.437  0.50 13.24 ?  99  ASN   A H    1 
ATOM   2061 H H    B ASN   A 1 99  ? 23.818 -2.187  -9.412  0.50 13.99 ?  99  ASN   A H    1 
ATOM   2062 H HA   A ASN   A 1 99  ? 21.335 -1.360  -8.607  0.50 14.04 ?  99  ASN   A HA   1 
ATOM   2063 H HA   B ASN   A 1 99  ? 21.362 -1.331  -8.672  0.50 15.55 ?  99  ASN   A HA   1 
ATOM   2064 H HB2  A ASN   A 1 99  ? 23.134 0.124   -8.132  0.50 14.38 ?  99  ASN   A HB2  1 
ATOM   2065 H HB2  B ASN   A 1 99  ? 23.324 0.115   -8.513  0.50 17.04 ?  99  ASN   A HB2  1 
ATOM   2066 H HB3  A ASN   A 1 99  ? 23.344 0.300   -9.697  0.50 14.38 ?  99  ASN   A HB3  1 
ATOM   2067 H HB3  B ASN   A 1 99  ? 23.252 0.206   -10.097 0.50 17.04 ?  99  ASN   A HB3  1 
ATOM   2068 H HD21 A ASN   A 1 99  ? 21.368 2.955   -8.170  0.50 16.04 ?  99  ASN   A HD21 1 
ATOM   2069 H HD21 B ASN   A 1 99  ? 21.550 2.909   -8.314  0.50 19.20 ?  99  ASN   A HD21 1 
ATOM   2070 H HD22 A ASN   A 1 99  ? 22.616 2.290   -7.703  0.50 16.04 ?  99  ASN   A HD22 1 
ATOM   2071 H HD22 B ASN   A 1 99  ? 22.845 2.238   -8.008  0.50 19.20 ?  99  ASN   A HD22 1 
ATOM   2072 N N    A VAL   A 1 100 ? 20.307 -1.963  -10.748 0.50 13.57 ?  100 VAL   A N    1 
ATOM   2073 N N    B VAL   A 1 100 ? 20.158 -1.767  -10.765 0.50 13.98 ?  100 VAL   A N    1 
ATOM   2074 C CA   A VAL   A 1 100 ? 19.649 -2.199  -12.031 0.50 15.66 ?  100 VAL   A CA   1 
ATOM   2075 C CA   B VAL   A 1 100 ? 19.500 -1.971  -12.049 0.50 15.82 ?  100 VAL   A CA   1 
ATOM   2076 C C    A VAL   A 1 100 ? 19.536 -0.908  -12.834 0.50 16.30 ?  100 VAL   A C    1 
ATOM   2077 C C    B VAL   A 1 100 ? 19.418 -0.662  -12.823 0.50 15.85 ?  100 VAL   A C    1 
ATOM   2078 O O    A VAL   A 1 100 ? 19.659 -0.913  -14.065 0.50 17.40 ?  100 VAL   A O    1 
ATOM   2079 O O    B VAL   A 1 100 ? 19.393 -0.663  -14.059 0.50 16.36 ?  100 VAL   A O    1 
ATOM   2080 C CB   A VAL   A 1 100 ? 18.280 -2.872  -11.801 0.50 17.00 ?  100 VAL   A CB   1 
ATOM   2081 C CB   B VAL   A 1 100 ? 18.122 -2.629  -11.851 0.50 17.43 ?  100 VAL   A CB   1 
ATOM   2082 C CG1  A VAL   A 1 100 ? 17.528 -3.056  -13.111 0.50 17.85 ?  100 VAL   A CG1  1 
ATOM   2083 C CG1  B VAL   A 1 100 ? 17.437 -2.846  -13.190 0.50 18.40 ?  100 VAL   A CG1  1 
ATOM   2084 C CG2  A VAL   A 1 100 ? 18.465 -4.215  -11.102 0.50 17.69 ?  100 VAL   A CG2  1 
ATOM   2085 C CG2  B VAL   A 1 100 ? 18.269 -3.946  -11.107 0.50 18.10 ?  100 VAL   A CG2  1 
ATOM   2086 H H    A VAL   A 1 100 ? 19.859 -2.258  -10.073 0.50 16.30 ?  100 VAL   A H    1 
ATOM   2087 H H    B VAL   A 1 100 ? 19.639 -1.805  -10.074 0.50 16.79 ?  100 VAL   A H    1 
ATOM   2088 H HA   A VAL   A 1 100 ? 20.188 -2.811  -12.552 0.50 18.81 ?  100 VAL   A HA   1 
ATOM   2089 H HA   B VAL   A 1 100 ? 20.041 -2.584  -12.566 0.50 19.01 ?  100 VAL   A HA   1 
ATOM   2090 H HB   A VAL   A 1 100 ? 17.740 -2.312  -11.223 0.50 20.42 ?  100 VAL   A HB   1 
ATOM   2091 H HB   B VAL   A 1 100 ? 17.564 -2.041  -11.321 0.50 20.93 ?  100 VAL   A HB   1 
ATOM   2092 H HG11 A VAL   A 1 100 ? 16.774 -3.651  -12.963 0.50 21.43 ?  100 VAL   A HG11 1 
ATOM   2093 H HG11 B VAL   A 1 100 ? 16.650 -3.396  -13.053 0.50 22.10 ?  100 VAL   A HG11 1 
ATOM   2094 H HG12 A VAL   A 1 100 ? 17.208 -2.193  -13.417 0.50 21.43 ?  100 VAL   A HG12 1 
ATOM   2095 H HG12 B VAL   A 1 100 ? 17.181 -1.988  -13.561 0.50 22.10 ?  100 VAL   A HG12 1 
ATOM   2096 H HG13 A VAL   A 1 100 ? 18.126 -3.443  -13.768 0.50 21.43 ?  100 VAL   A HG13 1 
ATOM   2097 H HG13 B VAL   A 1 100 ? 18.053 -3.297  -13.790 0.50 22.10 ?  100 VAL   A HG13 1 
ATOM   2098 H HG21 A VAL   A 1 100 ? 17.608 -4.668  -11.052 0.50 21.25 ?  100 VAL   A HG21 1 
ATOM   2099 H HG21 B VAL   A 1 100 ? 17.405 -4.383  -11.067 0.50 21.74 ?  100 VAL   A HG21 1 
ATOM   2100 H HG22 A VAL   A 1 100 ? 19.092 -4.752  -11.612 0.50 21.25 ?  100 VAL   A HG22 1 
ATOM   2101 H HG22 B VAL   A 1 100 ? 18.902 -4.508  -11.582 0.50 21.74 ?  100 VAL   A HG22 1 
ATOM   2102 H HG23 A VAL   A 1 100 ? 18.811 -4.063  -10.209 0.50 21.25 ?  100 VAL   A HG23 1 
ATOM   2103 H HG23 B VAL   A 1 100 ? 18.593 -3.769  -10.210 0.50 21.74 ?  100 VAL   A HG23 1 
ATOM   2104 N N    A ASN   A 1 101 ? 19.317 0.220   -12.158 0.50 17.10 ?  101 ASN   A N    1 
ATOM   2105 N N    B ASN   A 1 101 ? 19.386 0.470   -12.127 0.50 17.40 ?  101 ASN   A N    1 
ATOM   2106 C CA   A ASN   A 1 101 ? 19.238 1.499   -12.857 0.50 18.35 ?  101 ASN   A CA   1 
ATOM   2107 C CA   B ASN   A 1 101 ? 19.380 1.758   -12.805 0.50 19.58 ?  101 ASN   A CA   1 
ATOM   2108 C C    A ASN   A 1 101 ? 20.576 1.924   -13.458 0.50 20.22 ?  101 ASN   A C    1 
ATOM   2109 C C    B ASN   A 1 101 ? 20.759 2.167   -13.314 0.50 21.85 ?  101 ASN   A C    1 
ATOM   2110 O O    A ASN   A 1 101 ? 20.614 2.909   -14.205 0.50 21.20 ?  101 ASN   A O    1 
ATOM   2111 O O    B ASN   A 1 101 ? 20.873 3.199   -13.987 0.50 23.19 ?  101 ASN   A O    1 
ATOM   2112 C CB   A ASN   A 1 101 ? 18.648 2.558   -11.921 0.50 17.81 ?  101 ASN   A CB   1 
ATOM   2113 C CB   B ASN   A 1 101 ? 18.782 2.817   -11.882 0.50 19.98 ?  101 ASN   A CB   1 
ATOM   2114 C CG   A ASN   A 1 101 ? 17.272 2.160   -11.394 0.50 17.06 ?  101 ASN   A CG   1 
ATOM   2115 C CG   B ASN   A 1 101 ? 17.420 2.413   -11.367 0.50 19.85 ?  101 ASN   A CG   1 
ATOM   2116 O OD1  A ASN   A 1 101 ? 16.466 1.568   -12.118 0.50 16.78 ?  101 ASN   A OD1  1 
ATOM   2117 O OD1  B ASN   A 1 101 ? 16.518 2.105   -12.151 0.50 19.87 ?  101 ASN   A OD1  1 
ATOM   2118 N ND2  A ASN   A 1 101 ? 17.004 2.466   -10.129 0.50 16.74 ?  101 ASN   A ND2  1 
ATOM   2119 N ND2  B ASN   A 1 101 ? 17.272 2.371   -10.047 0.50 19.73 ?  101 ASN   A ND2  1 
ATOM   2120 H H    A ASN   A 1 101 ? 19.209 0.273   -11.310 0.50 20.53 ?  101 ASN   A H    1 
ATOM   2121 H H    B ASN   A 1 101 ? 19.356 0.518   -11.268 0.50 20.89 ?  101 ASN   A H    1 
ATOM   2122 H HA   A ASN   A 1 101 ? 18.625 1.406   -13.599 0.50 22.03 ?  101 ASN   A HA   1 
ATOM   2123 H HA   B ASN   A 1 101 ? 18.802 1.686   -13.577 0.50 23.51 ?  101 ASN   A HA   1 
ATOM   2124 H HB2  A ASN   A 1 101 ? 19.237 2.684   -11.162 0.50 21.39 ?  101 ASN   A HB2  1 
ATOM   2125 H HB2  B ASN   A 1 101 ? 19.369 2.948   -11.125 0.50 23.99 ?  101 ASN   A HB2  1 
ATOM   2126 H HB3  A ASN   A 1 101 ? 18.552 3.396   -12.408 0.50 21.39 ?  101 ASN   A HB3  1 
ATOM   2127 H HB3  B ASN   A 1 101 ? 18.678 3.643   -12.378 0.50 23.99 ?  101 ASN   A HB3  1 
ATOM   2128 H HD21 A ASN   A 1 101 ? 16.240 2.263   -9.791  0.50 20.11 ?  101 ASN   A HD21 1 
ATOM   2129 H HD21 B ASN   A 1 101 ? 16.519 2.136   -9.704  0.50 23.70 ?  101 ASN   A HD21 1 
ATOM   2130 H HD22 A ASN   A 1 101 ? 17.589 2.879   -9.652  0.50 20.11 ?  101 ASN   A HD22 1 
ATOM   2131 H HD22 B ASN   A 1 101 ? 17.926 2.593   -9.534  0.50 23.70 ?  101 ASN   A HD22 1 
ATOM   2132 N N    A LYS   A 1 102 ? 21.657 1.193   -13.168 0.50 21.74 ?  102 LYS   A N    1 
ATOM   2133 N N    B LYS   A 1 102 ? 21.799 1.381   -13.020 0.50 23.12 ?  102 LYS   A N    1 
ATOM   2134 C CA   A LYS   A 1 102 ? 22.942 1.352   -13.841 0.50 23.21 ?  102 LYS   A CA   1 
ATOM   2135 C CA   B LYS   A 1 102 ? 23.107 1.538   -13.642 0.50 24.41 ?  102 LYS   A CA   1 
ATOM   2136 C C    A LYS   A 1 102 ? 23.226 0.216   -14.821 0.50 23.30 ?  102 LYS   A C    1 
ATOM   2137 C C    B LYS   A 1 102 ? 23.404 0.471   -14.686 0.50 24.96 ?  102 LYS   A C    1 
ATOM   2138 O O    A LYS   A 1 102 ? 24.329 0.146   -15.371 0.50 23.61 ?  102 LYS   A O    1 
ATOM   2139 O O    B LYS   A 1 102 ? 24.428 0.574   -15.371 0.50 25.19 ?  102 LYS   A O    1 
ATOM   2140 C CB   A LYS   A 1 102 ? 24.081 1.423   -12.818 0.50 24.45 ?  102 LYS   A CB   1 
ATOM   2141 C CB   B LYS   A 1 102 ? 24.221 1.521   -12.582 0.50 25.16 ?  102 LYS   A CB   1 
ATOM   2142 C CG   A LYS   A 1 102 ? 23.978 2.558   -11.813 0.50 25.52 ?  102 LYS   A CG   1 
ATOM   2143 C CG   B LYS   A 1 102 ? 24.225 2.704   -11.629 0.50 25.68 ?  102 LYS   A CG   1 
ATOM   2144 C CD   A LYS   A 1 102 ? 25.125 2.506   -10.809 0.50 26.60 ?  102 LYS   A CD   1 
ATOM   2145 C CD   B LYS   A 1 102 ? 25.357 2.564   -10.617 0.50 26.03 ?  102 LYS   A CD   1 
ATOM   2146 C CE   A LYS   A 1 102 ? 25.060 3.663   -9.824  0.50 27.58 ?  102 LYS   A CE   1 
ATOM   2147 C CE   B LYS   A 1 102 ? 25.468 3.778   -9.709  0.50 26.54 ?  102 LYS   A CE   1 
ATOM   2148 N NZ   A LYS   A 1 102 ? 26.145 3.591   -8.803  0.50 28.10 ?  102 LYS   A NZ   1 
ATOM   2149 N NZ   B LYS   A 1 102 ? 26.566 3.622   -8.710  0.50 26.54 ?  102 LYS   A NZ   1 
ATOM   2150 H H    A LYS   A 1 102 ? 21.666 0.574   -12.564 0.50 26.11 ?  102 LYS   A H    1 
ATOM   2151 H H    B LYS   A 1 102 ? 21.769 0.735   -12.452 0.50 27.76 ?  102 LYS   A H    1 
ATOM   2152 H HA   A LYS   A 1 102 ? 22.928 2.188   -14.333 0.50 27.87 ?  102 LYS   A HA   1 
ATOM   2153 H HA   B LYS   A 1 102 ? 23.146 2.388   -14.092 0.50 29.31 ?  102 LYS   A HA   1 
ATOM   2154 H HB2  A LYS   A 1 102 ? 24.101 0.591   -12.317 0.50 29.35 ?  102 LYS   A HB2  1 
ATOM   2155 H HB2  B LYS   A 1 102 ? 24.132 0.718   -12.047 0.50 30.22 ?  102 LYS   A HB2  1 
ATOM   2156 H HB3  A LYS   A 1 102 ? 24.918 1.533   -13.296 0.50 29.35 ?  102 LYS   A HB3  1 
ATOM   2157 H HB3  B LYS   A 1 102 ? 25.079 1.515   -13.033 0.50 30.22 ?  102 LYS   A HB3  1 
ATOM   2158 H HG2  A LYS   A 1 102 ? 24.021 3.407   -12.279 0.50 30.64 ?  102 LYS   A HG2  1 
ATOM   2159 H HG2  B LYS   A 1 102 ? 24.362 3.524   -12.131 0.50 30.84 ?  102 LYS   A HG2  1 
ATOM   2160 H HG3  A LYS   A 1 102 ? 23.144 2.482   -11.324 0.50 30.64 ?  102 LYS   A HG3  1 
ATOM   2161 H HG3  B LYS   A 1 102 ? 23.384 2.737   -11.148 0.50 30.84 ?  102 LYS   A HG3  1 
ATOM   2162 H HD2  A LYS   A 1 102 ? 25.076 1.676   -10.308 0.50 31.93 ?  102 LYS   A HD2  1 
ATOM   2163 H HD2  B LYS   A 1 102 ? 25.193 1.785   -10.062 0.50 31.25 ?  102 LYS   A HD2  1 
ATOM   2164 H HD3  A LYS   A 1 102 ? 25.969 2.559   -11.285 0.50 31.93 ?  102 LYS   A HD3  1 
ATOM   2165 H HD3  B LYS   A 1 102 ? 26.198 2.463   -11.091 0.50 31.25 ?  102 LYS   A HD3  1 
ATOM   2166 H HE2  A LYS   A 1 102 ? 25.155 4.498   -10.308 0.50 33.12 ?  102 LYS   A HE2  1 
ATOM   2167 H HE2  B LYS   A 1 102 ? 25.657 4.563   -10.247 0.50 31.86 ?  102 LYS   A HE2  1 
ATOM   2168 H HE3  A LYS   A 1 102 ? 24.208 3.640   -9.362  0.50 33.12 ?  102 LYS   A HE3  1 
ATOM   2169 H HE3  B LYS   A 1 102 ? 24.634 3.894   -9.228  0.50 31.86 ?  102 LYS   A HE3  1 
ATOM   2170 H HZ1  A LYS   A 1 102 ? 26.081 4.278   -8.242  0.50 33.73 ?  102 LYS   A HZ1  1 
ATOM   2171 H HZ1  B LYS   A 1 102 ? 26.611 4.343   -8.191  0.50 31.86 ?  102 LYS   A HZ1  1 
ATOM   2172 H HZ2  A LYS   A 1 102 ? 26.077 2.833   -8.341  0.50 33.73 ?  102 LYS   A HZ2  1 
ATOM   2173 H HZ2  B LYS   A 1 102 ? 26.413 2.908   -8.200  0.50 31.86 ?  102 LYS   A HZ2  1 
ATOM   2174 H HZ3  A LYS   A 1 102 ? 26.940 3.615   -9.202  0.50 33.73 ?  102 LYS   A HZ3  1 
ATOM   2175 H HZ3  B LYS   A 1 102 ? 27.345 3.517   -9.128  0.50 31.86 ?  102 LYS   A HZ3  1 
ATOM   2176 N N    A GLY   A 1 103 ? 22.275 -0.693  -15.028 0.50 23.58 ?  103 GLY   A N    1 
ATOM   2177 N N    B GLY   A 1 103 ? 22.548 -0.540  -14.829 0.50 25.22 ?  103 GLY   A N    1 
ATOM   2178 C CA   A GLY   A 1 103 ? 22.474 -1.796  -15.949 0.50 23.39 ?  103 GLY   A CA   1 
ATOM   2179 C CA   B GLY   A 1 103 ? 22.780 -1.596  -15.793 0.50 24.88 ?  103 GLY   A CA   1 
ATOM   2180 C C    A GLY   A 1 103 ? 23.275 -2.961  -15.409 0.50 23.03 ?  103 GLY   A C    1 
ATOM   2181 C C    B GLY   A 1 103 ? 23.626 -2.743  -15.293 0.50 24.74 ?  103 GLY   A C    1 
ATOM   2182 O O    A GLY   A 1 103 ? 23.707 -3.814  -16.190 0.50 23.52 ?  103 GLY   A O    1 
ATOM   2183 O O    B GLY   A 1 103 ? 24.255 -3.433  -16.104 0.50 25.22 ?  103 GLY   A O    1 
ATOM   2184 H H    A GLY   A 1 103 ? 21.507 -0.692  -14.644 0.50 28.31 ?  103 GLY   A H    1 
ATOM   2185 H H    B GLY   A 1 103 ? 21.820 -0.636  -14.374 0.50 30.28 ?  103 GLY   A H    1 
ATOM   2186 H HA2  A GLY   A 1 103 ? 21.612 -2.145  -16.209 0.50 28.09 ?  103 GLY   A HA2  1 
ATOM   2187 H HA2  B GLY   A 1 103 ? 21.927 -1.960  -16.079 0.50 29.87 ?  103 GLY   A HA2  1 
ATOM   2188 H HA3  A GLY   A 1 103 ? 22.914 -1.455  -16.748 0.50 28.09 ?  103 GLY   A HA3  1 
ATOM   2189 H HA3  B GLY   A 1 103 ? 23.223 -1.223  -16.570 0.50 29.87 ?  103 GLY   A HA3  1 
ATOM   2190 N N    A GLU   A 1 104 ? 23.461 -3.045  -14.097 0.50 21.42 ?  104 GLU   A N    1 
ATOM   2191 N N    B GLU   A 1 104 ? 23.654 -2.979  -13.985 0.50 23.02 ?  104 GLU   A N    1 
ATOM   2192 C CA   A GLU   A 1 104 ? 24.373 -4.025  -13.522 0.50 20.04 ?  104 GLU   A CA   1 
ATOM   2193 C CA   B GLU   A 1 104 ? 24.489 -4.017  -13.398 0.50 21.48 ?  104 GLU   A CA   1 
ATOM   2194 C C    A GLU   A 1 104 ? 23.717 -5.401  -13.416 0.50 19.53 ?  104 GLU   A C    1 
ATOM   2195 C C    B GLU   A 1 104 ? 23.702 -5.315  -13.250 0.50 22.07 ?  104 GLU   A C    1 
ATOM   2196 O O    A GLU   A 1 104 ? 22.494 -5.530  -13.303 0.50 19.63 ?  104 GLU   A O    1 
ATOM   2197 O O    B GLU   A 1 104 ? 22.508 -5.304  -12.935 0.50 22.60 ?  104 GLU   A O    1 
ATOM   2198 C CB   A GLU   A 1 104 ? 24.886 -3.532  -12.166 0.50 19.32 ?  104 GLU   A CB   1 
ATOM   2199 C CB   B GLU   A 1 104 ? 25.039 -3.536  -12.052 0.50 19.51 ?  104 GLU   A CB   1 
ATOM   2200 C CG   A GLU   A 1 104 ? 25.761 -2.284  -12.309 0.50 19.45 ?  104 GLU   A CG   1 
ATOM   2201 C CG   B GLU   A 1 104 ? 26.011 -2.369  -12.231 0.50 18.44 ?  104 GLU   A CG   1 
ATOM   2202 C CD   A GLU   A 1 104 ? 26.175 -1.647  -10.998 0.50 19.41 ?  104 GLU   A CD   1 
ATOM   2203 C CD   B GLU   A 1 104 ? 26.227 -1.520  -10.994 0.50 17.19 ?  104 GLU   A CD   1 
ATOM   2204 O OE1  A GLU   A 1 104 ? 25.595 -1.977  -9.944  0.50 18.63 ?  104 GLU   A OE1  1 
ATOM   2205 O OE1  B GLU   A 1 104 ? 25.598 -1.780  -9.946  0.50 15.79 ?  104 GLU   A OE1  1 
ATOM   2206 O OE2  A GLU   A 1 104 ? 27.091 -0.796  -11.031 0.50 20.63 -1 104 GLU   A OE2  1 
ATOM   2207 O OE2  B GLU   A 1 104 ? 27.042 -0.571  -11.091 0.50 17.75 -1 104 GLU   A OE2  1 
ATOM   2208 H H    A GLU   A 1 104 ? 23.063 -2.549  -13.521 0.50 25.73 ?  104 GLU   A H    1 
ATOM   2209 H H    B GLU   A 1 104 ? 23.190 -2.542  -13.410 0.50 27.64 ?  104 GLU   A H    1 
ATOM   2210 H HA   A GLU   A 1 104 ? 25.142 -4.110  -14.107 0.50 24.07 ?  104 GLU   A HA   1 
ATOM   2211 H HA   B GLU   A 1 104 ? 25.242 -4.191  -13.981 0.50 25.79 ?  104 GLU   A HA   1 
ATOM   2212 H HB2  A GLU   A 1 104 ? 24.131 -3.309  -11.600 0.50 23.20 ?  104 GLU   A HB2  1 
ATOM   2213 H HB2  B GLU   A 1 104 ? 24.306 -3.238  -11.492 0.50 23.43 ?  104 GLU   A HB2  1 
ATOM   2214 H HB3  A GLU   A 1 104 ? 25.420 -4.230  -11.755 0.50 23.20 ?  104 GLU   A HB3  1 
ATOM   2215 H HB3  B GLU   A 1 104 ? 25.517 -4.262  -11.621 0.50 23.43 ?  104 GLU   A HB3  1 
ATOM   2216 H HG2  A GLU   A 1 104 ? 26.573 -2.524  -12.780 0.50 23.36 ?  104 GLU   A HG2  1 
ATOM   2217 H HG2  B GLU   A 1 104 ? 26.875 -2.719  -12.496 0.50 22.14 ?  104 GLU   A HG2  1 
ATOM   2218 H HG3  A GLU   A 1 104 ? 25.272 -1.615  -12.810 0.50 23.36 ?  104 GLU   A HG3  1 
ATOM   2219 H HG3  B GLU   A 1 104 ? 25.671 -1.780  -12.922 0.50 22.14 ?  104 GLU   A HG3  1 
ATOM   2220 N N    A ASP   A 1 105 ? 24.555 -6.434  -13.453 0.50 20.23 ?  105 ASP   A N    1 
ATOM   2221 N N    B ASP   A 1 105 ? 24.382 -6.435  -13.484 0.50 21.99 ?  105 ASP   A N    1 
ATOM   2222 C CA   A ASP   A 1 105 ? 24.089 -7.811  -13.578 0.50 21.12 ?  105 ASP   A CA   1 
ATOM   2223 C CA   B ASP   A 1 105 ? 23.708 -7.721  -13.601 0.50 22.40 ?  105 ASP   A CA   1 
ATOM   2224 C C    A ASP   A 1 105 ? 23.379 -8.258  -12.304 0.50 19.33 ?  105 ASP   A C    1 
ATOM   2225 C C    B ASP   A 1 105 ? 23.147 -8.175  -12.260 0.50 20.44 ?  105 ASP   A C    1 
ATOM   2226 O O    A ASP   A 1 105 ? 23.996 -8.346  -11.240 0.50 17.61 ?  105 ASP   A O    1 
ATOM   2227 O O    B ASP   A 1 105 ? 23.865 -8.226  -11.259 0.50 18.93 ?  105 ASP   A O    1 
ATOM   2228 C CB   A ASP   A 1 105 ? 25.289 -8.712  -13.860 0.50 23.40 ?  105 ASP   A CB   1 
ATOM   2229 C CB   B ASP   A 1 105 ? 24.674 -8.770  -14.146 0.50 24.67 ?  105 ASP   A CB   1 
ATOM   2230 C CG   A ASP   A 1 105 ? 24.893 -10.134 -14.181 0.50 25.49 ?  105 ASP   A CG   1 
ATOM   2231 C CG   B ASP   A 1 105 ? 24.085 -10.161 -14.111 0.50 27.00 ?  105 ASP   A CG   1 
ATOM   2232 O OD1  A ASP   A 1 105 ? 23.679 -10.406 -14.275 0.50 25.82 ?  105 ASP   A OD1  1 
ATOM   2233 O OD1  B ASP   A 1 105 ? 22.939 -10.321 -14.584 0.50 27.91 ?  105 ASP   A OD1  1 
ATOM   2234 O OD2  A ASP   A 1 105 ? 25.799 -10.982 -14.339 0.50 26.54 -1 105 ASP   A OD2  1 
ATOM   2235 O OD2  B ASP   A 1 105 ? 24.757 -11.088 -13.620 0.50 27.95 -1 105 ASP   A OD2  1 
ATOM   2236 H H    A ASP   A 1 105 ? 25.413 -6.356  -13.413 0.50 24.30 ?  105 ASP   A H    1 
ATOM   2237 H H    B ASP   A 1 105 ? 25.237 -6.476  -13.578 0.50 26.41 ?  105 ASP   A H    1 
ATOM   2238 H HA   A ASP   A 1 105 ? 23.467 -7.874  -14.318 0.50 25.37 ?  105 ASP   A HA   1 
ATOM   2239 H HA   B ASP   A 1 105 ? 22.973 -7.644  -14.218 0.50 26.90 ?  105 ASP   A HA   1 
ATOM   2240 H HB2  A ASP   A 1 105 ? 25.778 -8.356  -14.619 0.50 28.10 ?  105 ASP   A HB2  1 
ATOM   2241 H HB2  B ASP   A 1 105 ? 24.861 -8.578  -15.076 0.50 29.63 ?  105 ASP   A HB2  1 
ATOM   2242 H HB3  A ASP   A 1 105 ? 25.858 -8.733  -13.077 0.50 28.10 ?  105 ASP   A HB3  1 
ATOM   2243 H HB3  B ASP   A 1 105 ? 25.502 -8.742  -13.630 0.50 29.63 ?  105 ASP   A HB3  1 
ATOM   2244 N N    A ILE   A 1 106 ? 22.085 -8.570  -12.418 0.50 19.31 ?  106 ILE   A N    1 
ATOM   2245 N N    B ILE   A 1 106 ? 21.860 -8.534  -12.254 0.50 20.52 ?  106 ILE   A N    1 
ATOM   2246 C CA   A ILE   A 1 106 ? 21.309 -8.976  -11.252 0.50 18.76 ?  106 ILE   A CA   1 
ATOM   2247 C CA   B ILE   A 1 106 ? 21.185 -8.925  -11.023 0.50 20.42 ?  106 ILE   A CA   1 
ATOM   2248 C C    A ILE   A 1 106 ? 21.836 -10.268 -10.648 0.50 17.87 ?  106 ILE   A C    1 
ATOM   2249 C C    B ILE   A 1 106 ? 21.734 -10.226 -10.456 0.50 19.79 ?  106 ILE   A C    1 
ATOM   2250 O O    A ILE   A 1 106 ? 21.615 -10.527 -9.463  0.50 16.92 ?  106 ILE   A O    1 
ATOM   2251 O O    B ILE   A 1 106 ? 21.575 -10.485 -9.259  0.50 19.46 ?  106 ILE   A O    1 
ATOM   2252 C CB   A ILE   A 1 106 ? 19.804 -9.067  -11.595 0.50 19.92 ?  106 ILE   A CB   1 
ATOM   2253 C CB   B ILE   A 1 106 ? 19.657 -8.972  -11.239 0.50 21.78 ?  106 ILE   A CB   1 
ATOM   2254 C CG1  A ILE   A 1 106 ? 18.957 -9.138  -10.321 0.50 20.21 ?  106 ILE   A CG1  1 
ATOM   2255 C CG1  B ILE   A 1 106 ? 18.913 -9.006  -9.899  0.50 22.32 ?  106 ILE   A CG1  1 
ATOM   2256 C CG2  A ILE   A 1 106 ? 19.521 -10.280 -12.461 0.50 20.48 ?  106 ILE   A CG2  1 
ATOM   2257 C CG2  B ILE   A 1 106 ? 19.265 -10.171 -12.091 0.50 22.65 ?  106 ILE   A CG2  1 
ATOM   2258 C CD1  A ILE   A 1 106 ? 19.057 -7.910  -9.444  0.50 20.50 ?  106 ILE   A CD1  1 
ATOM   2259 C CD1  B ILE   A 1 106 ? 19.169 -7.797  -9.021  0.50 22.55 ?  106 ILE   A CD1  1 
ATOM   2260 H H    A ILE   A 1 106 ? 21.645 -8.553  -13.152 0.50 23.19 ?  106 ILE   A H    1 
ATOM   2261 H H    B ILE   A 1 106 ? 21.364 -8.556  -12.949 0.50 24.64 ?  106 ILE   A H    1 
ATOM   2262 H HA   A ILE   A 1 106 ? 21.411 -8.297  -10.576 0.50 22.53 ?  106 ILE   A HA   1 
ATOM   2263 H HA   B ILE   A 1 106 ? 21.363 -8.250  -10.361 0.50 24.52 ?  106 ILE   A HA   1 
ATOM   2264 H HB   A ILE   A 1 106 ? 19.552 -8.270  -12.089 0.50 23.93 ?  106 ILE   A HB   1 
ATOM   2265 H HB   B ILE   A 1 106 ? 19.394 -8.168  -11.711 0.50 26.15 ?  106 ILE   A HB   1 
ATOM   2266 H HG12 A ILE   A 1 106 ? 18.025 -9.242  -10.571 0.50 24.27 ?  106 ILE   A HG12 1 
ATOM   2267 H HG12 B ILE   A 1 106 ? 17.959 -9.046  -10.073 0.50 26.80 ?  106 ILE   A HG12 1 
ATOM   2268 H HG13 A ILE   A 1 106 ? 19.241 -9.901  -9.795  0.50 24.27 ?  106 ILE   A HG13 1 
ATOM   2269 H HG13 B ILE   A 1 106 ? 19.188 -9.794  -9.406  0.50 26.80 ?  106 ILE   A HG13 1 
ATOM   2270 H HG21 A ILE   A 1 106 ? 18.635 -10.189 -12.846 0.50 24.60 ?  106 ILE   A HG21 1 
ATOM   2271 H HG21 B ILE   A 1 106 ? 18.343 -10.068 -12.375 0.50 27.20 ?  106 ILE   A HG21 1 
ATOM   2272 H HG22 A ILE   A 1 106 ? 20.187 -10.325 -13.161 0.50 24.60 ?  106 ILE   A HG22 1 
ATOM   2273 H HG22 B ILE   A 1 106 ? 19.847 -10.209 -12.866 0.50 27.20 ?  106 ILE   A HG22 1 
ATOM   2274 H HG23 A ILE   A 1 106 ? 19.562 -11.076 -11.909 0.50 24.60 ?  106 ILE   A HG23 1 
ATOM   2275 H HG23 B ILE   A 1 106 ? 19.361 -10.980 -11.565 0.50 27.20 ?  106 ILE   A HG23 1 
ATOM   2276 H HD11 A ILE   A 1 106 ? 18.328 -7.917  -8.807  0.50 24.62 ?  106 ILE   A HD11 1 
ATOM   2277 H HD11 B ILE   A 1 106 ? 18.481 -7.752  -8.341  0.50 27.08 ?  106 ILE   A HD11 1 
ATOM   2278 H HD12 A ILE   A 1 106 ? 19.907 -7.926  -8.972  0.50 24.62 ?  106 ILE   A HD12 1 
ATOM   2279 H HD12 B ILE   A 1 106 ? 20.041 -7.888  -8.604  0.50 27.08 ?  106 ILE   A HD12 1 
ATOM   2280 H HD13 A ILE   A 1 106 ? 19.004 -7.118  -10.002 0.50 24.62 ?  106 ILE   A HD13 1 
ATOM   2281 H HD13 B ILE   A 1 106 ? 19.144 -6.998  -9.571  0.50 27.08 ?  106 ILE   A HD13 1 
ATOM   2282 N N    A GLN   A 1 107 ? 22.528 -11.094 -11.441 0.50 18.72 ?  107 GLN   A N    1 
ATOM   2283 N N    B GLN   A 1 107 ? 22.389 -11.053 -11.278 0.50 20.60 ?  107 GLN   A N    1 
ATOM   2284 C CA   A GLN   A 1 107 ? 23.147 -12.302 -10.904 0.50 20.83 ?  107 GLN   A CA   1 
ATOM   2285 C CA   B GLN   A 1 107 ? 22.997 -12.271 -10.754 0.50 21.55 ?  107 GLN   A CA   1 
ATOM   2286 C C    A GLN   A 1 107 ? 24.105 -11.979 -9.766  0.50 19.09 ?  107 GLN   A C    1 
ATOM   2287 C C    B GLN   A 1 107 ? 24.060 -11.960 -9.708  0.50 19.42 ?  107 GLN   A C    1 
ATOM   2288 O O    A GLN   A 1 107 ? 24.339 -12.822 -8.892  0.50 20.71 ?  107 GLN   A O    1 
ATOM   2289 O O    B GLN   A 1 107 ? 24.325 -12.800 -8.839  0.50 20.70 ?  107 GLN   A O    1 
ATOM   2290 C CB   A GLN   A 1 107 ? 23.877 -13.053 -12.023 0.50 24.51 ?  107 GLN   A CB   1 
ATOM   2291 C CB   B GLN   A 1 107 ? 23.573 -13.122 -11.892 0.50 24.84 ?  107 GLN   A CB   1 
ATOM   2292 C CG   A GLN   A 1 107 ? 23.027 -13.305 -13.266 0.50 28.25 ?  107 GLN   A CG   1 
ATOM   2293 C CG   B GLN   A 1 107 ? 22.672 -13.225 -13.125 0.50 28.16 ?  107 GLN   A CG   1 
ATOM   2294 C CD   A GLN   A 1 107 ? 21.770 -14.093 -12.963 0.50 31.15 ?  107 GLN   A CD   1 
ATOM   2295 C CD   B GLN   A 1 107 ? 21.279 -13.739 -12.810 0.50 30.71 ?  107 GLN   A CD   1 
ATOM   2296 O OE1  A GLN   A 1 107 ? 21.822 -15.140 -12.318 0.50 32.19 ?  107 GLN   A OE1  1 
ATOM   2297 O OE1  B GLN   A 1 107 ? 21.112 -14.701 -12.060 0.50 31.67 ?  107 GLN   A OE1  1 
ATOM   2298 N NE2  A GLN   A 1 107 ? 20.629 -13.586 -13.419 0.50 32.24 ?  107 GLN   A NE2  1 
ATOM   2299 N NE2  B GLN   A 1 107 ? 20.266 -13.096 -13.388 0.50 31.30 ?  107 GLN   A NE2  1 
ATOM   2300 H H    A GLN   A 1 107 ? 22.639 -10.984 -12.285 0.50 22.49 ?  107 GLN   A H    1 
ATOM   2301 H H    B GLN   A 1 107 ? 22.497 -10.930 -12.120 0.50 24.74 ?  107 GLN   A H    1 
ATOM   2302 H HA   A GLN   A 1 107 ? 22.461 -12.891 -10.554 0.50 25.02 ?  107 GLN   A HA   1 
ATOM   2303 H HA   B GLN   A 1 107 ? 22.314 -12.802 -10.320 0.50 25.88 ?  107 GLN   A HA   1 
ATOM   2304 H HB2  A GLN   A 1 107 ? 24.650 -12.537 -12.298 0.50 29.43 ?  107 GLN   A HB2  1 
ATOM   2305 H HB2  B GLN   A 1 107 ? 24.421 -12.746 -12.172 0.50 29.82 ?  107 GLN   A HB2  1 
ATOM   2306 H HB3  A GLN   A 1 107 ? 24.164 -13.919 -11.689 0.50 29.43 ?  107 GLN   A HB3  1 
ATOM   2307 H HB3  B GLN   A 1 107 ? 23.713 -14.025 -11.565 0.50 29.82 ?  107 GLN   A HB3  1 
ATOM   2308 H HG2  A GLN   A 1 107 ? 22.763 -12.456 -13.653 0.50 33.92 ?  107 GLN   A HG2  1 
ATOM   2309 H HG2  B GLN   A 1 107 ? 22.578 -12.351 -13.527 0.50 33.81 ?  107 GLN   A HG2  1 
ATOM   2310 H HG3  A GLN   A 1 107 ? 23.550 -13.810 -13.908 0.50 33.92 ?  107 GLN   A HG3  1 
ATOM   2311 H HG3  B GLN   A 1 107 ? 23.079 -13.833 -13.761 0.50 33.81 ?  107 GLN   A HG3  1 
ATOM   2312 H HE21 A GLN   A 1 107 ? 20.632 -12.850 -13.864 0.50 38.71 ?  107 GLN   A HE21 1 
ATOM   2313 H HE21 B GLN   A 1 107 ? 20.420 -12.427 -13.906 0.50 37.58 ?  107 GLN   A HE21 1 
ATOM   2314 H HE22 A GLN   A 1 107 ? 19.888 -13.996 -13.272 0.50 38.71 ?  107 GLN   A HE22 1 
ATOM   2315 H HE22 B GLN   A 1 107 ? 19.457 -13.350 -13.244 0.50 37.58 ?  107 GLN   A HE22 1 
ATOM   2316 N N    . LEU   A 1 108 ? 24.650 -10.760 -9.744  1.00 15.86 ?  108 LEU   A N    1 
ATOM   2317 C CA   . LEU   A 1 108 ? 25.581 -10.362 -8.703  1.00 13.29 ?  108 LEU   A CA   1 
ATOM   2318 C C    . LEU   A 1 108 ? 24.898 -10.202 -7.355  1.00 11.60 ?  108 LEU   A C    1 
ATOM   2319 O O    . LEU   A 1 108 ? 25.591 -10.055 -6.347  1.00 11.69 ?  108 LEU   A O    1 
ATOM   2320 C CB   . LEU   A 1 108 ? 26.302 -9.068  -9.098  1.00 12.66 ?  108 LEU   A CB   1 
ATOM   2321 C CG   . LEU   A 1 108 ? 27.317 -9.265  -10.225 1.00 14.37 ?  108 LEU   A CG   1 
ATOM   2322 C CD1  . LEU   A 1 108 ? 27.783 -7.935  -10.786 1.00 15.27 ?  108 LEU   A CD1  1 
ATOM   2323 C CD2  . LEU   A 1 108 ? 28.515 -10.070 -9.737  1.00 16.39 ?  108 LEU   A CD2  1 
ATOM   2324 H H    A LEU   A 1 108 ? 24.488 -10.148 -10.320 0.50 19.06 ?  108 LEU   A H    1 
ATOM   2325 H H    B LEU   A 1 108 ? 24.525 -10.173 -10.354 0.50 19.06 ?  108 LEU   A H    1 
ATOM   2326 H HA   . LEU   A 1 108 ? 26.251 -11.056 -8.599  1.00 15.96 ?  108 LEU   A HA   1 
ATOM   2327 H HB2  . LEU   A 1 108 ? 25.645 -8.422  -9.400  1.00 15.21 ?  108 LEU   A HB2  1 
ATOM   2328 H HB3  . LEU   A 1 108 ? 26.776 -8.722  -8.327  1.00 15.21 ?  108 LEU   A HB3  1 
ATOM   2329 H HG   . LEU   A 1 108 ? 26.898 -9.766  -10.944 1.00 17.26 ?  108 LEU   A HG   1 
ATOM   2330 H HD11 . LEU   A 1 108 ? 28.390 -8.100  -11.526 1.00 18.34 ?  108 LEU   A HD11 1 
ATOM   2331 H HD12 . LEU   A 1 108 ? 27.013 -7.436  -11.094 1.00 18.34 ?  108 LEU   A HD12 1 
ATOM   2332 H HD13 . LEU   A 1 108 ? 28.242 -7.443  -10.087 1.00 18.34 ?  108 LEU   A HD13 1 
ATOM   2333 H HD21 . LEU   A 1 108 ? 29.215 -10.028 -10.403 1.00 19.68 ?  108 LEU   A HD21 1 
ATOM   2334 H HD22 . LEU   A 1 108 ? 28.826 -9.691  -8.900  1.00 19.68 ?  108 LEU   A HD22 1 
ATOM   2335 H HD23 . LEU   A 1 108 ? 28.242 -10.992 -9.600  1.00 19.68 ?  108 LEU   A HD23 1 
ATOM   2336 N N    . LEU   A 1 109 ? 23.565 -10.245 -7.307  1.00 11.04 ?  109 LEU   A N    1 
ATOM   2337 C CA   . LEU   A 1 109 ? 22.878 -10.128 -6.029  1.00 10.10 ?  109 LEU   A CA   1 
ATOM   2338 C C    . LEU   A 1 109 ? 23.235 -11.282 -5.099  1.00 9.45  ?  109 LEU   A C    1 
ATOM   2339 O O    . LEU   A 1 109 ? 23.372 -11.088 -3.885  1.00 9.76  ?  109 LEU   A O    1 
ATOM   2340 C CB   . LEU   A 1 109 ? 21.370 -10.041 -6.261  1.00 10.76 ?  109 LEU   A CB   1 
ATOM   2341 C CG   . LEU   A 1 109 ? 20.505 -9.745  -5.040  1.00 10.64 ?  109 LEU   A CG   1 
ATOM   2342 C CD1  . LEU   A 1 109 ? 20.956 -8.478  -4.344  1.00 11.34 ?  109 LEU   A CD1  1 
ATOM   2343 C CD2  . LEU   A 1 109 ? 19.042 -9.639  -5.450  1.00 11.86 ?  109 LEU   A CD2  1 
ATOM   2344 H H    . LEU   A 1 109 ? 23.046 -10.349 -7.986  1.00 13.27 ?  109 LEU   A H    1 
ATOM   2345 H HA   . LEU   A 1 109 ? 23.165 -9.308  -5.602  1.00 12.14 ?  109 LEU   A HA   1 
ATOM   2346 H HB2  . LEU   A 1 109 ? 21.208 -9.335  -6.905  1.00 12.93 ?  109 LEU   A HB2  1 
ATOM   2347 H HB3  . LEU   A 1 109 ? 21.072 -10.886 -6.628  1.00 12.93 ?  109 LEU   A HB3  1 
ATOM   2348 H HG   . LEU   A 1 109 ? 20.586 -10.478 -4.411  1.00 12.79 ?  109 LEU   A HG   1 
ATOM   2349 H HD11 . LEU   A 1 109 ? 20.286 -8.212  -3.700  1.00 13.62 ?  109 LEU   A HD11 1 
ATOM   2350 H HD12 . LEU   A 1 109 ? 21.802 -8.644  -3.898  1.00 13.62 ?  109 LEU   A HD12 1 
ATOM   2351 H HD13 . LEU   A 1 109 ? 21.070 -7.776  -5.010  1.00 13.62 ?  109 LEU   A HD13 1 
ATOM   2352 H HD21 . LEU   A 1 109 ? 18.518 -9.351  -4.683  1.00 14.25 ?  109 LEU   A HD21 1 
ATOM   2353 H HD22 . LEU   A 1 109 ? 18.955 -8.995  -6.168  1.00 14.25 ?  109 LEU   A HD22 1 
ATOM   2354 H HD23 . LEU   A 1 109 ? 18.730 -10.511 -5.749  1.00 14.25 ?  109 LEU   A HD23 1 
ATOM   2355 N N    . LYS   A 1 110 ? 23.389 -12.492 -5.644  1.00 8.97  ?  110 LYS   A N    1 
ATOM   2356 C CA   . LYS   A 1 110 ? 23.772 -13.620 -4.797  1.00 8.91  ?  110 LYS   A CA   1 
ATOM   2357 C C    . LYS   A 1 110 ? 25.155 -13.398 -4.190  1.00 8.69  ?  110 LYS   A C    1 
ATOM   2358 O O    . LYS   A 1 110 ? 25.354 -13.599 -2.989  1.00 8.87  ?  110 LYS   A O    1 
ATOM   2359 C CB   . LYS   A 1 110 ? 23.690 -14.939 -5.573  1.00 9.66  ?  110 LYS   A CB   1 
ATOM   2360 C CG   . LYS   A 1 110 ? 23.900 -16.149 -4.670  1.00 9.86  ?  110 LYS   A CG   1 
ATOM   2361 C CD   . LYS   A 1 110 ? 23.648 -17.479 -5.370  1.00 10.41 ?  110 LYS   A CD   1 
ATOM   2362 C CE   . LYS   A 1 110 ? 23.774 -18.661 -4.412  1.00 11.38 ?  110 LYS   A CE   1 
ATOM   2363 N NZ   . LYS   A 1 110 ? 22.600 -18.792 -3.503  1.00 12.11 ?  110 LYS   A NZ   1 
ATOM   2364 H H    . LYS   A 1 110 ? 23.276 -12.684 -6.473  1.00 10.78 ?  110 LYS   A H    1 
ATOM   2365 H HA   . LYS   A 1 110 ? 23.136 -13.684 -4.065  1.00 10.72 ?  110 LYS   A HA   1 
ATOM   2366 H HB2  . LYS   A 1 110 ? 22.817 -15.017 -5.986  1.00 11.61 ?  110 LYS   A HB2  1 
ATOM   2367 H HB3  . LYS   A 1 110 ? 24.383 -14.949 -6.256  1.00 11.61 ?  110 LYS   A HB3  1 
ATOM   2368 H HG2  . LYS   A 1 110 ? 24.817 -16.150 -4.350  1.00 11.85 ?  110 LYS   A HG2  1 
ATOM   2369 H HG3  . LYS   A 1 110 ? 23.291 -16.089 -3.918  1.00 11.85 ?  110 LYS   A HG3  1 
ATOM   2370 H HD2  . LYS   A 1 110 ? 22.754 -17.482 -5.737  1.00 12.51 ?  110 LYS   A HD2  1 
ATOM   2371 H HD3  . LYS   A 1 110 ? 24.304 -17.595 -6.076  1.00 12.51 ?  110 LYS   A HD3  1 
ATOM   2372 H HE2  . LYS   A 1 110 ? 23.850 -19.479 -4.921  1.00 13.68 ?  110 LYS   A HE2  1 
ATOM   2373 H HE3  . LYS   A 1 110 ? 24.565 -18.539 -3.858  1.00 13.68 ?  110 LYS   A HE3  1 
ATOM   2374 H HZ1  . LYS   A 1 110 ? 22.711 -19.487 -2.960  1.00 14.55 ?  110 LYS   A HZ1  1 
ATOM   2375 H HZ2  . LYS   A 1 110 ? 22.512 -18.053 -3.011  1.00 14.55 ?  110 LYS   A HZ2  1 
ATOM   2376 H HZ3  . LYS   A 1 110 ? 21.860 -18.910 -3.980  1.00 14.55 ?  110 LYS   A HZ3  1 
ATOM   2377 N N    . SER   A 1 111 ? 26.112 -12.956 -5.007  1.00 8.94  ?  111 SER   A N    1 
ATOM   2378 C CA   . SER   A 1 111 ? 27.443 -12.647 -4.491  1.00 9.36  ?  111 SER   A CA   1 
ATOM   2379 C C    . SER   A 1 111 ? 27.374 -11.608 -3.381  1.00 8.73  ?  111 SER   A C    1 
ATOM   2380 O O    . SER   A 1 111 ? 28.075 -11.715 -2.371  1.00 9.29  ?  111 SER   A O    1 
ATOM   2381 C CB   . SER   A 1 111 ? 28.333 -12.150 -5.629  1.00 10.53 ?  111 SER   A CB   1 
ATOM   2382 O OG   . SER   A 1 111 ? 28.447 -13.139 -6.639  1.00 12.67 ?  111 SER   A OG   1 
ATOM   2383 H H    . SER   A 1 111 ? 26.010 -12.822 -5.849  1.00 10.75 ?  111 SER   A H    1 
ATOM   2384 H HA   . SER   A 1 111 ? 27.836 -13.455 -4.127  1.00 11.25 ?  111 SER   A HA   1 
ATOM   2385 H HB2  . SER   A 1 111 ? 27.935 -11.357 -6.017  1.00 12.66 ?  111 SER   A HB2  1 
ATOM   2386 H HB3  . SER   A 1 111 ? 29.211 -11.944 -5.274  1.00 12.66 ?  111 SER   A HB3  1 
ATOM   2387 H HG   . SER   A 1 111 ? 28.954 -12.857 -7.255  1.00 15.22 ?  111 SER   A HG   1 
ATOM   2388 N N    . ALA   A 1 112 ? 26.534 -10.588 -3.558  1.00 8.70  ?  112 ALA   A N    1 
ATOM   2389 C CA   . ALA   A 1 112 ? 26.381 -9.553  -2.539  1.00 8.66  ?  112 ALA   A CA   1 
ATOM   2390 C C    . ALA   A 1 112 ? 25.907 -10.156 -1.218  1.00 8.43  ?  112 ALA   A C    1 
ATOM   2391 O O    . ALA   A 1 112 ? 26.465 -9.869  -0.153  1.00 8.69  ?  112 ALA   A O    1 
ATOM   2392 C CB   . ALA   A 1 112 ? 25.420 -8.472  -3.035  1.00 9.18  ?  112 ALA   A CB   1 
ATOM   2393 H H    . ALA   A 1 112 ? 26.046 -10.471 -4.254  1.00 10.46 ?  112 ALA   A H    1 
ATOM   2394 H HA   . ALA   A 1 112 ? 27.240 -9.134  -2.380  1.00 10.41 ?  112 ALA   A HA   1 
ATOM   2395 H HB1  . ALA   A 1 112 ? 25.340 -7.779  -2.354  1.00 11.04 ?  112 ALA   A HB1  1 
ATOM   2396 H HB2  . ALA   A 1 112 ? 25.769 -8.085  -3.853  1.00 11.04 ?  112 ALA   A HB2  1 
ATOM   2397 H HB3  . ALA   A 1 112 ? 24.549 -8.867  -3.200  1.00 11.04 ?  112 ALA   A HB3  1 
ATOM   2398 N N    . TYR   A 1 113 ? 24.871 -10.998 -1.264  1.00 8.63  ?  113 TYR   A N    1 
ATOM   2399 C CA   . TYR   A 1 113 ? 24.369 -11.610 -0.035  1.00 8.30  ?  113 TYR   A CA   1 
ATOM   2400 C C    . TYR   A 1 113 ? 25.379 -12.566 0.602   1.00 8.02  ?  113 TYR   A C    1 
ATOM   2401 O O    . TYR   A 1 113 ? 25.342 -12.763 1.820   1.00 8.56  ?  113 TYR   A O    1 
ATOM   2402 C CB   . TYR   A 1 113 ? 23.050 -12.333 -0.304  1.00 8.76  ?  113 TYR   A CB   1 
ATOM   2403 C CG   . TYR   A 1 113 ? 21.830 -11.440 -0.200  1.00 8.61  ?  113 TYR   A CG   1 
ATOM   2404 C CD1  . TYR   A 1 113 ? 21.477 -10.865 1.010   1.00 8.66  ?  113 TYR   A CD1  1 
ATOM   2405 C CD2  . TYR   A 1 113 ? 21.017 -11.193 -1.305  1.00 8.77  ?  113 TYR   A CD2  1 
ATOM   2406 C CE1  . TYR   A 1 113 ? 20.353 -10.069 1.125   1.00 9.28  ?  113 TYR   A CE1  1 
ATOM   2407 C CE2  . TYR   A 1 113 ? 19.876 -10.392 -1.199  1.00 9.20  ?  113 TYR   A CE2  1 
ATOM   2408 C CZ   . TYR   A 1 113 ? 19.554 -9.838  0.019   1.00 9.13  ?  113 TYR   A CZ   1 
ATOM   2409 O OH   . TYR   A 1 113 ? 18.434 -9.045  0.171   1.00 9.84  ?  113 TYR   A OH   1 
ATOM   2410 H H    . TYR   A 1 113 ? 24.451 -11.223 -1.978  1.00 10.37 ?  113 TYR   A H    1 
ATOM   2411 H HA   . TYR   A 1 113 ? 24.196 -10.906 0.608   1.00 9.98  ?  113 TYR   A HA   1 
ATOM   2412 H HB2  . TYR   A 1 113 ? 23.068 -12.696 -1.200  1.00 10.53 ?  113 TYR   A HB2  1 
ATOM   2413 H HB3  . TYR   A 1 113 ? 22.947 -13.045 0.343   1.00 10.53 ?  113 TYR   A HB3  1 
ATOM   2414 H HD1  . TYR   A 1 113 ? 22.008 -11.019 1.761   1.00 10.42 ?  113 TYR   A HD1  1 
ATOM   2415 H HD2  . TYR   A 1 113 ? 21.231 -11.577 -2.122  1.00 10.54 ?  113 TYR   A HD2  1 
ATOM   2416 H HE1  . TYR   A 1 113 ? 20.133 -9.690  1.948   1.00 11.16 ?  113 TYR   A HE1  1 
ATOM   2417 H HE2  . TYR   A 1 113 ? 19.335 -10.234 -1.939  1.00 11.06 ?  113 TYR   A HE2  1 
ATOM   2418 H HH   . TYR   A 1 113 ? 18.032 -8.983  -0.573  1.00 11.82 ?  113 TYR   A HH   1 
ATOM   2419 N N    . GLU   A 1 114 ? 26.273 -13.179 -0.187  1.00 8.42  ?  114 GLU   A N    1 
ATOM   2420 C CA   . GLU   A 1 114 ? 27.264 -14.080 0.404   1.00 8.44  ?  114 GLU   A CA   1 
ATOM   2421 C C    . GLU   A 1 114 ? 28.122 -13.375 1.452   1.00 8.57  ?  114 GLU   A C    1 
ATOM   2422 O O    . GLU   A 1 114 ? 28.599 -14.012 2.396   1.00 8.74  ?  114 GLU   A O    1 
ATOM   2423 C CB   . GLU   A 1 114 ? 28.131 -14.714 -0.692  1.00 8.73  ?  114 GLU   A CB   1 
ATOM   2424 C CG   . GLU   A 1 114 ? 27.367 -15.769 -1.477  1.00 8.97  ?  114 GLU   A CG   1 
ATOM   2425 C CD   . GLU   A 1 114 ? 28.071 -16.303 -2.721  1.00 9.59  ?  114 GLU   A CD   1 
ATOM   2426 O OE1  . GLU   A 1 114 ? 29.028 -15.675 -3.224  1.00 9.90  ?  114 GLU   A OE1  1 
ATOM   2427 O OE2  . GLU   A 1 114 ? 27.625 -17.375 -3.201  1.00 10.81 -1 114 GLU   A OE2  1 
ATOM   2428 H H    . GLU   A 1 114 ? 26.318 -13.091 -1.048  1.00 10.12 ?  114 GLU   A H    1 
ATOM   2429 H HA   . GLU   A 1 114 ? 26.792 -14.798 0.843   1.00 10.15 ?  114 GLU   A HA   1 
ATOM   2430 H HB2  . GLU   A 1 114 ? 28.418 -14.031 -1.320  1.00 10.49 ?  114 GLU   A HB2  1 
ATOM   2431 H HB3  . GLU   A 1 114 ? 28.898 -15.144 -0.289  1.00 10.49 ?  114 GLU   A HB3  1 
ATOM   2432 H HG2  . GLU   A 1 114 ? 27.198 -16.527 -0.895  1.00 10.78 ?  114 GLU   A HG2  1 
ATOM   2433 H HG3  . GLU   A 1 114 ? 26.519 -15.390 -1.764  1.00 10.78 ?  114 GLU   A HG3  1 
ATOM   2434 N N    . ASN   A 1 115 ? 28.309 -12.058 1.325   1.00 8.48  ?  115 ASN   A N    1 
ATOM   2435 C CA   . ASN   A 1 115 ? 29.075 -11.331 2.332   1.00 8.55  ?  115 ASN   A CA   1 
ATOM   2436 C C    . ASN   A 1 115 ? 28.463 -11.471 3.720   1.00 8.33  ?  115 ASN   A C    1 
ATOM   2437 O O    . ASN   A 1 115 ? 29.182 -11.402 4.723   1.00 8.79  ?  115 ASN   A O    1 
ATOM   2438 C CB   . ASN   A 1 115 ? 29.175 -9.852  1.956   1.00 8.75  ?  115 ASN   A CB   1 
ATOM   2439 C CG   . ASN   A 1 115 ? 29.966 -9.635  0.695   1.00 9.62  ?  115 ASN   A CG   1 
ATOM   2440 O OD1  . ASN   A 1 115 ? 31.183 -9.753  0.701   1.00 13.18 ?  115 ASN   A OD1  1 
ATOM   2441 N ND2  . ASN   A 1 115 ? 29.289 -9.320  -0.389  1.00 9.32  ?  115 ASN   A ND2  1 
ATOM   2442 H H    . ASN   A 1 115 ? 27.999 -11.570 0.684   1.00 10.19 ?  115 ASN   A H    1 
ATOM   2443 H HA   . ASN   A 1 115 ? 29.968 -11.694 2.368   1.00 10.28 ?  115 ASN   A HA   1 
ATOM   2444 H HB2  . ASN   A 1 115 ? 28.278 -9.498  1.828   1.00 10.52 ?  115 ASN   A HB2  1 
ATOM   2445 H HB3  . ASN   A 1 115 ? 29.614 -9.375  2.681   1.00 10.52 ?  115 ASN   A HB3  1 
ATOM   2446 H HD21 . ASN   A 1 115 ? 29.700 -9.185  -1.128  1.00 11.21 ?  115 ASN   A HD21 1 
ATOM   2447 H HD22 . ASN   A 1 115 ? 28.428 -9.259  -0.357  1.00 11.21 ?  115 ASN   A HD22 1 
ATOM   2448 N N    . PHE   A 1 116 ? 27.137 -11.638 3.802   1.00 8.35  ?  116 PHE   A N    1 
ATOM   2449 C CA   . PHE   A 1 116 ? 26.488 -11.743 5.107   1.00 8.45  ?  116 PHE   A CA   1 
ATOM   2450 C C    . PHE   A 1 116 ? 26.973 -12.977 5.871   1.00 8.66  ?  116 PHE   A C    1 
ATOM   2451 O O    . PHE   A 1 116 ? 26.906 -12.998 7.100   1.00 9.13  ?  116 PHE   A O    1 
ATOM   2452 C CB   . PHE   A 1 116 ? 24.959 -11.872 4.968   1.00 8.59  ?  116 PHE   A CB   1 
ATOM   2453 C CG   . PHE   A 1 116 ? 24.200 -10.625 4.522   1.00 8.13  ?  116 PHE   A CG   1 
ATOM   2454 C CD1  . PHE   A 1 116 ? 24.766 -9.597  3.779   1.00 8.57  ?  116 PHE   A CD1  1 
ATOM   2455 C CD2  . PHE   A 1 116 ? 22.849 -10.523 4.853   1.00 8.88  ?  116 PHE   A CD2  1 
ATOM   2456 C CE1  . PHE   A 1 116 ? 23.994 -8.508  3.379   1.00 8.75  ?  116 PHE   A CE1  1 
ATOM   2457 C CE2  . PHE   A 1 116 ? 22.082 -9.444  4.461   1.00 9.02  ?  116 PHE   A CE2  1 
ATOM   2458 C CZ   . PHE   A 1 116 ? 22.647 -8.439  3.721   1.00 8.64  ?  116 PHE   A CZ   1 
ATOM   2459 H H    . PHE   A 1 116 ? 26.596 -11.687 3.124   1.00 10.04 ?  116 PHE   A H    1 
ATOM   2460 H HA   . PHE   A 1 116 ? 26.680 -10.952 5.630   1.00 10.16 ?  116 PHE   A HA   1 
ATOM   2461 H HB2  . PHE   A 1 116 ? 24.771 -12.572 4.320   1.00 10.33 ?  116 PHE   A HB2  1 
ATOM   2462 H HB3  . PHE   A 1 116 ? 24.599 -12.133 5.830   1.00 10.33 ?  116 PHE   A HB3  1 
ATOM   2463 H HD1  . PHE   A 1 116 ? 25.662 -9.653  3.532   1.00 10.30 ?  116 PHE   A HD1  1 
ATOM   2464 H HD2  . PHE   A 1 116 ? 22.452 -11.210 5.340   1.00 10.67 ?  116 PHE   A HD2  1 
ATOM   2465 H HE1  . PHE   A 1 116 ? 24.387 -7.829  2.880   1.00 10.52 ?  116 PHE   A HE1  1 
ATOM   2466 H HE2  . PHE   A 1 116 ? 21.185 -9.407  4.698   1.00 10.85 ?  116 PHE   A HE2  1 
ATOM   2467 H HZ   . PHE   A 1 116 ? 22.142 -7.705  3.464   1.00 10.39 ?  116 PHE   A HZ   1 
ATOM   2468 N N    . ASN   A 1 117 ? 27.408 -14.029 5.162   1.00 8.83  ?  117 ASN   A N    1 
ATOM   2469 C CA   . ASN   A 1 117 ? 27.786 -15.279 5.823   1.00 8.80  ?  117 ASN   A CA   1 
ATOM   2470 C C    . ASN   A 1 117 ? 29.056 -15.155 6.649   1.00 9.16  ?  117 ASN   A C    1 
ATOM   2471 O O    . ASN   A 1 117 ? 29.364 -16.073 7.418   1.00 10.07 ?  117 ASN   A O    1 
ATOM   2472 C CB   . ASN   A 1 117 ? 27.898 -16.397 4.794   1.00 9.18  ?  117 ASN   A CB   1 
ATOM   2473 C CG   . ASN   A 1 117 ? 26.538 -16.787 4.265   1.00 9.05  ?  117 ASN   A CG   1 
ATOM   2474 O OD1  . ASN   A 1 117 ? 25.570 -16.827 5.027   1.00 10.00 ?  117 ASN   A OD1  1 
ATOM   2475 N ND2  . ASN   A 1 117 ? 26.440 -17.034 2.975   1.00 9.16  ?  117 ASN   A ND2  1 
ATOM   2476 H H    . ASN   A 1 117 ? 27.479 -14.045 4.302   1.00 10.61 ?  117 ASN   A H    1 
ATOM   2477 H HA   . ASN   A 1 117 ? 27.072 -15.519 6.431   1.00 10.58 ?  117 ASN   A HA   1 
ATOM   2478 H HB2  . ASN   A 1 117 ? 28.443 -16.096 4.048   1.00 11.03 ?  117 ASN   A HB2  1 
ATOM   2479 H HB3  . ASN   A 1 117 ? 28.296 -17.175 5.209   1.00 11.03 ?  117 ASN   A HB3  1 
ATOM   2480 H HD21 . ASN   A 1 117 ? 25.683 -17.253 2.635   1.00 11.01 ?  117 ASN   A HD21 1 
ATOM   2481 H HD22 . ASN   A 1 117 ? 27.138 -16.982 2.471   1.00 11.01 ?  117 ASN   A HD22 1 
ATOM   2482 N N    . GLN   A 1 118 ? 29.780 -14.044 6.525   1.00 9.35  ?  118 GLN   A N    1 
ATOM   2483 C CA   . GLN   A 1 118 ? 30.961 -13.796 7.342   1.00 9.85  ?  118 GLN   A CA   1 
ATOM   2484 C C    . GLN   A 1 118 ? 30.624 -13.224 8.713   1.00 9.70  ?  118 GLN   A C    1 
ATOM   2485 O O    . GLN   A 1 118 ? 31.544 -12.930 9.485   1.00 11.38 ?  118 GLN   A O    1 
ATOM   2486 C CB   . GLN   A 1 118 ? 31.937 -12.881 6.595   1.00 10.09 ?  118 GLN   A CB   1 
ATOM   2487 C CG   . GLN   A 1 118 ? 32.418 -13.467 5.272   1.00 10.34 ?  118 GLN   A CG   1 
ATOM   2488 C CD   . GLN   A 1 118 ? 33.240 -14.735 5.453   1.00 10.57 ?  118 GLN   A CD   1 
ATOM   2489 O OE1  . GLN   A 1 118 ? 34.109 -14.804 6.331   1.00 11.40 ?  118 GLN   A OE1  1 
ATOM   2490 N NE2  . GLN   A 1 118 ? 32.983 -15.737 4.614   1.00 10.86 ?  118 GLN   A NE2  1 
ATOM   2491 H H    . GLN   A 1 118 ? 29.601 -13.404 5.971   1.00 11.23 ?  118 GLN   A H    1 
ATOM   2492 H HA   . GLN   A 1 118 ? 31.407 -14.644 7.484   1.00 11.84 ?  118 GLN   A HA   1 
ATOM   2493 H HB2  . GLN   A 1 118 ? 31.497 -12.036 6.409   1.00 12.13 ?  118 GLN   A HB2  1 
ATOM   2494 H HB3  . GLN   A 1 118 ? 32.715 -12.730 7.157   1.00 12.13 ?  118 GLN   A HB3  1 
ATOM   2495 H HG2  . GLN   A 1 118 ? 31.649 -13.677 4.718   1.00 12.42 ?  118 GLN   A HG2  1 
ATOM   2496 H HG3  . GLN   A 1 118 ? 32.979 -12.813 4.821   1.00 12.42 ?  118 GLN   A HG3  1 
ATOM   2497 H HE21 . GLN   A 1 118 ? 32.365 -15.651 4.012   1.00 13.05 ?  118 GLN   A HE21 1 
ATOM   2498 H HE22 . GLN   A 1 118 ? 33.410 -16.479 4.676   1.00 13.05 ?  118 GLN   A HE22 1 
ATOM   2499 N N    . HIS   A 1 119 ? 29.337 -13.081 9.037   1.00 9.45  ?  119 HIS   A N    1 
ATOM   2500 C CA   . HIS   A 1 119 ? 28.887 -12.477 10.286  1.00 9.84  ?  119 HIS   A CA   1 
ATOM   2501 C C    . HIS   A 1 119 ? 27.755 -13.308 10.863  1.00 9.99  ?  119 HIS   A C    1 
ATOM   2502 O O    . HIS   A 1 119 ? 26.802 -13.641 10.154  1.00 10.41 ?  119 HIS   A O    1 
ATOM   2503 C CB   . HIS   A 1 119 ? 28.418 -11.048 10.017  1.00 10.34 ?  119 HIS   A CB   1 
ATOM   2504 C CG   . HIS   A 1 119 ? 29.488 -10.226 9.396   1.00 11.65 ?  119 HIS   A CG   1 
ATOM   2505 N ND1  . HIS   A 1 119 ? 30.463 -9.609  10.143  1.00 13.84 ?  119 HIS   A ND1  1 
ATOM   2506 C CD2  . HIS   A 1 119 ? 29.825 -10.044 8.099   1.00 12.58 ?  119 HIS   A CD2  1 
ATOM   2507 C CE1  . HIS   A 1 119 ? 31.324 -9.024  9.328   1.00 14.31 ?  119 HIS   A CE1  1 
ATOM   2508 N NE2  . HIS   A 1 119 ? 30.968 -9.283  8.083   1.00 14.17 ?  119 HIS   A NE2  1 
ATOM   2509 H H    . HIS   A 1 119 ? 28.685 -13.347 8.539   1.00 11.36 ?  119 HIS   A H    1 
ATOM   2510 H HA   . HIS   A 1 119 ? 29.621 -12.462 10.925  1.00 11.82 ?  119 HIS   A HA   1 
ATOM   2511 H HB2  . HIS   A 1 119 ? 27.663 -11.076 9.414   1.00 12.42 ?  119 HIS   A HB2  1 
ATOM   2512 H HB3  . HIS   A 1 119 ? 28.170 -10.638 10.858  1.00 12.42 ?  119 HIS   A HB3  1 
ATOM   2513 H HD2  . HIS   A 1 119 ? 29.367 -10.375 7.356   1.00 15.12 ?  119 HIS   A HD2  1 
ATOM   2514 H HE1  . HIS   A 1 119 ? 32.056 -8.511  9.581   1.00 17.19 ?  119 HIS   A HE1  1 
ATOM   2515 H HE2  . HIS   A 1 119 ? 31.366 -8.998  7.373   1.00 17.03 ?  119 HIS   A HE2  1 
ATOM   2516 N N    . GLU   A 1 120 ? 27.852 -13.630 12.152  1.00 10.57 ?  120 GLU   A N    1 
ATOM   2517 C CA   . GLU   A 1 120 ? 26.899 -14.570 12.735  1.00 12.83 ?  120 GLU   A CA   1 
ATOM   2518 C C    . GLU   A 1 120 ? 25.484 -14.008 12.814  1.00 11.08 ?  120 GLU   A C    1 
ATOM   2519 O O    . GLU   A 1 120 ? 24.512 -14.771 12.698  1.00 11.22 ?  120 GLU   A O    1 
ATOM   2520 C CB   . GLU   A 1 120 ? 27.375 -15.008 14.120  1.00 18.04 ?  120 GLU   A CB   1 
ATOM   2521 C CG   . GLU   A 1 120 ? 28.566 -15.947 14.087  1.00 26.96 ?  120 GLU   A CG   1 
ATOM   2522 C CD   . GLU   A 1 120 ? 28.800 -16.625 15.422  1.00 35.67 ?  120 GLU   A CD   1 
ATOM   2523 O OE1  . GLU   A 1 120 ? 28.348 -16.084 16.454  1.00 37.84 ?  120 GLU   A OE1  1 
ATOM   2524 O OE2  . GLU   A 1 120 ? 29.431 -17.704 15.441  1.00 40.59 -1 120 GLU   A OE2  1 
ATOM   2525 H H    . GLU   A 1 120 ? 28.457 -13.336 12.696  1.00 12.70 ?  120 GLU   A H    1 
ATOM   2526 H HA   . GLU   A 1 120 ? 26.871 -15.361 12.184  1.00 15.42 ?  120 GLU   A HA   1 
ATOM   2527 H HB2  . GLU   A 1 120 ? 27.636 -14.230 14.636  1.00 21.67 ?  120 GLU   A HB2  1 
ATOM   2528 H HB3  . GLU   A 1 120 ? 26.653 -15.474 14.573  1.00 21.67 ?  120 GLU   A HB3  1 
ATOM   2529 H HG2  . GLU   A 1 120 ? 28.416 -16.632 13.415  1.00 32.37 ?  120 GLU   A HG2  1 
ATOM   2530 H HG3  . GLU   A 1 120 ? 29.367 -15.444 13.876  1.00 32.37 ?  120 GLU   A HG3  1 
ATOM   2531 N N    . VAL   A 1 121 ? 25.352 -12.700 13.041  1.00 10.58 ?  121 VAL   A N    1 
ATOM   2532 C CA   . VAL   A 1 121 ? 24.061 -12.031 13.181  1.00 10.66 ?  121 VAL   A CA   1 
ATOM   2533 C C    . VAL   A 1 121 ? 24.170 -10.643 12.557  1.00 9.56  ?  121 VAL   A C    1 
ATOM   2534 O O    . VAL   A 1 121 ? 25.142 -9.922  12.801  1.00 10.37 ?  121 VAL   A O    1 
ATOM   2535 C CB   . VAL   A 1 121 ? 23.642 -11.898 14.664  1.00 13.64 ?  121 VAL   A CB   1 
ATOM   2536 C CG1  . VAL   A 1 121 ? 22.277 -11.221 14.782  1.00 14.28 ?  121 VAL   A CG1  1 
ATOM   2537 C CG2  . VAL   A 1 121 ? 23.634 -13.239 15.367  1.00 15.81 ?  121 VAL   A CG2  1 
ATOM   2538 H H    . VAL   A 1 121 ? 26.019 -12.159 13.118  1.00 12.71 ?  121 VAL   A H    1 
ATOM   2539 H HA   . VAL   A 1 121 ? 23.382 -12.534 12.708  1.00 12.82 ?  121 VAL   A HA   1 
ATOM   2540 H HB   . VAL   A 1 121 ? 24.286 -11.333 15.116  1.00 16.39 ?  121 VAL   A HB   1 
ATOM   2541 H HG11 . VAL   A 1 121 ? 21.964 -11.300 15.697  1.00 17.15 ?  121 VAL   A HG11 1 
ATOM   2542 H HG12 . VAL   A 1 121 ? 22.364 -10.281 14.547  1.00 17.15 ?  121 VAL   A HG12 1 
ATOM   2543 H HG13 . VAL   A 1 121 ? 21.653 -11.655 14.181  1.00 17.15 ?  121 VAL   A HG13 1 
ATOM   2544 H HG21 . VAL   A 1 121 ? 23.294 -13.121 16.271  1.00 18.99 ?  121 VAL   A HG21 1 
ATOM   2545 H HG22 . VAL   A 1 121 ? 23.053 -13.850 14.881  1.00 18.99 ?  121 VAL   A HG22 1 
ATOM   2546 H HG23 . VAL   A 1 121 ? 24.533 -13.591 15.396  1.00 18.99 ?  121 VAL   A HG23 1 
ATOM   2547 N N    . LEU   A 1 122 ? 23.148 -10.246 11.791  1.00 9.14  ?  122 LEU   A N    1 
ATOM   2548 C CA   . LEU   A 1 122 ? 23.142 -8.948  11.119  1.00 9.36  ?  122 LEU   A CA   1 
ATOM   2549 C C    . LEU   A 1 122 ? 21.742 -8.367  11.093  1.00 8.69  ?  122 LEU   A C    1 
ATOM   2550 O O    . LEU   A 1 122 ? 20.760 -9.096  10.952  1.00 10.03 ?  122 LEU   A O    1 
ATOM   2551 C CB   . LEU   A 1 122 ? 23.549 -9.034  9.637   1.00 11.05 ?  122 LEU   A CB   1 
ATOM   2552 C CG   . LEU   A 1 122 ? 24.754 -9.882  9.255   1.00 10.76 ?  122 LEU   A CG   1 
ATOM   2553 C CD1  . LEU   A 1 122 ? 24.350 -11.331 9.014   1.00 11.95 ?  122 LEU   A CD1  1 
ATOM   2554 C CD2  . LEU   A 1 122 ? 25.407 -9.287  8.019   1.00 10.32 ?  122 LEU   A CD2  1 
ATOM   2555 H H    . LEU   A 1 122 ? 22.444 -10.714 11.638  1.00 10.98 ?  122 LEU   A H    1 
ATOM   2556 H HA   . LEU   A 1 122 ? 23.740 -8.330  11.573  1.00 11.25 ?  122 LEU   A HA   1 
ATOM   2557 H HB2  . LEU   A 1 122 ? 22.799 -9.386  9.140   1.00 13.29 ?  122 LEU   A HB2  1 
ATOM   2558 H HB3  . LEU   A 1 122 ? 23.738 -8.133  9.326   1.00 13.29 ?  122 LEU   A HB3  1 
ATOM   2559 H HG   . LEU   A 1 122 ? 25.409 -9.862  9.971   1.00 12.93 ?  122 LEU   A HG   1 
ATOM   2560 H HD11 . LEU   A 1 122 ? 25.129 -11.841 8.744   1.00 14.36 ?  122 LEU   A HD11 1 
ATOM   2561 H HD12 . LEU   A 1 122 ? 23.985 -11.696 9.836   1.00 14.36 ?  122 LEU   A HD12 1 
ATOM   2562 H HD13 . LEU   A 1 122 ? 23.678 -11.360 8.314   1.00 14.36 ?  122 LEU   A HD13 1 
ATOM   2563 H HD21 . LEU   A 1 122 ? 26.143 -9.857  7.737   1.00 12.41 ?  122 LEU   A HD21 1 
ATOM   2564 H HD22 . LEU   A 1 122 ? 24.748 -9.227  7.308   1.00 12.41 ?  122 LEU   A HD22 1 
ATOM   2565 H HD23 . LEU   A 1 122 ? 25.744 -8.400  8.229   1.00 12.41 ?  122 LEU   A HD23 1 
ATOM   2566 N N    . LEU   A 1 123 ? 21.676 -7.037  11.176  1.00 8.60  ?  123 LEU   A N    1 
ATOM   2567 C CA   . LEU   A 1 123 ? 20.500 -6.244  10.822  1.00 8.53  ?  123 LEU   A CA   1 
ATOM   2568 C C    . LEU   A 1 123 ? 20.727 -5.695  9.420   1.00 7.97  ?  123 LEU   A C    1 
ATOM   2569 O O    . LEU   A 1 123 ? 21.775 -5.098  9.163   1.00 8.82  ?  123 LEU   A O    1 
ATOM   2570 C CB   . LEU   A 1 123 ? 20.355 -5.078  11.803  1.00 9.04  ?  123 LEU   A CB   1 
ATOM   2571 C CG   . LEU   A 1 123 ? 19.302 -4.019  11.460  1.00 9.66  ?  123 LEU   A CG   1 
ATOM   2572 C CD1  . LEU   A 1 123 ? 17.903 -4.622  11.447  1.00 10.45 ?  123 LEU   A CD1  1 
ATOM   2573 C CD2  . LEU   A 1 123 ? 19.382 -2.845  12.435  1.00 10.55 ?  123 LEU   A CD2  1 
ATOM   2574 H H    . LEU   A 1 123 ? 22.334 -6.545  11.447  1.00 10.34 ?  123 LEU   A H    1 
ATOM   2575 H HA   . LEU   A 1 123 ? 19.697 -6.794  10.842  1.00 10.25 ?  123 LEU   A HA   1 
ATOM   2576 H HB2  . LEU   A 1 123 ? 20.112 -5.438  12.674  1.00 10.87 ?  123 LEU   A HB2  1 
ATOM   2577 H HB3  . LEU   A 1 123 ? 21.201 -4.622  11.867  1.00 10.87 ?  123 LEU   A HB3  1 
ATOM   2578 H HG   . LEU   A 1 123 ? 19.472 -3.670  10.570  1.00 11.61 ?  123 LEU   A HG   1 
ATOM   2579 H HD11 . LEU   A 1 123 ? 17.252 -3.926  11.269  1.00 12.56 ?  123 LEU   A HD11 1 
ATOM   2580 H HD12 . LEU   A 1 123 ? 17.854 -5.303  10.755  1.00 12.56 ?  123 LEU   A HD12 1 
ATOM   2581 H HD13 . LEU   A 1 123 ? 17.723 -5.025  12.314  1.00 12.56 ?  123 LEU   A HD13 1 
ATOM   2582 H HD21 . LEU   A 1 123 ? 18.707 -2.190  12.197  1.00 12.68 ?  123 LEU   A HD21 1 
ATOM   2583 H HD22 . LEU   A 1 123 ? 19.220 -3.176  13.333  1.00 12.68 ?  123 LEU   A HD22 1 
ATOM   2584 H HD23 . LEU   A 1 123 ? 20.263 -2.453  12.377  1.00 12.68 ?  123 LEU   A HD23 1 
ATOM   2585 N N    . ALA   A 1 124 ? 19.759 -5.882  8.522   1.00 7.87  ?  124 ALA   A N    1 
ATOM   2586 C CA   . ALA   A 1 124 ? 20.012 -5.558  7.127   1.00 7.98  ?  124 ALA   A CA   1 
ATOM   2587 C C    . ALA   A 1 124 ? 18.759 -5.112  6.391   1.00 7.98  ?  124 ALA   A C    1 
ATOM   2588 O O    . ALA   A 1 124 ? 17.643 -5.507  6.759   1.00 8.42  ?  124 ALA   A O    1 
ATOM   2589 C CB   . ALA   A 1 124 ? 20.597 -6.766  6.385   1.00 8.53  ?  124 ALA   A CB   1 
ATOM   2590 H H    . ALA   A 1 124 ? 18.975 -6.191  8.693   1.00 9.46  ?  124 ALA   A H    1 
ATOM   2591 H HA   . ALA   A 1 124 ? 20.669 -4.849  7.105   1.00 9.59  ?  124 ALA   A HA   1 
ATOM   2592 H HB1  . ALA   A 1 124 ? 20.755 -6.525  5.457   1.00 10.25 ?  124 ALA   A HB1  1 
ATOM   2593 H HB2  . ALA   A 1 124 ? 21.445 -7.015  6.802   1.00 10.25 ?  124 ALA   A HB2  1 
ATOM   2594 H HB3  . ALA   A 1 124 ? 19.979 -7.506  6.436   1.00 10.25 ?  124 ALA   A HB3  1 
ATOM   2595 N N    A PRO   A 1 125 ? 18.925 -4.362  5.300   0.50 7.63  ?  125 PRO   A N    1 
ATOM   2596 N N    B PRO   A 1 125 ? 18.905 -4.263  5.370   0.50 8.23  ?  125 PRO   A N    1 
ATOM   2597 C CA   A PRO   A 1 125 ? 17.862 -4.138  4.322   0.50 7.94  ?  125 PRO   A CA   1 
ATOM   2598 C CA   B PRO   A 1 125 ? 17.793 -3.991  4.456   0.50 8.38  ?  125 PRO   A CA   1 
ATOM   2599 C C    A PRO   A 1 125 ? 17.944 -5.201  3.231   0.50 7.75  ?  125 PRO   A C    1 
ATOM   2600 C C    B PRO   A 1 125 ? 17.808 -5.005  3.326   0.50 8.07  ?  125 PRO   A C    1 
ATOM   2601 O O    A PRO   A 1 125 ? 18.934 -5.925  3.103   0.50 8.05  ?  125 PRO   A O    1 
ATOM   2602 O O    B PRO   A 1 125 ? 18.704 -5.856  3.270   0.50 8.76  ?  125 PRO   A O    1 
ATOM   2603 C CB   A PRO   A 1 125 ? 18.275 -2.785  3.733   0.50 7.73  ?  125 PRO   A CB   1 
ATOM   2604 C CB   B PRO   A 1 125 ? 18.127 -2.592  3.936   0.50 8.74  ?  125 PRO   A CB   1 
ATOM   2605 C CG   A PRO   A 1 125 ? 19.797 -2.912  3.638   0.50 7.24  ?  125 PRO   A CG   1 
ATOM   2606 C CG   B PRO   A 1 125 ? 19.625 -2.624  3.844   0.50 9.50  ?  125 PRO   A CG   1 
ATOM   2607 C CD   A PRO   A 1 125 ? 20.196 -3.748  4.858   0.50 7.08  ?  125 PRO   A CD   1 
ATOM   2608 C CD   B PRO   A 1 125 ? 20.107 -3.495  4.995   0.50 9.03  ?  125 PRO   A CD   1 
ATOM   2609 H HA   A PRO   A 1 125 ? 16.984 -4.112  4.729   0.50 9.55  ?  125 PRO   A HA   1 
ATOM   2610 H HA   B PRO   A 1 125 ? 16.938 -4.001  4.916   0.50 10.08 ?  125 PRO   A HA   1 
ATOM   2611 H HB2  A PRO   A 1 125 ? 17.876 -2.672  2.856   0.50 9.30  ?  125 PRO   A HB2  1 
ATOM   2612 H HB2  B PRO   A 1 125 ? 17.723 -2.457  3.063   0.50 10.51 ?  125 PRO   A HB2  1 
ATOM   2613 H HB3  A PRO   A 1 125 ? 18.016 -2.075  4.335   0.50 9.30  ?  125 PRO   A HB3  1 
ATOM   2614 H HB3  B PRO   A 1 125 ? 17.824 -1.923  4.570   0.50 10.51 ?  125 PRO   A HB3  1 
ATOM   2615 H HG2  A PRO   A 1 125 ? 20.040 -3.365  2.814   0.50 8.71  ?  125 PRO   A HG2  1 
ATOM   2616 H HG2  B PRO   A 1 125 ? 19.888 -3.011  2.997   0.50 11.42 ?  125 PRO   A HG2  1 
ATOM   2617 H HG3  A PRO   A 1 125 ? 20.200 -2.030  3.676   0.50 8.71  ?  125 PRO   A HG3  1 
ATOM   2618 H HG3  B PRO   A 1 125 ? 19.972 -1.726  3.933   0.50 11.42 ?  125 PRO   A HG3  1 
ATOM   2619 H HD2  A PRO   A 1 125 ? 20.847 -4.423  4.599   0.50 8.52  ?  125 PRO   A HD2  1 
ATOM   2620 H HD2  B PRO   A 1 125 ? 20.818 -4.088  4.697   0.50 10.85 ?  125 PRO   A HD2  1 
ATOM   2621 H HD3  A PRO   A 1 125 ? 20.550 -3.170  5.554   0.50 8.52  ?  125 PRO   A HD3  1 
ATOM   2622 H HD3  B PRO   A 1 125 ? 20.397 -2.945  5.741   0.50 10.85 ?  125 PRO   A HD3  1 
ATOM   2623 N N    A LEU   A 1 126 ? 16.888 -5.270  2.424   0.50 7.79  ?  126 LEU   A N    1 
ATOM   2624 N N    B LEU   A 1 126 ? 16.843 -4.923  2.414   0.50 8.58  ?  126 LEU   A N    1 
ATOM   2625 C CA   A LEU   A 1 126 ? 16.933 -6.101  1.229   0.50 7.98  ?  126 LEU   A CA   1 
ATOM   2626 C CA   B LEU   A 1 126 ? 16.828 -5.788  1.237   0.50 8.31  ?  126 LEU   A CA   1 
ATOM   2627 C C    A LEU   A 1 126 ? 17.880 -5.481  0.212   0.50 8.38  ?  126 LEU   A C    1 
ATOM   2628 C C    B LEU   A 1 126 ? 17.782 -5.226  0.188   0.50 8.11  ?  126 LEU   A C    1 
ATOM   2629 O O    A LEU   A 1 126 ? 17.733 -4.313  -0.164  0.50 9.03  ?  126 LEU   A O    1 
ATOM   2630 O O    B LEU   A 1 126 ? 17.519 -4.174  -0.406  0.50 8.52  ?  126 LEU   A O    1 
ATOM   2631 C CB   A LEU   A 1 126 ? 15.539 -6.262  0.631   0.50 8.08  ?  126 LEU   A CB   1 
ATOM   2632 C CB   B LEU   A 1 126 ? 15.416 -5.876  0.671   0.50 9.22  ?  126 LEU   A CB   1 
ATOM   2633 C CG   A LEU   A 1 126 ? 14.621 -7.211  1.397   0.50 8.99  ?  126 LEU   A CG   1 
ATOM   2634 C CG   B LEU   A 1 126 ? 14.447 -6.720  1.487   0.50 10.16 ?  126 LEU   A CG   1 
ATOM   2635 C CD1  A LEU   A 1 126 ? 13.200 -7.103  0.872   0.50 9.93  ?  126 LEU   A CD1  1 
ATOM   2636 C CD1  B LEU   A 1 126 ? 13.056 -6.568  0.907   0.50 10.96 ?  126 LEU   A CD1  1 
ATOM   2637 C CD2  A LEU   A 1 126 ? 15.128 -8.644  1.290   0.50 8.75  ?  126 LEU   A CD2  1 
ATOM   2638 C CD2  B LEU   A 1 126 ? 14.863 -8.181  1.481   0.50 10.33 ?  126 LEU   A CD2  1 
ATOM   2639 H H    A LEU   A 1 126 ? 16.151 -4.849  2.538   0.50 9.37  ?  126 LEU   A H    1 
ATOM   2640 H H    B LEU   A 1 126 ? 16.181 -4.374  2.453   0.50 10.32 ?  126 LEU   A H    1 
ATOM   2641 H HA   A LEU   A 1 126 ? 17.275 -6.977  1.458   0.50 9.60  ?  126 LEU   A HA   1 
ATOM   2642 H HA   B LEU   A 1 126 ? 17.118 -6.682  1.484   0.50 9.99  ?  126 LEU   A HA   1 
ATOM   2643 H HB2  A LEU   A 1 126 ? 15.109 -5.396  0.608   0.50 9.72  ?  126 LEU   A HB2  1 
ATOM   2644 H HB2  B LEU   A 1 126 ? 15.045 -4.980  0.618   0.50 11.08 ?  126 LEU   A HB2  1 
ATOM   2645 H HB3  A LEU   A 1 126 ? 15.626 -6.609  -0.272  0.50 9.72  ?  126 LEU   A HB3  1 
ATOM   2646 H HB3  B LEU   A 1 126 ? 15.456 -6.264  -0.216  0.50 11.08 ?  126 LEU   A HB3  1 
ATOM   2647 H HG   A LEU   A 1 126 ? 14.616 -6.963  2.336   0.50 10.81 ?  126 LEU   A HG   1 
ATOM   2648 H HG   B LEU   A 1 126 ? 14.429 -6.403  2.406   0.50 12.21 ?  126 LEU   A HG   1 
ATOM   2649 H HD11 A LEU   A 1 126 ? 12.631 -7.710  1.368   0.50 11.93 ?  126 LEU   A HD11 1 
ATOM   2650 H HD11 B LEU   A 1 126 ? 12.437 -7.107  1.421   0.50 13.17 ?  126 LEU   A HD11 1 
ATOM   2651 H HD12 A LEU   A 1 126 ? 12.892 -6.190  0.987   0.50 11.93 ?  126 LEU   A HD12 1 
ATOM   2652 H HD12 B LEU   A 1 126 ? 12.797 -5.634  0.945   0.50 13.17 ?  126 LEU   A HD12 1 
ATOM   2653 H HD13 A LEU   A 1 126 ? 13.195 -7.337  -0.070  0.50 11.93 ?  126 LEU   A HD13 1 
ATOM   2654 H HD13 B LEU   A 1 126 ? 13.069 -6.869  -0.017  0.50 13.17 ?  126 LEU   A HD13 1 
ATOM   2655 H HD21 A LEU   A 1 126 ? 14.449 -9.244  1.626   0.50 10.51 ?  126 LEU   A HD21 1 
ATOM   2656 H HD21 B LEU   A 1 126 ? 14.141 -8.718  1.838   0.50 12.42 ?  126 LEU   A HD21 1 
ATOM   2657 H HD22 A LEU   A 1 126 ? 15.317 -8.839  0.359   0.50 10.51 ?  126 LEU   A HD22 1 
ATOM   2658 H HD22 B LEU   A 1 126 ? 15.055 -8.446  0.567   0.50 12.42 ?  126 LEU   A HD22 1 
ATOM   2659 H HD23 A LEU   A 1 126 ? 15.940 -8.731  1.816   0.50 10.51 ?  126 LEU   A HD23 1 
ATOM   2660 H HD23 B LEU   A 1 126 ? 15.657 -8.284  2.028   0.50 12.42 ?  126 LEU   A HD23 1 
ATOM   2661 N N    A LEU   A 1 127 ? 18.856 -6.267  -0.228  0.50 8.45  ?  127 LEU   A N    1 
ATOM   2662 N N    B LEU   A 1 127 ? 18.881 -5.933  -0.063  0.50 7.89  ?  127 LEU   A N    1 
ATOM   2663 C CA   A LEU   A 1 127 ? 19.867 -5.770  -1.147  0.50 7.99  ?  127 LEU   A CA   1 
ATOM   2664 C CA   B LEU   A 1 127 ? 19.874 -5.436  -1.004  0.50 8.32  ?  127 LEU   A CA   1 
ATOM   2665 C C    A LEU   A 1 127 ? 19.260 -5.511  -2.518  0.50 7.65  ?  127 LEU   A C    1 
ATOM   2666 C C    B LEU   A 1 127 ? 19.285 -5.330  -2.404  0.50 8.24  ?  127 LEU   A C    1 
ATOM   2667 O O    A LEU   A 1 127 ? 18.451 -6.293  -3.024  0.50 7.71  ?  127 LEU   A O    1 
ATOM   2668 O O    B LEU   A 1 127 ? 18.412 -6.107  -2.801  0.50 8.60  ?  127 LEU   A O    1 
ATOM   2669 C CB   A LEU   A 1 127 ? 21.016 -6.771  -1.255  0.50 7.85  ?  127 LEU   A CB   1 
ATOM   2670 C CB   B LEU   A 1 127 ? 21.090 -6.358  -1.036  0.50 9.39  ?  127 LEU   A CB   1 
ATOM   2671 C CG   A LEU   A 1 127 ? 21.839 -6.990  0.016   0.50 7.74  ?  127 LEU   A CG   1 
ATOM   2672 C CG   B LEU   A 1 127 ? 21.889 -6.455  0.263   0.50 11.04 ?  127 LEU   A CG   1 
ATOM   2673 C CD1  A LEU   A 1 127 ? 22.966 -7.956  -0.276  0.50 7.75  ?  127 LEU   A CD1  1 
ATOM   2674 C CD1  B LEU   A 1 127 ? 23.041 -7.425  0.096   0.50 11.86 ?  127 LEU   A CD1  1 
ATOM   2675 C CD2  A LEU   A 1 127 ? 22.390 -5.677  0.556   0.50 7.78  ?  127 LEU   A CD2  1 
ATOM   2676 C CD2  B LEU   A 1 127 ? 22.395 -5.086  0.696   0.50 11.76 ?  127 LEU   A CD2  1 
ATOM   2677 H H    A LEU   A 1 127 ? 18.954 -7.097  -0.007  0.50 10.16 ?  127 LEU   A H    1 
ATOM   2678 H H    B LEU   A 1 127 ? 19.074 -6.693  0.298   0.50 9.48  ?  127 LEU   A H    1 
ATOM   2679 H HA   A LEU   A 1 127 ? 20.224 -4.938  -0.811  0.50 9.61  ?  127 LEU   A HA   1 
ATOM   2680 H HA   B LEU   A 1 127 ? 20.158 -4.554  -0.723  0.50 10.00 ?  127 LEU   A HA   1 
ATOM   2681 H HB2  A LEU   A 1 127 ? 20.653 -7.638  -1.507  0.50 9.44  ?  127 LEU   A HB2  1 
ATOM   2682 H HB2  B LEU   A 1 127 ? 20.786 -7.252  -1.260  0.50 11.29 ?  127 LEU   A HB2  1 
ATOM   2683 H HB3  A LEU   A 1 127 ? 21.631 -6.470  -1.940  0.50 9.44  ?  127 LEU   A HB3  1 
ATOM   2684 H HB3  B LEU   A 1 127 ? 21.690 -6.038  -1.726  0.50 11.29 ?  127 LEU   A HB3  1 
ATOM   2685 H HG   A LEU   A 1 127 ? 21.274 -7.388  0.702   0.50 9.31  ?  127 LEU   A HG   1 
ATOM   2686 H HG   B LEU   A 1 127 ? 21.307 -6.794  0.963   0.50 13.27 ?  127 LEU   A HG   1 
ATOM   2687 H HD11 A LEU   A 1 127 ? 23.432 -8.163  0.552   0.50 9.32  ?  127 LEU   A HD11 1 
ATOM   2688 H HD11 B LEU   A 1 127 ? 23.609 -7.371  0.879   0.50 14.25 ?  127 LEU   A HD11 1 
ATOM   2689 H HD12 A LEU   A 1 127 ? 22.596 -8.770  -0.656  0.50 9.32  ?  127 LEU   A HD12 1 
ATOM   2690 H HD12 B LEU   A 1 127 ? 22.684 -8.322  0.005   0.50 14.25 ?  127 LEU   A HD12 1 
ATOM   2691 H HD13 A LEU   A 1 127 ? 23.577 -7.546  -0.906  0.50 9.32  ?  127 LEU   A HD13 1 
ATOM   2692 H HD13 B LEU   A 1 127 ? 23.542 -7.182  -0.696  0.50 14.25 ?  127 LEU   A HD13 1 
ATOM   2693 H HD21 A LEU   A 1 127 ? 23.046 -5.866  1.246   0.50 9.35  ?  127 LEU   A HD21 1 
ATOM   2694 H HD21 B LEU   A 1 127 ? 23.017 -5.200  1.431   0.50 14.13 ?  127 LEU   A HD21 1 
ATOM   2695 H HD22 A LEU   A 1 127 ? 22.811 -5.191  -0.173  0.50 9.35  ?  127 LEU   A HD22 1 
ATOM   2696 H HD22 B LEU   A 1 127 ? 22.843 -4.664  -0.054  0.50 14.13 ?  127 LEU   A HD22 1 
ATOM   2697 H HD23 A LEU   A 1 127 ? 21.663 -5.154  0.924   0.50 9.35  ?  127 LEU   A HD23 1 
ATOM   2698 H HD23 B LEU   A 1 127 ? 21.643 -4.543  0.981   0.50 14.13 ?  127 LEU   A HD23 1 
ATOM   2699 N N    A SER   A 1 128 ? 19.662 -4.396  -3.113  0.50 8.14  ?  128 SER   A N    1 
ATOM   2700 N N    B SER   A 1 128 ? 19.785 -4.347  -3.150  0.50 8.56  ?  128 SER   A N    1 
ATOM   2701 C CA   A SER   A 1 128 ? 19.230 -3.942  -4.429  0.50 8.67  ?  128 SER   A CA   1 
ATOM   2702 C CA   B SER   A 1 128 ? 19.424 -4.022  -4.527  0.50 8.24  ?  128 SER   A CA   1 
ATOM   2703 C C    A SER   A 1 128 ? 17.772 -3.493  -4.466  0.50 8.96  ?  128 SER   A C    1 
ATOM   2704 C C    B SER   A 1 128 ? 17.988 -3.523  -4.690  0.50 8.03  ?  128 SER   A C    1 
ATOM   2705 O O    A SER   A 1 128 ? 17.244 -3.238  -5.551  0.50 9.80  ?  128 SER   A O    1 
ATOM   2706 O O    B SER   A 1 128 ? 17.612 -3.140  -5.799  0.50 8.76  ?  128 SER   A O    1 
ATOM   2707 C CB   A SER   A 1 128 ? 19.548 -4.940  -5.550  0.50 8.71  ?  128 SER   A CB   1 
ATOM   2708 C CB   B SER   A 1 128 ? 19.741 -5.142  -5.528  0.50 8.22  ?  128 SER   A CB   1 
ATOM   2709 O OG   A SER   A 1 128 ? 20.950 -5.135  -5.673  0.50 9.55  ?  128 SER   A OG   1 
ATOM   2710 O OG   B SER   A 1 128 ? 21.149 -5.326  -5.630  0.50 8.30  ?  128 SER   A OG   1 
ATOM   2711 H H    A SER   A 1 128 ? 20.225 -3.859  -2.747  0.50 9.79  ?  128 SER   A H    1 
ATOM   2712 H H    B SER   A 1 128 ? 20.402 -3.818  -2.852  0.50 10.29 ?  128 SER   A H    1 
ATOM   2713 H HA   A SER   A 1 128 ? 19.758 -3.161  -4.622  0.50 10.43 ?  128 SER   A HA   1 
ATOM   2714 H HA   B SER   A 1 128 ? 19.985 -3.278  -4.786  0.50 9.90  ?  128 SER   A HA   1 
ATOM   2715 H HB2  A SER   A 1 128 ? 19.126 -5.791  -5.354  0.50 10.47 ?  128 SER   A HB2  1 
ATOM   2716 H HB2  B SER   A 1 128 ? 19.334 -5.967  -5.225  0.50 9.89  ?  128 SER   A HB2  1 
ATOM   2717 H HB3  A SER   A 1 128 ? 19.210 -4.587  -6.389  0.50 10.47 ?  128 SER   A HB3  1 
ATOM   2718 H HB3  B SER   A 1 128 ? 19.382 -4.895  -6.399  0.50 9.89  ?  128 SER   A HB3  1 
ATOM   2719 H HG   A SER   A 1 128 ? 21.331 -4.401  -5.832  0.50 11.48 ?  128 SER   A HG   1 
ATOM   2720 H HG   B SER   A 1 128 ? 21.506 -4.612  -5.902  0.50 9.98  ?  128 SER   A HG   1 
ATOM   2721 N N    A ALA   A 1 129 ? 17.121 -3.361  -3.309  0.50 9.01  ?  129 ALA   A N    1 
ATOM   2722 N N    B ALA   A 1 129 ? 17.187 -3.500  -3.627  0.50 8.82  ?  129 ALA   A N    1 
ATOM   2723 C CA   A ALA   A 1 129 ? 15.756 -2.865  -3.244  0.50 8.41  ?  129 ALA   A CA   1 
ATOM   2724 C CA   B ALA   A 1 129 ? 15.833 -2.966  -3.688  0.50 9.06  ?  129 ALA   A CA   1 
ATOM   2725 C C    A ALA   A 1 129 ? 15.749 -1.336  -3.274  0.50 7.92  ?  129 ALA   A C    1 
ATOM   2726 C C    B ALA   A 1 129 ? 15.873 -1.437  -3.623  0.50 8.87  ?  129 ALA   A C    1 
ATOM   2727 O O    A ALA   A 1 129 ? 16.794 -0.679  -3.366  0.50 8.30  ?  129 ALA   A O    1 
ATOM   2728 O O    B ALA   A 1 129 ? 16.936 -0.809  -3.667  0.50 8.88  ?  129 ALA   A O    1 
ATOM   2729 C CB   A ALA   A 1 129 ? 15.057 -3.395  -1.991  0.50 8.92  ?  129 ALA   A CB   1 
ATOM   2730 C CB   B ALA   A 1 129 ? 14.972 -3.595  -2.591  0.50 9.90  ?  129 ALA   A CB   1 
ATOM   2731 H H    A ALA   A 1 129 ? 17.456 -3.555  -2.538  0.50 10.83 ?  129 ALA   A H    1 
ATOM   2732 H H    B ALA   A 1 129 ? 17.407 -3.802  -2.845  0.50 10.61 ?  129 ALA   A H    1 
ATOM   2733 H HA   A ALA   A 1 129 ? 15.268 -3.188  -4.015  0.50 10.11 ?  129 ALA   A HA   1 
ATOM   2734 H HA   B ALA   A 1 129 ? 15.447 -3.208  -4.539  0.50 10.89 ?  129 ALA   A HA   1 
ATOM   2735 H HB1  A ALA   A 1 129 ? 14.145 -3.061  -1.974  0.50 10.72 ?  129 ALA   A HB1  1 
ATOM   2736 H HB1  B ALA   A 1 129 ? 14.075 -3.235  -2.652  0.50 11.91 ?  129 ALA   A HB1  1 
ATOM   2737 H HB2  A ALA   A 1 129 ? 15.054 -4.363  -2.018  0.50 10.72 ?  129 ALA   A HB2  1 
ATOM   2738 H HB2  B ALA   A 1 129 ? 14.953 -4.557  -2.711  0.50 11.91 ?  129 ALA   A HB2  1 
ATOM   2739 H HB3  A ALA   A 1 129 ? 15.536 -3.085  -1.207  0.50 10.72 ?  129 ALA   A HB3  1 
ATOM   2740 H HB3  B ALA   A 1 129 ? 15.356 -3.380  -1.723  0.50 11.91 ?  129 ALA   A HB3  1 
ATOM   2741 N N    A GLY   A 1 130 ? 14.551 -0.762  -3.193  0.50 8.92  ?  130 GLY   A N    1 
ATOM   2742 N N    B GLY   A 1 130 ? 14.700 -0.819  -3.535  0.50 9.38  ?  130 GLY   A N    1 
ATOM   2743 C CA   A GLY   A 1 130 ? 14.441 0.687   -3.196  0.50 9.35  ?  130 GLY   A CA   1 
ATOM   2744 C CA   B GLY   A 1 130 ? 14.659 0.631   -3.471  0.50 9.35  ?  130 GLY   A CA   1 
ATOM   2745 C C    A GLY   A 1 130 ? 15.050 1.272   -4.453  0.50 9.18  ?  130 GLY   A C    1 
ATOM   2746 C C    B GLY   A 1 130 ? 15.299 1.252   -4.695  0.50 9.21  ?  130 GLY   A C    1 
ATOM   2747 O O    A GLY   A 1 130 ? 14.806 0.798   -5.566  0.50 9.43  ?  130 GLY   A O    1 
ATOM   2748 O O    B GLY   A 1 130 ? 15.079 0.819   -5.831  0.50 9.49  ?  130 GLY   A O    1 
ATOM   2749 H H    A GLY   A 1 130 ? 13.799 -1.182  -3.139  0.50 10.72 ?  130 GLY   A H    1 
ATOM   2750 H H    B GLY   A 1 130 ? 13.937 -1.217  -3.509  0.50 11.27 ?  130 GLY   A H    1 
ATOM   2751 H HA2  A GLY   A 1 130 ? 13.503 0.945   -3.141  0.50 11.24 ?  130 GLY   A HA2  1 
ATOM   2752 H HA2  B GLY   A 1 130 ? 13.736 0.920   -3.417  0.50 11.24 ?  130 GLY   A HA2  1 
ATOM   2753 H HA3  A GLY   A 1 130 ? 14.907 1.051   -2.431  0.50 11.24 ?  130 GLY   A HA3  1 
ATOM   2754 H HA3  B GLY   A 1 130 ? 15.128 0.934   -2.675  0.50 11.24 ?  130 GLY   A HA3  1 
ATOM   2755 N N    A ILE   A 1 131 ? 15.860 2.320   -4.278  0.50 9.22  ?  131 ILE   A N    1 
ATOM   2756 N N    B ILE   A 1 131 ? 16.124 2.278   -4.462  0.50 9.40  ?  131 ILE   A N    1 
ATOM   2757 C CA   A ILE   A 1 131 ? 16.400 3.062   -5.415  0.50 8.87  ?  131 ILE   A CA   1 
ATOM   2758 C CA   B ILE   A 1 131 ? 16.724 3.029   -5.562  0.50 9.11  ?  131 ILE   A CA   1 
ATOM   2759 C C    A ILE   A 1 131 ? 17.435 2.283   -6.214  0.50 8.82  ?  131 ILE   A C    1 
ATOM   2760 C C    B ILE   A 1 131 ? 17.714 2.218   -6.384  0.50 9.44  ?  131 ILE   A C    1 
ATOM   2761 O O    A ILE   A 1 131 ? 17.866 2.764   -7.268  0.50 9.37  ?  131 ILE   A O    1 
ATOM   2762 O O    B ILE   A 1 131 ? 18.146 2.692   -7.442  0.50 10.42 ?  131 ILE   A O    1 
ATOM   2763 C CB   A ILE   A 1 131 ? 16.926 4.458   -5.011  0.50 9.35  ?  131 ILE   A CB   1 
ATOM   2764 C CB   B ILE   A 1 131 ? 17.355 4.361   -5.096  0.50 9.73  ?  131 ILE   A CB   1 
ATOM   2765 C CG1  A ILE   A 1 131 ? 18.172 4.360   -4.122  0.50 10.00 ?  131 ILE   A CG1  1 
ATOM   2766 C CG1  B ILE   A 1 131 ? 18.613 4.121   -4.249  0.50 10.37 ?  131 ILE   A CG1  1 
ATOM   2767 C CG2  A ILE   A 1 131 ? 15.819 5.259   -4.333  0.50 9.87  ?  131 ILE   A CG2  1 
ATOM   2768 C CG2  B ILE   A 1 131 ? 16.333 5.199   -4.338  0.50 9.83  ?  131 ILE   A CG2  1 
ATOM   2769 C CD1  A ILE   A 1 131 ? 18.803 5.710   -3.799  0.50 11.16 ?  131 ILE   A CD1  1 
ATOM   2770 C CD1  B ILE   A 1 131 ? 19.277 5.407   -3.753  0.50 11.62 ?  131 ILE   A CD1  1 
ATOM   2771 H H    A ILE   A 1 131 ? 16.098 2.621   -3.513  0.50 11.08 ?  131 ILE   A H    1 
ATOM   2772 H H    B ILE   A 1 131 ? 16.340 2.556   -3.678  0.50 11.30 ?  131 ILE   A H    1 
ATOM   2773 H HA   A ILE   A 1 131 ? 15.665 3.226   -6.021  0.50 10.66 ?  131 ILE   A HA   1 
ATOM   2774 H HA   B ILE   A 1 131 ? 16.009 3.260   -6.167  0.50 10.95 ?  131 ILE   A HA   1 
ATOM   2775 H HB   A ILE   A 1 131 ? 17.176 4.928   -5.819  0.50 11.24 ?  131 ILE   A HB   1 
ATOM   2776 H HB   B ILE   A 1 131 ? 17.615 4.853   -5.889  0.50 11.70 ?  131 ILE   A HB   1 
ATOM   2777 H HG12 A ILE   A 1 131 ? 17.928 3.937   -3.282  0.50 12.02 ?  131 ILE   A HG12 1 
ATOM   2778 H HG12 B ILE   A 1 131 ? 18.371 3.592   -3.475  0.50 12.47 ?  131 ILE   A HG12 1 
ATOM   2779 H HG13 A ILE   A 1 131 ? 18.842 3.823   -4.574  0.50 12.02 ?  131 ILE   A HG13 1 
ATOM   2780 H HG13 B ILE   A 1 131 ? 19.266 3.645   -4.784  0.50 12.47 ?  131 ILE   A HG13 1 
ATOM   2781 H HG21 A ILE   A 1 131 ? 16.118 6.172   -4.207  0.50 11.86 ?  131 ILE   A HG21 1 
ATOM   2782 H HG21 B ILE   A 1 131 ? 16.680 6.097   -4.227  0.50 11.81 ?  131 ILE   A HG21 1 
ATOM   2783 H HG22 A ILE   A 1 131 ? 15.031 5.245   -4.901  0.50 11.86 ?  131 ILE   A HG22 1 
ATOM   2784 H HG22 B ILE   A 1 131 ? 15.507 5.224   -4.846  0.50 11.81 ?  131 ILE   A HG22 1 
ATOM   2785 H HG23 A ILE   A 1 131 ? 15.614 4.853   -3.476  0.50 11.86 ?  131 ILE   A HG23 1 
ATOM   2786 H HG23 B ILE   A 1 131 ? 16.174 4.794   -3.471  0.50 11.81 ?  131 ILE   A HG23 1 
ATOM   2787 H HD11 A ILE   A 1 131 ? 19.642 5.563   -3.330  0.50 13.41 ?  131 ILE   A HD11 1 
ATOM   2788 H HD11 B ILE   A 1 131 ? 20.129 5.187   -3.346  0.50 13.96 ?  131 ILE   A HD11 1 
ATOM   2789 H HD12 A ILE   A 1 131 ? 18.969 6.187   -4.626  0.50 13.41 ?  131 ILE   A HD12 1 
ATOM   2790 H HD12 B ILE   A 1 131 ? 19.415 6.006   -4.504  0.50 13.96 ?  131 ILE   A HD12 1 
ATOM   2791 H HD13 A ILE   A 1 131 ? 18.198 6.218   -3.238  0.50 13.41 ?  131 ILE   A HD13 1 
ATOM   2792 H HD13 B ILE   A 1 131 ? 18.700 5.832   -3.096  0.50 13.96 ?  131 ILE   A HD13 1 
ATOM   2793 N N    A PHE   A 1 132 ? 17.841 1.092   -5.760  0.50 8.82  ?  132 PHE   A N    1 
ATOM   2794 N N    B PHE   A 1 132 ? 18.088 1.012   -5.934  0.50 8.81  ?  132 PHE   A N    1 
ATOM   2795 C CA   A PHE   A 1 132 ? 18.687 0.231   -6.579  0.50 9.06  ?  132 PHE   A CA   1 
ATOM   2796 C CA   B PHE   A 1 132 ? 18.958 0.156   -6.737  0.50 9.02  ?  132 PHE   A CA   1 
ATOM   2797 C C    A PHE   A 1 132 ? 17.906 -0.508  -7.663  0.50 9.14  ?  132 PHE   A C    1 
ATOM   2798 C C    B PHE   A 1 132 ? 18.203 -0.642  -7.801  0.50 9.89  ?  132 PHE   A C    1 
ATOM   2799 O O    A PHE   A 1 132 ? 18.524 -1.108  -8.547  0.50 9.42  ?  132 PHE   A O    1 
ATOM   2800 O O    B PHE   A 1 132 ? 18.842 -1.341  -8.597  0.50 11.15 ?  132 PHE   A O    1 
ATOM   2801 C CB   A PHE   A 1 132 ? 19.461 -0.761  -5.702  0.50 9.60  ?  132 PHE   A CB   1 
ATOM   2802 C CB   B PHE   A 1 132 ? 19.786 -0.782  -5.847  0.50 8.49  ?  132 PHE   A CB   1 
ATOM   2803 C CG   A PHE   A 1 132 ? 20.702 -0.183  -5.056  0.50 9.43  ?  132 PHE   A CG   1 
ATOM   2804 C CG   B PHE   A 1 132 ? 21.000 -0.131  -5.213  0.50 8.41  ?  132 PHE   A CG   1 
ATOM   2805 C CD1  A PHE   A 1 132 ? 20.613 0.845   -4.130  0.50 10.31 ?  132 PHE   A CD1  1 
ATOM   2806 C CD1  B PHE   A 1 132 ? 20.867 0.930   -4.331  0.50 9.05  ?  132 PHE   A CD1  1 
ATOM   2807 C CD2  A PHE   A 1 132 ? 21.953 -0.706  -5.345  0.50 9.86  ?  132 PHE   A CD2  1 
ATOM   2808 C CD2  B PHE   A 1 132 ? 22.273 -0.613  -5.474  0.50 10.00 ?  132 PHE   A CD2  1 
ATOM   2809 C CE1  A PHE   A 1 132 ? 21.752 1.360   -3.527  0.50 10.55 ?  132 PHE   A CE1  1 
ATOM   2810 C CE1  B PHE   A 1 132 ? 21.984 1.515   -3.741  0.50 9.60  ?  132 PHE   A CE1  1 
ATOM   2811 C CE2  A PHE   A 1 132 ? 23.097 -0.197  -4.744  0.50 9.95  ?  132 PHE   A CE2  1 
ATOM   2812 C CE2  B PHE   A 1 132 ? 23.392 -0.036  -4.885  0.50 10.62 ?  132 PHE   A CE2  1 
ATOM   2813 C CZ   A PHE   A 1 132 ? 22.992 0.841   -3.834  0.50 10.36 ?  132 PHE   A CZ   1 
ATOM   2814 C CZ   B PHE   A 1 132 ? 23.244 1.029   -4.017  0.50 10.11 ?  132 PHE   A CZ   1 
ATOM   2815 H H    A PHE   A 1 132 ? 17.639 0.765   -4.991  0.50 10.60 ?  132 PHE   A H    1 
ATOM   2816 H H    B PHE   A 1 132 ? 17.859 0.672   -5.168  0.50 10.59 ?  132 PHE   A H    1 
ATOM   2817 H HA   A PHE   A 1 132 ? 19.339 0.784   -7.028  0.50 10.89 ?  132 PHE   A HA   1 
ATOM   2818 H HA   B PHE   A 1 132 ? 19.588 0.724   -7.193  0.50 10.84 ?  132 PHE   A HA   1 
ATOM   2819 H HB2  A PHE   A 1 132 ? 18.880 -1.068  -4.989  0.50 11.54 ?  132 PHE   A HB2  1 
ATOM   2820 H HB2  B PHE   A 1 132 ? 19.227 -1.117  -5.128  0.50 10.21 ?  132 PHE   A HB2  1 
ATOM   2821 H HB3  A PHE   A 1 132 ? 19.737 -1.516  -6.247  0.50 11.54 ?  132 PHE   A HB3  1 
ATOM   2822 H HB3  B PHE   A 1 132 ? 20.101 -1.529  -6.386  0.50 10.21 ?  132 PHE   A HB3  1 
ATOM   2823 H HD1  A PHE   A 1 132 ? 19.784 1.199   -3.917  0.50 12.40 ?  132 PHE   A HD1  1 
ATOM   2824 H HD1  B PHE   A 1 132 ? 20.020 1.259   -4.138  0.50 10.88 ?  132 PHE   A HD1  1 
ATOM   2825 H HD2  A PHE   A 1 132 ? 22.036 -1.404  -5.959  0.50 11.85 ?  132 PHE   A HD2  1 
ATOM   2826 H HD2  B PHE   A 1 132 ? 22.385 -1.333  -6.056  0.50 12.02 ?  132 PHE   A HD2  1 
ATOM   2827 H HE1  A PHE   A 1 132 ? 21.682 2.054   -2.913  0.50 12.68 ?  132 PHE   A HE1  1 
ATOM   2828 H HE1  B PHE   A 1 132 ? 21.875 2.231   -3.156  0.50 11.53 ?  132 PHE   A HE1  1 
ATOM   2829 H HE2  A PHE   A 1 132 ? 23.936 -0.551  -4.957  0.50 11.96 ?  132 PHE   A HE2  1 
ATOM   2830 H HE2  B PHE   A 1 132 ? 24.243 -0.365  -5.076  0.50 12.76 ?  132 PHE   A HE2  1 
ATOM   2831 H HZ   A PHE   A 1 132 ? 23.758 1.184   -3.431  0.50 12.45 ?  132 PHE   A HZ   1 
ATOM   2832 H HZ   B PHE   A 1 132 ? 23.991 1.421   -3.624  0.50 12.15 ?  132 PHE   A HZ   1 
ATOM   2833 N N    A GLY   A 1 133 ? 16.575 -0.496  -7.613  0.50 9.25  ?  133 GLY   A N    1 
ATOM   2834 N N    B GLY   A 1 133 ? 16.870 -0.574  -7.827  0.50 9.97  ?  133 GLY   A N    1 
ATOM   2835 C CA   A GLY   A 1 133 ? 15.761 -0.835  -8.762  0.50 10.13 ?  133 GLY   A CA   1 
ATOM   2836 C CA   B GLY   A 1 133 ? 16.109 -0.964  -8.994  0.50 10.50 ?  133 GLY   A CA   1 
ATOM   2837 C C    A GLY   A 1 133 ? 15.445 -2.296  -8.990  0.50 10.60 ?  133 GLY   A C    1 
ATOM   2838 C C    B GLY   A 1 133 ? 15.615 -2.397  -9.049  0.50 11.15 ?  133 GLY   A C    1 
ATOM   2839 O O    A GLY   A 1 133 ? 14.809 -2.608  -10.005 0.50 12.12 ?  133 GLY   A O    1 
ATOM   2840 O O    B GLY   A 1 133 ? 14.831 -2.718  -9.951  0.50 13.26 ?  133 GLY   A O    1 
ATOM   2841 H H    A GLY   A 1 133 ? 16.120 -0.292  -6.916  0.50 11.12 ?  133 GLY   A H    1 
ATOM   2842 H H    B GLY   A 1 133 ? 16.385 -0.309  -7.165  0.50 11.99 ?  133 GLY   A H    1 
ATOM   2843 H HA2  A GLY   A 1 133 ? 14.914 -0.378  -8.682  0.50 12.18 ?  133 GLY   A HA2  1 
ATOM   2844 H HA2  B GLY   A 1 133 ? 15.329 -0.399  -9.053  0.50 12.63 ?  133 GLY   A HA2  1 
ATOM   2845 H HA3  A GLY   A 1 133 ? 16.202 -0.517  -9.563  0.50 12.18 ?  133 GLY   A HA3  1 
ATOM   2846 H HA3  B GLY   A 1 133 ? 16.654 -0.800  -9.780  0.50 12.63 ?  133 GLY   A HA3  1 
ATOM   2847 N N    A ALA   A 1 134 ? 15.857 -3.200  -8.103  0.50 10.30 ?  134 ALA   A N    1 
ATOM   2848 N N    B ALA   A 1 134 ? 16.036 -3.273  -8.137  0.50 10.42 ?  134 ALA   A N    1 
ATOM   2849 C CA   A ALA   A 1 134 ? 15.550 -4.609  -8.297  0.50 11.23 ?  134 ALA   A CA   1 
ATOM   2850 C CA   B ALA   A 1 134 ? 15.608 -4.662  -8.211  0.50 10.64 ?  134 ALA   A CA   1 
ATOM   2851 C C    A ALA   A 1 134 ? 14.179 -4.952  -7.712  0.50 11.24 ?  134 ALA   A C    1 
ATOM   2852 C C    B ALA   A 1 134 ? 14.250 -4.853  -7.541  0.50 10.22 ?  134 ALA   A C    1 
ATOM   2853 O O    A ALA   A 1 134 ? 13.556 -4.163  -6.999  0.50 12.28 ?  134 ALA   A O    1 
ATOM   2854 O O    B ALA   A 1 134 ? 13.806 -4.044  -6.720  0.50 10.93 ?  134 ALA   A O    1 
ATOM   2855 C CB   A ALA   A 1 134 ? 16.643 -5.496  -7.693  0.50 12.42 ?  134 ALA   A CB   1 
ATOM   2856 C CB   B ALA   A 1 134 ? 16.630 -5.591  -7.552  0.50 11.61 ?  134 ALA   A CB   1 
ATOM   2857 H H    A ALA   A 1 134 ? 16.318 -3.025  -7.390  0.50 12.38 ?  134 ALA   A H    1 
ATOM   2858 H H    B ALA   A 1 134 ? 16.565 -3.090  -7.479  0.50 12.52 ?  134 ALA   A H    1 
ATOM   2859 H HA   A ALA   A 1 134 ? 15.520 -4.795  -9.247  0.50 13.49 ?  134 ALA   A HA   1 
ATOM   2860 H HA   B ALA   A 1 134 ? 15.534 -4.921  -9.144  0.50 12.79 ?  134 ALA   A HA   1 
ATOM   2861 H HB1  A ALA   A 1 134 ? 16.421 -6.427  -7.849  0.50 14.92 ?  134 ALA   A HB1  1 
ATOM   2862 H HB1  B ALA   A 1 134 ? 16.319 -6.505  -7.626  0.50 13.95 ?  134 ALA   A HB1  1 
ATOM   2863 H HB2  A ALA   A 1 134 ? 17.494 -5.287  -8.118  0.50 14.92 ?  134 ALA   A HB2  1 
ATOM   2864 H HB2  B ALA   A 1 134 ? 17.485 -5.494  -8.003  0.50 13.95 ?  134 ALA   A HB2  1 
ATOM   2865 H HB3  A ALA   A 1 134 ? 16.704 -5.325  -6.740  0.50 14.92 ?  134 ALA   A HB3  1 
ATOM   2866 H HB3  B ALA   A 1 134 ? 16.722 -5.345  -6.618  0.50 13.95 ?  134 ALA   A HB3  1 
ATOM   2867 N N    A ASP   A 1 135 ? 13.705 -6.150  -8.046  0.50 11.50 ?  135 ASP   A N    1 
ATOM   2868 N N    B ASP   A 1 135 ? 13.599 -5.955  -7.899  0.50 10.35 ?  135 ASP   A N    1 
ATOM   2869 C CA   A ASP   A 1 135 ? 12.448 -6.662  -7.507  0.50 11.94 ?  135 ASP   A CA   1 
ATOM   2870 C CA   B ASP   A 1 135 ? 12.326 -6.334  -7.295  0.50 11.06 ?  135 ASP   A CA   1 
ATOM   2871 C C    A ASP   A 1 135 ? 12.672 -7.106  -6.067  0.50 11.23 ?  135 ASP   A C    1 
ATOM   2872 C C    B ASP   A 1 135 ? 12.573 -6.811  -5.869  0.50 10.54 ?  135 ASP   A C    1 
ATOM   2873 O O    A ASP   A 1 135 ? 13.466 -8.024  -5.832  0.50 11.16 ?  135 ASP   A O    1 
ATOM   2874 O O    B ASP   A 1 135 ? 13.320 -7.779  -5.671  0.50 10.29 ?  135 ASP   A O    1 
ATOM   2875 C CB   A ASP   A 1 135 ? 11.994 -7.854  -8.344  0.50 13.49 ?  135 ASP   A CB   1 
ATOM   2876 C CB   B ASP   A 1 135 ? 11.703 -7.453  -8.125  0.50 12.70 ?  135 ASP   A CB   1 
ATOM   2877 C CG   A ASP   A 1 135 ? 10.723 -8.523  -7.814  0.50 15.01 ?  135 ASP   A CG   1 
ATOM   2878 C CG   B ASP   A 1 135 ? 10.316 -7.859  -7.633  0.50 14.73 ?  135 ASP   A CG   1 
ATOM   2879 O OD1  A ASP   A 1 135 ? 10.157 -8.082  -6.795  0.50 14.91 ?  135 ASP   A OD1  1 
ATOM   2880 O OD1  B ASP   A 1 135 ? 9.920  -7.448  -6.518  0.50 15.52 ?  135 ASP   A OD1  1 
ATOM   2881 O OD2  A ASP   A 1 135 ? 10.289 -9.515  -8.436  0.50 16.87 -1 135 ASP   A OD2  1 
ATOM   2882 O OD2  B ASP   A 1 135 ? 9.617  -8.589  -8.372  0.50 16.81 -1 135 ASP   A OD2  1 
ATOM   2883 H H    A ASP   A 1 135 ? 14.094 -6.688  -8.591  0.50 13.82 ?  135 ASP   A H    1 
ATOM   2884 H H    B ASP   A 1 135 ? 13.875 -6.508  -8.496  0.50 12.44 ?  135 ASP   A H    1 
ATOM   2885 H HA   A ASP   A 1 135 ? 11.773 -5.970  -7.543  0.50 14.34 ?  135 ASP   A HA   1 
ATOM   2886 H HA   B ASP   A 1 135 ? 11.724 -5.571  -7.299  0.50 13.30 ?  135 ASP   A HA   1 
ATOM   2887 H HB2  A ASP   A 1 135 ? 11.802 -7.551  -9.239  0.50 16.21 ?  135 ASP   A HB2  1 
ATOM   2888 H HB2  B ASP   A 1 135 ? 11.631 -7.152  -9.044  0.50 15.26 ?  135 ASP   A HB2  1 
ATOM   2889 H HB3  A ASP   A 1 135 ? 12.704 -8.515  -8.357  0.50 16.21 ?  135 ASP   A HB3  1 
ATOM   2890 H HB3  B ASP   A 1 135 ? 12.281 -8.231  -8.075  0.50 15.26 ?  135 ASP   A HB3  1 
ATOM   2891 N N    A PRO   A 1 136 ? 12.010 -6.493  -5.081  0.50 10.95 ?  136 PRO   A N    1 
ATOM   2892 N N    B PRO   A 1 136 ? 11.989 -6.168  -4.854  0.50 10.45 ?  136 PRO   A N    1 
ATOM   2893 C CA   A PRO   A 1 136 ? 12.262 -6.891  -3.686  0.50 11.03 ?  136 PRO   A CA   1 
ATOM   2894 C CA   B PRO   A 1 136 ? 12.241 -6.604  -3.469  0.50 10.93 ?  136 PRO   A CA   1 
ATOM   2895 C C    A PRO   A 1 136 ? 11.831 -8.311  -3.363  0.50 10.59 ?  136 PRO   A C    1 
ATOM   2896 C C    B PRO   A 1 136 ? 11.823 -8.040  -3.183  0.50 10.25 ?  136 PRO   A C    1 
ATOM   2897 O O    A PRO   A 1 136 ? 12.451 -8.946  -2.503  0.50 10.79 ?  136 PRO   A O    1 
ATOM   2898 O O    B PRO   A 1 136 ? 12.418 -8.684  -2.310  0.50 9.55  ?  136 PRO   A O    1 
ATOM   2899 C CB   A PRO   A 1 136 ? 11.480 -5.848  -2.875  0.50 11.69 ?  136 PRO   A CB   1 
ATOM   2900 C CB   B PRO   A 1 136 ? 11.449 -5.585  -2.635  0.50 11.80 ?  136 PRO   A CB   1 
ATOM   2901 C CG   A PRO   A 1 136 ? 10.411 -5.374  -3.807  0.50 12.37 ?  136 PRO   A CG   1 
ATOM   2902 C CG   B PRO   A 1 136 ? 10.437 -5.017  -3.587  0.50 12.51 ?  136 PRO   A CG   1 
ATOM   2903 C CD   A PRO   A 1 136 ? 11.014 -5.412  -5.179  0.50 11.63 ?  136 PRO   A CD   1 
ATOM   2904 C CD   B PRO   A 1 136 ? 11.123 -4.980  -4.905  0.50 11.30 ?  136 PRO   A CD   1 
ATOM   2905 H HA   A PRO   A 1 136 ? 13.207 -6.800  -3.478  0.50 13.26 ?  136 PRO   A HA   1 
ATOM   2906 H HA   B PRO   A 1 136 ? 13.183 -6.502  -3.255  0.50 13.13 ?  136 PRO   A HA   1 
ATOM   2907 H HB2  A PRO   A 1 136 ? 11.092 -6.264  -2.089  0.50 14.05 ?  136 PRO   A HB2  1 
ATOM   2908 H HB2  B PRO   A 1 136 ? 11.007 -6.027  -1.895  0.50 14.18 ?  136 PRO   A HB2  1 
ATOM   2909 H HB3  A PRO   A 1 136 ? 12.070 -5.119  -2.623  0.50 14.05 ?  136 PRO   A HB3  1 
ATOM   2910 H HB3  B PRO   A 1 136 ? 12.040 -4.882  -2.313  0.50 14.18 ?  136 PRO   A HB3  1 
ATOM   2911 H HG2  A PRO   A 1 136 ? 9.648  -5.966  -3.756  0.50 14.87 ?  136 PRO   A HG2  1 
ATOM   2912 H HG2  B PRO   A 1 136 ? 9.663  -5.600  -3.630  0.50 15.04 ?  136 PRO   A HG2  1 
ATOM   2913 H HG3  A PRO   A 1 136 ? 10.158 -4.466  -3.576  0.50 14.87 ?  136 PRO   A HG3  1 
ATOM   2914 H HG3  B PRO   A 1 136 ? 10.182 -4.124  -3.311  0.50 15.04 ?  136 PRO   A HG3  1 
ATOM   2915 H HD2  A PRO   A 1 136 ? 10.341 -5.637  -5.841  0.50 13.97 ?  136 PRO   A HD2  1 
ATOM   2916 H HD2  B PRO   A 1 136 ? 10.475 -5.062  -5.625  0.50 13.58 ?  136 PRO   A HD2  1 
ATOM   2917 H HD3  A PRO   A 1 136 ? 11.449 -4.568  -5.389  0.50 13.97 ?  136 PRO   A HD3  1 
ATOM   2918 H HD3  B PRO   A 1 136 ? 11.655 -4.173  -4.996  0.50 13.58 ?  136 PRO   A HD3  1 
ATOM   2919 N N    A ILE   A 1 137 ? 10.781 -8.826  -4.007  0.50 10.58 ?  137 ILE   A N    1 
ATOM   2920 N N    B ILE   A 1 137 ? 10.807 -8.560  -3.874  0.50 10.79 ?  137 ILE   A N    1 
ATOM   2921 C CA   A ILE   A 1 137 ? 10.420 -10.230 -3.828  0.50 11.08 ?  137 ILE   A CA   1 
ATOM   2922 C CA   B ILE   A 1 137 ? 10.420 -9.955  -3.670  0.50 11.16 ?  137 ILE   A CA   1 
ATOM   2923 C C    A ILE   A 1 137 ? 11.579 -11.121 -4.247  0.50 10.77 ?  137 ILE   A C    1 
ATOM   2924 C C    B ILE   A 1 137 ? 11.556 -10.885 -4.083  0.50 10.77 ?  137 ILE   A C    1 
ATOM   2925 O O    A ILE   A 1 137 ? 11.894 -12.117 -3.584  0.50 11.14 ?  137 ILE   A O    1 
ATOM   2926 O O    B ILE   A 1 137 ? 11.872 -11.857 -3.385  0.50 10.69 ?  137 ILE   A O    1 
ATOM   2927 C CB   A ILE   A 1 137 ? 9.127  -10.553 -4.601  0.50 12.36 ?  137 ILE   A CB   1 
ATOM   2928 C CB   B ILE   A 1 137 ? 9.116  -10.268 -4.427  0.50 12.34 ?  137 ILE   A CB   1 
ATOM   2929 C CG1  A ILE   A 1 137 ? 7.956  -9.746  -4.035  0.50 14.38 ?  137 ILE   A CG1  1 
ATOM   2930 C CG1  B ILE   A 1 137 ? 7.965  -9.398  -3.913  0.50 14.43 ?  137 ILE   A CG1  1 
ATOM   2931 C CG2  A ILE   A 1 137 ? 8.834  -12.052 -4.558  0.50 12.53 ?  137 ILE   A CG2  1 
ATOM   2932 C CG2  B ILE   A 1 137 ? 8.766  -11.743 -4.297  0.50 12.69 ?  137 ILE   A CG2  1 
ATOM   2933 C CD1  A ILE   A 1 137 ? 6.684  -9.864  -4.834  0.50 16.14 ?  137 ILE   A CD1  1 
ATOM   2934 C CD1  B ILE   A 1 137 ? 6.673  -9.633  -4.644  0.50 15.87 ?  137 ILE   A CD1  1 
ATOM   2935 H H    A ILE   A 1 137 ? 10.275 -8.392  -4.542  0.50 12.71 ?  137 ILE   A H    1 
ATOM   2936 H H    B ILE   A 1 137 ? 10.334 -8.124  -4.446  0.50 12.97 ?  137 ILE   A H    1 
ATOM   2937 H HA   A ILE   A 1 137 ? 10.251 -10.399 -2.890  0.50 13.31 ?  137 ILE   A HA   1 
ATOM   2938 H HA   B ILE   A 1 137 ? 10.248 -10.086 -2.723  0.50 13.41 ?  137 ILE   A HA   1 
ATOM   2939 H HB   A ILE   A 1 137 ? 9.252  -10.297 -5.526  0.50 14.85 ?  137 ILE   A HB   1 
ATOM   2940 H HB   B ILE   A 1 137 ? 9.251  -10.061 -5.363  0.50 14.83 ?  137 ILE   A HB   1 
ATOM   2941 H HG12 A ILE   A 1 137 ? 7.774  -10.050 -3.133  0.50 17.27 ?  137 ILE   A HG12 1 
ATOM   2942 H HG12 B ILE   A 1 137 ? 7.814  -9.591  -2.974  0.50 17.34 ?  137 ILE   A HG12 1 
ATOM   2943 H HG13 A ILE   A 1 137 ? 8.208  -8.806  -4.017  0.50 17.27 ?  137 ILE   A HG13 1 
ATOM   2944 H HG13 B ILE   A 1 137 ? 8.198  -8.460  -4.021  0.50 17.34 ?  137 ILE   A HG13 1 
ATOM   2945 H HG21 A ILE   A 1 137 ? 7.921  -12.215 -4.847  0.50 15.06 ?  137 ILE   A HG21 1 
ATOM   2946 H HG21 B ILE   A 1 137 ? 7.948  -11.921 -4.782  0.50 15.24 ?  137 ILE   A HG21 1 
ATOM   2947 H HG22 A ILE   A 1 137 ? 9.447  -12.511 -5.151  0.50 15.06 ?  137 ILE   A HG22 1 
ATOM   2948 H HG22 B ILE   A 1 137 ? 9.483  -12.274 -4.669  0.50 15.24 ?  137 ILE   A HG22 1 
ATOM   2949 H HG23 A ILE   A 1 137 ? 8.948  -12.368 -3.650  0.50 15.06 ?  137 ILE   A HG23 1 
ATOM   2950 H HG23 B ILE   A 1 137 ? 8.647  -11.953 -3.358  0.50 15.24 ?  137 ILE   A HG23 1 
ATOM   2951 H HD11 A ILE   A 1 137 ? 5.968  -10.147 -4.243  0.50 19.39 ?  137 ILE   A HD11 1 
ATOM   2952 H HD11 B ILE   A 1 137 ? 6.045  -8.951  -4.381  0.50 19.07 ?  137 ILE   A HD11 1 
ATOM   2953 H HD12 A ILE   A 1 137 ? 6.480  -8.997  -5.215  0.50 19.39 ?  137 ILE   A HD12 1 
ATOM   2954 H HD12 B ILE   A 1 137 ? 6.834  -9.588  -5.602  0.50 19.07 ?  137 ILE   A HD12 1 
ATOM   2955 H HD13 A ILE   A 1 137 ? 6.808  -10.512 -5.543  0.50 19.39 ?  137 ILE   A HD13 1 
ATOM   2956 H HD13 B ILE   A 1 137 ? 6.323  -10.509 -4.410  0.50 19.07 ?  137 ILE   A HD13 1 
ATOM   2957 N N    A HIS   A 1 138 ? 12.242 -10.766 -5.348  0.50 10.78 ?  138 HIS   A N    1 
ATOM   2958 N N    B HIS   A 1 138 ? 12.187 -10.598 -5.226  0.50 11.34 ?  138 HIS   A N    1 
ATOM   2959 C CA   A HIS   A 1 138 ? 13.437 -11.491 -5.757  0.50 10.72 ?  138 HIS   A CA   1 
ATOM   2960 C CA   B HIS   A 1 138 ? 13.315 -11.403 -5.686  0.50 11.19 ?  138 HIS   A CA   1 
ATOM   2961 C C    A HIS   A 1 138 ? 14.568 -11.318 -4.749  0.50 10.47 ?  138 HIS   A C    1 
ATOM   2962 C C    B HIS   A 1 138 ? 14.487 -11.307 -4.719  0.50 10.77 ?  138 HIS   A C    1 
ATOM   2963 O O    A HIS   A 1 138 ? 15.270 -12.286 -4.428  0.50 10.63 ?  138 HIS   A O    1 
ATOM   2964 O O    B HIS   A 1 138 ? 15.132 -12.314 -4.404  0.50 11.27 ?  138 HIS   A O    1 
ATOM   2965 C CB   A HIS   A 1 138 ? 13.868 -11.044 -7.151  0.50 11.55 ?  138 HIS   A CB   1 
ATOM   2966 C CB   B HIS   A 1 138 ? 13.726 -10.950 -7.088  0.50 11.43 ?  138 HIS   A CB   1 
ATOM   2967 C CG   A HIS   A 1 138 ? 15.117 -11.711 -7.626  0.50 12.46 ?  138 HIS   A CG   1 
ATOM   2968 C CG   B HIS   A 1 138 ? 15.001 -11.564 -7.575  0.50 12.10 ?  138 HIS   A CG   1 
ATOM   2969 N ND1  A HIS   A 1 138 ? 15.186 -13.064 -7.883  0.50 13.94 ?  138 HIS   A ND1  1 
ATOM   2970 N ND1  B HIS   A 1 138 ? 15.134 -12.914 -7.818  0.50 13.46 ?  138 HIS   A ND1  1 
ATOM   2971 C CD2  A HIS   A 1 138 ? 16.354 -11.218 -7.867  0.50 12.65 ?  138 HIS   A CD2  1 
ATOM   2972 C CD2  B HIS   A 1 138 ? 16.203 -11.010 -7.865  0.50 12.28 ?  138 HIS   A CD2  1 
ATOM   2973 C CE1  A HIS   A 1 138 ? 16.409 -13.372 -8.274  0.50 14.05 ?  138 HIS   A CE1  1 
ATOM   2974 C CE1  B HIS   A 1 138 ? 16.362 -13.165 -8.236  0.50 13.35 ?  138 HIS   A CE1  1 
ATOM   2975 N NE2  A HIS   A 1 138 ? 17.138 -12.270 -8.275  0.50 13.29 ?  138 HIS   A NE2  1 
ATOM   2976 N NE2  B HIS   A 1 138 ? 17.031 -12.027 -8.275  0.50 12.83 ?  138 HIS   A NE2  1 
ATOM   2977 H H    A HIS   A 1 138 ? 12.020 -10.113 -5.864  0.50 12.95 ?  138 HIS   A H    1 
ATOM   2978 H H    B HIS   A 1 138 ? 11.982 -9.939  -5.741  0.50 13.62 ?  138 HIS   A H    1 
ATOM   2979 H HA   A HIS   A 1 138 ? 13.221 -12.433 -5.802  0.50 12.88 ?  138 HIS   A HA   1 
ATOM   2980 H HA   B HIS   A 1 138 ? 13.038 -12.327 -5.732  0.50 13.45 ?  138 HIS   A HA   1 
ATOM   2981 H HB2  A HIS   A 1 138 ? 13.157 -11.257 -7.778  0.50 13.88 ?  138 HIS   A HB2  1 
ATOM   2982 H HB2  B HIS   A 1 138 ? 13.021 -11.197 -7.711  0.50 13.73 ?  138 HIS   A HB2  1 
ATOM   2983 H HB3  A HIS   A 1 138 ? 14.023 -10.089 -7.140  0.50 13.88 ?  138 HIS   A HB3  1 
ATOM   2984 H HB3  B HIS   A 1 138 ? 13.839 -9.988  -7.087  0.50 13.73 ?  138 HIS   A HB3  1 
ATOM   2985 H HD1  A HIS   A 1 138 ? 14.531 -13.621 -7.804  0.50 16.75 ?  138 HIS   A HD1  1 
ATOM   2986 H HD1  B HIS   A 1 138 ? 14.514 -13.502 -7.712  0.50 16.17 ?  138 HIS   A HD1  1 
ATOM   2987 H HD2  A HIS   A 1 138 ? 16.615 -10.331 -7.775  0.50 15.20 ?  138 HIS   A HD2  1 
ATOM   2988 H HD2  B HIS   A 1 138 ? 16.423 -10.109 -7.799  0.50 14.76 ?  138 HIS   A HD2  1 
ATOM   2989 H HE1  A HIS   A 1 138 ? 16.705 -14.219 -8.508  0.50 16.88 ?  138 HIS   A HE1  1 
ATOM   2990 H HE1  B HIS   A 1 138 ? 16.699 -14.000 -8.465  0.50 16.04 ?  138 HIS   A HE1  1 
ATOM   2991 N N    . SER   A 1 139 ? 14.768 -10.101 -4.232  1.00 10.26 ?  139 SER   A N    1 
ATOM   2992 C CA   . SER   A 1 139 ? 15.847 -9.913  -3.273  1.00 9.96  ?  139 SER   A CA   1 
ATOM   2993 C C    . SER   A 1 139 ? 15.640 -10.765 -2.028  1.00 9.75  ?  139 SER   A C    1 
ATOM   2994 O O    . SER   A 1 139 ? 16.598 -11.361 -1.517  1.00 9.74  ?  139 SER   A O    1 
ATOM   2995 C CB   . SER   A 1 139 ? 15.977 -8.436  -2.908  1.00 10.37 ?  139 SER   A CB   1 
ATOM   2996 O OG   . SER   A 1 139 ? 17.068 -8.269  -2.018  1.00 10.54 ?  139 SER   A OG   1 
ATOM   2997 H H    A SER   A 1 139 ? 14.311 -9.397  -4.416  0.50 12.33 ?  139 SER   A H    1 
ATOM   2998 H H    B SER   A 1 139 ? 14.343 -9.382  -4.433  0.50 12.33 ?  139 SER   A H    1 
ATOM   2999 H HA   . SER   A 1 139 ? 16.683 -10.186 -3.684  1.00 11.97 ?  139 SER   A HA   1 
ATOM   3000 H HB2  . SER   A 1 139 ? 16.144 -7.914  -3.711  1.00 12.46 ?  139 SER   A HB2  1 
ATOM   3001 H HB3  . SER   A 1 139 ? 15.160 -8.134  -2.478  1.00 12.46 ?  139 SER   A HB3  1 
ATOM   3002 H HG   . SER   A 1 139 ? 17.147 -7.457  -1.801  1.00 12.67 ?  139 SER   A HG   1 
ATOM   3003 N N    . LEU   A 1 140 ? 14.402 -10.834 -1.526  1.00 9.77  ?  140 LEU   A N    1 
ATOM   3004 C CA   . LEU   A 1 140 ? 14.139 -11.659 -0.352  1.00 9.60  ?  140 LEU   A CA   1 
ATOM   3005 C C    . LEU   A 1 140 ? 14.402 -13.133 -0.655  1.00 9.71  ?  140 LEU   A C    1 
ATOM   3006 O O    . LEU   A 1 140 ? 14.969 -13.859 0.172   1.00 10.26 ?  140 LEU   A O    1 
ATOM   3007 C CB   . LEU   A 1 140 ? 12.703 -11.439 0.126   1.00 9.85  ?  140 LEU   A CB   1 
ATOM   3008 C CG   . LEU   A 1 140 ? 12.240 -12.325 1.281   1.00 10.33 ?  140 LEU   A CG   1 
ATOM   3009 C CD1  . LEU   A 1 140 ? 13.142 -12.153 2.493   1.00 10.67 ?  140 LEU   A CD1  1 
ATOM   3010 C CD2  . LEU   A 1 140 ? 10.791 -12.029 1.645   1.00 11.43 ?  140 LEU   A CD2  1 
ATOM   3011 H H    . LEU   A 1 140 ? 13.717 -10.423 -1.840  1.00 11.74 ?  140 LEU   A H    1 
ATOM   3012 H HA   . LEU   A 1 140 ? 14.736 -11.391 0.364   1.00 11.54 ?  140 LEU   A HA   1 
ATOM   3013 H HB2  . LEU   A 1 140 ? 12.617 -10.521 0.420   1.00 11.84 ?  140 LEU   A HB2  1 
ATOM   3014 H HB3  . LEU   A 1 140 ? 12.106 -11.601 -0.618  1.00 11.84 ?  140 LEU   A HB3  1 
ATOM   3015 H HG   . LEU   A 1 140 ? 12.283 -13.255 1.004   1.00 12.42 ?  140 LEU   A HG   1 
ATOM   3016 H HD11 . LEU   A 1 140 ? 12.770 -12.653 3.237   1.00 12.82 ?  140 LEU   A HD11 1 
ATOM   3017 H HD12 . LEU   A 1 140 ? 14.025 -12.498 2.277   1.00 12.82 ?  140 LEU   A HD12 1 
ATOM   3018 H HD13 . LEU   A 1 140 ? 13.197 -11.215 2.716   1.00 12.82 ?  140 LEU   A HD13 1 
ATOM   3019 H HD21 . LEU   A 1 140 ? 10.524 -12.613 2.379   1.00 13.74 ?  140 LEU   A HD21 1 
ATOM   3020 H HD22 . LEU   A 1 140 ? 10.711 -11.105 1.915   1.00 13.74 ?  140 LEU   A HD22 1 
ATOM   3021 H HD23 . LEU   A 1 140 ? 10.226 -12.202 0.874   1.00 13.74 ?  140 LEU   A HD23 1 
ATOM   3022 N N    . ARG   A 1 141 ? 13.998 -13.590 -1.842  1.00 10.13 ?  141 ARG   A N    1 
ATOM   3023 C CA   . ARG   A 1 141 ? 14.234 -14.974 -2.235  1.00 10.98 ?  141 ARG   A CA   1 
ATOM   3024 C C    . ARG   A 1 141 ? 15.730 -15.286 -2.264  1.00 10.45 ?  141 ARG   A C    1 
ATOM   3025 O O    . ARG   A 1 141 ? 16.184 -16.303 -1.723  1.00 10.89 ?  141 ARG   A O    1 
ATOM   3026 C CB   . ARG   A 1 141 ? 13.605 -15.201 -3.612  1.00 12.57 ?  141 ARG   A CB   1 
ATOM   3027 C CG   . ARG   A 1 141 ? 13.604 -16.630 -4.095  1.00 15.75 ?  141 ARG   A CG   1 
ATOM   3028 C CD   . ARG   A 1 141 ? 12.578 -17.429 -3.352  1.00 17.42 ?  141 ARG   A CD   1 
ATOM   3029 N NE   . ARG   A 1 141 ? 13.191 -18.183 -2.276  1.00 17.81 ?  141 ARG   A NE   1 
ATOM   3030 C CZ   . ARG   A 1 141 ? 12.510 -18.777 -1.306  1.00 18.60 ?  141 ARG   A CZ   1 
ATOM   3031 N NH1  . ARG   A 1 141 ? 11.207 -18.594 -1.164  1.00 18.72 ?  141 ARG   A NH1  1 
ATOM   3032 N NH2  . ARG   A 1 141 ? 13.152 -19.574 -0.458  1.00 19.17 ?  141 ARG   A NH2  1 
ATOM   3033 H H    . ARG   A 1 141 ? 13.586 -13.120 -2.428  1.00 12.17 ?  141 ARG   A H    1 
ATOM   3034 H HA   . ARG   A 1 141 ? 13.811 -15.570 -1.600  1.00 13.20 ?  141 ARG   A HA   1 
ATOM   3035 H HB2  . ARG   A 1 141 ? 12.687 -14.892 -3.587  1.00 15.11 ?  141 ARG   A HB2  1 
ATOM   3036 H HB3  . ARG   A 1 141 ? 14.102 -14.676 -4.262  1.00 15.11 ?  141 ARG   A HB3  1 
ATOM   3037 H HG2  . ARG   A 1 141 ? 13.385 -16.651 -5.041  1.00 18.92 ?  141 ARG   A HG2  1 
ATOM   3038 H HG3  . ARG   A 1 141 ? 14.477 -17.028 -3.944  1.00 18.92 ?  141 ARG   A HG3  1 
ATOM   3039 H HD2  . ARG   A 1 141 ? 11.920 -16.832 -2.962  1.00 20.92 ?  141 ARG   A HD2  1 
ATOM   3040 H HD3  . ARG   A 1 141 ? 12.148 -18.049 -3.962  1.00 20.92 ?  141 ARG   A HD3  1 
ATOM   3041 H HE   . ARG   A 1 141 ? 14.035 -18.341 -2.326  1.00 21.39 ?  141 ARG   A HE   1 
ATOM   3042 H HH11 . ARG   A 1 141 ? 10.777 -18.092 -1.712  1.00 22.48 ?  141 ARG   A HH11 1 
ATOM   3043 H HH12 . ARG   A 1 141 ? 10.784 -18.988 -0.524  1.00 22.48 ?  141 ARG   A HH12 1 
ATOM   3044 H HH21 . ARG   A 1 141 ? 14.001 -19.696 -0.539  1.00 23.03 ?  141 ARG   A HH21 1 
ATOM   3045 H HH22 . ARG   A 1 141 ? 12.726 -19.956 0.185   1.00 23.03 ?  141 ARG   A HH22 1 
ATOM   3046 N N    . VAL   A 1 142 ? 16.522 -14.410 -2.888  1.00 10.10 ?  142 VAL   A N    1 
ATOM   3047 C CA   . VAL   A 1 142 ? 17.967 -14.627 -2.931  1.00 10.08 ?  142 VAL   A CA   1 
ATOM   3048 C C    . VAL   A 1 142 ? 18.548 -14.618 -1.524  1.00 9.57  ?  142 VAL   A C    1 
ATOM   3049 O O    . VAL   A 1 142 ? 19.411 -15.438 -1.190  1.00 9.70  ?  142 VAL   A O    1 
ATOM   3050 C CB   . VAL   A 1 142 ? 18.655 -13.602 -3.854  1.00 10.44 ?  142 VAL   A CB   1 
ATOM   3051 C CG1  . VAL   A 1 142 ? 20.169 -13.814 -3.837  1.00 10.42 ?  142 VAL   A CG1  1 
ATOM   3052 C CG2  . VAL   A 1 142 ? 18.139 -13.730 -5.272  1.00 11.50 ?  142 VAL   A CG2  1 
ATOM   3053 H H    . VAL   A 1 142 ? 16.253 -13.690 -3.284  1.00 12.14 ?  142 VAL   A H    1 
ATOM   3054 H HA   . VAL   A 1 142 ? 18.132 -15.498 -3.308  1.00 12.11 ?  142 VAL   A HA   1 
ATOM   3055 H HB   . VAL   A 1 142 ? 18.473 -12.697 -3.542  1.00 12.54 ?  142 VAL   A HB   1 
ATOM   3056 H HG11 . VAL   A 1 142 ? 20.568 -13.315 -4.569  1.00 12.53 ?  142 VAL   A HG11 1 
ATOM   3057 H HG12 . VAL   A 1 142 ? 20.528 -13.493 -2.992  1.00 12.53 ?  142 VAL   A HG12 1 
ATOM   3058 H HG13 . VAL   A 1 142 ? 20.356 -14.757 -3.940  1.00 12.53 ?  142 VAL   A HG13 1 
ATOM   3059 H HG21 . VAL   A 1 142 ? 18.601 -13.087 -5.834  1.00 13.82 ?  142 VAL   A HG21 1 
ATOM   3060 H HG22 . VAL   A 1 142 ? 18.319 -14.630 -5.584  1.00 13.82 ?  142 VAL   A HG22 1 
ATOM   3061 H HG23 . VAL   A 1 142 ? 17.190 -13.557 -5.275  1.00 13.82 ?  142 VAL   A HG23 1 
ATOM   3062 N N    . CYS   A 1 143 ? 18.089 -13.699 -0.676  1.00 9.44  ?  143 CYS   A N    1 
ATOM   3063 C CA   . CYS   A 1 143 ? 18.557 -13.672 0.704   1.00 9.60  ?  143 CYS   A CA   1 
ATOM   3064 C C    . CYS   A 1 143 ? 18.340 -15.021 1.382   1.00 9.36  ?  143 CYS   A C    1 
ATOM   3065 O O    . CYS   A 1 143 ? 19.267 -15.614 1.945   1.00 9.38  ?  143 CYS   A O    1 
ATOM   3066 C CB   . CYS   A 1 143 ? 17.820 -12.572 1.463   1.00 9.88  ?  143 CYS   A CB   1 
ATOM   3067 S SG   . CYS   A 1 143 ? 18.342 -12.403 3.188   1.00 10.25 ?  143 CYS   A SG   1 
ATOM   3068 H H    . CYS   A 1 143 ? 17.513 -13.092 -0.873  1.00 11.34 ?  143 CYS   A H    1 
ATOM   3069 H HA   . CYS   A 1 143 ? 19.505 -13.480 0.720   1.00 11.54 ?  143 CYS   A HA   1 
ATOM   3070 H HB2  . CYS   A 1 143 ? 17.976 -11.729 1.018   1.00 11.88 ?  143 CYS   A HB2  1 
ATOM   3071 H HB3  . CYS   A 1 143 ? 16.874 -12.775 1.463   1.00 11.88 ?  143 CYS   A HB3  1 
ATOM   3072 H HG   . CYS   A 1 143 ? 17.746 -11.480 3.672   1.00 12.32 ?  143 CYS   A HG   1 
ATOM   3073 N N    . VAL   A 1 144 ? 17.109 -15.520 1.336   1.00 9.81  ?  144 VAL   A N    1 
ATOM   3074 C CA   . VAL   A 1 144 ? 16.773 -16.756 2.031   1.00 10.82 ?  144 VAL   A CA   1 
ATOM   3075 C C    . VAL   A 1 144 ? 17.580 -17.922 1.485   1.00 10.68 ?  144 VAL   A C    1 
ATOM   3076 O O    . VAL   A 1 144 ? 17.961 -18.833 2.234   1.00 11.49 ?  144 VAL   A O    1 
ATOM   3077 C CB   . VAL   A 1 144 ? 15.256 -16.995 1.929   1.00 13.46 ?  144 VAL   A CB   1 
ATOM   3078 C CG1  . VAL   A 1 144 ? 14.901 -18.421 2.269   1.00 15.12 ?  144 VAL   A CG1  1 
ATOM   3079 C CG2  . VAL   A 1 144 ? 14.514 -15.992 2.819   1.00 13.48 ?  144 VAL   A CG2  1 
ATOM   3080 H H    . VAL   A 1 144 ? 16.446 -15.160 0.914   1.00 11.79 ?  144 VAL   A H    1 
ATOM   3081 H HA   . VAL   A 1 144 ? 16.990 -16.656 2.967   1.00 13.01 ?  144 VAL   A HA   1 
ATOM   3082 H HB   . VAL   A 1 144 ? 14.974 -16.831 1.012   1.00 16.17 ?  144 VAL   A HB   1 
ATOM   3083 H HG11 . VAL   A 1 144 ? 13.950 -18.470 2.463   1.00 18.17 ?  144 VAL   A HG11 1 
ATOM   3084 H HG12 . VAL   A 1 144 ? 15.111 -18.991 1.515   1.00 18.17 ?  144 VAL   A HG12 1 
ATOM   3085 H HG13 . VAL   A 1 144 ? 15.409 -18.693 3.049   1.00 18.17 ?  144 VAL   A HG13 1 
ATOM   3086 H HG21 . VAL   A 1 144 ? 13.561 -16.174 2.787   1.00 16.20 ?  144 VAL   A HG21 1 
ATOM   3087 H HG22 . VAL   A 1 144 ? 14.833 -16.077 3.731   1.00 16.20 ?  144 VAL   A HG22 1 
ATOM   3088 H HG23 . VAL   A 1 144 ? 14.684 -15.088 2.497   1.00 16.20 ?  144 VAL   A HG23 1 
ATOM   3089 N N    . ASP   A 1 145 ? 17.836 -17.930 0.179   1.00 10.95 ?  145 ASP   A N    1 
ATOM   3090 C CA   . ASP   A 1 145 ? 18.543 -19.027 -0.471  1.00 11.51 ?  145 ASP   A CA   1 
ATOM   3091 C C    . ASP   A 1 145 ? 20.064 -18.885 -0.440  1.00 11.06 ?  145 ASP   A C    1 
ATOM   3092 O O    . ASP   A 1 145 ? 20.763 -19.778 -0.931  1.00 13.23 ?  145 ASP   A O    1 
ATOM   3093 C CB   . ASP   A 1 145 ? 18.081 -19.160 -1.924  1.00 12.96 ?  145 ASP   A CB   1 
ATOM   3094 C CG   . ASP   A 1 145 ? 16.620 -19.570 -2.042  1.00 15.32 ?  145 ASP   A CG   1 
ATOM   3095 O OD1  . ASP   A 1 145 ? 16.062 -20.116 -1.067  1.00 15.71 ?  145 ASP   A OD1  1 
ATOM   3096 O OD2  . ASP   A 1 145 ? 16.026 -19.345 -3.114  1.00 16.76 -1 145 ASP   A OD2  1 
ATOM   3097 H H    . ASP   A 1 145 ? 17.594 -17.305 -0.363  1.00 13.16 ?  145 ASP   A H    1 
ATOM   3098 H HA   . ASP   A 1 145 ? 18.313 -19.852 -0.015  1.00 13.83 ?  145 ASP   A HA   1 
ATOM   3099 H HB2  . ASP   A 1 145 ? 18.197 -18.309 -2.373  1.00 15.58 ?  145 ASP   A HB2  1 
ATOM   3100 H HB3  . ASP   A 1 145 ? 18.608 -19.844 -2.361  1.00 15.58 ?  145 ASP   A HB3  1 
ATOM   3101 N N    . THR   A 1 146 ? 20.597 -17.805 0.121   1.00 9.97  ?  146 THR   A N    1 
ATOM   3102 C CA   . THR   A 1 146 ? 22.038 -17.561 0.134   1.00 9.43  ?  146 THR   A CA   1 
ATOM   3103 C C    . THR   A 1 146 ? 22.600 -17.387 1.533   1.00 9.33  ?  146 THR   A C    1 
ATOM   3104 O O    . THR   A 1 146 ? 23.680 -17.913 1.836   1.00 10.18 ?  146 THR   A O    1 
ATOM   3105 C CB   . THR   A 1 146 ? 22.361 -16.300 -0.691  1.00 9.44  ?  146 THR   A CB   1 
ATOM   3106 O OG1  . THR   A 1 146 ? 21.825 -16.440 -2.005  1.00 9.94  ?  146 THR   A OG1  1 
ATOM   3107 C CG2  . THR   A 1 146 ? 23.859 -16.075 -0.791  1.00 10.28 ?  146 THR   A CG2  1 
ATOM   3108 H H    . THR   A 1 146 ? 20.138 -17.179 0.498   1.00 11.98 ?  146 THR   A H    1 
ATOM   3109 H HA   . THR   A 1 146 ? 22.492 -18.311 -0.278  1.00 11.33 ?  146 THR   A HA   1 
ATOM   3110 H HB   . THR   A 1 146 ? 21.972 -15.524 -0.265  1.00 11.35 ?  146 THR   A HB   1 
ATOM   3111 H HG1  . THR   A 1 146 ? 20.987 -16.508 -1.966  1.00 11.95 ?  146 THR   A HG1  1 
ATOM   3112 H HG21 . THR   A 1 146 ? 24.049 -15.400 -1.461  1.00 12.36 ?  146 THR   A HG21 1 
ATOM   3113 H HG22 . THR   A 1 146 ? 24.211 -15.779 0.062   1.00 12.36 ?  146 THR   A HG22 1 
ATOM   3114 H HG23 . THR   A 1 146 ? 24.302 -16.901 -1.046  1.00 12.36 ?  146 THR   A HG23 1 
ATOM   3115 N N    . VAL   A 1 147 ? 21.919 -16.621 2.379   1.00 9.34  ?  147 VAL   A N    1 
ATOM   3116 C CA   . VAL   A 1 147 ? 22.411 -16.330 3.716   1.00 9.43  ?  147 VAL   A CA   1 
ATOM   3117 C C    . VAL   A 1 147 ? 22.093 -17.504 4.631   1.00 9.52  ?  147 VAL   A C    1 
ATOM   3118 O O    . VAL   A 1 147 ? 20.950 -17.968 4.690   1.00 10.30 ?  147 VAL   A O    1 
ATOM   3119 C CB   . VAL   A 1 147 ? 21.801 -15.023 4.246   1.00 9.52  ?  147 VAL   A CB   1 
ATOM   3120 C CG1  . VAL   A 1 147 ? 22.347 -14.712 5.624   1.00 10.77 ?  147 VAL   A CG1  1 
ATOM   3121 C CG2  . VAL   A 1 147 ? 22.063 -13.871 3.276   1.00 9.44  ?  147 VAL   A CG2  1 
ATOM   3122 H H    . VAL   A 1 147 ? 21.152 -16.265 2.205   1.00 11.22 ?  147 VAL   A H    1 
ATOM   3123 H HA   . VAL   A 1 147 ? 23.372 -16.222 3.681   1.00 11.33 ?  147 VAL   A HA   1 
ATOM   3124 H HB   . VAL   A 1 147 ? 20.842 -15.129 4.325   1.00 11.45 ?  147 VAL   A HB   1 
ATOM   3125 H HG11 . VAL   A 1 147 ? 22.101 -13.808 5.868   1.00 12.95 ?  147 VAL   A HG11 1 
ATOM   3126 H HG12 . VAL   A 1 147 ? 21.970 -15.340 6.264   1.00 12.95 ?  147 VAL   A HG12 1 
ATOM   3127 H HG13 . VAL   A 1 147 ? 23.314 -14.799 5.609   1.00 12.95 ?  147 VAL   A HG13 1 
ATOM   3128 H HG21 . VAL   A 1 147 ? 21.736 -13.045 3.674   1.00 11.35 ?  147 VAL   A HG21 1 
ATOM   3129 H HG22 . VAL   A 1 147 ? 23.015 -13.804 3.114   1.00 11.35 ?  147 VAL   A HG22 1 
ATOM   3130 H HG23 . VAL   A 1 147 ? 21.593 -14.043 2.446   1.00 11.35 ?  147 VAL   A HG23 1 
ATOM   3131 N N    . ARG   A 1 148 ? 23.119 -17.985 5.337   1.00 9.52  ?  148 ARG   A N    1 
ATOM   3132 C CA   . ARG   A 1 148 ? 22.999 -19.067 6.302   1.00 9.90  ?  148 ARG   A CA   1 
ATOM   3133 C C    . ARG   A 1 148 ? 23.140 -18.597 7.738   1.00 10.50 ?  148 ARG   A C    1 
ATOM   3134 O O    . ARG   A 1 148 ? 22.733 -19.321 8.655   1.00 11.87 ?  148 ARG   A O    1 
ATOM   3135 C CB   . ARG   A 1 148 ? 24.031 -20.162 6.000   1.00 10.41 ?  148 ARG   A CB   1 
ATOM   3136 C CG   . ARG   A 1 148 ? 23.833 -20.800 4.635   1.00 11.59 ?  148 ARG   A CG   1 
ATOM   3137 C CD   . ARG   A 1 148 ? 24.912 -21.830 4.299   1.00 12.56 ?  148 ARG   A CD   1 
ATOM   3138 N NE   . ARG   A 1 148 ? 26.250 -21.251 4.319   1.00 12.47 ?  148 ARG   A NE   1 
ATOM   3139 C CZ   . ARG   A 1 148 ? 26.749 -20.490 3.353   1.00 11.97 ?  148 ARG   A CZ   1 
ATOM   3140 N NH1  . ARG   A 1 148 ? 26.062 -20.235 2.251   1.00 12.86 ?  148 ARG   A NH1  1 
ATOM   3141 N NH2  . ARG   A 1 148 ? 27.970 -19.970 3.498   1.00 12.60 ?  148 ARG   A NH2  1 
ATOM   3142 H H    . ARG   A 1 148 ? 23.929 -17.685 5.257   1.00 11.44 ?  148 ARG   A H    1 
ATOM   3143 H HA   . ARG   A 1 148 ? 22.119 -19.457 6.204   1.00 11.90 ?  148 ARG   A HA   1 
ATOM   3144 H HB2  . ARG   A 1 148 ? 24.918 -19.783 6.027   1.00 12.51 ?  148 ARG   A HB2  1 
ATOM   3145 H HB3  . ARG   A 1 148 ? 23.944 -20.864 6.666   1.00 12.51 ?  148 ARG   A HB3  1 
ATOM   3146 H HG2  . ARG   A 1 148 ? 22.970 -21.243 4.615   1.00 13.93 ?  148 ARG   A HG2  1 
ATOM   3147 H HG3  . ARG   A 1 148 ? 23.860 -20.102 3.958   1.00 13.93 ?  148 ARG   A HG3  1 
ATOM   3148 H HD2  . ARG   A 1 148 ? 24.882 -22.547 4.950   1.00 15.09 ?  148 ARG   A HD2  1 
ATOM   3149 H HD3  . ARG   A 1 148 ? 24.744 -22.187 3.408   1.00 15.09 ?  148 ARG   A HD3  1 
ATOM   3150 H HE   . ARG   A 1 148 ? 26.750 -21.419 4.992   1.00 14.99 ?  148 ARG   A HE   1 
ATOM   3151 H HH11 . ARG   A 1 148 ? 25.273 -20.556 2.144   1.00 15.45 ?  148 ARG   A HH11 1 
ATOM   3152 H HH12 . ARG   A 1 148 ? 26.402 -19.728 1.640   1.00 15.45 ?  148 ARG   A HH12 1 
ATOM   3153 H HH21 . ARG   A 1 148 ? 28.415 -20.121 4.212   1.00 15.14 ?  148 ARG   A HH21 1 
ATOM   3154 H HH22 . ARG   A 1 148 ? 28.295 -19.463 2.882   1.00 15.14 ?  148 ARG   A HH22 1 
ATOM   3155 N N    . THR   A 1 149 ? 23.699 -17.412 7.953   1.00 10.11 ?  149 THR   A N    1 
ATOM   3156 C CA   . THR   A 1 149 ? 23.783 -16.818 9.271   1.00 10.24 ?  149 THR   A CA   1 
ATOM   3157 C C    . THR   A 1 149 ? 22.459 -16.124 9.592   1.00 9.72  ?  149 THR   A C    1 
ATOM   3158 O O    . THR   A 1 149 ? 21.508 -16.134 8.800   1.00 10.34 ?  149 THR   A O    1 
ATOM   3159 C CB   . THR   A 1 149 ? 24.982 -15.879 9.325   1.00 10.62 ?  149 THR   A CB   1 
ATOM   3160 O OG1  . THR   A 1 149 ? 24.838 -14.938 8.257   1.00 10.65 ?  149 THR   A OG1  1 
ATOM   3161 C CG2  . THR   A 1 149 ? 26.295 -16.666 9.192   1.00 11.25 ?  149 THR   A CG2  1 
ATOM   3162 H H    . THR   A 1 149 ? 24.049 -16.924 7.331   1.00 12.15 ?  149 THR   A H    1 
ATOM   3163 H HA   . THR   A 1 149 ? 23.915 -17.526 9.925   1.00 12.31 ?  149 THR   A HA   1 
ATOM   3164 H HB   . THR   A 1 149 ? 24.980 -15.417 10.175  1.00 12.76 ?  149 THR   A HB   1 
ATOM   3165 H HG1  . THR   A 1 149 ? 25.488 -14.406 8.262   1.00 12.80 ?  149 THR   A HG1  1 
ATOM   3166 H HG21 . THR   A 1 149 ? 27.049 -16.060 9.244   1.00 13.52 ?  149 THR   A HG21 1 
ATOM   3167 H HG22 . THR   A 1 149 ? 26.368 -17.321 9.906   1.00 13.52 ?  149 THR   A HG22 1 
ATOM   3168 H HG23 . THR   A 1 149 ? 26.323 -17.131 8.339   1.00 13.52 ?  149 THR   A HG23 1 
ATOM   3169 N N    . ASN   A 1 150 ? 22.353 -15.568 10.791  1.00 10.19 ?  150 ASN   A N    1 
ATOM   3170 C CA   . ASN   A 1 150 ? 21.067 -15.073 11.285  1.00 10.54 ?  150 ASN   A CA   1 
ATOM   3171 C C    . ASN   A 1 150 ? 20.871 -13.630 10.843  1.00 9.99  ?  150 ASN   A C    1 
ATOM   3172 O O    . ASN   A 1 150 ? 21.598 -12.730 11.284  1.00 11.79 ?  150 ASN   A O    1 
ATOM   3173 C CB   . ASN   A 1 150 ? 21.020 -15.202 12.800  1.00 13.12 ?  150 ASN   A CB   1 
ATOM   3174 C CG   . ASN   A 1 150 ? 20.913 -16.638 13.243  1.00 17.84 ?  150 ASN   A CG   1 
ATOM   3175 O OD1  . ASN   A 1 150 ? 20.275 -17.453 12.576  1.00 19.41 ?  150 ASN   A OD1  1 
ATOM   3176 N ND2  . ASN   A 1 150 ? 21.562 -16.970 14.354  1.00 20.07 ?  150 ASN   A ND2  1 
ATOM   3177 H H    . ASN   A 1 150 ? 23.003 -15.466 11.338  1.00 12.24 ?  150 ASN   A H    1 
ATOM   3178 H HA   . ASN   A 1 150 ? 20.347 -15.611 10.912  1.00 12.67 ?  150 ASN   A HA   1 
ATOM   3179 H HB2  . ASN   A 1 150 ? 21.832 -14.829 13.177  1.00 15.76 ?  150 ASN   A HB2  1 
ATOM   3180 H HB3  . ASN   A 1 150 ? 20.245 -14.729 13.139  1.00 15.76 ?  150 ASN   A HB3  1 
ATOM   3181 H HD21 . ASN   A 1 150 ? 21.537 -17.781 14.649  1.00 24.10 ?  150 ASN   A HD21 1 
ATOM   3182 H HD22 . ASN   A 1 150 ? 22.002 -16.373 14.793  1.00 24.10 ?  150 ASN   A HD22 1 
ATOM   3183 N N    . VAL   A 1 151 ? 19.890 -13.406 9.975   1.00 9.66  ?  151 VAL   A N    1 
ATOM   3184 C CA   . VAL   A 1 151 ? 19.664 -12.093 9.392   1.00 9.40  ?  151 VAL   A CA   1 
ATOM   3185 C C    . VAL   A 1 151 ? 18.279 -11.586 9.775   1.00 9.22  ?  151 VAL   A C    1 
ATOM   3186 O O    . VAL   A 1 151 ? 17.273 -12.300 9.638   1.00 10.55 ?  151 VAL   A O    1 
ATOM   3187 C CB   . VAL   A 1 151 ? 19.931 -12.069 7.873   1.00 10.62 ?  151 VAL   A CB   1 
ATOM   3188 C CG1  . VAL   A 1 151 ? 19.115 -13.094 7.121   1.00 12.08 ?  151 VAL   A CG1  1 
ATOM   3189 C CG2  . VAL   A 1 151 ? 19.721 -10.660 7.306   1.00 10.99 ?  151 VAL   A CG2  1 
ATOM   3190 H H    . VAL   A 1 151 ? 19.337 -14.007 9.701   1.00 11.61 ?  151 VAL   A H    1 
ATOM   3191 H HA   . VAL   A 1 151 ? 20.306 -11.479 9.784   1.00 11.30 ?  151 VAL   A HA   1 
ATOM   3192 H HB   . VAL   A 1 151 ? 20.869 -12.289 7.723   1.00 12.76 ?  151 VAL   A HB   1 
ATOM   3193 H HG11 . VAL   A 1 151 ? 19.303 -13.025 6.171   1.00 14.51 ?  151 VAL   A HG11 1 
ATOM   3194 H HG12 . VAL   A 1 151 ? 19.351 -13.982 7.438   1.00 14.51 ?  151 VAL   A HG12 1 
ATOM   3195 H HG13 . VAL   A 1 151 ? 18.172 -12.928 7.281   1.00 14.51 ?  151 VAL   A HG13 1 
ATOM   3196 H HG21 . VAL   A 1 151 ? 20.031 -10.641 6.383   1.00 13.21 ?  151 VAL   A HG21 1 
ATOM   3197 H HG22 . VAL   A 1 151 ? 18.777 -10.444 7.337   1.00 13.21 ?  151 VAL   A HG22 1 
ATOM   3198 H HG23 . VAL   A 1 151 ? 20.228 -10.026 7.834   1.00 13.21 ?  151 VAL   A HG23 1 
ATOM   3199 N N    . TYR   A 1 152 ? 18.265 -10.348 10.274  1.00 9.07  ?  152 TYR   A N    1 
ATOM   3200 C CA   . TYR   A 1 152 ? 17.080 -9.609  10.684  1.00 8.73  ?  152 TYR   A CA   1 
ATOM   3201 C C    . TYR   A 1 152 ? 16.880 -8.505  9.653   1.00 8.37  ?  152 TYR   A C    1 
ATOM   3202 O O    . TYR   A 1 152 ? 17.646 -7.536  9.611   1.00 9.10  ?  152 TYR   A O    1 
ATOM   3203 C CB   . TYR   A 1 152 ? 17.288 -9.076  12.101  1.00 9.23  ?  152 TYR   A CB   1 
ATOM   3204 C CG   . TYR   A 1 152 ? 17.255 -10.214 13.089  1.00 10.06 ?  152 TYR   A CG   1 
ATOM   3205 C CD1  . TYR   A 1 152 ? 18.388 -10.969 13.350  1.00 11.47 ?  152 TYR   A CD1  1 
ATOM   3206 C CD2  . TYR   A 1 152 ? 16.074 -10.579 13.711  1.00 10.24 ?  152 TYR   A CD2  1 
ATOM   3207 C CE1  . TYR   A 1 152 ? 18.351 -12.048 14.214  1.00 12.88 ?  152 TYR   A CE1  1 
ATOM   3208 C CE2  . TYR   A 1 152 ? 16.023 -11.664 14.579  1.00 11.74 ?  152 TYR   A CE2  1 
ATOM   3209 C CZ   . TYR   A 1 152 ? 17.165 -12.390 14.829  1.00 12.80 ?  152 TYR   A CZ   1 
ATOM   3210 O OH   . TYR   A 1 152 ? 17.121 -13.475 15.690  1.00 15.06 ?  152 TYR   A OH   1 
ATOM   3211 H H    . TYR   A 1 152 ? 18.987 -9.882  10.379  1.00 10.90 ?  152 TYR   A H    1 
ATOM   3212 H HA   . TYR   A 1 152 ? 16.308 -10.194 10.677  1.00 10.50 ?  152 TYR   A HA   1 
ATOM   3213 H HB2  . TYR   A 1 152 ? 18.155 -8.648  12.164  1.00 11.10 ?  152 TYR   A HB2  1 
ATOM   3214 H HB3  . TYR   A 1 152 ? 16.584 -8.450  12.326  1.00 11.10 ?  152 TYR   A HB3  1 
ATOM   3215 H HD1  . TYR   A 1 152 ? 19.187 -10.745 12.929  1.00 13.79 ?  152 TYR   A HD1  1 
ATOM   3216 H HD2  . TYR   A 1 152 ? 15.296 -10.095 13.535  1.00 12.31 ?  152 TYR   A HD2  1 
ATOM   3217 H HE1  . TYR   A 1 152 ? 19.123 -12.534 14.384  1.00 15.48 ?  152 TYR   A HE1  1 
ATOM   3218 H HE2  . TYR   A 1 152 ? 15.220 -11.885 14.994  1.00 14.11 ?  152 TYR   A HE2  1 
ATOM   3219 H HH   . TYR   A 1 152 ? 16.340 -13.557 15.999  1.00 18.09 ?  152 TYR   A HH   1 
ATOM   3220 N N    A LEU   A 1 153 ? 15.830 -8.628  8.846   0.50 8.51  ?  153 LEU   A N    1 
ATOM   3221 N N    B LEU   A 1 153 ? 15.897 -8.710  8.777   0.50 8.48  ?  153 LEU   A N    1 
ATOM   3222 C CA   A LEU   A 1 153 ? 15.568 -7.701  7.753   0.50 8.49  ?  153 LEU   A CA   1 
ATOM   3223 C CA   B LEU   A 1 153 ? 15.613 -7.809  7.669   0.50 8.80  ?  153 LEU   A CA   1 
ATOM   3224 C C    A LEU   A 1 153 ? 14.582 -6.622  8.181   0.50 8.72  ?  153 LEU   A C    1 
ATOM   3225 C C    B LEU   A 1 153 ? 14.600 -6.754  8.084   0.50 8.68  ?  153 LEU   A C    1 
ATOM   3226 O O    A LEU   A 1 153 ? 13.471 -6.931  8.634   0.50 9.81  ?  153 LEU   A O    1 
ATOM   3227 O O    B LEU   A 1 153 ? 13.611 -7.055  8.763   0.50 9.41  ?  153 LEU   A O    1 
ATOM   3228 C CB   A LEU   A 1 153 ? 14.992 -8.448  6.552   0.50 8.43  ?  153 LEU   A CB   1 
ATOM   3229 C CB   B LEU   A 1 153 ? 15.049 -8.597  6.484   0.50 9.06  ?  153 LEU   A CB   1 
ATOM   3230 C CG   A LEU   A 1 153 ? 15.904 -9.436  5.826   0.50 8.62  ?  153 LEU   A CG   1 
ATOM   3231 C CG   B LEU   A 1 153 ? 15.998 -9.627  5.869   0.50 9.46  ?  153 LEU   A CG   1 
ATOM   3232 C CD1  A LEU   A 1 153 ? 15.070 -10.327 4.923   0.50 9.20  ?  153 LEU   A CD1  1 
ATOM   3233 C CD1  B LEU   A 1 153 ? 15.270 -10.480 4.836   0.50 9.94  ?  153 LEU   A CD1  1 
ATOM   3234 C CD2  A LEU   A 1 153 ? 16.953 -8.705  5.014   0.50 8.41  ?  153 LEU   A CD2  1 
ATOM   3235 C CD2  B LEU   A 1 153 ? 17.207 -8.938  5.247   0.50 9.28  ?  153 LEU   A CD2  1 
ATOM   3236 H H    A LEU   A 1 153 ? 15.237 -9.253  8.922   0.50 10.23 ?  153 LEU   A H    1 
ATOM   3237 H H    B LEU   A 1 153 ? 15.367 -9.393  8.809   0.50 10.19 ?  153 LEU   A H    1 
ATOM   3238 H HA   A LEU   A 1 153 ? 16.399 -7.279  7.497   0.50 10.20 ?  153 LEU   A HA   1 
ATOM   3239 H HA   B LEU   A 1 153 ? 16.429 -7.375  7.394   0.50 10.58 ?  153 LEU   A HA   1 
ATOM   3240 H HB2  A LEU   A 1 153 ? 14.218 -8.940  6.858   0.50 10.13 ?  153 LEU   A HB2  1 
ATOM   3241 H HB2  B LEU   A 1 153 ? 14.253 -9.070  6.776   0.50 10.89 ?  153 LEU   A HB2  1 
ATOM   3242 H HB3  A LEU   A 1 153 ? 14.715 -7.783  5.904   0.50 10.13 ?  153 LEU   A HB3  1 
ATOM   3243 H HB3  B LEU   A 1 153 ? 14.810 -7.967  5.784   0.50 10.89 ?  153 LEU   A HB3  1 
ATOM   3244 H HG   A LEU   A 1 153 ? 16.356 -9.993  6.480   0.50 10.36 ?  153 LEU   A HG   1 
ATOM   3245 H HG   B LEU   A 1 153 ? 16.317 -10.215 6.571   0.50 11.37 ?  153 LEU   A HG   1 
ATOM   3246 H HD11 A LEU   A 1 153 ? 15.658 -10.950 4.470   0.50 11.06 ?  153 LEU   A HD11 1 
ATOM   3247 H HD11 B LEU   A 1 153 ? 15.783 -11.285 4.672   0.50 11.94 ?  153 LEU   A HD11 1 
ATOM   3248 H HD12 A LEU   A 1 153 ? 14.426 -10.809 5.462   0.50 11.06 ?  153 LEU   A HD12 1 
ATOM   3249 H HD12 B LEU   A 1 153 ? 14.394 -10.712 5.180   0.50 11.94 ?  153 LEU   A HD12 1 
ATOM   3250 H HD13 A LEU   A 1 153 ? 14.611 -9.772  4.273   0.50 11.06 ?  153 LEU   A HD13 1 
ATOM   3251 H HD13 B LEU   A 1 153 ? 15.177 -9.970  4.016   0.50 11.94 ?  153 LEU   A HD13 1 
ATOM   3252 H HD21 A LEU   A 1 153 ? 17.511 -9.358  4.570   0.50 10.11 ?  153 LEU   A HD21 1 
ATOM   3253 H HD21 B LEU   A 1 153 ? 17.762 -9.605  4.819   0.50 11.15 ?  153 LEU   A HD21 1 
ATOM   3254 H HD22 A LEU   A 1 153 ? 16.503 -8.148  4.358   0.50 10.11 ?  153 LEU   A HD22 1 
ATOM   3255 H HD22 B LEU   A 1 153 ? 16.898 -8.292  4.595   0.50 11.15 ?  153 LEU   A HD22 1 
ATOM   3256 H HD23 A LEU   A 1 153 ? 17.484 -8.156  5.608   0.50 10.11 ?  153 LEU   A HD23 1 
ATOM   3257 H HD23 B LEU   A 1 153 ? 17.709 -8.491  5.946   0.50 11.15 ?  153 LEU   A HD23 1 
ATOM   3258 N N    A ALA   A 1 154 ? 14.981 -5.361  8.003   0.50 8.25  ?  154 ALA   A N    1 
ATOM   3259 N N    B ALA   A 1 154 ? 14.837 -5.523  7.636   0.50 8.09  ?  154 ALA   A N    1 
ATOM   3260 C CA   A ALA   A 1 154 ? 14.112 -4.209  8.215   0.50 9.38  ?  154 ALA   A CA   1 
ATOM   3261 C CA   B ALA   A 1 154 ? 13.950 -4.402  7.903   0.50 8.72  ?  154 ALA   A CA   1 
ATOM   3262 C C    A ALA   A 1 154 ? 13.605 -3.716  6.864   0.50 9.40  ?  154 ALA   A C    1 
ATOM   3263 C C    B ALA   A 1 154 ? 13.411 -3.861  6.591   0.50 8.44  ?  154 ALA   A C    1 
ATOM   3264 O O    A ALA   A 1 154 ? 14.406 -3.402  5.975   0.50 8.80  ?  154 ALA   A O    1 
ATOM   3265 O O    B ALA   A 1 154 ? 14.173 -3.643  5.642   0.50 9.28  ?  154 ALA   A O    1 
ATOM   3266 C CB   A ALA   A 1 154 ? 14.869 -3.088  8.926   0.50 10.17 ?  154 ALA   A CB   1 
ATOM   3267 C CB   B ALA   A 1 154 ? 14.679 -3.288  8.653   0.50 9.60  ?  154 ALA   A CB   1 
ATOM   3268 H H    A ALA   A 1 154 ? 15.781 -5.142  7.753   0.50 9.92  ?  154 ALA   A H    1 
ATOM   3269 H H    B ALA   A 1 154 ? 15.519 -5.321  7.150   0.50 9.72  ?  154 ALA   A H    1 
ATOM   3270 H HA   A ALA   A 1 154 ? 13.355 -4.466  8.757   0.50 11.28 ?  154 ALA   A HA   1 
ATOM   3271 H HA   B ALA   A 1 154 ? 13.205 -4.702  8.441   0.50 10.48 ?  154 ALA   A HA   1 
ATOM   3272 H HB1  A ALA   A 1 154 ? 14.270 -2.335  9.052   0.50 12.22 ?  154 ALA   A HB1  1 
ATOM   3273 H HB1  B ALA   A 1 154 ? 14.062 -2.559  8.810   0.50 11.54 ?  154 ALA   A HB1  1 
ATOM   3274 H HB2  A ALA   A 1 154 ? 15.179 -3.413  9.784   0.50 12.22 ?  154 ALA   A HB2  1 
ATOM   3275 H HB2  B ALA   A 1 154 ? 15.006 -3.637  9.496   0.50 11.54 ?  154 ALA   A HB2  1 
ATOM   3276 H HB3  A ALA   A 1 154 ? 15.625 -2.819  8.380   0.50 12.22 ?  154 ALA   A HB3  1 
ATOM   3277 H HB3  B ALA   A 1 154 ? 15.426 -2.978  8.112   0.50 11.54 ?  154 ALA   A HB3  1 
ATOM   3278 N N    A VAL   A 1 155 ? 12.282 -3.626  6.723   0.50 10.43 ?  155 VAL   A N    1 
ATOM   3279 N N    B VAL   A 1 155 ? 12.099 -3.631  6.557   0.50 8.87  ?  155 VAL   A N    1 
ATOM   3280 C CA   A VAL   A 1 155 ? 11.631 -3.114  5.519   0.50 11.27 ?  155 VAL   A CA   1 
ATOM   3281 C CA   B VAL   A 1 155 ? 11.401 -3.035  5.426   0.50 9.57  ?  155 VAL   A CA   1 
ATOM   3282 C C    A VAL   A 1 155 ? 10.908 -1.822  5.888   0.50 12.19 ?  155 VAL   A C    1 
ATOM   3283 C C    B VAL   A 1 155 ? 10.440 -2.008  6.009   0.50 10.37 ?  155 VAL   A C    1 
ATOM   3284 O O    A VAL   A 1 155 ? 10.039 -1.820  6.769   0.50 12.29 ?  155 VAL   A O    1 
ATOM   3285 O O    B VAL   A 1 155 ? 9.611  -2.350  6.857   0.50 10.72 ?  155 VAL   A O    1 
ATOM   3286 C CB   A VAL   A 1 155 ? 10.660 -4.142  4.915   0.50 11.64 ?  155 VAL   A CB   1 
ATOM   3287 C CB   B VAL   A 1 155 ? 10.636 -4.095  4.611   0.50 10.33 ?  155 VAL   A CB   1 
ATOM   3288 C CG1  A VAL   A 1 155 ? 9.919  -3.530  3.730   0.50 12.41 ?  155 VAL   A CG1  1 
ATOM   3289 C CG1  B VAL   A 1 155 ? 9.816  -3.436  3.515   0.50 11.39 ?  155 VAL   A CG1  1 
ATOM   3290 C CG2  A VAL   A 1 155 ? 11.406 -5.409  4.495   0.50 11.92 ?  155 VAL   A CG2  1 
ATOM   3291 C CG2  B VAL   A 1 155 ? 11.610 -5.113  4.024   0.50 11.01 ?  155 VAL   A CG2  1 
ATOM   3292 H H    A VAL   A 1 155 ? 11.723 -3.862  7.334   0.50 12.53 ?  155 VAL   A H    1 
ATOM   3293 H H    B VAL   A 1 155 ? 11.570 -3.815  7.216   0.50 10.66 ?  155 VAL   A H    1 
ATOM   3294 H HA   A VAL   A 1 155 ? 12.304 -2.907  4.853   0.50 13.54 ?  155 VAL   A HA   1 
ATOM   3295 H HA   B VAL   A 1 155 ? 12.028 -2.585  4.845   0.50 11.51 ?  155 VAL   A HA   1 
ATOM   3296 H HB   A VAL   A 1 155 ? 10.001 -4.387  5.584   0.50 13.98 ?  155 VAL   A HB   1 
ATOM   3297 H HB   B VAL   A 1 155 ? 10.023 -4.568  5.201   0.50 12.41 ?  155 VAL   A HB   1 
ATOM   3298 H HG11 A VAL   A 1 155 ? 9.493  -4.239  3.224   0.50 14.92 ?  155 VAL   A HG11 1 
ATOM   3299 H HG11 B VAL   A 1 155 ? 9.534  -4.118  2.884   0.50 13.69 ?  155 VAL   A HG11 1 
ATOM   3300 H HG12 A VAL   A 1 155 ? 9.246  -2.910  4.057   0.50 14.92 ?  155 VAL   A HG12 1 
ATOM   3301 H HG12 B VAL   A 1 155 ? 9.039  -3.011  3.909   0.50 13.69 ?  155 VAL   A HG12 1 
ATOM   3302 H HG13 A VAL   A 1 155 ? 10.555 -3.060  3.167   0.50 14.92 ?  155 VAL   A HG13 1 
ATOM   3303 H HG13 B VAL   A 1 155 ? 10.366 -2.778  3.066   0.50 13.69 ?  155 VAL   A HG13 1 
ATOM   3304 H HG21 A VAL   A 1 155 ? 10.776 -6.031  4.100   0.50 14.33 ?  155 VAL   A HG21 1 
ATOM   3305 H HG21 B VAL   A 1 155 ? 11.111 -5.766  3.507   0.50 13.23 ?  155 VAL   A HG21 1 
ATOM   3306 H HG22 A VAL   A 1 155 ? 12.087 -5.171  3.843   0.50 14.33 ?  155 VAL   A HG22 1 
ATOM   3307 H HG22 B VAL   A 1 155 ? 12.242 -4.652  3.454   0.50 13.23 ?  155 VAL   A HG22 1 
ATOM   3308 H HG23 A VAL   A 1 155 ? 11.820 -5.805  5.275   0.50 14.33 ?  155 VAL   A HG23 1 
ATOM   3309 H HG23 B VAL   A 1 155 ? 12.078 -5.558  4.749   0.50 13.23 ?  155 VAL   A HG23 1 
ATOM   3310 N N    A PHE   A 1 156 ? 11.255 -0.728  5.201   0.50 13.49 ?  156 PHE   A N    1 
ATOM   3311 N N    B PHE   A 1 156 ? 10.566 -0.746  5.591   0.50 10.99 ?  156 PHE   A N    1 
ATOM   3312 C CA   A PHE   A 1 156 ? 10.751 0.592   5.581   0.50 14.67 ?  156 PHE   A CA   1 
ATOM   3313 C CA   B PHE   A 1 156 ? 9.724  0.293   6.176   0.50 11.82 ?  156 PHE   A CA   1 
ATOM   3314 C C    A PHE   A 1 156 ? 9.271  0.758   5.247   0.50 14.87 ?  156 PHE   A C    1 
ATOM   3315 C C    B PHE   A 1 156 ? 8.371  0.400   5.480   0.50 12.05 ?  156 PHE   A C    1 
ATOM   3316 O O    A PHE   A 1 156 ? 8.497  1.285   6.057   0.50 15.57 ?  156 PHE   A O    1 
ATOM   3317 O O    B PHE   A 1 156 ? 7.342  0.589   6.144   0.50 12.37 ?  156 PHE   A O    1 
ATOM   3318 C CB   A PHE   A 1 156 ? 11.586 1.671   4.890   0.50 15.59 ?  156 PHE   A CB   1 
ATOM   3319 C CB   B PHE   A 1 156 ? 10.441 1.648   6.154   0.50 12.23 ?  156 PHE   A CB   1 
ATOM   3320 C CG   A PHE   A 1 156 ? 11.147 3.074   5.198   0.50 16.58 ?  156 PHE   A CG   1 
ATOM   3321 C CG   B PHE   A 1 156 ? 9.650  2.746   6.800   0.50 12.78 ?  156 PHE   A CG   1 
ATOM   3322 C CD1  A PHE   A 1 156 ? 11.158 3.547   6.500   0.50 17.78 ?  156 PHE   A CD1  1 
ATOM   3323 C CD1  B PHE   A 1 156 ? 9.724  2.958   8.167   0.50 13.14 ?  156 PHE   A CD1  1 
ATOM   3324 C CD2  A PHE   A 1 156 ? 10.744 3.926   4.183   0.50 17.29 ?  156 PHE   A CD2  1 
ATOM   3325 C CD2  B PHE   A 1 156 ? 8.815  3.551   6.045   0.50 13.38 ?  156 PHE   A CD2  1 
ATOM   3326 C CE1  A PHE   A 1 156 ? 10.765 4.844   6.784   0.50 18.52 ?  156 PHE   A CE1  1 
ATOM   3327 C CE1  B PHE   A 1 156 ? 8.986  3.966   8.765   0.50 13.84 ?  156 PHE   A CE1  1 
ATOM   3328 C CE2  A PHE   A 1 156 ? 10.349 5.223   4.460   0.50 18.11 ?  156 PHE   A CE2  1 
ATOM   3329 C CE2  B PHE   A 1 156 ? 8.074  4.554   6.636   0.50 14.00 ?  156 PHE   A CE2  1 
ATOM   3330 C CZ   A PHE   A 1 156 ? 10.361 5.682   5.762   0.50 18.56 ?  156 PHE   A CZ   1 
ATOM   3331 C CZ   B PHE   A 1 156 ? 8.162  4.764   7.997   0.50 13.97 ?  156 PHE   A CZ   1 
ATOM   3332 H H    A PHE   A 1 156 ? 11.782 -0.726  4.516   0.50 16.20 ?  156 PHE   A H    1 
ATOM   3333 H H    B PHE   A 1 156 ? 11.119 -0.467  4.984   0.50 13.21 ?  156 PHE   A H    1 
ATOM   3334 H HA   A PHE   A 1 156 ? 10.850 0.702   6.532   0.50 17.62 ?  156 PHE   A HA   1 
ATOM   3335 H HA   B PHE   A 1 156 ? 9.562  0.069   7.102   0.50 14.20 ?  156 PHE   A HA   1 
ATOM   3336 H HB2  A PHE   A 1 156 ? 12.508 1.581   5.175   0.50 18.73 ?  156 PHE   A HB2  1 
ATOM   3337 H HB2  B PHE   A 1 156 ? 11.285 1.562   6.633   0.50 14.70 ?  156 PHE   A HB2  1 
ATOM   3338 H HB3  A PHE   A 1 156 ? 11.527 1.550   3.929   0.50 18.73 ?  156 PHE   A HB3  1 
ATOM   3339 H HB3  B PHE   A 1 156 ? 10.612 1.902   5.235   0.50 14.70 ?  156 PHE   A HB3  1 
ATOM   3340 H HD1  A PHE   A 1 156 ? 11.430 2.986   7.192   0.50 21.35 ?  156 PHE   A HD1  1 
ATOM   3341 H HD1  B PHE   A 1 156 ? 10.282 2.422   8.689   0.50 15.79 ?  156 PHE   A HD1  1 
ATOM   3342 H HD2  A PHE   A 1 156 ? 10.737 3.620   3.305   0.50 20.77 ?  156 PHE   A HD2  1 
ATOM   3343 H HD2  B PHE   A 1 156 ? 8.760  3.415   5.127   0.50 16.07 ?  156 PHE   A HD2  1 
ATOM   3344 H HE1  A PHE   A 1 156 ? 10.770 5.148   7.664   0.50 22.24 ?  156 PHE   A HE1  1 
ATOM   3345 H HE1  B PHE   A 1 156 ? 9.048  4.105   9.685   0.50 16.62 ?  156 PHE   A HE1  1 
ATOM   3346 H HE2  A PHE   A 1 156 ? 10.076 5.782   3.770   0.50 21.75 ?  156 PHE   A HE2  1 
ATOM   3347 H HE2  B PHE   A 1 156 ? 7.527  5.093   6.114   0.50 16.82 ?  156 PHE   A HE2  1 
ATOM   3348 H HZ   A PHE   A 1 156 ? 10.091 6.550   5.952   0.50 22.29 ?  156 PHE   A HZ   1 
ATOM   3349 H HZ   B PHE   A 1 156 ? 7.668  5.443   8.396   0.50 16.79 ?  156 PHE   A HZ   1 
ATOM   3350 N N    A ASP   A 1 157 ? 8.869  0.346   4.048   0.50 14.84 ?  157 ASP   A N    1 
ATOM   3351 N N    B ASP   A 1 157 ? 8.366  0.298   4.152   0.50 12.10 ?  157 ASP   A N    1 
ATOM   3352 C CA   A ASP   A 1 157 ? 7.519  0.579   3.546   0.50 15.16 ?  157 ASP   A CA   1 
ATOM   3353 C CA   B ASP   A 1 157 ? 7.154  0.335   3.342   0.50 12.83 ?  157 ASP   A CA   1 
ATOM   3354 C C    A ASP   A 1 157 ? 6.573  -0.464  4.138   0.50 14.45 ?  157 ASP   A C    1 
ATOM   3355 C C    B ASP   A 1 157 ? 6.202  -0.783  3.747   0.50 12.70 ?  157 ASP   A C    1 
ATOM   3356 O O    A ASP   A 1 157 ? 6.783  -1.665  3.946   0.50 13.59 ?  157 ASP   A O    1 
ATOM   3357 O O    B ASP   A 1 157 ? 6.480  -1.962  3.505   0.50 12.64 ?  157 ASP   A O    1 
ATOM   3358 C CB   A ASP   A 1 157 ? 7.564  0.446   2.024   0.50 16.23 ?  157 ASP   A CB   1 
ATOM   3359 C CB   B ASP   A 1 157 ? 7.561  0.203   1.871   0.50 14.43 ?  157 ASP   A CB   1 
ATOM   3360 C CG   A ASP   A 1 157 ? 6.283  0.921   1.357   0.50 17.65 ?  157 ASP   A CG   1 
ATOM   3361 C CG   B ASP   A 1 157 ? 6.396  0.209   0.927   0.50 16.16 ?  157 ASP   A CG   1 
ATOM   3362 O OD1  A ASP   A 1 157 ? 6.052  2.152   1.307   0.50 19.77 ?  157 ASP   A OD1  1 
ATOM   3363 O OD1  B ASP   A 1 157 ? 5.240  0.267   1.390   0.50 16.61 ?  157 ASP   A OD1  1 
ATOM   3364 O OD2  A ASP   A 1 157 ? 5.511  0.058   0.880   0.50 18.04 -1 157 ASP   A OD2  1 
ATOM   3365 O OD2  B ASP   A 1 157 ? 6.658  0.147   -0.295  0.50 17.22 -1 157 ASP   A OD2  1 
ATOM   3366 H H    A ASP   A 1 157 ? 9.368  -0.074  3.484   0.50 17.83 ?  157 ASP   A H    1 
ATOM   3367 H H    B ASP   A 1 157 ? 9.082  0.209   3.680   0.50 14.54 ?  157 ASP   A H    1 
ATOM   3368 H HA   A ASP   A 1 157 ? 7.210  1.474   3.765   0.50 18.21 ?  157 ASP   A HA   1 
ATOM   3369 H HA   B ASP   A 1 157 ? 6.705  1.183   3.463   0.50 15.42 ?  157 ASP   A HA   1 
ATOM   3370 H HB2  A ASP   A 1 157 ? 8.306  0.972   1.675   0.50 19.50 ?  157 ASP   A HB2  1 
ATOM   3371 H HB2  B ASP   A 1 157 ? 8.140  0.941   1.633   0.50 17.34 ?  157 ASP   A HB2  1 
ATOM   3372 H HB3  A ASP   A 1 157 ? 7.722  -0.494  1.796   0.50 19.50 ?  157 ASP   A HB3  1 
ATOM   3373 H HB3  B ASP   A 1 157 ? 8.011  -0.639  1.736   0.50 17.34 ?  157 ASP   A HB3  1 
ATOM   3374 N N    A LYS   A 1 158 ? 5.533  -0.019  4.857   0.50 15.05 ?  158 LYS   A N    1 
ATOM   3375 N N    B LYS   A 1 158 ? 5.069  -0.411  4.350   0.50 13.00 ?  158 LYS   A N    1 
ATOM   3376 C CA   A LYS   A 1 158 ? 4.594  -0.979  5.436   0.50 15.60 ?  158 LYS   A CA   1 
ATOM   3377 C CA   B LYS   A 1 158 ? 4.127  -1.399  4.870   0.50 13.80 ?  158 LYS   A CA   1 
ATOM   3378 C C    A LYS   A 1 158 ? 3.856  -1.749  4.350   0.50 14.67 ?  158 LYS   A C    1 
ATOM   3379 C C    B LYS   A 1 158 ? 3.512  -2.237  3.752   0.50 12.48 ?  158 LYS   A C    1 
ATOM   3380 O O    A LYS   A 1 158 ? 3.647  -2.962  4.471   0.50 14.32 ?  158 LYS   A O    1 
ATOM   3381 O O    B LYS   A 1 158 ? 3.397  -3.461  3.882   0.50 12.48 ?  158 LYS   A O    1 
ATOM   3382 C CB   A LYS   A 1 158 ? 3.609  -0.279  6.374   0.50 16.80 ?  158 LYS   A CB   1 
ATOM   3383 C CB   B LYS   A 1 158 ? 3.045  -0.688  5.691   0.50 16.29 ?  158 LYS   A CB   1 
ATOM   3384 C CG   A LYS   A 1 158 ? 2.405  -1.136  6.770   0.50 18.30 ?  158 LYS   A CG   1 
ATOM   3385 C CG   B LYS   A 1 158 ? 2.010  -1.608  6.334   0.50 18.40 ?  158 LYS   A CG   1 
ATOM   3386 C CD   A LYS   A 1 158 ? 2.793  -2.436  7.474   0.50 20.01 ?  158 LYS   A CD   1 
ATOM   3387 C CD   B LYS   A 1 158 ? 2.643  -2.596  7.303   0.50 19.90 ?  158 LYS   A CD   1 
ATOM   3388 C CE   A LYS   A 1 158 ? 1.541  -3.219  7.857   0.50 21.35 ?  158 LYS   A CE   1 
ATOM   3389 C CE   B LYS   A 1 158 ? 1.623  -3.119  8.303   0.50 20.73 ?  158 LYS   A CE   1 
ATOM   3390 N NZ   A LYS   A 1 158 ? 1.824  -4.544  8.481   0.50 21.76 ?  158 LYS   A NZ   1 
ATOM   3391 N NZ   B LYS   A 1 158 ? 2.091  -4.337  9.023   0.50 21.33 ?  158 LYS   A NZ   1 
ATOM   3392 H H    A LYS   A 1 158 ? 5.356  0.812   5.013   0.50 18.08 ?  158 LYS   A H    1 
ATOM   3393 H H    B LYS   A 1 158 ? 4.834  0.402   4.467   0.50 15.62 ?  158 LYS   A H    1 
ATOM   3394 H HA   A LYS   A 1 158 ? 5.094  -1.616  5.957   0.50 18.74 ?  158 LYS   A HA   1 
ATOM   3395 H HA   B LYS   A 1 158 ? 4.601  -2.001  5.461   0.50 16.58 ?  158 LYS   A HA   1 
ATOM   3396 H HB2  A LYS   A 1 158 ? 4.076  -0.035  7.188   0.50 20.18 ?  158 LYS   A HB2  1 
ATOM   3397 H HB2  B LYS   A 1 158 ? 3.479  -0.191  6.405   0.50 19.57 ?  158 LYS   A HB2  1 
ATOM   3398 H HB3  A LYS   A 1 158 ? 3.272  0.521   5.939   0.50 20.18 ?  158 LYS   A HB3  1 
ATOM   3399 H HB3  B LYS   A 1 158 ? 2.572  -0.071  5.111   0.50 19.57 ?  158 LYS   A HB3  1 
ATOM   3400 H HG2  A LYS   A 1 158 ? 1.851  -0.626  7.378   0.50 21.98 ?  158 LYS   A HG2  1 
ATOM   3401 H HG2  B LYS   A 1 158 ? 1.371  -1.069  6.828   0.50 22.10 ?  158 LYS   A HG2  1 
ATOM   3402 H HG3  A LYS   A 1 158 ? 1.891  -1.362  5.976   0.50 21.98 ?  158 LYS   A HG3  1 
ATOM   3403 H HG3  B LYS   A 1 158 ? 1.554  -2.112  5.642   0.50 22.10 ?  158 LYS   A HG3  1 
ATOM   3404 H HD2  A LYS   A 1 158 ? 3.330  -2.983  6.879   0.50 24.03 ?  158 LYS   A HD2  1 
ATOM   3405 H HD2  B LYS   A 1 158 ? 3.009  -3.346  6.809   0.50 23.90 ?  158 LYS   A HD2  1 
ATOM   3406 H HD3  A LYS   A 1 158 ? 3.288  -2.228  8.282   0.50 24.03 ?  158 LYS   A HD3  1 
ATOM   3407 H HD3  B LYS   A 1 158 ? 3.343  -2.141  7.791   0.50 23.90 ?  158 LYS   A HD3  1 
ATOM   3408 H HE2  A LYS   A 1 158 ? 1.028  -2.696  8.493   0.50 25.63 ?  158 LYS   A HE2  1 
ATOM   3409 H HE2  B LYS   A 1 158 ? 1.446  -2.431  8.965   0.50 24.89 ?  158 LYS   A HE2  1 
ATOM   3410 H HE3  A LYS   A 1 158 ? 1.013  -3.374  7.058   0.50 25.63 ?  158 LYS   A HE3  1 
ATOM   3411 H HE3  B LYS   A 1 158 ? 0.806  -3.344  7.832   0.50 24.89 ?  158 LYS   A HE3  1 
ATOM   3412 H HZ1  A LYS   A 1 158 ? 1.060  -4.955  8.683   0.50 26.13 ?  158 LYS   A HZ1  1 
ATOM   3413 H HZ1  B LYS   A 1 158 ? 1.530  -4.534  9.684   0.50 25.61 ?  158 LYS   A HZ1  1 
ATOM   3414 H HZ2  A LYS   A 1 158 ? 2.285  -5.055  7.916   0.50 26.13 ?  158 LYS   A HZ2  1 
ATOM   3415 H HZ2  B LYS   A 1 158 ? 2.130  -5.028  8.461   0.50 25.61 ?  158 LYS   A HZ2  1 
ATOM   3416 H HZ3  A LYS   A 1 158 ? 2.299  -4.435  9.225   0.50 26.13 ?  158 LYS   A HZ3  1 
ATOM   3417 H HZ3  B LYS   A 1 158 ? 2.901  -4.198  9.365   0.50 25.61 ?  158 LYS   A HZ3  1 
ATOM   3418 N N    A ASN   A 1 159 ? 3.440  -1.059  3.287   0.50 14.06 ?  159 ASN   A N    1 
ATOM   3419 N N    B ASN   A 1 159 ? 3.093  -1.603  2.654   0.50 12.31 ?  159 ASN   A N    1 
ATOM   3420 C CA   A ASN   A 1 159 ? 2.790  -1.742  2.174   0.50 14.51 ?  159 ASN   A CA   1 
ATOM   3421 C CA   B ASN   A 1 159 ? 2.522  -2.365  1.547   0.50 13.15 ?  159 ASN   A CA   1 
ATOM   3422 C C    A ASN   A 1 159 ? 3.689  -2.829  1.594   0.50 13.96 ?  159 ASN   A C    1 
ATOM   3423 C C    B ASN   A 1 159 ? 3.495  -3.434  1.067   0.50 12.24 ?  159 ASN   A C    1 
ATOM   3424 O O    A ASN   A 1 159 ? 3.247  -3.961  1.375   0.50 13.12 ?  159 ASN   A O    1 
ATOM   3425 O O    B ASN   A 1 159 ? 3.110  -4.590  0.838   0.50 12.35 ?  159 ASN   A O    1 
ATOM   3426 C CB   A ASN   A 1 159 ? 2.389  -0.724  1.103   0.50 15.85 ?  159 ASN   A CB   1 
ATOM   3427 C CB   B ASN   A 1 159 ? 2.132  -1.417  0.408   0.50 15.24 ?  159 ASN   A CB   1 
ATOM   3428 C CG   A ASN   A 1 159 ? 1.093  -0.005  1.440   0.50 17.86 ?  159 ASN   A CG   1 
ATOM   3429 C CG   B ASN   A 1 159 ? 1.528  -2.146  -0.775  0.50 17.67 ?  159 ASN   A CG   1 
ATOM   3430 O OD1  A ASN   A 1 159 ? 0.209  -0.574  2.081   0.50 18.90 ?  159 ASN   A OD1  1 
ATOM   3431 O OD1  B ASN   A 1 159 ? 0.331  -2.432  -0.794  0.50 18.95 ?  159 ASN   A OD1  1 
ATOM   3432 N ND2  A ASN   A 1 159 ? 0.972  1.247   1.002   0.50 18.57 ?  159 ASN   A ND2  1 
ATOM   3433 N ND2  B ASN   A 1 159 ? 2.351  -2.445  -1.773  0.50 18.53 ?  159 ASN   A ND2  1 
ATOM   3434 H H    A ASN   A 1 159 ? 3.508  -0.207  3.190   0.50 16.89 ?  159 ASN   A H    1 
ATOM   3435 H H    B ASN   A 1 159 ? 3.134  -0.749  2.528   0.50 14.79 ?  159 ASN   A H    1 
ATOM   3436 H HA   A ASN   A 1 159 ? 1.974  -2.166  2.490   0.50 17.43 ?  159 ASN   A HA   1 
ATOM   3437 H HA   B ASN   A 1 159 ? 1.716  -2.802  1.850   0.50 15.80 ?  159 ASN   A HA   1 
ATOM   3438 H HB2  A ASN   A 1 159 ? 3.084  -0.052  1.020   0.50 19.04 ?  159 ASN   A HB2  1 
ATOM   3439 H HB2  B ASN   A 1 159 ? 1.473  -0.775  0.733   0.50 18.31 ?  159 ASN   A HB2  1 
ATOM   3440 H HB3  A ASN   A 1 159 ? 2.267  -1.179  0.252   0.50 19.04 ?  159 ASN   A HB3  1 
ATOM   3441 H HB3  B ASN   A 1 159 ? 2.920  -0.941  0.097   0.50 18.31 ?  159 ASN   A HB3  1 
ATOM   3442 H HD21 A ASN   A 1 159 ? 0.250  1.695   1.159   0.50 22.31 ?  159 ASN   A HD21 1 
ATOM   3443 H HD21 B ASN   A 1 159 ? 2.054  -2.858  -2.469  0.50 22.26 ?  159 ASN   A HD21 1 
ATOM   3444 H HD22 A ASN   A 1 159 ? 1.610  1.616   0.557   0.50 22.31 ?  159 ASN   A HD22 1 
ATOM   3445 H HD22 B ASN   A 1 159 ? 3.181  -2.231  -1.724  0.50 22.26 ?  159 ASN   A HD22 1 
ATOM   3446 N N    A LEU   A 1 160 ? 4.961  -2.509  1.345   0.50 13.56 ?  160 LEU   A N    1 
ATOM   3447 N N    B LEU   A 1 160 ? 4.771  -3.068  0.940   0.50 12.13 ?  160 LEU   A N    1 
ATOM   3448 C CA   A LEU   A 1 160 ? 5.848  -3.499  0.736   0.50 13.79 ?  160 LEU   A CA   1 
ATOM   3449 C CA   B LEU   A 1 160 ? 5.785  -4.029  0.533   0.50 12.62 ?  160 LEU   A CA   1 
ATOM   3450 C C    A LEU   A 1 160 ? 6.045  -4.701  1.648   0.50 13.52 ?  160 LEU   A C    1 
ATOM   3451 C C    B LEU   A 1 160 ? 6.042  -5.062  1.628   0.50 12.35 ?  160 LEU   A C    1 
ATOM   3452 O O    A LEU   A 1 160 ? 6.080  -5.846  1.182   0.50 13.52 ?  160 LEU   A O    1 
ATOM   3453 O O    B LEU   A 1 160 ? 6.100  -6.265  1.351   0.50 12.12 ?  160 LEU   A O    1 
ATOM   3454 C CB   A LEU   A 1 160 ? 7.196  -2.874  0.371   0.50 14.12 ?  160 LEU   A CB   1 
ATOM   3455 C CB   B LEU   A 1 160 ? 7.071  -3.291  0.178   0.50 13.26 ?  160 LEU   A CB   1 
ATOM   3456 C CG   A LEU   A 1 160 ? 8.259  -3.890  -0.070  0.50 14.52 ?  160 LEU   A CG   1 
ATOM   3457 C CG   B LEU   A 1 160 ? 8.223  -4.202  -0.214  0.50 14.04 ?  160 LEU   A CG   1 
ATOM   3458 C CD1  A LEU   A 1 160 ? 7.820  -4.662  -1.309  0.50 15.06 ?  160 LEU   A CD1  1 
ATOM   3459 C CD1  B LEU   A 1 160 ? 7.813  -5.050  -1.397  0.50 14.57 ?  160 LEU   A CD1  1 
ATOM   3460 C CD2  A LEU   A 1 160 ? 9.606  -3.228  -0.310  0.50 14.51 ?  160 LEU   A CD2  1 
ATOM   3461 C CD2  B LEU   A 1 160 ? 9.443  -3.370  -0.524  0.50 14.59 ?  160 LEU   A CD2  1 
ATOM   3462 H H    A LEU   A 1 160 ? 5.319  -1.745  1.519   0.50 16.29 ?  160 LEU   A H    1 
ATOM   3463 H H    B LEU   A 1 160 ? 5.069  -2.272  1.075   0.50 14.58 ?  160 LEU   A H    1 
ATOM   3464 H HA   A LEU   A 1 160 ? 5.438  -3.814  -0.077  0.50 16.56 ?  160 LEU   A HA   1 
ATOM   3465 H HA   B LEU   A 1 160 ? 5.469  -4.492  -0.264  0.50 15.17 ?  160 LEU   A HA   1 
ATOM   3466 H HB2  A LEU   A 1 160 ? 7.064  -2.235  -0.354  0.50 16.96 ?  160 LEU   A HB2  1 
ATOM   3467 H HB2  B LEU   A 1 160 ? 6.895  -2.700  -0.574  0.50 15.93 ?  160 LEU   A HB2  1 
ATOM   3468 H HB3  A LEU   A 1 160 ? 7.545  -2.422  1.149   0.50 16.96 ?  160 LEU   A HB3  1 
ATOM   3469 H HB3  B LEU   A 1 160 ? 7.351  -2.771  0.944   0.50 15.93 ?  160 LEU   A HB3  1 
ATOM   3470 H HG   A LEU   A 1 160 ? 8.389  -4.533  0.640   0.50 17.45 ?  160 LEU   A HG   1 
ATOM   3471 H HG   B LEU   A 1 160 ? 8.439  -4.790  0.526   0.50 16.87 ?  160 LEU   A HG   1 
ATOM   3472 H HD11 A LEU   A 1 160 ? 8.547  -5.240  -1.592  0.50 18.09 ?  160 LEU   A HD11 1 
ATOM   3473 H HD11 B LEU   A 1 160 ? 8.582  -5.540  -1.706  0.50 17.51 ?  160 LEU   A HD11 1 
ATOM   3474 H HD12 A LEU   A 1 160 ? 7.041  -5.199  -1.088  0.50 18.09 ?  160 LEU   A HD12 1 
ATOM   3475 H HD12 B LEU   A 1 160 ? 7.118  -5.668  -1.119  0.50 17.51 ?  160 LEU   A HD12 1 
ATOM   3476 H HD13 A LEU   A 1 160 ? 7.602  -4.035  -2.014  0.50 18.09 ?  160 LEU   A HD13 1 
ATOM   3477 H HD13 B LEU   A 1 160 ? 7.477  -4.467  -2.098  0.50 17.51 ?  160 LEU   A HD13 1 
ATOM   3478 H HD21 A LEU   A 1 160 ? 10.245 -3.908  -0.583  0.50 17.43 ?  160 LEU   A HD21 1 
ATOM   3479 H HD21 B LEU   A 1 160 ? 10.154 -3.948  -0.839  0.50 17.53 ?  160 LEU   A HD21 1 
ATOM   3480 H HD22 A LEU   A 1 160 ? 9.513  -2.564  -1.010  0.50 17.43 ?  160 LEU   A HD22 1 
ATOM   3481 H HD22 B LEU   A 1 160 ? 9.218  -2.718  -1.210  0.50 17.53 ?  160 LEU   A HD22 1 
ATOM   3482 H HD23 A LEU   A 1 160 ? 9.902  -2.808  0.511   0.50 17.43 ?  160 LEU   A HD23 1 
ATOM   3483 H HD23 B LEU   A 1 160 ? 9.722  -2.912  0.286   0.50 17.53 ?  160 LEU   A HD23 1 
ATOM   3484 N N    A TYR   A 1 161 ? 6.181  -4.463  2.950   0.50 13.34 ?  161 TYR   A N    1 
ATOM   3485 N N    B TYR   A 1 161 ? 6.223  -4.611  2.875   0.50 12.31 ?  161 TYR   A N    1 
ATOM   3486 C CA   A TYR   A 1 161 ? 6.352  -5.561  3.891   0.50 13.03 ?  161 TYR   A CA   1 
ATOM   3487 C CA   B TYR   A 1 161 ? 6.375  -5.553  3.984   0.50 12.02 ?  161 TYR   A CA   1 
ATOM   3488 C C    A TYR   A 1 161 ? 5.228  -6.586  3.763   0.50 12.88 ?  161 TYR   A C    1 
ATOM   3489 C C    B TYR   A 1 161 ? 5.248  -6.577  3.980   0.50 12.36 ?  161 TYR   A C    1 
ATOM   3490 O O    A TYR   A 1 161 ? 5.480  -7.793  3.687   0.50 12.10 ?  161 TYR   A O    1 
ATOM   3491 O O    B TYR   A 1 161 ? 5.489  -7.786  4.062   0.50 11.69 ?  161 TYR   A O    1 
ATOM   3492 C CB   A TYR   A 1 161 ? 6.420  -4.995  5.304   0.50 13.01 ?  161 TYR   A CB   1 
ATOM   3493 C CB   B TYR   A 1 161 ? 6.440  -4.832  5.341   0.50 11.73 ?  161 TYR   A CB   1 
ATOM   3494 C CG   A TYR   A 1 161 ? 6.354  -6.047  6.369   0.50 12.31 ?  161 TYR   A CG   1 
ATOM   3495 C CG   B TYR   A 1 161 ? 6.369  -5.797  6.526   0.50 11.03 ?  161 TYR   A CG   1 
ATOM   3496 C CD1  A TYR   A 1 161 ? 7.496  -6.723  6.765   0.50 11.75 ?  161 TYR   A CD1  1 
ATOM   3497 C CD1  B TYR   A 1 161 ? 7.511  -6.444  7.003   0.50 10.17 ?  161 TYR   A CD1  1 
ATOM   3498 C CD2  A TYR   A 1 161 ? 5.151  -6.371  6.978   0.50 12.10 ?  161 TYR   A CD2  1 
ATOM   3499 C CD2  B TYR   A 1 161 ? 5.160  -6.078  7.152   0.50 11.50 ?  161 TYR   A CD2  1 
ATOM   3500 C CE1  A TYR   A 1 161 ? 7.444  -7.693  7.735   0.50 10.83 ?  161 TYR   A CE1  1 
ATOM   3501 C CE1  B TYR   A 1 161 ? 7.442  -7.348  8.070   0.50 10.72 ?  161 TYR   A CE1  1 
ATOM   3502 C CE2  A TYR   A 1 161 ? 5.087  -7.342  7.951   0.50 11.24 ?  161 TYR   A CE2  1 
ATOM   3503 C CE2  B TYR   A 1 161 ? 5.084  -6.975  8.217   0.50 11.65 ?  161 TYR   A CE2  1 
ATOM   3504 C CZ   A TYR   A 1 161 ? 6.238  -8.000  8.330   0.50 10.22 ?  161 TYR   A CZ   1 
ATOM   3505 C CZ   B TYR   A 1 161 ? 6.222  -7.604  8.670   0.50 11.65 ?  161 TYR   A CZ   1 
ATOM   3506 O OH   A TYR   A 1 161 ? 6.192  -8.971  9.303   0.50 9.94  ?  161 TYR   A OH   1 
ATOM   3507 O OH   B TYR   A 1 161 ? 6.132  -8.487  9.727   0.50 13.08 ?  161 TYR   A OH   1 
ATOM   3508 H H    A TYR   A 1 161 ? 6.175  -3.685  3.316   0.50 16.03 ?  161 TYR   A H    1 
ATOM   3509 H H    B TYR   A 1 161 ? 6.264  -3.784  3.089   0.50 14.80 ?  161 TYR   A H    1 
ATOM   3510 H HA   A TYR   A 1 161 ? 7.186  -6.017  3.706   0.50 15.65 ?  161 TYR   A HA   1 
ATOM   3511 H HA   B TYR   A 1 161 ? 7.204  -6.034  3.870   0.50 14.44 ?  161 TYR   A HA   1 
ATOM   3512 H HB2  A TYR   A 1 161 ? 7.260  -4.521  5.406   0.50 15.63 ?  161 TYR   A HB2  1 
ATOM   3513 H HB2  B TYR   A 1 161 ? 7.276  -4.345  5.401   0.50 14.10 ?  161 TYR   A HB2  1 
ATOM   3514 H HB3  A TYR   A 1 161 ? 5.677  -4.390  5.436   0.50 15.63 ?  161 TYR   A HB3  1 
ATOM   3515 H HB3  B TYR   A 1 161 ? 5.692  -4.217  5.413   0.50 14.10 ?  161 TYR   A HB3  1 
ATOM   3516 H HD1  A TYR   A 1 161 ? 8.309  -6.522  6.359   0.50 14.12 ?  161 TYR   A HD1  1 
ATOM   3517 H HD1  B TYR   A 1 161 ? 8.334  -6.276  6.601   0.50 12.22 ?  161 TYR   A HD1  1 
ATOM   3518 H HD2  A TYR   A 1 161 ? 4.373  -5.926  6.721   0.50 14.54 ?  161 TYR   A HD2  1 
ATOM   3519 H HD2  B TYR   A 1 161 ? 4.382  -5.671  6.856   0.50 13.82 ?  161 TYR   A HD2  1 
ATOM   3520 H HE1  A TYR   A 1 161 ? 8.219  -8.141  7.986   0.50 13.02 ?  161 TYR   A HE1  1 
ATOM   3521 H HE1  B TYR   A 1 161 ? 8.218  -7.766  8.382   0.50 12.89 ?  161 TYR   A HE1  1 
ATOM   3522 H HE2  A TYR   A 1 161 ? 4.272  -7.546  8.351   0.50 13.51 ?  161 TYR   A HE2  1 
ATOM   3523 H HE2  B TYR   A 1 161 ? 4.266  -7.154  8.629   0.50 14.00 ?  161 TYR   A HE2  1 
ATOM   3524 H HH   A TYR   A 1 161 ? 5.401  -9.056  9.576   0.50 11.95 ?  161 TYR   A HH   1 
ATOM   3525 H HH   B TYR   A 1 161 ? 5.334  -8.544  9.997   0.50 15.71 ?  161 TYR   A HH   1 
ATOM   3526 N N    A ASP   A 1 162 ? 3.976  -6.119  3.737   0.50 13.53 ?  162 ASP   A N    1 
ATOM   3527 N N    B ASP   A 1 162 ? 4.002  -6.108  3.881   0.50 13.24 ?  162 ASP   A N    1 
ATOM   3528 C CA   A ASP   A 1 162 ? 2.838  -7.034  3.658   0.50 14.29 ?  162 ASP   A CA   1 
ATOM   3529 C CA   B ASP   A 1 162 ? 2.871  -7.033  3.862   0.50 14.21 ?  162 ASP   A CA   1 
ATOM   3530 C C    A ASP   A 1 162 ? 2.913  -7.896  2.402   0.50 14.63 ?  162 ASP   A C    1 
ATOM   3531 C C    B ASP   A 1 162 ? 2.881  -7.901  2.608   0.50 14.49 ?  162 ASP   A C    1 
ATOM   3532 O O    A ASP   A 1 162 ? 2.586  -9.089  2.437   0.50 15.20 ?  162 ASP   A O    1 
ATOM   3533 O O    B ASP   A 1 162 ? 2.542  -9.089  2.668   0.50 14.91 ?  162 ASP   A O    1 
ATOM   3534 C CB   A ASP   A 1 162 ? 1.520  -6.247  3.678   0.50 15.38 ?  162 ASP   A CB   1 
ATOM   3535 C CB   B ASP   A 1 162 ? 1.550  -6.269  3.994   0.50 14.90 ?  162 ASP   A CB   1 
ATOM   3536 C CG   A ASP   A 1 162 ? 1.152  -5.705  5.055   0.50 16.58 ?  162 ASP   A CG   1 
ATOM   3537 C CG   B ASP   A 1 162 ? 1.353  -5.664  5.385   0.50 16.12 ?  162 ASP   A CG   1 
ATOM   3538 O OD1  A ASP   A 1 162 ? 1.848  -6.002  6.045   0.50 17.50 ?  162 ASP   A OD1  1 
ATOM   3539 O OD1  B ASP   A 1 162 ? 1.954  -6.173  6.356   0.50 16.88 ?  162 ASP   A OD1  1 
ATOM   3540 O OD2  A ASP   A 1 162 ? 0.133  -4.979  5.141   0.50 17.03 -1 162 ASP   A OD2  1 
ATOM   3541 O OD2  B ASP   A 1 162 ? 0.594  -4.676  5.509   0.50 17.23 -1 162 ASP   A OD2  1 
ATOM   3542 H H    A ASP   A 1 162 ? 3.759  -5.296  3.759   0.50 16.25 ?  162 ASP   A H    1 
ATOM   3543 H H    B ASP   A 1 162 ? 3.785  -5.278  3.835   0.50 15.91 ?  162 ASP   A H    1 
ATOM   3544 H HA   A ASP   A 1 162 ? 2.843  -7.634  4.421   0.50 17.16 ?  162 ASP   A HA   1 
ATOM   3545 H HA   B ASP   A 1 162 ? 2.941  -7.627  4.626   0.50 17.07 ?  162 ASP   A HA   1 
ATOM   3546 H HB2  A ASP   A 1 162 ? 1.593  -5.499  3.072   0.50 18.47 ?  162 ASP   A HB2  1 
ATOM   3547 H HB2  B ASP   A 1 162 ? 1.538  -5.543  3.353   0.50 17.90 ?  162 ASP   A HB2  1 
ATOM   3548 H HB3  A ASP   A 1 162 ? 0.796  -6.831  3.412   0.50 18.47 ?  162 ASP   A HB3  1 
ATOM   3549 H HB3  B ASP   A 1 162 ? 0.813  -6.882  3.808   0.50 17.90 ?  162 ASP   A HB3  1 
ATOM   3550 N N    A LYS   A 1 163 ? 3.329  -7.307  1.278   0.50 15.89 ?  163 LYS   A N    1 
ATOM   3551 N N    B LYS   A 1 163 ? 3.263  -7.330  1.462   0.50 15.77 ?  163 LYS   A N    1 
ATOM   3552 C CA   A LYS   A 1 163 ? 3.427  -8.066  0.035   0.50 16.50 ?  163 LYS   A CA   1 
ATOM   3553 C CA   B LYS   A 1 163 ? 3.345  -8.117  0.234   0.50 16.67 ?  163 LYS   A CA   1 
ATOM   3554 C C    A LYS   A 1 163 ? 4.510  -9.138  0.117   0.50 15.46 ?  163 LYS   A C    1 
ATOM   3555 C C    B LYS   A 1 163 ? 4.481  -9.132  0.305   0.50 15.60 ?  163 LYS   A C    1 
ATOM   3556 O O    A LYS   A 1 163 ? 4.344  -10.234 -0.430  0.50 16.12 ?  163 LYS   A O    1 
ATOM   3557 O O    B LYS   A 1 163 ? 4.335  -10.268 -0.159  0.50 16.50 ?  163 LYS   A O    1 
ATOM   3558 C CB   A LYS   A 1 163 ? 3.704  -7.119  -1.131  0.50 19.10 ?  163 LYS   A CB   1 
ATOM   3559 C CB   B LYS   A 1 163 ? 3.514  -7.186  -0.968  0.50 19.19 ?  163 LYS   A CB   1 
ATOM   3560 C CG   A LYS   A 1 163 ? 3.704  -7.793  -2.492  0.50 22.31 ?  163 LYS   A CG   1 
ATOM   3561 C CG   B LYS   A 1 163 ? 3.697  -7.879  -2.312  0.50 22.16 ?  163 LYS   A CG   1 
ATOM   3562 C CD   A LYS   A 1 163 ? 4.106  -6.821  -3.587  0.50 25.04 ?  163 LYS   A CD   1 
ATOM   3563 C CD   B LYS   A 1 163 ? 3.649  -6.854  -3.440  0.50 24.80 ?  163 LYS   A CD   1 
ATOM   3564 C CE   A LYS   A 1 163 ? 4.002  -7.464  -4.959  0.50 27.22 ?  163 LYS   A CE   1 
ATOM   3565 C CE   B LYS   A 1 163 ? 3.874  -7.483  -4.804  0.50 26.84 ?  163 LYS   A CE   1 
ATOM   3566 N NZ   A LYS   A 1 163 ? 4.625  -6.628  -6.022  0.50 28.14 ?  163 LYS   A NZ   1 
ATOM   3567 N NZ   B LYS   A 1 163 ? 5.052  -6.882  -5.496  0.50 27.68 ?  163 LYS   A NZ   1 
ATOM   3568 H H    A LYS   A 1 163 ? 3.546  -6.478  1.211   0.50 19.09 ?  163 LYS   A H    1 
ATOM   3569 H H    B LYS   A 1 163 ? 3.480  -6.503  1.370   0.50 18.94 ?  163 LYS   A H    1 
ATOM   3570 H HA   A LYS   A 1 163 ? 2.578  -8.505  -0.135  0.50 19.81 ?  163 LYS   A HA   1 
ATOM   3571 H HA   B LYS   A 1 163 ? 2.516  -8.606  0.115   0.50 20.03 ?  163 LYS   A HA   1 
ATOM   3572 H HB2  A LYS   A 1 163 ? 3.020  -6.430  -1.145  0.50 22.94 ?  163 LYS   A HB2  1 
ATOM   3573 H HB2  B LYS   A 1 163 ? 2.722  -6.627  -1.041  0.50 23.05 ?  163 LYS   A HB2  1 
ATOM   3574 H HB3  A LYS   A 1 163 ? 4.575  -6.714  -1.005  0.50 22.94 ?  163 LYS   A HB3  1 
ATOM   3575 H HB3  B LYS   A 1 163 ? 4.291  -6.628  -0.823  0.50 23.05 ?  163 LYS   A HB3  1 
ATOM   3576 H HG2  A LYS   A 1 163 ? 4.338  -8.526  -2.490  0.50 26.79 ?  163 LYS   A HG2  1 
ATOM   3577 H HG2  B LYS   A 1 163 ? 4.562  -8.319  -2.338  0.50 26.61 ?  163 LYS   A HG2  1 
ATOM   3578 H HG3  A LYS   A 1 163 ? 2.811  -8.121  -2.687  0.50 26.79 ?  163 LYS   A HG3  1 
ATOM   3579 H HG3  B LYS   A 1 163 ? 2.984  -8.522  -2.451  0.50 26.61 ?  163 LYS   A HG3  1 
ATOM   3580 H HD2  A LYS   A 1 163 ? 3.514  -6.051  -3.566  0.50 30.07 ?  163 LYS   A HD2  1 
ATOM   3581 H HD2  B LYS   A 1 163 ? 2.777  -6.429  -3.448  0.50 29.78 ?  163 LYS   A HD2  1 
ATOM   3582 H HD3  A LYS   A 1 163 ? 5.024  -6.542  -3.447  0.50 30.07 ?  163 LYS   A HD3  1 
ATOM   3583 H HD3  B LYS   A 1 163 ? 4.342  -6.189  -3.298  0.50 29.78 ?  163 LYS   A HD3  1 
ATOM   3584 H HE2  A LYS   A 1 163 ? 4.448  -8.325  -4.942  0.50 32.69 ?  163 LYS   A HE2  1 
ATOM   3585 H HE2  B LYS   A 1 163 ? 4.023  -8.436  -4.701  0.50 32.23 ?  163 LYS   A HE2  1 
ATOM   3586 H HE3  A LYS   A 1 163 ? 3.066  -7.582  -5.181  0.50 32.69 ?  163 LYS   A HE3  1 
ATOM   3587 H HE3  B LYS   A 1 163 ? 3.094  -7.329  -5.357  0.50 32.23 ?  163 LYS   A HE3  1 
ATOM   3588 H HZ1  A LYS   A 1 163 ? 4.548  -7.033  -6.811  0.50 33.79 ?  163 LYS   A HZ1  1 
ATOM   3589 H HZ1  B LYS   A 1 163 ? 5.211  -7.312  -6.258  0.50 33.24 ?  163 LYS   A HZ1  1 
ATOM   3590 H HZ2  A LYS   A 1 163 ? 4.219  -5.837  -6.062  0.50 33.79 ?  163 LYS   A HZ2  1 
ATOM   3591 H HZ2  B LYS   A 1 163 ? 4.893  -6.024  -5.676  0.50 33.24 ?  163 LYS   A HZ2  1 
ATOM   3592 H HZ3  A LYS   A 1 163 ? 5.488  -6.502  -5.844  0.50 33.79 ?  163 LYS   A HZ3  1 
ATOM   3593 H HZ3  B LYS   A 1 163 ? 5.773  -6.938  -4.977  0.50 33.24 ?  163 LYS   A HZ3  1 
ATOM   3594 N N    A LEU   A 1 164 ? 5.634  -8.833  0.773   0.50 13.88 ?  164 LEU   A N    1 
ATOM   3595 N N    B LEU   A 1 164 ? 5.619  -8.738  0.885   0.50 13.59 ?  164 LEU   A N    1 
ATOM   3596 C CA   A LEU   A 1 164 ? 6.718  -9.806  0.896   0.50 13.15 ?  164 LEU   A CA   1 
ATOM   3597 C CA   B LEU   A 1 164 ? 6.732  -9.670  1.050   0.50 12.66 ?  164 LEU   A CA   1 
ATOM   3598 C C    A LEU   A 1 164 ? 6.295  -10.984 1.761   0.50 12.97 ?  164 LEU   A C    1 
ATOM   3599 C C    B LEU   A 1 164 ? 6.322  -10.864 1.899   0.50 12.55 ?  164 LEU   A C    1 
ATOM   3600 O O    A LEU   A 1 164 ? 6.556  -12.143 1.421   0.50 13.53 ?  164 LEU   A O    1 
ATOM   3601 O O    B LEU   A 1 164 ? 6.678  -12.007 1.592   0.50 12.91 ?  164 LEU   A O    1 
ATOM   3602 C CB   A LEU   A 1 164 ? 7.950  -9.135  1.499   0.50 12.58 ?  164 LEU   A CB   1 
ATOM   3603 C CB   B LEU   A 1 164 ? 7.915  -8.951  1.697   0.50 11.50 ?  164 LEU   A CB   1 
ATOM   3604 C CG   A LEU   A 1 164 ? 8.671  -8.119  0.614   0.50 12.78 ?  164 LEU   A CG   1 
ATOM   3605 C CG   B LEU   A 1 164 ? 8.684  -7.985  0.796   0.50 11.94 ?  164 LEU   A CG   1 
ATOM   3606 C CD1  A LEU   A 1 164 ? 9.584  -7.244  1.456   0.50 12.62 ?  164 LEU   A CD1  1 
ATOM   3607 C CD1  B LEU   A 1 164 ? 9.559  -7.076  1.639   0.50 12.05 ?  164 LEU   A CD1  1 
ATOM   3608 C CD2  A LEU   A 1 164 ? 9.465  -8.826  -0.474  0.50 12.95 ?  164 LEU   A CD2  1 
ATOM   3609 C CD2  B LEU   A 1 164 ? 9.523  -8.738  -0.233  0.50 12.24 ?  164 LEU   A CD2  1 
ATOM   3610 H H    A LEU   A 1 164 ? 5.792  -8.079  1.150   0.50 16.68 ?  164 LEU   A H    1 
ATOM   3611 H H    B LEU   A 1 164 ? 5.765  -7.947  1.185   0.50 16.32 ?  164 LEU   A H    1 
ATOM   3612 H HA   A LEU   A 1 164 ? 6.948  -10.148 0.019   0.50 15.80 ?  164 LEU   A HA   1 
ATOM   3613 H HA   B LEU   A 1 164 ? 7.010  -9.995  0.180   0.50 15.21 ?  164 LEU   A HA   1 
ATOM   3614 H HB2  A LEU   A 1 164 ? 7.679  -8.673  2.305   0.50 15.12 ?  164 LEU   A HB2  1 
ATOM   3615 H HB2  B LEU   A 1 164 ? 7.583  -8.436  2.451   0.50 13.82 ?  164 LEU   A HB2  1 
ATOM   3616 H HB3  A LEU   A 1 164 ? 8.593  -9.825  1.722   0.50 15.12 ?  164 LEU   A HB3  1 
ATOM   3617 H HB3  B LEU   A 1 164 ? 8.542  -9.616  2.010   0.50 13.82 ?  164 LEU   A HB3  1 
ATOM   3618 H HG   A LEU   A 1 164 ? 8.014  -7.546  0.188   0.50 15.35 ?  164 LEU   A HG   1 
ATOM   3619 H HG   B LEU   A 1 164 ? 8.051  -7.429  0.315   0.50 14.35 ?  164 LEU   A HG   1 
ATOM   3620 H HD11 A LEU   A 1 164 ? 10.039 -6.614  0.877   0.50 15.17 ?  164 LEU   A HD11 1 
ATOM   3621 H HD11 B LEU   A 1 164 ? 10.050 -6.480  1.055   0.50 14.48 ?  164 LEU   A HD11 1 
ATOM   3622 H HD12 A LEU   A 1 164 ? 9.050  -6.766  2.111   0.50 15.17 ?  164 LEU   A HD12 1 
ATOM   3623 H HD12 B LEU   A 1 164 ? 8.992  -6.561  2.237   0.50 14.48 ?  164 LEU   A HD12 1 
ATOM   3624 H HD13 A LEU   A 1 164 ? 10.233 -7.808  1.907   0.50 15.17 ?  164 LEU   A HD13 1 
ATOM   3625 H HD13 B LEU   A 1 164 ? 10.174 -7.620  2.155   0.50 14.48 ?  164 LEU   A HD13 1 
ATOM   3626 H HD21 A LEU   A 1 164 ? 9.927  -8.162  -1.009  0.50 15.56 ?  164 LEU   A HD21 1 
ATOM   3627 H HD21 B LEU   A 1 164 ? 10.033 -8.097  -0.755  0.50 14.71 ?  164 LEU   A HD21 1 
ATOM   3628 H HD22 A LEU   A 1 164 ? 10.109 -9.421  -0.058  0.50 15.56 ?  164 LEU   A HD22 1 
ATOM   3629 H HD22 B LEU   A 1 164 ? 10.126 -9.340  0.230   0.50 14.71 ?  164 LEU   A HD22 1 
ATOM   3630 H HD23 A LEU   A 1 164 ? 8.856  -9.335  -1.031  0.50 15.56 ?  164 LEU   A HD23 1 
ATOM   3631 H HD23 B LEU   A 1 164 ? 8.934  -9.243  -0.815  0.50 14.71 ?  164 LEU   A HD23 1 
ATOM   3632 N N    A VAL   A 1 165 ? 5.660  -10.698 2.898   0.50 12.65 ?  165 VAL   A N    1 
ATOM   3633 N N    B VAL   A 1 165 ? 5.589  -10.612 2.984   0.50 12.33 ?  165 VAL   A N    1 
ATOM   3634 C CA   A VAL   A 1 165 ? 5.174  -11.761 3.769   0.50 12.71 ?  165 VAL   A CA   1 
ATOM   3635 C CA   B VAL   A 1 165 ? 5.123  -11.695 3.842   0.50 12.80 ?  165 VAL   A CA   1 
ATOM   3636 C C    A VAL   A 1 165 ? 4.132  -12.595 3.040   0.50 12.82 ?  165 VAL   A C    1 
ATOM   3637 C C    B VAL   A 1 165 ? 4.113  -12.566 3.104   0.50 12.98 ?  165 VAL   A C    1 
ATOM   3638 O O    A VAL   A 1 165 ? 4.244  -13.824 2.954   0.50 13.23 ?  165 VAL   A O    1 
ATOM   3639 O O    B VAL   A 1 165 ? 4.224  -13.797 3.088   0.50 13.27 ?  165 VAL   A O    1 
ATOM   3640 C CB   A VAL   A 1 165 ? 4.620  -11.164 5.076   0.50 12.88 ?  165 VAL   A CB   1 
ATOM   3641 C CB   B VAL   A 1 165 ? 4.536  -11.113 5.140   0.50 13.26 ?  165 VAL   A CB   1 
ATOM   3642 C CG1  A VAL   A 1 165 ? 3.870  -12.222 5.880   0.50 13.04 ?  165 VAL   A CG1  1 
ATOM   3643 C CG1  B VAL   A 1 165 ? 3.828  -12.196 5.942   0.50 13.57 ?  165 VAL   A CG1  1 
ATOM   3644 C CG2  A VAL   A 1 165 ? 5.746  -10.546 5.895   0.50 13.32 ?  165 VAL   A CG2  1 
ATOM   3645 C CG2  B VAL   A 1 165 ? 5.628  -10.442 5.963   0.50 13.50 ?  165 VAL   A CG2  1 
ATOM   3646 H H    A VAL   A 1 165 ? 5.492  -9.907  3.181   0.50 15.21 ?  165 VAL   A H    1 
ATOM   3647 H H    B VAL   A 1 165 ? 5.361  -9.824  3.246   0.50 14.82 ?  165 VAL   A H    1 
ATOM   3648 H HA   A VAL   A 1 165 ? 5.909  -12.348 4.003   0.50 15.28 ?  165 VAL   A HA   1 
ATOM   3649 H HA   B VAL   A 1 165 ? 5.879  -12.251 4.082   0.50 15.38 ?  165 VAL   A HA   1 
ATOM   3650 H HB   A VAL   A 1 165 ? 3.992  -10.458 4.860   0.50 15.47 ?  165 VAL   A HB   1 
ATOM   3651 H HB   B VAL   A 1 165 ? 3.880  -10.435 4.912   0.50 15.93 ?  165 VAL   A HB   1 
ATOM   3652 H HG11 A VAL   A 1 165 ? 3.768  -11.909 6.794   0.50 15.66 ?  165 VAL   A HG11 1 
ATOM   3653 H HG11 B VAL   A 1 165 ? 3.706  -11.880 6.850   0.50 16.30 ?  165 VAL   A HG11 1 
ATOM   3654 H HG12 A VAL   A 1 165 ? 2.993  -12.357 5.483   0.50 15.66 ?  165 VAL   A HG12 1 
ATOM   3655 H HG12 B VAL   A 1 165 ? 2.964  -12.373 5.536   0.50 16.30 ?  165 VAL   A HG12 1 
ATOM   3656 H HG13 A VAL   A 1 165 ? 4.374  -13.046 5.866   0.50 15.66 ?  165 VAL   A HG13 1 
ATOM   3657 H HG13 B VAL   A 1 165 ? 4.371  -12.995 5.937   0.50 16.30 ?  165 VAL   A HG13 1 
ATOM   3658 H HG21 A VAL   A 1 165 ? 5.381  -10.194 6.722   0.50 16.00 ?  165 VAL   A HG21 1 
ATOM   3659 H HG21 B VAL   A 1 165 ? 5.233  -10.057 6.760   0.50 16.22 ?  165 VAL   A HG21 1 
ATOM   3660 H HG22 A VAL   A 1 165 ? 6.407  -11.228 6.088   0.50 16.00 ?  165 VAL   A HG22 1 
ATOM   3661 H HG22 B VAL   A 1 165 ? 6.291  -11.106 6.208   0.50 16.22 ?  165 VAL   A HG22 1 
ATOM   3662 H HG23 A VAL   A 1 165 ? 6.150  -9.829  5.381   0.50 16.00 ?  165 VAL   A HG23 1 
ATOM   3663 H HG23 B VAL   A 1 165 ? 6.042  -9.744  5.430   0.50 16.22 ?  165 VAL   A HG23 1 
ATOM   3664 N N    . SER   A 1 166 ? 3.116  -11.935 2.478   1.00 13.52 ?  166 SER   A N    1 
ATOM   3665 C CA   . SER   A 1 166 ? 2.000  -12.675 1.898   1.00 14.51 ?  166 SER   A CA   1 
ATOM   3666 C C    . SER   A 1 166 ? 2.417  -13.518 0.701   1.00 15.53 ?  166 SER   A C    1 
ATOM   3667 O O    . SER   A 1 166 ? 1.768  -14.531 0.407   1.00 18.01 ?  166 SER   A O    1 
ATOM   3668 C CB   . SER   A 1 166 ? 0.873  -11.717 1.494   1.00 16.17 ?  166 SER   A CB   1 
ATOM   3669 O OG   . SER   A 1 166 ? 0.263  -11.092 2.618   1.00 18.70 ?  166 SER   A OG   1 
ATOM   3670 H H    A SER   A 1 166 ? 3.050  -11.082 2.423   0.50 16.24 ?  166 SER   A H    1 
ATOM   3671 H H    B SER   A 1 166 ? 3.056  -11.085 2.388   0.50 16.24 ?  166 SER   A H    1 
ATOM   3672 H HA   . SER   A 1 166 ? 1.639  -13.282 2.565   1.00 17.43 ?  166 SER   A HA   1 
ATOM   3673 H HB2  . SER   A 1 166 ? 1.229  -11.031 0.916   1.00 19.42 ?  166 SER   A HB2  1 
ATOM   3674 H HB3  . SER   A 1 166 ? 0.182  -12.218 1.023   1.00 19.42 ?  166 SER   A HB3  1 
ATOM   3675 H HG   . SER   A 1 166 ? 0.850  -10.652 3.043   1.00 22.46 ?  166 SER   A HG   1 
ATOM   3676 N N    . SER   A 1 167 ? 3.474  -13.122 -0.005  1.00 14.89 ?  167 SER   A N    1 
ATOM   3677 C CA   . SER   A 1 167 ? 3.912  -13.839 -1.192  1.00 16.19 ?  167 SER   A CA   1 
ATOM   3678 C C    . SER   A 1 167 ? 5.089  -14.765 -0.921  1.00 16.05 ?  167 SER   A C    1 
ATOM   3679 O O    . SER   A 1 167 ? 5.601  -15.382 -1.860  1.00 17.15 ?  167 SER   A O    1 
ATOM   3680 C CB   . SER   A 1 167 ? 4.282  -12.848 -2.308  1.00 17.30 ?  167 SER   A CB   1 
ATOM   3681 O OG   . SER   A 1 167 ? 5.398  -12.045 -1.942  1.00 17.97 ?  167 SER   A OG   1 
ATOM   3682 H H    . SER   A 1 167 ? 3.954  -12.434 0.190   1.00 17.89 ?  167 SER   A H    1 
ATOM   3683 H HA   . SER   A 1 167 ? 3.170  -14.378 -1.513  1.00 19.45 ?  167 SER   A HA   1 
ATOM   3684 H HB2  . SER   A 1 167 ? 4.500  -13.353 -3.106  1.00 20.78 ?  167 SER   A HB2  1 
ATOM   3685 H HB3  . SER   A 1 167 ? 3.512  -12.276 -2.483  1.00 20.78 ?  167 SER   A HB3  1 
ATOM   3686 H HG   . SER   A 1 167 ? 5.202  -11.603 -1.251  1.00 21.58 ?  167 SER   A HG   1 
ATOM   3687 N N    A PHE   A 1 168 ? 5.515  -14.894 0.332   0.50 15.66 ?  168 PHE   A N    1 
ATOM   3688 N N    B PHE   A 1 168 ? 5.540  -14.873 0.327   0.50 15.87 ?  168 PHE   A N    1 
ATOM   3689 C CA   A PHE   A 1 168 ? 6.702  -15.679 0.629   0.50 16.08 ?  168 PHE   A CA   1 
ATOM   3690 C CA   B PHE   A 1 168 ? 6.726  -15.670 0.612   0.50 16.44 ?  168 PHE   A CA   1 
ATOM   3691 C C    A PHE   A 1 168 ? 6.407  -17.166 0.518   0.50 18.45 ?  168 PHE   A C    1 
ATOM   3692 C C    B PHE   A 1 168 ? 6.403  -17.153 0.548   0.50 19.02 ?  168 PHE   A C    1 
ATOM   3693 O O    A PHE   A 1 168 ? 5.507  -17.686 1.186   0.50 19.35 ?  168 PHE   A O    1 
ATOM   3694 O O    B PHE   A 1 168 ? 5.410  -17.611 1.123   0.50 19.99 ?  168 PHE   A O    1 
ATOM   3695 C CB   A PHE   A 1 168 ? 7.208  -15.377 2.033   0.50 15.26 ?  168 PHE   A CB   1 
ATOM   3696 C CB   B PHE   A 1 168 ? 7.301  -15.349 1.989   0.50 15.28 ?  168 PHE   A CB   1 
ATOM   3697 C CG   A PHE   A 1 168 ? 8.493  -16.070 2.352   0.50 14.34 ?  168 PHE   A CG   1 
ATOM   3698 C CG   B PHE   A 1 168 ? 8.526  -16.158 2.310   0.50 14.22 ?  168 PHE   A CG   1 
ATOM   3699 C CD1  A PHE   A 1 168 ? 9.677  -15.616 1.806   0.50 14.78 ?  168 PHE   A CD1  1 
ATOM   3700 C CD1  B PHE   A 1 168 ? 9.705  -15.929 1.624   0.50 14.35 ?  168 PHE   A CD1  1 
ATOM   3701 C CD2  A PHE   A 1 168 ? 8.527  -17.191 3.167   0.50 13.96 ?  168 PHE   A CD2  1 
ATOM   3702 C CD2  B PHE   A 1 168 ? 8.503  -17.167 3.263   0.50 13.88 ?  168 PHE   A CD2  1 
ATOM   3703 C CE1  A PHE   A 1 168 ? 10.871 -16.248 2.077   0.50 14.52 ?  168 PHE   A CE1  1 
ATOM   3704 C CE1  B PHE   A 1 168 ? 10.840 -16.668 1.889   0.50 13.95 ?  168 PHE   A CE1  1 
ATOM   3705 C CE2  A PHE   A 1 168 ? 9.726  -17.828 3.442   0.50 14.08 ?  168 PHE   A CE2  1 
ATOM   3706 C CE2  B PHE   A 1 168 ? 9.644  -17.913 3.533   0.50 14.06 ?  168 PHE   A CE2  1 
ATOM   3707 C CZ   A PHE   A 1 168 ? 10.896 -17.355 2.894   0.50 14.18 ?  168 PHE   A CZ   1 
ATOM   3708 C CZ   B PHE   A 1 168 ? 10.811 -17.660 2.842   0.50 13.99 ?  168 PHE   A CZ   1 
ATOM   3709 H H    A PHE   A 1 168 ? 5.143  -14.530 1.018   0.50 18.81 ?  168 PHE   A H    1 
ATOM   3710 H H    B PHE   A 1 168 ? 5.190  -14.492 1.011   0.50 19.06 ?  168 PHE   A H    1 
ATOM   3711 H HA   A PHE   A 1 168 ? 7.401  -15.455 -0.008  0.50 19.32 ?  168 PHE   A HA   1 
ATOM   3712 H HA   B PHE   A 1 168 ? 7.406  -15.476 -0.052  0.50 19.75 ?  168 PHE   A HA   1 
ATOM   3713 H HB2  A PHE   A 1 168 ? 7.355  -14.423 2.116   0.50 18.34 ?  168 PHE   A HB2  1 
ATOM   3714 H HB2  B PHE   A 1 168 ? 7.546  -14.410 2.019   0.50 18.36 ?  168 PHE   A HB2  1 
ATOM   3715 H HB3  A PHE   A 1 168 ? 6.543  -15.669 2.674   0.50 18.34 ?  168 PHE   A HB3  1 
ATOM   3716 H HB3  B PHE   A 1 168 ? 6.630  -15.538 2.664   0.50 18.36 ?  168 PHE   A HB3  1 
ATOM   3717 H HD1  A PHE   A 1 168 ? 9.670  -14.868 1.251   0.50 17.75 ?  168 PHE   A HD1  1 
ATOM   3718 H HD1  B PHE   A 1 168 ? 9.734  -15.261 0.980   0.50 17.24 ?  168 PHE   A HD1  1 
ATOM   3719 H HD2  A PHE   A 1 168 ? 7.737  -17.515 3.540   0.50 16.77 ?  168 PHE   A HD2  1 
ATOM   3720 H HD2  B PHE   A 1 168 ? 7.716  -17.341 3.731   0.50 16.67 ?  168 PHE   A HD2  1 
ATOM   3721 H HE1  A PHE   A 1 168 ? 11.663 -15.926 1.706   0.50 17.44 ?  168 PHE   A HE1  1 
ATOM   3722 H HE1  B PHE   A 1 168 ? 11.627 -16.496 1.422   0.50 16.76 ?  168 PHE   A HE1  1 
ATOM   3723 H HE2  A PHE   A 1 168 ? 9.737  -18.577 3.996   0.50 16.92 ?  168 PHE   A HE2  1 
ATOM   3724 H HE2  B PHE   A 1 168 ? 9.619  -18.585 4.178   0.50 16.89 ?  168 PHE   A HE2  1 
ATOM   3725 H HZ   A PHE   A 1 168 ? 11.701 -17.780 3.078   0.50 17.04 ?  168 PHE   A HZ   1 
ATOM   3726 H HZ   B PHE   A 1 168 ? 11.578 -18.160 3.021   0.50 16.80 ?  168 PHE   A HZ   1 
ATOM   3727 N N    A LEU   A 1 169 ? 7.192  -17.855 -0.302  0.50 21.57 ?  169 LEU   A N    1 
ATOM   3728 N N    B LEU   A 1 169 ? 7.265  -17.907 -0.125  0.50 21.92 ?  169 LEU   A N    1 
ATOM   3729 C CA   A LEU   A 1 169 ? 7.032  -19.287 -0.465  0.50 25.53 ?  169 LEU   A CA   1 
ATOM   3730 C CA   B LEU   A 1 169 ? 7.072  -19.340 -0.251  0.50 25.91 ?  169 LEU   A CA   1 
ATOM   3731 C C    A LEU   A 1 169 ? 7.929  -20.014 0.524   0.50 26.73 ?  169 LEU   A C    1 
ATOM   3732 C C    B LEU   A 1 169 ? 8.010  -20.073 0.695   0.50 27.26 ?  169 LEU   A C    1 
ATOM   3733 O O    A LEU   A 1 169 ? 7.471  -20.438 1.586   0.50 27.12 ?  169 LEU   A O    1 
ATOM   3734 O O    B LEU   A 1 169 ? 7.573  -20.615 1.712   0.50 27.83 ?  169 LEU   A O    1 
ATOM   3735 C CB   A LEU   A 1 169 ? 7.361  -19.702 -1.900  0.50 27.45 ?  169 LEU   A CB   1 
ATOM   3736 C CB   B LEU   A 1 169 ? 7.311  -19.780 -1.697  0.50 27.94 ?  169 LEU   A CB   1 
ATOM   3737 C CG   A LEU   A 1 169 ? 7.050  -21.155 -2.263  0.50 29.15 ?  169 LEU   A CG   1 
ATOM   3738 C CG   B LEU   A 1 169 ? 6.851  -21.194 -2.054  0.50 29.57 ?  169 LEU   A CG   1 
ATOM   3739 C CD1  A LEU   A 1 169 ? 5.621  -21.508 -1.878  0.50 29.63 ?  169 LEU   A CD1  1 
ATOM   3740 C CD1  B LEU   A 1 169 ? 5.405  -21.405 -1.635  0.50 30.04 ?  169 LEU   A CD1  1 
ATOM   3741 C CD2  A LEU   A 1 169 ? 7.278  -21.397 -3.748  0.50 29.59 ?  169 LEU   A CD2  1 
ATOM   3742 C CD2  B LEU   A 1 169 ? 7.020  -21.449 -3.545  0.50 30.03 ?  169 LEU   A CD2  1 
ATOM   3743 O OXT  A LEU   A 1 169 ? 9.127  -20.179 0.294   0.50 26.62 -1 169 LEU   A OXT  1 
ATOM   3744 O OXT  B LEU   A 1 169 ? 9.219  -20.129 0.474   0.50 27.05 -1 169 LEU   A OXT  1 
ATOM   3745 H H    A LEU   A 1 169 ? 7.822  -17.514 -0.778  0.50 25.91 ?  169 LEU   A H    1 
ATOM   3746 H H    B LEU   A 1 169 ? 7.970  -17.609 -0.518  0.50 26.33 ?  169 LEU   A H    1 
ATOM   3747 H HA   A LEU   A 1 169 ? 6.115  -19.526 -0.272  0.50 30.65 ?  169 LEU   A HA   1 
ATOM   3748 H HA   B LEU   A 1 169 ? 6.164  -19.557 -0.001  0.50 31.11 ?  169 LEU   A HA   1 
ATOM   3749 H HB2  A LEU   A 1 169 ? 6.854  -19.138 -2.503  0.50 32.96 ?  169 LEU   A HB2  1 
ATOM   3750 H HB2  B LEU   A 1 169 ? 6.840  -19.168 -2.282  0.50 33.55 ?  169 LEU   A HB2  1 
ATOM   3751 H HB3  A LEU   A 1 169 ? 8.309  -19.565 -2.050  0.50 32.96 ?  169 LEU   A HB3  1 
ATOM   3752 H HB3  B LEU   A 1 169 ? 8.263  -19.732 -1.878  0.50 33.55 ?  169 LEU   A HB3  1 
ATOM   3753 H HG   A LEU   A 1 169 ? 7.646  -21.739 -1.770  0.50 35.00 ?  169 LEU   A HG   1 
ATOM   3754 H HG   B LEU   A 1 169 ? 7.400  -21.836 -1.576  0.50 35.51 ?  169 LEU   A HG   1 
ATOM   3755 H HD11 A LEU   A 1 169 ? 5.370  -22.332 -2.320  0.50 35.58 ?  169 LEU   A HD11 1 
ATOM   3756 H HD11 B LEU   A 1 169 ? 5.056  -22.183 -2.092  0.50 36.07 ?  169 LEU   A HD11 1 
ATOM   3757 H HD12 A LEU   A 1 169 ? 5.572  -21.621 -0.915  0.50 35.58 ?  169 LEU   A HD12 1 
ATOM   3758 H HD12 B LEU   A 1 169 ? 5.370  -21.540 -0.675  0.50 36.07 ?  169 LEU   A HD12 1 
ATOM   3759 H HD13 A LEU   A 1 169 ? 5.032  -20.790 -2.158  0.50 35.58 ?  169 LEU   A HD13 1 
ATOM   3760 H HD13 B LEU   A 1 169 ? 4.890  -20.619 -1.878  0.50 36.07 ?  169 LEU   A HD13 1 
ATOM   3761 H HD21 A LEU   A 1 169 ? 7.081  -22.325 -3.950  0.50 35.53 ?  169 LEU   A HD21 1 
ATOM   3762 H HD21 B LEU   A 1 169 ? 6.731  -22.353 -3.745  0.50 36.05 ?  169 LEU   A HD21 1 
ATOM   3763 H HD22 A LEU   A 1 169 ? 6.691  -20.815 -4.257  0.50 35.53 ?  169 LEU   A HD22 1 
ATOM   3764 H HD22 B LEU   A 1 169 ? 6.477  -20.812 -4.036  0.50 36.05 ?  169 LEU   A HD22 1 
ATOM   3765 H HD23 A LEU   A 1 169 ? 8.204  -21.201 -3.960  0.50 35.53 ?  169 LEU   A HD23 1 
ATOM   3766 H HD23 B LEU   A 1 169 ? 7.954  -21.340 -3.781  0.50 36.05 ?  169 LEU   A HD23 1 
ATOM   3767 N N    A SER   B 1 1   ? 50.713 -9.150  -23.693 0.50 27.73 ?  1   SER   B N    1 
ATOM   3768 N N    B SER   B 1 1   ? 50.772 -9.320  -23.848 0.50 25.14 ?  1   SER   B N    1 
ATOM   3769 C CA   A SER   B 1 1   ? 51.251 -10.246 -22.862 0.50 27.33 ?  1   SER   B CA   1 
ATOM   3770 C CA   B SER   B 1 1   ? 51.203 -10.316 -22.844 0.50 25.18 ?  1   SER   B CA   1 
ATOM   3771 C C    A SER   B 1 1   ? 50.191 -11.311 -22.628 0.50 26.09 ?  1   SER   B C    1 
ATOM   3772 C C    B SER   B 1 1   ? 50.106 -11.344 -22.593 0.50 24.48 ?  1   SER   B C    1 
ATOM   3773 O O    A SER   B 1 1   ? 49.003 -11.118 -22.915 0.50 25.76 ?  1   SER   B O    1 
ATOM   3774 O O    B SER   B 1 1   ? 48.937 -11.156 -22.963 0.50 23.61 ?  1   SER   B O    1 
ATOM   3775 C CB   A SER   B 1 1   ? 51.753 -9.710  -21.523 0.50 27.65 ?  1   SER   B CB   1 
ATOM   3776 C CB   B SER   B 1 1   ? 51.585 -9.634  -21.532 0.50 25.34 ?  1   SER   B CB   1 
ATOM   3777 O OG   A SER   B 1 1   ? 50.672 -9.364  -20.679 0.50 28.95 ?  1   SER   B OG   1 
ATOM   3778 O OG   B SER   B 1 1   ? 50.459 -9.513  -20.683 0.50 26.62 ?  1   SER   B OG   1 
ATOM   3779 H H1   A SER   B 1 1   ? 50.425 -9.488  -24.461 0.50 33.30 ?  1   SER   B H1   1 
ATOM   3780 H H1   B SER   B 1 1   ? 51.492 -8.966  -24.230 0.50 30.18 ?  1   SER   B H1   1 
ATOM   3781 H H2   A SER   B 1 1   ? 50.045 -8.762  -23.260 0.50 33.30 ?  1   SER   B H2   1 
ATOM   3782 H H2   B SER   B 1 1   ? 50.275 -9.725  -24.461 0.50 30.18 ?  1   SER   B H2   1 
ATOM   3783 H H3   A SER   B 1 1   ? 51.361 -8.563  -23.844 0.50 33.30 ?  1   SER   B H3   1 
ATOM   3784 H H3   B SER   B 1 1   ? 50.302 -8.687  -23.444 0.50 30.18 ?  1   SER   B H3   1 
ATOM   3785 H HA   A SER   B 1 1   ? 51.994 -10.649 -23.329 0.50 32.82 ?  1   SER   B HA   1 
ATOM   3786 H HA   B SER   B 1 1   ? 51.982 -10.773 -23.188 0.50 30.23 ?  1   SER   B HA   1 
ATOM   3787 H HB2  A SER   B 1 1   ? 52.287 -10.398 -21.096 0.50 33.19 ?  1   SER   B HB2  1 
ATOM   3788 H HB2  B SER   B 1 1   ? 52.265 -10.168 -21.092 0.50 30.43 ?  1   SER   B HB2  1 
ATOM   3789 H HB3  A SER   B 1 1   ? 52.293 -8.921  -21.680 0.50 33.19 ?  1   SER   B HB3  1 
ATOM   3790 H HB3  B SER   B 1 1   ? 51.931 -8.747  -21.721 0.50 30.43 ?  1   SER   B HB3  1 
ATOM   3791 H HG   A SER   B 1 1   ? 50.940 -8.849  -20.073 0.50 34.75 ?  1   SER   B HG   1 
ATOM   3792 H HG   B SER   B 1 1   ? 50.661 -9.056  -20.009 0.50 31.97 ?  1   SER   B HG   1 
ATOM   3793 N N    A MET   B 1 2   ? 50.641 -12.436 -22.091 0.50 25.12 ?  2   MET   B N    1 
ATOM   3794 N N    B MET   B 1 2   ? 50.502 -12.434 -21.947 0.50 24.64 ?  2   MET   B N    1 
ATOM   3795 C CA   A MET   B 1 2   ? 49.816 -13.620 -21.913 0.50 24.56 ?  2   MET   B CA   1 
ATOM   3796 C CA   B MET   B 1 2   ? 49.669 -13.622 -21.789 0.50 24.85 ?  2   MET   B CA   1 
ATOM   3797 C C    A MET   B 1 2   ? 49.574 -13.813 -20.426 0.50 21.05 ?  2   MET   B C    1 
ATOM   3798 C C    B MET   B 1 2   ? 49.408 -13.831 -20.302 0.50 22.43 ?  2   MET   B C    1 
ATOM   3799 O O    A MET   B 1 2   ? 50.520 -14.026 -19.663 0.50 20.61 ?  2   MET   B O    1 
ATOM   3800 O O    B MET   B 1 2   ? 50.290 -14.291 -19.570 0.50 23.02 ?  2   MET   B O    1 
ATOM   3801 C CB   A MET   B 1 2   ? 50.529 -14.832 -22.507 0.50 28.20 ?  2   MET   B CB   1 
ATOM   3802 C CB   B MET   B 1 2   ? 50.393 -14.814 -22.395 0.50 27.94 ?  2   MET   B CB   1 
ATOM   3803 C CG   A MET   B 1 2   ? 49.659 -16.065 -22.669 0.50 31.29 ?  2   MET   B CG   1 
ATOM   3804 C CG   B MET   B 1 2   ? 49.505 -15.971 -22.816 0.50 30.36 ?  2   MET   B CG   1 
ATOM   3805 S SD   A MET   B 1 2   ? 50.485 -17.333 -23.648 0.50 34.07 ?  2   MET   B SD   1 
ATOM   3806 S SD   B MET   B 1 2   ? 50.376 -17.120 -23.895 0.50 32.63 ?  2   MET   B SD   1 
ATOM   3807 C CE   A MET   B 1 2   ? 51.036 -16.341 -25.034 0.50 34.47 ?  2   MET   B CE   1 
ATOM   3808 C CE   B MET   B 1 2   ? 51.249 -15.966 -24.943 0.50 32.91 ?  2   MET   B CE   1 
ATOM   3809 H H    A MET   B 1 2   ? 51.449 -12.542 -21.808 0.50 30.16 ?  2   MET   B H    1 
ATOM   3810 H H    B MET   B 1 2   ? 51.281 -12.518 -21.589 0.50 29.59 ?  2   MET   B H    1 
ATOM   3811 H HA   A MET   B 1 2   ? 48.972 -13.513 -22.369 0.50 29.49 ?  2   MET   B HA   1 
ATOM   3812 H HA   B MET   B 1 2   ? 48.832 -13.502 -22.263 0.50 29.84 ?  2   MET   B HA   1 
ATOM   3813 H HB2  A MET   B 1 2   ? 50.859 -14.563 -23.376 0.50 33.85 ?  2   MET   B HB2  1 
ATOM   3814 H HB2  B MET   B 1 2   ? 50.869 -14.472 -23.162 0.50 33.55 ?  2   MET   B HB2  1 
ATOM   3815 H HB3  A MET   B 1 2   ? 51.274 -15.079 -21.939 0.50 33.85 ?  2   MET   B HB3  1 
ATOM   3816 H HB3  B MET   B 1 2   ? 51.027 -15.170 -21.758 0.50 33.55 ?  2   MET   B HB3  1 
ATOM   3817 H HG2  A MET   B 1 2   ? 49.465 -16.433 -21.791 0.50 37.56 ?  2   MET   B HG2  1 
ATOM   3818 H HG2  B MET   B 1 2   ? 49.217 -16.452 -22.023 0.50 36.45 ?  2   MET   B HG2  1 
ATOM   3819 H HG3  A MET   B 1 2   ? 48.836 -15.823 -23.121 0.50 37.56 ?  2   MET   B HG3  1 
ATOM   3820 H HG3  B MET   B 1 2   ? 48.738 -15.639 -23.300 0.50 36.45 ?  2   MET   B HG3  1 
ATOM   3821 H HE1  A MET   B 1 2   ? 51.184 -16.918 -25.789 0.50 41.39 ?  2   MET   B HE1  1 
ATOM   3822 H HE1  B MET   B 1 2   ? 51.491 -16.420 -25.749 0.50 39.51 ?  2   MET   B HE1  1 
ATOM   3823 H HE2  A MET   B 1 2   ? 50.346 -15.686 -25.241 0.50 41.39 ?  2   MET   B HE2  1 
ATOM   3824 H HE2  B MET   B 1 2   ? 50.661 -15.217 -25.144 0.50 39.51 ?  2   MET   B HE2  1 
ATOM   3825 H HE3  A MET   B 1 2   ? 51.860 -15.881 -24.794 0.50 41.39 ?  2   MET   B HE3  1 
ATOM   3826 H HE3  B MET   B 1 2   ? 52.047 -15.647 -24.482 0.50 39.51 ?  2   MET   B HE3  1 
ATOM   3827 N N    A VAL   B 1 3   ? 48.312 -13.708 -20.014 0.50 18.75 ?  3   VAL   B N    1 
ATOM   3828 N N    B VAL   B 1 3   ? 48.200 -13.493 -19.857 0.50 20.00 ?  3   VAL   B N    1 
ATOM   3829 C CA   A VAL   B 1 3   ? 47.905 -13.956 -18.639 0.50 17.49 ?  3   VAL   B CA   1 
ATOM   3830 C CA   B VAL   B 1 3   ? 47.771 -13.744 -18.487 0.50 18.35 ?  3   VAL   B CA   1 
ATOM   3831 C C    A VAL   B 1 3   ? 46.679 -14.859 -18.661 0.50 15.75 ?  3   VAL   B C    1 
ATOM   3832 C C    B VAL   B 1 3   ? 46.525 -14.616 -18.517 0.50 16.05 ?  3   VAL   B C    1 
ATOM   3833 O O    A VAL   B 1 3   ? 45.992 -14.995 -19.677 0.50 15.68 ?  3   VAL   B O    1 
ATOM   3834 O O    B VAL   B 1 3   ? 45.693 -14.519 -19.424 0.50 15.73 ?  3   VAL   B O    1 
ATOM   3835 C CB   A VAL   B 1 3   ? 47.604 -12.650 -17.869 0.50 18.89 ?  3   VAL   B CB   1 
ATOM   3836 C CB   B VAL   B 1 3   ? 47.525 -12.448 -17.678 0.50 19.28 ?  3   VAL   B CB   1 
ATOM   3837 C CG1  A VAL   B 1 3   ? 48.862 -11.793 -17.752 0.50 19.46 ?  3   VAL   B CG1  1 
ATOM   3838 C CG1  B VAL   B 1 3   ? 48.800 -11.618 -17.599 0.50 19.69 ?  3   VAL   B CG1  1 
ATOM   3839 C CG2  A VAL   B 1 3   ? 46.483 -11.876 -18.550 0.50 19.67 ?  3   VAL   B CG2  1 
ATOM   3840 C CG2  B VAL   B 1 3   ? 46.382 -11.639 -18.277 0.50 19.64 ?  3   VAL   B CG2  1 
ATOM   3841 H H    A VAL   B 1 3   ? 47.663 -13.488 -20.528 0.50 22.52 ?  3   VAL   B H    1 
ATOM   3842 H H    B VAL   B 1 3   ? 47.600 -13.118 -20.345 0.50 24.02 ?  3   VAL   B H    1 
ATOM   3843 H HA   A VAL   B 1 3   ? 48.620 -14.423 -18.172 0.50 21.01 ?  3   VAL   B HA   1 
ATOM   3844 H HA   B VAL   B 1 3   ? 48.459 -14.244 -18.029 0.50 22.04 ?  3   VAL   B HA   1 
ATOM   3845 H HB   A VAL   B 1 3   ? 47.312 -12.875 -16.971 0.50 22.69 ?  3   VAL   B HB   1 
ATOM   3846 H HB   B VAL   B 1 3   ? 47.274 -12.688 -16.773 0.50 23.16 ?  3   VAL   B HB   1 
ATOM   3847 H HG11 A VAL   B 1 3   ? 48.647 -10.987 -17.258 0.50 23.37 ?  3   VAL   B HG11 1 
ATOM   3848 H HG11 B VAL   B 1 3   ? 48.626 -10.822 -17.073 0.50 23.65 ?  3   VAL   B HG11 1 
ATOM   3849 H HG12 A VAL   B 1 3   ? 49.544 -12.298 -17.283 0.50 23.37 ?  3   VAL   B HG12 1 
ATOM   3850 H HG12 B VAL   B 1 3   ? 49.493 -12.149 -17.178 0.50 23.65 ?  3   VAL   B HG12 1 
ATOM   3851 H HG13 A VAL   B 1 3   ? 49.170 -11.565 -18.642 0.50 23.37 ?  3   VAL   B HG13 1 
ATOM   3852 H HG13 B VAL   B 1 3   ? 49.070 -11.371 -18.497 0.50 23.65 ?  3   VAL   B HG13 1 
ATOM   3853 H HG21 A VAL   B 1 3   ? 46.392 -11.013 -18.119 0.50 23.63 ?  3   VAL   B HG21 1 
ATOM   3854 H HG21 B VAL   B 1 3   ? 46.359 -10.766 -17.854 0.50 23.58 ?  3   VAL   B HG21 1 
ATOM   3855 H HG22 A VAL   B 1 3   ? 46.706 -11.756 -19.486 0.50 23.63 ?  3   VAL   B HG22 1 
ATOM   3856 H HG22 B VAL   B 1 3   ? 46.530 -11.542 -19.230 0.50 23.58 ?  3   VAL   B HG22 1 
ATOM   3857 H HG23 A VAL   B 1 3   ? 45.656 -12.376 -18.468 0.50 23.63 ?  3   VAL   B HG23 1 
ATOM   3858 H HG23 B VAL   B 1 3   ? 45.546 -12.105 -18.117 0.50 23.58 ?  3   VAL   B HG23 1 
ATOM   3859 N N    . ASN   B 1 4   ? 46.409 -15.483 -17.515 1.00 14.64 ?  4   ASN   B N    1 
ATOM   3860 C CA   . ASN   B 1 4   ? 45.279 -16.405 -17.391 1.00 13.52 ?  4   ASN   B CA   1 
ATOM   3861 C C    . ASN   B 1 4   ? 45.215 -17.370 -18.573 1.00 14.13 ?  4   ASN   B C    1 
ATOM   3862 O O    . ASN   B 1 4   ? 44.148 -17.631 -19.129 1.00 15.42 ?  4   ASN   B O    1 
ATOM   3863 C CB   . ASN   B 1 4   ? 43.953 -15.663 -17.212 1.00 13.07 ?  4   ASN   B CB   1 
ATOM   3864 C CG   . ASN   B 1 4   ? 43.920 -14.833 -15.951 1.00 12.45 ?  4   ASN   B CG   1 
ATOM   3865 O OD1  . ASN   B 1 4   ? 44.204 -15.338 -14.868 1.00 12.15 ?  4   ASN   B OD1  1 
ATOM   3866 N ND2  . ASN   B 1 4   ? 43.573 -13.558 -16.080 1.00 12.88 ?  4   ASN   B ND2  1 
ATOM   3867 H H    A ASN   B 1 4   ? 46.860 -15.387 -16.791 0.50 17.59 ?  4   ASN   B H    1 
ATOM   3868 H H    B ASN   B 1 4   ? 46.990 -15.568 -16.888 0.50 17.59 ?  4   ASN   B H    1 
ATOM   3869 H HA   . ASN   B 1 4   ? 45.416 -16.940 -16.592 1.00 16.25 ?  4   ASN   B HA   1 
ATOM   3870 H HB2  . ASN   B 1 4   ? 43.810 -15.072 -17.963 1.00 15.70 ?  4   ASN   B HB2  1 
ATOM   3871 H HB3  . ASN   B 1 4   ? 43.231 -16.315 -17.162 1.00 15.70 ?  4   ASN   B HB3  1 
ATOM   3872 H HD21 . ASN   B 1 4   ? 43.544 -13.045 -15.389 1.00 15.48 ?  4   ASN   B HD21 1 
ATOM   3873 H HD22 . ASN   B 1 4   ? 43.383 -13.241 -16.857 1.00 15.48 ?  4   ASN   B HD22 1 
ATOM   3874 N N    . SER   B 1 5   ? 46.372 -17.905 -18.964 1.00 15.46 ?  5   SER   B N    1 
ATOM   3875 C CA   . SER   B 1 5   ? 46.464 -18.824 -20.099 1.00 18.17 ?  5   SER   B CA   1 
ATOM   3876 C C    . SER   B 1 5   ? 46.485 -20.244 -19.545 1.00 19.20 ?  5   SER   B C    1 
ATOM   3877 O O    . SER   B 1 5   ? 47.526 -20.891 -19.453 1.00 21.31 ?  5   SER   B O    1 
ATOM   3878 C CB   . SER   B 1 5   ? 47.703 -18.525 -20.937 1.00 20.29 ?  5   SER   B CB   1 
ATOM   3879 O OG   . SER   B 1 5   ? 48.885 -18.740 -20.186 1.00 22.89 ?  5   SER   B OG   1 
ATOM   3880 H H    . SER   B 1 5   ? 47.128 -17.747 -18.585 1.00 18.57 ?  5   SER   B H    1 
ATOM   3881 H HA   . SER   B 1 5   ? 45.681 -18.728 -20.660 1.00 21.83 ?  5   SER   B HA   1 
ATOM   3882 H HB2  . SER   B 1 5   ? 47.707 -19.105 -21.715 1.00 24.37 ?  5   SER   B HB2  1 
ATOM   3883 H HB3  . SER   B 1 5   ? 47.661 -17.599 -21.215 1.00 24.37 ?  5   SER   B HB3  1 
ATOM   3884 H HG   . SER   B 1 5   ? 48.951 -19.552 -19.980 1.00 27.49 ?  5   SER   B HG   1 
ATOM   3885 N N    . PHE   B 1 6   ? 45.305 -20.720 -19.160 1.00 19.07 ?  6   PHE   B N    1 
ATOM   3886 C CA   . PHE   B 1 6   ? 45.158 -22.061 -18.612 1.00 18.58 ?  6   PHE   B CA   1 
ATOM   3887 C C    . PHE   B 1 6   ? 45.104 -23.071 -19.748 1.00 21.47 ?  6   PHE   B C    1 
ATOM   3888 O O    . PHE   B 1 6   ? 44.405 -22.860 -20.743 1.00 23.76 ?  6   PHE   B O    1 
ATOM   3889 C CB   . PHE   B 1 6   ? 43.872 -22.144 -17.789 1.00 16.42 ?  6   PHE   B CB   1 
ATOM   3890 C CG   . PHE   B 1 6   ? 43.874 -21.261 -16.571 1.00 14.61 ?  6   PHE   B CG   1 
ATOM   3891 C CD1  . PHE   B 1 6   ? 44.395 -21.719 -15.377 1.00 13.41 ?  6   PHE   B CD1  1 
ATOM   3892 C CD2  . PHE   B 1 6   ? 43.368 -19.968 -16.626 1.00 14.29 ?  6   PHE   B CD2  1 
ATOM   3893 C CE1  . PHE   B 1 6   ? 44.394 -20.911 -14.246 1.00 13.07 ?  6   PHE   B CE1  1 
ATOM   3894 C CE2  . PHE   B 1 6   ? 43.369 -19.151 -15.504 1.00 14.75 ?  6   PHE   B CE2  1 
ATOM   3895 C CZ   . PHE   B 1 6   ? 43.888 -19.615 -14.316 1.00 13.59 ?  6   PHE   B CZ   1 
ATOM   3896 H H    . PHE   B 1 6   ? 44.568 -20.283 -19.209 1.00 22.90 ?  6   PHE   B H    1 
ATOM   3897 H HA   . PHE   B 1 6   ? 45.912 -22.272 -18.039 1.00 22.31 ?  6   PHE   B HA   1 
ATOM   3898 H HB2  . PHE   B 1 6   ? 43.125 -21.877 -18.345 1.00 19.72 ?  6   PHE   B HB2  1 
ATOM   3899 H HB3  . PHE   B 1 6   ? 43.748 -23.060 -17.490 1.00 19.72 ?  6   PHE   B HB3  1 
ATOM   3900 H HD1  . PHE   B 1 6   ? 44.748 -22.578 -15.322 1.00 16.11 ?  6   PHE   B HD1  1 
ATOM   3901 H HD2  . PHE   B 1 6   ? 43.013 -19.655 -17.424 1.00 17.16 ?  6   PHE   B HD2  1 
ATOM   3902 H HE1  . PHE   B 1 6   ? 44.762 -21.220 -13.447 1.00 15.71 ?  6   PHE   B HE1  1 
ATOM   3903 H HE2  . PHE   B 1 6   ? 43.022 -18.288 -15.555 1.00 17.71 ?  6   PHE   B HE2  1 
ATOM   3904 H HZ   . PHE   B 1 6   ? 43.896 -19.068 -13.562 1.00 16.32 ?  6   PHE   B HZ   1 
ATOM   3905 N N    A SER   B 1 7   ? 45.843 -24.169 -19.611 0.50 21.85 ?  7   SER   B N    1 
ATOM   3906 N N    B SER   B 1 7   ? 45.840 -24.171 -19.582 0.50 21.80 ?  7   SER   B N    1 
ATOM   3907 C CA   A SER   B 1 7   ? 45.917 -25.153 -20.681 0.50 22.98 ?  7   SER   B CA   1 
ATOM   3908 C CA   B SER   B 1 7   ? 45.988 -25.195 -20.605 0.50 22.80 ?  7   SER   B CA   1 
ATOM   3909 C C    A SER   B 1 7   ? 45.822 -26.561 -20.115 0.50 22.11 ?  7   SER   B C    1 
ATOM   3910 C C    B SER   B 1 7   ? 45.994 -26.570 -19.952 0.50 21.60 ?  7   SER   B C    1 
ATOM   3911 O O    A SER   B 1 7   ? 46.398 -26.863 -19.066 0.50 22.71 ?  7   SER   B O    1 
ATOM   3912 O O    B SER   B 1 7   ? 46.552 -26.748 -18.865 0.50 22.00 ?  7   SER   B O    1 
ATOM   3913 C CB   A SER   B 1 7   ? 47.210 -24.999 -21.491 0.50 24.58 ?  7   SER   B CB   1 
ATOM   3914 C CB   B SER   B 1 7   ? 47.296 -24.994 -21.384 0.50 24.56 ?  7   SER   B CB   1 
ATOM   3915 O OG   A SER   B 1 7   ? 47.154 -25.763 -22.682 0.50 25.96 ?  7   SER   B OG   1 
ATOM   3916 O OG   B SER   B 1 7   ? 47.503 -26.035 -22.322 0.50 25.91 ?  7   SER   B OG   1 
ATOM   3917 H H    A SER   B 1 7   ? 46.304 -24.367 -18.910 0.50 26.24 ?  7   SER   B H    1 
ATOM   3918 H H    B SER   B 1 7   ? 46.272 -24.351 -18.858 0.50 26.18 ?  7   SER   B H    1 
ATOM   3919 H HA   A SER   B 1 7   ? 45.169 -25.027 -21.283 0.50 27.60 ?  7   SER   B HA   1 
ATOM   3920 H HA   B SER   B 1 7   ? 45.245 -25.153 -21.225 0.50 27.38 ?  7   SER   B HA   1 
ATOM   3921 H HB2  A SER   B 1 7   ? 47.324 -24.065 -21.726 0.50 29.51 ?  7   SER   B HB2  1 
ATOM   3922 H HB2  B SER   B 1 7   ? 47.252 -24.146 -21.853 0.50 29.49 ?  7   SER   B HB2  1 
ATOM   3923 H HB3  A SER   B 1 7   ? 47.958 -25.300 -20.953 0.50 29.51 ?  7   SER   B HB3  1 
ATOM   3924 H HB3  B SER   B 1 7   ? 48.037 -24.985 -20.757 0.50 29.49 ?  7   SER   B HB3  1 
ATOM   3925 H HG   A SER   B 1 7   ? 47.869 -25.677 -23.114 0.50 31.17 ?  7   SER   B HG   1 
ATOM   3926 H HG   B SER   B 1 7   ? 48.220 -25.903 -22.741 0.50 31.11 ?  7   SER   B HG   1 
ATOM   3927 N N    A GLY   B 1 8   ? 45.089 -27.419 -20.824 0.50 21.54 ?  8   GLY   B N    1 
ATOM   3928 N N    B GLY   B 1 8   ? 45.367 -27.538 -20.620 0.50 20.96 ?  8   GLY   B N    1 
ATOM   3929 C CA   A GLY   B 1 8   ? 45.006 -28.819 -20.469 0.50 20.54 ?  8   GLY   B CA   1 
ATOM   3930 C CA   B GLY   B 1 8   ? 45.386 -28.910 -20.154 0.50 19.87 ?  8   GLY   B CA   1 
ATOM   3931 C C    A GLY   B 1 8   ? 44.058 -29.148 -19.344 0.50 19.26 ?  8   GLY   B C    1 
ATOM   3932 C C    B GLY   B 1 8   ? 44.385 -29.232 -19.071 0.50 18.77 ?  8   GLY   B C    1 
ATOM   3933 O O    A GLY   B 1 8   ? 44.157 -30.239 -18.770 0.50 20.14 ?  8   GLY   B O    1 
ATOM   3934 O O    B GLY   B 1 8   ? 44.557 -30.233 -18.364 0.50 19.10 ?  8   GLY   B O    1 
ATOM   3935 H H    A GLY   B 1 8   ? 44.636 -27.206 -21.523 0.50 25.87 ?  8   GLY   B H    1 
ATOM   3936 H H    B GLY   B 1 8   ? 44.919 -27.418 -21.345 0.50 25.17 ?  8   GLY   B H    1 
ATOM   3937 H HA2  A GLY   B 1 8   ? 44.713 -29.322 -21.243 0.50 24.67 ?  8   GLY   B HA2  1 
ATOM   3938 H HA2  B GLY   B 1 8   ? 45.218 -29.500 -20.908 0.50 23.87 ?  8   GLY   B HA2  1 
ATOM   3939 H HA3  A GLY   B 1 8   ? 45.889 -29.134 -20.222 0.50 24.67 ?  8   GLY   B HA3  1 
ATOM   3940 H HA3  B GLY   B 1 8   ? 46.263 -29.114 -19.803 0.50 23.87 ?  8   GLY   B HA3  1 
ATOM   3941 N N    A TYR   B 1 9   ? 43.122 -28.259 -19.020 0.50 18.08 ?  9   TYR   B N    1 
ATOM   3942 N N    B TYR   B 1 9   ? 43.343 -28.422 -18.914 0.50 18.11 ?  9   TYR   B N    1 
ATOM   3943 C CA   A TYR   B 1 9   ? 42.180 -28.512 -17.942 0.50 16.92 ?  9   TYR   B CA   1 
ATOM   3944 C CA   B TYR   B 1 9   ? 42.334 -28.659 -17.895 0.50 16.92 ?  9   TYR   B CA   1 
ATOM   3945 C C    A TYR   B 1 9   ? 40.992 -29.309 -18.443 0.50 16.67 ?  9   TYR   B C    1 
ATOM   3946 C C    B TYR   B 1 9   ? 41.150 -29.435 -18.467 0.50 16.44 ?  9   TYR   B C    1 
ATOM   3947 O O    A TYR   B 1 9   ? 40.513 -29.102 -19.561 0.50 18.22 ?  9   TYR   B O    1 
ATOM   3948 O O    B TYR   B 1 9   ? 40.850 -29.369 -19.662 0.50 17.75 ?  9   TYR   B O    1 
ATOM   3949 C CB   A TYR   B 1 9   ? 41.667 -27.208 -17.341 0.50 16.30 ?  9   TYR   B CB   1 
ATOM   3950 C CB   B TYR   B 1 9   ? 41.867 -27.334 -17.284 0.50 16.62 ?  9   TYR   B CB   1 
ATOM   3951 C CG   A TYR   B 1 9   ? 42.660 -26.580 -16.413 0.50 15.45 ?  9   TYR   B CG   1 
ATOM   3952 C CG   B TYR   B 1 9   ? 42.880 -26.727 -16.332 0.50 16.14 ?  9   TYR   B CG   1 
ATOM   3953 C CD1  A TYR   B 1 9   ? 43.747 -25.884 -16.913 0.50 15.43 ?  9   TYR   B CD1  1 
ATOM   3954 C CD1  B TYR   B 1 9   ? 44.044 -26.128 -16.808 0.50 16.24 ?  9   TYR   B CD1  1 
ATOM   3955 C CD2  A TYR   B 1 9   ? 42.531 -26.701 -15.038 0.50 15.13 ?  9   TYR   B CD2  1 
ATOM   3956 C CD2  B TYR   B 1 9   ? 42.678 -26.758 -14.959 0.50 15.64 ?  9   TYR   B CD2  1 
ATOM   3957 C CE1  A TYR   B 1 9   ? 44.674 -25.316 -16.075 0.50 15.86 ?  9   TYR   B CE1  1 
ATOM   3958 C CE1  B TYR   B 1 9   ? 44.978 -25.585 -15.942 0.50 16.29 ?  9   TYR   B CE1  1 
ATOM   3959 C CE2  A TYR   B 1 9   ? 43.456 -26.134 -14.187 0.50 15.38 ?  9   TYR   B CE2  1 
ATOM   3960 C CE2  B TYR   B 1 9   ? 43.604 -26.211 -14.085 0.50 15.86 ?  9   TYR   B CE2  1 
ATOM   3961 C CZ   A TYR   B 1 9   ? 44.527 -25.440 -14.715 0.50 15.94 ?  9   TYR   B CZ   1 
ATOM   3962 C CZ   B TYR   B 1 9   ? 44.751 -25.625 -14.586 0.50 16.39 ?  9   TYR   B CZ   1 
ATOM   3963 O OH   A TYR   B 1 9   ? 45.459 -24.873 -13.885 0.50 16.76 ?  9   TYR   B OH   1 
ATOM   3964 O OH   B TYR   B 1 9   ? 45.679 -25.092 -13.726 0.50 16.86 ?  9   TYR   B OH   1 
ATOM   3965 H H    A TYR   B 1 9   ? 43.001 -27.512 -19.426 0.50 21.72 ?  9   TYR   B H    1 
ATOM   3966 H H    B TYR   B 1 9   ? 43.192 -27.725 -19.396 0.50 21.75 ?  9   TYR   B H    1 
ATOM   3967 H HA   A TYR   B 1 9   ? 42.615 -29.020 -17.242 0.50 20.32 ?  9   TYR   B HA   1 
ATOM   3968 H HA   B TYR   B 1 9   ? 42.715 -29.193 -17.185 0.50 20.32 ?  9   TYR   B HA   1 
ATOM   3969 H HB2  A TYR   B 1 9   ? 41.469 -26.577 -18.052 0.50 19.58 ?  9   TYR   B HB2  1 
ATOM   3970 H HB2  B TYR   B 1 9   ? 41.710 -26.690 -17.992 0.50 19.96 ?  9   TYR   B HB2  1 
ATOM   3971 H HB3  A TYR   B 1 9   ? 40.869 -27.406 -16.835 0.50 19.58 ?  9   TYR   B HB3  1 
ATOM   3972 H HB3  B TYR   B 1 9   ? 41.053 -27.484 -16.784 0.50 19.96 ?  9   TYR   B HB3  1 
ATOM   3973 H HD1  A TYR   B 1 9   ? 43.852 -25.802 -17.833 0.50 18.53 ?  9   TYR   B HD1  1 
ATOM   3974 H HD1  B TYR   B 1 9   ? 44.202 -26.098 -17.723 0.50 19.51 ?  9   TYR   B HD1  1 
ATOM   3975 H HD2  A TYR   B 1 9   ? 41.804 -27.171 -14.686 0.50 18.17 ?  9   TYR   B HD2  1 
ATOM   3976 H HD2  B TYR   B 1 9   ? 41.906 -27.153 -14.619 0.50 18.78 ?  9   TYR   B HD2  1 
ATOM   3977 H HE1  A TYR   B 1 9   ? 45.397 -24.854 -16.424 0.50 19.05 ?  9   TYR   B HE1  1 
ATOM   3978 H HE1  B TYR   B 1 9   ? 45.751 -25.185 -16.273 0.50 19.57 ?  9   TYR   B HE1  1 
ATOM   3979 H HE2  A TYR   B 1 9   ? 43.353 -26.221 -13.266 0.50 18.48 ?  9   TYR   B HE2  1 
ATOM   3980 H HE2  B TYR   B 1 9   ? 43.452 -26.242 -13.166 0.50 19.05 ?  9   TYR   B HE2  1 
ATOM   3981 H HH   A TYR   B 1 9   ? 46.046 -24.492 -14.340 0.50 20.13 ?  9   TYR   B HH   1 
ATOM   3982 H HH   B TYR   B 1 9   ? 46.322 -24.766 -14.155 0.50 20.25 ?  9   TYR   B HH   1 
ATOM   3983 N N    . LEU   B 1 10  ? 40.504 -30.200 -17.591 1.00 15.18 ?  10  LEU   B N    1 
ATOM   3984 C CA   . LEU   B 1 10  ? 39.303 -30.959 -17.891 1.00 14.88 ?  10  LEU   B CA   1 
ATOM   3985 C C    . LEU   B 1 10  ? 38.110 -30.198 -17.325 1.00 14.07 ?  10  LEU   B C    1 
ATOM   3986 O O    . LEU   B 1 10  ? 38.122 -29.785 -16.162 1.00 14.08 ?  10  LEU   B O    1 
ATOM   3987 C CB   . LEU   B 1 10  ? 39.404 -32.338 -17.242 1.00 15.75 ?  10  LEU   B CB   1 
ATOM   3988 C CG   . LEU   B 1 10  ? 38.238 -33.270 -17.542 1.00 17.52 ?  10  LEU   B CG   1 
ATOM   3989 C CD1  . LEU   B 1 10  ? 38.321 -33.774 -18.976 1.00 19.00 ?  10  LEU   B CD1  1 
ATOM   3990 C CD2  . LEU   B 1 10  ? 38.186 -34.424 -16.556 1.00 18.97 ?  10  LEU   B CD2  1 
ATOM   3991 H H    A LEU   B 1 10  ? 40.843 -30.373 -16.818 0.50 18.24 ?  10  LEU   B H    1 
ATOM   3992 H H    B LEU   B 1 10  ? 40.763 -30.303 -16.774 0.50 18.24 ?  10  LEU   B H    1 
ATOM   3993 H HA   . LEU   B 1 10  ? 39.197 -31.062 -18.848 1.00 17.88 ?  10  LEU   B HA   1 
ATOM   3994 H HB2  . LEU   B 1 10  ? 40.216 -32.771 -17.556 1.00 18.92 ?  10  LEU   B HB2  1 
ATOM   3995 H HB3  . LEU   B 1 10  ? 39.452 -32.227 -16.278 1.00 18.92 ?  10  LEU   B HB3  1 
ATOM   3996 H HG   . LEU   B 1 10  ? 37.411 -32.775 -17.452 1.00 21.04 ?  10  LEU   B HG   1 
ATOM   3997 H HD11 . LEU   B 1 10  ? 37.594 -34.396 -19.131 1.00 22.81 ?  10  LEU   B HD11 1 
ATOM   3998 H HD12 . LEU   B 1 10  ? 38.243 -33.017 -19.578 1.00 22.81 ?  10  LEU   B HD12 1 
ATOM   3999 H HD13 . LEU   B 1 10  ? 39.172 -34.216 -19.105 1.00 22.81 ?  10  LEU   B HD13 1 
ATOM   4000 H HD21 . LEU   B 1 10  ? 37.433 -34.993 -16.782 1.00 22.78 ?  10  LEU   B HD21 1 
ATOM   4001 H HD22 . LEU   B 1 10  ? 39.012 -34.924 -16.613 1.00 22.78 ?  10  LEU   B HD22 1 
ATOM   4002 H HD23 . LEU   B 1 10  ? 38.073 -34.065 -15.662 1.00 22.78 ?  10  LEU   B HD23 1 
ATOM   4003 N N    . LYS   B 1 11  ? 37.083 -30.017 -18.146 1.00 15.02 ?  11  LYS   B N    1 
ATOM   4004 C CA   . LYS   B 1 11  ? 35.894 -29.288 -17.733 1.00 17.03 ?  11  LYS   B CA   1 
ATOM   4005 C C    . LYS   B 1 11  ? 34.984 -30.207 -16.922 1.00 16.32 ?  11  LYS   B C    1 
ATOM   4006 O O    . LYS   B 1 11  ? 34.574 -31.266 -17.408 1.00 18.87 ?  11  LYS   B O    1 
ATOM   4007 C CB   . LYS   B 1 11  ? 35.171 -28.777 -18.977 1.00 20.75 ?  11  LYS   B CB   1 
ATOM   4008 C CG   . LYS   B 1 11  ? 34.006 -27.845 -18.713 1.00 24.04 ?  11  LYS   B CG   1 
ATOM   4009 C CD   . LYS   B 1 11  ? 33.228 -27.590 -19.998 1.00 26.98 ?  11  LYS   B CD   1 
ATOM   4010 C CE   . LYS   B 1 11  ? 32.171 -26.515 -19.814 1.00 29.10 ?  11  LYS   B CE   1 
ATOM   4011 N NZ   . LYS   B 1 11  ? 32.784 -25.176 -19.617 1.00 30.23 ?  11  LYS   B NZ   1 
ATOM   4012 H H    . LYS   B 1 11  ? 37.047 -30.318 -18.951 1.00 18.04 ?  11  LYS   B H    1 
ATOM   4013 H HA   . LYS   B 1 11  ? 36.148 -28.530 -17.182 1.00 20.45 ?  11  LYS   B HA   1 
ATOM   4014 H HB2  . LYS   B 1 11  ? 35.810 -28.295 -19.527 1.00 24.91 ?  11  LYS   B HB2  1 
ATOM   4015 H HB3  . LYS   B 1 11  ? 34.830 -29.539 -19.469 1.00 24.91 ?  11  LYS   B HB3  1 
ATOM   4016 H HG2  . LYS   B 1 11  ? 33.406 -28.250 -18.068 1.00 28.87 ?  11  LYS   B HG2  1 
ATOM   4017 H HG3  . LYS   B 1 11  ? 34.339 -26.996 -18.383 1.00 28.87 ?  11  LYS   B HG3  1 
ATOM   4018 H HD2  . LYS   B 1 11  ? 33.843 -27.297 -20.690 1.00 32.39 ?  11  LYS   B HD2  1 
ATOM   4019 H HD3  . LYS   B 1 11  ? 32.785 -28.410 -20.271 1.00 32.39 ?  11  LYS   B HD3  1 
ATOM   4020 H HE2  . LYS   B 1 11  ? 31.609 -26.481 -20.604 1.00 34.94 ?  11  LYS   B HE2  1 
ATOM   4021 H HE3  . LYS   B 1 11  ? 31.638 -26.726 -19.032 1.00 34.94 ?  11  LYS   B HE3  1 
ATOM   4022 H HZ1  . LYS   B 1 11  ? 32.148 -24.557 -19.553 1.00 36.29 ?  11  LYS   B HZ1  1 
ATOM   4023 H HZ2  . LYS   B 1 11  ? 33.270 -25.170 -18.873 1.00 36.29 ?  11  LYS   B HZ2  1 
ATOM   4024 H HZ3  . LYS   B 1 11  ? 33.310 -24.978 -20.308 1.00 36.29 ?  11  LYS   B HZ3  1 
ATOM   4025 N N    . LEU   B 1 12  ? 34.661 -29.802 -15.694 1.00 15.01 ?  12  LEU   B N    1 
ATOM   4026 C CA   . LEU   B 1 12  ? 33.702 -30.513 -14.855 1.00 14.92 ?  12  LEU   B CA   1 
ATOM   4027 C C    . LEU   B 1 12  ? 32.306 -29.915 -14.946 1.00 14.74 ?  12  LEU   B C    1 
ATOM   4028 O O    . LEU   B 1 12  ? 31.320 -30.637 -15.112 1.00 15.40 ?  12  LEU   B O    1 
ATOM   4029 C CB   . LEU   B 1 12  ? 34.165 -30.516 -13.394 1.00 14.43 ?  12  LEU   B CB   1 
ATOM   4030 C CG   . LEU   B 1 12  ? 35.500 -31.201 -13.109 1.00 14.05 ?  12  LEU   B CG   1 
ATOM   4031 C CD1  . LEU   B 1 12  ? 35.824 -31.160 -11.626 1.00 14.27 ?  12  LEU   B CD1  1 
ATOM   4032 C CD2  . LEU   B 1 12  ? 35.484 -32.633 -13.619 1.00 15.32 ?  12  LEU   B CD2  1 
ATOM   4033 H H    . LEU   B 1 12  ? 34.988 -29.097 -15.320 1.00 18.03 ?  12  LEU   B H    1 
ATOM   4034 H HA   . LEU   B 1 12  ? 33.641 -31.429 -15.158 1.00 17.92 ?  12  LEU   B HA   1 
ATOM   4035 H HB2  . LEU   B 1 12  ? 34.242 -29.596 -13.098 1.00 17.33 ?  12  LEU   B HB2  1 
ATOM   4036 H HB3  . LEU   B 1 12  ? 33.489 -30.968 -12.865 1.00 17.33 ?  12  LEU   B HB3  1 
ATOM   4037 H HG   . LEU   B 1 12  ? 36.200 -30.726 -13.581 1.00 16.89 ?  12  LEU   B HG   1 
ATOM   4038 H HD11 . LEU   B 1 12  ? 36.679 -31.600 -11.478 1.00 17.14 ?  12  LEU   B HD11 1 
ATOM   4039 H HD12 . LEU   B 1 12  ? 35.876 -30.236 -11.338 1.00 17.14 ?  12  LEU   B HD12 1 
ATOM   4040 H HD13 . LEU   B 1 12  ? 35.127 -31.623 -11.135 1.00 17.14 ?  12  LEU   B HD13 1 
ATOM   4041 H HD21 . LEU   B 1 12  ? 36.266 -33.094 -13.284 1.00 18.41 ?  12  LEU   B HD21 1 
ATOM   4042 H HD22 . LEU   B 1 12  ? 34.678 -33.070 -13.305 1.00 18.41 ?  12  LEU   B HD22 1 
ATOM   4043 H HD23 . LEU   B 1 12  ? 35.496 -32.621 -14.591 1.00 18.41 ?  12  LEU   B HD23 1 
ATOM   4044 N N    . THR   B 1 13  ? 32.212 -28.598 -14.820 1.00 14.92 ?  13  THR   B N    1 
ATOM   4045 C CA   . THR   B 1 13  ? 30.984 -27.851 -15.027 1.00 14.80 ?  13  THR   B CA   1 
ATOM   4046 C C    . THR   B 1 13  ? 31.311 -26.646 -15.905 1.00 16.19 ?  13  THR   B C    1 
ATOM   4047 O O    . THR   B 1 13  ? 32.456 -26.443 -16.327 1.00 17.00 ?  13  THR   B O    1 
ATOM   4048 C CB   . THR   B 1 13  ? 30.375 -27.386 -13.696 1.00 14.46 ?  13  THR   B CB   1 
ATOM   4049 O OG1  . THR   B 1 13  ? 31.209 -26.361 -13.136 1.00 14.30 ?  13  THR   B OG1  1 
ATOM   4050 C CG2  . THR   B 1 13  ? 30.258 -28.548 -12.707 1.00 14.98 ?  13  THR   B CG2  1 
ATOM   4051 H H    . THR   B 1 13  ? 32.872 -28.093 -14.599 1.00 17.92 ?  13  THR   B H    1 
ATOM   4052 H HA   . THR   B 1 13  ? 30.332 -28.405 -15.481 1.00 17.78 ?  13  THR   B HA   1 
ATOM   4053 H HB   . THR   B 1 13  ? 29.481 -27.029 -13.851 1.00 17.37 ?  13  THR   B HB   1 
ATOM   4054 H HG1  . THR   B 1 13  ? 30.906 -25.600 -13.344 1.00 17.18 ?  13  THR   B HG1  1 
ATOM   4055 H HG21 . THR   B 1 13  ? 29.724 -28.283 -11.941 1.00 18.00 ?  13  THR   B HG21 1 
ATOM   4056 H HG22 . THR   B 1 13  ? 29.832 -29.307 -13.137 1.00 18.00 ?  13  THR   B HG22 1 
ATOM   4057 H HG23 . THR   B 1 13  ? 31.139 -28.814 -12.402 1.00 18.00 ?  13  THR   B HG23 1 
ATOM   4058 N N    A ASP   B 1 14  ? 30.290 -25.829 -16.163 0.50 17.01 ?  14  ASP   B N    1 
ATOM   4059 N N    B ASP   B 1 14  ? 30.297 -25.817 -16.163 0.50 17.02 ?  14  ASP   B N    1 
ATOM   4060 C CA   A ASP   B 1 14  ? 30.486 -24.656 -17.007 0.50 18.18 ?  14  ASP   B CA   1 
ATOM   4061 C CA   B ASP   B 1 14  ? 30.495 -24.655 -17.024 0.50 18.08 ?  14  ASP   B CA   1 
ATOM   4062 C C    A ASP   B 1 14  ? 31.600 -23.760 -16.480 0.50 16.61 ?  14  ASP   B C    1 
ATOM   4063 C C    B ASP   B 1 14  ? 31.486 -23.650 -16.454 0.50 16.53 ?  14  ASP   B C    1 
ATOM   4064 O O    A ASP   B 1 14  ? 32.292 -23.107 -17.271 0.50 17.50 ?  14  ASP   B O    1 
ATOM   4065 O O    B ASP   B 1 14  ? 31.930 -22.760 -17.189 0.50 17.29 ?  14  ASP   B O    1 
ATOM   4066 C CB   A ASP   B 1 14  ? 29.174 -23.878 -17.133 0.50 20.94 ?  14  ASP   B CB   1 
ATOM   4067 C CB   B ASP   B 1 14  ? 29.167 -23.943 -17.276 0.50 20.76 ?  14  ASP   B CB   1 
ATOM   4068 C CG   A ASP   B 1 14  ? 28.184 -24.542 -18.066 0.50 23.89 ?  14  ASP   B CG   1 
ATOM   4069 C CG   B ASP   B 1 14  ? 28.312 -24.658 -18.303 0.50 23.52 ?  14  ASP   B CG   1 
ATOM   4070 O OD1  A ASP   B 1 14  ? 28.515 -25.585 -18.674 0.50 24.71 ?  14  ASP   B OD1  1 
ATOM   4071 O OD1  B ASP   B 1 14  ? 28.884 -25.308 -19.204 0.50 24.26 ?  14  ASP   B OD1  1 
ATOM   4072 O OD2  A ASP   B 1 14  ? 27.059 -24.017 -18.182 0.50 24.98 -1 14  ASP   B OD2  1 
ATOM   4073 O OD2  B ASP   B 1 14  ? 27.070 -24.580 -18.208 0.50 24.38 -1 14  ASP   B OD2  1 
ATOM   4074 H H    A ASP   B 1 14  ? 29.492 -25.920 -15.855 0.50 20.43 ?  14  ASP   B H    1 
ATOM   4075 H H    B ASP   B 1 14  ? 29.498 -25.906 -15.856 0.50 20.44 ?  14  ASP   B H    1 
ATOM   4076 H HA   A ASP   B 1 14  ? 30.747 -24.941 -17.891 0.50 21.83 ?  14  ASP   B HA   1 
ATOM   4077 H HA   B ASP   B 1 14  ? 30.832 -24.961 -17.879 0.50 21.72 ?  14  ASP   B HA   1 
ATOM   4078 H HB2  A ASP   B 1 14  ? 28.736 -23.833 -16.271 0.50 25.15 ?  14  ASP   B HB2  1 
ATOM   4079 H HB2  B ASP   B 1 14  ? 28.669 -23.898 -16.444 0.50 24.94 ?  14  ASP   B HB2  1 
ATOM   4080 H HB3  A ASP   B 1 14  ? 29.352 -22.987 -17.467 0.50 25.15 ?  14  ASP   B HB3  1 
ATOM   4081 H HB3  B ASP   B 1 14  ? 29.352 -23.041 -17.595 0.50 24.94 ?  14  ASP   B HB3  1 
ATOM   4082 N N    . ASN   B 1 15  ? 31.813 -23.739 -15.163 1.00 14.70 ?  15  ASN   B N    1 
ATOM   4083 C CA   . ASN   B 1 15  ? 32.765 -22.814 -14.559 1.00 12.70 ?  15  ASN   B CA   1 
ATOM   4084 C C    . ASN   B 1 15  ? 33.859 -23.464 -13.722 1.00 11.41 ?  15  ASN   B C    1 
ATOM   4085 O O    . ASN   B 1 15  ? 34.687 -22.731 -13.173 1.00 12.10 ?  15  ASN   B O    1 
ATOM   4086 C CB   . ASN   B 1 15  ? 32.043 -21.759 -13.704 1.00 12.66 ?  15  ASN   B CB   1 
ATOM   4087 C CG   . ASN   B 1 15  ? 31.417 -22.353 -12.465 1.00 12.49 ?  15  ASN   B CG   1 
ATOM   4088 O OD1  . ASN   B 1 15  ? 30.474 -23.147 -12.554 1.00 14.13 ?  15  ASN   B OD1  1 
ATOM   4089 N ND2  . ASN   B 1 15  ? 31.938 -21.998 -11.302 1.00 12.11 ?  15  ASN   B ND2  1 
ATOM   4090 H H    A ASN   B 1 15  ? 31.425 -24.264 -14.600 0.50 17.66 ?  15  ASN   B H    1 
ATOM   4091 H H    B ASN   B 1 15  ? 31.465 -24.300 -14.610 0.50 17.66 ?  15  ASN   B H    1 
ATOM   4092 H HA   . ASN   B 1 15  ? 33.211 -22.331 -15.266 1.00 15.25 ?  15  ASN   B HA   1 
ATOM   4093 H HB2  . ASN   B 1 15  ? 32.686 -21.079 -13.424 1.00 15.21 ?  15  ASN   B HB2  1 
ATOM   4094 H HB3  . ASN   B 1 15  ? 31.339 -21.342 -14.228 1.00 15.21 ?  15  ASN   B HB3  1 
ATOM   4095 H HD21 . ASN   B 1 15  ? 31.611 -22.310 -10.567 1.00 14.55 ?  15  ASN   B HD21 1 
ATOM   4096 H HD22 . ASN   B 1 15  ? 32.601 -21.447 -11.269 1.00 14.55 ?  15  ASN   B HD22 1 
ATOM   4097 N N    . VAL   B 1 16  ? 33.897 -24.790 -13.600 1.00 11.56 ?  16  VAL   B N    1 
ATOM   4098 C CA   . VAL   B 1 16  ? 34.893 -25.476 -12.782 1.00 11.13 ?  16  VAL   B CA   1 
ATOM   4099 C C    . VAL   B 1 16  ? 35.689 -26.421 -13.668 1.00 11.35 ?  16  VAL   B C    1 
ATOM   4100 O O    . VAL   B 1 16  ? 35.111 -27.293 -14.334 1.00 12.65 ?  16  VAL   B O    1 
ATOM   4101 C CB   . VAL   B 1 16  ? 34.253 -26.238 -11.607 1.00 11.77 ?  16  VAL   B CB   1 
ATOM   4102 C CG1  . VAL   B 1 16  ? 35.326 -26.976 -10.806 1.00 11.78 ?  16  VAL   B CG1  1 
ATOM   4103 C CG2  . VAL   B 1 16  ? 33.441 -25.293 -10.722 1.00 12.49 ?  16  VAL   B CG2  1 
ATOM   4104 H H    . VAL   B 1 16  ? 33.342 -25.323 -13.988 1.00 13.89 ?  16  VAL   B H    1 
ATOM   4105 H HA   . VAL   B 1 16  ? 35.507 -24.820 -12.416 1.00 13.38 ?  16  VAL   B HA   1 
ATOM   4106 H HB   . VAL   B 1 16  ? 33.648 -26.905 -11.966 1.00 14.15 ?  16  VAL   B HB   1 
ATOM   4107 H HG11 . VAL   B 1 16  ? 34.939 -27.278 -9.968  1.00 14.15 ?  16  VAL   B HG11 1 
ATOM   4108 H HG12 . VAL   B 1 16  ? 35.641 -27.740 -11.314 1.00 14.15 ?  16  VAL   B HG12 1 
ATOM   4109 H HG13 . VAL   B 1 16  ? 36.062 -26.370 -10.626 1.00 14.15 ?  16  VAL   B HG13 1 
ATOM   4110 H HG21 . VAL   B 1 16  ? 33.090 -25.793 -9.969  1.00 15.00 ?  16  VAL   B HG21 1 
ATOM   4111 H HG22 . VAL   B 1 16  ? 34.017 -24.581 -10.408 1.00 15.00 ?  16  VAL   B HG22 1 
ATOM   4112 H HG23 . VAL   B 1 16  ? 32.711 -24.924 -11.244 1.00 15.00 ?  16  VAL   B HG23 1 
ATOM   4113 N N    . TYR   B 1 17  ? 37.015 -26.264 -13.635 1.00 11.50 ?  17  TYR   B N    1 
ATOM   4114 C CA   . TYR   B 1 17  ? 37.964 -27.011 -14.448 1.00 12.03 ?  17  TYR   B CA   1 
ATOM   4115 C C    . TYR   B 1 17  ? 39.013 -27.619 -13.527 1.00 11.28 ?  17  TYR   B C    1 
ATOM   4116 O O    . TYR   B 1 17  ? 39.271 -27.088 -12.443 1.00 11.55 ?  17  TYR   B O    1 
ATOM   4117 C CB   . TYR   B 1 17  ? 38.666 -26.070 -15.439 1.00 13.77 ?  17  TYR   B CB   1 
ATOM   4118 C CG   . TYR   B 1 17  ? 37.730 -25.306 -16.342 1.00 16.72 ?  17  TYR   B CG   1 
ATOM   4119 C CD1  . TYR   B 1 17  ? 37.110 -24.136 -15.916 1.00 17.87 ?  17  TYR   B CD1  1 
ATOM   4120 C CD2  . TYR   B 1 17  ? 37.466 -25.754 -17.628 1.00 18.63 ?  17  TYR   B CD2  1 
ATOM   4121 C CE1  . TYR   B 1 17  ? 36.249 -23.436 -16.747 1.00 19.19 ?  17  TYR   B CE1  1 
ATOM   4122 C CE2  . TYR   B 1 17  ? 36.611 -25.063 -18.467 1.00 20.05 ?  17  TYR   B CE2  1 
ATOM   4123 C CZ   . TYR   B 1 17  ? 36.005 -23.909 -18.021 1.00 20.54 ?  17  TYR   B CZ   1 
ATOM   4124 O OH   . TYR   B 1 17  ? 35.157 -23.223 -18.855 1.00 21.93 ?  17  TYR   B OH   1 
ATOM   4125 H H    . TYR   B 1 17  ? 37.412 -25.694 -13.117 1.00 13.82 ?  17  TYR   B H    1 
ATOM   4126 H HA   . TYR   B 1 17  ? 37.509 -27.720 -14.935 1.00 14.46 ?  17  TYR   B HA   1 
ATOM   4127 H HB2  . TYR   B 1 17  ? 39.198 -25.429 -14.947 1.00 16.54 ?  17  TYR   B HB2  1 
ATOM   4128 H HB3  . TYR   B 1 17  ? 39.231 -26.602 -16.011 1.00 16.54 ?  17  TYR   B HB3  1 
ATOM   4129 H HD1  . TYR   B 1 17  ? 37.271 -23.818 -15.059 1.00 21.47 ?  17  TYR   B HD1  1 
ATOM   4130 H HD2  . TYR   B 1 17  ? 37.868 -26.533 -17.935 1.00 22.38 ?  17  TYR   B HD2  1 
ATOM   4131 H HE1  . TYR   B 1 17  ? 35.837 -22.654 -16.450 1.00 23.04 ?  17  TYR   B HE1  1 
ATOM   4132 H HE2  . TYR   B 1 17  ? 36.439 -25.378 -19.328 1.00 24.08 ?  17  TYR   B HE2  1 
ATOM   4133 H HH   . TYR   B 1 17  ? 35.091 -23.612 -19.596 1.00 26.33 ?  17  TYR   B HH   1 
ATOM   4134 N N    . ILE   B 1 18  ? 39.639 -28.719 -13.955 1.00 11.17 ?  18  ILE   B N    1 
ATOM   4135 C CA   . ILE   B 1 18  ? 40.563 -29.445 -13.084 1.00 11.06 ?  18  ILE   B CA   1 
ATOM   4136 C C    . ILE   B 1 18  ? 41.737 -29.993 -13.891 1.00 11.53 ?  18  ILE   B C    1 
ATOM   4137 O O    . ILE   B 1 18  ? 41.586 -30.398 -15.049 1.00 12.98 ?  18  ILE   B O    1 
ATOM   4138 C CB   . ILE   B 1 18  ? 39.815 -30.541 -12.286 1.00 11.60 ?  18  ILE   B CB   1 
ATOM   4139 C CG1  . ILE   B 1 18  ? 40.668 -31.090 -11.137 1.00 12.05 ?  18  ILE   B CG1  1 
ATOM   4140 C CG2  . ILE   B 1 18  ? 39.320 -31.654 -13.211 1.00 12.16 ?  18  ILE   B CG2  1 
ATOM   4141 C CD1  . ILE   B 1 18  ? 39.840 -31.894 -10.132 1.00 13.76 ?  18  ILE   B CD1  1 
ATOM   4142 H H    . ILE   B 1 18  ? 39.550 -29.064 -14.737 1.00 13.43 ?  18  ILE   B H    1 
ATOM   4143 H HA   . ILE   B 1 18  ? 40.924 -28.830 -12.430 1.00 13.29 ?  18  ILE   B HA   1 
ATOM   4144 H HB   . ILE   B 1 18  ? 39.028 -30.137 -11.889 1.00 13.93 ?  18  ILE   B HB   1 
ATOM   4145 H HG12 . ILE   B 1 18  ? 41.352 -31.673 -11.493 1.00 14.48 ?  18  ILE   B HG12 1 
ATOM   4146 H HG13 . ILE   B 1 18  ? 41.070 -30.347 -10.661 1.00 14.48 ?  18  ILE   B HG13 1 
ATOM   4147 H HG21 . ILE   B 1 18  ? 38.726 -32.244 -12.714 1.00 14.61 ?  18  ILE   B HG21 1 
ATOM   4148 H HG22 . ILE   B 1 18  ? 38.844 -31.258 -13.953 1.00 14.61 ?  18  ILE   B HG22 1 
ATOM   4149 H HG23 . ILE   B 1 18  ? 40.083 -32.160 -13.536 1.00 14.61 ?  18  ILE   B HG23 1 
ATOM   4150 H HD11 . ILE   B 1 18  ? 40.411 -32.167 -9.397  1.00 16.54 ?  18  ILE   B HD11 1 
ATOM   4151 H HD12 . ILE   B 1 18  ? 39.116 -31.339 -9.799  1.00 16.54 ?  18  ILE   B HD12 1 
ATOM   4152 H HD13 . ILE   B 1 18  ? 39.476 -32.677 -10.575 1.00 16.54 ?  18  ILE   B HD13 1 
ATOM   4153 N N    A LYS   B 1 19  ? 42.912 -30.017 -13.263 0.50 11.87 ?  19  LYS   B N    1 
ATOM   4154 N N    B LYS   B 1 19  ? 42.917 -30.007 -13.267 0.50 11.73 ?  19  LYS   B N    1 
ATOM   4155 C CA   A LYS   B 1 19  ? 44.126 -30.486 -13.915 0.50 12.55 ?  19  LYS   B CA   1 
ATOM   4156 C CA   B LYS   B 1 19  ? 44.132 -30.491 -13.908 0.50 12.28 ?  19  LYS   B CA   1 
ATOM   4157 C C    A LYS   B 1 19  ? 45.020 -31.160 -12.884 0.50 12.32 ?  19  LYS   B C    1 
ATOM   4158 C C    B LYS   B 1 19  ? 45.009 -31.174 -12.871 0.50 12.23 ?  19  LYS   B C    1 
ATOM   4159 O O    A LYS   B 1 19  ? 45.100 -30.714 -11.738 0.50 12.10 ?  19  LYS   B O    1 
ATOM   4160 O O    B LYS   B 1 19  ? 45.070 -30.755 -11.713 0.50 12.20 ?  19  LYS   B O    1 
ATOM   4161 C CB   A LYS   B 1 19  ? 44.883 -29.310 -14.552 0.50 14.00 ?  19  LYS   B CB   1 
ATOM   4162 C CB   B LYS   B 1 19  ? 44.922 -29.340 -14.554 0.50 13.35 ?  19  LYS   B CB   1 
ATOM   4163 C CG   A LYS   B 1 19  ? 46.073 -29.704 -15.408 0.50 15.59 ?  19  LYS   B CG   1 
ATOM   4164 C CG   B LYS   B 1 19  ? 46.192 -29.758 -15.288 0.50 14.70 ?  19  LYS   B CG   1 
ATOM   4165 C CD   A LYS   B 1 19  ? 46.768 -28.469 -15.966 0.50 17.03 ?  19  LYS   B CD   1 
ATOM   4166 C CD   B LYS   B 1 19  ? 46.928 -28.540 -15.839 0.50 16.22 ?  19  LYS   B CD   1 
ATOM   4167 C CE   A LYS   B 1 19  ? 47.945 -28.840 -16.847 0.50 18.65 ?  19  LYS   B CE   1 
ATOM   4168 C CE   B LYS   B 1 19  ? 48.105 -28.937 -16.715 0.50 17.99 ?  19  LYS   B CE   1 
ATOM   4169 N NZ   A LYS   B 1 19  ? 48.695 -27.639 -17.304 0.50 19.48 ?  19  LYS   B NZ   1 
ATOM   4170 N NZ   B LYS   B 1 19  ? 48.845 -27.749 -17.228 0.50 18.85 ?  19  LYS   B NZ   1 
ATOM   4171 H H    A LYS   B 1 19  ? 43.031 -29.758 -12.448 0.50 14.26 ?  19  LYS   B H    1 
ATOM   4172 H H    B LYS   B 1 19  ? 43.036 -29.736 -12.455 0.50 14.10 ?  19  LYS   B H    1 
ATOM   4173 H HA   A LYS   B 1 19  ? 43.902 -31.126 -14.607 0.50 15.08 ?  19  LYS   B HA   1 
ATOM   4174 H HA   B LYS   B 1 19  ? 43.905 -31.135 -14.593 0.50 14.75 ?  19  LYS   B HA   1 
ATOM   4175 H HB2  A LYS   B 1 19  ? 44.268 -28.816 -15.117 0.50 16.82 ?  19  LYS   B HB2  1 
ATOM   4176 H HB2  B LYS   B 1 19  ? 44.347 -28.899 -15.198 0.50 16.04 ?  19  LYS   B HB2  1 
ATOM   4177 H HB3  A LYS   B 1 19  ? 45.208 -28.730 -13.843 0.50 16.82 ?  19  LYS   B HB3  1 
ATOM   4178 H HB3  B LYS   B 1 19  ? 45.176 -28.709 -13.861 0.50 16.04 ?  19  LYS   B HB3  1 
ATOM   4179 H HG2  A LYS   B 1 19  ? 46.709 -30.197 -14.869 0.50 18.73 ?  19  LYS   B HG2  1 
ATOM   4180 H HG2  B LYS   B 1 19  ? 46.784 -30.220 -14.676 0.50 17.66 ?  19  LYS   B HG2  1 
ATOM   4181 H HG3  A LYS   B 1 19  ? 45.766 -30.246 -16.152 0.50 18.73 ?  19  LYS   B HG3  1 
ATOM   4182 H HG3  B LYS   B 1 19  ? 45.956 -30.335 -16.032 0.50 17.66 ?  19  LYS   B HG3  1 
ATOM   4183 H HD2  A LYS   B 1 19  ? 46.136 -27.959 -16.499 0.50 20.45 ?  19  LYS   B HD2  1 
ATOM   4184 H HD2  B LYS   B 1 19  ? 46.315 -28.013 -16.375 0.50 19.48 ?  19  LYS   B HD2  1 
ATOM   4185 H HD3  A LYS   B 1 19  ? 47.096 -27.927 -15.230 0.50 20.45 ?  19  LYS   B HD3  1 
ATOM   4186 H HD3  B LYS   B 1 19  ? 47.265 -28.009 -15.099 0.50 19.48 ?  19  LYS   B HD3  1 
ATOM   4187 H HE2  A LYS   B 1 19  ? 48.552 -29.407 -16.345 0.50 22.39 ?  19  LYS   B HE2  1 
ATOM   4188 H HE2  B LYS   B 1 19  ? 48.720 -29.477 -16.195 0.50 21.61 ?  19  LYS   B HE2  1 
ATOM   4189 H HE3  A LYS   B 1 19  ? 47.619 -29.313 -17.630 0.50 22.39 ?  19  LYS   B HE3  1 
ATOM   4190 H HE3  B LYS   B 1 19  ? 47.778 -29.443 -17.476 0.50 21.61 ?  19  LYS   B HE3  1 
ATOM   4191 H HZ1  A LYS   B 1 19  ? 49.346 -27.882 -17.860 0.50 23.40 ?  19  LYS   B HZ1  1 
ATOM   4192 H HZ1  B LYS   B 1 19  ? 49.495 -28.009 -17.776 0.50 22.64 ?  19  LYS   B HZ1  1 
ATOM   4193 H HZ2  A LYS   B 1 19  ? 48.146 -27.081 -17.727 0.50 23.40 ?  19  LYS   B HZ2  1 
ATOM   4194 H HZ2  B LYS   B 1 19  ? 48.289 -27.214 -17.672 0.50 22.64 ?  19  LYS   B HZ2  1 
ATOM   4195 H HZ3  A LYS   B 1 19  ? 49.052 -27.221 -16.605 0.50 23.40 ?  19  LYS   B HZ3  1 
ATOM   4196 H HZ3  B LYS   B 1 19  ? 49.200 -27.297 -16.550 0.50 22.64 ?  19  LYS   B HZ3  1 
ATOM   4197 N N    . ASN   B 1 20  ? 45.708 -32.219 -13.306 1.00 12.89 ?  20  ASN   B N    1 
ATOM   4198 C CA   . ASN   B 1 20  ? 46.732 -32.852 -12.481 1.00 13.83 ?  20  ASN   B CA   1 
ATOM   4199 C C    . ASN   B 1 20  ? 48.007 -32.035 -12.670 1.00 14.37 ?  20  ASN   B C    1 
ATOM   4200 O O    . ASN   B 1 20  ? 48.659 -32.116 -13.716 1.00 16.57 ?  20  ASN   B O    1 
ATOM   4201 C CB   . ASN   B 1 20  ? 46.905 -34.307 -12.908 1.00 15.25 ?  20  ASN   B CB   1 
ATOM   4202 C CG   . ASN   B 1 20  ? 48.073 -35.004 -12.228 1.00 16.68 ?  20  ASN   B CG   1 
ATOM   4203 O OD1  . ASN   B 1 20  ? 48.729 -35.862 -12.829 1.00 19.33 ?  20  ASN   B OD1  1 
ATOM   4204 N ND2  . ASN   B 1 20  ? 48.326 -34.665 -10.974 1.00 16.03 ?  20  ASN   B ND2  1 
ATOM   4205 H H    A ASN   B 1 20  ? 45.605 -32.584 -14.074 0.50 15.49 ?  20  ASN   B H    1 
ATOM   4206 H H    B ASN   B 1 20  ? 45.610 -32.574 -14.079 0.50 15.49 ?  20  ASN   B H    1 
ATOM   4207 H HA   . ASN   B 1 20  ? 46.455 -32.825 -11.547 1.00 16.62 ?  20  ASN   B HA   1 
ATOM   4208 H HB2  . ASN   B 1 20  ? 46.096 -34.797 -12.682 1.00 18.32 ?  20  ASN   B HB2  1 
ATOM   4209 H HB3  . ASN   B 1 20  ? 47.051 -34.333 -13.863 1.00 18.32 ?  20  ASN   B HB3  1 
ATOM   4210 H HD21 . ASN   B 1 20  ? 48.982 -35.026 -10.557 1.00 19.25 ?  20  ASN   B HD21 1 
ATOM   4211 H HD22 . ASN   B 1 20  ? 47.845 -34.067 -10.576 1.00 19.25 ?  20  ASN   B HD22 1 
ATOM   4212 N N    . ALA   B 1 21  ? 48.346 -31.212 -11.674 1.00 14.22 ?  21  ALA   B N    1 
ATOM   4213 C CA   . ALA   B 1 21  ? 49.454 -30.280 -11.816 1.00 14.94 ?  21  ALA   B CA   1 
ATOM   4214 C C    . ALA   B 1 21  ? 49.901 -29.786 -10.450 1.00 14.12 ?  21  ALA   B C    1 
ATOM   4215 O O    . ALA   B 1 21  ? 49.150 -29.820 -9.470  1.00 14.23 ?  21  ALA   B O    1 
ATOM   4216 C CB   . ALA   B 1 21  ? 49.072 -29.093 -12.702 1.00 16.47 ?  21  ALA   B CB   1 
ATOM   4217 H H    . ALA   B 1 21  ? 47.942 -31.173 -10.906 1.00 17.08 ?  21  ALA   B H    1 
ATOM   4218 H HA   . ALA   B 1 21  ? 50.196 -30.743 -12.227 1.00 17.95 ?  21  ALA   B HA   1 
ATOM   4219 H HB1  . ALA   B 1 21  ? 49.860 -28.550 -12.842 1.00 19.79 ?  21  ALA   B HB1  1 
ATOM   4220 H HB2  . ALA   B 1 21  ? 48.744 -29.432 -13.548 1.00 19.79 ?  21  ALA   B HB2  1 
ATOM   4221 H HB3  . ALA   B 1 21  ? 48.380 -28.578 -12.259 1.00 19.79 ?  21  ALA   B HB3  1 
ATOM   4222 N N    . ASP   B 1 22  ? 51.156 -29.336 -10.420 1.00 14.02 ?  22  ASP   B N    1 
ATOM   4223 C CA   . ASP   B 1 22  ? 51.755 -28.637 -9.291  1.00 13.68 ?  22  ASP   B CA   1 
ATOM   4224 C C    . ASP   B 1 22  ? 51.349 -27.166 -9.391  1.00 12.34 ?  22  ASP   B C    1 
ATOM   4225 O O    . ASP   B 1 22  ? 51.671 -26.501 -10.380 1.00 12.74 ?  22  ASP   B O    1 
ATOM   4226 C CB   . ASP   B 1 22  ? 53.272 -28.815 -9.439  1.00 15.32 ?  22  ASP   B CB   1 
ATOM   4227 C CG   . ASP   B 1 22  ? 54.098 -28.047 -8.415  1.00 17.21 ?  22  ASP   B CG   1 
ATOM   4228 O OD1  . ASP   B 1 22  ? 53.724 -26.931 -8.014  1.00 17.49 ?  22  ASP   B OD1  1 
ATOM   4229 O OD2  . ASP   B 1 22  ? 55.181 -28.555 -8.045  1.00 19.56 -1 22  ASP   B OD2  1 
ATOM   4230 H H    . ASP   B 1 22  ? 51.708 -29.439 -11.075 1.00 16.84 ?  22  ASP   B H    1 
ATOM   4231 H HA   . ASP   B 1 22  ? 51.462 -29.018 -8.445  1.00 16.44 ?  22  ASP   B HA   1 
ATOM   4232 H HB2  . ASP   B 1 22  ? 53.494 -29.754 -9.351  1.00 18.40 ?  22  ASP   B HB2  1 
ATOM   4233 H HB3  . ASP   B 1 22  ? 53.538 -28.498 -10.319 1.00 18.40 ?  22  ASP   B HB3  1 
ATOM   4234 N N    . ILE   B 1 23  ? 50.628 -26.665 -8.380  1.00 11.77 ?  23  ILE   B N    1 
ATOM   4235 C CA   . ILE   B 1 23  ? 50.039 -25.327 -8.464  1.00 11.06 ?  23  ILE   B CA   1 
ATOM   4236 C C    . ILE   B 1 23  ? 51.097 -24.240 -8.606  1.00 11.21 ?  23  ILE   B C    1 
ATOM   4237 O O    . ILE   B 1 23  ? 50.830 -23.198 -9.213  1.00 10.59 ?  23  ILE   B O    1 
ATOM   4238 C CB   . ILE   B 1 23  ? 49.087 -25.078 -7.275  1.00 11.61 ?  23  ILE   B CB   1 
ATOM   4239 C CG1  . ILE   B 1 23  ? 48.249 -23.816 -7.493  1.00 12.32 ?  23  ILE   B CG1  1 
ATOM   4240 C CG2  . ILE   B 1 23  ? 49.844 -25.026 -5.963  1.00 12.83 ?  23  ILE   B CG2  1 
ATOM   4241 C CD1  . ILE   B 1 23  ? 47.139 -23.643 -6.472  1.00 13.03 ?  23  ILE   B CD1  1 
ATOM   4242 H H    . ILE   B 1 23  ? 50.467 -27.082 -7.643  1.00 14.14 ?  23  ILE   B H    1 
ATOM   4243 H HA   . ILE   B 1 23  ? 49.498 -25.297 -9.267  1.00 13.29 ?  23  ILE   B HA   1 
ATOM   4244 H HB   . ILE   B 1 23  ? 48.470 -25.827 -7.233  1.00 13.96 ?  23  ILE   B HB   1 
ATOM   4245 H HG12 . ILE   B 1 23  ? 48.832 -23.038 -7.436  1.00 14.80 ?  23  ILE   B HG12 1 
ATOM   4246 H HG13 . ILE   B 1 23  ? 47.843 -23.851 -8.376  1.00 14.80 ?  23  ILE   B HG13 1 
ATOM   4247 H HG21 . ILE   B 1 23  ? 49.207 -25.037 -5.233  1.00 15.42 ?  23  ILE   B HG21 1 
ATOM   4248 H HG22 . ILE   B 1 23  ? 50.427 -25.797 -5.909  1.00 15.42 ?  23  ILE   B HG22 1 
ATOM   4249 H HG23 . ILE   B 1 23  ? 50.367 -24.210 -5.936  1.00 15.42 ?  23  ILE   B HG23 1 
ATOM   4250 H HD11 . ILE   B 1 23  ? 46.596 -22.881 -6.723  1.00 15.66 ?  23  ILE   B HD11 1 
ATOM   4251 H HD12 . ILE   B 1 23  ? 46.598 -24.448 -6.463  1.00 15.66 ?  23  ILE   B HD12 1 
ATOM   4252 H HD13 . ILE   B 1 23  ? 47.535 -23.499 -5.600  1.00 15.66 ?  23  ILE   B HD13 1 
ATOM   4253 N N    . VAL   B 1 24  ? 52.294 -24.444 -8.044  1.00 11.33 ?  24  VAL   B N    1 
ATOM   4254 C CA   . VAL   B 1 24  ? 53.366 -23.461 -8.211  1.00 11.76 ?  24  VAL   B CA   1 
ATOM   4255 C C    . VAL   B 1 24  ? 53.818 -23.417 -9.663  1.00 11.99 ?  24  VAL   B C    1 
ATOM   4256 O O    . VAL   B 1 24  ? 53.956 -22.341 -10.263 1.00 12.43 ?  24  VAL   B O    1 
ATOM   4257 C CB   . VAL   B 1 24  ? 54.547 -23.775 -7.272  1.00 12.87 ?  24  VAL   B CB   1 
ATOM   4258 C CG1  . VAL   B 1 24  ? 55.757 -22.908 -7.628  1.00 13.45 ?  24  VAL   B CG1  1 
ATOM   4259 C CG2  . VAL   B 1 24  ? 54.146 -23.557 -5.833  1.00 14.08 ?  24  VAL   B CG2  1 
ATOM   4260 H H    . VAL   B 1 24  ? 52.503 -25.133 -7.566  1.00 13.62 ?  24  VAL   B H    1 
ATOM   4261 H HA   . VAL   B 1 24  ? 53.027 -22.589 -7.976  1.00 14.13 ?  24  VAL   B HA   1 
ATOM   4262 H HB   . VAL   B 1 24  ? 54.802 -24.707 -7.372  1.00 15.47 ?  24  VAL   B HB   1 
ATOM   4263 H HG11 . VAL   B 1 24  ? 56.355 -22.868 -6.862  1.00 16.16 ?  24  VAL   B HG11 1 
ATOM   4264 H HG12 . VAL   B 1 24  ? 56.221 -23.304 -8.382  1.00 16.16 ?  24  VAL   B HG12 1 
ATOM   4265 H HG13 . VAL   B 1 24  ? 55.454 -22.014 -7.852  1.00 16.16 ?  24  VAL   B HG13 1 
ATOM   4266 H HG21 . VAL   B 1 24  ? 54.878 -23.824 -5.255  1.00 16.91 ?  24  VAL   B HG21 1 
ATOM   4267 H HG22 . VAL   B 1 24  ? 53.947 -22.617 -5.702  1.00 16.91 ?  24  VAL   B HG22 1 
ATOM   4268 H HG23 . VAL   B 1 24  ? 53.360 -24.092 -5.638  1.00 16.91 ?  24  VAL   B HG23 1 
ATOM   4269 N N    . GLU   B 1 25  ? 54.077 -24.590 -10.244 1.00 12.81 ?  25  GLU   B N    1 
ATOM   4270 C CA   . GLU   B 1 25  ? 54.466 -24.640 -11.647 1.00 14.04 ?  25  GLU   B CA   1 
ATOM   4271 C C    . GLU   B 1 25  ? 53.365 -24.086 -12.537 1.00 13.19 ?  25  GLU   B C    1 
ATOM   4272 O O    . GLU   B 1 25  ? 53.640 -23.371 -13.510 1.00 14.05 ?  25  GLU   B O    1 
ATOM   4273 C CB   . GLU   B 1 25  ? 54.832 -26.074 -12.030 1.00 17.31 ?  25  GLU   B CB   1 
ATOM   4274 C CG   . GLU   B 1 25  ? 56.129 -26.542 -11.391 1.00 22.22 ?  25  GLU   B CG   1 
ATOM   4275 C CD   . GLU   B 1 25  ? 57.249 -25.517 -11.495 1.00 27.24 ?  25  GLU   B CD   1 
ATOM   4276 O OE1  . GLU   B 1 25  ? 57.609 -25.134 -12.629 1.00 29.09 ?  25  GLU   B OE1  1 
ATOM   4277 O OE2  . GLU   B 1 25  ? 57.759 -25.076 -10.439 1.00 29.10 -1 25  GLU   B OE2  1 
ATOM   4278 H H    . GLU   B 1 25  ? 54.035 -25.360 -9.850  1.00 15.39 ?  25  GLU   B H    1 
ATOM   4279 H HA   . GLU   B 1 25  ? 55.235 -24.073 -11.775 1.00 16.87 ?  25  GLU   B HA   1 
ATOM   4280 H HB2  . GLU   B 1 25  ? 54.125 -26.675 -11.735 1.00 20.79 ?  25  GLU   B HB2  1 
ATOM   4281 H HB3  . GLU   B 1 25  ? 54.931 -26.132 -12.992 1.00 20.79 ?  25  GLU   B HB3  1 
ATOM   4282 H HG2  . GLU   B 1 25  ? 55.981 -26.707 -10.452 1.00 26.68 ?  25  GLU   B HG2  1 
ATOM   4283 H HG3  . GLU   B 1 25  ? 56.427 -27.351 -11.836 1.00 26.68 ?  25  GLU   B HG3  1 
ATOM   4284 N N    . GLU   B 1 26  ? 52.110 -24.397 -12.210 1.00 12.57 ?  26  GLU   B N    1 
ATOM   4285 C CA   . GLU   B 1 26  ? 50.984 -23.865 -12.970 1.00 12.89 ?  26  GLU   B CA   1 
ATOM   4286 C C    . GLU   B 1 26  ? 50.943 -22.348 -12.893 1.00 12.33 ?  26  GLU   B C    1 
ATOM   4287 O O    . GLU   B 1 26  ? 50.735 -21.673 -13.906 1.00 13.66 ?  26  GLU   B O    1 
ATOM   4288 C CB   . GLU   B 1 26  ? 49.669 -24.440 -12.441 1.00 14.73 ?  26  GLU   B CB   1 
ATOM   4289 C CG   . GLU   B 1 26  ? 49.257 -25.745 -13.072 1.00 18.02 ?  26  GLU   B CG   1 
ATOM   4290 C CD   . GLU   B 1 26  ? 49.034 -25.641 -14.572 1.00 19.54 ?  26  GLU   B CD   1 
ATOM   4291 O OE1  . GLU   B 1 26  ? 48.084 -24.959 -15.017 1.00 19.97 ?  26  GLU   B OE1  1 
ATOM   4292 O OE2  . GLU   B 1 26  ? 49.811 -26.266 -15.308 1.00 21.50 -1 26  GLU   B OE2  1 
ATOM   4293 H H    . GLU   B 1 26  ? 51.882 -24.915 -11.555 1.00 15.10 ?  26  GLU   B H    1 
ATOM   4294 H HA   . GLU   B 1 26  ? 51.079 -24.118 -13.898 1.00 15.49 ?  26  GLU   B HA   1 
ATOM   4295 H HB2  . GLU   B 1 26  ? 49.753 -24.592 -11.487 1.00 17.70 ?  26  GLU   B HB2  1 
ATOM   4296 H HB3  . GLU   B 1 26  ? 48.959 -23.798 -12.606 1.00 17.70 ?  26  GLU   B HB3  1 
ATOM   4297 H HG2  . GLU   B 1 26  ? 49.955 -26.394 -12.920 1.00 21.64 ?  26  GLU   B HG2  1 
ATOM   4298 H HG3  . GLU   B 1 26  ? 48.425 -26.043 -12.673 1.00 21.64 ?  26  GLU   B HG3  1 
ATOM   4299 N N    . ALA   B 1 27  ? 51.095 -21.795 -11.688 1.00 11.65 ?  27  ALA   B N    1 
ATOM   4300 C CA   . ALA   B 1 27  ? 51.049 -20.343 -11.548 1.00 12.20 ?  27  ALA   B CA   1 
ATOM   4301 C C    . ALA   B 1 27  ? 52.120 -19.682 -12.405 1.00 13.02 ?  27  ALA   B C    1 
ATOM   4302 O O    . ALA   B 1 27  ? 51.862 -18.674 -13.082 1.00 13.52 ?  27  ALA   B O    1 
ATOM   4303 C CB   . ALA   B 1 27  ? 51.199 -19.947 -10.078 1.00 12.36 ?  27  ALA   B CB   1 
ATOM   4304 H H    . ALA   B 1 27  ? 51.216 -22.229 -10.952 1.00 14.01 ?  27  ALA   B H    1 
ATOM   4305 H HA   . ALA   B 1 27  ? 50.189 -20.024 -11.852 1.00 14.66 ?  27  ALA   B HA   1 
ATOM   4306 H HB1  . ALA   B 1 27  ? 51.158 -18.981 -10.005 1.00 14.86 ?  27  ALA   B HB1  1 
ATOM   4307 H HB2  . ALA   B 1 27  ? 50.469 -20.345 -9.570  1.00 14.86 ?  27  ALA   B HB2  1 
ATOM   4308 H HB3  . ALA   B 1 27  ? 52.047 -20.271 -9.744  1.00 14.86 ?  27  ALA   B HB3  1 
ATOM   4309 N N    . LYS   B 1 28  ? 53.332 -20.237 -12.391 1.00 14.21 ?  28  LYS   B N    1 
ATOM   4310 C CA   . LYS   B 1 28  ? 54.411 -19.626 -13.160 1.00 16.87 ?  28  LYS   B CA   1 
ATOM   4311 C C    . LYS   B 1 28  ? 54.145 -19.692 -14.659 1.00 17.68 ?  28  LYS   B C    1 
ATOM   4312 O O    . LYS   B 1 28  ? 54.565 -18.793 -15.399 1.00 18.70 ?  28  LYS   B O    1 
ATOM   4313 C CB   . LYS   B 1 28  ? 55.765 -20.237 -12.783 1.00 20.33 ?  28  LYS   B CB   1 
ATOM   4314 C CG   . LYS   B 1 28  ? 56.173 -19.914 -11.348 1.00 23.52 ?  28  LYS   B CG   1 
ATOM   4315 C CD   . LYS   B 1 28  ? 57.595 -20.341 -11.016 1.00 28.09 ?  28  LYS   B CD   1 
ATOM   4316 C CE   . LYS   B 1 28  ? 57.680 -21.819 -10.707 1.00 32.39 ?  28  LYS   B CE   1 
ATOM   4317 N NZ   . LYS   B 1 28  ? 59.027 -22.197 -10.192 1.00 34.20 ?  28  LYS   B NZ   1 
ATOM   4318 H H    . LYS   B 1 28  ? 53.557 -20.938 -11.945 1.00 17.08 ?  28  LYS   B H    1 
ATOM   4319 H HA   . LYS   B 1 28  ? 54.456 -18.685 -12.928 1.00 20.27 ?  28  LYS   B HA   1 
ATOM   4320 H HB2  . LYS   B 1 28  ? 55.717 -21.200 -12.871 1.00 24.42 ?  28  LYS   B HB2  1 
ATOM   4321 H HB3  . LYS   B 1 28  ? 56.451 -19.882 -13.374 1.00 24.42 ?  28  LYS   B HB3  1 
ATOM   4322 H HG2  . LYS   B 1 28  ? 56.106 -18.955 -11.213 1.00 28.24 ?  28  LYS   B HG2  1 
ATOM   4323 H HG3  . LYS   B 1 28  ? 55.571 -20.375 -10.743 1.00 28.24 ?  28  LYS   B HG3  1 
ATOM   4324 H HD2  . LYS   B 1 28  ? 58.168 -20.152 -11.776 1.00 33.73 ?  28  LYS   B HD2  1 
ATOM   4325 H HD3  . LYS   B 1 28  ? 57.898 -19.846 -10.238 1.00 33.73 ?  28  LYS   B HD3  1 
ATOM   4326 H HE2  . LYS   B 1 28  ? 57.022 -22.041 -10.030 1.00 38.89 ?  28  LYS   B HE2  1 
ATOM   4327 H HE3  . LYS   B 1 28  ? 57.511 -22.325 -11.517 1.00 38.89 ?  28  LYS   B HE3  1 
ATOM   4328 H HZ1  . LYS   B 1 28  ? 59.053 -23.069 -10.017 1.00 41.06 ?  28  LYS   B HZ1  1 
ATOM   4329 H HZ2  . LYS   B 1 28  ? 59.650 -22.005 -10.798 1.00 41.06 ?  28  LYS   B HZ2  1 
ATOM   4330 H HZ3  . LYS   B 1 28  ? 59.204 -21.748 -9.443  1.00 41.06 ?  28  LYS   B HZ3  1 
ATOM   4331 N N    A LYS   B 1 29  ? 53.442 -20.727 -15.123 0.50 18.48 ?  29  LYS   B N    1 
ATOM   4332 N N    B LYS   B 1 29  ? 53.431 -20.719 -15.119 0.50 18.48 ?  29  LYS   B N    1 
ATOM   4333 C CA   A LYS   B 1 29  ? 53.159 -20.872 -16.548 0.50 20.50 ?  29  LYS   B CA   1 
ATOM   4334 C CA   B LYS   B 1 29  ? 53.161 -20.865 -16.544 0.50 20.47 ?  29  LYS   B CA   1 
ATOM   4335 C C    A LYS   B 1 29  ? 51.901 -20.128 -16.989 0.50 19.43 ?  29  LYS   B C    1 
ATOM   4336 C C    B LYS   B 1 29  ? 51.901 -20.127 -16.990 0.50 19.40 ?  29  LYS   B C    1 
ATOM   4337 O O    A LYS   B 1 29  ? 51.892 -19.518 -18.063 0.50 20.29 ?  29  LYS   B O    1 
ATOM   4338 O O    B LYS   B 1 29  ? 51.890 -19.521 -18.066 0.50 20.26 ?  29  LYS   B O    1 
ATOM   4339 C CB   A LYS   B 1 29  ? 53.040 -22.354 -16.918 0.50 24.15 ?  29  LYS   B CB   1 
ATOM   4340 C CB   B LYS   B 1 29  ? 53.053 -22.348 -16.904 0.50 24.07 ?  29  LYS   B CB   1 
ATOM   4341 C CG   A LYS   B 1 29  ? 52.784 -22.598 -18.398 0.50 27.36 ?  29  LYS   B CG   1 
ATOM   4342 C CG   B LYS   B 1 29  ? 52.864 -22.617 -18.385 0.50 27.21 ?  29  LYS   B CG   1 
ATOM   4343 C CD   A LYS   B 1 29  ? 52.990 -24.060 -18.767 0.50 29.79 ?  29  LYS   B CD   1 
ATOM   4344 C CD   B LYS   B 1 29  ? 53.157 -24.072 -18.730 0.50 29.56 ?  29  LYS   B CD   1 
ATOM   4345 C CE   A LYS   B 1 29  ? 51.920 -24.952 -18.158 0.50 31.36 ?  29  LYS   B CE   1 
ATOM   4346 C CE   B LYS   B 1 29  ? 52.140 -25.021 -18.112 0.50 31.09 ?  29  LYS   B CE   1 
ATOM   4347 N NZ   A LYS   B 1 29  ? 52.110 -26.378 -18.549 0.50 32.38 ?  29  LYS   B NZ   1 
ATOM   4348 N NZ   B LYS   B 1 29  ? 52.400 -26.438 -18.501 0.50 32.06 ?  29  LYS   B NZ   1 
ATOM   4349 H H    A LYS   B 1 29  ? 53.121 -21.359 -14.628 0.50 22.19 ?  29  LYS   B H    1 
ATOM   4350 H H    B LYS   B 1 29  ? 53.091 -21.340 -14.621 0.50 22.20 ?  29  LYS   B H    1 
ATOM   4351 H HA   A LYS   B 1 29  ? 53.904 -20.507 -17.043 0.50 24.62 ?  29  LYS   B HA   1 
ATOM   4352 H HA   B LYS   B 1 29  ? 53.907 -20.496 -17.034 0.50 24.58 ?  29  LYS   B HA   1 
ATOM   4353 H HB2  A LYS   B 1 29  ? 53.869 -22.802 -16.684 0.50 29.00 ?  29  LYS   B HB2  1 
ATOM   4354 H HB2  B LYS   B 1 29  ? 53.871 -22.790 -16.626 0.50 28.91 ?  29  LYS   B HB2  1 
ATOM   4355 H HB3  A LYS   B 1 29  ? 52.305 -22.744 -16.422 0.50 29.00 ?  29  LYS   B HB3  1 
ATOM   4356 H HB3  B LYS   B 1 29  ? 52.297 -22.727 -16.434 0.50 28.91 ?  29  LYS   B HB3  1 
ATOM   4357 H HG2  A LYS   B 1 29  ? 51.868 -22.359 -18.609 0.50 32.85 ?  29  LYS   B HG2  1 
ATOM   4358 H HG2  B LYS   B 1 29  ? 51.945 -22.425 -18.628 0.50 32.68 ?  29  LYS   B HG2  1 
ATOM   4359 H HG3  A LYS   B 1 29  ? 53.400 -22.063 -18.924 0.50 32.85 ?  29  LYS   B HG3  1 
ATOM   4360 H HG3  B LYS   B 1 29  ? 53.470 -22.055 -18.893 0.50 32.68 ?  29  LYS   B HG3  1 
ATOM   4361 H HD2  A LYS   B 1 29  ? 52.951 -24.156 -19.731 0.50 35.76 ?  29  LYS   B HD2  1 
ATOM   4362 H HD2  B LYS   B 1 29  ? 53.128 -24.184 -19.692 0.50 35.50 ?  29  LYS   B HD2  1 
ATOM   4363 H HD3  A LYS   B 1 29  ? 53.853 -24.355 -18.435 0.50 35.76 ?  29  LYS   B HD3  1 
ATOM   4364 H HD3  B LYS   B 1 29  ? 54.035 -24.310 -18.391 0.50 35.50 ?  29  LYS   B HD3  1 
ATOM   4365 H HE2  A LYS   B 1 29  ? 51.965 -24.894 -17.191 0.50 37.66 ?  29  LYS   B HE2  1 
ATOM   4366 H HE2  B LYS   B 1 29  ? 52.188 -24.959 -17.145 0.50 37.33 ?  29  LYS   B HE2  1 
ATOM   4367 H HE3  A LYS   B 1 29  ? 51.048 -24.663 -18.471 0.50 37.66 ?  29  LYS   B HE3  1 
ATOM   4368 H HE3  B LYS   B 1 29  ? 51.251 -24.780 -18.419 0.50 37.33 ?  29  LYS   B HE3  1 
ATOM   4369 H HZ1  A LYS   B 1 29  ? 51.474 -26.881 -18.183 0.50 38.87 ?  29  LYS   B HZ1  1 
ATOM   4370 H HZ1  B LYS   B 1 29  ? 51.793 -26.973 -18.129 0.50 38.49 ?  29  LYS   B HZ1  1 
ATOM   4371 H HZ2  A LYS   B 1 29  ? 52.069 -26.459 -19.434 0.50 38.87 ?  29  LYS   B HZ2  1 
ATOM   4372 H HZ2  B LYS   B 1 29  ? 52.357 -26.524 -19.386 0.50 38.49 ?  29  LYS   B HZ2  1 
ATOM   4373 H HZ3  A LYS   B 1 29  ? 52.904 -26.667 -18.269 0.50 38.87 ?  29  LYS   B HZ3  1 
ATOM   4374 H HZ3  B LYS   B 1 29  ? 53.210 -26.686 -18.226 0.50 38.49 ?  29  LYS   B HZ3  1 
ATOM   4375 N N    . VAL   B 1 30  ? 50.837 -20.176 -16.185 1.00 18.10 ?  30  VAL   B N    1 
ATOM   4376 C CA   . VAL   B 1 30  ? 49.553 -19.580 -16.569 1.00 17.72 ?  30  VAL   B CA   1 
ATOM   4377 C C    . VAL   B 1 30  ? 49.545 -18.066 -16.407 1.00 16.66 ?  30  VAL   B C    1 
ATOM   4378 O O    . VAL   B 1 30  ? 48.816 -17.359 -17.117 1.00 17.90 ?  30  VAL   B O    1 
ATOM   4379 C CB   . VAL   B 1 30  ? 48.455 -20.203 -15.684 1.00 18.51 ?  30  VAL   B CB   1 
ATOM   4380 C CG1  . VAL   B 1 30  ? 47.172 -19.378 -15.724 1.00 18.67 ?  30  VAL   B CG1  1 
ATOM   4381 C CG2  . VAL   B 1 30  ? 48.196 -21.646 -16.084 1.00 19.32 ?  30  VAL   B CG2  1 
ATOM   4382 H H    A VAL   B 1 30  ? 50.827 -20.557 -15.409 0.50 21.74 ?  30  VAL   B H    1 
ATOM   4383 H H    B VAL   B 1 30  ? 50.823 -20.573 -15.417 0.50 21.74 ?  30  VAL   B H    1 
ATOM   4384 H HA   . VAL   B 1 30  ? 49.360 -19.810 -17.494 1.00 21.28 ?  30  VAL   B HA   1 
ATOM   4385 H HB   . VAL   B 1 30  ? 48.766 -20.215 -14.766 1.00 22.24 ?  30  VAL   B HB   1 
ATOM   4386 H HG11 . VAL   B 1 30  ? 46.432 -19.956 -15.487 1.00 22.43 ?  30  VAL   B HG11 1 
ATOM   4387 H HG12 . VAL   B 1 30  ? 47.240 -18.654 -15.084 1.00 22.43 ?  30  VAL   B HG12 1 
ATOM   4388 H HG13 . VAL   B 1 30  ? 47.040 -19.036 -16.616 1.00 22.43 ?  30  VAL   B HG13 1 
ATOM   4389 H HG21 . VAL   B 1 30  ? 47.497 -22.013 -15.515 1.00 23.21 ?  30  VAL   B HG21 1 
ATOM   4390 H HG22 . VAL   B 1 30  ? 47.907 -21.670 -17.011 1.00 23.21 ?  30  VAL   B HG22 1 
ATOM   4391 H HG23 . VAL   B 1 30  ? 49.010 -22.157 -15.977 1.00 23.21 ?  30  VAL   B HG23 1 
ATOM   4392 N N    A LYS   B 1 31  ? 50.315 -17.552 -15.460 0.50 16.17 ?  31  LYS   B N    1 
ATOM   4393 N N    B LYS   B 1 31  ? 50.325 -17.553 -15.468 0.50 16.25 ?  31  LYS   B N    1 
ATOM   4394 C CA   A LYS   B 1 31  ? 50.351 -16.136 -15.113 0.50 16.32 ?  31  LYS   B CA   1 
ATOM   4395 C CA   B LYS   B 1 31  ? 50.347 -16.140 -15.121 0.50 16.44 ?  31  LYS   B CA   1 
ATOM   4396 C C    A LYS   B 1 31  ? 48.961 -15.652 -14.702 0.50 14.38 ?  31  LYS   B C    1 
ATOM   4397 C C    B LYS   B 1 31  ? 48.940 -15.690 -14.736 0.50 14.48 ?  31  LYS   B C    1 
ATOM   4398 O O    A LYS   B 1 31  ? 48.426 -14.702 -15.292 0.50 15.20 ?  31  LYS   B O    1 
ATOM   4399 O O    B LYS   B 1 31  ? 48.358 -14.818 -15.397 0.50 15.19 ?  31  LYS   B O    1 
ATOM   4400 C CB   A LYS   B 1 31  ? 50.958 -15.320 -16.259 0.50 18.82 ?  31  LYS   B CB   1 
ATOM   4401 C CB   B LYS   B 1 31  ? 50.947 -15.322 -16.268 0.50 18.92 ?  31  LYS   B CB   1 
ATOM   4402 C CG   A LYS   B 1 31  ? 52.408 -15.698 -16.561 0.50 21.22 ?  31  LYS   B CG   1 
ATOM   4403 C CG   B LYS   B 1 31  ? 52.344 -15.797 -16.662 0.50 21.21 ?  31  LYS   B CG   1 
ATOM   4404 C CD   A LYS   B 1 31  ? 52.977 -14.885 -17.711 0.50 23.39 ?  31  LYS   B CD   1 
ATOM   4405 C CD   B LYS   B 1 31  ? 52.909 -15.012 -17.829 0.50 23.24 ?  31  LYS   B CD   1 
ATOM   4406 C CE   A LYS   B 1 31  ? 54.447 -15.187 -17.924 0.50 25.28 ?  31  LYS   B CE   1 
ATOM   4407 C CE   B LYS   B 1 31  ? 54.382 -15.313 -18.026 0.50 24.99 ?  31  LYS   B CE   1 
ATOM   4408 N NZ   A LYS   B 1 31  ? 55.231 -14.883 -16.698 0.50 26.30 ?  31  LYS   B NZ   1 
ATOM   4409 N NZ   B LYS   B 1 31  ? 55.168 -14.965 -16.811 0.50 25.87 ?  31  LYS   B NZ   1 
ATOM   4410 H H    A LYS   B 1 31  ? 50.845 -18.037 -14.993 0.50 19.42 ?  31  LYS   B H    1 
ATOM   4411 H H    B LYS   B 1 31  ? 50.868 -18.029 -15.006 0.50 19.52 ?  31  LYS   B H    1 
ATOM   4412 H HA   A LYS   B 1 31  ? 50.917 -16.045 -14.343 0.50 19.61 ?  31  LYS   B HA   1 
ATOM   4413 H HA   B LYS   B 1 31  ? 50.913 -16.034 -14.352 0.50 19.75 ?  31  LYS   B HA   1 
ATOM   4414 H HB2  A LYS   B 1 31  ? 50.437 -15.465 -17.065 0.50 22.60 ?  31  LYS   B HB2  1 
ATOM   4415 H HB2  B LYS   B 1 31  ? 50.374 -15.392 -17.046 0.50 22.72 ?  31  LYS   B HB2  1 
ATOM   4416 H HB3  A LYS   B 1 31  ? 50.936 -14.385 -16.013 0.50 22.60 ?  31  LYS   B HB3  1 
ATOM   4417 H HB3  B LYS   B 1 31  ? 51.013 -14.397 -15.984 0.50 22.72 ?  31  LYS   B HB3  1 
ATOM   4418 H HG2  A LYS   B 1 31  ? 52.944 -15.536 -15.768 0.50 25.49 ?  31  LYS   B HG2  1 
ATOM   4419 H HG2  B LYS   B 1 31  ? 52.936 -15.691 -15.901 0.50 25.47 ?  31  LYS   B HG2  1 
ATOM   4420 H HG3  A LYS   B 1 31  ? 52.448 -16.640 -16.800 0.50 25.49 ?  31  LYS   B HG3  1 
ATOM   4421 H HG3  B LYS   B 1 31  ? 52.302 -16.733 -16.921 0.50 25.47 ?  31  LYS   B HG3  1 
ATOM   4422 H HD2  A LYS   B 1 31  ? 52.497 -15.105 -18.524 0.50 28.08 ?  31  LYS   B HD2  1 
ATOM   4423 H HD2  B LYS   B 1 31  ? 52.435 -15.258 -18.638 0.50 27.91 ?  31  LYS   B HD2  1 
ATOM   4424 H HD3  A LYS   B 1 31  ? 52.884 -13.941 -17.509 0.50 28.08 ?  31  LYS   B HD3  1 
ATOM   4425 H HD3  B LYS   B 1 31  ? 52.810 -14.065 -17.653 0.50 27.91 ?  31  LYS   B HD3  1 
ATOM   4426 H HE2  A LYS   B 1 31  ? 54.558 -16.130 -18.132 0.50 30.35 ?  31  LYS   B HE2  1 
ATOM   4427 H HE2  B LYS   B 1 31  ? 54.498 -16.261 -18.202 0.50 30.01 ?  31  LYS   B HE2  1 
ATOM   4428 H HE3  A LYS   B 1 31  ? 54.789 -14.641 -18.650 0.50 30.35 ?  31  LYS   B HE3  1 
ATOM   4429 H HE3  B LYS   B 1 31  ? 54.721 -14.789 -18.768 0.50 30.01 ?  31  LYS   B HE3  1 
ATOM   4430 H HZ1  A LYS   B 1 31  ? 56.101 -14.951 -16.868 0.50 31.57 ?  31  LYS   B HZ1  1 
ATOM   4431 H HZ1  B LYS   B 1 31  ? 56.038 -14.996 -16.991 0.50 31.07 ?  31  LYS   B HZ1  1 
ATOM   4432 H HZ2  A LYS   B 1 31  ? 55.053 -14.055 -16.424 0.50 31.57 ?  31  LYS   B HZ2  1 
ATOM   4433 H HZ2  B LYS   B 1 31  ? 54.957 -14.144 -16.539 0.50 31.07 ?  31  LYS   B HZ2  1 
ATOM   4434 H HZ3  A LYS   B 1 31  ? 55.016 -15.454 -16.050 0.50 31.57 ?  31  LYS   B HZ3  1 
ATOM   4435 H HZ3  B LYS   B 1 31  ? 54.988 -15.540 -16.155 0.50 31.07 ?  31  LYS   B HZ3  1 
ATOM   4436 N N    . PRO   B 1 32  ? 48.354 -16.267 -13.682 1.00 12.60 ?  32  PRO   B N    1 
ATOM   4437 C CA   . PRO   B 1 32  ? 46.976 -15.912 -13.318 1.00 11.28 ?  32  PRO   B CA   1 
ATOM   4438 C C    . PRO   B 1 32  ? 46.886 -14.568 -12.614 1.00 11.45 ?  32  PRO   B C    1 
ATOM   4439 O O    . PRO   B 1 32  ? 47.809 -14.131 -11.922 1.00 12.76 ?  32  PRO   B O    1 
ATOM   4440 C CB   . PRO   B 1 32  ? 46.579 -17.034 -12.350 1.00 11.74 ?  32  PRO   B CB   1 
ATOM   4441 C CG   . PRO   B 1 32  ? 47.879 -17.369 -11.667 1.00 12.18 ?  32  PRO   B CG   1 
ATOM   4442 C CD   . PRO   B 1 32  ? 48.934 -17.242 -12.733 1.00 12.43 ?  32  PRO   B CD   1 
ATOM   4443 H HA   . PRO   B 1 32  ? 46.393 -15.923 -14.096 1.00 13.55 ?  32  PRO   B HA   1 
ATOM   4444 H HB2  . PRO   B 1 32  ? 45.921 -16.712 -11.714 1.00 14.11 ?  32  PRO   B HB2  1 
ATOM   4445 H HB3  . PRO   B 1 32  ? 46.240 -17.798 -12.845 1.00 14.11 ?  32  PRO   B HB3  1 
ATOM   4446 H HG2  . PRO   B 1 32  ? 48.040 -16.735 -10.946 1.00 14.63 ?  32  PRO   B HG2  1 
ATOM   4447 H HG3  . PRO   B 1 32  ? 47.846 -18.274 -11.322 1.00 14.63 ?  32  PRO   B HG3  1 
ATOM   4448 H HD2  . PRO   B 1 32  ? 49.752 -16.891 -12.349 1.00 14.94 ?  32  PRO   B HD2  1 
ATOM   4449 H HD3  . PRO   B 1 32  ? 49.072 -18.093 -13.163 1.00 14.94 ?  32  PRO   B HD3  1 
ATOM   4450 N N    . THR   B 1 33  ? 45.734 -13.917 -12.786 1.00 10.80 ?  33  THR   B N    1 
ATOM   4451 C CA   . THR   B 1 33  ? 45.432 -12.741 -11.982 1.00 10.95 ?  33  THR   B CA   1 
ATOM   4452 C C    . THR   B 1 33  ? 45.384 -13.093 -10.502 1.00 10.80 ?  33  THR   B C    1 
ATOM   4453 O O    . THR   B 1 33  ? 45.844 -12.308 -9.659  1.00 11.96 ?  33  THR   B O    1 
ATOM   4454 C CB   . THR   B 1 33  ? 44.108 -12.118 -12.432 1.00 11.76 ?  33  THR   B CB   1 
ATOM   4455 O OG1  . THR   B 1 33  ? 44.163 -11.838 -13.833 1.00 11.82 ?  33  THR   B OG1  1 
ATOM   4456 C CG2  . THR   B 1 33  ? 43.831 -10.831 -11.667 1.00 13.14 ?  33  THR   B CG2  1 
ATOM   4457 H H    . THR   B 1 33  ? 45.116 -14.141 -13.347 1.00 12.98 ?  33  THR   B H    1 
ATOM   4458 H HA   . THR   B 1 33  ? 46.126 -12.083 -12.112 1.00 13.16 ?  33  THR   B HA   1 
ATOM   4459 H HB   . THR   B 1 33  ? 43.378 -12.741 -12.257 1.00 14.13 ?  33  THR   B HB   1 
ATOM   4460 H HG1  . THR   B 1 33  ? 43.436 -11.487 -14.086 1.00 14.21 ?  33  THR   B HG1  1 
ATOM   4461 H HG21 . THR   B 1 33  ? 43.081 -10.366 -12.067 1.00 15.79 ?  33  THR   B HG21 1 
ATOM   4462 H HG22 . THR   B 1 33  ? 43.620 -11.033 -10.743 1.00 15.79 ?  33  THR   B HG22 1 
ATOM   4463 H HG23 . THR   B 1 33  ? 44.612 -10.259 -11.698 1.00 15.79 ?  33  THR   B HG23 1 
ATOM   4464 N N    . VAL   B 1 34  ? 44.834 -14.263 -10.165 1.00 10.32 ?  34  VAL   B N    1 
ATOM   4465 C CA   . VAL   B 1 34  ? 44.645 -14.661 -8.774  1.00 9.78  ?  34  VAL   B CA   1 
ATOM   4466 C C    . VAL   B 1 34  ? 45.074 -16.109 -8.605  1.00 8.94  ?  34  VAL   B C    1 
ATOM   4467 O O    . VAL   B 1 34  ? 44.553 -17.000 -9.289  1.00 9.67  ?  34  VAL   B O    1 
ATOM   4468 C CB   . VAL   B 1 34  ? 43.176 -14.516 -8.328  1.00 10.92 ?  34  VAL   B CB   1 
ATOM   4469 C CG1  . VAL   B 1 34  ? 43.005 -14.983 -6.879  1.00 11.27 ?  34  VAL   B CG1  1 
ATOM   4470 C CG2  . VAL   B 1 34  ? 42.681 -13.090 -8.512  1.00 11.94 ?  34  VAL   B CG2  1 
ATOM   4471 H H    . VAL   B 1 34  ? 44.574 -14.855 -10.734 1.00 12.40 ?  34  VAL   B H    1 
ATOM   4472 H HA   . VAL   B 1 34  ? 45.200 -14.108 -8.199  1.00 11.76 ?  34  VAL   B HA   1 
ATOM   4473 H HB   . VAL   B 1 34  ? 42.630 -15.089 -8.886  1.00 13.12 ?  34  VAL   B HB   1 
ATOM   4474 H HG11 . VAL   B 1 34  ? 42.140 -14.679 -6.549  1.00 13.54 ?  34  VAL   B HG11 1 
ATOM   4475 H HG12 . VAL   B 1 34  ? 43.039 -15.954 -6.846  1.00 13.54 ?  34  VAL   B HG12 1 
ATOM   4476 H HG13 . VAL   B 1 34  ? 43.711 -14.608 -6.333  1.00 13.54 ?  34  VAL   B HG13 1 
ATOM   4477 H HG21 . VAL   B 1 34  ? 41.767 -13.030 -8.194  1.00 14.34 ?  34  VAL   B HG21 1 
ATOM   4478 H HG22 . VAL   B 1 34  ? 43.249 -12.490 -8.005  1.00 14.34 ?  34  VAL   B HG22 1 
ATOM   4479 H HG23 . VAL   B 1 34  ? 42.718 -12.863 -9.455  1.00 14.34 ?  34  VAL   B HG23 1 
ATOM   4480 N N    . VAL   B 1 35  ? 45.984 -16.353 -7.665  1.00 8.61  ?  35  VAL   B N    1 
ATOM   4481 C CA   . VAL   B 1 35  ? 46.224 -17.692 -7.141  1.00 8.53  ?  35  VAL   B CA   1 
ATOM   4482 C C    . VAL   B 1 35  ? 45.682 -17.748 -5.721  1.00 8.28  ?  35  VAL   B C    1 
ATOM   4483 O O    . VAL   B 1 35  ? 45.898 -16.822 -4.931  1.00 8.69  ?  35  VAL   B O    1 
ATOM   4484 C CB   . VAL   B 1 35  ? 47.708 -18.113 -7.219  1.00 9.06  ?  35  VAL   B CB   1 
ATOM   4485 C CG1  . VAL   B 1 35  ? 48.599 -17.271 -6.292  1.00 9.74  ?  35  VAL   B CG1  1 
ATOM   4486 C CG2  . VAL   B 1 35  ? 47.850 -19.606 -6.917  1.00 9.78  ?  35  VAL   B CG2  1 
ATOM   4487 H H    . VAL   B 1 35  ? 46.489 -15.745 -7.312  1.00 10.35 ?  35  VAL   B H    1 
ATOM   4488 H HA   . VAL   B 1 35  ? 45.713 -18.322 -7.671  1.00 10.26 ?  35  VAL   B HA   1 
ATOM   4489 H HB   . VAL   B 1 35  ? 48.017 -17.971 -8.128  1.00 10.89 ?  35  VAL   B HB   1 
ATOM   4490 H HG11 . VAL   B 1 35  ? 49.524 -17.485 -6.468  1.00 11.70 ?  35  VAL   B HG11 1 
ATOM   4491 H HG12 . VAL   B 1 35  ? 48.431 -16.333 -6.464  1.00 11.70 ?  35  VAL   B HG12 1 
ATOM   4492 H HG13 . VAL   B 1 35  ? 48.376 -17.482 -5.369  1.00 11.70 ?  35  VAL   B HG13 1 
ATOM   4493 H HG21 . VAL   B 1 35  ? 48.776 -19.865 -7.017  1.00 11.75 ?  35  VAL   B HG21 1 
ATOM   4494 H HG22 . VAL   B 1 35  ? 47.553 -19.777 -6.008  1.00 11.75 ?  35  VAL   B HG22 1 
ATOM   4495 H HG23 . VAL   B 1 35  ? 47.297 -20.111 -7.540  1.00 11.75 ?  35  VAL   B HG23 1 
ATOM   4496 N N    . VAL   B 1 36  ? 44.963 -18.830 -5.402  1.00 7.84  ?  36  VAL   B N    1 
ATOM   4497 C CA   . VAL   B 1 36  ? 44.416 -19.040 -4.071  1.00 7.94  ?  36  VAL   B CA   1 
ATOM   4498 C C    . VAL   B 1 36  ? 45.424 -19.803 -3.222  1.00 7.66  ?  36  VAL   B C    1 
ATOM   4499 O O    . VAL   B 1 36  ? 45.965 -20.834 -3.647  1.00 8.79  ?  36  VAL   B O    1 
ATOM   4500 C CB   . VAL   B 1 36  ? 43.082 -19.800 -4.150  1.00 8.24  ?  36  VAL   B CB   1 
ATOM   4501 C CG1  . VAL   B 1 36  ? 42.580 -20.166 -2.761  1.00 8.90  ?  36  VAL   B CG1  1 
ATOM   4502 C CG2  . VAL   B 1 36  ? 42.050 -18.969 -4.901  1.00 8.73  ?  36  VAL   B CG2  1 
ATOM   4503 H H    . VAL   B 1 36  ? 44.788 -19.468 -5.955  1.00 9.43  ?  36  VAL   B H    1 
ATOM   4504 H HA   . VAL   B 1 36  ? 44.252 -18.179 -3.656  1.00 9.55  ?  36  VAL   B HA   1 
ATOM   4505 H HB   . VAL   B 1 36  ? 43.214 -20.622 -4.644  1.00 9.91  ?  36  VAL   B HB   1 
ATOM   4506 H HG11 . VAL   B 1 36  ? 41.641 -20.392 -2.817  1.00 10.70 ?  36  VAL   B HG11 1 
ATOM   4507 H HG12 . VAL   B 1 36  ? 43.089 -20.915 -2.428  1.00 10.70 ?  36  VAL   B HG12 1 
ATOM   4508 H HG13 . VAL   B 1 36  ? 42.697 -19.394 -2.176  1.00 10.70 ?  36  VAL   B HG13 1 
ATOM   4509 H HG21 . VAL   B 1 36  ? 41.208 -19.449 -4.921  1.00 10.50 ?  36  VAL   B HG21 1 
ATOM   4510 H HG22 . VAL   B 1 36  ? 41.936 -18.119 -4.447  1.00 10.50 ?  36  VAL   B HG22 1 
ATOM   4511 H HG23 . VAL   B 1 36  ? 42.365 -18.817 -5.808  1.00 10.50 ?  36  VAL   B HG23 1 
ATOM   4512 N N    . ASN   B 1 37  ? 45.646 -19.311 -2.008  1.00 8.25  ?  37  ASN   B N    1 
ATOM   4513 C CA   . ASN   B 1 37  ? 46.394 -20.037 -0.997  1.00 8.62  ?  37  ASN   B CA   1 
ATOM   4514 C C    . ASN   B 1 37  ? 45.448 -20.708 -0.013  1.00 8.22  ?  37  ASN   B C    1 
ATOM   4515 O O    . ASN   B 1 37  ? 44.440 -20.128 0.403   1.00 8.97  ?  37  ASN   B O    1 
ATOM   4516 C CB   . ASN   B 1 37  ? 47.319 -19.090 -0.241  1.00 8.58  ?  37  ASN   B CB   1 
ATOM   4517 C CG   . ASN   B 1 37  ? 48.174 -19.804 0.777   1.00 8.82  ?  37  ASN   B CG   1 
ATOM   4518 O OD1  . ASN   B 1 37  ? 48.521 -20.981 0.605   1.00 9.69  ?  37  ASN   B OD1  1 
ATOM   4519 N ND2  . ASN   B 1 37  ? 48.514 -19.104 1.851   1.00 9.39  ?  37  ASN   B ND2  1 
ATOM   4520 H H    . ASN   B 1 37  ? 45.361 -18.546 -1.735  1.00 9.92  ?  37  ASN   B H    1 
ATOM   4521 H HA   . ASN   B 1 37  ? 46.934 -20.726 -1.420  1.00 10.36 ?  37  ASN   B HA   1 
ATOM   4522 H HB2  . ASN   B 1 37  ? 47.909 -18.657 -0.875  1.00 10.31 ?  37  ASN   B HB2  1 
ATOM   4523 H HB3  . ASN   B 1 37  ? 46.784 -18.432 0.225   1.00 10.31 ?  37  ASN   B HB3  1 
ATOM   4524 H HD21 . ASN   B 1 37  ? 49.000 -19.465 2.462   1.00 11.28 ?  37  ASN   B HD21 1 
ATOM   4525 H HD22 . ASN   B 1 37  ? 48.251 -18.296 1.941   1.00 11.28 ?  37  ASN   B HD22 1 
ATOM   4526 N N    . ALA   B 1 38  ? 45.797 -21.939 0.360   1.00 8.29  ?  38  ALA   B N    1 
ATOM   4527 C CA   . ALA   B 1 38  ? 45.143 -22.686 1.434   1.00 9.07  ?  38  ALA   B CA   1 
ATOM   4528 C C    . ALA   B 1 38  ? 45.724 -22.200 2.760   1.00 8.85  ?  38  ALA   B C    1 
ATOM   4529 O O    . ALA   B 1 38  ? 46.627 -22.807 3.345   1.00 9.60  ?  38  ALA   B O    1 
ATOM   4530 C CB   . ALA   B 1 38  ? 45.364 -24.181 1.238   1.00 10.37 ?  38  ALA   B CB   1 
ATOM   4531 H H    . ALA   B 1 38  ? 46.448 -22.376 0.001   1.00 9.96  ?  38  ALA   B H    1 
ATOM   4532 H HA   . ALA   B 1 38  ? 44.191 -22.505 1.427   1.00 10.90 ?  38  ALA   B HA   1 
ATOM   4533 H HB1  . ALA   B 1 38  ? 44.916 -24.664 1.960   1.00 12.47 ?  38  ALA   B HB1  1 
ATOM   4534 H HB2  . ALA   B 1 38  ? 44.981 -24.448 0.387   1.00 12.47 ?  38  ALA   B HB2  1 
ATOM   4535 H HB3  . ALA   B 1 38  ? 46.310 -24.372 1.255   1.00 12.47 ?  38  ALA   B HB3  1 
ATOM   4536 N N    . ALA   B 1 39  ? 45.207 -21.062 3.221   1.00 8.73  ?  39  ALA   B N    1 
ATOM   4537 C CA   . ALA   B 1 39  ? 45.752 -20.333 4.356   1.00 9.25  ?  39  ALA   B CA   1 
ATOM   4538 C C    . ALA   B 1 39  ? 45.128 -20.776 5.679   1.00 9.15  ?  39  ALA   B C    1 
ATOM   4539 O O    . ALA   B 1 39  ? 44.099 -21.456 5.723   1.00 9.95  ?  39  ALA   B O    1 
ATOM   4540 C CB   . ALA   B 1 39  ? 45.515 -18.831 4.156   1.00 9.90  ?  39  ALA   B CB   1 
ATOM   4541 H H    . ALA   B 1 39  ? 44.513 -20.686 2.876   1.00 10.49 ?  39  ALA   B H    1 
ATOM   4542 H HA   . ALA   B 1 39  ? 46.701 -20.486 4.406   1.00 11.12 ?  39  ALA   B HA   1 
ATOM   4543 H HB1  . ALA   B 1 39  ? 45.881 -18.351 4.916   1.00 11.90 ?  39  ALA   B HB1  1 
ATOM   4544 H HB2  . ALA   B 1 39  ? 45.965 -18.549 3.342   1.00 11.90 ?  39  ALA   B HB2  1 
ATOM   4545 H HB3  . ALA   B 1 39  ? 44.564 -18.663 4.083   1.00 11.90 ?  39  ALA   B HB3  1 
ATOM   4546 N N    . ASN   B 1 40  ? 45.767 -20.350 6.770   1.00 10.11 ?  40  ASN   B N    1 
ATOM   4547 C CA   . ASN   B 1 40  ? 45.197 -20.403 8.108   1.00 10.62 ?  40  ASN   B CA   1 
ATOM   4548 C C    . ASN   B 1 40  ? 45.025 -18.977 8.638   1.00 10.29 ?  40  ASN   B C    1 
ATOM   4549 O O    . ASN   B 1 40  ? 45.442 -17.997 8.007   1.00 10.45 ?  40  ASN   B O    1 
ATOM   4550 C CB   . ASN   B 1 40  ? 46.038 -21.286 9.045   1.00 11.60 ?  40  ASN   B CB   1 
ATOM   4551 C CG   . ASN   B 1 40  ? 47.493 -20.888 9.077   1.00 12.64 ?  40  ASN   B CG   1 
ATOM   4552 O OD1  . ASN   B 1 40  ? 47.815 -19.707 9.149   1.00 14.39 ?  40  ASN   B OD1  1 
ATOM   4553 N ND2  . ASN   B 1 40  ? 48.384 -21.871 9.026   1.00 12.60 ?  40  ASN   B ND2  1 
ATOM   4554 H H    . ASN   B 1 40  ? 46.558 -20.020 6.751   1.00 12.15 ?  40  ASN   B H    1 
ATOM   4555 H HA   . ASN   B 1 40  ? 44.314 -20.797 8.057   1.00 12.77 ?  40  ASN   B HA   1 
ATOM   4556 H HB2  . ASN   B 1 40  ? 45.688 -21.213 9.949   1.00 13.94 ?  40  ASN   B HB2  1 
ATOM   4557 H HB3  . ASN   B 1 40  ? 45.986 -22.206 8.744   1.00 13.94 ?  40  ASN   B HB3  1 
ATOM   4558 H HD21 . ASN   B 1 40  ? 49.228 -21.700 9.045   1.00 15.14 ?  40  ASN   B HD21 1 
ATOM   4559 H HD22 . ASN   B 1 40  ? 48.119 -22.691 8.972   1.00 15.14 ?  40  ASN   B HD22 1 
ATOM   4560 N N    . VAL   B 1 41  ? 44.369 -18.851 9.795   1.00 10.80 ?  41  VAL   B N    1 
ATOM   4561 C CA   . VAL   B 1 41  ? 43.915 -17.530 10.240  1.00 11.30 ?  41  VAL   B CA   1 
ATOM   4562 C C    . VAL   B 1 41  ? 45.069 -16.589 10.552  1.00 11.06 ?  41  VAL   B C    1 
ATOM   4563 O O    . VAL   B 1 41  ? 44.897 -15.366 10.474  1.00 11.38 ?  41  VAL   B O    1 
ATOM   4564 C CB   . VAL   B 1 41  ? 42.923 -17.606 11.418  1.00 12.67 ?  41  VAL   B CB   1 
ATOM   4565 C CG1  . VAL   B 1 41  ? 41.627 -18.282 10.995  1.00 13.20 ?  41  VAL   B CG1  1 
ATOM   4566 C CG2  . VAL   B 1 41  ? 43.542 -18.301 12.617  1.00 13.79 ?  41  VAL   B CG2  1 
ATOM   4567 H H    . VAL   B 1 41  ? 44.179 -19.496 10.323  1.00 12.98 ?  41  VAL   B H    1 
ATOM   4568 H HA   . VAL   B 1 41  ? 43.429 -17.127 9.507   1.00 13.58 ?  41  VAL   B HA   1 
ATOM   4569 H HB   . VAL   B 1 41  ? 42.696 -16.703 11.692  1.00 15.23 ?  41  VAL   B HB   1 
ATOM   4570 H HG11 . VAL   B 1 41  ? 41.007 -18.281 11.743  1.00 15.85 ?  41  VAL   B HG11 1 
ATOM   4571 H HG12 . VAL   B 1 41  ? 41.244 -17.796 10.248  1.00 15.85 ?  41  VAL   B HG12 1 
ATOM   4572 H HG13 . VAL   B 1 41  ? 41.820 -19.197 10.730  1.00 15.85 ?  41  VAL   B HG13 1 
ATOM   4573 H HG21 . VAL   B 1 41  ? 42.893 -18.333 13.337  1.00 16.57 ?  41  VAL   B HG21 1 
ATOM   4574 H HG22 . VAL   B 1 41  ? 43.795 -19.204 12.364  1.00 16.57 ?  41  VAL   B HG22 1 
ATOM   4575 H HG23 . VAL   B 1 41  ? 44.325 -17.806 12.900  1.00 16.57 ?  41  VAL   B HG23 1 
ATOM   4576 N N    . TYR   B 1 42  ? 46.233 -17.110 10.941  1.00 11.44 ?  42  TYR   B N    1 
ATOM   4577 C CA   . TYR   B 1 42  ? 47.385 -16.258 11.209  1.00 12.26 ?  42  TYR   B CA   1 
ATOM   4578 C C    . TYR   B 1 42  ? 48.354 -16.183 10.031  1.00 11.29 ?  42  TYR   B C    1 
ATOM   4579 O O    . TYR   B 1 42  ? 49.439 -15.608 10.167  1.00 12.21 ?  42  TYR   B O    1 
ATOM   4580 C CB   . TYR   B 1 42  ? 48.081 -16.653 12.520  1.00 14.48 ?  42  TYR   B CB   1 
ATOM   4581 C CG   . TYR   B 1 42  ? 47.468 -15.975 13.745  1.00 14.80 ?  42  TYR   B CG   1 
ATOM   4582 C CD1  . TYR   B 1 42  ? 47.699 -14.627 14.004  1.00 14.05 ?  42  TYR   B CD1  1 
ATOM   4583 C CD2  . TYR   B 1 42  ? 46.659 -16.675 14.628  1.00 16.83 ?  42  TYR   B CD2  1 
ATOM   4584 C CE1  . TYR   B 1 42  ? 47.146 -13.999 15.107  1.00 15.02 ?  42  TYR   B CE1  1 
ATOM   4585 C CE2  . TYR   B 1 42  ? 46.106 -16.055 15.738  1.00 17.25 ?  42  TYR   B CE2  1 
ATOM   4586 C CZ   . TYR   B 1 42  ? 46.348 -14.715 15.970  1.00 17.28 ?  42  TYR   B CZ   1 
ATOM   4587 O OH   . TYR   B 1 42  ? 45.802 -14.094 17.073  1.00 19.77 ?  42  TYR   B OH   1 
ATOM   4588 H H    . TYR   B 1 42  ? 46.378 -17.955 11.043  1.00 13.75 ?  42  TYR   B H    1 
ATOM   4589 H HA   . TYR   B 1 42  ? 47.054 -15.360 11.342  1.00 14.73 ?  42  TYR   B HA   1 
ATOM   4590 H HB2  . TYR   B 1 42  ? 48.007 -17.612 12.641  1.00 17.39 ?  42  TYR   B HB2  1 
ATOM   4591 H HB3  . TYR   B 1 42  ? 49.014 -16.395 12.469  1.00 17.39 ?  42  TYR   B HB3  1 
ATOM   4592 H HD1  . TYR   B 1 42  ? 48.240 -14.141 13.417  1.00 16.88 ?  42  TYR   B HD1  1 
ATOM   4593 H HD2  . TYR   B 1 42  ? 46.490 -17.578 14.471  1.00 20.22 ?  42  TYR   B HD2  1 
ATOM   4594 H HE1  . TYR   B 1 42  ? 47.317 -13.100 15.262  1.00 18.05 ?  42  TYR   B HE1  1 
ATOM   4595 H HE2  . TYR   B 1 42  ? 45.566 -16.541 16.317  1.00 20.72 ?  42  TYR   B HE2  1 
ATOM   4596 H HH   . TYR   B 1 42  ? 46.035 -13.289 17.086  1.00 23.74 ?  42  TYR   B HH   1 
ATOM   4597 N N    . LEU   B 1 43  ? 47.961 -16.701 8.868   1.00 10.45 ?  43  LEU   B N    1 
ATOM   4598 C CA   . LEU   B 1 43  ? 48.771 -16.625 7.656   1.00 10.16 ?  43  LEU   B CA   1 
ATOM   4599 C C    . LEU   B 1 43  ? 50.183 -17.134 7.908   1.00 10.66 ?  43  LEU   B C    1 
ATOM   4600 O O    . LEU   B 1 43  ? 51.164 -16.531 7.474   1.00 11.41 ?  43  LEU   B O    1 
ATOM   4601 C CB   . LEU   B 1 43  ? 48.787 -15.215 7.063   1.00 10.39 ?  43  LEU   B CB   1 
ATOM   4602 C CG   . LEU   B 1 43  ? 47.431 -14.606 6.680   1.00 10.42 ?  43  LEU   B CG   1 
ATOM   4603 C CD1  . LEU   B 1 43  ? 47.639 -13.211 6.106   1.00 11.67 ?  43  LEU   B CD1  1 
ATOM   4604 C CD2  . LEU   B 1 43  ? 46.675 -15.485 5.695   1.00 10.80 ?  43  LEU   B CD2  1 
ATOM   4605 H H    . LEU   B 1 43  ? 47.220 -17.123 8.754   1.00 12.56 ?  43  LEU   B H    1 
ATOM   4606 H HA   . LEU   B 1 43  ? 48.374 -17.208 6.991   1.00 12.21 ?  43  LEU   B HA   1 
ATOM   4607 H HB2  . LEU   B 1 43  ? 49.200 -14.621 7.706   1.00 12.49 ?  43  LEU   B HB2  1 
ATOM   4608 H HB3  . LEU   B 1 43  ? 49.324 -15.239 6.255   1.00 12.49 ?  43  LEU   B HB3  1 
ATOM   4609 H HG   . LEU   B 1 43  ? 46.890 -14.516 7.480   1.00 12.53 ?  43  LEU   B HG   1 
ATOM   4610 H HD11 . LEU   B 1 43  ? 46.777 -12.830 5.872   1.00 14.02 ?  43  LEU   B HD11 1 
ATOM   4611 H HD12 . LEU   B 1 43  ? 48.071 -12.652 6.777   1.00 14.02 ?  43  LEU   B HD12 1 
ATOM   4612 H HD13 . LEU   B 1 43  ? 48.201 -13.269 5.319   1.00 14.02 ?  43  LEU   B HD13 1 
ATOM   4613 H HD21 . LEU   B 1 43  ? 45.872 -15.017 5.409   1.00 12.98 ?  43  LEU   B HD21 1 
ATOM   4614 H HD22 . LEU   B 1 43  ? 47.243 -15.662 4.930   1.00 12.98 ?  43  LEU   B HD22 1 
ATOM   4615 H HD23 . LEU   B 1 43  ? 46.436 -16.314 6.133   1.00 12.98 ?  43  LEU   B HD23 1 
ATOM   4616 N N    . LYS   B 1 44  ? 50.285 -18.258 8.620   1.00 10.27 ?  44  LYS   B N    1 
ATOM   4617 C CA   . LYS   B 1 44  ? 51.553 -18.938 8.852   1.00 10.72 ?  44  LYS   B CA   1 
ATOM   4618 C C    . LYS   B 1 44  ? 51.668 -20.053 7.821   1.00 10.70 ?  44  LYS   B C    1 
ATOM   4619 O O    . LYS   B 1 44  ? 50.956 -21.060 7.898   1.00 11.87 ?  44  LYS   B O    1 
ATOM   4620 C CB   . LYS   B 1 44  ? 51.624 -19.453 10.288  1.00 12.73 ?  44  LYS   B CB   1 
ATOM   4621 C CG   . LYS   B 1 44  ? 51.789 -18.338 11.315  1.00 15.51 ?  44  LYS   B CG   1 
ATOM   4622 C CD   . LYS   B 1 44  ? 53.004 -17.479 10.959  1.00 18.52 ?  44  LYS   B CD   1 
ATOM   4623 C CE   . LYS   B 1 44  ? 53.435 -16.560 12.075  1.00 21.15 ?  44  LYS   B CE   1 
ATOM   4624 N NZ   . LYS   B 1 44  ? 54.646 -15.772 11.711  1.00 22.36 ?  44  LYS   B NZ   1 
ATOM   4625 H H    . LYS   B 1 44  ? 49.615 -18.645 8.993   1.00 12.35 ?  44  LYS   B H    1 
ATOM   4626 H HA   . LYS   B 1 44  ? 52.283 -18.322 8.690   1.00 12.89 ?  44  LYS   B HA   1 
ATOM   4627 H HB2  . LYS   B 1 44  ? 50.799 -19.925 10.494  1.00 15.30 ?  44  LYS   B HB2  1 
ATOM   4628 H HB3  . LYS   B 1 44  ? 52.378 -20.053 10.372  1.00 15.30 ?  44  LYS   B HB3  1 
ATOM   4629 H HG2  . LYS   B 1 44  ? 51.001 -17.779 11.320  1.00 18.63 ?  44  LYS   B HG2  1 
ATOM   4630 H HG3  . LYS   B 1 44  ? 51.937 -18.730 12.194  1.00 18.63 ?  44  LYS   B HG3  1 
ATOM   4631 H HD2  . LYS   B 1 44  ? 53.748 -18.066 10.733  1.00 22.25 ?  44  LYS   B HD2  1 
ATOM   4632 H HD3  . LYS   B 1 44  ? 52.780 -16.925 10.195  1.00 22.25 ?  44  LYS   B HD3  1 
ATOM   4633 H HE2  . LYS   B 1 44  ? 52.721 -15.934 12.254  1.00 25.40 ?  44  LYS   B HE2  1 
ATOM   4634 H HE3  . LYS   B 1 44  ? 53.637 -17.085 12.864  1.00 25.40 ?  44  LYS   B HE3  1 
ATOM   4635 H HZ1  . LYS   B 1 44  ? 54.873 -15.235 12.385  1.00 26.85 ?  44  LYS   B HZ1  1 
ATOM   4636 H HZ2  . LYS   B 1 44  ? 55.327 -16.316 11.533  1.00 26.85 ?  44  LYS   B HZ2  1 
ATOM   4637 H HZ3  . LYS   B 1 44  ? 54.481 -15.272 10.991  1.00 26.85 ?  44  LYS   B HZ3  1 
ATOM   4638 N N    . HIS   B 1 45  ? 52.529 -19.839 6.829   1.00 10.50 ?  45  HIS   B N    1 
ATOM   4639 C CA   . HIS   B 1 45  ? 52.554 -20.665 5.623   1.00 10.60 ?  45  HIS   B CA   1 
ATOM   4640 C C    . HIS   B 1 45  ? 53.569 -21.791 5.784   1.00 12.72 ?  45  HIS   B C    1 
ATOM   4641 O O    . HIS   B 1 45  ? 54.619 -21.820 5.152   1.00 14.81 ?  45  HIS   B O    1 
ATOM   4642 C CB   . HIS   B 1 45  ? 52.873 -19.806 4.410   1.00 10.50 ?  45  HIS   B CB   1 
ATOM   4643 C CG   . HIS   B 1 45  ? 51.999 -18.604 4.296   1.00 10.20 ?  45  HIS   B CG   1 
ATOM   4644 N ND1  . HIS   B 1 45  ? 50.620 -18.681 4.257   1.00 10.53 ?  45  HIS   B ND1  1 
ATOM   4645 C CD2  . HIS   B 1 45  ? 52.315 -17.291 4.237   1.00 11.06 ?  45  HIS   B CD2  1 
ATOM   4646 C CE1  . HIS   B 1 45  ? 50.132 -17.458 4.158   1.00 10.05 ?  45  HIS   B CE1  1 
ATOM   4647 N NE2  . HIS   B 1 45  ? 51.136 -16.599 4.141   1.00 10.58 ?  45  HIS   B NE2  1 
ATOM   4648 H H    . HIS   B 1 45  ? 53.108 -19.207 6.824   1.00 12.61 ?  45  HIS   B H    1 
ATOM   4649 H HA   . HIS   B 1 45  ? 51.677 -21.064 5.488   1.00 12.74 ?  45  HIS   B HA   1 
ATOM   4650 H HB2  . HIS   B 1 45  ? 53.792 -19.508 4.471   1.00 12.62 ?  45  HIS   B HB2  1 
ATOM   4651 H HB3  . HIS   B 1 45  ? 52.753 -20.343 3.607   1.00 12.62 ?  45  HIS   B HB3  1 
ATOM   4652 H HD2  . HIS   B 1 45  ? 53.168 -16.924 4.250   1.00 13.29 ?  45  HIS   B HD2  1 
ATOM   4653 H HE1  . HIS   B 1 45  ? 49.230 -17.243 4.100   1.00 12.08 ?  45  HIS   B HE1  1 
ATOM   4654 H HE2  . HIS   B 1 45  ? 51.057 -15.745 4.090   1.00 12.72 ?  45  HIS   B HE2  1 
ATOM   4655 N N    A GLY   B 1 46  ? 53.205 -22.757 6.627   0.50 13.43 ?  46  GLY   B N    1 
ATOM   4656 N N    B GLY   B 1 46  ? 53.220 -22.741 6.645   0.50 13.40 ?  46  GLY   B N    1 
ATOM   4657 C CA   A GLY   B 1 46  ? 54.128 -23.807 7.018   0.50 14.87 ?  46  GLY   B CA   1 
ATOM   4658 C CA   B GLY   B 1 46  ? 54.143 -23.805 6.981   0.50 14.80 ?  46  GLY   B CA   1 
ATOM   4659 C C    A GLY   B 1 46  ? 54.188 -25.040 6.138   0.50 15.89 ?  46  GLY   B C    1 
ATOM   4660 C C    B GLY   B 1 46  ? 54.178 -24.949 5.987   0.50 15.92 ?  46  GLY   B C    1 
ATOM   4661 O O    A GLY   B 1 46  ? 55.277 -25.521 5.811   0.50 18.18 ?  46  GLY   B O    1 
ATOM   4662 O O    B GLY   B 1 46  ? 55.221 -25.240 5.395   0.50 17.55 ?  46  GLY   B O    1 
ATOM   4663 H H    A GLY   B 1 46  ? 52.427 -22.811 7.001   0.50 16.14 ?  46  GLY   B H    1 
ATOM   4664 H H    B GLY   B 1 46  ? 52.458 -22.785 7.051   0.50 16.09 ?  46  GLY   B H    1 
ATOM   4665 H HA2  A GLY   B 1 46  ? 55.019 -23.429 7.063   0.50 17.86 ?  46  GLY   B HA2  1 
ATOM   4666 H HA2  B GLY   B 1 46  ? 55.037 -23.435 7.043   0.50 17.78 ?  46  GLY   B HA2  1 
ATOM   4667 H HA3  A GLY   B 1 46  ? 53.890 -24.114 7.904   0.50 17.86 ?  46  GLY   B HA3  1 
ATOM   4668 H HA3  B GLY   B 1 46  ? 53.906 -24.164 7.851   0.50 17.78 ?  46  GLY   B HA3  1 
ATOM   4669 N N    . GLY   B 1 47  ? 53.032 -25.592 5.771   1.00 15.29 ?  47  GLY   B N    1 
ATOM   4670 C CA   . GLY   B 1 47  ? 52.978 -26.866 5.086   1.00 13.42 ?  47  GLY   B CA   1 
ATOM   4671 C C    . GLY   B 1 47  ? 52.061 -26.854 3.878   1.00 11.61 ?  47  GLY   B C    1 
ATOM   4672 O O    . GLY   B 1 47  ? 51.407 -25.853 3.577   1.00 11.81 ?  47  GLY   B O    1 
ATOM   4673 H H    A GLY   B 1 47  ? 52.258 -25.255 5.937   0.50 18.37 ?  47  GLY   B H    1 
ATOM   4674 H H    B GLY   B 1 47  ? 52.261 -25.298 6.016   0.50 18.37 ?  47  GLY   B H    1 
ATOM   4675 H HA2  . GLY   B 1 47  ? 53.868 -27.118 4.790   1.00 16.12 ?  47  GLY   B HA2  1 
ATOM   4676 H HA3  . GLY   B 1 47  ? 52.664 -27.547 5.705   1.00 16.12 ?  47  GLY   B HA3  1 
ATOM   4677 N N    . GLY   B 1 48  ? 52.023 -27.996 3.193   1.00 10.93 ?  48  GLY   B N    1 
ATOM   4678 C CA   . GLY   B 1 48  ? 51.099 -28.152 2.085   1.00 11.07 ?  48  GLY   B CA   1 
ATOM   4679 C C    . GLY   B 1 48  ? 51.233 -27.045 1.064   1.00 10.60 ?  48  GLY   B C    1 
ATOM   4680 O O    . GLY   B 1 48  ? 52.335 -26.578 0.751   1.00 11.02 ?  48  GLY   B O    1 
ATOM   4681 H H    . GLY   B 1 48  ? 52.527 -28.675 3.342   1.00 13.13 ?  48  GLY   B H    1 
ATOM   4682 H HA2  . GLY   B 1 48  ? 51.264 -28.998 1.643   1.00 13.30 ?  48  GLY   B HA2  1 
ATOM   4683 H HA3  . GLY   B 1 48  ? 50.191 -28.149 2.420   1.00 13.30 ?  48  GLY   B HA3  1 
ATOM   4684 N N    . VAL   B 1 49  ? 50.084 -26.609 0.541   1.00 10.37 ?  49  VAL   B N    1 
ATOM   4685 C CA   . VAL   B 1 49  ? 50.064 -25.585 -0.501  1.00 10.38 ?  49  VAL   B CA   1 
ATOM   4686 C C    . VAL   B 1 49  ? 50.724 -24.297 -0.017  1.00 9.57  ?  49  VAL   B C    1 
ATOM   4687 O O    . VAL   B 1 49  ? 51.510 -23.679 -0.744  1.00 10.32 ?  49  VAL   B O    1 
ATOM   4688 C CB   . VAL   B 1 49  ? 48.620 -25.340 -0.977  1.00 11.83 ?  49  VAL   B CB   1 
ATOM   4689 C CG1  . VAL   B 1 49  ? 48.545 -24.098 -1.853  1.00 12.00 ?  49  VAL   B CG1  1 
ATOM   4690 C CG2  . VAL   B 1 49  ? 48.093 -26.560 -1.724  1.00 13.44 ?  49  VAL   B CG2  1 
ATOM   4691 H H    . VAL   B 1 49  ? 49.300 -26.887 0.773   1.00 12.47 ?  49  VAL   B H    1 
ATOM   4692 H HA   . VAL   B 1 49  ? 50.570 -25.900 -1.262  1.00 12.48 ?  49  VAL   B HA   1 
ATOM   4693 H HB   . VAL   B 1 49  ? 48.053 -25.195 -0.207  1.00 14.21 ?  49  VAL   B HB   1 
ATOM   4694 H HG11 . VAL   B 1 49  ? 47.715 -24.115 -2.359  1.00 14.42 ?  49  VAL   B HG11 1 
ATOM   4695 H HG12 . VAL   B 1 49  ? 48.565 -23.306 -1.290  1.00 14.42 ?  49  VAL   B HG12 1 
ATOM   4696 H HG13 . VAL   B 1 49  ? 49.299 -24.089 -2.464  1.00 14.42 ?  49  VAL   B HG13 1 
ATOM   4697 H HG21 . VAL   B 1 49  ? 47.186 -26.385 -2.018  1.00 16.15 ?  49  VAL   B HG21 1 
ATOM   4698 H HG22 . VAL   B 1 49  ? 48.663 -26.728 -2.495  1.00 16.15 ?  49  VAL   B HG22 1 
ATOM   4699 H HG23 . VAL   B 1 49  ? 48.110 -27.325 -1.131  1.00 16.15 ?  49  VAL   B HG23 1 
ATOM   4700 N N    . ALA   B 1 50  ? 50.377 -23.848 1.192   1.00 9.41  ?  50  ALA   B N    1 
ATOM   4701 C CA   . ALA   B 1 50  ? 50.895 -22.572 1.676   1.00 9.38  ?  50  ALA   B CA   1 
ATOM   4702 C C    . ALA   B 1 50  ? 52.414 -22.594 1.782   1.00 9.56  ?  50  ALA   B C    1 
ATOM   4703 O O    . ALA   B 1 50  ? 53.091 -21.624 1.410   1.00 9.69  ?  50  ALA   B O    1 
ATOM   4704 C CB   . ALA   B 1 50  ? 50.259 -22.221 3.021   1.00 9.55  ?  50  ALA   B CB   1 
ATOM   4705 H H    . ALA   B 1 50  ? 49.859 -24.260 1.742   1.00 11.31 ?  50  ALA   B H    1 
ATOM   4706 H HA   . ALA   B 1 50  ? 50.662 -21.878 1.050   1.00 11.27 ?  50  ALA   B HA   1 
ATOM   4707 H HB1  . ALA   B 1 50  ? 50.611 -21.371 3.332   1.00 11.48 ?  50  ALA   B HB1  1 
ATOM   4708 H HB2  . ALA   B 1 50  ? 49.294 -22.154 2.908   1.00 11.48 ?  50  ALA   B HB2  1 
ATOM   4709 H HB3  . ALA   B 1 50  ? 50.463 -22.917 3.668   1.00 11.48 ?  50  ALA   B HB3  1 
ATOM   4710 N N    . GLY   B 1 51  ? 52.968 -23.692 2.293   1.00 10.03 ?  51  GLY   B N    1 
ATOM   4711 C CA   . GLY   B 1 51  ? 54.411 -23.799 2.367   1.00 10.57 ?  51  GLY   B CA   1 
ATOM   4712 C C    . GLY   B 1 51  ? 55.060 -23.748 0.999   1.00 10.54 ?  51  GLY   B C    1 
ATOM   4713 O O    . GLY   B 1 51  ? 56.098 -23.107 0.817   1.00 11.36 ?  51  GLY   B O    1 
ATOM   4714 H H    . GLY   B 1 51  ? 52.543 -24.378 2.592   1.00 12.05 ?  51  GLY   B H    1 
ATOM   4715 H HA2  . GLY   B 1 51  ? 54.766 -23.067 2.900   1.00 12.70 ?  51  GLY   B HA2  1 
ATOM   4716 H HA3  . GLY   B 1 51  ? 54.659 -24.635 2.794   1.00 12.70 ?  51  GLY   B HA3  1 
ATOM   4717 N N    . ALA   B 1 52  ? 54.456 -24.413 0.016   1.00 10.44 ?  52  ALA   B N    1 
ATOM   4718 C CA   . ALA   B 1 52  ? 55.017 -24.415 -1.328  1.00 10.84 ?  52  ALA   B CA   1 
ATOM   4719 C C    . ALA   B 1 52  ? 54.937 -23.034 -1.974  1.00 10.18 ?  52  ALA   B C    1 
ATOM   4720 O O    . ALA   B 1 52  ? 55.906 -22.579 -2.602  1.00 10.73 ?  52  ALA   B O    1 
ATOM   4721 C CB   . ALA   B 1 52  ? 54.308 -25.461 -2.181  1.00 11.62 ?  52  ALA   B CB   1 
ATOM   4722 H H    . ALA   B 1 52  ? 53.723 -24.857 0.103   1.00 12.54 ?  52  ALA   B H    1 
ATOM   4723 H HA   . ALA   B 1 52  ? 55.951 -24.660 -1.270  1.00 13.02 ?  52  ALA   B HA   1 
ATOM   4724 H HB1  . ALA   B 1 52  ? 54.694 -25.454 -3.071  1.00 13.96 ?  52  ALA   B HB1  1 
ATOM   4725 H HB2  . ALA   B 1 52  ? 54.434 -26.335 -1.774  1.00 13.96 ?  52  ALA   B HB2  1 
ATOM   4726 H HB3  . ALA   B 1 52  ? 53.365 -25.250 -2.225  1.00 13.96 ?  52  ALA   B HB3  1 
ATOM   4727 N N    . LEU   B 1 53  ? 53.794 -22.355 -1.848  1.00 9.71  ?  53  LEU   B N    1 
ATOM   4728 C CA   . LEU   B 1 53  ? 53.681 -21.019 -2.421  1.00 10.11 ?  53  LEU   B CA   1 
ATOM   4729 C C    . LEU   B 1 53  ? 54.682 -20.075 -1.771  1.00 9.95  ?  53  LEU   B C    1 
ATOM   4730 O O    . LEU   B 1 53  ? 55.384 -19.322 -2.456  1.00 10.52 ?  53  LEU   B O    1 
ATOM   4731 C CB   . LEU   B 1 53  ? 52.254 -20.480 -2.264  1.00 10.50 ?  53  LEU   B CB   1 
ATOM   4732 C CG   . LEU   B 1 53  ? 51.129 -21.194 -3.011  1.00 10.92 ?  53  LEU   B CG   1 
ATOM   4733 C CD1  . LEU   B 1 53  ? 49.781 -20.585 -2.642  1.00 12.36 ?  53  LEU   B CD1  1 
ATOM   4734 C CD2  . LEU   B 1 53  ? 51.335 -21.153 -4.521  1.00 12.68 ?  53  LEU   B CD2  1 
ATOM   4735 H H    . LEU   B 1 53  ? 53.092 -22.634 -1.437  1.00 11.67 ?  53  LEU   B H    1 
ATOM   4736 H HA   . LEU   B 1 53  ? 53.886 -21.065 -3.369  1.00 12.15 ?  53  LEU   B HA   1 
ATOM   4737 H HB2  . LEU   B 1 53  ? 52.029 -20.509 -1.325  1.00 12.62 ?  53  LEU   B HB2  1 
ATOM   4738 H HB3  . LEU   B 1 53  ? 52.251 -19.560 -2.567  1.00 12.62 ?  53  LEU   B HB3  1 
ATOM   4739 H HG   . LEU   B 1 53  ? 51.109 -22.122 -2.739  1.00 13.13 ?  53  LEU   B HG   1 
ATOM   4740 H HD11 . LEU   B 1 53  ? 49.077 -21.052 -3.124  1.00 14.85 ?  53  LEU   B HD11 1 
ATOM   4741 H HD12 . LEU   B 1 53  ? 49.639 -20.680 -1.685  1.00 14.85 ?  53  LEU   B HD12 1 
ATOM   4742 H HD13 . LEU   B 1 53  ? 49.776 -19.646 -2.884  1.00 14.85 ?  53  LEU   B HD13 1 
ATOM   4743 H HD21 . LEU   B 1 53  ? 50.626 -21.655 -4.951  1.00 15.24 ?  53  LEU   B HD21 1 
ATOM   4744 H HD22 . LEU   B 1 53  ? 51.311 -20.230 -4.818  1.00 15.24 ?  53  LEU   B HD22 1 
ATOM   4745 H HD23 . LEU   B 1 53  ? 52.194 -21.548 -4.732  1.00 15.24 ?  53  LEU   B HD23 1 
ATOM   4746 N N    . ASN   B 1 54  ? 54.774 -20.109 -0.443  1.00 9.72  ?  54  ASN   B N    1 
ATOM   4747 C CA   . ASN   B 1 54  ? 55.686 -19.199 0.231   1.00 10.37 ?  54  ASN   B CA   1 
ATOM   4748 C C    . ASN   B 1 54  ? 57.133 -19.475 -0.167  1.00 10.50 ?  54  ASN   B C    1 
ATOM   4749 O O    . ASN   B 1 54  ? 57.909 -18.539 -0.400  1.00 10.84 ?  54  ASN   B O    1 
ATOM   4750 C CB   . ASN   B 1 54  ? 55.522 -19.283 1.742   1.00 10.98 ?  54  ASN   B CB   1 
ATOM   4751 C CG   . ASN   B 1 54  ? 56.498 -18.372 2.460   1.00 10.85 ?  54  ASN   B CG   1 
ATOM   4752 O OD1  . ASN   B 1 54  ? 56.521 -17.159 2.212   1.00 11.31 ?  54  ASN   B OD1  1 
ATOM   4753 N ND2  . ASN   B 1 54  ? 57.332 -18.945 3.317   1.00 12.67 ?  54  ASN   B ND2  1 
ATOM   4754 H H    . ASN   B 1 54  ? 54.332 -20.635 0.071   1.00 11.68 ?  54  ASN   B H    1 
ATOM   4755 H HA   . ASN   B 1 54  ? 55.474 -18.291 -0.042  1.00 12.46 ?  54  ASN   B HA   1 
ATOM   4756 H HB2  . ASN   B 1 54  ? 54.617 -19.009 1.977   1.00 13.20 ?  54  ASN   B HB2  1 
ATOM   4757 H HB3  . ASN   B 1 54  ? 55.683 -20.189 2.032   1.00 13.20 ?  54  ASN   B HB3  1 
ATOM   4758 H HD21 . ASN   B 1 54  ? 57.905 -18.467 3.744   1.00 15.22 ?  54  ASN   B HD21 1 
ATOM   4759 H HD22 . ASN   B 1 54  ? 57.292 -19.792 3.452   1.00 15.22 ?  54  ASN   B HD22 1 
ATOM   4760 N N    . LYS   B 1 55  ? 57.518 -20.751 -0.243  1.00 10.91 ?  55  LYS   B N    1 
ATOM   4761 C CA   . LYS   B 1 55  ? 58.876 -21.085 -0.658  1.00 12.08 ?  55  LYS   B CA   1 
ATOM   4762 C C    . LYS   B 1 55  ? 59.176 -20.540 -2.048  1.00 11.75 ?  55  LYS   B C    1 
ATOM   4763 O O    . LYS   B 1 55  ? 60.275 -20.031 -2.297  1.00 12.38 ?  55  LYS   B O    1 
ATOM   4764 C CB   . LYS   B 1 55  ? 59.079 -22.600 -0.607  1.00 13.29 ?  55  LYS   B CB   1 
ATOM   4765 C CG   . LYS   B 1 55  ? 60.471 -23.050 -0.988  1.00 17.28 ?  55  LYS   B CG   1 
ATOM   4766 C CD   . LYS   B 1 55  ? 60.634 -24.555 -0.869  1.00 20.68 ?  55  LYS   B CD   1 
ATOM   4767 C CE   . LYS   B 1 55  ? 60.543 -25.020 0.582   1.00 23.77 ?  55  LYS   B CE   1 
ATOM   4768 N NZ   . LYS   B 1 55  ? 61.059 -26.397 0.763   1.00 25.20 ?  55  LYS   B NZ   1 
ATOM   4769 H H    . LYS   B 1 55  ? 57.015 -21.427 -0.062  1.00 13.11 ?  55  LYS   B H    1 
ATOM   4770 H HA   . LYS   B 1 55  ? 59.500 -20.680 -0.036  1.00 14.51 ?  55  LYS   B HA   1 
ATOM   4771 H HB2  . LYS   B 1 55  ? 58.906 -22.903 0.299   1.00 15.97 ?  55  LYS   B HB2  1 
ATOM   4772 H HB3  . LYS   B 1 55  ? 58.455 -23.020 -1.217  1.00 15.97 ?  55  LYS   B HB3  1 
ATOM   4773 H HG2  . LYS   B 1 55  ? 60.648 -22.801 -1.909  1.00 20.75 ?  55  LYS   B HG2  1 
ATOM   4774 H HG3  . LYS   B 1 55  ? 61.117 -22.627 -0.398  1.00 20.75 ?  55  LYS   B HG3  1 
ATOM   4775 H HD2  . LYS   B 1 55  ? 59.930 -24.996 -1.372  1.00 24.83 ?  55  LYS   B HD2  1 
ATOM   4776 H HD3  . LYS   B 1 55  ? 61.504 -24.814 -1.213  1.00 24.83 ?  55  LYS   B HD3  1 
ATOM   4777 H HE2  . LYS   B 1 55  ? 61.066 -24.416 1.137   1.00 28.54 ?  55  LYS   B HE2  1 
ATOM   4778 H HE3  . LYS   B 1 55  ? 59.611 -24.998 0.860   1.00 28.54 ?  55  LYS   B HE3  1 
ATOM   4779 H HZ1  . LYS   B 1 55  ? 60.962 -26.646 1.612   1.00 30.26 ?  55  LYS   B HZ1  1 
ATOM   4780 H HZ2  . LYS   B 1 55  ? 60.606 -26.958 0.242   1.00 30.26 ?  55  LYS   B HZ2  1 
ATOM   4781 H HZ3  . LYS   B 1 55  ? 61.919 -26.428 0.546   1.00 30.26 ?  55  LYS   B HZ3  1 
ATOM   4782 N N    . ALA   B 1 56  ? 58.210 -20.624 -2.966  1.00 11.47 ?  56  ALA   B N    1 
ATOM   4783 C CA   . ALA   B 1 56  ? 58.432 -20.119 -4.315  1.00 12.12 ?  56  ALA   B CA   1 
ATOM   4784 C C    . ALA   B 1 56  ? 58.702 -18.621 -4.313  1.00 11.90 ?  56  ALA   B C    1 
ATOM   4785 O O    . ALA   B 1 56  ? 59.440 -18.123 -5.176  1.00 12.94 ?  56  ALA   B O    1 
ATOM   4786 C CB   . ALA   B 1 56  ? 57.239 -20.453 -5.206  1.00 13.36 ?  56  ALA   B CB   1 
ATOM   4787 H H    . ALA   B 1 56  ? 57.424 -20.952 -2.829  1.00 13.78 ?  56  ALA   B H    1 
ATOM   4788 H HA   . ALA   B 1 56  ? 59.213 -20.555 -4.682  1.00 14.56 ?  56  ALA   B HA   1 
ATOM   4789 H HB1  . ALA   B 1 56  ? 57.413 -20.116 -6.100  1.00 16.05 ?  56  ALA   B HB1  1 
ATOM   4790 H HB2  . ALA   B 1 56  ? 57.129 -21.416 -5.232  1.00 16.05 ?  56  ALA   B HB2  1 
ATOM   4791 H HB3  . ALA   B 1 56  ? 56.444 -20.036 -4.843  1.00 16.05 ?  56  ALA   B HB3  1 
ATOM   4792 N N    . THR   B 1 57  ? 58.139 -17.892 -3.346  1.00 11.77 ?  57  THR   B N    1 
ATOM   4793 C CA   . THR   B 1 57  ? 58.371 -16.457 -3.213  1.00 11.77 ?  57  THR   B CA   1 
ATOM   4794 C C    . THR   B 1 57  ? 59.619 -16.134 -2.399  1.00 12.30 ?  57  THR   B C    1 
ATOM   4795 O O    . THR   B 1 57  ? 59.850 -14.959 -2.086  1.00 12.91 ?  57  THR   B O    1 
ATOM   4796 C CB   . THR   B 1 57  ? 57.168 -15.737 -2.573  1.00 11.21 ?  57  THR   B CB   1 
ATOM   4797 O OG1  . THR   B 1 57  ? 57.144 -15.962 -1.157  1.00 11.21 ?  57  THR   B OG1  1 
ATOM   4798 C CG2  . THR   B 1 57  ? 55.850 -16.149 -3.217  1.00 11.34 ?  57  THR   B CG2  1 
ATOM   4799 H H    . THR   B 1 57  ? 57.600 -18.209 -2.750  1.00 14.14 ?  57  THR   B H    1 
ATOM   4800 H HA   . THR   B 1 57  ? 58.489 -16.085 -4.100  1.00 14.14 ?  57  THR   B HA   1 
ATOM   4801 H HB   . THR   B 1 57  ? 57.271 -14.785 -2.726  1.00 13.47 ?  57  THR   B HB   1 
ATOM   4802 H HG1  . THR   B 1 57  ? 57.073 -16.791 -1.003  1.00 13.48 ?  57  THR   B HG1  1 
ATOM   4803 H HG21 . THR   B 1 57  ? 55.119 -15.637 -2.839  1.00 13.62 ?  57  THR   B HG21 1 
ATOM   4804 H HG22 . THR   B 1 57  ? 55.882 -15.995 -4.175  1.00 13.62 ?  57  THR   B HG22 1 
ATOM   4805 H HG23 . THR   B 1 57  ? 55.682 -17.093 -3.060  1.00 13.62 ?  57  THR   B HG23 1 
ATOM   4806 N N    . ASN   B 1 58  ? 60.416 -17.139 -2.041  1.00 13.25 ?  58  ASN   B N    1 
ATOM   4807 C CA   . ASN   B 1 58  ? 61.614 -16.921 -1.235  1.00 16.07 ?  58  ASN   B CA   1 
ATOM   4808 C C    . ASN   B 1 58  ? 61.270 -16.213 0.076   1.00 13.81 ?  58  ASN   B C    1 
ATOM   4809 O O    . ASN   B 1 58  ? 61.999 -15.334 0.542   1.00 14.48 ?  58  ASN   B O    1 
ATOM   4810 C CB   . ASN   B 1 58  ? 62.697 -16.166 -2.014  1.00 24.95 ?  58  ASN   B CB   1 
ATOM   4811 C CG   . ASN   B 1 58  ? 64.058 -16.249 -1.350  1.00 34.39 ?  58  ASN   B CG   1 
ATOM   4812 O OD1  . ASN   B 1 58  ? 64.369 -17.225 -0.666  1.00 37.51 ?  58  ASN   B OD1  1 
ATOM   4813 N ND2  . ASN   B 1 58  ? 64.877 -15.220 -1.547  1.00 37.46 ?  58  ASN   B ND2  1 
ATOM   4814 H H    . ASN   B 1 58  ? 60.284 -17.964 -2.251  1.00 15.92 ?  58  ASN   B H    1 
ATOM   4815 H HA   . ASN   B 1 58  ? 61.985 -17.788 -1.007  1.00 19.30 ?  58  ASN   B HA   1 
ATOM   4816 H HB2  . ASN   B 1 58  ? 62.775 -16.549 -2.903  1.00 29.96 ?  58  ASN   B HB2  1 
ATOM   4817 H HB3  . ASN   B 1 58  ? 62.454 -15.231 -2.076  1.00 29.96 ?  58  ASN   B HB3  1 
ATOM   4818 H HD21 . ASN   B 1 58  ? 65.662 -15.219 -1.193  1.00 44.98 ?  58  ASN   B HD21 1 
ATOM   4819 H HD22 . ASN   B 1 58  ? 64.623 -14.555 -2.029  1.00 44.98 ?  58  ASN   B HD22 1 
ATOM   4820 N N    . ASN   B 1 59  ? 60.147 -16.604 0.677   1.00 12.81 ?  59  ASN   B N    1 
ATOM   4821 C CA   . ASN   B 1 59  ? 59.670 -16.135 1.979   1.00 12.82 ?  59  ASN   B CA   1 
ATOM   4822 C C    . ASN   B 1 59  ? 59.070 -14.729 1.926   1.00 12.18 ?  59  ASN   B C    1 
ATOM   4823 O O    . ASN   B 1 59  ? 58.631 -14.227 2.971   1.00 12.25 ?  59  ASN   B O    1 
ATOM   4824 C CB   . ASN   B 1 59  ? 60.740 -16.195 3.084   1.00 13.93 ?  59  ASN   B CB   1 
ATOM   4825 C CG   . ASN   B 1 59  ? 60.147 -16.372 4.462   1.00 15.11 ?  59  ASN   B CG   1 
ATOM   4826 O OD1  . ASN   B 1 59  ? 59.312 -17.253 4.682   1.00 15.36 ?  59  ASN   B OD1  1 
ATOM   4827 N ND2  . ASN   B 1 59  ? 60.566 -15.531 5.402   1.00 15.73 ?  59  ASN   B ND2  1 
ATOM   4828 H H    . ASN   B 1 59  ? 59.610 -17.178 0.329   1.00 15.39 ?  59  ASN   B H    1 
ATOM   4829 H HA   . ASN   B 1 59  ? 58.960 -16.730 2.260   1.00 15.40 ?  59  ASN   B HA   1 
ATOM   4830 H HB2  . ASN   B 1 59  ? 61.327 -16.949 2.923   1.00 16.73 ?  59  ASN   B HB2  1 
ATOM   4831 H HB3  . ASN   B 1 59  ? 61.248 -15.371 3.089   1.00 16.73 ?  59  ASN   B HB3  1 
ATOM   4832 H HD21 . ASN   B 1 59  ? 60.260 -15.589 6.207   1.00 18.90 ?  59  ASN   B HD21 1 
ATOM   4833 H HD22 . ASN   B 1 59  ? 61.148 -14.927 5.211   1.00 18.90 ?  59  ASN   B HD22 1 
ATOM   4834 N N    . ALA   B 1 60  ? 59.011 -14.081 0.759   1.00 12.27 ?  60  ALA   B N    1 
ATOM   4835 C CA   . ALA   B 1 60  ? 58.413 -12.751 0.693   1.00 12.06 ?  60  ALA   B CA   1 
ATOM   4836 C C    . ALA   B 1 60  ? 56.941 -12.778 1.084   1.00 11.09 ?  60  ALA   B C    1 
ATOM   4837 O O    . ALA   B 1 60  ? 56.437 -11.824 1.694   1.00 11.68 ?  60  ALA   B O    1 
ATOM   4838 C CB   . ALA   B 1 60  ? 58.597 -12.161 -0.708  1.00 12.91 ?  60  ALA   B CB   1 
ATOM   4839 H H    . ALA   B 1 60  ? 59.303 -14.387 0.014   1.00 14.75 ?  60  ALA   B H    1 
ATOM   4840 H HA   . ALA   B 1 60  ? 58.871 -12.172 1.318   1.00 14.50 ?  60  ALA   B HA   1 
ATOM   4841 H HB1  . ALA   B 1 60  ? 58.197 -11.281 -0.736  1.00 15.51 ?  60  ALA   B HB1  1 
ATOM   4842 H HB2  . ALA   B 1 60  ? 59.548 -12.101 -0.901  1.00 15.51 ?  60  ALA   B HB2  1 
ATOM   4843 H HB3  . ALA   B 1 60  ? 58.167 -12.743 -1.355  1.00 15.51 ?  60  ALA   B HB3  1 
ATOM   4844 N N    . MET   B 1 61  ? 56.237 -13.853 0.740   1.00 10.89 ?  61  MET   B N    1 
ATOM   4845 C CA   . MET   B 1 61  ? 54.840 -13.975 1.133   1.00 10.57 ?  61  MET   B CA   1 
ATOM   4846 C C    . MET   B 1 61  ? 54.701 -13.991 2.653   1.00 10.53 ?  61  MET   B C    1 
ATOM   4847 O O    . MET   B 1 61  ? 53.806 -13.338 3.207   1.00 10.60 ?  61  MET   B O    1 
ATOM   4848 C CB   . MET   B 1 61  ? 54.256 -15.238 0.501   1.00 10.36 ?  61  MET   B CB   1 
ATOM   4849 C CG   . MET   B 1 61  ? 52.809 -15.532 0.907   1.00 10.31 ?  61  MET   B CG   1 
ATOM   4850 S SD   . MET   B 1 61  ? 52.179 -17.040 0.148   1.00 10.95 ?  61  MET   B SD   1 
ATOM   4851 C CE   . MET   B 1 61  ? 51.931 -16.469 -1.533  1.00 12.44 ?  61  MET   B CE   1 
ATOM   4852 H H    . MET   B 1 61  ? 56.541 -14.518 0.283   1.00 13.09 ?  61  MET   B H    1 
ATOM   4853 H HA   . MET   B 1 61  ? 54.346 -13.220 0.778   1.00 12.71 ?  61  MET   B HA   1 
ATOM   4854 H HB2  . MET   B 1 61  ? 54.273 -15.147 -0.467  1.00 12.45 ?  61  MET   B HB2  1 
ATOM   4855 H HB3  . MET   B 1 61  ? 54.792 -16.002 0.764   1.00 12.45 ?  61  MET   B HB3  1 
ATOM   4856 H HG2  . MET   B 1 61  ? 52.759 -15.641 1.870   1.00 12.40 ?  61  MET   B HG2  1 
ATOM   4857 H HG3  . MET   B 1 61  ? 52.242 -14.793 0.628   1.00 12.40 ?  61  MET   B HG3  1 
ATOM   4858 H HE1  . MET   B 1 61  ? 51.557 -17.193 -2.060  1.00 14.95 ?  61  MET   B HE1  1 
ATOM   4859 H HE2  . MET   B 1 61  ? 51.321 -15.715 -1.526  1.00 14.95 ?  61  MET   B HE2  1 
ATOM   4860 H HE3  . MET   B 1 61  ? 52.786 -16.199 -1.904  1.00 14.95 ?  61  MET   B HE3  1 
ATOM   4861 N N    . GLN   B 1 62  ? 55.583 -14.715 3.351   1.00 10.48 ?  62  GLN   B N    1 
ATOM   4862 C CA   . GLN   B 1 62  ? 55.479 -14.778 4.806   1.00 10.91 ?  62  GLN   B CA   1 
ATOM   4863 C C    . GLN   B 1 62  ? 55.764 -13.426 5.448   1.00 11.30 ?  62  GLN   B C    1 
ATOM   4864 O O    . GLN   B 1 62  ? 55.075 -13.027 6.395   1.00 11.62 ?  62  GLN   B O    1 
ATOM   4865 C CB   . GLN   B 1 62  ? 56.425 -15.836 5.366   1.00 11.24 ?  62  GLN   B CB   1 
ATOM   4866 C CG   . GLN   B 1 62  ? 56.210 -16.100 6.847   1.00 11.42 ?  62  GLN   B CG   1 
ATOM   4867 C CD   . GLN   B 1 62  ? 54.839 -16.690 7.103   1.00 10.92 ?  62  GLN   B CD   1 
ATOM   4868 O OE1  . GLN   B 1 62  ? 54.582 -17.844 6.759   1.00 11.42 ?  62  GLN   B OE1  1 
ATOM   4869 N NE2  . GLN   B 1 62  ? 53.934 -15.888 7.659   1.00 11.50 ?  62  GLN   B NE2  1 
ATOM   4870 H H    . GLN   B 1 62  ? 56.230 -15.168 3.008   1.00 12.59 ?  62  GLN   B H    1 
ATOM   4871 H HA   . GLN   B 1 62  ? 54.571 -15.032 5.035   1.00 13.11 ?  62  GLN   B HA   1 
ATOM   4872 H HB2  . GLN   B 1 62  ? 56.286 -16.667 4.889   1.00 13.51 ?  62  GLN   B HB2  1 
ATOM   4873 H HB3  . GLN   B 1 62  ? 57.340 -15.532 5.240   1.00 13.51 ?  62  GLN   B HB3  1 
ATOM   4874 H HG2  . GLN   B 1 62  ? 56.879 -16.729 7.155   1.00 13.73 ?  62  GLN   B HG2  1 
ATOM   4875 H HG3  . GLN   B 1 62  ? 56.288 -15.263 7.336   1.00 13.73 ?  62  GLN   B HG3  1 
ATOM   4876 H HE21 . GLN   B 1 62  ? 54.150 -15.078 7.875   1.00 13.81 ?  62  GLN   B HE21 1 
ATOM   4877 H HE22 . GLN   B 1 62  ? 53.145 -16.176 7.819   1.00 13.81 ?  62  GLN   B HE22 1 
ATOM   4878 N N    . VAL   B 1 63  ? 56.777 -12.708 4.958   1.00 11.72 ?  63  VAL   B N    1 
ATOM   4879 C CA   . VAL   B 1 63  ? 57.083 -11.394 5.517   1.00 12.44 ?  63  VAL   B CA   1 
ATOM   4880 C C    . VAL   B 1 63  ? 55.890 -10.458 5.346   1.00 11.93 ?  63  VAL   B C    1 
ATOM   4881 O O    . VAL   B 1 63  ? 55.479 -9.759  6.282   1.00 12.80 ?  63  VAL   B O    1 
ATOM   4882 C CB   . VAL   B 1 63  ? 58.373 -10.833 4.889   1.00 13.93 ?  63  VAL   B CB   1 
ATOM   4883 C CG1  . VAL   B 1 63  ? 58.605 -9.399  5.338   1.00 14.66 ?  63  VAL   B CG1  1 
ATOM   4884 C CG2  . VAL   B 1 63  ? 59.562 -11.700 5.268   1.00 14.59 ?  63  VAL   B CG2  1 
ATOM   4885 H H    . VAL   B 1 63  ? 57.287 -12.952 4.308   1.00 14.09 ?  63  VAL   B H    1 
ATOM   4886 H HA   . VAL   B 1 63  ? 57.243 -11.496 6.465   1.00 14.94 ?  63  VAL   B HA   1 
ATOM   4887 H HB   . VAL   B 1 63  ? 58.292 -10.838 3.922   1.00 16.73 ?  63  VAL   B HB   1 
ATOM   4888 H HG11 . VAL   B 1 63  ? 59.520 -9.148  5.134   1.00 17.61 ?  63  VAL   B HG11 1 
ATOM   4889 H HG12 . VAL   B 1 63  ? 57.991 -8.814  4.868   1.00 17.61 ?  63  VAL   B HG12 1 
ATOM   4890 H HG13 . VAL   B 1 63  ? 58.455 -9.340  6.295   1.00 17.61 ?  63  VAL   B HG13 1 
ATOM   4891 H HG21 . VAL   B 1 63  ? 60.366 -11.323 4.878   1.00 17.53 ?  63  VAL   B HG21 1 
ATOM   4892 H HG22 . VAL   B 1 63  ? 59.641 -11.720 6.235   1.00 17.53 ?  63  VAL   B HG22 1 
ATOM   4893 H HG23 . VAL   B 1 63  ? 59.419 -12.597 4.929   1.00 17.53 ?  63  VAL   B HG23 1 
ATOM   4894 N N    . GLU   B 1 64  ? 55.314 -10.440 4.143   1.00 11.69 ?  64  GLU   B N    1 
ATOM   4895 C CA   . GLU   B 1 64  ? 54.147 -9.601  3.877   1.00 11.26 ?  64  GLU   B CA   1 
ATOM   4896 C C    . GLU   B 1 64  ? 52.964 -10.007 4.752   1.00 10.71 ?  64  GLU   B C    1 
ATOM   4897 O O    . GLU   B 1 64  ? 52.223 -9.149  5.260   1.00 11.61 ?  64  GLU   B O    1 
ATOM   4898 C CB   . GLU   B 1 64  ? 53.791 -9.731  2.396   1.00 11.28 ?  64  GLU   B CB   1 
ATOM   4899 C CG   . GLU   B 1 64  ? 52.529 -9.009  1.971   1.00 11.76 ?  64  GLU   B CG   1 
ATOM   4900 C CD   . GLU   B 1 64  ? 51.987 -9.505  0.636   1.00 12.36 ?  64  GLU   B CD   1 
ATOM   4901 O OE1  . GLU   B 1 64  ? 52.168 -10.707 0.305   1.00 13.24 ?  64  GLU   B OE1  1 
ATOM   4902 O OE2  . GLU   B 1 64  ? 51.359 -8.686  -0.081  1.00 13.38 -1 64  GLU   B OE2  1 
ATOM   4903 H H    . GLU   B 1 64  ? 55.582 -10.905 3.466   1.00 14.05 ?  64  GLU   B H    1 
ATOM   4904 H HA   . GLU   B 1 64  ? 54.371 -8.675  4.061   1.00 13.54 ?  64  GLU   B HA   1 
ATOM   4905 H HB2  . GLU   B 1 64  ? 54.525 -9.368  1.868   1.00 13.56 ?  64  GLU   B HB2  1 
ATOM   4906 H HB3  . GLU   B 1 64  ? 53.680 -10.670 2.188   1.00 13.56 ?  64  GLU   B HB3  1 
ATOM   4907 H HG2  . GLU   B 1 64  ? 51.836 -9.143  2.637   1.00 14.13 ?  64  GLU   B HG2  1 
ATOM   4908 H HG3  . GLU   B 1 64  ? 52.724 -8.061  1.888   1.00 14.13 ?  64  GLU   B HG3  1 
ATOM   4909 N N    . SER   B 1 65  ? 52.775 -11.314 4.930   1.00 10.72 ?  65  SER   B N    1 
ATOM   4910 C CA   . SER   B 1 65  ? 51.675 -11.826 5.733   1.00 10.90 ?  65  SER   B CA   1 
ATOM   4911 C C    . SER   B 1 65  ? 51.816 -11.425 7.197   1.00 11.03 ?  65  SER   B C    1 
ATOM   4912 O O    . SER   B 1 65  ? 50.824 -11.051 7.840   1.00 11.34 ?  65  SER   B O    1 
ATOM   4913 C CB   . SER   B 1 65  ? 51.603 -13.347 5.594   1.00 10.86 ?  65  SER   B CB   1 
ATOM   4914 O OG   . SER   B 1 65  ? 51.251 -13.735 4.270   1.00 11.06 ?  65  SER   B OG   1 
ATOM   4915 H H    . SER   B 1 65  ? 53.282 -11.930 4.599   1.00 12.89 ?  65  SER   B H    1 
ATOM   4916 H HA   . SER   B 1 65  ? 50.842 -11.455 5.400   1.00 13.10 ?  65  SER   B HA   1 
ATOM   4917 H HB2  . SER   B 1 65  ? 52.468 -13.722 5.809   1.00 13.05 ?  65  SER   B HB2  1 
ATOM   4918 H HB3  . SER   B 1 65  ? 50.931 -13.685 6.206   1.00 13.05 ?  65  SER   B HB3  1 
ATOM   4919 H HG   . SER   B 1 65  ? 51.825 -13.436 3.722   1.00 13.29 ?  65  SER   B HG   1 
ATOM   4920 N N    . ASP   B 1 66  ? 53.025 -11.533 7.758   1.00 11.32 ?  66  ASP   B N    1 
ATOM   4921 C CA   . ASP   B 1 66  ? 53.221 -11.147 9.153   1.00 11.82 ?  66  ASP   B CA   1 
ATOM   4922 C C    . ASP   B 1 66  ? 52.910 -9.669  9.361   1.00 11.97 ?  66  ASP   B C    1 
ATOM   4923 O O    . ASP   B 1 66  ? 52.333 -9.282  10.384  1.00 12.24 ?  66  ASP   B O    1 
ATOM   4924 C CB   . ASP   B 1 66  ? 54.651 -11.463 9.597   1.00 13.12 ?  66  ASP   B CB   1 
ATOM   4925 C CG   . ASP   B 1 66  ? 54.911 -12.956 9.740   1.00 15.11 ?  66  ASP   B CG   1 
ATOM   4926 O OD1  . ASP   B 1 66  ? 53.954 -13.760 9.673   1.00 15.75 ?  66  ASP   B OD1  1 
ATOM   4927 O OD2  . ASP   B 1 66  ? 56.090 -13.329 9.926   1.00 17.76 -1 66  ASP   B OD2  1 
ATOM   4928 H H    . ASP   B 1 66  ? 53.729 -11.829 7.363   1.00 13.60 ?  66  ASP   B H    1 
ATOM   4929 H HA   . ASP   B 1 66  ? 52.618 -11.655 9.715   1.00 14.20 ?  66  ASP   B HA   1 
ATOM   4930 H HB2  . ASP   B 1 66  ? 55.270 -11.109 8.941   1.00 15.76 ?  66  ASP   B HB2  1 
ATOM   4931 H HB3  . ASP   B 1 66  ? 54.811 -11.041 10.461  1.00 15.76 ?  66  ASP   B HB3  1 
ATOM   4932 N N    . ASP   B 1 67  ? 53.284 -8.823  8.400   1.00 11.72 ?  67  ASP   B N    1 
ATOM   4933 C CA   . ASP   B 1 67  ? 52.939 -7.410  8.498   1.00 12.05 ?  67  ASP   B CA   1 
ATOM   4934 C C    . ASP   B 1 67  ? 51.428 -7.201  8.414   1.00 12.03 ?  67  ASP   B C    1 
ATOM   4935 O O    . ASP   B 1 67  ? 50.864 -6.394  9.162   1.00 12.70 ?  67  ASP   B O    1 
ATOM   4936 C CB   . ASP   B 1 67  ? 53.664 -6.632  7.409   1.00 13.64 ?  67  ASP   B CB   1 
ATOM   4937 C CG   . ASP   B 1 67  ? 53.257 -5.189  7.385   1.00 15.01 ?  67  ASP   B CG   1 
ATOM   4938 O OD1  . ASP   B 1 67  ? 53.764 -4.401  8.216   1.00 15.91 ?  67  ASP   B OD1  1 
ATOM   4939 O OD2  . ASP   B 1 67  ? 52.400 -4.864  6.547   1.00 16.18 -1 67  ASP   B OD2  1 
ATOM   4940 H H    . ASP   B 1 67  ? 53.738 -9.037  7.698   1.00 14.08 ?  67  ASP   B H    1 
ATOM   4941 H HA   . ASP   B 1 67  ? 53.242 -7.071  9.353   1.00 14.48 ?  67  ASP   B HA   1 
ATOM   4942 H HB2  . ASP   B 1 67  ? 54.622 -6.667  7.570   1.00 16.39 ?  67  ASP   B HB2  1 
ATOM   4943 H HB3  . ASP   B 1 67  ? 53.461 -7.021  6.543   1.00 16.39 ?  67  ASP   B HB3  1 
ATOM   4944 N N    . TYR   B 1 68  ? 50.749 -7.933  7.525   1.00 11.55 ?  68  TYR   B N    1 
ATOM   4945 C CA   . TYR   B 1 68  ? 49.293 -7.848  7.451   1.00 12.46 ?  68  TYR   B CA   1 
ATOM   4946 C C    . TYR   B 1 68  ? 48.654 -8.192  8.793   1.00 11.95 ?  68  TYR   B C    1 
ATOM   4947 O O    . TYR   B 1 68  ? 47.728 -7.508  9.244   1.00 12.39 ?  68  TYR   B O    1 
ATOM   4948 C CB   . TYR   B 1 68  ? 48.756 -8.773  6.350   1.00 13.11 ?  68  TYR   B CB   1 
ATOM   4949 C CG   . TYR   B 1 68  ? 47.249 -8.920  6.402   1.00 14.43 ?  68  TYR   B CG   1 
ATOM   4950 C CD1  . TYR   B 1 68  ? 46.656 -9.877  7.217   1.00 15.48 ?  68  TYR   B CD1  1 
ATOM   4951 C CD2  . TYR   B 1 68  ? 46.426 -8.074  5.682   1.00 15.73 ?  68  TYR   B CD2  1 
ATOM   4952 C CE1  . TYR   B 1 68  ? 45.291 -9.999  7.302   1.00 16.63 ?  68  TYR   B CE1  1 
ATOM   4953 C CE2  . TYR   B 1 68  ? 45.042 -8.196  5.754   1.00 16.16 ?  68  TYR   B CE2  1 
ATOM   4954 C CZ   . TYR   B 1 68  ? 44.493 -9.157  6.570   1.00 16.28 ?  68  TYR   B CZ   1 
ATOM   4955 O OH   . TYR   B 1 68  ? 43.124 -9.268  6.655   1.00 17.36 ?  68  TYR   B OH   1 
ATOM   4956 H H    . TYR   B 1 68  ? 51.105 -8.491  6.970   1.00 13.87 ?  68  TYR   B H    1 
ATOM   4957 H HA   . TYR   B 1 68  ? 49.047 -6.941  7.232   1.00 14.97 ?  68  TYR   B HA   1 
ATOM   4958 H HB2  . TYR   B 1 68  ? 48.989 -8.399  5.488   1.00 15.75 ?  68  TYR   B HB2  1 
ATOM   4959 H HB3  . TYR   B 1 68  ? 49.149 -9.652  6.454   1.00 15.75 ?  68  TYR   B HB3  1 
ATOM   4960 H HD1  . TYR   B 1 68  ? 47.194 -10.454 7.716   1.00 18.60 ?  68  TYR   B HD1  1 
ATOM   4961 H HD2  . TYR   B 1 68  ? 46.801 -7.419  5.147   1.00 18.89 ?  68  TYR   B HD2  1 
ATOM   4962 H HE1  . TYR   B 1 68  ? 44.905 -10.659 7.840   1.00 19.98 ?  68  TYR   B HE1  1 
ATOM   4963 H HE2  . TYR   B 1 68  ? 44.492 -7.626  5.269   1.00 19.42 ?  68  TYR   B HE2  1 
ATOM   4964 H HH   . TYR   B 1 68  ? 42.749 -8.706  6.146   1.00 20.85 ?  68  TYR   B HH   1 
ATOM   4965 N N    . ILE   B 1 69  ? 49.125 -9.266  9.435   1.00 11.75 ?  69  ILE   B N    1 
ATOM   4966 C CA   . ILE   B 1 69  ? 48.564 -9.695  10.714  1.00 12.33 ?  69  ILE   B CA   1 
ATOM   4967 C C    . ILE   B 1 69  ? 48.824 -8.655  11.796  1.00 12.18 ?  69  ILE   B C    1 
ATOM   4968 O O    . ILE   B 1 69  ? 47.959 -8.381  12.633  1.00 12.74 ?  69  ILE   B O    1 
ATOM   4969 C CB   . ILE   B 1 69  ? 49.135 -11.072 11.107  1.00 13.17 ?  69  ILE   B CB   1 
ATOM   4970 C CG1  . ILE   B 1 69  ? 48.610 -12.172 10.180  1.00 13.47 ?  69  ILE   B CG1  1 
ATOM   4971 C CG2  . ILE   B 1 69  ? 48.828 -11.385 12.563  1.00 14.36 ?  69  ILE   B CG2  1 
ATOM   4972 C CD1  . ILE   B 1 69  ? 47.128 -12.450 10.304  1.00 13.76 ?  69  ILE   B CD1  1 
ATOM   4973 H H    . ILE   B 1 69  ? 49.770 -9.757  9.156   1.00 14.12 ?  69  ILE   B H    1 
ATOM   4974 H HA   . ILE   B 1 69  ? 47.606 -9.787  10.620  1.00 14.82 ?  69  ILE   B HA   1 
ATOM   4975 H HB   . ILE   B 1 69  ? 50.103 -11.034 11.009  1.00 15.82 ?  69  ILE   B HB   1 
ATOM   4976 H HG12 . ILE   B 1 69  ? 48.787 -11.908 9.263   1.00 16.19 ?  69  ILE   B HG12 1 
ATOM   4977 H HG13 . ILE   B 1 69  ? 49.083 -12.994 10.380  1.00 16.19 ?  69  ILE   B HG13 1 
ATOM   4978 H HG21 . ILE   B 1 69  ? 48.952 -12.338 12.707  1.00 17.26 ?  69  ILE   B HG21 1 
ATOM   4979 H HG22 . ILE   B 1 69  ? 49.430 -10.887 13.134  1.00 17.26 ?  69  ILE   B HG22 1 
ATOM   4980 H HG23 . ILE   B 1 69  ? 47.908 -11.143 12.749  1.00 17.26 ?  69  ILE   B HG23 1 
ATOM   4981 H HD11 . ILE   B 1 69  ? 46.902 -13.182 9.718   1.00 16.54 ?  69  ILE   B HD11 1 
ATOM   4982 H HD12 . ILE   B 1 69  ? 46.926 -12.682 11.224  1.00 16.54 ?  69  ILE   B HD12 1 
ATOM   4983 H HD13 . ILE   B 1 69  ? 46.636 -11.653 10.048  1.00 16.54 ?  69  ILE   B HD13 1 
ATOM   4984 N N    . ALA   B 1 70  ? 50.022 -8.074  11.820  1.00 12.09 ?  70  ALA   B N    1 
ATOM   4985 C CA   . ALA   B 1 70  ? 50.304 -7.044  12.813  1.00 12.02 ?  70  ALA   B CA   1 
ATOM   4986 C C    . ALA   B 1 70  ? 49.315 -5.891  12.701  1.00 12.02 ?  70  ALA   B C    1 
ATOM   4987 O O    . ALA   B 1 70  ? 48.865 -5.352  13.716  1.00 12.52 ?  70  ALA   B O    1 
ATOM   4988 C CB   . ALA   B 1 70  ? 51.742 -6.546  12.660  1.00 12.81 ?  70  ALA   B CB   1 
ATOM   4989 H H    . ALA   B 1 70  ? 50.665 -8.255  11.291  1.00 14.53 ?  70  ALA   B H    1 
ATOM   4990 H HA   . ALA   B 1 70  ? 50.219 -7.425  13.703  1.00 14.44 ?  70  ALA   B HA   1 
ATOM   4991 H HB1  . ALA   B 1 70  ? 51.927 -5.886  13.349  1.00 15.39 ?  70  ALA   B HB1  1 
ATOM   4992 H HB2  . ALA   B 1 70  ? 52.351 -7.298  12.759  1.00 15.39 ?  70  ALA   B HB2  1 
ATOM   4993 H HB3  . ALA   B 1 70  ? 51.851 -6.149  11.783  1.00 15.39 ?  70  ALA   B HB3  1 
ATOM   4994 N N    . THR   B 1 71  ? 48.951 -5.512  11.475  1.00 12.39 ?  71  THR   B N    1 
ATOM   4995 C CA   . THR   B 1 71  ? 48.062 -4.375  11.261  1.00 13.30 ?  71  THR   B CA   1 
ATOM   4996 C C    . THR   B 1 71  ? 46.593 -4.736  11.468  1.00 13.73 ?  71  THR   B C    1 
ATOM   4997 O O    . THR   B 1 71  ? 45.820 -3.922  11.987  1.00 15.28 ?  71  THR   B O    1 
ATOM   4998 C CB   . THR   B 1 71  ? 48.284 -3.816  9.853   1.00 15.43 ?  71  THR   B CB   1 
ATOM   4999 O OG1  . THR   B 1 71  ? 49.610 -3.285  9.756   1.00 17.54 ?  71  THR   B OG1  1 
ATOM   5000 C CG2  . THR   B 1 71  ? 47.276 -2.720  9.525   1.00 16.54 ?  71  THR   B CG2  1 
ATOM   5001 H H    . THR   B 1 71  ? 49.213 -5.895  10.755  1.00 14.88 ?  71  THR   B H    1 
ATOM   5002 H HA   . THR   B 1 71  ? 48.289 -3.673  11.893  1.00 15.98 ?  71  THR   B HA   1 
ATOM   5003 H HB   . THR   B 1 71  ? 48.182 -4.528  9.203   1.00 18.54 ?  71  THR   B HB   1 
ATOM   5004 H HG1  . THR   B 1 71  ? 49.740 -2.966  8.985   1.00 21.07 ?  71  THR   B HG1  1 
ATOM   5005 H HG21 . THR   B 1 71  ? 47.580 -2.208  8.757   1.00 19.87 ?  71  THR   B HG21 1 
ATOM   5006 H HG22 . THR   B 1 71  ? 46.413 -3.109  9.317   1.00 19.87 ?  71  THR   B HG22 1 
ATOM   5007 H HG23 . THR   B 1 71  ? 47.180 -2.119  10.281  1.00 19.87 ?  71  THR   B HG23 1 
ATOM   5008 N N    . ASN   B 1 72  ? 46.191 -5.949  11.074  1.00 13.57 ?  72  ASN   B N    1 
ATOM   5009 C CA   . ASN   B 1 72  ? 44.786 -6.303  10.946  1.00 14.28 ?  72  ASN   B CA   1 
ATOM   5010 C C    . ASN   B 1 72  ? 44.309 -7.404  11.884  1.00 14.70 ?  72  ASN   B C    1 
ATOM   5011 O O    . ASN   B 1 72  ? 43.093 -7.559  12.048  1.00 15.74 ?  72  ASN   B O    1 
ATOM   5012 C CB   . ASN   B 1 72  ? 44.479 -6.719  9.498   1.00 15.28 ?  72  ASN   B CB   1 
ATOM   5013 C CG   . ASN   B 1 72  ? 44.755 -5.609  8.515   1.00 16.25 ?  72  ASN   B CG   1 
ATOM   5014 O OD1  . ASN   B 1 72  ? 45.772 -5.612  7.815   1.00 17.46 ?  72  ASN   B OD1  1 
ATOM   5015 N ND2  . ASN   B 1 72  ? 43.872 -4.628  8.484   1.00 17.68 ?  72  ASN   B ND2  1 
ATOM   5016 H H    . ASN   B 1 72  ? 46.732 -6.592  10.870  1.00 16.30 ?  72  ASN   B H    1 
ATOM   5017 H HA   . ASN   B 1 72  ? 44.258 -5.514  11.136  1.00 17.16 ?  72  ASN   B HA   1 
ATOM   5018 H HB2  . ASN   B 1 72  ? 45.039 -7.474  9.257   1.00 18.36 ?  72  ASN   B HB2  1 
ATOM   5019 H HB3  . ASN   B 1 72  ? 43.546 -6.955  9.425   1.00 18.36 ?  72  ASN   B HB3  1 
ATOM   5020 H HD21 . ASN   B 1 72  ? 43.976 -3.965  7.944   1.00 21.24 ?  72  ASN   B HD21 1 
ATOM   5021 H HD22 . ASN   B 1 72  ? 43.174 -4.660  8.988   1.00 21.24 ?  72  ASN   B HD22 1 
ATOM   5022 N N    . GLY   B 1 73  ? 45.210 -8.160  12.504  1.00 14.09 ?  73  GLY   B N    1 
ATOM   5023 C CA   . GLY   B 1 73  ? 44.817 -9.307  13.286  1.00 13.73 ?  73  GLY   B CA   1 
ATOM   5024 C C    . GLY   B 1 73  ? 44.447 -10.489 12.417  1.00 12.63 ?  73  GLY   B C    1 
ATOM   5025 O O    . GLY   B 1 73  ? 44.427 -10.402 11.187  1.00 12.43 ?  73  GLY   B O    1 
ATOM   5026 H H    . GLY   B 1 73  ? 46.061 -8.029  12.474  1.00 16.93 ?  73  GLY   B H    1 
ATOM   5027 H HA2  . GLY   B 1 73  ? 45.546 -9.565  13.868  1.00 16.50 ?  73  GLY   B HA2  1 
ATOM   5028 H HA3  . GLY   B 1 73  ? 44.050 -9.075  13.832  1.00 16.50 ?  73  GLY   B HA3  1 
ATOM   5029 N N    . PRO   B 1 74  ? 44.147 -11.618 13.051  1.00 12.86 ?  74  PRO   B N    1 
ATOM   5030 C CA   . PRO   B 1 74  ? 43.887 -12.845 12.298  1.00 12.34 ?  74  PRO   B CA   1 
ATOM   5031 C C    . PRO   B 1 74  ? 42.584 -12.782 11.512  1.00 11.50 ?  74  PRO   B C    1 
ATOM   5032 O O    . PRO   B 1 74  ? 41.643 -12.046 11.836  1.00 12.74 ?  74  PRO   B O    1 
ATOM   5033 C CB   . PRO   B 1 74  ? 43.815 -13.916 13.393  1.00 13.42 ?  74  PRO   B CB   1 
ATOM   5034 C CG   . PRO   B 1 74  ? 43.370 -13.171 14.606  1.00 14.76 ?  74  PRO   B CG   1 
ATOM   5035 C CD   . PRO   B 1 74  ? 44.041 -11.832 14.503  1.00 14.38 ?  74  PRO   B CD   1 
ATOM   5036 H HA   . PRO   B 1 74  ? 44.629 -13.042 11.697  1.00 14.82 ?  74  PRO   B HA   1 
ATOM   5037 H HB2  . PRO   B 1 74  ? 43.169 -14.595 13.146  1.00 16.12 ?  74  PRO   B HB2  1 
ATOM   5038 H HB3  . PRO   B 1 74  ? 44.693 -14.308 13.530  1.00 16.12 ?  74  PRO   B HB3  1 
ATOM   5039 H HG2  . PRO   B 1 74  ? 42.407 -13.077 14.592  1.00 17.73 ?  74  PRO   B HG2  1 
ATOM   5040 H HG3  . PRO   B 1 74  ? 43.662 -13.642 15.401  1.00 17.73 ?  74  PRO   B HG3  1 
ATOM   5041 H HD2  . PRO   B 1 74  ? 43.486 -11.145 14.911  1.00 17.28 ?  74  PRO   B HD2  1 
ATOM   5042 H HD3  . PRO   B 1 74  ? 44.923 -11.859 14.904  1.00 17.28 ?  74  PRO   B HD3  1 
ATOM   5043 N N    . LEU   B 1 75  ? 42.552 -13.591 10.453  1.00 10.92 ?  75  LEU   B N    1 
ATOM   5044 C CA   . LEU   B 1 75  ? 41.341 -13.819 9.685   1.00 10.97 ?  75  LEU   B CA   1 
ATOM   5045 C C    . LEU   B 1 75  ? 40.369 -14.684 10.486  1.00 11.41 ?  75  LEU   B C    1 
ATOM   5046 O O    . LEU   B 1 75  ? 40.709 -15.237 11.533  1.00 12.37 ?  75  LEU   B O    1 
ATOM   5047 C CB   . LEU   B 1 75  ? 41.674 -14.524 8.368   1.00 11.30 ?  75  LEU   B CB   1 
ATOM   5048 C CG   . LEU   B 1 75  ? 42.508 -13.756 7.335   1.00 12.88 ?  75  LEU   B CG   1 
ATOM   5049 C CD1  . LEU   B 1 75  ? 42.699 -14.595 6.072   1.00 14.51 ?  75  LEU   B CD1  1 
ATOM   5050 C CD2  . LEU   B 1 75  ? 41.896 -12.427 6.990   1.00 16.38 ?  75  LEU   B CD2  1 
ATOM   5051 H H    . LEU   B 1 75  ? 43.233 -14.030 10.155  1.00 13.12 ?  75  LEU   B H    1 
ATOM   5052 H HA   . LEU   B 1 75  ? 40.912 -12.975 9.487   1.00 13.19 ?  75  LEU   B HA   1 
ATOM   5053 H HB2  . LEU   B 1 75  ? 42.162 -15.337 8.574   1.00 13.59 ?  75  LEU   B HB2  1 
ATOM   5054 H HB3  . LEU   B 1 75  ? 40.838 -14.763 7.932   1.00 13.59 ?  75  LEU   B HB3  1 
ATOM   5055 H HG   . LEU   B 1 75  ? 43.385 -13.590 7.708   1.00 15.48 ?  75  LEU   B HG   1 
ATOM   5056 H HD11 . LEU   B 1 75  ? 43.232 -14.092 5.434   1.00 17.43 ?  75  LEU   B HD11 1 
ATOM   5057 H HD12 . LEU   B 1 75  ? 43.157 -15.420 6.303   1.00 17.43 ?  75  LEU   B HD12 1 
ATOM   5058 H HD13 . LEU   B 1 75  ? 41.831 -14.798 5.688   1.00 17.43 ?  75  LEU   B HD13 1 
ATOM   5059 H HD21 . LEU   B 1 75  ? 42.404 -12.023 6.272   1.00 19.68 ?  75  LEU   B HD21 1 
ATOM   5060 H HD22 . LEU   B 1 75  ? 40.978 -12.567 6.713   1.00 19.68 ?  75  LEU   B HD22 1 
ATOM   5061 H HD23 . LEU   B 1 75  ? 41.922 -11.858 7.776   1.00 19.68 ?  75  LEU   B HD23 1 
ATOM   5062 N N    . LYS   B 1 76  ? 39.141 -14.790 9.975   1.00 12.50 ?  76  LYS   B N    1 
ATOM   5063 C CA   . LYS   B 1 76  ? 38.148 -15.752 10.442  1.00 13.74 ?  76  LYS   B CA   1 
ATOM   5064 C C    . LYS   B 1 76  ? 38.232 -17.019 9.592   1.00 12.14 ?  76  LYS   B C    1 
ATOM   5065 O O    . LYS   B 1 76  ? 38.502 -16.955 8.393   1.00 11.70 ?  76  LYS   B O    1 
ATOM   5066 C CB   . LYS   B 1 76  ? 36.729 -15.177 10.272  1.00 16.55 ?  76  LYS   B CB   1 
ATOM   5067 C CG   . LYS   B 1 76  ? 36.469 -13.782 10.863  1.00 18.73 ?  76  LYS   B CG   1 
ATOM   5068 C CD   . LYS   B 1 76  ? 35.075 -13.239 10.486  1.00 20.38 ?  76  LYS   B CD   1 
ATOM   5069 C CE   . LYS   B 1 76  ? 34.809 -11.870 11.099  1.00 22.33 ?  76  LYS   B CE   1 
ATOM   5070 N NZ   . LYS   B 1 76  ? 33.532 -11.263 10.618  1.00 23.16 ?  76  LYS   B NZ   1 
ATOM   5071 H H    . LYS   B 1 76  ? 38.853 -14.300 9.333   1.00 15.02 ?  76  LYS   B H    1 
ATOM   5072 H HA   . LYS   B 1 76  ? 38.297 -15.978 11.376  1.00 16.51 ?  76  LYS   B HA   1 
ATOM   5073 H HB2  . LYS   B 1 76  ? 36.538 -15.125 9.321   1.00 19.88 ?  76  LYS   B HB2  1 
ATOM   5074 H HB3  . LYS   B 1 76  ? 36.101 -15.786 10.691  1.00 19.88 ?  76  LYS   B HB3  1 
ATOM   5075 H HG2  . LYS   B 1 76  ? 36.526 -13.832 11.830  1.00 22.50 ?  76  LYS   B HG2  1 
ATOM   5076 H HG3  . LYS   B 1 76  ? 37.139 -13.164 10.523  1.00 22.50 ?  76  LYS   B HG3  1 
ATOM   5077 H HD2  . LYS   B 1 76  ? 35.020 -13.156 9.520   1.00 24.48 ?  76  LYS   B HD2  1 
ATOM   5078 H HD3  . LYS   B 1 76  ? 34.400 -13.855 10.808  1.00 24.48 ?  76  LYS   B HD3  1 
ATOM   5079 H HE2  . LYS   B 1 76  ? 34.753 -11.962 12.063  1.00 26.82 ?  76  LYS   B HE2  1 
ATOM   5080 H HE3  . LYS   B 1 76  ? 35.535 -11.272 10.864  1.00 26.82 ?  76  LYS   B HE3  1 
ATOM   5081 H HZ1  . LYS   B 1 76  ? 33.411 -10.464 10.999  1.00 27.81 ?  76  LYS   B HZ1  1 
ATOM   5082 H HZ2  . LYS   B 1 76  ? 33.556 -11.157 9.734   1.00 27.81 ?  76  LYS   B HZ2  1 
ATOM   5083 H HZ3  . LYS   B 1 76  ? 32.844 -11.787 10.828  1.00 27.81 ?  76  LYS   B HZ3  1 
ATOM   5084 N N    . VAL   B 1 77  ? 37.979 -18.181 10.207  1.00 12.45 ?  77  VAL   B N    1 
ATOM   5085 C CA   . VAL   B 1 77  ? 37.768 -19.387 9.409   1.00 12.36 ?  77  VAL   B CA   1 
ATOM   5086 C C    . VAL   B 1 77  ? 36.577 -19.149 8.493   1.00 11.42 ?  77  VAL   B C    1 
ATOM   5087 O O    . VAL   B 1 77  ? 35.514 -18.691 8.935   1.00 11.64 ?  77  VAL   B O    1 
ATOM   5088 C CB   . VAL   B 1 77  ? 37.578 -20.624 10.299  1.00 13.33 ?  77  VAL   B CB   1 
ATOM   5089 C CG1  . VAL   B 1 77  ? 37.294 -21.847 9.436   1.00 14.17 ?  77  VAL   B CG1  1 
ATOM   5090 C CG2  . VAL   B 1 77  ? 38.811 -20.857 11.167  1.00 14.82 ?  77  VAL   B CG2  1 
ATOM   5091 H H    . VAL   B 1 77  ? 37.924 -18.290 11.056  1.00 14.96 ?  77  VAL   B H    1 
ATOM   5092 H HA   . VAL   B 1 77  ? 38.542 -19.534 8.851   1.00 14.85 ?  77  VAL   B HA   1 
ATOM   5093 H HB   . VAL   B 1 77  ? 36.813 -20.480 10.886  1.00 16.02 ?  77  VAL   B HB   1 
ATOM   5094 H HG11 . VAL   B 1 77  ? 37.338 -22.638 9.994   1.00 17.02 ?  77  VAL   B HG11 1 
ATOM   5095 H HG12 . VAL   B 1 77  ? 36.404 -21.767 9.052   1.00 17.02 ?  77  VAL   B HG12 1 
ATOM   5096 H HG13 . VAL   B 1 77  ? 37.956 -21.895 8.734   1.00 17.02 ?  77  VAL   B HG13 1 
ATOM   5097 H HG21 . VAL   B 1 77  ? 38.677 -21.660 11.690  1.00 17.81 ?  77  VAL   B HG21 1 
ATOM   5098 H HG22 . VAL   B 1 77  ? 39.581 -20.955 10.591  1.00 17.81 ?  77  VAL   B HG22 1 
ATOM   5099 H HG23 . VAL   B 1 77  ? 38.929 -20.093 11.755  1.00 17.81 ?  77  VAL   B HG23 1 
ATOM   5100 N N    . GLY   B 1 78  ? 36.761 -19.424 7.204   1.00 10.86 ?  78  GLY   B N    1 
ATOM   5101 C CA   . GLY   B 1 78  ? 35.792 -19.094 6.186   1.00 10.81 ?  78  GLY   B CA   1 
ATOM   5102 C C    . GLY   B 1 78  ? 36.038 -17.772 5.494   1.00 10.08 ?  78  GLY   B C    1 
ATOM   5103 O O    . GLY   B 1 78  ? 35.364 -17.485 4.500   1.00 10.65 ?  78  GLY   B O    1 
ATOM   5104 H H    . GLY   B 1 78  ? 37.464 -19.809 6.894   1.00 13.05 ?  78  GLY   B H    1 
ATOM   5105 H HA2  . GLY   B 1 78  ? 35.788 -19.789 5.512   1.00 13.00 ?  78  GLY   B HA2  1 
ATOM   5106 H HA3  . GLY   B 1 78  ? 34.910 -19.052 6.585   1.00 13.00 ?  78  GLY   B HA3  1 
ATOM   5107 N N    . GLY   B 1 79  ? 36.984 -16.969 5.990   1.00 10.31 ?  79  GLY   B N    1 
ATOM   5108 C CA   . GLY   B 1 79  ? 37.291 -15.670 5.430   1.00 10.18 ?  79  GLY   B CA   1 
ATOM   5109 C C    . GLY   B 1 79  ? 38.525 -15.688 4.534   1.00 9.56  ?  79  GLY   B C    1 
ATOM   5110 O O    . GLY   B 1 79  ? 39.130 -16.725 4.269   1.00 9.91  ?  79  GLY   B O    1 
ATOM   5111 H H    . GLY   B 1 79  ? 37.477 -17.169 6.663   1.00 12.40 ?  79  GLY   B H    1 
ATOM   5112 H HA2  . GLY   B 1 79  ? 36.539 -15.354 4.904   1.00 12.24 ?  79  GLY   B HA2  1 
ATOM   5113 H HA3  . GLY   B 1 79  ? 37.450 -15.037 6.147   1.00 12.24 ?  79  GLY   B HA3  1 
ATOM   5114 N N    . SER   B 1 80  ? 38.889 -14.490 4.063   1.00 9.83  ?  80  SER   B N    1 
ATOM   5115 C CA   . SER   B 1 80  ? 39.993 -14.350 3.123   1.00 9.71  ?  80  SER   B CA   1 
ATOM   5116 C C    . SER   B 1 80  ? 40.576 -12.944 3.184   1.00 9.51  ?  80  SER   B C    1 
ATOM   5117 O O    . SER   B 1 80  ? 39.960 -12.011 3.703   1.00 10.83 ?  80  SER   B O    1 
ATOM   5118 C CB   . SER   B 1 80  ? 39.544 -14.642 1.688   1.00 10.36 ?  80  SER   B CB   1 
ATOM   5119 O OG   . SER   B 1 80  ? 38.709 -13.614 1.187   1.00 11.28 ?  80  SER   B OG   1 
ATOM   5120 H H    . SER   B 1 80  ? 38.513 -13.744 4.271   1.00 11.82 ?  80  SER   B H    1 
ATOM   5121 H HA   . SER   B 1 80  ? 40.685 -14.983 3.360   1.00 11.68 ?  80  SER   B HA   1 
ATOM   5122 H HB2  . SER   B 1 80  ? 40.323 -14.708 1.113   1.00 12.45 ?  80  SER   B HB2  1 
ATOM   5123 H HB3  . SER   B 1 80  ? 39.051 -15.479 1.670   1.00 12.45 ?  80  SER   B HB3  1 
ATOM   5124 H HG   . SER   B 1 80  ? 38.016 -13.545 1.669   1.00 13.56 ?  80  SER   B HG   1 
ATOM   5125 N N    . CYS   B 1 81  ? 41.761 -12.801 2.596   1.00 9.49  ?  81  CYS   B N    1 
ATOM   5126 C CA   . CYS   B 1 81  ? 42.305 -11.488 2.298   1.00 9.72  ?  81  CYS   B CA   1 
ATOM   5127 C C    . CYS   B 1 81  ? 43.081 -11.566 0.993   1.00 8.85  ?  81  CYS   B C    1 
ATOM   5128 O O    . CYS   B 1 81  ? 43.596 -12.627 0.622   1.00 9.78  ?  81  CYS   B O    1 
ATOM   5129 C CB   . CYS   B 1 81  ? 43.187 -10.940 3.430   1.00 10.62 ?  81  CYS   B CB   1 
ATOM   5130 S SG   . CYS   B 1 81  ? 44.709 -11.873 3.681   1.00 10.86 ?  81  CYS   B SG   1 
ATOM   5131 H H    . CYS   B 1 81  ? 42.265 -13.452 2.340   1.00 11.41 ?  81  CYS   B H    1 
ATOM   5132 H HA   . CYS   B 1 81  ? 41.572 -10.862 2.168   1.00 11.68 ?  81  CYS   B HA   1 
ATOM   5133 H HB2  . CYS   B 1 81  ? 43.434 -10.024 3.227   1.00 12.76 ?  81  CYS   B HB2  1 
ATOM   5134 H HB3  . CYS   B 1 81  ? 42.681 -10.964 4.261   1.00 12.76 ?  81  CYS   B HB3  1 
ATOM   5135 H HG   . CYS   B 1 81  ? 45.328 -11.382 4.589   1.00 13.05 ?  81  CYS   B HG   1 
ATOM   5136 N N    . VAL   B 1 82  ? 43.185 -10.424 0.318   1.00 9.41  ?  82  VAL   B N    1 
ATOM   5137 C CA   . VAL   B 1 82  ? 43.953 -10.298 -0.917  1.00 9.56  ?  82  VAL   B CA   1 
ATOM   5138 C C    . VAL   B 1 82  ? 45.291 -9.658  -0.588  1.00 9.90  ?  82  VAL   B C    1 
ATOM   5139 O O    . VAL   B 1 82  ? 45.339 -8.539  -0.056  1.00 10.96 ?  82  VAL   B O    1 
ATOM   5140 C CB   . VAL   B 1 82  ? 43.209 -9.454  -1.962  1.00 10.81 ?  82  VAL   B CB   1 
ATOM   5141 C CG1  . VAL   B 1 82  ? 44.067 -9.283  -3.214  1.00 12.18 ?  82  VAL   B CG1  1 
ATOM   5142 C CG2  . VAL   B 1 82  ? 41.860 -10.063 -2.296  1.00 11.79 ?  82  VAL   B CG2  1 
ATOM   5143 H H    . VAL   B 1 82  ? 42.807 -9.684  0.558   1.00 11.31 ?  82  VAL   B H    1 
ATOM   5144 H HA   . VAL   B 1 82  ? 44.114 -11.177 -1.290  1.00 11.49 ?  82  VAL   B HA   1 
ATOM   5145 H HB   . VAL   B 1 82  ? 43.053 -8.570  -1.594  1.00 12.99 ?  82  VAL   B HB   1 
ATOM   5146 H HG11 . VAL   B 1 82  ? 43.508 -8.965  -3.939  1.00 14.64 ?  82  VAL   B HG11 1 
ATOM   5147 H HG12 . VAL   B 1 82  ? 44.769 -8.632  -3.034  1.00 14.64 ?  82  VAL   B HG12 1 
ATOM   5148 H HG13 . VAL   B 1 82  ? 44.461 -10.136 -3.448  1.00 14.64 ?  82  VAL   B HG13 1 
ATOM   5149 H HG21 . VAL   B 1 82  ? 41.428 -9.528  -2.982  1.00 14.17 ?  82  VAL   B HG21 1 
ATOM   5150 H HG22 . VAL   B 1 82  ? 41.989 -10.969 -2.618  1.00 14.17 ?  82  VAL   B HG22 1 
ATOM   5151 H HG23 . VAL   B 1 82  ? 41.309 -10.075 -1.495  1.00 14.17 ?  82  VAL   B HG23 1 
ATOM   5152 N N    . LEU   B 1 83  ? 46.373 -10.343 -0.946  1.00 9.57  ?  83  LEU   B N    1 
ATOM   5153 C CA   . LEU   B 1 83  ? 47.726 -9.824  -0.818  1.00 9.50  ?  83  LEU   B CA   1 
ATOM   5154 C C    . LEU   B 1 83  ? 48.435 -9.960  -2.166  1.00 9.48  ?  83  LEU   B C    1 
ATOM   5155 O O    . LEU   B 1 83  ? 47.841 -10.380 -3.167  1.00 9.71  ?  83  LEU   B O    1 
ATOM   5156 C CB   . LEU   B 1 83  ? 48.473 -10.500 0.344   1.00 10.09 ?  83  LEU   B CB   1 
ATOM   5157 C CG   . LEU   B 1 83  ? 47.943 -10.143 1.740   1.00 11.48 ?  83  LEU   B CG   1 
ATOM   5158 C CD1  . LEU   B 1 83  ? 48.569 -11.022 2.819   1.00 11.63 ?  83  LEU   B CD1  1 
ATOM   5159 C CD2  . LEU   B 1 83  ? 48.154 -8.669  2.076   1.00 12.41 ?  83  LEU   B CD2  1 
ATOM   5160 H H    . LEU   B 1 83  ? 46.344 -11.142 -1.276  1.00 11.50 ?  83  LEU   B H    1 
ATOM   5161 H HA   . LEU   B 1 83  ? 47.673 -8.882  -0.615  1.00 11.42 ?  83  LEU   B HA   1 
ATOM   5162 H HB2  . LEU   B 1 83  ? 48.408 -11.461 0.245   1.00 12.13 ?  83  LEU   B HB2  1 
ATOM   5163 H HB3  . LEU   B 1 83  ? 49.406 -10.232 0.312   1.00 12.13 ?  83  LEU   B HB3  1 
ATOM   5164 H HG   . LEU   B 1 83  ? 46.990 -10.309 1.755   1.00 13.80 ?  83  LEU   B HG   1 
ATOM   5165 H HD11 . LEU   B 1 83  ? 48.201 -10.776 3.685   1.00 13.98 ?  83  LEU   B HD11 1 
ATOM   5166 H HD12 . LEU   B 1 83  ? 48.354 -11.955 2.631   1.00 13.98 ?  83  LEU   B HD12 1 
ATOM   5167 H HD13 . LEU   B 1 83  ? 49.528 -10.901 2.819   1.00 13.98 ?  83  LEU   B HD13 1 
ATOM   5168 H HD21 . LEU   B 1 83  ? 47.929 -8.523  3.009   1.00 14.92 ?  83  LEU   B HD21 1 
ATOM   5169 H HD22 . LEU   B 1 83  ? 49.083 -8.440  1.921   1.00 14.92 ?  83  LEU   B HD22 1 
ATOM   5170 H HD23 . LEU   B 1 83  ? 47.580 -8.133  1.509   1.00 14.92 ?  83  LEU   B HD23 1 
ATOM   5171 N N    . SER   B 1 84  ? 49.711 -9.591  -2.208  1.00 10.45 ?  84  SER   B N    1 
ATOM   5172 C CA   . SER   B 1 84  ? 50.452 -9.689  -3.455  1.00 10.92 ?  84  SER   B CA   1 
ATOM   5173 C C    . SER   B 1 84  ? 50.597 -11.142 -3.893  1.00 10.27 ?  84  SER   B C    1 
ATOM   5174 O O    . SER   B 1 84  ? 50.706 -12.054 -3.075  1.00 10.09 ?  84  SER   B O    1 
ATOM   5175 C CB   . SER   B 1 84  ? 51.850 -9.102  -3.284  1.00 12.70 ?  84  SER   B CB   1 
ATOM   5176 O OG   . SER   B 1 84  ? 52.595 -9.285  -4.474  1.00 14.49 ?  84  SER   B OG   1 
ATOM   5177 H H    . SER   B 1 84  ? 50.159 -9.276  -1.540  1.00 12.55 ?  84  SER   B H    1 
ATOM   5178 H HA   . SER   B 1 84  ? 49.992 -9.197  -4.151  1.00 13.12 ?  84  SER   B HA   1 
ATOM   5179 H HB2  . SER   B 1 84  ? 51.777 -8.148  -3.091  1.00 15.26 ?  84  SER   B HB2  1 
ATOM   5180 H HB3  . SER   B 1 84  ? 52.304 -9.550  -2.554  1.00 15.26 ?  84  SER   B HB3  1 
ATOM   5181 H HG   . SER   B 1 84  ? 53.363 -8.952  -4.387  1.00 17.40 ?  84  SER   B HG   1 
ATOM   5182 N N    . GLY   B 1 85  ? 50.656 -11.348 -5.204  1.00 11.38 ?  85  GLY   B N    1 
ATOM   5183 C CA   . GLY   B 1 85  ? 51.007 -12.634 -5.759  1.00 11.85 ?  85  GLY   B CA   1 
ATOM   5184 C C    . GLY   B 1 85  ? 52.480 -12.835 -6.047  1.00 11.23 ?  85  GLY   B C    1 
ATOM   5185 O O    . GLY   B 1 85  ? 52.855 -13.913 -6.510  1.00 11.48 ?  85  GLY   B O    1 
ATOM   5186 H H    . GLY   B 1 85  ? 50.503 -10.744 -5.792  1.00 13.68 ?  85  GLY   B H    1 
ATOM   5187 H HA2  . GLY   B 1 85  ? 50.727 -13.328 -5.142  1.00 14.24 ?  85  GLY   B HA2  1 
ATOM   5188 H HA3  . GLY   B 1 85  ? 50.525 -12.758 -6.586  1.00 14.24 ?  85  GLY   B HA3  1 
ATOM   5189 N N    . HIS   B 1 86  ? 53.332 -11.843 -5.807  1.00 10.81 ?  86  HIS   B N    1 
ATOM   5190 C CA   . HIS   B 1 86  ? 54.793 -12.018 -5.893  1.00 10.62 ?  86  HIS   B CA   1 
ATOM   5191 C C    . HIS   B 1 86  ? 55.162 -12.525 -7.287  1.00 10.81 ?  86  HIS   B C    1 
ATOM   5192 O O    . HIS   B 1 86  ? 54.781 -11.895 -8.288  1.00 11.84 ?  86  HIS   B O    1 
ATOM   5193 C CB   . HIS   B 1 86  ? 55.282 -12.869 -4.724  1.00 10.98 ?  86  HIS   B CB   1 
ATOM   5194 C CG   . HIS   B 1 86  ? 54.972 -12.273 -3.394  1.00 11.28 ?  86  HIS   B CG   1 
ATOM   5195 N ND1  . HIS   B 1 86  ? 55.787 -11.341 -2.788  1.00 12.68 ?  86  HIS   B ND1  1 
ATOM   5196 C CD2  . HIS   B 1 86  ? 53.902 -12.433 -2.580  1.00 11.47 ?  86  HIS   B CD2  1 
ATOM   5197 C CE1  . HIS   B 1 86  ? 55.234 -10.963 -1.650  1.00 12.67 ?  86  HIS   B CE1  1 
ATOM   5198 N NE2  . HIS   B 1 86  ? 54.093 -11.612 -1.498  1.00 11.91 ?  86  HIS   B NE2  1 
ATOM   5199 H H    . HIS   B 1 86  ? 53.097 -11.048 -5.598  1.00 12.99 ?  86  HIS   B H    1 
ATOM   5200 H HA   . HIS   B 1 86  ? 55.209 -11.144 -5.797  1.00 12.76 ?  86  HIS   B HA   1 
ATOM   5201 H HB2  . HIS   B 1 86  ? 54.862 -13.738 -4.771  1.00 13.20 ?  86  HIS   B HB2  1 
ATOM   5202 H HB3  . HIS   B 1 86  ? 56.248 -12.963 -4.786  1.00 13.20 ?  86  HIS   B HB3  1 
ATOM   5203 H HD2  . HIS   B 1 86  ? 53.173 -12.997 -2.726  1.00 13.79 ?  86  HIS   B HD2  1 
ATOM   5204 H HE1  . HIS   B 1 86  ? 55.597 -10.357 -1.047  1.00 15.23 ?  86  HIS   B HE1  1 
ATOM   5205 H HE2  . HIS   B 1 86  ? 53.561 -11.542 -0.825  1.00 14.32 ?  86  HIS   B HE2  1 
ATOM   5206 N N    . ASN   B 1 87  ? 55.933 -13.607 -7.401  1.00 11.19 ?  87  ASN   B N    1 
ATOM   5207 C CA   . ASN   B 1 87  ? 56.331 -14.177 -8.680  1.00 11.98 ?  87  ASN   B CA   1 
ATOM   5208 C C    . ASN   B 1 87  ? 55.353 -15.227 -9.183  1.00 11.77 ?  87  ASN   B C    1 
ATOM   5209 O O    . ASN   B 1 87  ? 55.677 -15.950 -10.134 1.00 13.46 ?  87  ASN   B O    1 
ATOM   5210 C CB   . ASN   B 1 87  ? 57.727 -14.802 -8.566  1.00 13.83 ?  87  ASN   B CB   1 
ATOM   5211 C CG   . ASN   B 1 87  ? 57.785 -15.919 -7.526  1.00 15.12 ?  87  ASN   B CG   1 
ATOM   5212 O OD1  . ASN   B 1 87  ? 57.141 -15.840 -6.476  1.00 13.95 ?  87  ASN   B OD1  1 
ATOM   5213 N ND2  . ASN   B 1 87  ? 58.538 -16.976 -7.828  1.00 17.30 ?  87  ASN   B ND2  1 
ATOM   5214 H H    . ASN   B 1 87  ? 56.250 -14.040 -6.728  1.00 13.45 ?  87  ASN   B H    1 
ATOM   5215 H HA   . ASN   B 1 87  ? 56.370 -13.470 -9.341  1.00 14.39 ?  87  ASN   B HA   1 
ATOM   5216 H HB2  . ASN   B 1 87  ? 57.975 -15.177 -9.427  1.00 16.62 ?  87  ASN   B HB2  1 
ATOM   5217 H HB3  . ASN   B 1 87  ? 58.359 -14.113 -8.310  1.00 16.62 ?  87  ASN   B HB3  1 
ATOM   5218 H HD21 . ASN   B 1 87  ? 58.603 -17.624 -7.273  1.00 20.78 ?  87  ASN   B HD21 1 
ATOM   5219 H HD22 . ASN   B 1 87  ? 58.967 -16.998 -8.575  1.00 20.78 ?  87  ASN   B HD22 1 
ATOM   5220 N N    . LEU   B 1 88  ? 54.172 -15.328 -8.568  1.00 10.78 ?  88  LEU   B N    1 
ATOM   5221 C CA   . LEU   B 1 88  ? 53.195 -16.358 -8.898  1.00 10.99 ?  88  LEU   B CA   1 
ATOM   5222 C C    . LEU   B 1 88  ? 51.963 -15.842 -9.621  1.00 10.51 ?  88  LEU   B C    1 
ATOM   5223 O O    . LEU   B 1 88  ? 51.369 -16.587 -10.412 1.00 12.34 ?  88  LEU   B O    1 
ATOM   5224 C CB   . LEU   B 1 88  ? 52.722 -17.047 -7.613  1.00 11.98 ?  88  LEU   B CB   1 
ATOM   5225 C CG   . LEU   B 1 88  ? 53.836 -17.695 -6.803  1.00 14.09 ?  88  LEU   B CG   1 
ATOM   5226 C CD1  . LEU   B 1 88  ? 53.331 -18.036 -5.410  1.00 16.00 ?  88  LEU   B CD1  1 
ATOM   5227 C CD2  . LEU   B 1 88  ? 54.341 -18.932 -7.515  1.00 17.24 ?  88  LEU   B CD2  1 
ATOM   5228 H H    . LEU   B 1 88  ? 53.912 -14.801 -7.935  1.00 12.95 ?  88  LEU   B H    1 
ATOM   5229 H HA   . LEU   B 1 88  ? 53.613 -17.025 -9.455  1.00 13.21 ?  88  LEU   B HA   1 
ATOM   5230 H HB2  . LEU   B 1 88  ? 52.285 -16.394 -7.044  1.00 14.39 ?  88  LEU   B HB2  1 
ATOM   5231 H HB3  . LEU   B 1 88  ? 52.089 -17.747 -7.849  1.00 14.39 ?  88  LEU   B HB3  1 
ATOM   5232 H HG   . LEU   B 1 88  ? 54.572 -17.068 -6.712  1.00 16.93 ?  88  LEU   B HG   1 
ATOM   5233 H HD11 . LEU   B 1 88  ? 53.977 -18.613 -4.973  1.00 19.22 ?  88  LEU   B HD11 1 
ATOM   5234 H HD12 . LEU   B 1 88  ? 53.222 -17.217 -4.901  1.00 19.22 ?  88  LEU   B HD12 1 
ATOM   5235 H HD13 . LEU   B 1 88  ? 52.480 -18.493 -5.489  1.00 19.22 ?  88  LEU   B HD13 1 
ATOM   5236 H HD21 . LEU   B 1 88  ? 55.003 -19.366 -6.956  1.00 20.71 ?  88  LEU   B HD21 1 
ATOM   5237 H HD22 . LEU   B 1 88  ? 53.595 -19.530 -7.673  1.00 20.71 ?  88  LEU   B HD22 1 
ATOM   5238 H HD23 . LEU   B 1 88  ? 54.741 -18.668 -8.358  1.00 20.71 ?  88  LEU   B HD23 1 
ATOM   5239 N N    . ALA   B 1 89  ? 51.551 -14.608 -9.347  1.00 10.35 ?  89  ALA   B N    1 
ATOM   5240 C CA   . ALA   B 1 89  ? 50.256 -14.119 -9.799  1.00 9.69  ?  89  ALA   B CA   1 
ATOM   5241 C C    . ALA   B 1 89  ? 50.223 -12.628 -9.528  1.00 10.00 ?  89  ALA   B C    1 
ATOM   5242 O O    . ALA   B 1 89  ? 51.059 -12.103 -8.795  1.00 11.03 ?  89  ALA   B O    1 
ATOM   5243 C CB   . ALA   B 1 89  ? 49.112 -14.796 -9.044  1.00 9.97  ?  89  ALA   B CB   1 
ATOM   5244 H H    . ALA   B 1 89  ? 51.995 -14.029 -8.889  1.00 12.44 ?  89  ALA   B H    1 
ATOM   5245 H HA   . ALA   B 1 89  ? 50.145 -14.271 -10.748 1.00 11.65 ?  89  ALA   B HA   1 
ATOM   5246 H HB1  . ALA   B 1 89  ? 48.263 -14.460 -9.383  1.00 11.99 ?  89  ALA   B HB1  1 
ATOM   5247 H HB2  . ALA   B 1 89  ? 49.164 -15.755 -9.189  1.00 11.99 ?  89  ALA   B HB2  1 
ATOM   5248 H HB3  . ALA   B 1 89  ? 49.190 -14.598 -8.100  1.00 11.99 ?  89  ALA   B HB3  1 
ATOM   5249 N N    . LYS   B 1 90  ? 49.230 -11.942 -10.095 1.00 11.06 ?  90  LYS   B N    1 
ATOM   5250 C CA   . LYS   B 1 90  ? 49.039 -10.553 -9.698  1.00 11.53 ?  90  LYS   B CA   1 
ATOM   5251 C C    . LYS   B 1 90  ? 48.718 -10.472 -8.209  1.00 11.20 ?  90  LYS   B C    1 
ATOM   5252 O O    . LYS   B 1 90  ? 49.352 -9.715  -7.458  1.00 12.78 ?  90  LYS   B O    1 
ATOM   5253 C CB   . LYS   B 1 90  ? 47.963 -9.895  -10.562 1.00 12.91 ?  90  LYS   B CB   1 
ATOM   5254 C CG   . LYS   B 1 90  ? 47.663 -8.452  -10.200 1.00 13.20 ?  90  LYS   B CG   1 
ATOM   5255 C CD   . LYS   B 1 90  ? 48.856 -7.538  -10.318 1.00 15.93 ?  90  LYS   B CD   1 
ATOM   5256 C CE   . LYS   B 1 90  ? 48.420 -6.116  -10.035 1.00 17.97 ?  90  LYS   B CE   1 
ATOM   5257 N NZ   . LYS   B 1 90  ? 49.567 -5.181  -9.949  1.00 18.34 ?  90  LYS   B NZ   1 
ATOM   5258 H H    . LYS   B 1 90  ? 48.674 -12.248 -10.678 1.00 13.29 ?  90  LYS   B H    1 
ATOM   5259 H HA   . LYS   B 1 90  ? 49.866 -10.078 -9.848  1.00 13.86 ?  90  LYS   B HA   1 
ATOM   5260 H HB2  . LYS   B 1 90  ? 48.258 -9.909  -11.490 1.00 15.52 ?  90  LYS   B HB2  1 
ATOM   5261 H HB3  . LYS   B 1 90  ? 47.139 -10.400 -10.479 1.00 15.52 ?  90  LYS   B HB3  1 
ATOM   5262 H HG2  . LYS   B 1 90  ? 46.973 -8.117  -10.795 1.00 15.86 ?  90  LYS   B HG2  1 
ATOM   5263 H HG3  . LYS   B 1 90  ? 47.347 -8.416  -9.282  1.00 15.86 ?  90  LYS   B HG3  1 
ATOM   5264 H HD2  . LYS   B 1 90  ? 49.530 -7.790  -9.667  1.00 19.14 ?  90  LYS   B HD2  1 
ATOM   5265 H HD3  . LYS   B 1 90  ? 49.215 -7.581  -11.218 1.00 19.14 ?  90  LYS   B HD3  1 
ATOM   5266 H HE2  . LYS   B 1 90  ? 47.841 -5.807  -10.752 1.00 21.58 ?  90  LYS   B HE2  1 
ATOM   5267 H HE3  . LYS   B 1 90  ? 47.948 -6.082  -9.189  1.00 21.58 ?  90  LYS   B HE3  1 
ATOM   5268 H HZ1  . LYS   B 1 90  ? 49.284 -4.352  -9.785  1.00 22.03 ?  90  LYS   B HZ1  1 
ATOM   5269 H HZ2  . LYS   B 1 90  ? 50.119 -5.430  -9.296  1.00 22.03 ?  90  LYS   B HZ2  1 
ATOM   5270 H HZ3  . LYS   B 1 90  ? 50.021 -5.179  -10.719 1.00 22.03 ?  90  LYS   B HZ3  1 
ATOM   5271 N N    . HIS   B 1 91  ? 47.763 -11.290 -7.760  1.00 9.59  ?  91  HIS   B N    1 
ATOM   5272 C CA   . HIS   B 1 91  ? 47.302 -11.314 -6.385  1.00 9.50  ?  91  HIS   B CA   1 
ATOM   5273 C C    . HIS   B 1 91  ? 47.305 -12.742 -5.869  1.00 8.97  ?  91  HIS   B C    1 
ATOM   5274 O O    . HIS   B 1 91  ? 47.070 -13.695 -6.622  1.00 9.59  ?  91  HIS   B O    1 
ATOM   5275 C CB   . HIS   B 1 91  ? 45.853 -10.840 -6.265  1.00 11.25 ?  91  HIS   B CB   1 
ATOM   5276 C CG   . HIS   B 1 91  ? 45.625 -9.447  -6.736  1.00 14.79 ?  91  HIS   B CG   1 
ATOM   5277 N ND1  . HIS   B 1 91  ? 46.176 -8.348  -6.113  1.00 17.65 ?  91  HIS   B ND1  1 
ATOM   5278 C CD2  . HIS   B 1 91  ? 44.867 -8.966  -7.746  1.00 17.30 ?  91  HIS   B CD2  1 
ATOM   5279 C CE1  . HIS   B 1 91  ? 45.785 -7.248  -6.734  1.00 18.68 ?  91  HIS   B CE1  1 
ATOM   5280 N NE2  . HIS   B 1 91  ? 44.985 -7.597  -7.726  1.00 18.74 ?  91  HIS   B NE2  1 
ATOM   5281 H H    . HIS   B 1 91  ? 47.353 -11.861 -8.256  1.00 11.52 ?  91  HIS   B H    1 
ATOM   5282 H HA   . HIS   B 1 91  ? 47.876 -10.757 -5.823  1.00 11.42 ?  91  HIS   B HA   1 
ATOM   5283 H HB2  . HIS   B 1 91  ? 45.290 -11.421 -6.792  1.00 13.52 ?  91  HIS   B HB2  1 
ATOM   5284 H HB3  . HIS   B 1 91  ? 45.587 -10.880 -5.330  1.00 13.52 ?  91  HIS   B HB3  1 
ATOM   5285 H HD1  . HIS   B 1 91  ? 46.700 -8.368  -5.426  1.00 21.20 ?  91  HIS   B HD1  1 
ATOM   5286 H HD2  . HIS   B 1 91  ? 44.371 -9.460  -8.349  1.00 20.78 ?  91  HIS   B HD2  1 
ATOM   5287 H HE1  . HIS   B 1 91  ? 46.030 -6.374  -6.505  1.00 22.43 ?  91  HIS   B HE1  1 
ATOM   5288 N N    . CYS   B 1 92  ? 47.498 -12.877 -4.563  1.00 8.87  ?  92  CYS   B N    1 
ATOM   5289 C CA   . CYS   B 1 92  ? 47.202 -14.113 -3.852  1.00 8.54  ?  92  CYS   B CA   1 
ATOM   5290 C C    . CYS   B 1 92  ? 45.981 -13.884 -2.967  1.00 8.17  ?  92  CYS   B C    1 
ATOM   5291 O O    . CYS   B 1 92  ? 45.978 -12.983 -2.117  1.00 9.31  ?  92  CYS   B O    1 
ATOM   5292 C CB   . CYS   B 1 92  ? 48.384 -14.572 -3.004  1.00 9.04  ?  92  CYS   B CB   1 
ATOM   5293 S SG   . CYS   B 1 92  ? 48.027 -16.109 -2.109  1.00 9.26  ?  92  CYS   B SG   1 
ATOM   5294 H H    . CYS   B 1 92  ? 47.809 -12.253 -4.050  1.00 10.67 ?  92  CYS   B H    1 
ATOM   5295 H HA   . CYS   B 1 92  ? 46.999 -14.809 -4.499  1.00 10.26 ?  92  CYS   B HA   1 
ATOM   5296 H HB2  . CYS   B 1 92  ? 49.147 -14.721 -3.579  1.00 10.87 ?  92  CYS   B HB2  1 
ATOM   5297 H HB3  . CYS   B 1 92  ? 48.583 -13.885 -2.350  1.00 10.87 ?  92  CYS   B HB3  1 
ATOM   5298 H HG   . CYS   B 1 92  ? 49.003 -16.420 -1.484  1.00 11.13 ?  92  CYS   B HG   1 
ATOM   5299 N N    . LEU   B 1 93  ? 44.946 -14.692 -3.182  1.00 8.18  ?  93  LEU   B N    1 
ATOM   5300 C CA   . LEU   B 1 93  ? 43.768 -14.706 -2.324  1.00 8.37  ?  93  LEU   B CA   1 
ATOM   5301 C C    . LEU   B 1 93  ? 43.994 -15.775 -1.258  1.00 7.92  ?  93  LEU   B C    1 
ATOM   5302 O O    . LEU   B 1 93  ? 43.949 -16.977 -1.552  1.00 8.36  ?  93  LEU   B O    1 
ATOM   5303 C CB   . LEU   B 1 93  ? 42.513 -15.000 -3.140  1.00 8.55  ?  93  LEU   B CB   1 
ATOM   5304 C CG   . LEU   B 1 93  ? 41.214 -15.024 -2.334  1.00 9.45  ?  93  LEU   B CG   1 
ATOM   5305 C CD1  . LEU   B 1 93  ? 40.860 -13.637 -1.844  1.00 10.00 ?  93  LEU   B CD1  1 
ATOM   5306 C CD2  . LEU   B 1 93  ? 40.094 -15.618 -3.164  1.00 9.86  ?  93  LEU   B CD2  1 
ATOM   5307 H H    . LEU   B 1 93  ? 44.908 -15.266 -3.830  1.00 9.83  ?  93  LEU   B H    1 
ATOM   5308 H HA   . LEU   B 1 93  ? 43.671 -13.845 -1.893  1.00 10.07 ?  93  LEU   B HA   1 
ATOM   5309 H HB2  . LEU   B 1 93  ? 42.421 -14.313 -3.821  1.00 10.28 ?  93  LEU   B HB2  1 
ATOM   5310 H HB3  . LEU   B 1 93  ? 42.611 -15.865 -3.562  1.00 10.28 ?  93  LEU   B HB3  1 
ATOM   5311 H HG   . LEU   B 1 93  ? 41.337 -15.586 -1.555  1.00 11.36 ?  93  LEU   B HG   1 
ATOM   5312 H HD11 . LEU   B 1 93  ? 40.001 -13.669 -1.399  1.00 12.02 ?  93  LEU   B HD11 1 
ATOM   5313 H HD12 . LEU   B 1 93  ? 41.543 -13.334 -1.226  1.00 12.02 ?  93  LEU   B HD12 1 
ATOM   5314 H HD13 . LEU   B 1 93  ? 40.815 -13.035 -2.607  1.00 12.02 ?  93  LEU   B HD13 1 
ATOM   5315 H HD21 . LEU   B 1 93  ? 39.278 -15.618 -2.636  1.00 11.85 ?  93  LEU   B HD21 1 
ATOM   5316 H HD22 . LEU   B 1 93  ? 39.969 -15.077 -3.960  1.00 11.85 ?  93  LEU   B HD22 1 
ATOM   5317 H HD23 . LEU   B 1 93  ? 40.329 -16.524 -3.410  1.00 11.85 ?  93  LEU   B HD23 1 
ATOM   5318 N N    . HIS   B 1 94  ? 44.265 -15.341 -0.032  1.00 7.98  ?  94  HIS   B N    1 
ATOM   5319 C CA   . HIS   B 1 94  ? 44.484 -16.253 1.085   1.00 8.16  ?  94  HIS   B CA   1 
ATOM   5320 C C    . HIS   B 1 94  ? 43.124 -16.614 1.657   1.00 8.59  ?  94  HIS   B C    1 
ATOM   5321 O O    . HIS   B 1 94  ? 42.447 -15.742 2.202   1.00 10.04 ?  94  HIS   B O    1 
ATOM   5322 C CB   . HIS   B 1 94  ? 45.350 -15.575 2.145   1.00 8.56  ?  94  HIS   B CB   1 
ATOM   5323 C CG   . HIS   B 1 94  ? 46.736 -15.279 1.679   1.00 8.57  ?  94  HIS   B CG   1 
ATOM   5324 N ND1  . HIS   B 1 94  ? 47.765 -16.189 1.767   1.00 8.88  ?  94  HIS   B ND1  1 
ATOM   5325 C CD2  . HIS   B 1 94  ? 47.243 -14.172 1.081   1.00 9.16  ?  94  HIS   B CD2  1 
ATOM   5326 C CE1  . HIS   B 1 94  ? 48.854 -15.639 1.259   1.00 8.95  ?  94  HIS   B CE1  1 
ATOM   5327 N NE2  . HIS   B 1 94  ? 48.569 -14.417 0.839   1.00 9.38  ?  94  HIS   B NE2  1 
ATOM   5328 H H    . HIS   B 1 94  ? 44.329 -14.503 0.181   1.00 9.59  ?  94  HIS   B H    1 
ATOM   5329 H HA   . HIS   B 1 94  ? 44.921 -17.057 0.770   1.00 9.81  ?  94  HIS   B HA   1 
ATOM   5330 H HB2  . HIS   B 1 94  ? 44.930 -14.742 2.400   1.00 10.29 ?  94  HIS   B HB2  1 
ATOM   5331 H HB3  . HIS   B 1 94  ? 45.411 -16.167 2.910   1.00 10.29 ?  94  HIS   B HB3  1 
ATOM   5332 H HD2  . HIS   B 1 94  ? 46.786 -13.389 0.884   1.00 11.01 ?  94  HIS   B HD2  1 
ATOM   5333 H HE1  . HIS   B 1 94  ? 49.684 -16.056 1.210   1.00 10.76 ?  94  HIS   B HE1  1 
ATOM   5334 H HE2  . HIS   B 1 94  ? 49.124 -13.878 0.474   1.00 11.28 ?  94  HIS   B HE2  1 
ATOM   5335 N N    . VAL   B 1 95  ? 42.695 -17.870 1.509   1.00 8.23  ?  95  VAL   B N    1 
ATOM   5336 C CA   . VAL   B 1 95  ? 41.368 -18.310 1.939   1.00 8.55  ?  95  VAL   B CA   1 
ATOM   5337 C C    . VAL   B 1 95  ? 41.534 -19.348 3.032   1.00 8.83  ?  95  VAL   B C    1 
ATOM   5338 O O    . VAL   B 1 95  ? 42.301 -20.302 2.870   1.00 9.28  ?  95  VAL   B O    1 
ATOM   5339 C CB   . VAL   B 1 95  ? 40.550 -18.905 0.777   1.00 8.75  ?  95  VAL   B CB   1 
ATOM   5340 C CG1  . VAL   B 1 95  ? 39.170 -19.352 1.258   1.00 10.02 ?  95  VAL   B CG1  1 
ATOM   5341 C CG2  . VAL   B 1 95  ? 40.437 -17.922 -0.363  1.00 9.11  ?  95  VAL   B CG2  1 
ATOM   5342 H H    . VAL   B 1 95  ? 43.160 -18.500 1.153   1.00 9.89  ?  95  VAL   B H    1 
ATOM   5343 H HA   . VAL   B 1 95  ? 40.876 -17.558 2.307   1.00 10.28 ?  95  VAL   B HA   1 
ATOM   5344 H HB   . VAL   B 1 95  ? 41.009 -19.686 0.443   1.00 10.52 ?  95  VAL   B HB   1 
ATOM   5345 H HG11 . VAL   B 1 95  ? 38.612 -19.543 0.483   1.00 12.05 ?  95  VAL   B HG11 1 
ATOM   5346 H HG12 . VAL   B 1 95  ? 39.264 -20.156 1.794   1.00 12.05 ?  95  VAL   B HG12 1 
ATOM   5347 H HG13 . VAL   B 1 95  ? 38.768 -18.646 1.784   1.00 12.05 ?  95  VAL   B HG13 1 
ATOM   5348 H HG21 . VAL   B 1 95  ? 39.865 -18.304 -1.049  1.00 10.96 ?  95  VAL   B HG21 1 
ATOM   5349 H HG22 . VAL   B 1 95  ? 40.052 -17.098 -0.032  1.00 10.96 ?  95  VAL   B HG22 1 
ATOM   5350 H HG23 . VAL   B 1 95  ? 41.321 -17.759 -0.722  1.00 10.96 ?  95  VAL   B HG23 1 
ATOM   5351 N N    . VAL   B 1 96  ? 40.796 -19.184 4.124   1.00 8.96  ?  96  VAL   B N    1 
ATOM   5352 C CA   . VAL   B 1 96  ? 40.872 -20.097 5.262   1.00 9.61  ?  96  VAL   B CA   1 
ATOM   5353 C C    . VAL   B 1 96  ? 39.683 -21.056 5.210   1.00 9.54  ?  96  VAL   B C    1 
ATOM   5354 O O    . VAL   B 1 96  ? 38.562 -20.705 5.591   1.00 10.24 ?  96  VAL   B O    1 
ATOM   5355 C CB   . VAL   B 1 96  ? 40.920 -19.342 6.594   1.00 10.15 ?  96  VAL   B CB   1 
ATOM   5356 C CG1  . VAL   B 1 96  ? 41.102 -20.329 7.745   1.00 11.06 ?  96  VAL   B CG1  1 
ATOM   5357 C CG2  . VAL   B 1 96  ? 42.037 -18.312 6.602   1.00 10.90 ?  96  VAL   B CG2  1 
ATOM   5358 H H    . VAL   B 1 96  ? 40.229 -18.550 4.232   1.00 10.77 ?  96  VAL   B H    1 
ATOM   5359 H HA   . VAL   B 1 96  ? 41.688 -20.624 5.194   1.00 11.55 ?  96  VAL   B HA   1 
ATOM   5360 H HB   . VAL   B 1 96  ? 40.077 -18.879 6.730   1.00 12.20 ?  96  VAL   B HB   1 
ATOM   5361 H HG11 . VAL   B 1 96  ? 41.275 -19.829 8.565   1.00 13.29 ?  96  VAL   B HG11 1 
ATOM   5362 H HG12 . VAL   B 1 96  ? 40.299 -20.857 7.849   1.00 13.29 ?  96  VAL   B HG12 1 
ATOM   5363 H HG13 . VAL   B 1 96  ? 41.860 -20.904 7.553   1.00 13.29 ?  96  VAL   B HG13 1 
ATOM   5364 H HG21 . VAL   B 1 96  ? 42.085 -17.898 7.481   1.00 13.10 ?  96  VAL   B HG21 1 
ATOM   5365 H HG22 . VAL   B 1 96  ? 42.877 -18.750 6.399   1.00 13.10 ?  96  VAL   B HG22 1 
ATOM   5366 H HG23 . VAL   B 1 96  ? 41.848 -17.633 5.933   1.00 13.10 ?  96  VAL   B HG23 1 
ATOM   5367 N N    . GLY   B 1 97  ? 39.924 -22.291 4.773   1.00 9.86  ?  97  GLY   B N    1 
ATOM   5368 C CA   . GLY   B 1 97  ? 38.953 -23.351 4.931   1.00 10.25 ?  97  GLY   B CA   1 
ATOM   5369 C C    . GLY   B 1 97  ? 39.063 -23.959 6.310   1.00 10.80 ?  97  GLY   B C    1 
ATOM   5370 O O    . GLY   B 1 97  ? 40.105 -23.842 6.968   1.00 11.46 ?  97  GLY   B O    1 
ATOM   5371 H H    . GLY   B 1 97  ? 40.654 -22.537 4.383   1.00 11.85 ?  97  GLY   B H    1 
ATOM   5372 H HA2  . GLY   B 1 97  ? 38.060 -22.989 4.807   1.00 12.31 ?  97  GLY   B HA2  1 
ATOM   5373 H HA3  . GLY   B 1 97  ? 39.105 -24.040 4.265   1.00 12.31 ?  97  GLY   B HA3  1 
ATOM   5374 N N    . PRO   B 1 98  ? 38.009 -24.637 6.769   1.00 11.39 ?  98  PRO   B N    1 
ATOM   5375 C CA   . PRO   B 1 98  ? 38.097 -25.333 8.055   1.00 12.11 ?  98  PRO   B CA   1 
ATOM   5376 C C    . PRO   B 1 98  ? 39.124 -26.453 8.013   1.00 11.77 ?  98  PRO   B C    1 
ATOM   5377 O O    . PRO   B 1 98  ? 39.227 -27.197 7.037   1.00 12.26 ?  98  PRO   B O    1 
ATOM   5378 C CB   . PRO   B 1 98  ? 36.680 -25.879 8.256   1.00 12.40 ?  98  PRO   B CB   1 
ATOM   5379 C CG   . PRO   B 1 98  ? 36.125 -26.006 6.887   1.00 12.15 ?  98  PRO   B CG   1 
ATOM   5380 C CD   . PRO   B 1 98  ? 36.693 -24.830 6.135   1.00 11.30 ?  98  PRO   B CD   1 
ATOM   5381 H HA   . PRO   B 1 98  ? 38.317 -24.713 8.763   1.00 14.55 ?  98  PRO   B HA   1 
ATOM   5382 H HB2  . PRO   B 1 98  ? 36.721 -26.748 8.692   1.00 14.89 ?  98  PRO   B HB2  1 
ATOM   5383 H HB3  . PRO   B 1 98  ? 36.159 -25.256 8.781   1.00 14.89 ?  98  PRO   B HB3  1 
ATOM   5384 H HG2  . PRO   B 1 98  ? 36.421 -26.844 6.492   1.00 14.60 ?  98  PRO   B HG2  1 
ATOM   5385 H HG3  . PRO   B 1 98  ? 35.160 -25.964 6.920   1.00 14.60 ?  98  PRO   B HG3  1 
ATOM   5386 H HD2  . PRO   B 1 98  ? 36.790 -25.046 5.192   1.00 13.58 ?  98  PRO   B HD2  1 
ATOM   5387 H HD3  . PRO   B 1 98  ? 36.142 -24.044 6.267   1.00 13.58 ?  98  PRO   B HD3  1 
ATOM   5388 N N    . ASN   B 1 99  ? 39.868 -26.582 9.101   1.00 12.73 ?  99  ASN   B N    1 
ATOM   5389 C CA   . ASN   B 1 99  ? 40.843 -27.653 9.266   1.00 13.39 ?  99  ASN   B CA   1 
ATOM   5390 C C    . ASN   B 1 99  ? 40.209 -28.732 10.146  1.00 15.25 ?  99  ASN   B C    1 
ATOM   5391 O O    . ASN   B 1 99  ? 40.112 -28.579 11.367  1.00 15.90 ?  99  ASN   B O    1 
ATOM   5392 C CB   . ASN   B 1 99  ? 42.122 -27.097 9.874   1.00 13.71 ?  99  ASN   B CB   1 
ATOM   5393 C CG   . ASN   B 1 99  ? 43.240 -28.115 9.897   1.00 14.89 ?  99  ASN   B CG   1 
ATOM   5394 O OD1  . ASN   B 1 99  ? 42.998 -29.304 10.067  1.00 15.84 ?  99  ASN   B OD1  1 
ATOM   5395 N ND2  . ASN   B 1 99  ? 44.469 -27.656 9.718   1.00 15.66 ?  99  ASN   B ND2  1 
ATOM   5396 H H    . ASN   B 1 99  ? 39.830 -26.045 9.773   1.00 15.29 ?  99  ASN   B H    1 
ATOM   5397 H HA   . ASN   B 1 99  ? 41.051 -28.043 8.403   1.00 16.08 ?  99  ASN   B HA   1 
ATOM   5398 H HB2  . ASN   B 1 99  ? 42.418 -26.340 9.356   1.00 16.47 ?  99  ASN   B HB2  1 
ATOM   5399 H HB3  . ASN   B 1 99  ? 41.942 -26.830 10.792  1.00 16.47 ?  99  ASN   B HB3  1 
ATOM   5400 H HD21 . ASN   B 1 99  ? 45.137 -28.199 9.724   1.00 18.81 ?  99  ASN   B HD21 1 
ATOM   5401 H HD22 . ASN   B 1 99  ? 44.596 -26.817 9.604   1.00 18.81 ?  99  ASN   B HD22 1 
ATOM   5402 N N    A VAL   B 1 100 ? 39.751 -29.815 9.513   0.50 16.90 ?  100 VAL   B N    1 
ATOM   5403 N N    B VAL   B 1 100 ? 39.766 -29.820 9.511   0.50 16.80 ?  100 VAL   B N    1 
ATOM   5404 C CA   A VAL   B 1 100 ? 39.128 -30.906 10.259  0.50 19.28 ?  100 VAL   B CA   1 
ATOM   5405 C CA   B VAL   B 1 100 ? 39.132 -30.917 10.239  0.50 19.09 ?  100 VAL   B CA   1 
ATOM   5406 C C    A VAL   B 1 100 ? 40.125 -31.559 11.207  0.50 19.94 ?  100 VAL   B C    1 
ATOM   5407 C C    B VAL   B 1 100 ? 40.119 -31.586 11.186  0.50 19.77 ?  100 VAL   B C    1 
ATOM   5408 O O    A VAL   B 1 100 ? 39.745 -32.046 12.279  0.50 20.51 ?  100 VAL   B O    1 
ATOM   5409 O O    B VAL   B 1 100 ? 39.726 -32.114 12.233  0.50 20.19 ?  100 VAL   B O    1 
ATOM   5410 C CB   A VAL   B 1 100 ? 38.492 -31.926 9.292   0.50 21.71 ?  100 VAL   B CB   1 
ATOM   5411 C CB   B VAL   B 1 100 ? 38.510 -31.922 9.246   0.50 21.43 ?  100 VAL   B CB   1 
ATOM   5412 C CG1  A VAL   B 1 100 ? 38.015 -33.159 10.047  0.50 22.70 ?  100 VAL   B CG1  1 
ATOM   5413 C CG1  B VAL   B 1 100 ? 37.979 -33.148 9.978   0.50 22.42 ?  100 VAL   B CG1  1 
ATOM   5414 C CG2  A VAL   B 1 100 ? 37.337 -31.288 8.532   0.50 22.50 ?  100 VAL   B CG2  1 
ATOM   5415 C CG2  B VAL   B 1 100 ? 37.402 -31.256 8.444   0.50 22.11 ?  100 VAL   B CG2  1 
ATOM   5416 H H    A VAL   B 1 100 ? 39.776 -29.933 8.661   0.50 20.30 ?  100 VAL   B H    1 
ATOM   5417 H H    B VAL   B 1 100 ? 39.812 -29.939 8.660   0.50 20.18 ?  100 VAL   B H    1 
ATOM   5418 H HA   A VAL   B 1 100 ? 38.410 -30.539 10.798  0.50 23.16 ?  100 VAL   B HA   1 
ATOM   5419 H HA   B VAL   B 1 100 ? 38.409 -30.556 10.775  0.50 22.93 ?  100 VAL   B HA   1 
ATOM   5420 H HB   A VAL   B 1 100 ? 39.157 -32.210 8.648   0.50 26.08 ?  100 VAL   B HB   1 
ATOM   5421 H HB   B VAL   B 1 100 ? 39.194 -32.220 8.627   0.50 25.74 ?  100 VAL   B HB   1 
ATOM   5422 H HG11 A VAL   B 1 100 ? 37.423 -33.671 9.471   0.50 27.26 ?  100 VAL   B HG11 1 
ATOM   5423 H HG11 B VAL   B 1 100 ? 37.412 -33.654 9.373   0.50 26.92 ?  100 VAL   B HG11 1 
ATOM   5424 H HG12 A VAL   B 1 100 ? 38.781 -33.701 10.293  0.50 27.26 ?  100 VAL   B HG12 1 
ATOM   5425 H HG12 B VAL   B 1 100 ? 38.724 -33.699 10.265  0.50 26.92 ?  100 VAL   B HG12 1 
ATOM   5426 H HG13 A VAL   B 1 100 ? 37.536 -32.879 10.843  0.50 27.26 ?  100 VAL   B HG13 1 
ATOM   5427 H HG13 B VAL   B 1 100 ? 37.463 -32.860 10.747  0.50 26.92 ?  100 VAL   B HG13 1 
ATOM   5428 H HG21 A VAL   B 1 100 ? 36.951 -31.948 7.934   0.50 27.02 ?  100 VAL   B HG21 1 
ATOM   5429 H HG21 B VAL   B 1 100 ? 37.005 -31.912 7.849   0.50 26.55 ?  100 VAL   B HG21 1 
ATOM   5430 H HG22 A VAL   B 1 100 ? 36.667 -30.990 9.168   0.50 27.02 ?  100 VAL   B HG22 1 
ATOM   5431 H HG22 B VAL   B 1 100 ? 36.731 -30.917 9.057   0.50 26.55 ?  100 VAL   B HG22 1 
ATOM   5432 H HG23 A VAL   B 1 100 ? 37.672 -30.535 8.024   0.50 27.02 ?  100 VAL   B HG23 1 
ATOM   5433 H HG23 B VAL   B 1 100 ? 37.781 -30.528 7.930   0.50 26.55 ?  100 VAL   B HG23 1 
ATOM   5434 N N    . ASN   B 1 101 ? 41.408 -31.592 10.834  1.00 20.53 ?  101 ASN   B N    1 
ATOM   5435 C CA   . ASN   B 1 101 ? 42.424 -32.137 11.733  1.00 22.77 ?  101 ASN   B CA   1 
ATOM   5436 C C    . ASN   B 1 101 ? 42.578 -31.304 13.001  1.00 24.97 ?  101 ASN   B C    1 
ATOM   5437 O O    . ASN   B 1 101 ? 43.144 -31.795 13.987  1.00 26.08 ?  101 ASN   B O    1 
ATOM   5438 C CB   . ASN   B 1 101 ? 43.763 -32.282 11.006  1.00 23.02 ?  101 ASN   B CB   1 
ATOM   5439 C CG   . ASN   B 1 101 ? 43.755 -33.416 9.998   1.00 23.30 ?  101 ASN   B CG   1 
ATOM   5440 O OD1  . ASN   B 1 101 ? 43.083 -34.419 10.195  1.00 24.32 ?  101 ASN   B OD1  1 
ATOM   5441 N ND2  . ASN   B 1 101 ? 44.492 -33.255 8.909   1.00 23.25 ?  101 ASN   B ND2  1 
ATOM   5442 H H    A ASN   B 1 101 ? 41.705 -31.319 10.072  0.50 24.66 ?  101 ASN   B H    1 
ATOM   5443 H H    B ASN   B 1 101 ? 41.711 -31.296 10.083  0.50 24.66 ?  101 ASN   B H    1 
ATOM   5444 H HA   . ASN   B 1 101 ? 42.144 -33.019 12.005  1.00 27.35 ?  101 ASN   B HA   1 
ATOM   5445 H HB2  . ASN   B 1 101 ? 43.964 -31.466 10.527  1.00 27.64 ?  101 ASN   B HB2  1 
ATOM   5446 H HB3  . ASN   B 1 101 ? 44.458 -32.464 11.661  1.00 27.64 ?  101 ASN   B HB3  1 
ATOM   5447 H HD21 . ASN   B 1 101 ? 44.519 -33.879 8.315   1.00 27.92 ?  101 ASN   B HD21 1 
ATOM   5448 H HD22 . ASN   B 1 101 ? 44.944 -32.536 8.800   1.00 27.92 ?  101 ASN   B HD22 1 
ATOM   5449 N N    A LYS   B 1 102 ? 42.121 -30.050 12.985  0.50 26.46 ?  102 LYS   B N    1 
ATOM   5450 N N    B LYS   B 1 102 ? 42.071 -30.069 13.002  0.50 26.26 ?  102 LYS   B N    1 
ATOM   5451 C CA   A LYS   B 1 102 ? 42.109 -29.194 14.163  0.50 28.23 ?  102 LYS   B CA   1 
ATOM   5452 C CA   B LYS   B 1 102 ? 42.018 -29.229 14.191  0.50 27.84 ?  102 LYS   B CA   1 
ATOM   5453 C C    A LYS   B 1 102 ? 40.742 -29.157 14.834  0.50 27.87 ?  102 LYS   B C    1 
ATOM   5454 C C    B LYS   B 1 102 ? 40.631 -29.206 14.825  0.50 27.34 ?  102 LYS   B C    1 
ATOM   5455 O O    A LYS   B 1 102 ? 40.527 -28.341 15.735  0.50 28.32 ?  102 LYS   B O    1 
ATOM   5456 O O    B LYS   B 1 102 ? 40.406 -28.448 15.774  0.50 27.84 ?  102 LYS   B O    1 
ATOM   5457 C CB   A LYS   B 1 102 ? 42.525 -27.768 13.796  0.50 30.58 ?  102 LYS   B CB   1 
ATOM   5458 C CB   B LYS   B 1 102 ? 42.436 -27.797 13.852  0.50 30.15 ?  102 LYS   B CB   1 
ATOM   5459 C CG   A LYS   B 1 102 ? 43.990 -27.590 13.432  0.50 32.63 ?  102 LYS   B CG   1 
ATOM   5460 C CG   B LYS   B 1 102 ? 43.890 -27.627 13.447  0.50 32.17 ?  102 LYS   B CG   1 
ATOM   5461 C CD   A LYS   B 1 102 ? 44.274 -26.135 13.082  0.50 34.54 ?  102 LYS   B CD   1 
ATOM   5462 C CD   B LYS   B 1 102 ? 44.144 -26.197 12.997  0.50 34.01 ?  102 LYS   B CD   1 
ATOM   5463 C CE   A LYS   B 1 102 ? 45.742 -25.896 12.769  0.50 36.03 ?  102 LYS   B CE   1 
ATOM   5464 C CE   B LYS   B 1 102 ? 45.613 -25.934 12.717  0.50 35.46 ?  102 LYS   B CE   1 
ATOM   5465 N NZ   A LYS   B 1 102 ? 46.000 -24.473 12.402  0.50 36.83 ?  102 LYS   B NZ   1 
ATOM   5466 N NZ   B LYS   B 1 102 ? 45.833 -24.536 12.246  0.50 36.24 ?  102 LYS   B NZ   1 
ATOM   5467 H H    A LYS   B 1 102 ? 41.801 -29.664 12.284  0.50 31.77 ?  102 LYS   B H    1 
ATOM   5468 H H    B LYS   B 1 102 ? 41.739 -29.688 12.304  0.50 31.53 ?  102 LYS   B H    1 
ATOM   5469 H HA   A LYS   B 1 102 ? 42.756 -29.534 14.801  0.50 33.90 ?  102 LYS   B HA   1 
ATOM   5470 H HA   B LYS   B 1 102 ? 42.647 -29.572 14.844  0.50 33.43 ?  102 LYS   B HA   1 
ATOM   5471 H HB2  A LYS   B 1 102 ? 41.999 -27.479 13.035  0.50 36.71 ?  102 LYS   B HB2  1 
ATOM   5472 H HB2  B LYS   B 1 102 ? 41.890 -27.481 13.117  0.50 36.20 ?  102 LYS   B HB2  1 
ATOM   5473 H HB3  A LYS   B 1 102 ? 42.343 -27.189 14.554  0.50 36.71 ?  102 LYS   B HB3  1 
ATOM   5474 H HB3  B LYS   B 1 102 ? 42.285 -27.240 14.632  0.50 36.20 ?  102 LYS   B HB3  1 
ATOM   5475 H HG2  A LYS   B 1 102 ? 44.545 -27.837 14.189  0.50 39.18 ?  102 LYS   B HG2  1 
ATOM   5476 H HG2  B LYS   B 1 102 ? 44.464 -27.817 14.206  0.50 38.63 ?  102 LYS   B HG2  1 
ATOM   5477 H HG3  A LYS   B 1 102 ? 44.203 -28.139 12.662  0.50 39.18 ?  102 LYS   B HG3  1 
ATOM   5478 H HG3  B LYS   B 1 102 ? 44.094 -28.223 12.709  0.50 38.63 ?  102 LYS   B HG3  1 
ATOM   5479 H HD2  A LYS   B 1 102 ? 43.755 -25.890 12.300  0.50 41.47 ?  102 LYS   B HD2  1 
ATOM   5480 H HD2  B LYS   B 1 102 ? 43.646 -26.028 12.181  0.50 40.83 ?  102 LYS   B HD2  1 
ATOM   5481 H HD3  A LYS   B 1 102 ? 44.030 -25.573 13.834  0.50 41.47 ?  102 LYS   B HD3  1 
ATOM   5482 H HD3  B LYS   B 1 102 ? 43.855 -25.589 13.695  0.50 40.83 ?  102 LYS   B HD3  1 
ATOM   5483 H HE2  A LYS   B 1 102 ? 46.275 -26.109 13.551  0.50 43.25 ?  102 LYS   B HE2  1 
ATOM   5484 H HE2  B LYS   B 1 102 ? 46.123 -26.064 13.533  0.50 42.57 ?  102 LYS   B HE2  1 
ATOM   5485 H HE3  A LYS   B 1 102 ? 46.005 -26.455 12.021  0.50 43.25 ?  102 LYS   B HE3  1 
ATOM   5486 H HE3  B LYS   B 1 102 ? 45.922 -26.541 12.027  0.50 42.57 ?  102 LYS   B HE3  1 
ATOM   5487 H HZ1  A LYS   B 1 102 ? 46.864 -24.357 12.223  0.50 44.22 ?  102 LYS   B HZ1  1 
ATOM   5488 H HZ1  B LYS   B 1 102 ? 46.698 -24.401 12.088  0.50 43.51 ?  102 LYS   B HZ1  1 
ATOM   5489 H HZ2  A LYS   B 1 102 ? 45.524 -24.253 11.683  0.50 44.22 ?  102 LYS   B HZ2  1 
ATOM   5490 H HZ2  B LYS   B 1 102 ? 45.376 -24.393 11.496  0.50 43.51 ?  102 LYS   B HZ2  1 
ATOM   5491 H HZ3  A LYS   B 1 102 ? 45.770 -23.939 13.076  0.50 44.22 ?  102 LYS   B HZ3  1 
ATOM   5492 H HZ3  B LYS   B 1 102 ? 45.559 -23.959 12.866  0.50 43.51 ?  102 LYS   B HZ3  1 
ATOM   5493 N N    A GLY   B 1 103 ? 39.812 -30.006 14.404  0.50 27.19 ?  103 GLY   B N    1 
ATOM   5494 N N    B GLY   B 1 103 ? 39.694 -30.002 14.315  0.50 26.43 ?  103 GLY   B N    1 
ATOM   5495 C CA   A GLY   B 1 103 ? 38.481 -30.039 14.969  0.50 27.05 ?  103 GLY   B CA   1 
ATOM   5496 C CA   B GLY   B 1 103 ? 38.358 -30.053 14.876  0.50 26.03 ?  103 GLY   B CA   1 
ATOM   5497 C C    A GLY   B 1 103 ? 37.545 -28.964 14.465  0.50 26.42 ?  103 GLY   B C    1 
ATOM   5498 C C    B GLY   B 1 103 ? 37.432 -28.944 14.433  0.50 25.05 ?  103 GLY   B C    1 
ATOM   5499 O O    A GLY   B 1 103 ? 36.417 -28.866 14.965  0.50 26.80 ?  103 GLY   B O    1 
ATOM   5500 O O    B GLY   B 1 103 ? 36.388 -28.739 15.060  0.50 25.45 ?  103 GLY   B O    1 
ATOM   5501 H H    A GLY   B 1 103 ? 39.936 -30.577 13.774  0.50 32.64 ?  103 GLY   B H    1 
ATOM   5502 H H    B GLY   B 1 103 ? 39.813 -30.524 13.645  0.50 31.73 ?  103 GLY   B H    1 
ATOM   5503 H HA2  A GLY   B 1 103 ? 38.081 -30.900 14.773  0.50 32.47 ?  103 GLY   B HA2  1 
ATOM   5504 H HA2  B GLY   B 1 103 ? 37.950 -30.899 14.633  0.50 31.25 ?  103 GLY   B HA2  1 
ATOM   5505 H HA3  A GLY   B 1 103 ? 38.548 -29.954 15.934  0.50 32.47 ?  103 GLY   B HA3  1 
ATOM   5506 H HA3  B GLY   B 1 103 ? 38.422 -30.021 15.844  0.50 31.25 ?  103 GLY   B HA3  1 
ATOM   5507 N N    A GLU   B 1 104 ? 37.967 -28.159 13.494  0.50 25.10 ?  104 GLU   B N    1 
ATOM   5508 N N    B GLU   B 1 104 ? 37.774 -28.221 13.371  0.50 23.24 ?  104 GLU   B N    1 
ATOM   5509 C CA   A GLU   B 1 104 ? 37.132 -27.072 13.007  0.50 23.83 ?  104 GLU   B CA   1 
ATOM   5510 C CA   B GLU   B 1 104 ? 36.949 -27.112 12.917  0.50 21.55 ?  104 GLU   B CA   1 
ATOM   5511 C C    A GLU   B 1 104 ? 35.957 -27.613 12.196  0.50 24.21 ?  104 GLU   B C    1 
ATOM   5512 C C    B GLU   B 1 104 ? 35.786 -27.620 12.070  0.50 21.64 ?  104 GLU   B C    1 
ATOM   5513 O O    A GLU   B 1 104 ? 36.012 -28.706 11.626  0.50 24.76 ?  104 GLU   B O    1 
ATOM   5514 O O    B GLU   B 1 104 ? 35.860 -28.680 11.441  0.50 22.39 ?  104 GLU   B O    1 
ATOM   5515 C CB   A GLU   B 1 104 ? 37.973 -26.089 12.192  0.50 22.87 ?  104 GLU   B CB   1 
ATOM   5516 C CB   B GLU   B 1 104 ? 37.804 -26.106 12.146  0.50 20.55 ?  104 GLU   B CB   1 
ATOM   5517 C CG   A GLU   B 1 104 ? 39.082 -25.450 13.022  0.50 22.18 ?  104 GLU   B CG   1 
ATOM   5518 C CG   B GLU   B 1 104 ? 38.910 -25.516 13.014  0.50 19.78 ?  104 GLU   B CG   1 
ATOM   5519 C CD   A GLU   B 1 104 ? 39.999 -24.550 12.220  0.50 21.13 ?  104 GLU   B CD   1 
ATOM   5520 C CD   B GLU   B 1 104 ? 39.878 -24.628 12.261  0.50 18.57 ?  104 GLU   B CD   1 
ATOM   5521 O OE1  A GLU   B 1 104 ? 39.966 -24.599 10.972  0.50 19.47 ?  104 GLU   B OE1  1 
ATOM   5522 O OE1  B GLU   B 1 104 ? 39.874 -24.625 11.010  0.50 17.19 ?  104 GLU   B OE1  1 
ATOM   5523 O OE2  A GLU   B 1 104 ? 40.762 -23.788 12.850  0.50 21.93 -1 104 GLU   B OE2  1 
ATOM   5524 O OE2  B GLU   B 1 104 ? 40.656 -23.927 12.939  0.50 18.93 -1 104 GLU   B OE2  1 
ATOM   5525 H H    A GLU   B 1 104 ? 38.734 -28.218 13.110  0.50 30.14 ?  104 GLU   B H    1 
ATOM   5526 H H    B GLU   B 1 104 ? 38.481 -28.351 12.901  0.50 27.90 ?  104 GLU   B H    1 
ATOM   5527 H HA   A GLU   B 1 104 ? 36.774 -26.591 13.768  0.50 28.61 ?  104 GLU   B HA   1 
ATOM   5528 H HA   B GLU   B 1 104 ? 36.580 -26.658 13.691  0.50 25.88 ?  104 GLU   B HA   1 
ATOM   5529 H HB2  A GLU   B 1 104 ? 38.386 -26.557 11.451  0.50 27.47 ?  104 GLU   B HB2  1 
ATOM   5530 H HB2  B GLU   B 1 104 ? 38.216 -26.551 11.391  0.50 24.68 ?  104 GLU   B HB2  1 
ATOM   5531 H HB3  A GLU   B 1 104 ? 37.401 -25.379 11.861  0.50 27.47 ?  104 GLU   B HB3  1 
ATOM   5532 H HB3  B GLU   B 1 104 ? 37.239 -25.379 11.840  0.50 24.68 ?  104 GLU   B HB3  1 
ATOM   5533 H HG2  A GLU   B 1 104 ? 38.683 -24.914 13.726  0.50 26.63 ?  104 GLU   B HG2  1 
ATOM   5534 H HG2  B GLU   B 1 104 ? 38.507 -24.984 13.719  0.50 23.75 ?  104 GLU   B HG2  1 
ATOM   5535 H HG3  A GLU   B 1 104 ? 39.629 -26.149 13.414  0.50 26.63 ?  104 GLU   B HG3  1 
ATOM   5536 H HG3  B GLU   B 1 104 ? 39.425 -26.240 13.405  0.50 23.75 ?  104 GLU   B HG3  1 
ATOM   5537 N N    A ASP   B 1 105 ? 34.880 -26.831 12.162  0.50 24.11 ?  105 ASP   B N    1 
ATOM   5538 N N    B ASP   B 1 105 ? 34.700 -26.849 12.067  0.50 21.03 ?  105 ASP   B N    1 
ATOM   5539 C CA   A ASP   B 1 105 ? 33.603 -27.285 11.625  0.50 24.53 ?  105 ASP   B CA   1 
ATOM   5540 C CA   B ASP   B 1 105 ? 33.436 -27.318 11.511  0.50 21.14 ?  105 ASP   B CA   1 
ATOM   5541 C C    A ASP   B 1 105 ? 33.651 -27.325 10.101  0.50 23.28 ?  105 ASP   B C    1 
ATOM   5542 C C    B ASP   B 1 105 ? 33.494 -27.334 9.986   0.50 19.83 ?  105 ASP   B C    1 
ATOM   5543 O O    A ASP   B 1 105 ? 33.822 -26.288 9.449   0.50 22.93 ?  105 ASP   B O    1 
ATOM   5544 O O    B ASP   B 1 105 ? 33.636 -26.286 9.346   0.50 18.80 ?  105 ASP   B O    1 
ATOM   5545 C CB   A ASP   B 1 105 ? 32.491 -26.351 12.098  0.50 26.71 ?  105 ASP   B CB   1 
ATOM   5546 C CB   B ASP   B 1 105 ? 32.294 -26.429 11.998  0.50 23.29 ?  105 ASP   B CB   1 
ATOM   5547 C CG   A ASP   B 1 105 ? 31.114 -26.810 11.658  0.50 28.74 ?  105 ASP   B CG   1 
ATOM   5548 C CG   B ASP   B 1 105 ? 30.927 -27.025 11.712  0.50 25.25 ?  105 ASP   B CG   1 
ATOM   5549 O OD1  A ASP   B 1 105 ? 30.998 -27.932 11.120  0.50 29.16 ?  105 ASP   B OD1  1 
ATOM   5550 O OD1  B ASP   B 1 105 ? 30.825 -27.907 10.833  0.50 25.55 ?  105 ASP   B OD1  1 
ATOM   5551 O OD2  A ASP   B 1 105 ? 30.146 -26.042 11.846  0.50 29.76 -1 105 ASP   B OD2  1 
ATOM   5552 O OD2  B ASP   B 1 105 ? 29.951 -26.612 12.372  0.50 25.63 -1 105 ASP   B OD2  1 
ATOM   5553 H H    A ASP   B 1 105 ? 34.869 -26.022 12.450  0.50 28.95 ?  105 ASP   B H    1 
ATOM   5554 H H    B ASP   B 1 105 ? 34.672 -26.048 12.378  0.50 25.26 ?  105 ASP   B H    1 
ATOM   5555 H HA   A ASP   B 1 105 ? 33.413 -28.180 11.951  0.50 29.46 ?  105 ASP   B HA   1 
ATOM   5556 H HA   B ASP   B 1 105 ? 33.265 -28.221 11.817  0.50 25.38 ?  105 ASP   B HA   1 
ATOM   5557 H HB2  A ASP   B 1 105 ? 32.512 -26.302 13.070  0.50 32.07 ?  105 ASP   B HB2  1 
ATOM   5558 H HB2  B ASP   B 1 105 ? 32.373 -26.309 12.960  0.50 27.96 ?  105 ASP   B HB2  1 
ATOM   5559 H HB3  A ASP   B 1 105 ? 32.635 -25.471 11.721  0.50 32.07 ?  105 ASP   B HB3  1 
ATOM   5560 H HB3  B ASP   B 1 105 ? 32.348 -25.567 11.555  0.50 27.96 ?  105 ASP   B HB3  1 
ATOM   5561 N N    A ILE   B 1 106 ? 33.478 -28.523 9.537   0.50 22.71 ?  106 ILE   B N    1 
ATOM   5562 N N    B ILE   B 1 106 ? 33.371 -28.533 9.408   0.50 19.85 ?  106 ILE   B N    1 
ATOM   5563 C CA   A ILE   B 1 106 ? 33.476 -28.701 8.089   0.50 21.66 ?  106 ILE   B CA   1 
ATOM   5564 C CA   B ILE   B 1 106 ? 33.377 -28.698 7.958   0.50 19.25 ?  106 ILE   B CA   1 
ATOM   5565 C C    A ILE   B 1 106 ? 32.379 -27.882 7.415   0.50 20.39 ?  106 ILE   B C    1 
ATOM   5566 C C    B ILE   B 1 106 ? 32.274 -27.884 7.289   0.50 18.07 ?  106 ILE   B C    1 
ATOM   5567 O O    A ILE   B 1 106 ? 32.476 -27.579 6.221   0.50 19.89 ?  106 ILE   B O    1 
ATOM   5568 O O    B ILE   B 1 106 ? 32.367 -27.576 6.095   0.50 16.78 ?  106 ILE   B O    1 
ATOM   5569 C CB   A ILE   B 1 106 ? 33.366 -30.209 7.756   0.50 22.46 ?  106 ILE   B CB   1 
ATOM   5570 C CB   B ILE   B 1 106 ? 33.282 -30.204 7.616   0.50 20.53 ?  106 ILE   B CB   1 
ATOM   5571 C CG1  A ILE   B 1 106 ? 33.597 -30.461 6.264   0.50 22.67 ?  106 ILE   B CG1  1 
ATOM   5572 C CG1  B ILE   B 1 106 ? 33.565 -30.449 6.133   0.50 21.09 ?  106 ILE   B CG1  1 
ATOM   5573 C CG2  A ILE   B 1 106 ? 32.011 -30.755 8.186   0.50 23.19 ?  106 ILE   B CG2  1 
ATOM   5574 C CG2  B ILE   B 1 106 ? 31.915 -30.759 8.000   0.50 21.42 ?  106 ILE   B CG2  1 
ATOM   5575 C CD1  A ILE   B 1 106 ? 34.952 -30.000 5.776   0.50 22.76 ?  106 ILE   B CD1  1 
ATOM   5576 C CD1  B ILE   B 1 106 ? 34.940 -29.996 5.697   0.50 21.40 ?  106 ILE   B CD1  1 
ATOM   5577 H H    A ILE   B 1 106 ? 33.368 -29.251 9.979   0.50 27.27 ?  106 ILE   B H    1 
ATOM   5578 H H    B ILE   B 1 106 ? 33.296 -29.267 9.842   0.50 23.84 ?  106 ILE   B H    1 
ATOM   5579 H HA   A ILE   B 1 106 ? 34.326 -28.387 7.748   0.50 26.01 ?  106 ILE   B HA   1 
ATOM   5580 H HA   B ILE   B 1 106 ? 34.223 -28.371 7.621   0.50 23.12 ?  106 ILE   B HA   1 
ATOM   5581 H HB   A ILE   B 1 106 ? 34.053 -30.682 8.252   0.50 26.97 ?  106 ILE   B HB   1 
ATOM   5582 H HB   B ILE   B 1 106 ? 33.954 -30.676 8.133   0.50 24.65 ?  106 ILE   B HB   1 
ATOM   5583 H HG12 A ILE   B 1 106 ? 33.535 -31.416 6.095   0.50 27.22 ?  106 ILE   B HG12 1 
ATOM   5584 H HG12 B ILE   B 1 106 ? 33.500 -31.402 5.955   0.50 25.33 ?  106 ILE   B HG12 1 
ATOM   5585 H HG13 A ILE   B 1 106 ? 32.921 -29.993 5.754   0.50 27.22 ?  106 ILE   B HG13 1 
ATOM   5586 H HG13 B ILE   B 1 106 ? 32.912 -29.971 5.602   0.50 25.33 ?  106 ILE   B HG13 1 
ATOM   5587 H HG21 A ILE   B 1 106 ? 32.016 -31.720 8.088   0.50 27.85 ?  106 ILE   B HG21 1 
ATOM   5588 H HG21 B ILE   B 1 106 ? 31.935 -31.726 7.923   0.50 25.72 ?  106 ILE   B HG21 1 
ATOM   5589 H HG22 A ILE   B 1 106 ? 31.856 -30.518 9.113   0.50 27.85 ?  106 ILE   B HG22 1 
ATOM   5590 H HG22 B ILE   B 1 106 ? 31.718 -30.504 8.915   0.50 25.72 ?  106 ILE   B HG22 1 
ATOM   5591 H HG23 A ILE   B 1 106 ? 31.321 -30.369 7.625   0.50 27.85 ?  106 ILE   B HG23 1 
ATOM   5592 H HG23 B ILE   B 1 106 ? 31.245 -30.394 7.402   0.50 25.72 ?  106 ILE   B HG23 1 
ATOM   5593 H HD11 A ILE   B 1 106 ? 35.129 -30.401 4.912   0.50 27.34 ?  106 ILE   B HD11 1 
ATOM   5594 H HD11 B ILE   B 1 106 ? 35.151 -30.405 4.845   0.50 25.70 ?  106 ILE   B HD11 1 
ATOM   5595 H HD12 A ILE   B 1 106 ? 34.946 -29.033 5.696   0.50 27.34 ?  106 ILE   B HD12 1 
ATOM   5596 H HD12 B ILE   B 1 106 ? 34.942 -29.030 5.611   0.50 25.70 ?  106 ILE   B HD12 1 
ATOM   5597 H HD13 A ILE   B 1 106 ? 35.629 -30.276 6.414   0.50 27.34 ?  106 ILE   B HD13 1 
ATOM   5598 H HD13 B ILE   B 1 106 ? 35.589 -30.271 6.365   0.50 25.70 ?  106 ILE   B HD13 1 
ATOM   5599 N N    A GLN   B 1 107 ? 31.333 -27.509 8.155   0.50 20.55 ?  107 GLN   B N    1 
ATOM   5600 N N    B GLN   B 1 107 ? 31.232 -27.514 8.035   0.50 19.12 ?  107 GLN   B N    1 
ATOM   5601 C CA   A GLN   B 1 107 ? 30.256 -26.709 7.580   0.50 20.63 ?  107 GLN   B CA   1 
ATOM   5602 C CA   B GLN   B 1 107 ? 30.155 -26.709 7.470   0.50 20.07 ?  107 GLN   B CA   1 
ATOM   5603 C C    A GLN   B 1 107 ? 30.744 -25.364 7.048   0.50 18.56 ?  107 GLN   B C    1 
ATOM   5604 C C    B GLN   B 1 107 ? 30.636 -25.343 6.988   0.50 18.36 ?  107 GLN   B C    1 
ATOM   5605 O O    A GLN   B 1 107 ? 30.100 -24.798 6.158   0.50 19.49 ?  107 GLN   B O    1 
ATOM   5606 O O    B GLN   B 1 107 ? 29.975 -24.733 6.141   0.50 19.42 ?  107 GLN   B O    1 
ATOM   5607 C CB   A GLN   B 1 107 ? 29.157 -26.500 8.626   0.50 23.65 ?  107 GLN   B CB   1 
ATOM   5608 C CB   B GLN   B 1 107 ? 29.038 -26.551 8.507   0.50 23.36 ?  107 GLN   B CB   1 
ATOM   5609 C CG   A GLN   B 1 107 ? 27.832 -25.998 8.063   0.50 26.79 ?  107 GLN   B CG   1 
ATOM   5610 C CG   B GLN   B 1 107 ? 27.712 -26.050 7.949   0.50 26.72 ?  107 GLN   B CG   1 
ATOM   5611 C CD   A GLN   B 1 107 ? 27.776 -24.486 7.930   0.50 29.26 ?  107 GLN   B CD   1 
ATOM   5612 C CD   B GLN   B 1 107 ? 27.605 -24.537 7.948   0.50 29.37 ?  107 GLN   B CD   1 
ATOM   5613 O OE1  A GLN   B 1 107 ? 28.610 -23.769 8.485   0.50 30.18 ?  107 GLN   B OE1  1 
ATOM   5614 O OE1  B GLN   B 1 107 ? 28.447 -23.841 8.518   0.50 30.35 ?  107 GLN   B OE1  1 
ATOM   5615 N NE2  A GLN   B 1 107 ? 26.784 -23.993 7.190   0.50 30.09 ?  107 GLN   B NE2  1 
ATOM   5616 N NE2  B GLN   B 1 107 ? 26.560 -24.019 7.310   0.50 30.27 ?  107 GLN   B NE2  1 
ATOM   5617 H H    A GLN   B 1 107 ? 31.222 -27.713 8.979   0.50 24.68 ?  107 GLN   B H    1 
ATOM   5618 H H    B GLN   B 1 107 ? 31.126 -27.719 8.860   0.50 22.96 ?  107 GLN   B H    1 
ATOM   5619 H HA   A GLN   B 1 107 ? 29.869 -27.199 6.836   0.50 24.78 ?  107 GLN   B HA   1 
ATOM   5620 H HA   B GLN   B 1 107 ? 29.782 -27.179 6.708   0.50 24.10 ?  107 GLN   B HA   1 
ATOM   5621 H HB2  A GLN   B 1 107 ? 28.984 -27.345 9.067   0.50 28.40 ?  107 GLN   B HB2  1 
ATOM   5622 H HB2  B GLN   B 1 107 ? 28.874 -27.414 8.914   0.50 28.05 ?  107 GLN   B HB2  1 
ATOM   5623 H HB3  A GLN   B 1 107 ? 29.467 -25.851 9.278   0.50 28.40 ?  107 GLN   B HB3  1 
ATOM   5624 H HB3  B GLN   B 1 107 ? 29.331 -25.923 9.186   0.50 28.05 ?  107 GLN   B HB3  1 
ATOM   5625 H HG2  A GLN   B 1 107 ? 27.697 -26.378 7.182   0.50 32.16 ?  107 GLN   B HG2  1 
ATOM   5626 H HG2  B GLN   B 1 107 ? 27.616 -26.356 7.034   0.50 32.08 ?  107 GLN   B HG2  1 
ATOM   5627 H HG3  A GLN   B 1 107 ? 27.112 -26.275 8.655   0.50 32.16 ?  107 GLN   B HG3  1 
ATOM   5628 H HG3  B GLN   B 1 107 ? 26.987 -26.405 8.492   0.50 32.08 ?  107 GLN   B HG3  1 
ATOM   5629 H HE21 A GLN   B 1 107 ? 26.220 -24.525 6.815   0.50 36.13 ?  107 GLN   B HE21 1 
ATOM   5630 H HE21 B GLN   B 1 107 ? 25.993 -24.536 6.921   0.50 36.35 ?  107 GLN   B HE21 1 
ATOM   5631 H HE22 A GLN   B 1 107 ? 26.703 -23.143 7.087   0.50 36.13 ?  107 GLN   B HE22 1 
ATOM   5632 H HE22 B GLN   B 1 107 ? 26.452 -23.166 7.284   0.50 36.35 ?  107 GLN   B HE22 1 
ATOM   5633 N N    A LEU   B 1 108 ? 31.863 -24.843 7.559   0.50 16.27 ?  108 LEU   B N    1 
ATOM   5634 N N    B LEU   B 1 108 ? 31.769 -24.855 7.494   0.50 16.21 ?  108 LEU   B N    1 
ATOM   5635 C CA   A LEU   B 1 108 ? 32.396 -23.551 7.127   0.50 14.77 ?  108 LEU   B CA   1 
ATOM   5636 C CA   B LEU   B 1 108 ? 32.315 -23.560 7.095   0.50 14.83 ?  108 LEU   B CA   1 
ATOM   5637 C C    A LEU   B 1 108 ? 33.036 -23.593 5.746   0.50 13.25 ?  108 LEU   B C    1 
ATOM   5638 C C    B LEU   B 1 108 ? 32.983 -23.587 5.727   0.50 13.24 ?  108 LEU   B C    1 
ATOM   5639 O O    A LEU   B 1 108 ? 33.486 -22.546 5.259   0.50 13.14 ?  108 LEU   B O    1 
ATOM   5640 O O    B LEU   B 1 108 ? 33.402 -22.531 5.234   0.50 12.83 ?  108 LEU   B O    1 
ATOM   5641 C CB   A LEU   B 1 108 ? 33.410 -23.040 8.152   0.50 15.42 ?  108 LEU   B CB   1 
ATOM   5642 C CB   B LEU   B 1 108 ? 33.312 -23.076 8.147   0.50 15.30 ?  108 LEU   B CB   1 
ATOM   5643 C CG   A LEU   B 1 108 ? 32.805 -22.550 9.469   0.50 16.61 ?  108 LEU   B CG   1 
ATOM   5644 C CG   B LEU   B 1 108 ? 32.687 -22.742 9.502   0.50 16.32 ?  108 LEU   B CG   1 
ATOM   5645 C CD1  A LEU   B 1 108 ? 33.849 -22.502 10.573  0.50 16.99 ?  108 LEU   B CD1  1 
ATOM   5646 C CD1  B LEU   B 1 108 ? 33.756 -22.569 10.566  0.50 16.72 ?  108 LEU   B CD1  1 
ATOM   5647 C CD2  A LEU   B 1 108 ? 32.183 -21.180 9.271   0.50 17.14 ?  108 LEU   B CD2  1 
ATOM   5648 C CD2  B LEU   B 1 108 ? 31.844 -21.484 9.386   0.50 17.10 ?  108 LEU   B CD2  1 
ATOM   5649 H H    A LEU   B 1 108 ? 32.327 -25.220 8.172   0.50 19.54 ?  108 LEU   B H    1 
ATOM   5650 H H    B LEU   B 1 108 ? 32.240 -25.258 8.086   0.50 19.47 ?  108 LEU   B H    1 
ATOM   5651 H HA   A LEU   B 1 108 ? 31.668 -22.914 7.092   0.50 17.75 ?  108 LEU   B HA   1 
ATOM   5652 H HA   B LEU   B 1 108 ? 31.591 -22.918 7.054   0.50 17.81 ?  108 LEU   B HA   1 
ATOM   5653 H HB2  A LEU   B 1 108 ? 34.025 -23.756 8.364   0.50 18.52 ?  108 LEU   B HB2  1 
ATOM   5654 H HB2  B LEU   B 1 108 ? 33.972 -23.769 8.294   0.50 18.38 ?  108 LEU   B HB2  1 
ATOM   5655 H HB3  A LEU   B 1 108 ? 33.895 -22.296 7.762   0.50 18.52 ?  108 LEU   B HB3  1 
ATOM   5656 H HB3  B LEU   B 1 108 ? 33.745 -22.273 7.819   0.50 18.38 ?  108 LEU   B HB3  1 
ATOM   5657 H HG   A LEU   B 1 108 ? 32.104 -23.161 9.746   0.50 19.95 ?  108 LEU   B HG   1 
ATOM   5658 H HG   B LEU   B 1 108 ? 32.104 -23.469 9.774   0.50 19.60 ?  108 LEU   B HG   1 
ATOM   5659 H HD11 A LEU   B 1 108 ? 33.417 -22.252 11.406  0.50 20.41 ?  108 LEU   B HD11 1 
ATOM   5660 H HD11 B LEU   B 1 108 ? 33.331 -22.358 11.412  0.50 20.09 ?  108 LEU   B HD11 1 
ATOM   5661 H HD12 A LEU   B 1 108 ? 34.256 -23.377 10.661  0.50 20.41 ?  108 LEU   B HD12 1 
ATOM   5662 H HD12 B LEU   B 1 108 ? 34.260 -23.394 10.644  0.50 20.09 ?  108 LEU   B HD12 1 
ATOM   5663 H HD13 A LEU   B 1 108 ? 34.523 -21.844 10.341  0.50 20.41 ?  108 LEU   B HD13 1 
ATOM   5664 H HD13 B LEU   B 1 108 ? 34.347 -21.844 10.304  0.50 20.09 ?  108 LEU   B HD13 1 
ATOM   5665 H HD21 A LEU   B 1 108 ? 31.839 -20.865 10.122  0.50 20.59 ?  108 LEU   B HD21 1 
ATOM   5666 H HD21 B LEU   B 1 108 ? 31.570 -21.204 10.272  0.50 20.53 ?  108 LEU   B HD21 1 
ATOM   5667 H HD22 A LEU   B 1 108 ? 32.860 -20.571 8.942   0.50 20.59 ?  108 LEU   B HD22 1 
ATOM   5668 H HD22 B LEU   B 1 108 ? 32.377 -20.786 8.969   0.50 20.53 ?  108 LEU   B HD22 1 
ATOM   5669 H HD23 A LEU   B 1 108 ? 31.459 -21.252 8.629   0.50 20.59 ?  108 LEU   B HD23 1 
ATOM   5670 H HD23 B LEU   B 1 108 ? 31.064 -21.672 8.842   0.50 20.53 ?  108 LEU   B HD23 1 
ATOM   5671 N N    . LEU   B 1 109 ? 33.079 -24.762 5.107   1.00 12.46 ?  109 LEU   B N    1 
ATOM   5672 C CA   . LEU   B 1 109 ? 33.713 -24.871 3.802   1.00 11.47 ?  109 LEU   B CA   1 
ATOM   5673 C C    . LEU   B 1 109 ? 32.953 -24.083 2.742   1.00 10.61 ?  109 LEU   B C    1 
ATOM   5674 O O    . LEU   B 1 109 ? 33.571 -23.488 1.852   1.00 10.58 ?  109 LEU   B O    1 
ATOM   5675 C CB   . LEU   B 1 109 ? 33.821 -26.347 3.424   1.00 11.49 ?  109 LEU   B CB   1 
ATOM   5676 C CG   . LEU   B 1 109 ? 34.612 -26.685 2.163   1.00 11.60 ?  109 LEU   B CG   1 
ATOM   5677 C CD1  . LEU   B 1 109 ? 35.996 -26.045 2.173   1.00 11.80 ?  109 LEU   B CD1  1 
ATOM   5678 C CD2  . LEU   B 1 109 ? 34.737 -28.194 2.025   1.00 12.56 ?  109 LEU   B CD2  1 
ATOM   5679 H H    A LEU   B 1 109 ? 32.750 -25.497 5.402   0.50 14.97 ?  109 LEU   B H    1 
ATOM   5680 H H    B LEU   B 1 109 ? 32.784 -25.506 5.417   0.50 14.97 ?  109 LEU   B H    1 
ATOM   5681 H HA   . LEU   B 1 109 ? 34.608 -24.508 3.853   1.00 13.79 ?  109 LEU   B HA   1 
ATOM   5682 H HB2  . LEU   B 1 109 ? 34.249 -26.815 4.156   1.00 13.80 ?  109 LEU   B HB2  1 
ATOM   5683 H HB3  . LEU   B 1 109 ? 32.927 -26.697 3.297   1.00 13.80 ?  109 LEU   B HB3  1 
ATOM   5684 H HG   . LEU   B 1 109 ? 34.134 -26.360 1.382   1.00 13.93 ?  109 LEU   B HG   1 
ATOM   5685 H HD11 . LEU   B 1 109 ? 36.521 -26.406 1.440   1.00 14.18 ?  109 LEU   B HD11 1 
ATOM   5686 H HD12 . LEU   B 1 109 ? 35.901 -25.087 2.070   1.00 14.18 ?  109 LEU   B HD12 1 
ATOM   5687 H HD13 . LEU   B 1 109 ? 36.431 -26.248 3.017   1.00 14.18 ?  109 LEU   B HD13 1 
ATOM   5688 H HD21 . LEU   B 1 109 ? 35.302 -28.401 1.260   1.00 15.10 ?  109 LEU   B HD21 1 
ATOM   5689 H HD22 . LEU   B 1 109 ? 35.138 -28.555 2.832   1.00 15.10 ?  109 LEU   B HD22 1 
ATOM   5690 H HD23 . LEU   B 1 109 ? 33.856 -28.579 1.894   1.00 15.10 ?  109 LEU   B HD23 1 
ATOM   5691 N N    . LYS   B 1 110 ? 31.619 -24.056 2.815   1.00 10.61 ?  110 LYS   B N    1 
ATOM   5692 C CA   . LYS   B 1 110 ? 30.864 -23.292 1.827   1.00 10.58 ?  110 LYS   B CA   1 
ATOM   5693 C C    . LYS   B 1 110 ? 31.198 -21.804 1.921   1.00 10.02 ?  110 LYS   B C    1 
ATOM   5694 O O    . LYS   B 1 110 ? 31.455 -21.151 0.907   1.00 9.93  ?  110 LYS   B O    1 
ATOM   5695 C CB   . LYS   B 1 110 ? 29.363 -23.544 1.971   1.00 10.92 ?  110 LYS   B CB   1 
ATOM   5696 C CG   . LYS   B 1 110 ? 28.552 -22.914 0.839   1.00 11.45 ?  110 LYS   B CG   1 
ATOM   5697 C CD   . LYS   B 1 110 ? 27.090 -23.344 0.856   1.00 11.81 ?  110 LYS   B CD   1 
ATOM   5698 C CE   . LYS   B 1 110 ? 26.323 -22.818 -0.360  1.00 12.71 ?  110 LYS   B CE   1 
ATOM   5699 N NZ   . LYS   B 1 110 ? 26.662 -23.546 -1.613  1.00 13.02 ?  110 LYS   B NZ   1 
ATOM   5700 H H    . LYS   B 1 110 ? 31.144 -24.466 3.402   1.00 12.76 ?  110 LYS   B H    1 
ATOM   5701 H HA   . LYS   B 1 110 ? 31.121 -23.594 0.939   1.00 12.71 ?  110 LYS   B HA   1 
ATOM   5702 H HB2  . LYS   B 1 110 ? 29.199 -24.503 1.956   1.00 13.12 ?  110 LYS   B HB2  1 
ATOM   5703 H HB3  . LYS   B 1 110 ? 29.057 -23.169 2.808   1.00 13.12 ?  110 LYS   B HB3  1 
ATOM   5704 H HG2  . LYS   B 1 110 ? 28.574 -21.946 0.929   1.00 13.76 ?  110 LYS   B HG2  1 
ATOM   5705 H HG3  . LYS   B 1 110 ? 28.928 -23.175 -0.016  1.00 13.76 ?  110 LYS   B HG3  1 
ATOM   5706 H HD2  . LYS   B 1 110 ? 27.043 -24.317 0.845   1.00 14.20 ?  110 LYS   B HD2  1 
ATOM   5707 H HD3  . LYS   B 1 110 ? 26.661 -23.003 1.657   1.00 14.20 ?  110 LYS   B HD3  1 
ATOM   5708 H HE2  . LYS   B 1 110 ? 25.372 -22.916 -0.203  1.00 15.27 ?  110 LYS   B HE2  1 
ATOM   5709 H HE3  . LYS   B 1 110 ? 26.545 -21.882 -0.488  1.00 15.27 ?  110 LYS   B HE3  1 
ATOM   5710 H HZ1  . LYS   B 1 110 ? 26.202 -23.214 -2.296  1.00 15.64 ?  110 LYS   B HZ1  1 
ATOM   5711 H HZ2  . LYS   B 1 110 ? 27.534 -23.470 -1.786  1.00 15.64 ?  110 LYS   B HZ2  1 
ATOM   5712 H HZ3  . LYS   B 1 110 ? 26.464 -24.413 -1.526  1.00 15.64 ?  110 LYS   B HZ3  1 
ATOM   5713 N N    . SER   B 1 111 ? 31.225 -21.255 3.140   1.00 10.55 ?  111 SER   B N    1 
ATOM   5714 C CA   . SER   B 1 111 ? 31.613 -19.855 3.315   1.00 10.58 ?  111 SER   B CA   1 
ATOM   5715 C C    . SER   B 1 111 ? 32.996 -19.593 2.734   1.00 10.11 ?  111 SER   B C    1 
ATOM   5716 O O    . SER   B 1 111 ? 33.225 -18.556 2.100   1.00 10.51 ?  111 SER   B O    1 
ATOM   5717 C CB   . SER   B 1 111 ? 31.595 -19.485 4.797   1.00 11.91 ?  111 SER   B CB   1 
ATOM   5718 O OG   . SER   B 1 111 ? 30.286 -19.508 5.318   1.00 13.83 ?  111 SER   B OG   1 
ATOM   5719 H H    . SER   B 1 111 ? 31.028 -21.672 3.866   1.00 12.68 ?  111 SER   B H    1 
ATOM   5720 H HA   . SER   B 1 111 ? 30.979 -19.292 2.849   1.00 12.72 ?  111 SER   B HA   1 
ATOM   5721 H HB2  . SER   B 1 111 ? 32.137 -20.122 5.287   1.00 14.31 ?  111 SER   B HB2  1 
ATOM   5722 H HB3  . SER   B 1 111 ? 31.950 -18.593 4.901   1.00 14.31 ?  111 SER   B HB3  1 
ATOM   5723 H HG   . SER   B 1 111 ? 30.291 -19.308 6.136   1.00 16.62 ?  111 SER   B HG   1 
ATOM   5724 N N    . ALA   B 1 112 ? 33.935 -20.513 2.956   1.00 9.79  ?  112 ALA   B N    1 
ATOM   5725 C CA   . ALA   B 1 112 ? 35.279 -20.346 2.413   1.00 10.05 ?  112 ALA   B CA   1 
ATOM   5726 C C    . ALA   B 1 112 ? 35.246 -20.240 0.890   1.00 9.09  ?  112 ALA   B C    1 
ATOM   5727 O O    . ALA   B 1 112 ? 35.871 -19.350 0.303   1.00 9.55  ?  112 ALA   B O    1 
ATOM   5728 C CB   . ALA   B 1 112 ? 36.177 -21.498 2.875   1.00 10.51 ?  112 ALA   B CB   1 
ATOM   5729 H H    . ALA   B 1 112 ? 33.822 -21.235 3.418   1.00 11.76 ?  112 ALA   B H    1 
ATOM   5730 H HA   . ALA   B 1 112 ? 35.655 -19.526 2.762   1.00 12.08 ?  112 ALA   B HA   1 
ATOM   5731 H HB1  . ALA   B 1 112 ? 37.071 -21.364 2.514   1.00 12.63 ?  112 ALA   B HB1  1 
ATOM   5732 H HB2  . ALA   B 1 112 ? 36.216 -21.500 3.846   1.00 12.63 ?  112 ALA   B HB2  1 
ATOM   5733 H HB3  . ALA   B 1 112 ? 35.814 -22.336 2.556   1.00 12.63 ?  112 ALA   B HB3  1 
ATOM   5734 N N    . TYR   B 1 113 ? 34.520 -21.146 0.227   1.00 9.19  ?  113 TYR   B N    1 
ATOM   5735 C CA   . TYR   B 1 113 ? 34.447 -21.096 -1.228  1.00 8.78  ?  113 TYR   B CA   1 
ATOM   5736 C C    . TYR   B 1 113 ? 33.739 -19.847 -1.742  1.00 8.83  ?  113 TYR   B C    1 
ATOM   5737 O O    . TYR   B 1 113 ? 34.011 -19.412 -2.865  1.00 8.95  ?  113 TYR   B O    1 
ATOM   5738 C CB   . TYR   B 1 113 ? 33.774 -22.357 -1.773  1.00 9.20  ?  113 TYR   B CB   1 
ATOM   5739 C CG   . TYR   B 1 113 ? 34.735 -23.507 -2.028  1.00 9.79  ?  113 TYR   B CG   1 
ATOM   5740 C CD1  . TYR   B 1 113 ? 35.733 -23.402 -2.989  1.00 10.22 ?  113 TYR   B CD1  1 
ATOM   5741 C CD2  . TYR   B 1 113 ? 34.632 -24.699 -1.326  1.00 9.81  ?  113 TYR   B CD2  1 
ATOM   5742 C CE1  . TYR   B 1 113 ? 36.610 -24.436 -3.235  1.00 10.15 ?  113 TYR   B CE1  1 
ATOM   5743 C CE2  . TYR   B 1 113 ? 35.499 -25.755 -1.573  1.00 10.30 ?  113 TYR   B CE2  1 
ATOM   5744 C CZ   . TYR   B 1 113 ? 36.486 -25.618 -2.534  1.00 10.17 ?  113 TYR   B CZ   1 
ATOM   5745 O OH   . TYR   B 1 113 ? 37.368 -26.638 -2.812  1.00 10.78 ?  113 TYR   B OH   1 
ATOM   5746 H H    . TYR   B 1 113 ? 34.068 -21.782 0.597   1.00 11.05 ?  113 TYR   B H    1 
ATOM   5747 H HA   . TYR   B 1 113 ? 35.350 -21.077 -1.567  1.00 10.56 ?  113 TYR   B HA   1 
ATOM   5748 H HB2  . TYR   B 1 113 ? 33.112 -22.665 -1.132  1.00 11.06 ?  113 TYR   B HB2  1 
ATOM   5749 H HB3  . TYR   B 1 113 ? 33.340 -22.139 -2.612  1.00 11.06 ?  113 TYR   B HB3  1 
ATOM   5750 H HD1  . TYR   B 1 113 ? 35.822 -22.607 -3.472  1.00 12.28 ?  113 TYR   B HD1  1 
ATOM   5751 H HD2  . TYR   B 1 113 ? 33.960 -24.793 -0.693  1.00 11.79 ?  113 TYR   B HD2  1 
ATOM   5752 H HE1  . TYR   B 1 113 ? 37.273 -24.348 -3.889  1.00 12.20 ?  113 TYR   B HE1  1 
ATOM   5753 H HE2  . TYR   B 1 113 ? 35.412 -26.551 -1.104  1.00 12.38 ?  113 TYR   B HE2  1 
ATOM   5754 H HH   . TYR   B 1 113 ? 37.164 -27.319 -2.363  1.00 12.96 ?  113 TYR   B HH   1 
ATOM   5755 N N    . GLU   B 1 114 ? 32.816 -19.269 -0.964  1.00 8.95  ?  114 GLU   B N    1 
ATOM   5756 C CA   . GLU   B 1 114 ? 32.131 -18.061 -1.421  1.00 8.89  ?  114 GLU   B CA   1 
ATOM   5757 C C    . GLU   B 1 114 ? 33.112 -16.936 -1.714  1.00 8.68  ?  114 GLU   B C    1 
ATOM   5758 O O    . GLU   B 1 114 ? 32.838 -16.079 -2.559  1.00 9.20  ?  114 GLU   B O    1 
ATOM   5759 C CB   . GLU   B 1 114 ? 31.063 -17.638 -0.408  1.00 9.51  ?  114 GLU   B CB   1 
ATOM   5760 C CG   . GLU   B 1 114 ? 29.845 -18.550 -0.477  1.00 9.71  ?  114 GLU   B CG   1 
ATOM   5761 C CD   . GLU   B 1 114 ? 28.830 -18.365 0.636   1.00 9.74  ?  114 GLU   B CD   1 
ATOM   5762 O OE1  . GLU   B 1 114 ? 29.124 -17.748 1.682   1.00 10.17 ?  114 GLU   B OE1  1 
ATOM   5763 O OE2  . GLU   B 1 114 ? 27.702 -18.891 0.474   1.00 10.56 -1 114 GLU   B OE2  1 
ATOM   5764 H H    . GLU   B 1 114 ? 32.564 -19.560 -0.189  1.00 10.76 ?  114 GLU   B H    1 
ATOM   5765 H HA   . GLU   B 1 114 ? 31.678 -18.264 -2.247  1.00 10.68 ?  114 GLU   B HA   1 
ATOM   5766 H HB2  . GLU   B 1 114 ? 31.428 -17.687 0.491   1.00 11.43 ?  114 GLU   B HB2  1 
ATOM   5767 H HB3  . GLU   B 1 114 ? 30.772 -16.735 -0.604  1.00 11.43 ?  114 GLU   B HB3  1 
ATOM   5768 H HG2  . GLU   B 1 114 ? 29.392 -18.397 -1.316  1.00 11.67 ?  114 GLU   B HG2  1 
ATOM   5769 H HG3  . GLU   B 1 114 ? 30.154 -19.474 -0.438  1.00 11.67 ?  114 GLU   B HG3  1 
ATOM   5770 N N    . ASN   B 1 115 ? 34.274 -16.932 -1.058  1.00 8.76  ?  115 ASN   B N    1 
ATOM   5771 C CA   . ASN   B 1 115 ? 35.267 -15.900 -1.350  1.00 8.76  ?  115 ASN   B CA   1 
ATOM   5772 C C    . ASN   B 1 115 ? 35.684 -15.916 -2.815  1.00 8.43  ?  115 ASN   B C    1 
ATOM   5773 O O    . ASN   B 1 115 ? 36.073 -14.876 -3.367  1.00 9.27  ?  115 ASN   B O    1 
ATOM   5774 C CB   . ASN   B 1 115 ? 36.505 -16.082 -0.466  1.00 9.38  ?  115 ASN   B CB   1 
ATOM   5775 C CG   . ASN   B 1 115 ? 36.238 -15.816 0.991   1.00 10.00 ?  115 ASN   B CG   1 
ATOM   5776 O OD1  . ASN   B 1 115 ? 36.242 -14.671 1.429   1.00 12.26 ?  115 ASN   B OD1  1 
ATOM   5777 N ND2  . ASN   B 1 115 ? 36.077 -16.878 1.770   1.00 10.13 ?  115 ASN   B ND2  1 
ATOM   5778 H H    . ASN   B 1 115 ? 34.516 -17.504 -0.453  1.00 10.53 ?  115 ASN   B H    1 
ATOM   5779 H HA   . ASN   B 1 115 ? 34.887 -15.030 -1.153  1.00 10.53 ?  115 ASN   B HA   1 
ATOM   5780 H HB2  . ASN   B 1 115 ? 36.824 -16.992 -0.552  1.00 11.28 ?  115 ASN   B HB2  1 
ATOM   5781 H HB3  . ASN   B 1 115 ? 37.193 -15.461 -0.757  1.00 11.28 ?  115 ASN   B HB3  1 
ATOM   5782 H HD21 . ASN   B 1 115 ? 35.932 -16.776 2.613   1.00 12.17 ?  115 ASN   B HD21 1 
ATOM   5783 H HD22 . ASN   B 1 115 ? 36.098 -17.667 1.431   1.00 12.17 ?  115 ASN   B HD22 1 
ATOM   5784 N N    . PHE   B 1 116 ? 35.662 -17.092 -3.449  1.00 8.43  ?  116 PHE   B N    1 
ATOM   5785 C CA   . PHE   B 1 116 ? 36.090 -17.190 -4.841  1.00 8.86  ?  116 PHE   B CA   1 
ATOM   5786 C C    . PHE   B 1 116 ? 35.187 -16.367 -5.754  1.00 8.60  ?  116 PHE   B C    1 
ATOM   5787 O O    . PHE   B 1 116 ? 35.623 -15.932 -6.825  1.00 8.99  ?  116 PHE   B O    1 
ATOM   5788 C CB   . PHE   B 1 116 ? 36.061 -18.639 -5.363  1.00 8.72  ?  116 PHE   B CB   1 
ATOM   5789 C CG   . PHE   B 1 116 ? 37.126 -19.594 -4.807  1.00 8.66  ?  116 PHE   B CG   1 
ATOM   5790 C CD1  . PHE   B 1 116 ? 37.785 -19.403 -3.599  1.00 9.32  ?  116 PHE   B CD1  1 
ATOM   5791 C CD2  . PHE   B 1 116 ? 37.433 -20.732 -5.541  1.00 9.09  ?  116 PHE   B CD2  1 
ATOM   5792 C CE1  . PHE   B 1 116 ? 38.718 -20.340 -3.142  1.00 9.59  ?  116 PHE   B CE1  1 
ATOM   5793 C CE2  . PHE   B 1 116 ? 38.350 -21.669 -5.090  1.00 9.07  ?  116 PHE   B CE2  1 
ATOM   5794 C CZ   . PHE   B 1 116 ? 38.993 -21.476 -3.896  1.00 9.29  ?  116 PHE   B CZ   1 
ATOM   5795 H H    . PHE   B 1 116 ? 35.407 -17.841 -3.098  1.00 10.14 ?  116 PHE   B H    1 
ATOM   5796 H HA   . PHE   B 1 116 ? 36.994 -16.854 -4.924  1.00 10.65 ?  116 PHE   B HA   1 
ATOM   5797 H HB2  . PHE   B 1 116 ? 35.192 -19.019 -5.148  1.00 10.49 ?  116 PHE   B HB2  1 
ATOM   5798 H HB3  . PHE   B 1 116 ? 36.167 -18.615 -6.327  1.00 10.49 ?  116 PHE   B HB3  1 
ATOM   5799 H HD1  . PHE   B 1 116 ? 37.589 -18.647 -3.086  1.00 11.20 ?  116 PHE   B HD1  1 
ATOM   5800 H HD2  . PHE   B 1 116 ? 36.990 -20.885 -6.345  1.00 10.92 ?  116 PHE   B HD2  1 
ATOM   5801 H HE1  . PHE   B 1 116 ? 39.156 -20.199 -2.334  1.00 11.53 ?  116 PHE   B HE1  1 
ATOM   5802 H HE2  . PHE   B 1 116 ? 38.542 -22.423 -5.601  1.00 10.91 ?  116 PHE   B HE2  1 
ATOM   5803 H HZ   . PHE   B 1 116 ? 39.629 -22.087 -3.597  1.00 11.17 ?  116 PHE   B HZ   1 
ATOM   5804 N N    . ASN   B 1 117 ? 33.923 -16.159 -5.366  1.00 8.70  ?  117 ASN   B N    1 
ATOM   5805 C CA   . ASN   B 1 117 ? 32.980 -15.464 -6.240  1.00 8.89  ?  117 ASN   B CA   1 
ATOM   5806 C C    . ASN   B 1 117 ? 33.289 -13.980 -6.392  1.00 9.36  ?  117 ASN   B C    1 
ATOM   5807 O O    . ASN   B 1 117 ? 32.688 -13.323 -7.246  1.00 10.47 ?  117 ASN   B O    1 
ATOM   5808 C CB   . ASN   B 1 117 ? 31.556 -15.684 -5.750  1.00 9.25  ?  117 ASN   B CB   1 
ATOM   5809 C CG   . ASN   B 1 117 ? 31.101 -17.098 -5.998  1.00 9.33  ?  117 ASN   B CG   1 
ATOM   5810 O OD1  . ASN   B 1 117 ? 31.446 -17.685 -7.025  1.00 10.23 ?  117 ASN   B OD1  1 
ATOM   5811 N ND2  . ASN   B 1 117 ? 30.359 -17.669 -5.059  1.00 9.54  ?  117 ASN   B ND2  1 
ATOM   5812 H H    . ASN   B 1 117 ? 33.595 -16.410 -4.606  1.00 10.46 ?  117 ASN   B H    1 
ATOM   5813 H HA   . ASN   B 1 117 ? 33.044 -15.864 -7.117  1.00 10.68 ?  117 ASN   B HA   1 
ATOM   5814 H HB2  . ASN   B 1 117 ? 31.516 -15.514 -4.792  1.00 11.12 ?  117 ASN   B HB2  1 
ATOM   5815 H HB3  . ASN   B 1 117 ? 30.962 -15.074 -6.219  1.00 11.12 ?  117 ASN   B HB3  1 
ATOM   5816 H HD21 . ASN   B 1 117 ? 30.080 -18.472 -5.163  1.00 11.47 ?  117 ASN   B HD21 1 
ATOM   5817 H HD22 . ASN   B 1 117 ? 30.142 -17.222 -4.354  1.00 11.47 ?  117 ASN   B HD22 1 
ATOM   5818 N N    . GLN   B 1 118 ? 34.225 -13.451 -5.613  1.00 9.25  ?  118 GLN   B N    1 
ATOM   5819 C CA   . GLN   B 1 118 ? 34.650 -12.064 -5.750  1.00 9.70  ?  118 GLN   B CA   1 
ATOM   5820 C C    . GLN   B 1 118 ? 35.719 -11.875 -6.821  1.00 9.91  ?  118 GLN   B C    1 
ATOM   5821 O O    . GLN   B 1 118 ? 36.200 -10.751 -6.999  1.00 11.29 ?  118 GLN   B O    1 
ATOM   5822 C CB   . GLN   B 1 118 ? 35.131 -11.531 -4.398  1.00 10.38 ?  118 GLN   B CB   1 
ATOM   5823 C CG   . GLN   B 1 118 ? 34.058 -11.566 -3.327  1.00 10.27 ?  118 GLN   B CG   1 
ATOM   5824 C CD   . GLN   B 1 118 ? 32.880 -10.659 -3.651  1.00 10.21 ?  118 GLN   B CD   1 
ATOM   5825 O OE1  . GLN   B 1 118 ? 33.065 -9.519  -4.084  1.00 10.92 ?  118 GLN   B OE1  1 
ATOM   5826 N NE2  . GLN   B 1 118 ? 31.669 -11.157 -3.450  1.00 10.75 ?  118 GLN   B NE2  1 
ATOM   5827 H H    . GLN   B 1 118 ? 34.646 -13.880 -4.991  1.00 11.12 ?  118 GLN   B H    1 
ATOM   5828 H HA   . GLN   B 1 118 ? 33.881 -11.537 -6.022  1.00 11.66 ?  118 GLN   B HA   1 
ATOM   5829 H HB2  . GLN   B 1 118 ? 35.879 -12.063 -4.095  1.00 12.48 ?  118 GLN   B HB2  1 
ATOM   5830 H HB3  . GLN   B 1 118 ? 35.407 -10.603 -4.507  1.00 12.48 ?  118 GLN   B HB3  1 
ATOM   5831 H HG2  . GLN   B 1 118 ? 33.729 -12.476 -3.248  1.00 12.34 ?  118 GLN   B HG2  1 
ATOM   5832 H HG3  . GLN   B 1 118 ? 34.446 -11.279 -2.487  1.00 12.34 ?  118 GLN   B HG3  1 
ATOM   5833 H HE21 . GLN   B 1 118 ? 31.578 -11.957 -3.145  1.00 12.92 ?  118 GLN   B HE21 1 
ATOM   5834 H HE22 . GLN   B 1 118 ? 30.980 -10.676 -3.615  1.00 12.92 ?  118 GLN   B HE22 1 
ATOM   5835 N N    . HIS   B 1 119 ? 36.076 -12.931 -7.552  1.00 8.97  ?  119 HIS   B N    1 
ATOM   5836 C CA   . HIS   B 1 119 ? 37.121 -12.885 -8.566  1.00 9.60  ?  119 HIS   B CA   1 
ATOM   5837 C C    . HIS   B 1 119 ? 36.644 -13.625 -9.800  1.00 9.55  ?  119 HIS   B C    1 
ATOM   5838 O O    . HIS   B 1 119 ? 36.139 -14.744 -9.691  1.00 10.29 ?  119 HIS   B O    1 
ATOM   5839 C CB   . HIS   B 1 119 ? 38.401 -13.516 -8.015  1.00 10.23 ?  119 HIS   B CB   1 
ATOM   5840 C CG   . HIS   B 1 119 ? 38.891 -12.807 -6.802  1.00 11.57 ?  119 HIS   B CG   1 
ATOM   5841 N ND1  . HIS   B 1 119 ? 39.684 -11.682 -6.876  1.00 13.16 ?  119 HIS   B ND1  1 
ATOM   5842 C CD2  . HIS   B 1 119 ? 38.607 -12.987 -5.492  1.00 12.90 ?  119 HIS   B CD2  1 
ATOM   5843 C CE1  . HIS   B 1 119 ? 39.904 -11.227 -5.656  1.00 14.49 ?  119 HIS   B CE1  1 
ATOM   5844 N NE2  . HIS   B 1 119 ? 39.256 -11.995 -4.799  1.00 14.56 ?  119 HIS   B NE2  1 
ATOM   5845 H H    . HIS   B 1 119 ? 35.711 -13.712 -7.483  1.00 10.78 ?  119 HIS   B H    1 
ATOM   5846 H HA   . HIS   B 1 119 ? 37.301 -11.961 -8.809  1.00 11.54 ?  119 HIS   B HA   1 
ATOM   5847 H HB2  . HIS   B 1 119 ? 38.225 -14.435 -7.781  1.00 12.30 ?  119 HIS   B HB2  1 
ATOM   5848 H HB3  . HIS   B 1 119 ? 39.093 -13.466 -8.697  1.00 12.30 ?  119 HIS   B HB3  1 
ATOM   5849 H HD2  . HIS   B 1 119 ? 38.084 -13.663 -5.130  1.00 15.50 ?  119 HIS   B HD2  1 
ATOM   5850 H HE1  . HIS   B 1 119 ? 40.438 -10.496 -5.433  1.00 17.40 ?  119 HIS   B HE1  1 
ATOM   5851 H HE2  . HIS   B 1 119 ? 39.273 -11.912 -3.942  1.00 17.50 ?  119 HIS   B HE2  1 
ATOM   5852 N N    . GLU   B 1 120 ? 36.801 -13.013 -10.974 1.00 10.22 ?  120 GLU   B N    1 
ATOM   5853 C CA   . GLU   B 1 120 ? 36.207 -13.603 -12.171 1.00 11.67 ?  120 GLU   B CA   1 
ATOM   5854 C C    . GLU   B 1 120 ? 36.884 -14.902 -12.587 1.00 10.50 ?  120 GLU   B C    1 
ATOM   5855 O O    . GLU   B 1 120 ? 36.224 -15.773 -13.166 1.00 10.72 ?  120 GLU   B O    1 
ATOM   5856 C CB   . GLU   B 1 120 ? 36.206 -12.598 -13.320 1.00 16.07 ?  120 GLU   B CB   1 
ATOM   5857 C CG   . GLU   B 1 120 ? 35.252 -11.440 -13.087 1.00 22.54 ?  120 GLU   B CG   1 
ATOM   5858 C CD   . GLU   B 1 120 ? 35.075 -10.553 -14.303 1.00 29.40 ?  120 GLU   B CD   1 
ATOM   5859 O OE1  . GLU   B 1 120 ? 36.067 -10.327 -15.029 1.00 31.91 ?  120 GLU   B OE1  1 
ATOM   5860 O OE2  . GLU   B 1 120 ? 33.942 -10.079 -14.527 1.00 31.87 -1 120 GLU   B OE2  1 
ATOM   5861 H H    . GLU   B 1 120 ? 37.229 -12.276 -11.105 1.00 12.28 ?  120 GLU   B H    1 
ATOM   5862 H HA   . GLU   B 1 120 ? 35.283 -13.816 -11.980 1.00 14.02 ?  120 GLU   B HA   1 
ATOM   5863 H HB2  . GLU   B 1 120 ? 37.096 -12.233 -13.427 1.00 19.30 ?  120 GLU   B HB2  1 
ATOM   5864 H HB3  . GLU   B 1 120 ? 35.932 -13.049 -14.136 1.00 19.30 ?  120 GLU   B HB3  1 
ATOM   5865 H HG2  . GLU   B 1 120 ? 34.380 -11.794 -12.845 1.00 27.07 ?  120 GLU   B HG2  1 
ATOM   5866 H HG3  . GLU   B 1 120 ? 35.596 -10.888 -12.371 1.00 27.07 ?  120 GLU   B HG3  1 
ATOM   5867 N N    . VAL   B 1 121 ? 38.184 -15.041 -12.325 1.00 10.05 ?  121 VAL   B N    1 
ATOM   5868 C CA   . VAL   B 1 121 ? 38.932 -16.250 -12.670 1.00 10.09 ?  121 VAL   B CA   1 
ATOM   5869 C C    . VAL   B 1 121 ? 40.044 -16.451 -11.650 1.00 9.48  ?  121 VAL   B C    1 
ATOM   5870 O O    . VAL   B 1 121 ? 40.722 -15.492 -11.261 1.00 10.16 ?  121 VAL   B O    1 
ATOM   5871 C CB   . VAL   B 1 121 ? 39.450 -16.211 -14.127 1.00 11.72 ?  121 VAL   B CB   1 
ATOM   5872 C CG1  . VAL   B 1 121 ? 40.326 -14.991 -14.383 1.00 12.97 ?  121 VAL   B CG1  1 
ATOM   5873 C CG2  . VAL   B 1 121 ? 40.187 -17.497 -14.479 1.00 12.94 ?  121 VAL   B CG2  1 
ATOM   5874 H H    . VAL   B 1 121 ? 38.669 -14.433 -11.948 1.00 12.08 ?  121 VAL   B H    1 
ATOM   5875 H HA   . VAL   B 1 121 ? 38.328 -17.004 -12.601 1.00 12.13 ?  121 VAL   B HA   1 
ATOM   5876 H HB   . VAL   B 1 121 ? 38.684 -16.147 -14.723 1.00 14.09 ?  121 VAL   B HB   1 
ATOM   5877 H HG11 . VAL   B 1 121 ? 40.627 -15.005 -15.306 1.00 15.58 ?  121 VAL   B HG11 1 
ATOM   5878 H HG12 . VAL   B 1 121 ? 39.804 -14.187 -14.221 1.00 15.58 ?  121 VAL   B HG12 1 
ATOM   5879 H HG13 . VAL   B 1 121 ? 41.088 -15.017 -13.785 1.00 15.58 ?  121 VAL   B HG13 1 
ATOM   5880 H HG21 . VAL   B 1 121 ? 40.391 -17.493 -15.430 1.00 15.55 ?  121 VAL   B HG21 1 
ATOM   5881 H HG22 . VAL   B 1 121 ? 41.011 -17.539 -13.969 1.00 15.55 ?  121 VAL   B HG22 1 
ATOM   5882 H HG23 . VAL   B 1 121 ? 39.623 -18.254 -14.266 1.00 15.55 ?  121 VAL   B HG23 1 
ATOM   5883 N N    . LEU   B 1 122 ? 40.230 -17.704 -11.213 1.00 9.03  ?  122 LEU   B N    1 
ATOM   5884 C CA   . LEU   B 1 122 ? 41.212 -18.046 -10.188 1.00 8.89  ?  122 LEU   B CA   1 
ATOM   5885 C C    . LEU   B 1 122 ? 41.868 -19.377 -10.513 1.00 8.61  ?  122 LEU   B C    1 
ATOM   5886 O O    . LEU   B 1 122 ? 41.210 -20.301 -11.007 1.00 9.95  ?  122 LEU   B O    1 
ATOM   5887 C CB   . LEU   B 1 122 ? 40.555 -18.281 -8.815  1.00 10.69 ?  122 LEU   B CB   1 
ATOM   5888 C CG   . LEU   B 1 122 ? 39.526 -17.257 -8.326  1.00 10.61 ?  122 LEU   B CG   1 
ATOM   5889 C CD1  . LEU   B 1 122 ? 38.125 -17.606 -8.796  1.00 11.57 ?  122 LEU   B CD1  1 
ATOM   5890 C CD2  . LEU   B 1 122 ? 39.572 -17.147 -6.810  1.00 10.27 ?  122 LEU   B CD2  1 
ATOM   5891 H H    . LEU   B 1 122 ? 39.790 -18.387 -11.502 1.00 10.86 ?  122 LEU   B H    1 
ATOM   5892 H HA   . LEU   B 1 122 ? 41.888 -17.349 -10.113 1.00 10.69 ?  122 LEU   B HA   1 
ATOM   5893 H HB2  . LEU   B 1 122 ? 40.108 -19.137 -8.843  1.00 12.85 ?  122 LEU   B HB2  1 
ATOM   5894 H HB3  . LEU   B 1 122 ? 41.260 -18.310 -8.149  1.00 12.85 ?  122 LEU   B HB3  1 
ATOM   5895 H HG   . LEU   B 1 122 ? 39.750 -16.386 -8.685  1.00 12.75 ?  122 LEU   B HG   1 
ATOM   5896 H HD11 . LEU   B 1 122 ? 37.500 -16.959 -8.433  1.00 13.91 ?  122 LEU   B HD11 1 
ATOM   5897 H HD12 . LEU   B 1 122 ? 38.104 -17.577 -9.765  1.00 13.91 ?  122 LEU   B HD12 1 
ATOM   5898 H HD13 . LEU   B 1 122 ? 37.900 -18.496 -8.485  1.00 13.91 ?  122 LEU   B HD13 1 
ATOM   5899 H HD21 . LEU   B 1 122 ? 38.895 -16.517 -6.513  1.00 12.34 ?  122 LEU   B HD21 1 
ATOM   5900 H HD22 . LEU   B 1 122 ? 39.403 -18.020 -6.421  1.00 12.34 ?  122 LEU   B HD22 1 
ATOM   5901 H HD23 . LEU   B 1 122 ? 40.452 -16.832 -6.541  1.00 12.34 ?  122 LEU   B HD23 1 
ATOM   5902 N N    . LEU   B 1 123 ? 43.156 -19.484 -10.159 1.00 8.71  ?  123 LEU   B N    1 
ATOM   5903 C CA   . LEU   B 1 123 ? 43.871 -20.753 -10.028 1.00 8.92  ?  123 LEU   B CA   1 
ATOM   5904 C C    . LEU   B 1 123 ? 43.834 -21.147 -8.554  1.00 8.43  ?  123 LEU   B C    1 
ATOM   5905 O O    . LEU   B 1 123 ? 44.189 -20.325 -7.700  1.00 9.36  ?  123 LEU   B O    1 
ATOM   5906 C CB   . LEU   B 1 123 ? 45.325 -20.561 -10.473 1.00 9.23  ?  123 LEU   B CB   1 
ATOM   5907 C CG   . LEU   B 1 123 ? 46.271 -21.741 -10.229 1.00 9.81  ?  123 LEU   B CG   1 
ATOM   5908 C CD1  . LEU   B 1 123 ? 45.851 -22.976 -11.017 1.00 10.24 ?  123 LEU   B CD1  1 
ATOM   5909 C CD2  . LEU   B 1 123 ? 47.685 -21.334 -10.590 1.00 10.71 ?  123 LEU   B CD2  1 
ATOM   5910 H H    . LEU   B 1 123 ? 43.651 -18.805 -9.969  1.00 10.47 ?  123 LEU   B H    1 
ATOM   5911 H HA   . LEU   B 1 123 ? 43.445 -21.446 -10.564 1.00 10.72 ?  123 LEU   B HA   1 
ATOM   5912 H HB2  . LEU   B 1 123 ? 45.327 -20.386 -11.426 1.00 11.09 ?  123 LEU   B HB2  1 
ATOM   5913 H HB3  . LEU   B 1 123 ? 45.686 -19.799 -10.001 1.00 11.09 ?  123 LEU   B HB3  1 
ATOM   5914 H HG   . LEU   B 1 123 ? 46.262 -21.970 -9.286  1.00 11.80 ?  123 LEU   B HG   1 
ATOM   5915 H HD11 . LEU   B 1 123 ? 46.493 -23.681 -10.855 1.00 12.31 ?  123 LEU   B HD11 1 
ATOM   5916 H HD12 . LEU   B 1 123 ? 44.971 -23.249 -10.719 1.00 12.31 ?  123 LEU   B HD12 1 
ATOM   5917 H HD13 . LEU   B 1 123 ? 45.831 -22.750 -11.958 1.00 12.31 ?  123 LEU   B HD13 1 
ATOM   5918 H HD21 . LEU   B 1 123 ? 48.281 -22.080 -10.433 1.00 12.88 ?  123 LEU   B HD21 1 
ATOM   5919 H HD22 . LEU   B 1 123 ? 47.711 -21.075 -11.524 1.00 12.88 ?  123 LEU   B HD22 1 
ATOM   5920 H HD23 . LEU   B 1 123 ? 47.946 -20.579 -10.033 1.00 12.88 ?  123 LEU   B HD23 1 
ATOM   5921 N N    . ALA   B 1 124 ? 43.412 -22.378 -8.240  1.00 8.42  ?  124 ALA   B N    1 
ATOM   5922 C CA   . ALA   B 1 124 ? 43.150 -22.688 -6.842  1.00 8.53  ?  124 ALA   B CA   1 
ATOM   5923 C C    . ALA   B 1 124 ? 43.427 -24.148 -6.519  1.00 8.67  ?  124 ALA   B C    1 
ATOM   5924 O O    . ALA   B 1 124 ? 43.292 -25.025 -7.384  1.00 9.08  ?  124 ALA   B O    1 
ATOM   5925 C CB   . ALA   B 1 124 ? 41.693 -22.380 -6.479  1.00 9.13  ?  124 ALA   B CB   1 
ATOM   5926 H H    . ALA   B 1 124 ? 43.260 -23.024 -8.795  1.00 10.12 ?  124 ALA   B H    1 
ATOM   5927 H HA   . ALA   B 1 124 ? 43.719 -22.133 -6.294  1.00 10.26 ?  124 ALA   B HA   1 
ATOM   5928 H HB1  . ALA   B 1 124 ? 41.541 -22.590 -5.543  1.00 10.98 ?  124 ALA   B HB1  1 
ATOM   5929 H HB2  . ALA   B 1 124 ? 41.521 -21.433 -6.632  1.00 10.98 ?  124 ALA   B HB2  1 
ATOM   5930 H HB3  . ALA   B 1 124 ? 41.103 -22.911 -7.036  1.00 10.98 ?  124 ALA   B HB3  1 
ATOM   5931 N N    . PRO   B 1 125 ? 43.718 -24.445 -5.256  1.00 8.82  ?  125 PRO   B N    1 
ATOM   5932 C CA   . PRO   B 1 125 ? 43.654 -25.809 -4.734  1.00 9.44  ?  125 PRO   B CA   1 
ATOM   5933 C C    . PRO   B 1 125 ? 42.251 -26.088 -4.196  1.00 9.46  ?  125 PRO   B C    1 
ATOM   5934 O O    . PRO   B 1 125 ? 41.454 -25.175 -3.980  1.00 9.95  ?  125 PRO   B O    1 
ATOM   5935 C CB   . PRO   B 1 125 ? 44.637 -25.733 -3.562  1.00 10.60 ?  125 PRO   B CB   1 
ATOM   5936 C CG   . PRO   B 1 125 ? 44.381 -24.346 -2.991  1.00 10.63 ?  125 PRO   B CG   1 
ATOM   5937 C CD   . PRO   B 1 125 ? 44.033 -23.475 -4.188  1.00 9.49  ?  125 PRO   B CD   1 
ATOM   5938 H HA   . PRO   B 1 125 ? 43.927 -26.478 -5.382  1.00 11.34 ?  125 PRO   B HA   1 
ATOM   5939 H HB2  . PRO   B 1 125 ? 44.434 -26.421 -2.905  1.00 12.74 ?  125 PRO   B HB2  1 
ATOM   5940 H HB3  . PRO   B 1 125 ? 45.548 -25.815 -3.882  1.00 12.74 ?  125 PRO   B HB3  1 
ATOM   5941 H HG2  . PRO   B 1 125 ? 43.639 -24.377 -2.364  1.00 12.78 ?  125 PRO   B HG2  1 
ATOM   5942 H HG3  . PRO   B 1 125 ? 45.183 -24.017 -2.548  1.00 12.78 ?  125 PRO   B HG3  1 
ATOM   5943 H HD2  . PRO   B 1 125 ? 43.260 -22.922 -3.994  1.00 11.41 ?  125 PRO   B HD2  1 
ATOM   5944 H HD3  . PRO   B 1 125 ? 44.799 -22.930 -4.442  1.00 11.41 ?  125 PRO   B HD3  1 
ATOM   5945 N N    . LEU   B 1 126 ? 41.979 -27.370 -3.931  1.00 9.95  ?  126 LEU   B N    1 
ATOM   5946 C CA   . LEU   B 1 126 ? 40.758 -27.742 -3.222  1.00 10.53 ?  126 LEU   B CA   1 
ATOM   5947 C C    . LEU   B 1 126 ? 40.872 -27.343 -1.759  1.00 10.84 ?  126 LEU   B C    1 
ATOM   5948 O O    . LEU   B 1 126 ? 41.758 -27.809 -1.036  1.00 12.49 ?  126 LEU   B O    1 
ATOM   5949 C CB   . LEU   B 1 126 ? 40.504 -29.238 -3.340  1.00 11.84 ?  126 LEU   B CB   1 
ATOM   5950 C CG   . LEU   B 1 126 ? 39.967 -29.717 -4.689  1.00 12.61 ?  126 LEU   B CG   1 
ATOM   5951 C CD1  . LEU   B 1 126 ? 40.030 -31.234 -4.782  1.00 14.67 ?  126 LEU   B CD1  1 
ATOM   5952 C CD2  . LEU   B 1 126 ? 38.545 -29.242 -4.919  1.00 12.61 ?  126 LEU   B CD2  1 
ATOM   5953 H H    . LEU   B 1 126 ? 42.488 -28.036 -4.134  1.00 11.96 ?  126 LEU   B H    1 
ATOM   5954 H HA   . LEU   B 1 126 ? 40.009 -27.267 -3.612  1.00 12.65 ?  126 LEU   B HA   1 
ATOM   5955 H HB2  . LEU   B 1 126 ? 41.338 -29.704 -3.179  1.00 14.22 ?  126 LEU   B HB2  1 
ATOM   5956 H HB3  . LEU   B 1 126 ? 39.855 -29.491 -2.665  1.00 14.22 ?  126 LEU   B HB3  1 
ATOM   5957 H HG   . LEU   B 1 126 ? 40.522 -29.352 -5.397  1.00 15.15 ?  126 LEU   B HG   1 
ATOM   5958 H HD11 . LEU   B 1 126 ? 39.684 -31.513 -5.644  1.00 17.63 ?  126 LEU   B HD11 1 
ATOM   5959 H HD12 . LEU   B 1 126 ? 40.950 -31.520 -4.685  1.00 17.63 ?  126 LEU   B HD12 1 
ATOM   5960 H HD13 . LEU   B 1 126 ? 39.488 -31.615 -4.071  1.00 17.63 ?  126 LEU   B HD13 1 
ATOM   5961 H HD21 . LEU   B 1 126 ? 38.204 -29.646 -5.733  1.00 15.15 ?  126 LEU   B HD21 1 
ATOM   5962 H HD22 . LEU   B 1 126 ? 37.997 -29.509 -4.163  1.00 15.15 ?  126 LEU   B HD22 1 
ATOM   5963 H HD23 . LEU   B 1 126 ? 38.542 -28.276 -5.004  1.00 15.15 ?  126 LEU   B HD23 1 
ATOM   5964 N N    . LEU   B 1 127 ? 39.945 -26.508 -1.307  1.00 10.48 ?  127 LEU   B N    1 
ATOM   5965 C CA   . LEU   B 1 127 ? 39.994 -26.018 0.057   1.00 10.64 ?  127 LEU   B CA   1 
ATOM   5966 C C    . LEU   B 1 127 ? 39.720 -27.143 1.047   1.00 10.27 ?  127 LEU   B C    1 
ATOM   5967 O O    . LEU   B 1 127 ? 38.899 -28.040 0.816   1.00 10.77 ?  127 LEU   B O    1 
ATOM   5968 C CB   . LEU   B 1 127 ? 38.975 -24.897 0.270   1.00 10.98 ?  127 LEU   B CB   1 
ATOM   5969 C CG   . LEU   B 1 127 ? 39.140 -23.631 -0.573  1.00 11.66 ?  127 LEU   B CG   1 
ATOM   5970 C CD1  . LEU   B 1 127 ? 38.022 -22.659 -0.225  1.00 12.05 ?  127 LEU   B CD1  1 
ATOM   5971 C CD2  . LEU   B 1 127 ? 40.508 -22.990 -0.368  1.00 12.37 ?  127 LEU   B CD2  1 
ATOM   5972 H H    . LEU   B 1 127 ? 39.277 -26.204 -1.764  1.00 12.59 ?  127 LEU   B H    1 
ATOM   5973 H HA   . LEU   B 1 127 ? 40.880 -25.660 0.238   1.00 12.79 ?  127 LEU   B HA   1 
ATOM   5974 H HB2  . LEU   B 1 127 ? 38.095 -25.254 0.083   1.00 13.19 ?  127 LEU   B HB2  1 
ATOM   5975 H HB3  . LEU   B 1 127 ? 39.017 -24.625 1.202   1.00 13.19 ?  127 LEU   B HB3  1 
ATOM   5976 H HG   . LEU   B 1 127 ? 39.041 -23.856 -1.508  1.00 14.02 ?  127 LEU   B HG   1 
ATOM   5977 H HD11 . LEU   B 1 127 ? 38.125 -21.850 -0.758  1.00 14.48 ?  127 LEU   B HD11 1 
ATOM   5978 H HD12 . LEU   B 1 127 ? 37.165 -23.068 -0.411  1.00 14.48 ?  127 LEU   B HD12 1 
ATOM   5979 H HD13 . LEU   B 1 127 ? 38.081 -22.431 0.720   1.00 14.48 ?  127 LEU   B HD13 1 
ATOM   5980 H HD21 . LEU   B 1 127 ? 40.537 -22.144 -0.847  1.00 14.86 ?  127 LEU   B HD21 1 
ATOM   5981 H HD22 . LEU   B 1 127 ? 40.651 -22.838 0.578   1.00 14.86 ?  127 LEU   B HD22 1 
ATOM   5982 H HD23 . LEU   B 1 127 ? 41.187 -23.588 -0.716  1.00 14.86 ?  127 LEU   B HD23 1 
ATOM   5983 N N    . SER   B 1 128 ? 40.396 -27.054 2.186   1.00 10.60 ?  128 SER   B N    1 
ATOM   5984 C CA   . SER   B 1 128 ? 40.294 -27.974 3.311   1.00 11.06 ?  128 SER   B CA   1 
ATOM   5985 C C    . SER   B 1 128 ? 40.792 -29.381 2.987   1.00 11.87 ?  128 SER   B C    1 
ATOM   5986 O O    . SER   B 1 128 ? 40.693 -30.270 3.838   1.00 13.29 ?  128 SER   B O    1 
ATOM   5987 C CB   . SER   B 1 128 ? 38.894 -27.983 3.939   1.00 11.39 ?  128 SER   B CB   1 
ATOM   5988 O OG   . SER   B 1 128 ? 38.572 -26.707 4.477   1.00 11.98 ?  128 SER   B OG   1 
ATOM   5989 H H    . SER   B 1 128 ? 40.956 -26.415 2.341   1.00 12.74 ?  128 SER   B H    1 
ATOM   5990 H HA   . SER   B 1 128 ? 40.883 -27.631 4.000   1.00 13.29 ?  128 SER   B HA   1 
ATOM   5991 H HB2  . SER   B 1 128 ? 38.242 -28.224 3.264   1.00 13.68 ?  128 SER   B HB2  1 
ATOM   5992 H HB3  . SER   B 1 128 ? 38.878 -28.648 4.658   1.00 13.68 ?  128 SER   B HB3  1 
ATOM   5993 H HG   . SER   B 1 128 ? 39.130 -26.501 5.070   1.00 14.40 ?  128 SER   B HG   1 
ATOM   5994 N N    . ALA   B 1 129 ? 41.379 -29.597 1.809   1.00 12.81 ?  129 ALA   B N    1 
ATOM   5995 C CA   . ALA   B 1 129 ? 41.920 -30.897 1.451   1.00 13.42 ?  129 ALA   B CA   1 
ATOM   5996 C C    . ALA   B 1 129 ? 43.307 -31.077 2.054   1.00 12.66 ?  129 ALA   B C    1 
ATOM   5997 O O    . ALA   B 1 129 ? 43.873 -30.174 2.686   1.00 12.70 ?  129 ALA   B O    1 
ATOM   5998 C CB   . ALA   B 1 129 ? 41.964 -31.052 -0.067  1.00 15.23 ?  129 ALA   B CB   1 
ATOM   5999 H H    . ALA   B 1 129 ? 41.472 -28.997 1.200   1.00 15.39 ?  129 ALA   B H    1 
ATOM   6000 H HA   . ALA   B 1 129 ? 41.345 -31.586 1.810   1.00 16.12 ?  129 ALA   B HA   1 
ATOM   6001 H HB1  . ALA   B 1 129 ? 42.322 -31.926 -0.281  1.00 18.29 ?  129 ALA   B HB1  1 
ATOM   6002 H HB2  . ALA   B 1 129 ? 41.062 -30.967 -0.414  1.00 18.29 ?  129 ALA   B HB2  1 
ATOM   6003 H HB3  . ALA   B 1 129 ? 42.530 -30.358 -0.438  1.00 18.29 ?  129 ALA   B HB3  1 
ATOM   6004 N N    . GLY   B 1 130 ? 43.854 -32.272 1.858   1.00 12.89 ?  130 GLY   B N    1 
ATOM   6005 C CA   . GLY   B 1 130 ? 45.245 -32.514 2.201   1.00 13.18 ?  130 GLY   B CA   1 
ATOM   6006 C C    . GLY   B 1 130 ? 45.465 -32.408 3.692   1.00 13.21 ?  130 GLY   B C    1 
ATOM   6007 O O    . GLY   B 1 130 ? 44.770 -33.049 4.494   1.00 14.12 ?  130 GLY   B O    1 
ATOM   6008 H H    . GLY   B 1 130 ? 43.444 -32.956 1.529   1.00 15.49 ?  130 GLY   B H    1 
ATOM   6009 H HA2  . GLY   B 1 130 ? 45.505 -33.405 1.909   1.00 15.84 ?  130 GLY   B HA2  1 
ATOM   6010 H HA3  . GLY   B 1 130 ? 45.810 -31.867 1.752   1.00 15.84 ?  130 GLY   B HA3  1 
ATOM   6011 N N    . ILE   B 1 131 ? 46.432 -31.570 4.075   1.00 13.67 ?  131 ILE   B N    1 
ATOM   6012 C CA   . ILE   B 1 131 ? 46.777 -31.428 5.482   1.00 14.32 ?  131 ILE   B CA   1 
ATOM   6013 C C    . ILE   B 1 131 ? 45.652 -30.832 6.310   1.00 13.67 ?  131 ILE   B C    1 
ATOM   6014 O O    . ILE   B 1 131 ? 45.722 -30.896 7.542   1.00 15.18 ?  131 ILE   B O    1 
ATOM   6015 C CB   . ILE   B 1 131 ? 48.095 -30.647 5.683   1.00 16.29 ?  131 ILE   B CB   1 
ATOM   6016 C CG1  . ILE   B 1 131 ? 47.933 -29.172 5.286   1.00 17.09 ?  131 ILE   B CG1  1 
ATOM   6017 C CG2  . ILE   B 1 131 ? 49.229 -31.310 4.899   1.00 17.32 ?  131 ILE   B CG2  1 
ATOM   6018 C CD1  . ILE   B 1 131 ? 49.149 -28.313 5.603   1.00 18.22 ?  131 ILE   B CD1  1 
ATOM   6019 H H    . ILE   B 1 131 ? 46.897 -31.080 3.542   1.00 16.42 ?  131 ILE   B H    1 
ATOM   6020 H HA   . ILE   B 1 131 ? 46.925 -32.318 5.831   1.00 17.21 ?  131 ILE   B HA   1 
ATOM   6021 H HB   . ILE   B 1 131 ? 48.317 -30.684 6.626   1.00 19.57 ?  131 ILE   B HB   1 
ATOM   6022 H HG12 . ILE   B 1 131 ? 47.771 -29.126 4.331   1.00 20.53 ?  131 ILE   B HG12 1 
ATOM   6023 H HG13 . ILE   B 1 131 ? 47.175 -28.796 5.764   1.00 20.53 ?  131 ILE   B HG13 1 
ATOM   6024 H HG21 . ILE   B 1 131 ? 50.067 -30.901 5.158   1.00 20.81 ?  131 ILE   B HG21 1 
ATOM   6025 H HG22 . ILE   B 1 131 ? 49.241 -32.257 5.106   1.00 20.81 ?  131 ILE   B HG22 1 
ATOM   6026 H HG23 . ILE   B 1 131 ? 49.072 -31.180 3.951   1.00 20.81 ?  131 ILE   B HG23 1 
ATOM   6027 H HD11 . ILE   B 1 131 ? 48.936 -27.386 5.409   1.00 21.88 ?  131 ILE   B HD11 1 
ATOM   6028 H HD12 . ILE   B 1 131 ? 49.368 -28.412 6.542   1.00 21.88 ?  131 ILE   B HD12 1 
ATOM   6029 H HD13 . ILE   B 1 131 ? 49.892 -28.604 5.055   1.00 21.88 ?  131 ILE   B HD13 1 
ATOM   6030 N N    . PHE   B 1 132 ? 44.623 -30.259 5.675   1.00 12.45 ?  132 PHE   B N    1 
ATOM   6031 C CA   . PHE   B 1 132 ? 43.456 -29.760 6.397   1.00 12.66 ?  132 PHE   B CA   1 
ATOM   6032 C C    . PHE   B 1 132 ? 42.430 -30.853 6.710   1.00 13.72 ?  132 PHE   B C    1 
ATOM   6033 O O    . PHE   B 1 132 ? 41.508 -30.606 7.496   1.00 15.63 ?  132 PHE   B O    1 
ATOM   6034 C CB   . PHE   B 1 132 ? 42.780 -28.626 5.611   1.00 11.92 ?  132 PHE   B CB   1 
ATOM   6035 C CG   . PHE   B 1 132 ? 43.477 -27.279 5.719   1.00 12.38 ?  132 PHE   B CG   1 
ATOM   6036 C CD1  . PHE   B 1 132 ? 44.767 -27.093 5.239   1.00 13.73 ?  132 PHE   B CD1  1 
ATOM   6037 C CD2  . PHE   B 1 132 ? 42.805 -26.184 6.246   1.00 11.59 ?  132 PHE   B CD2  1 
ATOM   6038 C CE1  . PHE   B 1 132 ? 45.383 -25.850 5.325   1.00 13.93 ?  132 PHE   B CE1  1 
ATOM   6039 C CE2  . PHE   B 1 132 ? 43.416 -24.940 6.328   1.00 12.42 ?  132 PHE   B CE2  1 
ATOM   6040 C CZ   . PHE   B 1 132 ? 44.701 -24.777 5.867   1.00 13.52 ?  132 PHE   B CZ   1 
ATOM   6041 H H    . PHE   B 1 132 ? 44.580 -30.146 4.822   1.00 14.96 ?  132 PHE   B H    1 
ATOM   6042 H HA   . PHE   B 1 132 ? 43.755 -29.387 7.239   1.00 15.21 ?  132 PHE   B HA   1 
ATOM   6043 H HB2  . PHE   B 1 132 ? 42.766 -28.869 4.674   1.00 14.33 ?  132 PHE   B HB2  1 
ATOM   6044 H HB3  . PHE   B 1 132 ? 41.873 -28.517 5.937   1.00 14.33 ?  132 PHE   B HB3  1 
ATOM   6045 H HD1  . PHE   B 1 132 ? 45.230 -27.816 4.875   1.00 16.50 ?  132 PHE   B HD1  1 
ATOM   6046 H HD2  . PHE   B 1 132 ? 41.935 -26.292 6.561   1.00 13.93 ?  132 PHE   B HD2  1 
ATOM   6047 H HE1  . PHE   B 1 132 ? 46.254 -25.743 5.013   1.00 16.74 ?  132 PHE   B HE1  1 
ATOM   6048 H HE2  . PHE   B 1 132 ? 42.958 -24.218 6.698   1.00 14.93 ?  132 PHE   B HE2  1 
ATOM   6049 H HZ   . PHE   B 1 132 ? 45.116 -23.943 5.927   1.00 16.24 ?  132 PHE   B HZ   1 
ATOM   6050 N N    . GLY   B 1 133 ? 42.549 -32.045 6.115   1.00 13.40 ?  133 GLY   B N    1 
ATOM   6051 C CA   . GLY   B 1 133 ? 41.837 -33.213 6.603   1.00 14.33 ?  133 GLY   B CA   1 
ATOM   6052 C C    . GLY   B 1 133 ? 40.440 -33.471 6.071   1.00 14.70 ?  133 GLY   B C    1 
ATOM   6053 O O    . GLY   B 1 133 ? 39.850 -34.489 6.444   1.00 16.45 ?  133 GLY   B O    1 
ATOM   6054 H H    . GLY   B 1 133 ? 43.049 -32.195 5.429   1.00 16.10 ?  133 GLY   B H    1 
ATOM   6055 H HA2  . GLY   B 1 133 ? 42.370 -33.994 6.404   1.00 17.22 ?  133 GLY   B HA2  1 
ATOM   6056 H HA3  . GLY   B 1 133 ? 41.769 -33.139 7.567   1.00 17.22 ?  133 GLY   B HA3  1 
ATOM   6057 N N    . ALA   B 1 134 ? 39.878 -32.603 5.236   1.00 13.94 ?  134 ALA   B N    1 
ATOM   6058 C CA   . ALA   B 1 134 ? 38.549 -32.881 4.706   1.00 14.08 ?  134 ALA   B CA   1 
ATOM   6059 C C    . ALA   B 1 134 ? 38.631 -33.880 3.554   1.00 14.03 ?  134 ALA   B C    1 
ATOM   6060 O O    . ALA   B 1 134 ? 39.686 -34.081 2.945   1.00 15.22 ?  134 ALA   B O    1 
ATOM   6061 C CB   . ALA   B 1 134 ? 37.878 -31.593 4.232   1.00 14.73 ?  134 ALA   B CB   1 
ATOM   6062 H H    . ALA   B 1 134 ? 40.232 -31.857 4.970   1.00 16.74 ?  134 ALA   B H    1 
ATOM   6063 H HA   . ALA   B 1 134 ? 38.002 -33.260 5.412   1.00 16.92 ?  134 ALA   B HA   1 
ATOM   6064 H HB1  . ALA   B 1 134 ? 36.990 -31.802 3.902   1.00 17.70 ?  134 ALA   B HB1  1 
ATOM   6065 H HB2  . ALA   B 1 134 ? 37.813 -30.973 4.978   1.00 17.70 ?  134 ALA   B HB2  1 
ATOM   6066 H HB3  . ALA   B 1 134 ? 38.411 -31.199 3.524   1.00 17.70 ?  134 ALA   B HB3  1 
ATOM   6067 N N    . ASP   B 1 135 ? 37.494 -34.500 3.260   1.00 13.95 ?  135 ASP   B N    1 
ATOM   6068 C CA   . ASP   B 1 135 ? 37.398 -35.398 2.117   1.00 14.78 ?  135 ASP   B CA   1 
ATOM   6069 C C    . ASP   B 1 135 ? 37.501 -34.569 0.843   1.00 13.98 ?  135 ASP   B C    1 
ATOM   6070 O O    . ASP   B 1 135 ? 36.649 -33.700 0.612   1.00 13.91 ?  135 ASP   B O    1 
ATOM   6071 C CB   . ASP   B 1 135 ? 36.055 -36.125 2.172   1.00 16.76 ?  135 ASP   B CB   1 
ATOM   6072 C CG   . ASP   B 1 135 ? 35.865 -37.113 1.034   1.00 18.82 ?  135 ASP   B CG   1 
ATOM   6073 O OD1  . ASP   B 1 135 ? 36.732 -37.176 0.134   1.00 18.44 ?  135 ASP   B OD1  1 
ATOM   6074 O OD2  . ASP   B 1 135 ? 34.847 -37.846 1.055   1.00 21.76 -1 135 ASP   B OD2  1 
ATOM   6075 H H    . ASP   B 1 135 ? 36.763 -34.412 3.706   1.00 16.76 ?  135 ASP   B H    1 
ATOM   6076 H HA   . ASP   B 1 135 ? 38.119 -36.046 2.152   1.00 17.76 ?  135 ASP   B HA   1 
ATOM   6077 H HB2  . ASP   B 1 135 ? 36.004 -36.617 3.003   1.00 20.13 ?  135 ASP   B HB2  1 
ATOM   6078 H HB3  . ASP   B 1 135 ? 35.345 -35.468 2.126   1.00 20.13 ?  135 ASP   B HB3  1 
ATOM   6079 N N    . PRO   B 1 136 ? 38.513 -34.782 -0.003  1.00 13.99 ?  136 PRO   B N    1 
ATOM   6080 C CA   . PRO   B 1 136 ? 38.620 -33.955 -1.216  1.00 13.12 ?  136 PRO   B CA   1 
ATOM   6081 C C    . PRO   B 1 136 ? 37.439 -34.111 -2.152  1.00 12.63 ?  136 PRO   B C    1 
ATOM   6082 O O    . PRO   B 1 136 ? 37.118 -33.162 -2.876  1.00 11.98 ?  136 PRO   B O    1 
ATOM   6083 C CB   . PRO   B 1 136 ? 39.937 -34.426 -1.852  1.00 14.39 ?  136 PRO   B CB   1 
ATOM   6084 C CG   . PRO   B 1 136 ? 40.122 -35.824 -1.338  1.00 15.52 ?  136 PRO   B CG   1 
ATOM   6085 C CD   . PRO   B 1 136 ? 39.572 -35.802 0.062   1.00 14.95 ?  136 PRO   B CD   1 
ATOM   6086 H HA   . PRO   B 1 136 ? 38.708 -33.019 -0.978  1.00 15.76 ?  136 PRO   B HA   1 
ATOM   6087 H HB2  . PRO   B 1 136 ? 39.860 -34.421 -2.821  1.00 17.29 ?  136 PRO   B HB2  1 
ATOM   6088 H HB3  . PRO   B 1 136 ? 40.666 -33.852 -1.565  1.00 17.29 ?  136 PRO   B HB3  1 
ATOM   6089 H HG2  . PRO   B 1 136 ? 39.626 -36.446 -1.892  1.00 18.64 ?  136 PRO   B HG2  1 
ATOM   6090 H HG3  . PRO   B 1 136 ? 41.067 -36.050 -1.331  1.00 18.64 ?  136 PRO   B HG3  1 
ATOM   6091 H HD2  . PRO   B 1 136 ? 39.192 -36.665 0.290   1.00 17.96 ?  136 PRO   B HD2  1 
ATOM   6092 H HD3  . PRO   B 1 136 ? 40.257 -35.536 0.695   1.00 17.96 ?  136 PRO   B HD3  1 
ATOM   6093 N N    . ILE   B 1 137 ? 36.778 -35.273 -2.159  1.00 12.97 ?  137 ILE   B N    1 
ATOM   6094 C CA   . ILE   B 1 137 ? 35.566 -35.437 -2.957  1.00 13.30 ?  137 ILE   B CA   1 
ATOM   6095 C C    . ILE   B 1 137 ? 34.490 -34.469 -2.485  1.00 12.74 ?  137 ILE   B C    1 
ATOM   6096 O O    . ILE   B 1 137 ? 33.777 -33.858 -3.291  1.00 12.73 ?  137 ILE   B O    1 
ATOM   6097 C CB   . ILE   B 1 137 ? 35.096 -36.904 -2.902  1.00 15.41 ?  137 ILE   B CB   1 
ATOM   6098 C CG1  . ILE   B 1 137 ? 36.100 -37.800 -3.629  1.00 17.93 ?  137 ILE   B CG1  1 
ATOM   6099 C CG2  . ILE   B 1 137 ? 33.707 -37.051 -3.503  1.00 15.95 ?  137 ILE   B CG2  1 
ATOM   6100 C CD1  . ILE   B 1 137 ? 35.789 -39.278 -3.528  1.00 20.44 ?  137 ILE   B CD1  1 
ATOM   6101 H H    . ILE   B 1 137 ? 37.010 -35.972 -1.719  1.00 15.58 ?  137 ILE   B H    1 
ATOM   6102 H HA   . ILE   B 1 137 ? 35.765 -35.229 -3.885  1.00 15.98 ?  137 ILE   B HA   1 
ATOM   6103 H HB   . ILE   B 1 137 ? 35.055 -37.179 -1.977  1.00 18.51 ?  137 ILE   B HB   1 
ATOM   6104 H HG12 . ILE   B 1 137 ? 36.110 -37.565 -4.571  1.00 21.54 ?  137 ILE   B HG12 1 
ATOM   6105 H HG13 . ILE   B 1 137 ? 36.979 -37.658 -3.246  1.00 21.54 ?  137 ILE   B HG13 1 
ATOM   6106 H HG21 . ILE   B 1 137 ? 33.493 -37.994 -3.597  1.00 19.16 ?  137 ILE   B HG21 1 
ATOM   6107 H HG22 . ILE   B 1 137 ? 33.059 -36.634 -2.916  1.00 19.16 ?  137 ILE   B HG22 1 
ATOM   6108 H HG23 . ILE   B 1 137 ? 33.691 -36.624 -4.374  1.00 19.16 ?  137 ILE   B HG23 1 
ATOM   6109 H HD11 . ILE   B 1 137 ? 36.572 -39.783 -3.799  1.00 24.54 ?  137 ILE   B HD11 1 
ATOM   6110 H HD12 . ILE   B 1 137 ? 35.559 -39.492 -2.611  1.00 24.54 ?  137 ILE   B HD12 1 
ATOM   6111 H HD13 . ILE   B 1 137 ? 35.044 -39.489 -4.114  1.00 24.54 ?  137 ILE   B HD13 1 
ATOM   6112 N N    . HIS   B 1 138 ? 34.354 -34.317 -1.172  1.00 12.89 ?  138 HIS   B N    1 
ATOM   6113 C CA   . HIS   B 1 138 ? 33.402 -33.351 -0.641  1.00 13.41 ?  138 HIS   B CA   1 
ATOM   6114 C C    . HIS   B 1 138 ? 33.825 -31.921 -0.951  1.00 12.44 ?  138 HIS   B C    1 
ATOM   6115 O O    . HIS   B 1 138 ? 32.979 -31.076 -1.255  1.00 12.98 ?  138 HIS   B O    1 
ATOM   6116 C CB   . HIS   B 1 138 ? 33.261 -33.535 0.862   1.00 14.44 ?  138 HIS   B CB   1 
ATOM   6117 C CG   . HIS   B 1 138 ? 32.334 -32.550 1.494   1.00 15.30 ?  138 HIS   B CG   1 
ATOM   6118 N ND1  . HIS   B 1 138 ? 30.991 -32.484 1.185   1.00 16.68 ?  138 HIS   B ND1  1 
ATOM   6119 C CD2  . HIS   B 1 138 ? 32.560 -31.572 2.401   1.00 15.96 ?  138 HIS   B CD2  1 
ATOM   6120 C CE1  . HIS   B 1 138 ? 30.429 -31.513 1.882   1.00 16.68 ?  138 HIS   B CE1  1 
ATOM   6121 N NE2  . HIS   B 1 138 ? 31.358 -30.947 2.631   1.00 16.42 ?  138 HIS   B NE2  1 
ATOM   6122 H H    . HIS   B 1 138 ? 34.800 -34.749 -0.583  1.00 15.49 ?  138 HIS   B H    1 
ATOM   6123 H HA   . HIS   B 1 138 ? 32.534 -33.508 -1.052  1.00 16.12 ?  138 HIS   B HA   1 
ATOM   6124 H HB2  . HIS   B 1 138 ? 32.910 -34.423 1.036   1.00 17.35 ?  138 HIS   B HB2  1 
ATOM   6125 H HB3  . HIS   B 1 138 ? 34.129 -33.433 1.273   1.00 17.35 ?  138 HIS   B HB3  1 
ATOM   6126 H HD1  . HIS   B 1 138 ? 30.583 -32.998 0.625   1.00 20.03 ?  138 HIS   B HD1  1 
ATOM   6127 H HD2  . HIS   B 1 138 ? 33.367 -31.363 2.803   1.00 19.17 ?  138 HIS   B HD2  1 
ATOM   6128 H HE1  . HIS   B 1 138 ? 29.525 -31.279 1.855   1.00 20.04 ?  138 HIS   B HE1  1 
ATOM   6129 N N    . SER   B 1 139 ? 35.118 -31.620 -0.867  1.00 11.95 ?  139 SER   B N    1 
ATOM   6130 C CA   . SER   B 1 139 ? 35.558 -30.269 -1.188  1.00 11.69 ?  139 SER   B CA   1 
ATOM   6131 C C    . SER   B 1 139 ? 35.225 -29.920 -2.630  1.00 10.67 ?  139 SER   B C    1 
ATOM   6132 O O    . SER   B 1 139 ? 34.777 -28.804 -2.911  1.00 10.85 ?  139 SER   B O    1 
ATOM   6133 C CB   . SER   B 1 139 ? 37.052 -30.130 -0.910  1.00 12.10 ?  139 SER   B CB   1 
ATOM   6134 O OG   . SER   B 1 139 ? 37.464 -28.805 -1.187  1.00 12.48 ?  139 SER   B OG   1 
ATOM   6135 H H    . SER   B 1 139 ? 35.736 -32.166 -0.641  1.00 14.36 ?  139 SER   B H    1 
ATOM   6136 H HA   . SER   B 1 139 ? 35.085 -29.648 -0.622  1.00 14.05 ?  139 SER   B HA   1 
ATOM   6137 H HB2  . SER   B 1 139 ? 37.218 -30.327 0.026   1.00 14.55 ?  139 SER   B HB2  1 
ATOM   6138 H HB3  . SER   B 1 139 ? 37.544 -30.743 -1.475  1.00 14.55 ?  139 SER   B HB3  1 
ATOM   6139 H HG   . SER   B 1 139 ? 37.081 -28.266 -0.668  1.00 15.00 ?  139 SER   B HG   1 
ATOM   6140 N N    . LEU   B 1 140 ? 35.413 -30.862 -3.555  1.00 10.69 ?  140 LEU   B N    1 
ATOM   6141 C CA   . LEU   B 1 140 ? 35.057 -30.614 -4.945  1.00 10.88 ?  140 LEU   B CA   1 
ATOM   6142 C C    . LEU   B 1 140 ? 33.555 -30.385 -5.082  1.00 10.98 ?  140 LEU   B C    1 
ATOM   6143 O O    . LEU   B 1 140 ? 33.120 -29.500 -5.824  1.00 10.95 ?  140 LEU   B O    1 
ATOM   6144 C CB   . LEU   B 1 140 ? 35.533 -31.778 -5.819  1.00 11.03 ?  140 LEU   B CB   1 
ATOM   6145 C CG   . LEU   B 1 140 ? 35.176 -31.678 -7.295  1.00 11.00 ?  140 LEU   B CG   1 
ATOM   6146 C CD1  . LEU   B 1 140 ? 35.731 -30.398 -7.906  1.00 11.66 ?  140 LEU   B CD1  1 
ATOM   6147 C CD2  . LEU   B 1 140 ? 35.672 -32.899 -8.034  1.00 12.20 ?  140 LEU   B CD2  1 
ATOM   6148 H H    . LEU   B 1 140 ? 35.732 -31.648 -3.404  1.00 12.85 ?  140 LEU   B H    1 
ATOM   6149 H HA   . LEU   B 1 140 ? 35.511 -29.814 -5.245  1.00 13.08 ?  140 LEU   B HA   1 
ATOM   6150 H HB2  . LEU   B 1 140 ? 36.501 -31.832 -5.759  1.00 13.26 ?  140 LEU   B HB2  1 
ATOM   6151 H HB3  . LEU   B 1 140 ? 35.142 -32.598 -5.484  1.00 13.26 ?  140 LEU   B HB3  1 
ATOM   6152 H HG   . LEU   B 1 140 ? 34.211 -31.647 -7.382  1.00 13.22 ?  140 LEU   B HG   1 
ATOM   6153 H HD11 . LEU   B 1 140 ? 35.592 -30.421 -8.867  1.00 14.02 ?  140 LEU   B HD11 1 
ATOM   6154 H HD12 . LEU   B 1 140 ? 35.258 -29.633 -7.529  1.00 14.02 ?  140 LEU   B HD12 1 
ATOM   6155 H HD13 . LEU   B 1 140 ? 36.675 -30.331 -7.709  1.00 14.02 ?  140 LEU   B HD13 1 
ATOM   6156 H HD21 . LEU   B 1 140 ? 35.433 -32.812 -8.971  1.00 14.66 ?  140 LEU   B HD21 1 
ATOM   6157 H HD22 . LEU   B 1 140 ? 36.633 -32.953 -7.939  1.00 14.66 ?  140 LEU   B HD22 1 
ATOM   6158 H HD23 . LEU   B 1 140 ? 35.250 -33.682 -7.654  1.00 14.66 ?  140 LEU   B HD23 1 
ATOM   6159 N N    . ARG   B 1 141 ? 32.752 -31.173 -4.362  1.00 11.11 ?  141 ARG   B N    1 
ATOM   6160 C CA   . ARG   B 1 141 ? 31.301 -31.003 -4.356  1.00 12.18 ?  141 ARG   B CA   1 
ATOM   6161 C C    . ARG   B 1 141 ? 30.915 -29.591 -3.926  1.00 11.60 ?  141 ARG   B C    1 
ATOM   6162 O O    . ARG   B 1 141 ? 30.112 -28.911 -4.586  1.00 11.63 ?  141 ARG   B O    1 
ATOM   6163 C CB   . ARG   B 1 141 ? 30.712 -32.033 -3.385  1.00 13.61 ?  141 ARG   B CB   1 
ATOM   6164 C CG   . ARG   B 1 141 ? 29.253 -31.896 -3.047  1.00 16.33 ?  141 ARG   B CG   1 
ATOM   6165 C CD   . ARG   B 1 141 ? 28.441 -32.540 -4.094  1.00 17.93 ?  141 ARG   B CD   1 
ATOM   6166 N NE   . ARG   B 1 141 ? 28.191 -31.640 -5.209  1.00 18.43 ?  141 ARG   B NE   1 
ATOM   6167 C CZ   . ARG   B 1 141 ? 28.189 -32.005 -6.483  1.00 18.09 ?  141 ARG   B CZ   1 
ATOM   6168 N NH1  . ARG   B 1 141 ? 28.613 -33.201 -6.862  1.00 18.12 ?  141 ARG   B NH1  1 
ATOM   6169 N NH2  . ARG   B 1 141 ? 27.750 -31.148 -7.401  1.00 18.75 ?  141 ARG   B NH2  1 
ATOM   6170 H H    . ARG   B 1 141 ? 33.031 -31.814 -3.864  1.00 13.35 ?  141 ARG   B H    1 
ATOM   6171 H HA   . ARG   B 1 141 ? 30.948 -31.167 -5.242  1.00 14.63 ?  141 ARG   B HA   1 
ATOM   6172 H HB2  . ARG   B 1 141 ? 30.847 -32.919 -3.764  1.00 16.35 ?  141 ARG   B HB2  1 
ATOM   6173 H HB3  . ARG   B 1 141 ? 31.202 -31.976 -2.552  1.00 16.35 ?  141 ARG   B HB3  1 
ATOM   6174 H HG2  . ARG   B 1 141 ? 29.080 -32.327 -2.200  1.00 19.61 ?  141 ARG   B HG2  1 
ATOM   6175 H HG3  . ARG   B 1 141 ? 29.005 -30.952 -2.996  1.00 19.61 ?  141 ARG   B HG3  1 
ATOM   6176 H HD2  . ARG   B 1 141 ? 28.909 -33.329 -4.420  1.00 21.53 ?  141 ARG   B HD2  1 
ATOM   6177 H HD3  . ARG   B 1 141 ? 27.597 -32.804 -3.709  1.00 21.53 ?  141 ARG   B HD3  1 
ATOM   6178 H HE   . ARG   B 1 141 ? 27.998 -30.824 -5.026  1.00 22.13 ?  141 ARG   B HE   1 
ATOM   6179 H HH11 . ARG   B 1 141 ? 28.881 -33.776 -6.280  1.00 21.76 ?  141 ARG   B HH11 1 
ATOM   6180 H HH12 . ARG   B 1 141 ? 28.609 -33.412 -7.694  1.00 21.76 ?  141 ARG   B HH12 1 
ATOM   6181 H HH21 . ARG   B 1 141 ? 27.480 -30.366 -7.166  1.00 22.52 ?  141 ARG   B HH21 1 
ATOM   6182 H HH22 . ARG   B 1 141 ? 27.766 -31.364 -8.234  1.00 22.52 ?  141 ARG   B HH22 1 
ATOM   6183 N N    . VAL   B 1 142 ? 31.458 -29.146 -2.795  1.00 11.12 ?  142 VAL   B N    1 
ATOM   6184 C CA   . VAL   B 1 142 ? 31.119 -27.815 -2.310  1.00 10.96 ?  142 VAL   B CA   1 
ATOM   6185 C C    . VAL   B 1 142 ? 31.599 -26.755 -3.297  1.00 10.91 ?  142 VAL   B C    1 
ATOM   6186 O O    . VAL   B 1 142 ? 30.903 -25.763 -3.550  1.00 11.34 ?  142 VAL   B O    1 
ATOM   6187 C CB   . VAL   B 1 142 ? 31.660 -27.588 -0.884  1.00 11.67 ?  142 VAL   B CB   1 
ATOM   6188 C CG1  . VAL   B 1 142 ? 31.338 -26.163 -0.406  1.00 11.82 ?  142 VAL   B CG1  1 
ATOM   6189 C CG2  . VAL   B 1 142 ? 31.086 -28.614 0.080   1.00 12.21 ?  142 VAL   B CG2  1 
ATOM   6190 H H    . VAL   B 1 142 ? 32.014 -29.581 -2.303  1.00 13.36 ?  142 VAL   B H    1 
ATOM   6191 H HA   . VAL   B 1 142 ? 30.158 -27.745 -2.260  1.00 13.18 ?  142 VAL   B HA   1 
ATOM   6192 H HB   . VAL   B 1 142 ? 32.626 -27.687 -0.887  1.00 14.02 ?  142 VAL   B HB   1 
ATOM   6193 H HG11 . VAL   B 1 142 ? 31.519 -26.101 0.544   1.00 14.20 ?  142 VAL   B HG11 1 
ATOM   6194 H HG12 . VAL   B 1 142 ? 31.896 -25.533 -0.889  1.00 14.20 ?  142 VAL   B HG12 1 
ATOM   6195 H HG13 . VAL   B 1 142 ? 30.402 -25.978 -0.578  1.00 14.20 ?  142 VAL   B HG13 1 
ATOM   6196 H HG21 . VAL   B 1 142 ? 31.411 -28.427 0.973   1.00 14.68 ?  142 VAL   B HG21 1 
ATOM   6197 H HG22 . VAL   B 1 142 ? 30.119 -28.559 0.058   1.00 14.68 ?  142 VAL   B HG22 1 
ATOM   6198 H HG23 . VAL   B 1 142 ? 31.373 -29.499 -0.199  1.00 14.68 ?  142 VAL   B HG23 1 
ATOM   6199 N N    . CYS   B 1 143 ? 32.785 -26.951 -3.879  1.00 10.55 ?  143 CYS   B N    1 
ATOM   6200 C CA   . CYS   B 1 143 ? 33.283 -26.009 -4.878  1.00 10.78 ?  143 CYS   B CA   1 
ATOM   6201 C C    . CYS   B 1 143 ? 32.286 -25.859 -6.021  1.00 10.43 ?  143 CYS   B C    1 
ATOM   6202 O O    . CYS   B 1 143 ? 31.884 -24.746 -6.377  1.00 10.71 ?  143 CYS   B O    1 
ATOM   6203 C CB   . CYS   B 1 143 ? 34.641 -26.490 -5.405  1.00 10.86 ?  143 CYS   B CB   1 
ATOM   6204 S SG   . CYS   B 1 143 ? 35.398 -25.388 -6.617  1.00 11.23 ?  143 CYS   B SG   1 
ATOM   6205 H H    . CYS   B 1 143 ? 33.315 -27.606 -3.714  1.00 12.68 ?  143 CYS   B H    1 
ATOM   6206 H HA   . CYS   B 1 143 ? 33.413 -25.136 -4.470  1.00 12.95 ?  143 CYS   B HA   1 
ATOM   6207 H HB2  . CYS   B 1 143 ? 35.259 -26.574 -4.659  1.00 13.05 ?  143 CYS   B HB2  1 
ATOM   6208 H HB3  . CYS   B 1 143 ? 34.524 -27.353 -5.823  1.00 13.05 ?  143 CYS   B HB3  1 
ATOM   6209 H HG   . CYS   B 1 143 ? 36.461 -25.837 -6.946  1.00 13.50 ?  143 CYS   B HG   1 
ATOM   6210 N N    . VAL   B 1 144 ? 31.885 -26.978 -6.621  1.00 10.69 ?  144 VAL   B N    1 
ATOM   6211 C CA   . VAL   B 1 144 ? 30.977 -26.918 -7.762  1.00 11.74 ?  144 VAL   B CA   1 
ATOM   6212 C C    . VAL   B 1 144 ? 29.635 -26.306 -7.381  1.00 11.63 ?  144 VAL   B C    1 
ATOM   6213 O O    . VAL   B 1 144 ? 29.014 -25.600 -8.186  1.00 13.10 ?  144 VAL   B O    1 
ATOM   6214 C CB   . VAL   B 1 144 ? 30.827 -28.327 -8.350  1.00 14.32 ?  144 VAL   B CB   1 
ATOM   6215 C CG1  . VAL   B 1 144 ? 29.573 -28.446 -9.208  1.00 17.03 ?  144 VAL   B CG1  1 
ATOM   6216 C CG2  . VAL   B 1 144 ? 32.096 -28.720 -9.119  1.00 14.43 ?  144 VAL   B CG2  1 
ATOM   6217 H H    . VAL   B 1 144 ? 32.129 -27.770 -6.394  1.00 12.85 ?  144 VAL   B H    1 
ATOM   6218 H HA   . VAL   B 1 144 ? 31.368 -26.357 -8.446  1.00 14.11 ?  144 VAL   B HA   1 
ATOM   6219 H HB   . VAL   B 1 144 ? 30.737 -28.958 -7.619  1.00 17.20 ?  144 VAL   B HB   1 
ATOM   6220 H HG11 . VAL   B 1 144 ? 29.660 -29.227 -9.782  1.00 20.45 ?  144 VAL   B HG11 1 
ATOM   6221 H HG12 . VAL   B 1 144 ? 28.805 -28.550 -8.629  1.00 20.45 ?  144 VAL   B HG12 1 
ATOM   6222 H HG13 . VAL   B 1 144 ? 29.485 -27.650 -9.751  1.00 20.45 ?  144 VAL   B HG13 1 
ATOM   6223 H HG21 . VAL   B 1 144 ? 31.984 -29.615 -9.479  1.00 17.34 ?  144 VAL   B HG21 1 
ATOM   6224 H HG22 . VAL   B 1 144 ? 32.233 -28.089 -9.844  1.00 17.34 ?  144 VAL   B HG22 1 
ATOM   6225 H HG23 . VAL   B 1 144 ? 32.852 -28.700 -8.514  1.00 17.34 ?  144 VAL   B HG23 1 
ATOM   6226 N N    . ASP   B 1 145 ? 29.166 -26.553 -6.160  1.00 11.84 ?  145 ASP   B N    1 
ATOM   6227 C CA   . ASP   B 1 145 ? 27.854 -26.085 -5.735  1.00 12.38 ?  145 ASP   B CA   1 
ATOM   6228 C C    . ASP   B 1 145 ? 27.880 -24.662 -5.188  1.00 11.93 ?  145 ASP   B C    1 
ATOM   6229 O O    . ASP   B 1 145 ? 26.819 -24.124 -4.855  1.00 14.10 ?  145 ASP   B O    1 
ATOM   6230 C CB   . ASP   B 1 145 ? 27.262 -27.008 -4.659  1.00 14.06 ?  145 ASP   B CB   1 
ATOM   6231 C CG   . ASP   B 1 145 ? 26.915 -28.386 -5.171  1.00 15.96 ?  145 ASP   B CG   1 
ATOM   6232 O OD1  . ASP   B 1 145 ? 26.819 -28.581 -6.399  1.00 16.55 ?  145 ASP   B OD1  1 
ATOM   6233 O OD2  . ASP   B 1 145 ? 26.725 -29.275 -4.318  1.00 18.20 -1 145 ASP   B OD2  1 
ATOM   6234 H H    . ASP   B 1 145 ? 29.594 -26.992 -5.557  1.00 14.23 ?  145 ASP   B H    1 
ATOM   6235 H HA   . ASP   B 1 145 ? 27.260 -26.083 -6.500  1.00 14.88 ?  145 ASP   B HA   1 
ATOM   6236 H HB2  . ASP   B 1 145 ? 27.898 -27.120 -3.949  1.00 16.90 ?  145 ASP   B HB2  1 
ATOM   6237 H HB3  . ASP   B 1 145 ? 26.442 -26.604 -4.321  1.00 16.90 ?  145 ASP   B HB3  1 
ATOM   6238 N N    . THR   B 1 146 ? 29.056 -24.046 -5.075  1.00 10.59 ?  146 THR   B N    1 
ATOM   6239 C CA   . THR   B 1 146 ? 29.190 -22.723 -4.467  1.00 10.44 ?  146 THR   B CA   1 
ATOM   6240 C C    . THR   B 1 146 ? 29.824 -21.693 -5.383  1.00 10.14 ?  146 THR   B C    1 
ATOM   6241 O O    . THR   B 1 146 ? 29.371 -20.536 -5.425  1.00 10.52 ?  146 THR   B O    1 
ATOM   6242 C CB   . THR   B 1 146 ? 30.016 -22.825 -3.173  1.00 10.82 ?  146 THR   B CB   1 
ATOM   6243 O OG1  . THR   B 1 146 ? 29.448 -23.819 -2.313  1.00 11.29 ?  146 THR   B OG1  1 
ATOM   6244 C CG2  . THR   B 1 146 ? 30.080 -21.490 -2.446  1.00 10.99 ?  146 THR   B CG2  1 
ATOM   6245 H H    . THR   B 1 146 ? 29.808 -24.380 -5.342  1.00 12.72 ?  146 THR   B H    1 
ATOM   6246 H HA   . THR   B 1 146 ? 28.312 -22.398 -4.235  1.00 12.54 ?  146 THR   B HA   1 
ATOM   6247 H HB   . THR   B 1 146 ? 30.923 -23.079 -3.396  1.00 13.00 ?  146 THR   B HB   1 
ATOM   6248 H HG1  . THR   B 1 146 ? 29.490 -24.579 -2.701  1.00 13.57 ?  146 THR   B HG1  1 
ATOM   6249 H HG21 . THR   B 1 146 ? 30.445 -21.613 -1.557  1.00 13.20 ?  146 THR   B HG21 1 
ATOM   6250 H HG22 . THR   B 1 146 ? 30.645 -20.869 -2.935  1.00 13.20 ?  146 THR   B HG22 1 
ATOM   6251 H HG23 . THR   B 1 146 ? 29.189 -21.110 -2.370  1.00 13.20 ?  146 THR   B HG23 1 
ATOM   6252 N N    . VAL   B 1 147 ? 30.890 -22.066 -6.082  1.00 10.37 ?  147 VAL   B N    1 
ATOM   6253 C CA   . VAL   B 1 147 ? 31.618 -21.124 -6.917  1.00 10.03 ?  147 VAL   B CA   1 
ATOM   6254 C C    . VAL   B 1 147 ? 30.893 -20.992 -8.244  1.00 10.12 ?  147 VAL   B C    1 
ATOM   6255 O O    . VAL   B 1 147 ? 30.535 -21.997 -8.871  1.00 11.00 ?  147 VAL   B O    1 
ATOM   6256 C CB   . VAL   B 1 147 ? 33.072 -21.581 -7.113  1.00 10.06 ?  147 VAL   B CB   1 
ATOM   6257 C CG1  . VAL   B 1 147 ? 33.834 -20.561 -7.935  1.00 10.48 ?  147 VAL   B CG1  1 
ATOM   6258 C CG2  . VAL   B 1 147 ? 33.754 -21.797 -5.765  1.00 10.22 ?  147 VAL   B CG2  1 
ATOM   6259 H H    . VAL   B 1 147 ? 31.218 -22.865 -6.097  1.00 12.47 ?  147 VAL   B H    1 
ATOM   6260 H HA   . VAL   B 1 147 ? 31.638 -20.255 -6.491  1.00 12.05 ?  147 VAL   B HA   1 
ATOM   6261 H HB   . VAL   B 1 147 ? 33.089 -22.424 -7.598  1.00 12.09 ?  147 VAL   B HB   1 
ATOM   6262 H HG11 . VAL   B 1 147 ? 34.782 -20.774 -7.909  1.00 12.60 ?  147 VAL   B HG11 1 
ATOM   6263 H HG12 . VAL   B 1 147 ? 33.517 -20.587 -8.851  1.00 12.60 ?  147 VAL   B HG12 1 
ATOM   6264 H HG13 . VAL   B 1 147 ? 33.686 -19.680 -7.556  1.00 12.60 ?  147 VAL   B HG13 1 
ATOM   6265 H HG21 . VAL   B 1 147 ? 34.697 -22.003 -5.910  1.00 12.28 ?  147 VAL   B HG21 1 
ATOM   6266 H HG22 . VAL   B 1 147 ? 33.677 -20.988 -5.236  1.00 12.28 ?  147 VAL   B HG22 1 
ATOM   6267 H HG23 . VAL   B 1 147 ? 33.328 -22.536 -5.306  1.00 12.28 ?  147 VAL   B HG23 1 
ATOM   6268 N N    . ARG   B 1 148 ? 30.670 -19.745 -8.663  1.00 10.09 ?  148 ARG   B N    1 
ATOM   6269 C CA   . ARG   B 1 148 ? 30.054 -19.426 -9.939  1.00 10.36 ?  148 ARG   B CA   1 
ATOM   6270 C C    . ARG   B 1 148 ? 31.015 -18.760 -10.911 1.00 10.60 ?  148 ARG   B C    1 
ATOM   6271 O O    . ARG   B 1 148 ? 30.735 -18.749 -12.112 1.00 11.76 ?  148 ARG   B O    1 
ATOM   6272 C CB   . ARG   B 1 148 ? 28.818 -18.537 -9.722  1.00 10.69 ?  148 ARG   B CB   1 
ATOM   6273 C CG   . ARG   B 1 148 ? 27.744 -19.226 -8.888  1.00 11.54 ?  148 ARG   B CG   1 
ATOM   6274 C CD   . ARG   B 1 148 ? 26.542 -18.335 -8.586  1.00 12.55 ?  148 ARG   B CD   1 
ATOM   6275 N NE   . ARG   B 1 148 ? 26.932 -17.134 -7.859  1.00 12.21 ?  148 ARG   B NE   1 
ATOM   6276 C CZ   . ARG   B 1 148 ? 27.224 -17.097 -6.565  1.00 11.25 ?  148 ARG   B CZ   1 
ATOM   6277 N NH1  . ARG   B 1 148 ? 27.146 -18.178 -5.806  1.00 11.60 ?  148 ARG   B NH1  1 
ATOM   6278 N NH2  . ARG   B 1 148 ? 27.628 -15.950 -6.023  1.00 11.48 ?  148 ARG   B NH2  1 
ATOM   6279 H H    . ARG   B 1 148 ? 30.885 -19.045 -8.203  1.00 12.13 ?  148 ARG   B H    1 
ATOM   6280 H HA   . ARG   B 1 148 ? 29.751 -20.250 -10.344 1.00 12.45 ?  148 ARG   B HA   1 
ATOM   6281 H HB2  . ARG   B 1 148 ? 29.083 -17.726 -9.259  1.00 12.85 ?  148 ARG   B HB2  1 
ATOM   6282 H HB3  . ARG   B 1 148 ? 28.431 -18.315 -10.584 1.00 12.85 ?  148 ARG   B HB3  1 
ATOM   6283 H HG2  . ARG   B 1 148 ? 27.417 -20.002 -9.371  1.00 13.87 ?  148 ARG   B HG2  1 
ATOM   6284 H HG3  . ARG   B 1 148 ? 28.126 -19.500 -8.041  1.00 13.87 ?  148 ARG   B HG3  1 
ATOM   6285 H HD2  . ARG   B 1 148 ? 26.128 -18.062 -9.418  1.00 15.08 ?  148 ARG   B HD2  1 
ATOM   6286 H HD3  . ARG   B 1 148 ? 25.906 -18.827 -8.041  1.00 15.08 ?  148 ARG   B HD3  1 
ATOM   6287 H HE   . ARG   B 1 148 ? 26.981 -16.398 -8.298  1.00 14.67 ?  148 ARG   B HE   1 
ATOM   6288 H HH11 . ARG   B 1 148 ? 26.882 -18.927 -6.140  1.00 13.94 ?  148 ARG   B HH11 1 
ATOM   6289 H HH12 . ARG   B 1 148 ? 27.336 -18.132 -4.966  1.00 13.94 ?  148 ARG   B HH12 1 
ATOM   6290 H HH21 . ARG   B 1 148 ? 27.693 -15.244 -6.508  1.00 13.79 ?  148 ARG   B HH21 1 
ATOM   6291 H HH22 . ARG   B 1 148 ? 27.825 -15.914 -5.186  1.00 13.79 ?  148 ARG   B HH22 1 
ATOM   6292 N N    . THR   B 1 149 ? 32.123 -18.209 -10.424 1.00 10.38 ?  149 THR   B N    1 
ATOM   6293 C CA   . THR   B 1 149 ? 33.165 -17.651 -11.268 1.00 10.50 ?  149 THR   B CA   1 
ATOM   6294 C C    . THR   B 1 149 ? 34.056 -18.791 -11.763 1.00 9.94  ?  149 THR   B C    1 
ATOM   6295 O O    . THR   B 1 149 ? 33.869 -19.961 -11.415 1.00 10.40 ?  149 THR   B O    1 
ATOM   6296 C CB   . THR   B 1 149 ? 33.933 -16.594 -10.485 1.00 10.60 ?  149 THR   B CB   1 
ATOM   6297 O OG1  . THR   B 1 149 ? 34.388 -17.189 -9.266  1.00 10.56 ?  149 THR   B OG1  1 
ATOM   6298 C CG2  . THR   B 1 149 ? 33.049 -15.382 -10.195 1.00 11.12 ?  149 THR   B CG2  1 
ATOM   6299 H H    . THR   B 1 149 ? 32.285 -18.135 -9.583  1.00 12.48 ?  149 THR   B H    1 
ATOM   6300 H HA   . THR   B 1 149 ? 32.758 -17.221 -12.038 1.00 12.62 ?  149 THR   B HA   1 
ATOM   6301 H HB   . THR   B 1 149 ? 34.699 -16.306 -11.002 1.00 12.74 ?  149 THR   B HB   1 
ATOM   6302 H HG1  . THR   B 1 149 ? 34.805 -16.615 -8.808  1.00 12.70 ?  149 THR   B HG1  1 
ATOM   6303 H HG21 . THR   B 1 149 ? 33.556 -14.713 -9.709  1.00 13.37 ?  149 THR   B HG21 1 
ATOM   6304 H HG22 . THR   B 1 149 ? 32.737 -14.995 -11.030 1.00 13.37 ?  149 THR   B HG22 1 
ATOM   6305 H HG23 . THR   B 1 149 ? 32.284 -15.647 -9.665  1.00 13.37 ?  149 THR   B HG23 1 
ATOM   6306 N N    . ASN   B 1 150 ? 35.021 -18.470 -12.612 1.00 10.31 ?  150 ASN   B N    1 
ATOM   6307 C CA   . ASN   B 1 150 ? 35.783 -19.503 -13.304 1.00 10.69 ?  150 ASN   B CA   1 
ATOM   6308 C C    . ASN   B 1 150 ? 36.946 -19.949 -12.431 1.00 10.29 ?  150 ASN   B C    1 
ATOM   6309 O O    . ASN   B 1 150 ? 37.864 -19.171 -12.163 1.00 11.10 ?  150 ASN   B O    1 
ATOM   6310 C CB   . ASN   B 1 150 ? 36.259 -18.977 -14.650 1.00 12.21 ?  150 ASN   B CB   1 
ATOM   6311 C CG   . ASN   B 1 150 ? 35.113 -18.752 -15.592 1.00 14.81 ?  150 ASN   B CG   1 
ATOM   6312 O OD1  . ASN   B 1 150 ? 34.221 -19.585 -15.687 1.00 15.98 ?  150 ASN   B OD1  1 
ATOM   6313 N ND2  . ASN   B 1 150 ? 35.100 -17.614 -16.263 1.00 16.75 ?  150 ASN   B ND2  1 
ATOM   6314 H H    . ASN   B 1 150 ? 35.260 -17.662 -12.800 1.00 12.40 ?  150 ASN   B H    1 
ATOM   6315 H HA   . ASN   B 1 150 ? 35.206 -20.267 -13.464 1.00 12.85 ?  150 ASN   B HA   1 
ATOM   6316 H HB2  . ASN   B 1 150 ? 36.711 -18.128 -14.518 1.00 14.67 ?  150 ASN   B HB2  1 
ATOM   6317 H HB3  . ASN   B 1 150 ? 36.862 -19.620 -15.048 1.00 14.67 ?  150 ASN   B HB3  1 
ATOM   6318 H HD21 . ASN   B 1 150 ? 34.463 -17.444 -16.815 1.00 20.12 ?  150 ASN   B HD21 1 
ATOM   6319 H HD22 . ASN   B 1 150 ? 35.742 -17.048 -16.161 1.00 20.12 ?  150 ASN   B HD22 1 
ATOM   6320 N N    . VAL   B 1 151 ? 36.913 -21.201 -11.990 1.00 9.92  ?  151 VAL   B N    1 
ATOM   6321 C CA   . VAL   B 1 151 ? 37.935 -21.726 -11.098 1.00 10.01 ?  151 VAL   B CA   1 
ATOM   6322 C C    . VAL   B 1 151 ? 38.645 -22.898 -11.765 1.00 9.76  ?  151 VAL   B C    1 
ATOM   6323 O O    . VAL   B 1 151 ? 38.006 -23.833 -12.272 1.00 10.87 ?  151 VAL   B O    1 
ATOM   6324 C CB   . VAL   B 1 151 ? 37.373 -22.051 -9.698  1.00 11.59 ?  151 VAL   B CB   1 
ATOM   6325 C CG1  . VAL   B 1 151 ? 36.205 -23.036 -9.768  1.00 12.65 ?  151 VAL   B CG1  1 
ATOM   6326 C CG2  . VAL   B 1 151 ? 38.483 -22.538 -8.775  1.00 12.20 ?  151 VAL   B CG2  1 
ATOM   6327 H H    . VAL   B 1 151 ? 36.292 -21.767 -12.186 1.00 11.92 ?  151 VAL   B H    1 
ATOM   6328 H HA   . VAL   B 1 151 ? 38.598 -21.031 -10.970 1.00 12.04 ?  151 VAL   B HA   1 
ATOM   6329 H HB   . VAL   B 1 151 ? 37.029 -21.230 -9.314  1.00 13.93 ?  151 VAL   B HB   1 
ATOM   6330 H HG11 . VAL   B 1 151 ? 35.898 -23.227 -8.867  1.00 15.20 ?  151 VAL   B HG11 1 
ATOM   6331 H HG12 . VAL   B 1 151 ? 35.486 -22.639 -10.284 1.00 15.20 ?  151 VAL   B HG12 1 
ATOM   6332 H HG13 . VAL   B 1 151 ? 36.505 -23.854 -10.195 1.00 15.20 ?  151 VAL   B HG13 1 
ATOM   6333 H HG21 . VAL   B 1 151 ? 38.132 -22.617 -7.873  1.00 14.66 ?  151 VAL   B HG21 1 
ATOM   6334 H HG22 . VAL   B 1 151 ? 38.799 -23.402 -9.081  1.00 14.66 ?  151 VAL   B HG22 1 
ATOM   6335 H HG23 . VAL   B 1 151 ? 39.212 -21.896 -8.787  1.00 14.66 ?  151 VAL   B HG23 1 
ATOM   6336 N N    . TYR   B 1 152 ? 39.977 -22.806 -11.785 1.00 9.40  ?  152 TYR   B N    1 
ATOM   6337 C CA   . TYR   B 1 152 ? 40.884 -23.785 -12.367 1.00 9.83  ?  152 TYR   B CA   1 
ATOM   6338 C C    . TYR   B 1 152 ? 41.604 -24.456 -11.203 1.00 9.06  ?  152 TYR   B C    1 
ATOM   6339 O O    . TYR   B 1 152 ? 42.431 -23.828 -10.536 1.00 9.57  ?  152 TYR   B O    1 
ATOM   6340 C CB   . TYR   B 1 152 ? 41.852 -23.067 -13.312 1.00 10.65 ?  152 TYR   B CB   1 
ATOM   6341 C CG   . TYR   B 1 152 ? 41.169 -22.615 -14.579 1.00 11.09 ?  152 TYR   B CG   1 
ATOM   6342 C CD1  . TYR   B 1 152 ? 40.495 -21.401 -14.646 1.00 11.52 ?  152 TYR   B CD1  1 
ATOM   6343 C CD2  . TYR   B 1 152 ? 41.172 -23.426 -15.704 1.00 12.04 ?  152 TYR   B CD2  1 
ATOM   6344 C CE1  . TYR   B 1 152 ? 39.849 -21.011 -15.806 1.00 12.67 ?  152 TYR   B CE1  1 
ATOM   6345 C CE2  . TYR   B 1 152 ? 40.534 -23.047 -16.863 1.00 12.90 ?  152 TYR   B CE2  1 
ATOM   6346 C CZ   . TYR   B 1 152 ? 39.875 -21.837 -16.913 1.00 13.33 ?  152 TYR   B CZ   1 
ATOM   6347 O OH   . TYR   B 1 152 ? 39.240 -21.463 -18.075 1.00 15.65 ?  152 TYR   B OH   1 
ATOM   6348 H H    . TYR   B 1 152 ? 40.400 -22.143 -11.433 1.00 11.30 ?  152 TYR   B H    1 
ATOM   6349 H HA   . TYR   B 1 152 ? 40.380 -24.454 -12.864 1.00 11.82 ?  152 TYR   B HA   1 
ATOM   6350 H HB2  . TYR   B 1 152 ? 42.205 -22.284 -12.863 1.00 12.80 ?  152 TYR   B HB2  1 
ATOM   6351 H HB3  . TYR   B 1 152 ? 42.572 -23.669 -13.549 1.00 12.80 ?  152 TYR   B HB3  1 
ATOM   6352 H HD1  . TYR   B 1 152 ? 40.473 -20.845 -13.901 1.00 13.84 ?  152 TYR   B HD1  1 
ATOM   6353 H HD2  . TYR   B 1 152 ? 41.612 -24.249 -15.672 1.00 14.47 ?  152 TYR   B HD2  1 
ATOM   6354 H HE1  . TYR   B 1 152 ? 39.409 -20.195 -15.844 1.00 15.22 ?  152 TYR   B HE1  1 
ATOM   6355 H HE2  . TYR   B 1 152 ? 40.552 -23.602 -17.609 1.00 15.50 ?  152 TYR   B HE2  1 
ATOM   6356 H HH   . TYR   B 1 152 ? 38.885 -20.708 -17.970 1.00 18.80 ?  152 TYR   B HH   1 
ATOM   6357 N N    . LEU   B 1 153 ? 41.246 -25.714 -10.931 1.00 9.35  ?  153 LEU   B N    1 
ATOM   6358 C CA   . LEU   B 1 153 ? 41.747 -26.456 -9.784  1.00 9.23  ?  153 LEU   B CA   1 
ATOM   6359 C C    . LEU   B 1 153 ? 42.978 -27.259 -10.171 1.00 9.45  ?  153 LEU   B C    1 
ATOM   6360 O O    . LEU   B 1 153 ? 42.961 -27.986 -11.169 1.00 10.58 ?  153 LEU   B O    1 
ATOM   6361 C CB   . LEU   B 1 153 ? 40.668 -27.412 -9.275  1.00 9.73  ?  153 LEU   B CB   1 
ATOM   6362 C CG   . LEU   B 1 153 ? 39.403 -26.761 -8.715  1.00 10.35 ?  153 LEU   B CG   1 
ATOM   6363 C CD1  . LEU   B 1 153 ? 38.324 -27.815 -8.569  1.00 11.15 ?  153 LEU   B CD1  1 
ATOM   6364 C CD2  . LEU   B 1 153 ? 39.688 -26.097 -7.381  1.00 11.18 ?  153 LEU   B CD2  1 
ATOM   6365 H H    . LEU   B 1 153 ? 40.678 -26.163 -11.406 1.00 11.23 ?  153 LEU   B H    1 
ATOM   6366 H HA   . LEU   B 1 153 ? 41.971 -25.838 -9.072  1.00 11.10 ?  153 LEU   B HA   1 
ATOM   6367 H HB2  . LEU   B 1 153 ? 40.396 -27.987 -10.012 1.00 11.70 ?  153 LEU   B HB2  1 
ATOM   6368 H HB3  . LEU   B 1 153 ? 41.049 -27.957 -8.569  1.00 11.70 ?  153 LEU   B HB3  1 
ATOM   6369 H HG   . LEU   B 1 153 ? 39.084 -26.082 -9.335  1.00 12.44 ?  153 LEU   B HG   1 
ATOM   6370 H HD11 . LEU   B 1 153 ? 37.519 -27.397 -8.225  1.00 13.39 ?  153 LEU   B HD11 1 
ATOM   6371 H HD12 . LEU   B 1 153 ? 38.149 -28.207 -9.438  1.00 13.39 ?  153 LEU   B HD12 1 
ATOM   6372 H HD13 . LEU   B 1 153 ? 38.635 -28.495 -7.953  1.00 13.39 ?  153 LEU   B HD13 1 
ATOM   6373 H HD21 . LEU   B 1 153 ? 38.866 -25.727 -7.025  1.00 13.44 ?  153 LEU   B HD21 1 
ATOM   6374 H HD22 . LEU   B 1 153 ? 40.046 -26.760 -6.769  1.00 13.44 ?  153 LEU   B HD22 1 
ATOM   6375 H HD23 . LEU   B 1 153 ? 40.339 -25.388 -7.513  1.00 13.44 ?  153 LEU   B HD23 1 
ATOM   6376 N N    . ALA   B 1 154 ? 44.028 -27.150 -9.363  1.00 9.79  ?  154 ALA   B N    1 
ATOM   6377 C CA   . ALA   B 1 154 ? 45.254 -27.915 -9.541  1.00 10.74 ?  154 ALA   B CA   1 
ATOM   6378 C C    . ALA   B 1 154 ? 45.317 -28.992 -8.465  1.00 11.08 ?  154 ALA   B C    1 
ATOM   6379 O O    . ALA   B 1 154 ? 45.233 -28.689 -7.268  1.00 12.41 ?  154 ALA   B O    1 
ATOM   6380 C CB   . ALA   B 1 154 ? 46.474 -26.998 -9.469  1.00 11.79 ?  154 ALA   B CB   1 
ATOM   6381 H H    . ALA   B 1 154 ? 44.046 -26.621 -8.679  1.00 11.77 ?  154 ALA   B H    1 
ATOM   6382 H HA   . ALA   B 1 154 ? 45.247 -28.342 -10.406 1.00 12.90 ?  154 ALA   B HA   1 
ATOM   6383 H HB1  . ALA   B 1 154 ? 47.279 -27.529 -9.588  1.00 14.16 ?  154 ALA   B HB1  1 
ATOM   6384 H HB2  . ALA   B 1 154 ? 46.415 -26.330 -10.170 1.00 14.16 ?  154 ALA   B HB2  1 
ATOM   6385 H HB3  . ALA   B 1 154 ? 46.497 -26.560 -8.600  1.00 14.16 ?  154 ALA   B HB3  1 
ATOM   6386 N N    . VAL   B 1 155 ? 45.453 -30.242 -8.894  1.00 10.47 ?  155 VAL   B N    1 
ATOM   6387 C CA   . VAL   B 1 155 ? 45.561 -31.384 -7.996  1.00 10.85 ?  155 VAL   B CA   1 
ATOM   6388 C C    . VAL   B 1 155 ? 46.903 -32.056 -8.268  1.00 10.51 ?  155 VAL   B C    1 
ATOM   6389 O O    . VAL   B 1 155 ? 47.145 -32.550 -9.376  1.00 12.23 ?  155 VAL   B O    1 
ATOM   6390 C CB   . VAL   B 1 155 ? 44.400 -32.374 -8.197  1.00 12.27 ?  155 VAL   B CB   1 
ATOM   6391 C CG1  . VAL   B 1 155 ? 44.569 -33.578 -7.291  1.00 12.39 ?  155 VAL   B CG1  1 
ATOM   6392 C CG2  . VAL   B 1 155 ? 43.064 -31.688 -7.939  1.00 13.35 ?  155 VAL   B CG2  1 
ATOM   6393 H H    . VAL   B 1 155 ? 45.488 -30.457 -9.728  1.00 12.58 ?  155 VAL   B H    1 
ATOM   6394 H HA   . VAL   B 1 155 ? 45.551 -31.078 -7.077  1.00 13.04 ?  155 VAL   B HA   1 
ATOM   6395 H HB   . VAL   B 1 155 ? 44.407 -32.683 -9.116  1.00 14.74 ?  155 VAL   B HB   1 
ATOM   6396 H HG11 . VAL   B 1 155 ? 43.743 -34.084 -7.277  1.00 14.88 ?  155 VAL   B HG11 1 
ATOM   6397 H HG12 . VAL   B 1 155 ? 45.289 -34.139 -7.633  1.00 14.88 ?  155 VAL   B HG12 1 
ATOM   6398 H HG13 . VAL   B 1 155 ? 44.788 -33.277 -6.395  1.00 14.88 ?  155 VAL   B HG13 1 
ATOM   6399 H HG21 . VAL   B 1 155 ? 42.353 -32.341 -8.033  1.00 16.04 ?  155 VAL   B HG21 1 
ATOM   6400 H HG22 . VAL   B 1 155 ? 43.064 -31.327 -7.038  1.00 16.04 ?  155 VAL   B HG22 1 
ATOM   6401 H HG23 . VAL   B 1 155 ? 42.945 -30.973 -8.582  1.00 16.04 ?  155 VAL   B HG23 1 
ATOM   6402 N N    . PHE   B 1 156 ? 47.768 -32.088 -7.251  1.00 10.94 ?  156 PHE   B N    1 
ATOM   6403 C CA   . PHE   B 1 156 ? 49.146 -32.540 -7.444  1.00 12.11 ?  156 PHE   B CA   1 
ATOM   6404 C C    . PHE   B 1 156 ? 49.245 -34.040 -7.725  1.00 12.99 ?  156 PHE   B C    1 
ATOM   6405 O O    . PHE   B 1 156 ? 49.981 -34.465 -8.625  1.00 14.80 ?  156 PHE   B O    1 
ATOM   6406 C CB   . PHE   B 1 156 ? 49.965 -32.164 -6.211  1.00 12.63 ?  156 PHE   B CB   1 
ATOM   6407 C CG   . PHE   B 1 156 ? 51.386 -32.631 -6.260  1.00 13.28 ?  156 PHE   B CG   1 
ATOM   6408 C CD1  . PHE   B 1 156 ? 52.276 -32.083 -7.164  1.00 15.01 ?  156 PHE   B CD1  1 
ATOM   6409 C CD2  . PHE   B 1 156 ? 51.838 -33.600 -5.385  1.00 13.73 ?  156 PHE   B CD2  1 
ATOM   6410 C CE1  . PHE   B 1 156 ? 53.592 -32.497 -7.208  1.00 16.10 ?  156 PHE   B CE1  1 
ATOM   6411 C CE2  . PHE   B 1 156 ? 53.160 -34.021 -5.423  1.00 15.05 ?  156 PHE   B CE2  1 
ATOM   6412 C CZ   . PHE   B 1 156 ? 54.029 -33.469 -6.339  1.00 15.98 ?  156 PHE   B CZ   1 
ATOM   6413 H H    . PHE   B 1 156 ? 47.579 -31.860 -6.443  1.00 13.14 ?  156 PHE   B H    1 
ATOM   6414 H HA   . PHE   B 1 156 ? 49.522 -32.068 -8.202  1.00 14.55 ?  156 PHE   B HA   1 
ATOM   6415 H HB2  . PHE   B 1 156 ? 49.975 -31.197 -6.127  1.00 15.17 ?  156 PHE   B HB2  1 
ATOM   6416 H HB3  . PHE   B 1 156 ? 49.551 -32.556 -5.427  1.00 15.17 ?  156 PHE   B HB3  1 
ATOM   6417 H HD1  . PHE   B 1 156 ? 51.985 -31.423 -7.753  1.00 18.03 ?  156 PHE   B HD1  1 
ATOM   6418 H HD2  . PHE   B 1 156 ? 51.248 -33.976 -4.768  1.00 16.49 ?  156 PHE   B HD2  1 
ATOM   6419 H HE1  . PHE   B 1 156 ? 54.179 -32.123 -7.826  1.00 19.34 ?  156 PHE   B HE1  1 
ATOM   6420 H HE2  . PHE   B 1 156 ? 53.449 -34.683 -4.835  1.00 18.09 ?  156 PHE   B HE2  1 
ATOM   6421 H HZ   . PHE   B 1 156 ? 54.914 -33.755 -6.367  1.00 19.20 ?  156 PHE   B HZ   1 
ATOM   6422 N N    . ASP   B 1 157 ? 48.566 -34.860 -6.937  1.00 13.11 ?  157 ASP   B N    1 
ATOM   6423 C CA   . ASP   B 1 157 ? 48.725 -36.307 -7.028  1.00 14.25 ?  157 ASP   B CA   1 
ATOM   6424 C C    . ASP   B 1 157 ? 47.813 -36.859 -8.121  1.00 14.22 ?  157 ASP   B C    1 
ATOM   6425 O O    . ASP   B 1 157 ? 46.587 -36.749 -8.022  1.00 13.81 ?  157 ASP   B O    1 
ATOM   6426 C CB   . ASP   B 1 157 ? 48.363 -36.917 -5.680  1.00 16.02 ?  157 ASP   B CB   1 
ATOM   6427 C CG   . ASP   B 1 157 ? 48.499 -38.432 -5.656  1.00 17.78 ?  157 ASP   B CG   1 
ATOM   6428 O OD1  . ASP   B 1 157 ? 48.820 -39.050 -6.700  1.00 18.23 ?  157 ASP   B OD1  1 
ATOM   6429 O OD2  . ASP   B 1 157 ? 48.295 -39.006 -4.568  1.00 19.83 -1 157 ASP   B OD2  1 
ATOM   6430 H H    . ASP   B 1 157 ? 48.010 -34.603 -6.340  1.00 15.75 ?  157 ASP   B H    1 
ATOM   6431 H HA   . ASP   B 1 157 ? 49.646 -36.530 -7.242  1.00 17.12 ?  157 ASP   B HA   1 
ATOM   6432 H HB2  . ASP   B 1 157 ? 48.947 -36.544 -5.005  1.00 19.25 ?  157 ASP   B HB2  1 
ATOM   6433 H HB3  . ASP   B 1 157 ? 47.439 -36.691 -5.477  1.00 19.25 ?  157 ASP   B HB3  1 
ATOM   6434 N N    . LYS   B 1 158 ? 48.408 -37.476 -9.151  1.00 15.27 ?  158 LYS   B N    1 
ATOM   6435 C CA   . LYS   B 1 158 ? 47.630 -38.094 -10.228 1.00 16.43 ?  158 LYS   B CA   1 
ATOM   6436 C C    . LYS   B 1 158 ? 46.572 -39.061 -9.696  1.00 15.96 ?  158 LYS   B C    1 
ATOM   6437 O O    . LYS   B 1 158 ? 45.467 -39.154 -10.247 1.00 16.16 ?  158 LYS   B O    1 
ATOM   6438 C CB   . LYS   B 1 158 ? 48.580 -38.804 -11.202 1.00 18.15 ?  158 LYS   B CB   1 
ATOM   6439 C CG   . LYS   B 1 158 ? 47.902 -39.699 -12.228 1.00 19.99 ?  158 LYS   B CG   1 
ATOM   6440 C CD   . LYS   B 1 158 ? 47.057 -38.918 -13.207 1.00 22.19 ?  158 LYS   B CD   1 
ATOM   6441 C CE   . LYS   B 1 158 ? 46.464 -39.831 -14.264 1.00 23.87 ?  158 LYS   B CE   1 
ATOM   6442 N NZ   . LYS   B 1 158 ? 45.430 -39.131 -15.079 1.00 24.03 ?  158 LYS   B NZ   1 
ATOM   6443 H H    . LYS   B 1 158 ? 49.263 -37.544 -9.249  1.00 18.34 ?  158 LYS   B H    1 
ATOM   6444 H HA   . LYS   B 1 158 ? 47.175 -37.398 -10.726 1.00 19.74 ?  158 LYS   B HA   1 
ATOM   6445 H HB2  . LYS   B 1 158 ? 49.082 -38.130 -11.697 1.00 21.80 ?  158 LYS   B HB2  1 
ATOM   6446 H HB3  . LYS   B 1 158 ? 49.197 -39.353 -10.695 1.00 21.80 ?  158 LYS   B HB3  1 
ATOM   6447 H HG2  . LYS   B 1 158 ? 48.586 -40.167 -12.735 1.00 24.01 ?  158 LYS   B HG2  1 
ATOM   6448 H HG3  . LYS   B 1 158 ? 47.334 -40.349 -11.781 1.00 24.01 ?  158 LYS   B HG3  1 
ATOM   6449 H HD2  . LYS   B 1 158 ? 46.331 -38.485 -12.734 1.00 26.65 ?  158 LYS   B HD2  1 
ATOM   6450 H HD3  . LYS   B 1 158 ? 47.611 -38.258 -13.654 1.00 26.65 ?  158 LYS   B HD3  1 
ATOM   6451 H HE2  . LYS   B 1 158 ? 47.164 -40.134 -14.861 1.00 28.67 ?  158 LYS   B HE2  1 
ATOM   6452 H HE3  . LYS   B 1 158 ? 46.041 -40.592 -13.832 1.00 28.67 ?  158 LYS   B HE3  1 
ATOM   6453 H HZ1  . LYS   B 1 158 ? 45.095 -39.684 -15.690 1.00 28.85 ?  158 LYS   B HZ1  1 
ATOM   6454 H HZ2  . LYS   B 1 158 ? 44.770 -38.845 -14.554 1.00 28.85 ?  158 LYS   B HZ2  1 
ATOM   6455 H HZ3  . LYS   B 1 158 ? 45.794 -38.431 -15.492 1.00 28.85 ?  158 LYS   B HZ3  1 
ATOM   6456 N N    . ASN   B 1 159 ? 46.900 -39.822 -8.650  1.00 16.37 ?  159 ASN   B N    1 
ATOM   6457 C CA   . ASN   B 1 159 ? 45.938 -40.796 -8.142  1.00 17.32 ?  159 ASN   B CA   1 
ATOM   6458 C C    . ASN   B 1 159 ? 44.738 -40.121 -7.477  1.00 16.09 ?  159 ASN   B C    1 
ATOM   6459 O O    . ASN   B 1 159 ? 43.609 -40.623 -7.580  1.00 16.69 ?  159 ASN   B O    1 
ATOM   6460 C CB   . ASN   B 1 159 ? 46.640 -41.765 -7.202  1.00 19.17 ?  159 ASN   B CB   1 
ATOM   6461 C CG   . ASN   B 1 159 ? 47.672 -42.609 -7.917  1.00 21.24 ?  159 ASN   B CG   1 
ATOM   6462 O OD1  . ASN   B 1 159 ? 47.416 -43.119 -9.014  1.00 22.03 ?  159 ASN   B OD1  1 
ATOM   6463 N ND2  . ASN   B 1 159 ? 48.843 -42.770 -7.304  1.00 21.96 ?  159 ASN   B ND2  1 
ATOM   6464 H H    . ASN   B 1 159 ? 47.650 -39.782 -8.229  1.00 19.66 ?  159 ASN   B H    1 
ATOM   6465 H HA   . ASN   B 1 159 ? 45.609 -41.308 -8.897  1.00 20.80 ?  159 ASN   B HA   1 
ATOM   6466 H HB2  . ASN   B 1 159 ? 47.095 -41.272 -6.507  1.00 23.03 ?  159 ASN   B HB2  1 
ATOM   6467 H HB3  . ASN   B 1 159 ? 45.987 -42.369 -6.823  1.00 23.03 ?  159 ASN   B HB3  1 
ATOM   6468 H HD21 . ASN   B 1 159 ? 49.469 -43.242 -7.672  1.00 26.38 ?  159 ASN   B HD21 1 
ATOM   6469 H HD22 . ASN   B 1 159 ? 48.982 -42.414 -6.534  1.00 26.38 ?  159 ASN   B HD22 1 
ATOM   6470 N N    . LEU   B 1 160 ? 44.947 -38.982 -6.806  1.00 15.09 ?  160 LEU   B N    1 
ATOM   6471 C CA   . LEU   B 1 160 ? 43.811 -38.253 -6.258  1.00 14.02 ?  160 LEU   B CA   1 
ATOM   6472 C C    . LEU   B 1 160 ? 43.019 -37.590 -7.372  1.00 13.29 ?  160 LEU   B C    1 
ATOM   6473 O O    . LEU   B 1 160 ? 41.782 -37.593 -7.355  1.00 12.85 ?  160 LEU   B O    1 
ATOM   6474 C CB   . LEU   B 1 160 ? 44.275 -37.226 -5.227  1.00 13.93 ?  160 LEU   B CB   1 
ATOM   6475 C CG   . LEU   B 1 160 ? 43.149 -36.332 -4.691  1.00 14.09 ?  160 LEU   B CG   1 
ATOM   6476 C CD1  . LEU   B 1 160 ? 42.024 -37.168 -4.091  1.00 14.54 ?  160 LEU   B CD1  1 
ATOM   6477 C CD2  . LEU   B 1 160 ? 43.688 -35.352 -3.667  1.00 14.32 ?  160 LEU   B CD2  1 
ATOM   6478 H H    . LEU   B 1 160 ? 45.721 -38.622 -6.665  1.00 18.13 ?  160 LEU   B H    1 
ATOM   6479 H HA   . LEU   B 1 160 ? 43.231 -38.885 -5.814  1.00 16.84 ?  160 LEU   B HA   1 
ATOM   6480 H HB2  . LEU   B 1 160 ? 44.671 -37.699 -4.474  1.00 16.74 ?  160 LEU   B HB2  1 
ATOM   6481 H HB3  . LEU   B 1 160 ? 44.948 -36.653 -5.636  1.00 16.74 ?  160 LEU   B HB3  1 
ATOM   6482 H HG   . LEU   B 1 160 ? 42.782 -35.820 -5.425  1.00 16.93 ?  160 LEU   B HG   1 
ATOM   6483 H HD11 . LEU   B 1 160 ? 41.396 -36.577 -3.654  1.00 17.47 ?  160 LEU   B HD11 1 
ATOM   6484 H HD12 . LEU   B 1 160 ? 41.579 -37.661 -4.799  1.00 17.47 ?  160 LEU   B HD12 1 
ATOM   6485 H HD13 . LEU   B 1 160 ? 42.402 -37.789 -3.444  1.00 17.47 ?  160 LEU   B HD13 1 
ATOM   6486 H HD21 . LEU   B 1 160 ? 42.960 -34.787 -3.365  1.00 17.21 ?  160 LEU   B HD21 1 
ATOM   6487 H HD22 . LEU   B 1 160 ? 44.054 -35.847 -2.918  1.00 17.21 ?  160 LEU   B HD22 1 
ATOM   6488 H HD23 . LEU   B 1 160 ? 44.379 -34.812 -4.079  1.00 17.21 ?  160 LEU   B HD23 1 
ATOM   6489 N N    . TYR   B 1 161 ? 43.720 -37.019 -8.352  1.00 13.57 ?  161 TYR   B N    1 
ATOM   6490 C CA   . TYR   B 1 161 ? 43.053 -36.456 -9.517  1.00 13.49 ?  161 TYR   B CA   1 
ATOM   6491 C C    . TYR   B 1 161 ? 42.117 -37.483 -10.147 1.00 13.06 ?  161 TYR   B C    1 
ATOM   6492 O O    . TYR   B 1 161 ? 40.949 -37.190 -10.425 1.00 12.98 ?  161 TYR   B O    1 
ATOM   6493 C CB   . TYR   B 1 161 ? 44.100 -35.970 -10.526 1.00 14.21 ?  161 TYR   B CB   1 
ATOM   6494 C CG   . TYR   B 1 161 ? 43.530 -35.509 -11.842 1.00 14.61 ?  161 TYR   B CG   1 
ATOM   6495 C CD1  . TYR   B 1 161 ? 43.130 -34.191 -12.017 1.00 14.48 ?  161 TYR   B CD1  1 
ATOM   6496 C CD2  . TYR   B 1 161 ? 43.374 -36.388 -12.908 1.00 15.38 ?  161 TYR   B CD2  1 
ATOM   6497 C CE1  . TYR   B 1 161 ? 42.602 -33.762 -13.206 1.00 15.75 ?  161 TYR   B CE1  1 
ATOM   6498 C CE2  . TYR   B 1 161 ? 42.842 -35.965 -14.104 1.00 16.82 ?  161 TYR   B CE2  1 
ATOM   6499 C CZ   . TYR   B 1 161 ? 42.457 -34.650 -14.248 1.00 16.65 ?  161 TYR   B CZ   1 
ATOM   6500 O OH   . TYR   B 1 161 ? 41.926 -34.212 -15.434 1.00 18.34 ?  161 TYR   B OH   1 
ATOM   6501 H H    . TYR   B 1 161 ? 44.577 -36.955 -8.370  1.00 16.30 ?  161 TYR   B H    1 
ATOM   6502 H HA   . TYR   B 1 161 ? 42.524 -35.692 -9.246  1.00 16.20 ?  161 TYR   B HA   1 
ATOM   6503 H HB2  . TYR   B 1 161 ? 44.585 -35.219 -10.138 1.00 17.07 ?  161 TYR   B HB2  1 
ATOM   6504 H HB3  . TYR   B 1 161 ? 44.721 -36.692 -10.712 1.00 17.07 ?  161 TYR   B HB3  1 
ATOM   6505 H HD1  . TYR   B 1 161 ? 43.227 -33.582 -11.318 1.00 17.39 ?  161 TYR   B HD1  1 
ATOM   6506 H HD2  . TYR   B 1 161 ? 43.629 -37.276 -12.814 1.00 18.47 ?  161 TYR   B HD2  1 
ATOM   6507 H HE1  . TYR   B 1 161 ? 42.343 -32.870 -13.305 1.00 18.92 ?  161 TYR   B HE1  1 
ATOM   6508 H HE2  . TYR   B 1 161 ? 42.740 -36.561 -14.810 1.00 20.20 ?  161 TYR   B HE2  1 
ATOM   6509 H HH   . TYR   B 1 161 ? 41.889 -34.847 -15.984 1.00 22.02 ?  161 TYR   B HH   1 
ATOM   6510 N N    . ASP   B 1 162 ? 42.616 -38.704 -10.364 1.00 13.82 ?  162 ASP   B N    1 
ATOM   6511 C CA   . ASP   B 1 162 ? 41.795 -39.744 -10.981 1.00 14.46 ?  162 ASP   B CA   1 
ATOM   6512 C C    . ASP   B 1 162 ? 40.580 -40.079 -10.123 1.00 13.85 ?  162 ASP   B C    1 
ATOM   6513 O O    . ASP   B 1 162 ? 39.482 -40.301 -10.649 1.00 14.17 ?  162 ASP   B O    1 
ATOM   6514 C CB   . ASP   B 1 162 ? 42.629 -41.005 -11.225 1.00 16.17 ?  162 ASP   B CB   1 
ATOM   6515 C CG   . ASP   B 1 162 ? 43.630 -40.848 -12.355 1.00 17.53 ?  162 ASP   B CG   1 
ATOM   6516 O OD1  . ASP   B 1 162 ? 43.500 -39.906 -13.162 1.00 17.76 ?  162 ASP   B OD1  1 
ATOM   6517 O OD2  . ASP   B 1 162 ? 44.544 -41.693 -12.447 1.00 19.09 -1 162 ASP   B OD2  1 
ATOM   6518 H H    . ASP   B 1 162 ? 43.416 -38.950 -10.166 1.00 16.60 ?  162 ASP   B H    1 
ATOM   6519 H HA   . ASP   B 1 162 ? 41.475 -39.425 -11.836 1.00 17.38 ?  162 ASP   B HA   1 
ATOM   6520 H HB2  . ASP   B 1 162 ? 43.123 -41.218 -10.419 1.00 19.42 ?  162 ASP   B HB2  1 
ATOM   6521 H HB3  . ASP   B 1 162 ? 42.036 -41.733 -11.457 1.00 19.42 ?  162 ASP   B HB3  1 
ATOM   6522 N N    . LYS   B 1 163 ? 40.757 -40.142 -8.802  1.00 13.29 ?  163 LYS   B N    1 
ATOM   6523 C CA   . LYS   B 1 163 ? 39.631 -40.421 -7.922  1.00 14.12 ?  163 LYS   B CA   1 
ATOM   6524 C C    . LYS   B 1 163 ? 38.587 -39.316 -7.998  1.00 13.07 ?  163 LYS   B C    1 
ATOM   6525 O O    . LYS   B 1 163 ? 37.381 -39.592 -8.016  1.00 14.05 ?  163 LYS   B O    1 
ATOM   6526 C CB   . LYS   B 1 163 ? 40.107 -40.591 -6.484  1.00 17.82 ?  163 LYS   B CB   1 
ATOM   6527 C CG   . LYS   B 1 163 ? 39.013 -41.098 -5.568  1.00 24.54 ?  163 LYS   B CG   1 
ATOM   6528 C CD   . LYS   B 1 163 ? 39.474 -41.291 -4.139  1.00 31.08 ?  163 LYS   B CD   1 
ATOM   6529 C CE   . LYS   B 1 163 ? 38.392 -42.000 -3.335  1.00 35.75 ?  163 LYS   B CE   1 
ATOM   6530 N NZ   . LYS   B 1 163 ? 38.387 -41.599 -1.902  1.00 38.70 ?  163 LYS   B NZ   1 
ATOM   6531 H H    . LYS   B 1 163 ? 41.507 -40.024 -8.398  1.00 15.97 ?  163 LYS   B H    1 
ATOM   6532 H HA   . LYS   B 1 163 ? 39.210 -41.250 -8.201  1.00 16.96 ?  163 LYS   B HA   1 
ATOM   6533 H HB2  . LYS   B 1 163 ? 40.835 -41.232 -6.467  1.00 21.40 ?  163 LYS   B HB2  1 
ATOM   6534 H HB3  . LYS   B 1 163 ? 40.409 -39.734 -6.147  1.00 21.40 ?  163 LYS   B HB3  1 
ATOM   6535 H HG2  . LYS   B 1 163 ? 38.284 -40.459 -5.561  1.00 29.47 ?  163 LYS   B HG2  1 
ATOM   6536 H HG3  . LYS   B 1 163 ? 38.698 -41.955 -5.899  1.00 29.47 ?  163 LYS   B HG3  1 
ATOM   6537 H HD2  . LYS   B 1 163 ? 40.276 -41.839 -4.127  1.00 37.31 ?  163 LYS   B HD2  1 
ATOM   6538 H HD3  . LYS   B 1 163 ? 39.645 -40.428 -3.733  1.00 37.31 ?  163 LYS   B HD3  1 
ATOM   6539 H HE2  . LYS   B 1 163 ? 37.524 -41.788 -3.713  1.00 42.92 ?  163 LYS   B HE2  1 
ATOM   6540 H HE3  . LYS   B 1 163 ? 38.544 -42.958 -3.377  1.00 42.92 ?  163 LYS   B HE3  1 
ATOM   6541 H HZ1  . LYS   B 1 163 ? 37.742 -42.032 -1.468  1.00 46.45 ?  163 LYS   B HZ1  1 
ATOM   6542 H HZ2  . LYS   B 1 163 ? 39.170 -41.795 -1.530  1.00 46.45 ?  163 LYS   B HZ2  1 
ATOM   6543 H HZ3  . LYS   B 1 163 ? 38.243 -40.723 -1.833  1.00 46.45 ?  163 LYS   B HZ3  1 
ATOM   6544 N N    . LEU   B 1 164 ? 39.036 -38.063 -8.049  1.00 12.00 ?  164 LEU   B N    1 
ATOM   6545 C CA   . LEU   B 1 164 ? 38.124 -36.926 -8.107  1.00 11.56 ?  164 LEU   B CA   1 
ATOM   6546 C C    . LEU   B 1 164 ? 37.349 -36.904 -9.418  1.00 11.72 ?  164 LEU   B C    1 
ATOM   6547 O O    . LEU   B 1 164 ? 36.126 -36.710 -9.425  1.00 12.98 ?  164 LEU   B O    1 
ATOM   6548 C CB   . LEU   B 1 164 ? 38.920 -35.633 -7.939  1.00 11.28 ?  164 LEU   B CB   1 
ATOM   6549 C CG   . LEU   B 1 164 ? 39.442 -35.350 -6.533  1.00 12.17 ?  164 LEU   B CG   1 
ATOM   6550 C CD1  . LEU   B 1 164 ? 40.537 -34.286 -6.590  1.00 12.37 ?  164 LEU   B CD1  1 
ATOM   6551 C CD2  . LEU   B 1 164 ? 38.327 -34.911 -5.606  1.00 14.08 ?  164 LEU   B CD2  1 
ATOM   6552 H H    . LEU   B 1 164 ? 39.870 -37.846 -8.057  1.00 14.42 ?  164 LEU   B H    1 
ATOM   6553 H HA   . LEU   B 1 164 ? 37.491 -36.987 -7.384  1.00 13.89 ?  164 LEU   B HA   1 
ATOM   6554 H HB2  . LEU   B 1 164 ? 39.690 -35.666 -8.536  1.00 13.56 ?  164 LEU   B HB2  1 
ATOM   6555 H HB3  . LEU   B 1 164 ? 38.355 -34.888 -8.194  1.00 13.56 ?  164 LEU   B HB3  1 
ATOM   6556 H HG   . LEU   B 1 164 ? 39.842 -36.155 -6.176  1.00 14.62 ?  164 LEU   B HG   1 
ATOM   6557 H HD11 . LEU   B 1 164 ? 40.860 -34.107 -5.690  1.00 14.86 ?  164 LEU   B HD11 1 
ATOM   6558 H HD12 . LEU   B 1 164 ? 41.275 -34.609 -7.139  1.00 14.86 ?  164 LEU   B HD12 1 
ATOM   6559 H HD13 . LEU   B 1 164 ? 40.178 -33.471 -6.977  1.00 14.86 ?  164 LEU   B HD13 1 
ATOM   6560 H HD21 . LEU   B 1 164 ? 38.703 -34.696 -4.738  1.00 16.92 ?  164 LEU   B HD21 1 
ATOM   6561 H HD22 . LEU   B 1 164 ? 37.890 -34.131 -5.979  1.00 16.92 ?  164 LEU   B HD22 1 
ATOM   6562 H HD23 . LEU   B 1 164 ? 37.692 -35.639 -5.519  1.00 16.92 ?  164 LEU   B HD23 1 
ATOM   6563 N N    . VAL   B 1 165 ? 38.047 -37.078 -10.542 1.00 12.97 ?  165 VAL   B N    1 
ATOM   6564 C CA   . VAL   B 1 165 ? 37.395 -37.023 -11.846 1.00 13.97 ?  165 VAL   B CA   1 
ATOM   6565 C C    . VAL   B 1 165 ? 36.484 -38.228 -12.034 1.00 15.34 ?  165 VAL   B C    1 
ATOM   6566 O O    . VAL   B 1 165 ? 35.330 -38.099 -12.457 1.00 16.17 ?  165 VAL   B O    1 
ATOM   6567 C CB   . VAL   B 1 165 ? 38.442 -36.924 -12.971 1.00 15.09 ?  165 VAL   B CB   1 
ATOM   6568 C CG1  . VAL   B 1 165 ? 37.778 -37.026 -14.329 1.00 16.20 ?  165 VAL   B CG1  1 
ATOM   6569 C CG2  . VAL   B 1 165 ? 39.228 -35.633 -12.856 1.00 15.13 ?  165 VAL   B CG2  1 
ATOM   6570 H H    . VAL   B 1 165 ? 38.895 -37.220 -10.579 1.00 15.59 ?  165 VAL   B H    1 
ATOM   6571 H HA   . VAL   B 1 165 ? 36.842 -36.228 -11.889 1.00 16.79 ?  165 VAL   B HA   1 
ATOM   6572 H HB   . VAL   B 1 165 ? 39.068 -37.659 -12.887 1.00 18.12 ?  165 VAL   B HB   1 
ATOM   6573 H HG11 . VAL   B 1 165 ? 38.401 -36.732 -15.008 1.00 19.45 ?  165 VAL   B HG11 1 
ATOM   6574 H HG12 . VAL   B 1 165 ? 37.536 -37.955 -14.490 1.00 19.45 ?  165 VAL   B HG12 1 
ATOM   6575 H HG13 . VAL   B 1 165 ? 36.985 -36.473 -14.337 1.00 19.45 ?  165 VAL   B HG13 1 
ATOM   6576 H HG21 . VAL   B 1 165 ? 39.857 -35.578 -13.594 1.00 18.17 ?  165 VAL   B HG21 1 
ATOM   6577 H HG22 . VAL   B 1 165 ? 38.612 -34.883 -12.895 1.00 18.17 ?  165 VAL   B HG22 1 
ATOM   6578 H HG23 . VAL   B 1 165 ? 39.705 -35.625 -12.013 1.00 18.17 ?  165 VAL   B HG23 1 
ATOM   6579 N N    . SER   B 1 166 ? 36.993 -39.421 -11.717 1.00 15.86 ?  166 SER   B N    1 
ATOM   6580 C CA   . SER   B 1 166 ? 36.233 -40.632 -11.995 1.00 16.94 ?  166 SER   B CA   1 
ATOM   6581 C C    . SER   B 1 166 ? 34.967 -40.713 -11.155 1.00 16.94 ?  166 SER   B C    1 
ATOM   6582 O O    . SER   B 1 166 ? 33.995 -41.327 -11.593 1.00 18.55 ?  166 SER   B O    1 
ATOM   6583 C CB   . SER   B 1 166 ? 37.096 -41.884 -11.812 1.00 18.00 ?  166 SER   B CB   1 
ATOM   6584 O OG   . SER   B 1 166 ? 37.460 -42.087 -10.459 1.00 18.01 ?  166 SER   B OG   1 
ATOM   6585 H H    . SER   B 1 166 ? 37.767 -39.551 -11.359 1.00 19.06 ?  166 SER   B H    1 
ATOM   6586 H HA   . SER   B 1 166 ? 35.963 -40.610 -12.925 1.00 20.35 ?  166 SER   B HA   1 
ATOM   6587 H HB2  . SER   B 1 166 ? 36.591 -42.656 -12.120 1.00 21.62 ?  166 SER   B HB2  1 
ATOM   6588 H HB3  . SER   B 1 166 ? 37.902 -41.790 -12.346 1.00 21.62 ?  166 SER   B HB3  1 
ATOM   6589 H HG   . SER   B 1 166 ? 37.907 -41.435 -10.185 1.00 21.64 ?  166 SER   B HG   1 
ATOM   6590 N N    . SER   B 1 167 ? 34.946 -40.112 -9.965  1.00 15.72 ?  167 SER   B N    1 
ATOM   6591 C CA   . SER   B 1 167 ? 33.782 -40.168 -9.086  1.00 15.28 ?  167 SER   B CA   1 
ATOM   6592 C C    . SER   B 1 167 ? 32.865 -38.952 -9.193  1.00 15.09 ?  167 SER   B C    1 
ATOM   6593 O O    . SER   B 1 167 ? 31.787 -38.947 -8.585  1.00 15.34 ?  167 SER   B O    1 
ATOM   6594 C CB   . SER   B 1 167 ? 34.214 -40.348 -7.625  1.00 15.34 ?  167 SER   B CB   1 
ATOM   6595 O OG   . SER   B 1 167 ? 34.877 -39.192 -7.135  1.00 15.36 ?  167 SER   B OG   1 
ATOM   6596 H H    . SER   B 1 167 ? 35.600 -39.665 -9.644  1.00 18.88 ?  167 SER   B H    1 
ATOM   6597 H HA   . SER   B 1 167 ? 33.251 -40.944 -9.329  1.00 18.35 ?  167 SER   B HA   1 
ATOM   6598 H HB2  . SER   B 1 167 ? 33.422 -40.517 -7.085  1.00 18.42 ?  167 SER   B HB2  1 
ATOM   6599 H HB3  . SER   B 1 167 ? 34.814 -41.110 -7.570  1.00 18.42 ?  167 SER   B HB3  1 
ATOM   6600 H HG   . SER   B 1 167 ? 35.558 -39.042 -7.600  1.00 18.45 ?  167 SER   B HG   1 
ATOM   6601 N N    . PHE   B 1 168 ? 33.247 -37.925 -9.952  1.00 15.10 ?  168 PHE   B N    1 
ATOM   6602 C CA   . PHE   B 1 168 ? 32.424 -36.720 -10.015 1.00 14.69 ?  168 PHE   B CA   1 
ATOM   6603 C C    . PHE   B 1 168 ? 31.101 -36.977 -10.734 1.00 13.43 ?  168 PHE   B C    1 
ATOM   6604 O O    . PHE   B 1 168 ? 30.065 -36.374 -10.387 1.00 14.16 ?  168 PHE   B O    1 
ATOM   6605 C CB   . PHE   B 1 168 ? 33.188 -35.595 -10.712 1.00 15.21 ?  168 PHE   B CB   1 
ATOM   6606 C CG   . PHE   B 1 168 ? 32.397 -34.334 -10.820 1.00 15.64 ?  168 PHE   B CG   1 
ATOM   6607 C CD1  . PHE   B 1 168 ? 32.090 -33.608 -9.679  1.00 16.98 ?  168 PHE   B CD1  1 
ATOM   6608 C CD2  . PHE   B 1 168 ? 31.921 -33.894 -12.037 1.00 15.36 ?  168 PHE   B CD2  1 
ATOM   6609 C CE1  . PHE   B 1 168 ? 31.335 -32.458 -9.749  1.00 17.74 ?  168 PHE   B CE1  1 
ATOM   6610 C CE2  . PHE   B 1 168 ? 31.176 -32.722 -12.122 1.00 16.08 ?  168 PHE   B CE2  1 
ATOM   6611 C CZ   . PHE   B 1 168 ? 30.876 -32.007 -10.975 1.00 17.12 ?  168 PHE   B CZ   1 
ATOM   6612 H H    . PHE   B 1 168 ? 33.974 -37.893 -10.415 1.00 18.14 ?  168 PHE   B H    1 
ATOM   6613 H HA   . PHE   B 1 168 ? 32.222 -36.424 -9.116  1.00 17.64 ?  168 PHE   B HA   1 
ATOM   6614 H HB2  . PHE   B 1 168 ? 33.993 -35.397 -10.207 1.00 18.27 ?  168 PHE   B HB2  1 
ATOM   6615 H HB3  . PHE   B 1 168 ? 33.421 -35.876 -11.610 1.00 18.27 ?  168 PHE   B HB3  1 
ATOM   6616 H HD1  . PHE   B 1 168 ? 32.393 -33.912 -8.854  1.00 20.40 ?  168 PHE   B HD1  1 
ATOM   6617 H HD2  . PHE   B 1 168 ? 32.117 -34.366 -12.813 1.00 18.45 ?  168 PHE   B HD2  1 
ATOM   6618 H HE1  . PHE   B 1 168 ? 31.141 -31.982 -8.974  1.00 21.30 ?  168 PHE   B HE1  1 
ATOM   6619 H HE2  . PHE   B 1 168 ? 30.860 -32.429 -12.950 1.00 19.32 ?  168 PHE   B HE2  1 
ATOM   6620 H HZ   . PHE   B 1 168 ? 30.368 -31.230 -11.029 1.00 20.56 ?  168 PHE   B HZ   1 
ATOM   6621 N N    A LEU   B 1 169 ? 31.114 -37.855 -11.734 0.50 14.48 ?  169 LEU   B N    1 
ATOM   6622 N N    B LEU   B 1 169 ? 31.114 -37.861 -11.729 0.50 14.34 ?  169 LEU   B N    1 
ATOM   6623 C CA   A LEU   B 1 169 ? 29.927 -38.152 -12.521 0.50 16.53 ?  169 LEU   B CA   1 
ATOM   6624 C CA   B LEU   B 1 169 ? 29.928 -38.156 -12.517 0.50 16.37 ?  169 LEU   B CA   1 
ATOM   6625 C C    A LEU   B 1 169 ? 29.925 -39.608 -12.972 0.50 18.50 ?  169 LEU   B C    1 
ATOM   6626 C C    B LEU   B 1 169 ? 29.954 -39.582 -13.053 0.50 18.39 ?  169 LEU   B C    1 
ATOM   6627 O O    A LEU   B 1 169 ? 28.953 -40.114 -13.539 0.50 20.18 ?  169 LEU   B O    1 
ATOM   6628 O O    B LEU   B 1 169 ? 29.139 -39.959 -13.895 0.50 19.94 ?  169 LEU   B O    1 
ATOM   6629 C CB   A LEU   B 1 169 ? 29.857 -37.223 -13.735 0.50 17.92 ?  169 LEU   B CB   1 
ATOM   6630 C CB   B LEU   B 1 169 ? 29.822 -37.177 -13.686 0.50 17.75 ?  169 LEU   B CB   1 
ATOM   6631 C CG   A LEU   B 1 169 ? 28.636 -36.304 -13.795 0.50 19.89 ?  169 LEU   B CG   1 
ATOM   6632 C CG   B LEU   B 1 169 ? 28.500 -36.419 -13.815 0.50 19.81 ?  169 LEU   B CG   1 
ATOM   6633 C CD1  A LEU   B 1 169 ? 28.661 -35.462 -15.059 0.50 20.59 ?  169 LEU   B CD1  1 
ATOM   6634 C CD1  B LEU   B 1 169 ? 28.404 -35.800 -15.192 0.50 20.51 ?  169 LEU   B CD1  1 
ATOM   6635 C CD2  A LEU   B 1 169 ? 27.352 -37.112 -13.711 0.50 20.06 ?  169 LEU   B CD2  1 
ATOM   6636 C CD2  B LEU   B 1 169 ? 27.307 -37.319 -13.544 0.50 20.09 ?  169 LEU   B CD2  1 
ATOM   6637 O OXT  A LEU   B 1 169 ? 30.913 -40.314 -12.775 0.50 19.26 -1 169 LEU   B OXT  1 
ATOM   6638 O OXT  B LEU   B 1 169 ? 30.801 -40.387 -12.670 0.50 19.29 -1 169 LEU   B OXT  1 
ATOM   6639 H H    A LEU   B 1 169 ? 31.817 -38.295 -11.982 0.50 17.39 ?  169 LEU   B H    1 
ATOM   6640 H H    B LEU   B 1 169 ? 31.814 -38.305 -11.973 0.50 17.22 ?  169 LEU   B H    1 
ATOM   6641 H HA   A LEU   B 1 169 ? 29.146 -38.003 -11.973 0.50 19.85 ?  169 LEU   B HA   1 
ATOM   6642 H HA   B LEU   B 1 169 ? 29.154 -38.060 -11.948 0.50 19.66 ?  169 LEU   B HA   1 
ATOM   6643 H HB2  A LEU   B 1 169 ? 30.643 -36.656 -13.737 0.50 21.52 ?  169 LEU   B HB2  1 
ATOM   6644 H HB2  B LEU   B 1 169 ? 30.526 -36.516 -13.598 0.50 21.32 ?  169 LEU   B HB2  1 
ATOM   6645 H HB3  A LEU   B 1 169 ? 29.847 -37.766 -14.538 0.50 21.52 ?  169 LEU   B HB3  1 
ATOM   6646 H HB3  B LEU   B 1 169 ? 29.948 -37.672 -14.512 0.50 21.32 ?  169 LEU   B HB3  1 
ATOM   6647 H HG   A LEU   B 1 169 ? 28.656 -35.701 -13.036 0.50 23.88 ?  169 LEU   B HG   1 
ATOM   6648 H HG   B LEU   B 1 169 ? 28.487 -35.699 -13.163 0.50 23.79 ?  169 LEU   B HG   1 
ATOM   6649 H HD11 A LEU   B 1 169 ? 27.884 -34.883 -15.068 0.50 24.73 ?  169 LEU   B HD11 1 
ATOM   6650 H HD11 B LEU   B 1 169 ? 27.579 -35.295 -15.252 0.50 24.64 ?  169 LEU   B HD11 1 
ATOM   6651 H HD12 A LEU   B 1 169 ? 29.472 -34.934 -15.068 0.50 24.73 ?  169 LEU   B HD12 1 
ATOM   6652 H HD12 B LEU   B 1 169 ? 29.164 -35.211 -15.325 0.50 24.64 ?  169 LEU   B HD12 1 
ATOM   6653 H HD13 A LEU   B 1 169 ? 28.641 -36.054 -15.829 0.50 24.73 ?  169 LEU   B HD13 1 
ATOM   6654 H HD13 B LEU   B 1 169 ? 28.413 -36.507 -15.854 0.50 24.64 ?  169 LEU   B HD13 1 
ATOM   6655 H HD21 A LEU   B 1 169 ? 26.617 -36.579 -14.044 0.50 24.09 ?  169 LEU   B HD21 1 
ATOM   6656 H HD21 B LEU   B 1 169 ? 26.518 -36.931 -13.946 0.50 24.13 ?  169 LEU   B HD21 1 
ATOM   6657 H HD22 A LEU   B 1 169 ? 27.451 -37.915 -14.249 0.50 24.09 ?  169 LEU   B HD22 1 
ATOM   6658 H HD22 B LEU   B 1 169 ? 27.479 -38.195 -13.926 0.50 24.13 ?  169 LEU   B HD22 1 
ATOM   6659 H HD23 A LEU   B 1 169 ? 27.192 -37.357 -12.785 0.50 24.09 ?  169 LEU   B HD23 1 
ATOM   6660 H HD23 B LEU   B 1 169 ? 27.190 -37.394 -12.586 0.50 24.13 ?  169 LEU   B HD23 1 
HETATM 6661 S S    B DMS   C 2 .   ? 12.286 5.198   6.167   0.50 15.12 ?  301 DMS   A S    1 
HETATM 6662 O O    B DMS   C 2 .   ? 11.286 6.059   6.909   0.50 16.93 ?  301 DMS   A O    1 
HETATM 6663 C C1   B DMS   C 2 .   ? 13.771 6.134   6.120   0.50 13.27 ?  301 DMS   A C1   1 
HETATM 6664 C C2   B DMS   C 2 .   ? 11.739 5.275   4.434   0.50 16.12 ?  301 DMS   A C2   1 
HETATM 6665 H H11  B DMS   C 2 .   ? 14.496 5.531   5.686   0.50 15.95 ?  301 DMS   A H11  1 
HETATM 6666 H H12  B DMS   C 2 .   ? 13.948 6.429   7.087   0.50 15.95 ?  301 DMS   A H12  1 
HETATM 6667 H H13  B DMS   C 2 .   ? 13.427 6.898   5.541   0.50 15.95 ?  301 DMS   A H13  1 
HETATM 6668 H H21  B DMS   C 2 .   ? 12.401 4.668   3.925   0.50 19.37 ?  301 DMS   A H21  1 
HETATM 6669 H H22  B DMS   C 2 .   ? 10.756 4.918   4.389   0.50 19.37 ?  301 DMS   A H22  1 
HETATM 6670 H H23  B DMS   C 2 .   ? 11.807 6.273   4.179   0.50 19.37 ?  301 DMS   A H23  1 
HETATM 6671 N N2   B A1A47 D 3 .   ? 14.461 1.040   6.520   0.50 10.25 ?  302 A1A47 A N2   1 
HETATM 6672 C C3   B A1A47 D 3 .   ? 11.560 0.675   -0.401  0.50 13.45 ?  302 A1A47 A C3   1 
HETATM 6673 C C6   B A1A47 D 3 .   ? 14.822 1.431   2.950   0.50 9.80  ?  302 A1A47 A C6   1 
HETATM 6674 C C9   B A1A47 D 3 .   ? 15.058 3.020   5.274   0.50 10.73 ?  302 A1A47 A C9   1 
HETATM 6675 C C1   B A1A47 D 3 .   ? 11.057 1.270   2.017   0.50 12.03 ?  302 A1A47 A C1   1 
HETATM 6676 C C10  B A1A47 D 3 .   ? 14.706 1.660   5.361   0.50 10.01 ?  302 A1A47 A C10  1 
HETATM 6677 C C11  B A1A47 D 3 .   ? 14.595 0.864   4.217   0.50 9.60  ?  302 A1A47 A C11  1 
HETATM 6678 C C2   B A1A47 D 3 .   ? 12.145 1.068   0.965   0.50 11.86 ?  302 A1A47 A C2   1 
HETATM 6679 C C4   B A1A47 D 3 .   ? 11.863 -0.806  -0.594  0.50 13.71 ?  302 A1A47 A C4   1 
HETATM 6680 C C5   B A1A47 D 3 .   ? 12.788 -1.214  0.548   0.50 12.43 ?  302 A1A47 A C5   1 
HETATM 6681 C C7   B A1A47 D 3 .   ? 15.176 2.791   2.847   0.50 10.46 ?  302 A1A47 A C7   1 
HETATM 6682 C C8   B A1A47 D 3 .   ? 15.298 3.582   4.006   0.50 11.18 ?  302 A1A47 A C8   1 
HETATM 6683 N N1   B A1A47 D 3 .   ? 13.069 -0.002  1.321   0.50 11.12 ?  302 A1A47 A N1   1 
HETATM 6684 N N3   B A1A47 D 3 .   ? 14.250 -0.415  4.426   0.50 9.87  ?  302 A1A47 A N3   1 
HETATM 6685 O O1   B A1A47 D 3 .   ? 10.889 0.357   2.854   0.50 12.35 ?  302 A1A47 A O1   1 
HETATM 6686 O O2   B A1A47 D 3 .   ? 15.448 -0.779  1.707   0.50 9.71  ?  302 A1A47 A O2   1 
HETATM 6687 O O3   B A1A47 D 3 .   ? 15.070 1.241   0.330   0.50 10.44 ?  302 A1A47 A O3   1 
HETATM 6688 O O4   B A1A47 D 3 .   ? 10.418 2.341   1.965   0.50 12.90 ?  302 A1A47 A O4   1 
HETATM 6689 S S1   B A1A47 D 3 .   ? 14.702 0.442   1.474   0.50 9.98  ?  302 A1A47 A S1   1 
HETATM 6690 S S2   B A1A47 D 3 .   ? 14.101 -0.542  6.093   0.50 10.06 ?  302 A1A47 A S2   1 
HETATM 6691 H H3   B A1A47 D 3 .   ? 12.066 1.251   -1.178  0.50 16.16 ?  302 A1A47 A H3   1 
HETATM 6692 H H2   B A1A47 D 3 .   ? 10.492 0.887   -0.501  0.50 16.16 ?  302 A1A47 A H2   1 
HETATM 6693 H H10  B A1A47 D 3 .   ? 15.144 3.621   6.166   0.50 12.89 ?  302 A1A47 A H10  1 
HETATM 6694 H H1   B A1A47 D 3 .   ? 12.691 2.007   0.858   0.50 14.25 ?  302 A1A47 A H1   1 
HETATM 6695 H H4   B A1A47 D 3 .   ? 12.377 -0.945  -1.545  0.50 16.47 ?  302 A1A47 A H4   1 
HETATM 6696 H H5   B A1A47 D 3 .   ? 10.954 -1.395  -0.642  0.50 16.47 ?  302 A1A47 A H5   1 
HETATM 6697 H H6   B A1A47 D 3 .   ? 13.713 -1.671  0.196   0.50 14.93 ?  302 A1A47 A H6   1 
HETATM 6698 H H7   B A1A47 D 3 .   ? 12.288 -1.933  1.193   0.50 14.93 ?  302 A1A47 A H7   1 
HETATM 6699 H H8   B A1A47 D 3 .   ? 15.368 3.237   1.881   0.50 12.57 ?  302 A1A47 A H8   1 
HETATM 6700 H H9   B A1A47 D 3 .   ? 15.562 4.627   3.922   0.50 13.43 ?  302 A1A47 A H9   1 
HETATM 6701 O O    . HOH   E 4 .   ? 4.622  3.945   0.952   1.00 24.48 ?  401 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 14.834 -4.641  20.555  1.00 36.94 ?  402 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 11.582 -10.792 -10.083 1.00 38.50 ?  403 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 12.325 0.207   15.050  1.00 24.80 ?  404 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 8.082  -21.535 3.969   1.00 41.91 ?  405 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 34.413 -1.897  12.476  1.00 33.51 ?  406 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 15.218 -12.310 18.787  1.00 28.69 ?  407 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 7.654  -6.373  -6.561  1.00 36.55 ?  408 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 17.190 -18.148 15.038  1.00 23.67 ?  409 HOH   A O    1 
HETATM 6710 O O    B HOH   E 4 .   ? 7.118  -3.036  13.423  0.50 21.91 ?  410 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 13.977 -5.050  17.682  1.00 17.76 ?  411 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 26.892 11.433  1.698   1.00 14.98 ?  412 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 42.477 10.529  5.249   1.00 18.40 ?  413 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 0.557  -4.765  0.465   1.00 27.87 ?  414 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 28.974 0.479   -9.718  1.00 18.90 ?  415 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 36.103 -5.059  -0.577  1.00 25.91 ?  416 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 22.800 12.545  1.694   1.00 12.56 ?  417 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 15.108 3.808   17.955  1.00 33.30 ?  418 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 34.006 -0.934  -8.897  1.00 26.66 ?  419 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 9.792  -21.406 5.770   1.00 15.46 ?  420 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 26.456 -19.323 -1.853  1.00 12.06 ?  421 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 14.755 -14.055 16.746  1.00 19.84 ?  422 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 30.216 -13.272 -8.615  1.00 20.35 ?  423 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 19.800 -12.452 -9.019  1.00 22.29 ?  424 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 28.178 -6.363  19.601  1.00 36.01 ?  425 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? -0.503 -3.168  3.293   1.00 39.11 ?  426 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 28.305 -0.114  -13.394 1.00 29.77 ?  427 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 30.977 -18.171 7.745   1.00 18.59 ?  428 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 14.142 -4.524  -11.790 1.00 23.28 ?  429 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 38.309 10.113  7.192   1.00 36.44 ?  430 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 22.373 5.344   18.975  1.00 37.66 ?  431 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 21.248 -2.348  -2.149  1.00 12.01 ?  432 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 18.812 -21.995 6.851   1.00 27.39 ?  433 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 14.442 -24.727 11.623  1.00 29.48 ?  434 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 27.294 13.800  2.965   1.00 27.50 ?  435 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 18.738 -19.530 13.501  1.00 32.94 ?  436 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 7.955  -12.650 -0.805  1.00 17.76 ?  437 HOH   A O    1 
HETATM 6738 O O    A HOH   E 4 .   ? 3.595  -9.473  9.758   0.50 25.38 ?  438 HOH   A O    1 
HETATM 6739 O O    B HOH   E 4 .   ? 8.372  3.893   2.749   0.50 17.87 ?  439 HOH   A O    1 
HETATM 6740 O O    B HOH   E 4 .   ? 14.723 -3.036  2.974   0.50 8.85  ?  440 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 37.595 2.754   10.173  1.00 23.02 ?  441 HOH   A O    1 
HETATM 6742 O O    A HOH   E 4 .   ? 17.490 -1.707  0.482   0.50 12.52 ?  442 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 42.622 4.299   5.412   1.00 28.24 ?  443 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 30.983 6.212   -12.287 1.00 28.55 ?  444 HOH   A O    1 
HETATM 6745 O O    A HOH   E 4 .   ? 5.300  2.637   5.327   0.50 23.74 ?  445 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 13.296 -1.388  -6.511  1.00 14.22 ?  446 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 9.160  -10.228 19.434  1.00 35.69 ?  447 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 44.355 7.071   6.506   1.00 23.94 ?  448 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 21.912 -21.909 8.417   1.00 25.09 ?  449 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 17.102 -17.786 -5.074  1.00 23.60 ?  450 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 35.754 -12.674 6.784   1.00 13.96 ?  451 HOH   A O    1 
HETATM 6752 O O    A HOH   E 4 .   ? 14.273 0.566   6.846   0.50 23.10 ?  452 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 31.736 8.146   14.923  1.00 21.51 ?  453 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 31.796 -9.302  -6.690  1.00 18.79 ?  454 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 20.127 4.576   -7.540  1.00 15.68 ?  455 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 22.310 -19.240 11.359  1.00 28.09 ?  456 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 38.588 4.955   7.001   1.00 13.73 ?  457 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 39.805 -0.966  -5.202  1.00 18.43 ?  458 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? -0.704 -8.539  2.392   1.00 38.66 ?  459 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 13.501 -15.185 -7.441  1.00 23.79 ?  460 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 14.286 -21.096 -4.314  1.00 26.09 ?  461 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 28.491 -10.582 -13.966 1.00 42.08 ?  462 HOH   A O    1 
HETATM 6763 O O    B HOH   E 4 .   ? 14.348 7.908   10.481  0.50 22.22 ?  463 HOH   A O    1 
HETATM 6764 O O    B HOH   E 4 .   ? 18.234 -1.682  0.510   0.50 9.15  ?  464 HOH   A O    1 
HETATM 6765 O O    B HOH   E 4 .   ? 12.218 -1.931  -3.941  0.50 15.50 ?  465 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 24.032 -2.016  -2.099  1.00 8.91  ?  466 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 20.578 -19.624 -5.172  1.00 25.64 ?  467 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 33.635 -7.141  4.232   1.00 14.30 ?  468 HOH   A O    1 
HETATM 6769 O O    A HOH   E 4 .   ? 18.549 9.440   8.966   0.50 15.09 ?  469 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 37.466 11.912  5.015   1.00 25.16 ?  470 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 37.207 -2.850  9.729   1.00 36.47 ?  471 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 30.819 3.084   8.294   1.00 9.81  ?  472 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 31.053 -13.925 -2.529  1.00 11.03 ?  473 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 17.002 -19.307 4.911   1.00 12.10 ?  474 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 11.047 1.443   13.006  1.00 20.24 ?  475 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 24.645 2.060   -7.051  1.00 16.83 ?  476 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 24.464 3.621   -1.816  1.00 13.40 ?  477 HOH   A O    1 
HETATM 6778 O O    B HOH   E 4 .   ? 15.795 5.772   7.791   0.50 16.48 ?  478 HOH   A O    1 
HETATM 6779 O O    B HOH   E 4 .   ? 10.773 6.447   11.186  0.50 26.11 ?  479 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 27.525 -10.658 14.024  1.00 14.45 ?  480 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 15.130 -8.038  -9.510  1.00 17.64 ?  481 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 15.205 -21.643 14.239  1.00 14.92 ?  482 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 26.978 4.207   -0.650  1.00 10.96 ?  483 HOH   A O    1 
HETATM 6784 O O    B HOH   E 4 .   ? 18.765 9.251   9.480   0.50 18.26 ?  484 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 31.712 -7.295  -9.886  1.00 18.74 ?  485 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 15.548 11.997  7.958   1.00 38.22 ?  486 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 14.067 -23.123 7.464   1.00 14.74 ?  487 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 23.505 11.392  4.134   1.00 10.42 ?  488 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 16.468 -22.018 0.943   1.00 24.95 ?  489 HOH   A O    1 
HETATM 6790 O O    A HOH   E 4 .   ? 6.945  -8.177  11.878  0.50 15.55 ?  490 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 25.738 -0.744  -7.350  1.00 12.77 ?  491 HOH   A O    1 
HETATM 6792 O O    A HOH   E 4 .   ? 18.952 -0.658  -1.584  0.50 6.82  ?  492 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 24.267 -7.818  14.427  1.00 14.06 ?  493 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 24.745 -17.561 12.711  1.00 21.69 ?  494 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 43.943 8.472   -3.121  1.00 24.60 ?  495 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 14.549 -0.474  -12.026 1.00 23.18 ?  496 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 21.315 10.372  15.116  1.00 30.86 ?  497 HOH   A O    1 
HETATM 6798 O O    A HOH   E 4 .   ? 6.744  -3.405  12.929  0.50 21.52 ?  498 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 27.307 2.298   18.699  1.00 24.25 ?  499 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 24.116 4.015   -4.878  1.00 23.02 ?  500 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 27.303 -5.988  -13.945 1.00 34.94 ?  501 HOH   A O    1 
HETATM 6802 O O    B HOH   E 4 .   ? 9.996  3.720   -0.467  0.50 21.35 ?  502 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 21.437 3.247   -0.361  1.00 10.10 ?  503 HOH   A O    1 
HETATM 6804 O O    A HOH   E 4 .   ? 9.005  -12.151 17.207  0.50 32.27 ?  504 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 32.764 -9.246  5.887   1.00 17.21 ?  505 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 44.902 -0.680  2.947   1.00 36.10 ?  506 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 27.955 0.895   -7.160  1.00 11.72 ?  507 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 22.678 -11.998 21.835  1.00 35.29 ?  508 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 37.524 -1.980  5.749   1.00 23.71 ?  509 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 30.724 1.820   16.676  1.00 16.75 ?  510 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 43.379 7.906   2.730   1.00 22.38 ?  511 HOH   A O    1 
HETATM 6812 O O    A HOH   E 4 .   ? 6.464  -5.619  11.213  0.50 13.40 ?  512 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 18.628 -2.314  -16.326 1.00 39.42 ?  513 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 20.533 -20.011 2.740   1.00 14.71 ?  514 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 23.897 -20.267 -1.426  1.00 13.47 ?  515 HOH   A O    1 
HETATM 6816 O O    A HOH   E 4 .   ? 14.630 -3.653  3.134   0.50 9.29  ?  516 HOH   A O    1 
HETATM 6817 O O    B HOH   E 4 .   ? 5.577  2.201   7.735   0.50 28.36 ?  517 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 38.132 -1.349  -1.940  1.00 16.58 ?  518 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 30.096 -10.118 12.956  1.00 17.83 ?  519 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 10.507 -22.192 -1.244  1.00 43.99 ?  520 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 23.985 -15.663 -9.271  1.00 30.49 ?  521 HOH   A O    1 
HETATM 6822 O O    A HOH   E 4 .   ? 15.796 -0.949  5.313   0.50 20.72 ?  522 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 20.513 -17.879 24.790  1.00 48.56 ?  523 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 41.645 1.558   4.968   1.00 33.49 ?  524 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 30.350 -12.928 13.494  1.00 16.97 ?  525 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 36.702 -4.990  5.365   1.00 21.25 ?  526 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 21.667 -13.810 -8.153  1.00 38.29 ?  527 HOH   A O    1 
HETATM 6828 O O    A HOH   E 4 .   ? 16.015 6.956   3.051   0.50 11.84 ?  528 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 22.709 8.084   18.405  1.00 37.22 ?  529 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 35.062 -5.208  -3.116  1.00 15.93 ?  530 HOH   A O    1 
HETATM 6831 O O    B HOH   E 4 .   ? 19.243 -0.457  -1.879  0.50 10.99 ?  531 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 32.569 -10.662 3.130   1.00 26.42 ?  532 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 32.663 -4.243  -9.930  1.00 23.22 ?  533 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 16.280 16.737  8.733   1.00 26.35 ?  534 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 16.218 -14.295 20.330  1.00 35.59 ?  535 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 10.360 -13.709 -1.631  1.00 13.92 ?  536 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 40.918 -8.226  -6.748  1.00 34.84 ?  537 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 15.846 2.120   24.889  1.00 46.57 ?  538 HOH   A O    1 
HETATM 6839 O O    B HOH   E 4 .   ? 8.536  1.683   -1.986  0.50 18.86 ?  539 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 27.148 -3.365  19.303  1.00 31.56 ?  540 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? -1.339 -5.026  7.739   1.00 33.69 ?  541 HOH   A O    1 
HETATM 6842 O O    A HOH   E 4 .   ? 16.253 2.959   -1.390  0.50 8.10  ?  542 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 9.449  -16.292 -1.951  1.00 39.13 ?  543 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 18.439 -16.090 16.404  1.00 32.85 ?  544 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 23.587 -8.081  17.053  1.00 18.44 ?  545 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 18.492 4.858   -15.110 1.00 39.48 ?  546 HOH   A O    1 
HETATM 6847 O O    B HOH   E 4 .   ? 16.781 2.892   -1.551  0.50 10.52 ?  547 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 11.705 -10.820 17.075  1.00 18.55 ?  548 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 23.267 -20.956 1.278   1.00 15.15 ?  549 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 21.587 -14.717 18.129  1.00 40.14 ?  550 HOH   A O    1 
HETATM 6851 O O    . HOH   E 4 .   ? 21.312 -9.264  21.350  1.00 36.53 ?  551 HOH   A O    1 
HETATM 6852 O O    B HOH   E 4 .   ? 19.282 2.124   -0.805  0.50 11.26 ?  552 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 34.361 -8.102  -0.566  1.00 22.81 ?  553 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 23.238 7.593   -3.118  1.00 24.18 ?  554 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 31.325 -12.758 -0.010  1.00 17.24 ?  555 HOH   A O    1 
HETATM 6856 O O    A HOH   E 4 .   ? 18.858 2.042   -0.703  0.50 7.17  ?  556 HOH   A O    1 
HETATM 6857 O O    A HOH   E 4 .   ? 11.062 -0.374  1.979   0.50 23.01 ?  557 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 37.686 -8.800  -3.475  1.00 23.57 ?  558 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 30.631 14.792  2.867   1.00 17.65 ?  559 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 27.814 7.150   -6.328  1.00 33.81 ?  560 HOH   A O    1 
HETATM 6861 O O    . HOH   E 4 .   ? 29.854 -16.062 10.549  1.00 31.11 ?  561 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 19.492 -11.026 24.207  1.00 50.86 ?  562 HOH   A O    1 
HETATM 6863 O O    B HOH   E 4 .   ? 4.477  2.594   5.361   0.50 21.28 ?  563 HOH   A O    1 
HETATM 6864 O O    A HOH   E 4 .   ? 14.023 -0.337  3.506   0.50 39.14 ?  564 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 29.770 -1.933  -12.713 1.00 42.20 ?  565 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 25.474 8.266   -4.774  1.00 20.97 ?  566 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 32.465 -15.968 10.787  1.00 35.59 ?  567 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 24.921 5.626   20.788  1.00 45.98 ?  568 HOH   A O    1 
HETATM 6869 O O    . HOH   E 4 .   ? 19.842 -17.267 -5.103  1.00 20.88 ?  569 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 24.677 14.535  7.902   1.00 29.60 ?  570 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 26.901 11.731  -1.260  1.00 27.07 ?  571 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 27.443 -11.342 16.521  1.00 33.02 ?  572 HOH   A O    1 
HETATM 6873 O O    A HOH   E 4 .   ? 11.952 -13.398 16.318  0.50 25.20 ?  573 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 23.230 -22.443 -3.240  1.00 32.61 ?  574 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 15.725 -21.499 3.674   1.00 19.84 ?  575 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 39.671 -7.091  -3.602  1.00 40.62 ?  576 HOH   A O    1 
HETATM 6877 O O    . HOH   E 4 .   ? 21.937 5.257   -5.776  1.00 23.39 ?  577 HOH   A O    1 
HETATM 6878 O O    . HOH   E 4 .   ? 23.536 13.736  5.574   1.00 17.00 ?  578 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 18.729 10.856  11.410  1.00 28.89 ?  579 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 10.981 -14.958 -6.054  1.00 30.95 ?  580 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 12.332 1.525   17.402  1.00 39.64 ?  581 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 25.815 10.867  -3.754  1.00 23.85 ?  582 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 18.028 -16.174 -8.755  1.00 36.65 ?  583 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? 35.173 7.419   12.287  1.00 46.48 ?  584 HOH   A O    1 
HETATM 6885 O O    . HOH   E 4 .   ? 16.790 -20.591 16.199  1.00 24.77 ?  585 HOH   A O    1 
HETATM 6886 O O    . HOH   E 4 .   ? 15.684 -17.033 -7.031  1.00 28.59 ?  586 HOH   A O    1 
HETATM 6887 O O    . HOH   E 4 .   ? 28.902 8.952   17.561  1.00 34.97 ?  587 HOH   A O    1 
HETATM 6888 O O    . HOH   E 4 .   ? 17.343 -18.755 19.869  1.00 43.19 ?  588 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 14.028 -10.254 -10.799 1.00 26.55 ?  589 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 23.156 11.816  -4.057  1.00 16.20 ?  590 HOH   A O    1 
HETATM 6891 O O    B HOH   E 4 .   ? 5.695  3.972   3.383   0.50 20.53 ?  591 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 40.982 -4.010  -0.318  1.00 34.01 ?  592 HOH   A O    1 
HETATM 6893 O O    . HOH   E 4 .   ? 30.879 0.664   19.203  1.00 34.85 ?  593 HOH   A O    1 
HETATM 6894 O O    . HOH   E 4 .   ? 28.604 -7.862  -15.233 1.00 45.10 ?  594 HOH   A O    1 
HETATM 6895 O O    B HOH   E 4 .   ? 16.305 8.136   8.713   0.50 15.64 ?  595 HOH   A O    1 
HETATM 6896 O O    . HOH   E 4 .   ? 41.772 9.315   -4.097  1.00 27.56 ?  596 HOH   A O    1 
HETATM 6897 O O    . HOH   E 4 .   ? 44.556 10.466  -1.529  1.00 28.18 ?  597 HOH   A O    1 
HETATM 6898 O O    . HOH   E 4 .   ? 28.629 -4.640  -12.334 1.00 29.87 ?  598 HOH   A O    1 
HETATM 6899 O O    . HOH   E 4 .   ? 16.016 -6.636  -11.689 1.00 35.28 ?  599 HOH   A O    1 
HETATM 6900 O O    . HOH   E 4 .   ? 23.308 -12.874 19.365  1.00 39.59 ?  600 HOH   A O    1 
HETATM 6901 O O    . HOH   E 4 .   ? 40.500 -0.219  -7.878  1.00 32.42 ?  601 HOH   A O    1 
HETATM 6902 O O    . HOH   E 4 .   ? 18.411 -23.235 1.881   1.00 34.82 ?  602 HOH   A O    1 
HETATM 6903 O O    . HOH   E 4 .   ? 14.124 -25.360 8.956   1.00 26.25 ?  603 HOH   A O    1 
HETATM 6904 O O    . HOH   E 4 .   ? 19.946 -22.351 4.089   1.00 23.00 ?  604 HOH   A O    1 
HETATM 6905 O O    . HOH   E 4 .   ? 31.520 -0.627  -10.558 1.00 22.06 ?  605 HOH   A O    1 
HETATM 6906 O O    . HOH   E 4 .   ? 16.141 -23.395 5.698   1.00 25.28 ?  606 HOH   A O    1 
HETATM 6907 O O    . HOH   E 4 .   ? 39.176 2.349   7.600   1.00 28.29 ?  607 HOH   A O    1 
HETATM 6908 O O    . HOH   E 4 .   ? 30.773 5.831   -14.631 1.00 35.35 ?  608 HOH   A O    1 
HETATM 6909 O O    B HOH   E 4 .   ? 9.477  -1.211  -3.545  0.50 25.84 ?  609 HOH   A O    1 
HETATM 6910 O O    B HOH   E 4 .   ? 12.976 10.261  6.539   0.50 27.46 ?  610 HOH   A O    1 
HETATM 6911 O O    B HOH   E 4 .   ? 8.507  6.540   2.279   0.50 16.89 ?  611 HOH   A O    1 
HETATM 6912 O O    . HOH   E 4 .   ? 37.398 -6.628  7.480   1.00 21.51 ?  612 HOH   A O    1 
HETATM 6913 O O    B HOH   E 4 .   ? 14.919 7.744   4.564   0.50 17.30 ?  613 HOH   A O    1 
HETATM 6914 O O    . HOH   E 4 .   ? 30.751 -5.778  -11.909 1.00 43.89 ?  614 HOH   A O    1 
HETATM 6915 O O    . HOH   E 4 .   ? 23.050 -23.746 1.614   1.00 28.33 ?  615 HOH   A O    1 
HETATM 6916 O O    B HOH   E 4 .   ? 15.797 9.856   6.367   0.50 22.86 ?  616 HOH   A O    1 
HETATM 6917 O O    . HOH   E 4 .   ? 28.989 14.370  0.980   1.00 41.76 ?  617 HOH   A O    1 
HETATM 6918 O O    . HOH   E 4 .   ? 39.550 -0.058  6.624   1.00 27.10 ?  618 HOH   A O    1 
HETATM 6919 O O    . HOH   E 4 .   ? 38.092 13.871  6.829   1.00 41.42 ?  619 HOH   A O    1 
HETATM 6920 O O    . HOH   E 4 .   ? 20.412 -15.969 -7.414  1.00 26.01 ?  620 HOH   A O    1 
HETATM 6921 O O    . HOH   E 4 .   ? 8.053  -3.044  -5.569  1.00 39.09 ?  621 HOH   A O    1 
HETATM 6922 O O    . HOH   E 4 .   ? 21.975 -24.071 4.338   1.00 23.56 ?  622 HOH   A O    1 
HETATM 6923 O O    . HOH   E 4 .   ? 36.474 -6.510  10.205  1.00 41.36 ?  623 HOH   A O    1 
HETATM 6924 O O    . HOH   E 4 .   ? 17.352 -6.573  -14.123 1.00 30.41 ?  624 HOH   A O    1 
HETATM 6925 O O    A HOH   E 4 .   ? 14.849 8.648   4.954   0.50 32.16 ?  625 HOH   A O    1 
HETATM 6926 O O    . HOH   E 4 .   ? 24.132 8.957   -7.215  1.00 31.20 ?  626 HOH   A O    1 
HETATM 6927 O O    . HOH   E 4 .   ? 16.420 -21.116 18.845  1.00 32.32 ?  627 HOH   A O    1 
HETATM 6928 O O    B HOH   E 4 .   ? 5.725  6.779   4.777   0.50 14.73 ?  628 HOH   A O    1 
HETATM 6929 O O    . HOH   E 4 .   ? 15.896 -12.242 27.579  1.00 37.08 ?  629 HOH   A O    1 
HETATM 6930 O O    B HOH   E 4 .   ? 6.227  6.773   1.780   0.50 22.10 ?  630 HOH   A O    1 
HETATM 6931 O O    B HOH   E 4 .   ? 4.988  6.608   7.080   0.50 26.08 ?  631 HOH   A O    1 
HETATM 6932 O O    . HOH   E 4 .   ? 14.685 -22.776 19.940  1.00 34.23 ?  632 HOH   A O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 29.773 -22.382 5.414   1.00 18.54 ?  201 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 48.209 -6.869  15.584  1.00 30.99 ?  202 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 37.914 -39.429 -0.279  1.00 40.60 ?  203 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 47.383 -7.451  -4.007  1.00 36.15 ?  204 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 59.198 -18.762 6.785   1.00 33.58 ?  205 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 49.401 -22.658 -19.727 1.00 43.43 ?  206 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 41.274 -7.851  5.506   1.00 36.93 ?  207 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 41.910 -35.945 -17.370 1.00 26.89 ?  208 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 52.908 -13.373 -20.492 1.00 37.63 ?  209 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 56.347 -19.681 7.365   1.00 32.00 ?  210 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 27.715 -29.201 -1.894  1.00 31.11 ?  211 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 54.481 -9.341  -8.790  1.00 16.43 ?  212 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 58.202 -12.913 8.425   1.00 34.12 ?  213 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 27.824 -41.872 -15.153 1.00 33.26 ?  214 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 50.253 -3.344  7.189   1.00 35.42 ?  215 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 50.738 -6.124  0.261   1.00 26.55 ?  216 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 44.470 -7.277  2.122   1.00 29.29 ?  217 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 55.443 -16.497 -14.355 1.00 32.72 ?  218 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 30.218 -41.065 -8.151  1.00 14.30 ?  219 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 35.928 -43.211 -8.581  1.00 27.09 ?  220 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 56.723 -30.724 -7.800  1.00 33.00 ?  221 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 57.755 -24.502 4.955   1.00 33.81 ?  222 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 29.728 -34.177 -0.474  1.00 33.05 ?  223 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 57.366 -16.232 -12.215 1.00 17.48 ?  224 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 57.176 -26.804 -7.555  1.00 34.67 ?  225 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 37.142 -19.758 -18.143 1.00 37.39 ?  226 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 39.304 -10.894 6.077   1.00 25.26 ?  227 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 30.789 -28.751 4.224   1.00 20.97 ?  228 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 45.183 -34.911 6.866   1.00 36.28 ?  229 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 41.333 -9.645  13.086  1.00 19.87 ?  230 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 48.546 -36.437 -15.490 1.00 44.07 ?  231 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 40.627 -16.013 14.148  1.00 24.42 ?  232 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 35.102 -7.995  -3.088  1.00 16.26 ?  233 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 50.714 -12.957 -0.488  1.00 10.70 ?  234 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 46.341 -1.622  13.385  1.00 26.36 ?  235 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 41.492 -39.185 -14.887 1.00 20.11 ?  236 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 34.541 -36.378 -7.210  1.00 14.59 ?  237 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 28.390 -19.709 -13.165 1.00 21.96 ?  238 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 42.613 -22.868 3.795   1.00 9.91  ?  239 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 44.490 -27.753 -0.741  1.00 21.36 ?  240 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 34.826 -24.623 13.803  1.00 28.48 ?  241 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 25.421 -25.993 -1.368  1.00 28.31 ?  242 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 32.868 -43.831 -11.364 1.00 17.33 ?  243 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 49.784 -0.592  10.315  1.00 28.56 ?  244 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 41.841 -23.500 9.274   1.00 14.72 ?  245 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 29.817 -26.320 3.873   1.00 25.31 ?  246 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 30.726 -42.261 -10.640 1.00 26.43 ?  247 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 38.927 -11.994 12.345  1.00 30.70 ?  248 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 42.553 -25.375 2.596   1.00 13.26 ?  249 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 39.474 -11.109 0.298   1.00 14.92 ?  250 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 51.513 -13.877 10.970  1.00 28.50 ?  251 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 51.681 -6.490  4.426   1.00 18.46 ?  252 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 34.183 -18.568 11.360  1.00 20.23 ?  253 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 44.949 -43.563 -10.439 1.00 27.36 ?  254 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 58.131 -10.611 -4.080  1.00 18.87 ?  255 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 43.117 -43.279 -8.222  1.00 25.86 ?  256 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 29.729 -25.246 -10.890 1.00 14.02 ?  257 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 47.943 -22.770 5.796   1.00 15.55 ?  258 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 33.507 -16.994 8.022   1.00 17.30 ?  259 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 50.963 -39.998 -8.201  1.00 27.42 ?  260 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 31.787 -17.953 -14.565 1.00 29.46 ?  261 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 40.306 -12.751 -11.567 1.00 13.17 ?  262 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 38.441 -11.037 -2.307  1.00 17.17 ?  263 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 57.606 -24.412 -3.855  1.00 20.20 ?  264 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 43.265 -32.384 -17.073 1.00 19.43 ?  265 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 30.840 -15.725 2.585   1.00 11.24 ?  266 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 48.103 -24.490 -17.780 1.00 27.22 ?  267 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 42.334 -9.919  9.378   1.00 18.69 ?  268 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 57.489 -9.228  1.457   1.00 18.15 ?  269 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 27.137 -31.850 -10.055 1.00 19.58 ?  270 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 43.366 -15.802 -12.180 1.00 12.35 ?  271 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 49.331 -28.680 -6.898  1.00 13.45 ?  272 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 28.253 -34.385 -9.527  1.00 19.09 ?  273 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 34.935 -33.424 -19.196 1.00 25.77 ?  274 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 56.942 -8.684  8.453   1.00 17.94 ?  275 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 56.189 -23.482 -14.738 1.00 25.27 ?  276 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 27.949 -22.904 -8.077  1.00 14.84 ?  277 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 34.430 -12.778 2.562   1.00 24.82 ?  278 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 42.241 -10.086 -15.011 1.00 32.77 ?  279 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 46.601 -31.287 -4.767  1.00 17.26 ?  280 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 50.031 -24.566 5.728   1.00 29.70 ?  281 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 48.393 -25.043 3.072   1.00 11.07 ?  282 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 42.372 -34.681 3.736   1.00 26.10 ?  283 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 41.115 -5.547  11.540  1.00 42.31 ?  284 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 27.603 -26.755 -15.724 1.00 29.25 ?  285 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 36.784 -12.757 -1.557  1.00 24.22 ?  286 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 46.874 -29.521 9.793   1.00 27.68 ?  287 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 28.488 -31.003 -14.729 1.00 30.36 ?  288 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 47.094 -33.987 -4.615  1.00 14.38 ?  289 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 62.782 -20.167 -0.874  1.00 37.32 ?  290 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 51.266 -37.613 -9.535  1.00 23.58 ?  291 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 48.673 -20.027 5.911   1.00 12.10 ?  292 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 33.502 -15.328 -14.023 1.00 18.83 ?  293 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 59.749 -15.370 8.170   1.00 28.45 ?  294 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 40.227 -10.828 -9.585  1.00 14.79 ?  295 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 45.414 -33.417 -15.926 1.00 20.28 ?  296 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 57.000 -12.090 12.383  1.00 38.60 ?  297 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 45.965 -40.437 -3.578  1.00 26.91 ?  298 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 43.525 -15.438 18.284  1.00 33.07 ?  299 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 44.620 -27.463 1.943   1.00 13.34 ?  300 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 42.716 -12.257 -18.542 1.00 27.34 ?  301 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 52.487 -10.468 13.041  1.00 21.45 ?  302 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 37.320 -35.738 7.173   1.00 29.33 ?  303 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 53.029 -16.014 -12.778 1.00 26.88 ?  304 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 44.049 -29.341 -4.674  1.00 22.62 ?  305 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 34.995 -33.524 4.438   1.00 24.41 ?  306 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 52.589 -29.233 -12.982 1.00 22.29 ?  307 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 37.818 -10.263 -10.790 1.00 15.02 ?  308 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 25.929 -21.476 -3.567  1.00 13.76 ?  309 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 32.785 -34.587 -5.963  1.00 14.13 ?  310 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 52.666 -35.669 -8.557  1.00 25.79 ?  311 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 41.710 -8.078  1.314   1.00 22.84 ?  312 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 53.477 -30.190 4.529   1.00 17.35 ?  313 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 41.208 -24.533 15.777  1.00 38.75 ?  314 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 37.476 -18.200 13.127  1.00 25.28 ?  315 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 48.205 -32.617 -16.605 1.00 41.78 ?  316 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 38.327 -9.376  -13.348 1.00 24.57 ?  317 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 51.418 -32.943 -10.736 1.00 34.71 ?  318 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 37.252 -30.637 -21.053 1.00 29.13 ?  319 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 43.149 -21.450 10.632  1.00 14.17 ?  320 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 27.988 -14.800 -9.417  1.00 29.13 ?  321 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 57.614 -22.059 3.187   1.00 24.95 ?  322 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 62.684 -13.540 4.648   1.00 25.46 ?  323 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 44.533 -24.618 9.537   1.00 17.30 ?  324 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 39.425 -23.509 -20.273 1.00 32.33 ?  325 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 26.312 -21.025 -6.314  1.00 14.21 ?  326 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 33.552 -31.103 11.091  1.00 33.47 ?  327 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 53.640 -12.560 -22.381 1.00 35.01 ?  328 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 38.313 -12.752 7.903   1.00 16.17 ?  329 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 42.803 -20.266 -20.797 1.00 30.11 ?  330 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 59.978 -17.125 -10.484 1.00 31.65 ?  331 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 36.698 -12.410 4.238   1.00 15.96 ?  332 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 44.181 -1.751  7.588   1.00 40.17 ?  333 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 28.870 -42.943 -12.406 1.00 33.87 ?  334 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 47.107 -24.500 8.147   1.00 24.23 ?  335 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 51.678 -5.953  -7.882  1.00 46.92 ?  336 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 45.781 -36.278 -16.131 1.00 31.35 ?  337 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 48.591 -11.891 -13.918 1.00 24.06 ?  338 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 43.096 -34.709 0.094   1.00 17.28 ?  339 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 47.458 -27.453 1.965   1.00 12.71 ?  340 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 42.915 -43.491 -14.393 1.00 38.30 ?  341 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 36.972 -15.090 -16.519 1.00 34.88 ?  342 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 46.828 -19.903 12.300  1.00 29.36 ?  343 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 32.969 -14.685 1.000   1.00 16.55 ?  344 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 38.445 -12.240 -16.287 1.00 41.60 ?  345 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 37.111 -45.327 -9.802  1.00 37.47 ?  346 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 39.825 -44.314 -11.247 1.00 32.51 ?  347 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 62.481 -20.141 -4.835  1.00 42.35 ?  348 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 38.516 -22.375 15.023  1.00 42.20 ?  349 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 40.456 -43.496 -9.121  1.00 25.33 ?  350 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 27.754 -26.615 -0.624  1.00 27.79 ?  351 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 33.746 -9.300  -8.879  1.00 28.95 ?  352 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 44.203 -37.369 -17.740 1.00 33.82 ?  353 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 23.183 -23.749 6.671   1.00 31.45 ?  354 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 36.049 -8.603  -9.707  1.00 31.25 ?  355 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 55.635 -8.299  10.884  1.00 24.02 ?  356 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 34.643 -10.314 7.420   1.00 21.31 ?  357 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 56.545 -7.278  3.178   1.00 26.40 ?  358 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 34.108 -7.791  11.380  1.00 40.19 ?  359 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 61.490 -19.876 1.610   1.00 32.02 ?  360 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 43.122 -12.601 -21.273 1.00 41.59 ?  361 HOH   B O    1 
HETATM 7094 O O    . HOH   F 4 .   ? 56.927 -21.538 -16.399 1.00 35.47 ?  362 HOH   B O    1 
HETATM 7095 O O    . HOH   F 4 .   ? 40.220 -8.809  9.970   1.00 35.31 ?  363 HOH   B O    1 
HETATM 7096 O O    . HOH   F 4 .   ? 27.148 -26.002 -11.569 1.00 28.65 ?  364 HOH   B O    1 
HETATM 7097 O O    . HOH   F 4 .   ? 32.409 -23.640 14.079  1.00 37.72 ?  365 HOH   B O    1 
HETATM 7098 O O    . HOH   F 4 .   ? 36.194 -8.732  8.949   1.00 32.86 ?  366 HOH   B O    1 
HETATM 7099 O O    . HOH   F 4 .   ? 54.216 -5.740  3.033   1.00 32.98 ?  367 HOH   B O    1 
HETATM 7100 O O    . HOH   F 4 .   ? 58.980 -10.538 9.174   1.00 38.22 ?  368 HOH   B O    1 
HETATM 7101 O O    . HOH   F 4 .   ? 39.909 -6.987  7.817   1.00 40.72 ?  369 HOH   B O    1 
HETATM 7102 O O    . HOH   F 4 .   ? 48.339 -26.525 8.814   1.00 34.74 ?  370 HOH   B O    1 
HETATM 7103 O O    . HOH   F 4 .   ? 51.993 -13.009 13.312  1.00 32.83 ?  371 HOH   B O    1 
HETATM 7104 O O    . HOH   F 4 .   ? 41.793 -10.039 -17.411 1.00 46.99 ?  372 HOH   B O    1 
HETATM 7105 O O    . HOH   F 4 .   ? 56.047 -7.813  -0.569  1.00 34.23 ?  373 HOH   B O    1 
HETATM 7106 O O    . HOH   F 4 .   ? 39.978 -11.404 -14.001 1.00 26.35 ?  374 HOH   B O    1 
HETATM 7107 O O    . HOH   F 4 .   ? 63.064 -12.398 6.822   1.00 35.20 ?  375 HOH   B O    1 
HETATM 7108 O O    . HOH   F 4 .   ? 36.510 -22.787 13.332  1.00 22.38 ?  376 HOH   B O    1 
HETATM 7109 O O    . HOH   F 4 .   ? 38.026 -10.564 9.995   1.00 27.82 ?  377 HOH   B O    1 
HETATM 7110 O O    . HOH   F 4 .   ? 41.842 -6.813  -4.853  1.00 44.76 ?  378 HOH   B O    1 
HETATM 7111 O O    . HOH   F 4 .   ? 44.072 -5.597  -3.421  1.00 40.91 ?  379 HOH   B O    1 
HETATM 7112 O O    . HOH   F 4 .   ? 42.654 -17.109 -23.255 1.00 42.51 ?  380 HOH   B O    1 
HETATM 7113 O O    . HOH   F 4 .   ? 40.148 -7.568  3.257   1.00 32.18 ?  381 HOH   B O    1 
HETATM 7114 O O    . HOH   F 4 .   ? 52.835 -29.871 7.171   1.00 22.05 ?  382 HOH   B O    1 
HETATM 7115 O O    . HOH   F 4 .   ? 39.766 -14.102 15.757  1.00 45.27 ?  383 HOH   B O    1 
HETATM 7116 O O    . HOH   F 4 .   ? 60.482 -22.318 2.818   1.00 43.91 ?  384 HOH   B O    1 
HETATM 7117 O O    . HOH   F 4 .   ? 35.325 -20.275 13.278  1.00 26.29 ?  385 HOH   B O    1 
HETATM 7118 O O    . HOH   F 4 .   ? 46.745 -5.282  2.883   1.00 39.75 ?  386 HOH   B O    1 
HETATM 7119 O O    . HOH   F 4 .   ? 35.301 -33.719 7.252   1.00 37.97 ?  387 HOH   B O    1 
HETATM 7120 O O    . HOH   F 4 .   ? 23.906 -20.856 -7.758  1.00 25.12 ?  388 HOH   B O    1 
HETATM 7121 O O    . HOH   F 4 .   ? 40.905 -9.783  15.821  1.00 42.94 ?  389 HOH   B O    1 
HETATM 7122 O O    . HOH   F 4 .   ? 25.768 -18.893 -12.028 1.00 34.72 ?  390 HOH   B O    1 
HETATM 7123 O O    . HOH   F 4 .   ? 44.096 -31.707 -3.866  1.00 27.83 ?  391 HOH   B O    1 
HETATM 7124 O O    . HOH   F 4 .   ? 40.720 -6.614  -0.868  1.00 22.76 ?  392 HOH   B O    1 
HETATM 7125 O O    . HOH   F 4 .   ? 26.655 -28.000 -13.603 1.00 32.98 ?  393 HOH   B O    1 
HETATM 7126 O O    . HOH   F 4 .   ? 27.861 -27.097 2.162   1.00 29.31 ?  394 HOH   B O    1 
HETATM 7127 O O    . HOH   F 4 .   ? 45.812 -20.300 15.173  1.00 48.71 ?  395 HOH   B O    1 
HETATM 7128 O O    . HOH   F 4 .   ? 24.594 -20.705 -10.500 1.00 35.68 ?  396 HOH   B O    1 
HETATM 7129 O O    . HOH   F 4 .   ? 50.621 -30.841 8.690   1.00 27.40 ?  397 HOH   B O    1 
HETATM 7130 O O    . HOH   F 4 .   ? 34.348 -33.483 9.580   1.00 31.48 ?  398 HOH   B O    1 
HETATM 7131 O O    . HOH   F 4 .   ? 26.860 -30.694 -12.717 1.00 26.03 ?  399 HOH   B O    1 
HETATM 7132 O O    . HOH   F 4 .   ? 57.715 -6.433  -2.385  1.00 34.17 ?  400 HOH   B O    1 
HETATM 7133 O O    . HOH   F 4 .   ? 40.862 -11.812 -22.388 1.00 39.12 ?  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   ? 0.4652 0.4744 0.5417 -0.0088 -0.0190 0.0633  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.4588 0.4630 0.5364 -0.0087 -0.0248 0.0632  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.4613 0.4718 0.5312 -0.0100 -0.0188 0.0638  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.4549 0.4605 0.5256 -0.0110 -0.0244 0.0633  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4439 0.4613 0.4835 -0.0143 -0.0260 0.0685  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.4362 0.4482 0.4784 -0.0166 -0.0316 0.0676  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.4454 0.4624 0.4892 -0.0124 -0.0301 0.0707  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.4379 0.4498 0.4872 -0.0144 -0.0352 0.0695  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.4715 0.4774 0.5572 -0.0081 -0.0130 0.0599  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.4663 0.4674 0.5493 -0.0091 -0.0187 0.0594  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.4750 0.4792 0.5622 -0.0068 -0.0110 0.0577  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.4704 0.4697 0.5537 -0.0080 -0.0168 0.0570  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.4746 0.4795 0.5622 -0.0083 -0.0114 0.0596  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.4697 0.4698 0.5532 -0.0091 -0.0171 0.0599  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.4222 0.4479 0.4233 -0.0198 -0.0301 0.0705  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.4126 0.4323 0.4144 -0.0245 -0.0361 0.0689  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.3970 0.4316 0.3588 -0.0270 -0.0327 0.0706  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.3852 0.4137 0.3450 -0.0340 -0.0399 0.0674  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.3655 0.4140 0.3139 -0.0320 -0.0274 0.0573  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.3507 0.3928 0.2917 -0.0426 -0.0362 0.0515  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.3648 0.4130 0.3008 -0.0327 -0.0292 0.0630  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.3503 0.3911 0.2768 -0.0437 -0.0366 0.0581  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4005 0.4317 0.3334 -0.0291 -0.0390 0.0832  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.3893 0.4147 0.3201 -0.0344 -0.0467 0.0804  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4016 0.4291 0.3062 -0.0315 -0.0460 0.0974  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.3906 0.4126 0.2920 -0.0358 -0.0535 0.0964  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4026 0.4266 0.2952 -0.0335 -0.0513 0.1055  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.3917 0.4105 0.2799 -0.0378 -0.0581 0.1047  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4002 0.4281 0.3075 -0.0300 -0.0475 0.1032  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.3895 0.4108 0.2900 -0.0342 -0.0552 0.1044  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.3344 0.3949 0.2716 -0.0359 -0.0195 0.0402  5   SER   A N   
60   N N   B SER   A 5   ? 0.3156 0.3706 0.2407 -0.0494 -0.0325 0.0308  5   SER   A N   
61   C CA  A SER   A 5   ? 0.3046 0.3771 0.2398 -0.0392 -0.0093 0.0198  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.2820 0.3509 0.2004 -0.0560 -0.0254 0.0060  5   SER   A CA  
63   C C   A SER   A 5   ? 0.2716 0.3515 0.2103 -0.0381 -0.0047 0.0029  5   SER   A C   
64   C C   B SER   A 5   ? 0.2475 0.3255 0.1630 -0.0524 -0.0192 -0.0109 5   SER   A C   
65   O O   A SER   A 5   ? 0.2775 0.3582 0.2215 -0.0289 -0.0048 -0.0117 5   SER   A O   
66   O O   B SER   A 5   ? 0.2491 0.3266 0.1649 -0.0456 -0.0142 -0.0224 5   SER   A O   
67   C CB  A SER   A 5   ? 0.3100 0.3855 0.2497 -0.0429 -0.0013 0.0187  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.2865 0.3576 0.2111 -0.0640 -0.0203 0.0005  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3150 0.3906 0.2518 -0.0444 0.0070  0.0211  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.2902 0.3605 0.2082 -0.0694 -0.0133 0.0002  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.2310 0.3169 0.1624 -0.0473 0.0038  0.0034  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.2097 0.2971 0.1220 -0.0577 -0.0114 -0.0135 6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.1987 0.2822 0.1330 -0.0535 0.0126  0.0133  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.1843 0.2703 0.1154 -0.0585 0.0027  -0.0026 6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.1917 0.2782 0.1417 -0.0620 0.0284  0.0168  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.1853 0.2734 0.1409 -0.0624 0.0246  0.0073  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2010 0.2862 0.1796 -0.0663 0.0321  0.0313  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.1954 0.2832 0.1840 -0.0632 0.0321  0.0192  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.1859 0.2544 0.1266 -0.0450 0.0105  0.0236  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.1710 0.2432 0.1157 -0.0487 0.0053  0.0066  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.1793 0.2326 0.1296 -0.0384 0.0096  0.0304  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.1637 0.2210 0.1249 -0.0413 0.0071  0.0132  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.1751 0.2269 0.1398 -0.0358 0.0020  0.0377  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.1588 0.2144 0.1362 -0.0402 0.0001  0.0223  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.1853 0.2267 0.1515 -0.0277 0.0157  0.0308  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.1692 0.2147 0.1533 -0.0291 0.0151  0.0098  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.1760 0.2231 0.1465 -0.0362 0.0069  0.0414  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.1591 0.2093 0.1462 -0.0427 0.0072  0.0234  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.1858 0.2248 0.1623 -0.0251 0.0137  0.0282  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.1691 0.2096 0.1653 -0.0295 0.0137  0.0056  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.1826 0.2236 0.1573 -0.0310 0.0097  0.0342  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.1659 0.2074 0.1572 -0.0379 0.0105  0.0121  6   PHE   A CZ  
121  N N   . SER   A 7   ? 0.1814 0.2670 0.1336 -0.0619 0.0349  0.0060  7   SER   A N   
122  C CA  . SER   A 7   ? 0.1885 0.2676 0.1590 -0.0527 0.0404  -0.0009 7   SER   A CA  
123  C C   . SER   A 7   ? 0.1706 0.2205 0.1613 -0.0519 0.0414  -0.0009 7   SER   A C   
124  O O   . SER   A 7   ? 0.1841 0.2091 0.1744 -0.0606 0.0433  0.0036  7   SER   A O   
125  C CB  . SER   A 7   ? 0.2196 0.3122 0.1909 -0.0333 0.0500  -0.0049 7   SER   A CB  
126  O OG  . SER   A 7   ? 0.2457 0.3312 0.2394 -0.0213 0.0481  -0.0076 7   SER   A OG  
133  N N   A GLY   A 8   ? 0.1624 0.2053 0.1700 -0.0514 0.0395  -0.0060 8   GLY   A N   
134  N N   B GLY   A 8   ? 0.1585 0.2066 0.1688 -0.0437 0.0391  -0.0030 8   GLY   A N   
135  C CA  A GLY   A 8   ? 0.1572 0.1918 0.1815 -0.0427 0.0356  -0.0109 8   GLY   A CA  
136  C CA  B GLY   A 8   ? 0.1494 0.1924 0.1782 -0.0291 0.0313  -0.0059 8   GLY   A CA  
137  C C   A GLY   A 8   ? 0.1454 0.1783 0.1691 -0.0349 0.0335  -0.0055 8   GLY   A C   
138  C C   B GLY   A 8   ? 0.1327 0.1770 0.1596 -0.0166 0.0260  -0.0005 8   GLY   A C   
139  O O   A GLY   A 8   ? 0.1555 0.1819 0.1895 -0.0190 0.0199  -0.0191 8   GLY   A O   
140  O O   B GLY   A 8   ? 0.1400 0.1805 0.1781 0.0006  0.0166  -0.0154 8   GLY   A O   
147  N N   A TYR   A 9   ? 0.1341 0.1702 0.1667 -0.0316 0.0379  0.0069  9   TYR   A N   
148  N N   B TYR   A 9   ? 0.1194 0.1675 0.1549 -0.0101 0.0227  0.0137  9   TYR   A N   
149  C CA  A TYR   A 9   ? 0.1279 0.1649 0.1466 -0.0261 0.0364  0.0137  9   TYR   A CA  
150  C CA  B TYR   A 9   ? 0.1156 0.1633 0.1378 -0.0067 0.0211  0.0166  9   TYR   A CA  
151  C C   A TYR   A 9   ? 0.1303 0.1495 0.1368 -0.0183 0.0390  0.0291  9   TYR   A C   
152  C C   B TYR   A 9   ? 0.1161 0.1489 0.1305 -0.0026 0.0344  0.0227  9   TYR   A C   
153  O O   A TYR   A 9   ? 0.1432 0.1565 0.1381 -0.0081 0.0349  0.0272  9   TYR   A O   
154  O O   B TYR   A 9   ? 0.1285 0.1568 0.1453 -0.0023 0.0300  0.0205  9   TYR   A O   
155  C CB  A TYR   A 9   ? 0.1239 0.1768 0.1482 -0.0204 0.0297  0.0096  9   TYR   A CB  
156  C CB  B TYR   A 9   ? 0.1151 0.1747 0.1364 0.0015  0.0082  0.0133  9   TYR   A CB  
157  C CG  A TYR   A 9   ? 0.1149 0.1830 0.1434 -0.0138 0.0335  0.0064  9   TYR   A CG  
158  C CG  B TYR   A 9   ? 0.1093 0.1799 0.1147 0.0133  0.0075  0.0140  9   TYR   A CG  
159  C CD1 A TYR   A 9   ? 0.1133 0.1893 0.1430 -0.0179 0.0350  0.0059  9   TYR   A CD1 
160  C CD1 B TYR   A 9   ? 0.1113 0.1862 0.1142 0.0125  0.0091  0.0166  9   TYR   A CD1 
161  C CD2 A TYR   A 9   ? 0.1130 0.1804 0.1422 -0.0114 0.0279  0.0168  9   TYR   A CD2 
162  C CD2 B TYR   A 9   ? 0.1128 0.1783 0.1122 0.0154  0.0025  0.0207  9   TYR   A CD2 
163  C CE1 A TYR   A 9   ? 0.1074 0.1876 0.1370 -0.0189 0.0271  0.0050  9   TYR   A CE1 
164  C CE1 B TYR   A 9   ? 0.1128 0.1871 0.1121 0.0124  0.0035  0.0205  9   TYR   A CE1 
165  C CE2 A TYR   A 9   ? 0.1039 0.1808 0.1257 -0.0090 0.0275  0.0161  9   TYR   A CE2 
166  C CE2 B TYR   A 9   ? 0.1140 0.1844 0.1082 0.0154  0.0060  0.0176  9   TYR   A CE2 
167  C CZ  A TYR   A 9   ? 0.0937 0.1805 0.1264 -0.0171 0.0261  0.0111  9   TYR   A CZ  
168  C CZ  B TYR   A 9   ? 0.1176 0.1899 0.1151 0.0054  0.0059  0.0185  9   TYR   A CZ  
169  O OH  A TYR   A 9   ? 0.0842 0.1817 0.1280 -0.0245 0.0200  0.0054  9   TYR   A OH  
170  O OH  B TYR   A 9   ? 0.1356 0.1948 0.1330 0.0001  0.0083  0.0175  9   TYR   A OH  
189  N N   A LEU   A 10  ? 0.1244 0.1321 0.1410 -0.0210 0.0290  0.0368  10  LEU   A N   
190  N N   B LEU   A 10  ? 0.1151 0.1359 0.1426 -0.0017 0.0170  0.0235  10  LEU   A N   
191  C CA  A LEU   A 10  ? 0.1168 0.1265 0.1515 -0.0188 0.0215  0.0443  10  LEU   A CA  
192  C CA  B LEU   A 10  ? 0.1068 0.1302 0.1439 -0.0066 0.0135  0.0297  10  LEU   A CA  
193  C C   A LEU   A 10  ? 0.1086 0.1200 0.1408 -0.0199 0.0170  0.0401  10  LEU   A C   
194  C C   B LEU   A 10  ? 0.1006 0.1247 0.1296 -0.0095 0.0121  0.0294  10  LEU   A C   
195  O O   A LEU   A 10  ? 0.1067 0.1199 0.1390 -0.0218 0.0130  0.0376  10  LEU   A O   
196  O O   B LEU   A 10  ? 0.0975 0.1173 0.1345 -0.0091 0.0092  0.0346  10  LEU   A O   
197  C CB  A LEU   A 10  ? 0.1228 0.1376 0.1833 -0.0114 0.0092  0.0468  10  LEU   A CB  
198  C CB  B LEU   A 10  ? 0.1077 0.1323 0.1621 -0.0044 0.0077  0.0263  10  LEU   A CB  
199  C CG  A LEU   A 10  ? 0.1457 0.1555 0.2165 -0.0123 -0.0061 0.0544  10  LEU   A CG  
200  C CG  B LEU   A 10  ? 0.1241 0.1455 0.1798 -0.0014 0.0054  0.0072  10  LEU   A CG  
201  C CD1 A LEU   A 10  ? 0.1611 0.1622 0.2291 -0.0249 -0.0023 0.0517  10  LEU   A CD1 
202  C CD1 B LEU   A 10  ? 0.1404 0.1523 0.2155 -0.0165 0.0087  0.0033  10  LEU   A CD1 
203  C CD2 A LEU   A 10  ? 0.1445 0.1701 0.2298 0.0055  0.0027  0.0416  10  LEU   A CD2 
204  C CD2 B LEU   A 10  ? 0.1448 0.1645 0.2211 0.0023  -0.0137 -0.0001 10  LEU   A CD2 
227  N N   A LYS   A 11  ? 0.1110 0.1183 0.1348 -0.0192 0.0224  0.0292  11  LYS   A N   
228  N N   B LYS   A 11  ? 0.1054 0.1251 0.1121 -0.0104 0.0072  0.0291  11  LYS   A N   
229  C CA  A LYS   A 11  ? 0.1071 0.1118 0.1400 -0.0215 0.0194  0.0246  11  LYS   A CA  
230  C CA  B LYS   A 11  ? 0.1108 0.1181 0.1261 -0.0179 0.0073  0.0277  11  LYS   A CA  
231  C C   A LYS   A 11  ? 0.1084 0.1155 0.1424 -0.0162 0.0209  0.0115  11  LYS   A C   
232  C C   B LYS   A 11  ? 0.1056 0.1018 0.1239 -0.0192 0.0106  0.0200  11  LYS   A C   
233  O O   A LYS   A 11  ? 0.1190 0.1191 0.1714 -0.0307 0.0302  0.0028  11  LYS   A O   
234  O O   B LYS   A 11  ? 0.1012 0.0981 0.1536 -0.0215 0.0171  0.0027  11  LYS   A O   
235  C CB  A LYS   A 11  ? 0.1150 0.1113 0.1491 -0.0201 0.0158  0.0298  11  LYS   A CB  
236  C CB  B LYS   A 11  ? 0.1248 0.1196 0.1343 -0.0174 0.0078  0.0286  11  LYS   A CB  
237  C CG  A LYS   A 11  ? 0.1243 0.1113 0.1494 -0.0235 0.0192  0.0270  11  LYS   A CG  
238  C CG  B LYS   A 11  ? 0.1397 0.1251 0.1289 -0.0201 0.0050  0.0194  11  LYS   A CG  
239  C CD  A LYS   A 11  ? 0.1362 0.1144 0.1534 -0.0181 0.0175  0.0274  11  LYS   A CD  
240  C CD  B LYS   A 11  ? 0.1499 0.1345 0.1305 -0.0189 0.0070  0.0269  11  LYS   A CD  
241  C CE  A LYS   A 11  ? 0.1454 0.1026 0.1533 -0.0116 0.0084  0.0288  11  LYS   A CE  
242  C CE  B LYS   A 11  ? 0.1532 0.1298 0.1207 -0.0173 0.0015  0.0330  11  LYS   A CE  
243  N NZ  A LYS   A 11  ? 0.1435 0.0952 0.1551 -0.0022 -0.0028 0.0099  11  LYS   A NZ  
244  N NZ  B LYS   A 11  ? 0.1479 0.1271 0.1058 -0.0130 -0.0145 0.0256  11  LYS   A NZ  
271  N N   A LEU   A 12  ? 0.1000 0.1103 0.1216 -0.0175 0.0186  0.0087  12  LEU   A N   
272  N N   B LEU   A 12  ? 0.1042 0.1158 0.1111 -0.0162 0.0029  0.0216  12  LEU   A N   
273  C CA  A LEU   A 12  ? 0.1044 0.1121 0.1225 -0.0135 0.0111  0.0110  12  LEU   A CA  
274  C CA  B LEU   A 12  ? 0.1082 0.1291 0.1127 -0.0149 0.0067  0.0221  12  LEU   A CA  
275  C C   A LEU   A 12  ? 0.1071 0.1055 0.1399 -0.0174 0.0039  0.0142  12  LEU   A C   
276  C C   B LEU   A 12  ? 0.1132 0.1255 0.1159 -0.0159 0.0181  0.0265  12  LEU   A C   
277  O O   A LEU   A 12  ? 0.1155 0.1131 0.1469 -0.0238 0.0050  0.0048  12  LEU   A O   
278  O O   B LEU   A 12  ? 0.1232 0.1247 0.1106 -0.0082 0.0120  0.0225  12  LEU   A O   
279  C CB  A LEU   A 12  ? 0.1154 0.1091 0.1191 -0.0135 0.0075  0.0104  12  LEU   A CB  
280  C CB  B LEU   A 12  ? 0.1135 0.1344 0.1171 -0.0165 0.0038  0.0203  12  LEU   A CB  
281  C CG  A LEU   A 12  ? 0.1317 0.1170 0.1312 -0.0074 0.0120  0.0116  12  LEU   A CG  
282  C CG  B LEU   A 12  ? 0.1196 0.1328 0.1104 -0.0142 0.0113  0.0086  12  LEU   A CG  
283  C CD1 A LEU   A 12  ? 0.1461 0.1170 0.1398 0.0058  0.0176  0.0303  12  LEU   A CD1 
284  C CD1 B LEU   A 12  ? 0.1318 0.1403 0.1225 -0.0038 0.0255  0.0106  12  LEU   A CD1 
285  C CD2 A LEU   A 12  ? 0.1353 0.1224 0.1494 -0.0032 0.0167  0.0102  12  LEU   A CD2 
286  C CD2 B LEU   A 12  ? 0.1180 0.1300 0.1181 -0.0101 0.0110  -0.0086 12  LEU   A CD2 
309  N N   A THR   A 13  ? 0.1035 0.1043 0.1479 -0.0181 -0.0033 0.0134  13  THR   A N   
310  N N   B THR   A 13  ? 0.1077 0.1218 0.1330 -0.0167 0.0154  0.0171  13  THR   A N   
311  C CA  A THR   A 13  ? 0.1077 0.1116 0.1544 -0.0100 0.0064  0.0126  13  THR   A CA  
312  C CA  B THR   A 13  ? 0.1069 0.1184 0.1464 -0.0157 0.0232  0.0152  13  THR   A CA  
313  C C   A THR   A 13  ? 0.1090 0.1093 0.1572 -0.0101 0.0035  0.0243  13  THR   A C   
314  C C   B THR   A 13  ? 0.1124 0.1182 0.1523 -0.0170 0.0307  0.0263  13  THR   A C   
315  O O   A THR   A 13  ? 0.1051 0.1132 0.1485 -0.0013 0.0060  0.0223  13  THR   A O   
316  O O   B THR   A 13  ? 0.1182 0.1204 0.1559 -0.0128 0.0180  0.0258  13  THR   A O   
317  C CB  A THR   A 13  ? 0.1193 0.1236 0.1595 -0.0126 0.0073  0.0181  13  THR   A CB  
318  C CB  B THR   A 13  ? 0.1108 0.1316 0.1595 -0.0169 0.0258  0.0184  13  THR   A CB  
319  O OG1 A THR   A 13  ? 0.1225 0.1121 0.1662 -0.0090 0.0013  0.0212  13  THR   A OG1 
320  O OG1 B THR   A 13  ? 0.0961 0.1270 0.1644 -0.0170 0.0296  0.0160  13  THR   A OG1 
321  C CG2 A THR   A 13  ? 0.1287 0.1435 0.1858 -0.0157 0.0080  0.0148  13  THR   A CG2 
322  C CG2 B THR   A 13  ? 0.1200 0.1511 0.1797 -0.0158 0.0268  0.0138  13  THR   A CG2 
337  N N   A ASP   A 14  ? 0.1080 0.1172 0.1705 -0.0109 0.0037  0.0270  14  ASP   A N   
338  N N   B ASP   A 14  ? 0.1126 0.1187 0.1563 -0.0185 0.0248  0.0322  14  ASP   A N   
339  C CA  A ASP   A 14  ? 0.1133 0.1204 0.1775 -0.0096 -0.0025 0.0363  14  ASP   A CA  
340  C CA  B ASP   A 14  ? 0.1247 0.1201 0.1811 -0.0116 0.0125  0.0404  14  ASP   A CA  
341  C C   A ASP   A 14  ? 0.1121 0.1185 0.1634 -0.0075 -0.0102 0.0352  14  ASP   A C   
342  C C   B ASP   A 14  ? 0.1130 0.1152 0.1725 -0.0112 0.0036  0.0420  14  ASP   A C   
343  O O   A ASP   A 14  ? 0.1187 0.1186 0.1588 -0.0027 -0.0204 0.0385  14  ASP   A O   
344  O O   B ASP   A 14  ? 0.1186 0.1137 0.1909 -0.0127 0.0024  0.0555  14  ASP   A O   
345  C CB  A ASP   A 14  ? 0.1317 0.1323 0.2219 -0.0153 0.0004  0.0438  14  ASP   A CB  
346  C CB  B ASP   A 14  ? 0.1535 0.1203 0.2320 -0.0085 0.0030  0.0500  14  ASP   A CB  
347  C CG  A ASP   A 14  ? 0.1541 0.1567 0.2813 -0.0159 -0.0030 0.0476  14  ASP   A CG  
348  C CG  B ASP   A 14  ? 0.1746 0.1418 0.2917 -0.0053 -0.0056 0.0512  14  ASP   A CG  
349  O OD1 A ASP   A 14  ? 0.1630 0.1620 0.3053 -0.0256 -0.0083 0.0389  14  ASP   A OD1 
350  O OD1 B ASP   A 14  ? 0.1885 0.1564 0.3103 0.0035  -0.0150 0.0514  14  ASP   A OD1 
351  O OD2 A ASP   A 14  ? 0.1684 0.1764 0.3122 -0.0071 -0.0095 0.0496  14  ASP   A OD2 
352  O OD2 B ASP   A 14  ? 0.1860 0.1470 0.3066 -0.0042 -0.0182 0.0564  14  ASP   A OD2 
361  N N   . ASN   A 15  ? 0.1078 0.1167 0.1674 -0.0169 0.0047  0.0428  15  ASN   A N   
362  C CA  . ASN   A 15  ? 0.1078 0.1186 0.1805 -0.0159 -0.0109 0.0348  15  ASN   A CA  
363  C C   . ASN   A 15  ? 0.1095 0.1165 0.1903 -0.0170 -0.0013 0.0350  15  ASN   A C   
364  O O   . ASN   A 15  ? 0.1135 0.1192 0.2407 -0.0181 -0.0194 0.0335  15  ASN   A O   
365  C CB  . ASN   A 15  ? 0.1089 0.1171 0.1820 -0.0092 -0.0065 0.0293  15  ASN   A CB  
366  C CG  . ASN   A 15  ? 0.1096 0.1231 0.1754 -0.0044 -0.0017 0.0202  15  ASN   A CG  
367  O OD1 . ASN   A 15  ? 0.1232 0.1361 0.1832 -0.0244 -0.0008 0.0242  15  ASN   A OD1 
368  N ND2 . ASN   A 15  ? 0.1142 0.1354 0.1761 -0.0163 0.0142  0.0248  15  ASN   A ND2 
376  N N   . VAL   A 16  ? 0.1093 0.1135 0.1658 -0.0107 0.0005  0.0351  16  VAL   A N   
377  C CA  . VAL   A 16  ? 0.1071 0.1127 0.1650 -0.0106 0.0059  0.0311  16  VAL   A CA  
378  C C   . VAL   A 16  ? 0.1000 0.1165 0.1463 -0.0157 0.0006  0.0319  16  VAL   A C   
379  O O   . VAL   A 16  ? 0.0984 0.1138 0.1593 -0.0183 0.0063  0.0292  16  VAL   A O   
380  C CB  . VAL   A 16  ? 0.1213 0.1242 0.1540 0.0017  0.0210  0.0388  16  VAL   A CB  
381  C CG1 . VAL   A 16  ? 0.1374 0.1357 0.1568 0.0136  0.0217  0.0373  16  VAL   A CG1 
382  C CG2 . VAL   A 16  ? 0.1331 0.1404 0.1642 0.0081  0.0361  0.0358  16  VAL   A CG2 
392  N N   A TYR   A 17  ? 0.0979 0.1114 0.1424 -0.0089 0.0112  0.0313  17  TYR   A N   
393  N N   B TYR   A 17  ? 0.1007 0.1143 0.1434 -0.0197 0.0095  0.0367  17  TYR   A N   
394  C CA  A TYR   A 17  ? 0.1010 0.1122 0.1293 -0.0046 0.0064  0.0294  17  TYR   A CA  
395  C CA  B TYR   A 17  ? 0.1063 0.1181 0.1299 -0.0227 0.0058  0.0405  17  TYR   A CA  
396  C C   A TYR   A 17  ? 0.1044 0.1066 0.1442 -0.0053 0.0092  0.0214  17  TYR   A C   
397  C C   B TYR   A 17  ? 0.1028 0.1208 0.1367 -0.0211 0.0092  0.0346  17  TYR   A C   
398  O O   A TYR   A 17  ? 0.1008 0.0968 0.1587 -0.0044 0.0157  0.0268  17  TYR   A O   
399  O O   B TYR   A 17  ? 0.0989 0.1231 0.1440 -0.0191 0.0141  0.0468  17  TYR   A O   
400  C CB  A TYR   A 17  ? 0.1093 0.1191 0.1251 -0.0028 0.0046  0.0238  17  TYR   A CB  
401  C CB  B TYR   A 17  ? 0.1228 0.1201 0.1323 -0.0288 0.0005  0.0424  17  TYR   A CB  
402  C CG  A TYR   A 17  ? 0.1200 0.1284 0.1316 -0.0032 -0.0079 0.0215  17  TYR   A CG  
403  C CG  B TYR   A 17  ? 0.1394 0.1280 0.1375 -0.0300 -0.0109 0.0346  17  TYR   A CG  
404  C CD1 A TYR   A 17  ? 0.1221 0.1295 0.1392 0.0024  -0.0071 0.0292  17  TYR   A CD1 
405  C CD1 B TYR   A 17  ? 0.1439 0.1357 0.1423 -0.0228 -0.0105 0.0391  17  TYR   A CD1 
406  C CD2 A TYR   A 17  ? 0.1234 0.1310 0.1334 -0.0024 -0.0031 0.0239  17  TYR   A CD2 
407  C CD2 B TYR   A 17  ? 0.1509 0.1259 0.1330 -0.0397 -0.0066 0.0435  17  TYR   A CD2 
408  C CE1 A TYR   A 17  ? 0.1229 0.1306 0.1363 -0.0017 -0.0019 0.0259  17  TYR   A CE1 
409  C CE1 B TYR   A 17  ? 0.1511 0.1379 0.1471 -0.0234 -0.0205 0.0409  17  TYR   A CE1 
410  C CE2 A TYR   A 17  ? 0.1247 0.1284 0.1357 0.0024  -0.0030 0.0131  17  TYR   A CE2 
411  C CE2 B TYR   A 17  ? 0.1612 0.1300 0.1289 -0.0364 -0.0126 0.0339  17  TYR   A CE2 
412  C CZ  A TYR   A 17  ? 0.1218 0.1279 0.1327 -0.0000 -0.0044 0.0196  17  TYR   A CZ  
413  C CZ  B TYR   A 17  ? 0.1634 0.1327 0.1387 -0.0322 -0.0213 0.0376  17  TYR   A CZ  
414  O OH  A TYR   A 17  ? 0.1226 0.1292 0.1308 0.0035  0.0055  0.0245  17  TYR   A OH  
415  O OH  B TYR   A 17  ? 0.1807 0.1284 0.1545 -0.0292 -0.0280 0.0410  17  TYR   A OH  
434  N N   A ILE   A 18  ? 0.1093 0.1089 0.1414 -0.0030 0.0125  0.0301  18  ILE   A N   
435  N N   B ILE   A 18  ? 0.1006 0.1184 0.1264 -0.0192 0.0151  0.0371  18  ILE   A N   
436  C CA  A ILE   A 18  ? 0.1114 0.1110 0.1401 0.0007  0.0151  0.0222  18  ILE   A CA  
437  C CA  B ILE   A 18  ? 0.0974 0.1151 0.1130 -0.0187 0.0201  0.0233  18  ILE   A CA  
438  C C   A ILE   A 18  ? 0.1094 0.1154 0.1456 -0.0057 0.0058  0.0229  18  ILE   A C   
439  C C   B ILE   A 18  ? 0.0932 0.1262 0.0916 -0.0215 0.0029  0.0172  18  ILE   A C   
440  O O   A ILE   A 18  ? 0.1102 0.1218 0.1523 -0.0067 0.0140  0.0328  18  ILE   A O   
441  O O   B ILE   A 18  ? 0.0946 0.1361 0.1139 -0.0260 0.0207  0.0157  18  ILE   A O   
442  C CB  A ILE   A 18  ? 0.1189 0.1099 0.1198 0.0107  0.0132  0.0233  18  ILE   A CB  
443  C CB  B ILE   A 18  ? 0.1083 0.1081 0.1031 -0.0060 0.0248  0.0247  18  ILE   A CB  
444  C CG1 A ILE   A 18  ? 0.1201 0.1047 0.0932 0.0181  0.0200  0.0253  18  ILE   A CG1 
445  C CG1 B ILE   A 18  ? 0.1247 0.1158 0.1222 -0.0088 0.0257  0.0167  18  ILE   A CG1 
446  C CG2 A ILE   A 18  ? 0.1184 0.1160 0.1322 0.0125  0.0020  0.0144  18  ILE   A CG2 
447  C CG2 B ILE   A 18  ? 0.1132 0.1166 0.1329 -0.0128 0.0086  0.0289  18  ILE   A CG2 
448  C CD1 A ILE   A 18  ? 0.1460 0.1055 0.1158 0.0206  0.0078  0.0222  18  ILE   A CD1 
449  C CD1 B ILE   A 18  ? 0.1457 0.1291 0.1500 -0.0021 0.0275  0.0046  18  ILE   A CD1 
472  N N   A LYS   A 19  ? 0.1041 0.1164 0.1414 -0.0082 0.0056  0.0128  19  LYS   A N   
473  N N   B LYS   A 19  ? 0.0970 0.1301 0.0823 -0.0162 0.0065  0.0142  19  LYS   A N   
474  C CA  A LYS   A 19  ? 0.1080 0.1220 0.1381 -0.0095 0.0048  0.0186  19  LYS   A CA  
475  C CA  B LYS   A 19  ? 0.1043 0.1403 0.0831 -0.0090 0.0079  0.0092  19  LYS   A CA  
476  C C   A LYS   A 19  ? 0.1060 0.1218 0.1405 -0.0023 0.0132  0.0208  19  LYS   A C   
477  C C   B LYS   A 19  ? 0.1053 0.1481 0.1058 0.0055  0.0145  0.0039  19  LYS   A C   
478  O O   A LYS   A 19  ? 0.1100 0.1175 0.1397 -0.0000 0.0103  0.0193  19  LYS   A O   
479  O O   B LYS   A 19  ? 0.1116 0.1389 0.1064 0.0097  0.0180  0.0103  19  LYS   A O   
480  C CB  A LYS   A 19  ? 0.1122 0.1316 0.1416 -0.0064 -0.0072 0.0117  19  LYS   A CB  
481  C CB  B LYS   A 19  ? 0.1096 0.1545 0.0891 -0.0168 0.0085  0.0012  19  LYS   A CB  
482  C CG  A LYS   A 19  ? 0.1356 0.1478 0.1560 -0.0072 -0.0093 -0.0048 19  LYS   A CG  
483  C CG  B LYS   A 19  ? 0.1251 0.1642 0.0844 -0.0169 0.0069  -0.0005 19  LYS   A CG  
484  C CD  A LYS   A 19  ? 0.1485 0.1668 0.1642 -0.0090 -0.0067 -0.0126 19  LYS   A CD  
485  C CD  B LYS   A 19  ? 0.1308 0.1763 0.0984 -0.0164 0.0147  0.0047  19  LYS   A CD  
486  C CE  A LYS   A 19  ? 0.1580 0.1791 0.1727 -0.0143 -0.0064 -0.0154 19  LYS   A CE  
487  C CE  B LYS   A 19  ? 0.1361 0.1831 0.1119 -0.0204 -0.0047 -0.0005 19  LYS   A CE  
488  N NZ  A LYS   A 19  ? 0.1644 0.1896 0.1613 -0.0186 -0.0097 -0.0202 19  LYS   A NZ  
489  N NZ  B LYS   A 19  ? 0.1401 0.1877 0.1234 -0.0253 -0.0014 0.0049  19  LYS   A NZ  
516  N N   A ASN   A 20  ? 0.1177 0.1301 0.1667 0.0013  0.0246  0.0304  20  ASN   A N   
517  N N   B ASN   A 20  ? 0.1151 0.1668 0.1298 0.0195  0.0187  -0.0006 20  ASN   A N   
518  C CA  A ASN   A 20  ? 0.1429 0.1415 0.1866 0.0291  0.0458  0.0270  20  ASN   A CA  
519  C CA  B ASN   A 20  ? 0.1260 0.1825 0.1454 0.0333  0.0355  0.0082  20  ASN   A CA  
520  C C   A ASN   A 20  ? 0.1720 0.1416 0.2034 0.0301  0.0445  0.0183  20  ASN   A C   
521  C C   B ASN   A 20  ? 0.1467 0.1752 0.1350 0.0340  0.0393  -0.0007 20  ASN   A C   
522  O O   A ASN   A 20  ? 0.1916 0.1460 0.2232 0.0202  0.0496  0.0039  20  ASN   A O   
523  O O   B ASN   A 20  ? 0.1700 0.1836 0.1513 0.0207  0.0475  -0.0156 20  ASN   A O   
524  C CB  A ASN   A 20  ? 0.1512 0.1496 0.2060 0.0347  0.0470  0.0459  20  ASN   A CB  
525  C CB  B ASN   A 20  ? 0.1239 0.1978 0.1880 0.0349  0.0364  0.0340  20  ASN   A CB  
526  C CG  A ASN   A 20  ? 0.1578 0.1435 0.2277 0.0393  0.0482  0.0537  20  ASN   A CG  
527  C CG  B ASN   A 20  ? 0.1217 0.2049 0.2361 0.0334  0.0418  0.0516  20  ASN   A CG  
528  O OD1 A ASN   A 20  ? 0.1665 0.1484 0.2495 0.0240  0.0604  0.0434  20  ASN   A OD1 
529  O OD1 B ASN   A 20  ? 0.1275 0.2187 0.2802 0.0380  0.0547  0.0457  20  ASN   A OD1 
530  N ND2 A ASN   A 20  ? 0.1688 0.1458 0.2376 0.0448  0.0336  0.0533  20  ASN   A ND2 
531  N ND2 B ASN   A 20  ? 0.1251 0.2006 0.2331 0.0283  0.0319  0.0681  20  ASN   A ND2 
544  N N   A ALA   A 21  ? 0.1807 0.1396 0.2018 0.0273  0.0340  0.0149  21  ALA   A N   
545  N N   B ALA   A 21  ? 0.1516 0.1689 0.1390 0.0335  0.0172  -0.0048 21  ALA   A N   
546  C CA  A ALA   A 21  ? 0.1882 0.1434 0.1968 0.0208  0.0370  0.0172  21  ALA   A CA  
547  C CA  B ALA   A 21  ? 0.1567 0.1695 0.1632 0.0333  0.0078  0.0000  21  ALA   A CA  
548  C C   A ALA   A 21  ? 0.1841 0.1370 0.1869 0.0255  0.0529  0.0174  21  ALA   A C   
549  C C   B ALA   A 21  ? 0.1560 0.1640 0.1707 0.0238  0.0094  0.0063  21  ALA   A C   
550  O O   A ALA   A 21  ? 0.1847 0.1438 0.1917 0.0340  0.0566  0.0095  21  ALA   A O   
551  O O   B ALA   A 21  ? 0.1542 0.1660 0.1682 0.0113  0.0070  0.0076  21  ALA   A O   
552  C CB  A ALA   A 21  ? 0.2022 0.1554 0.2106 0.0059  0.0229  0.0283  21  ALA   A CB  
553  C CB  B ALA   A 21  ? 0.1662 0.1779 0.1840 0.0264  -0.0072 0.0100  21  ALA   A CB  
564  N N   A ASP   A 22  ? 0.1791 0.1316 0.1938 0.0172  0.0515  0.0079  22  ASP   A N   
565  N N   B ASP   A 22  ? 0.1534 0.1600 0.1806 0.0162  0.0122  0.0053  22  ASP   A N   
566  C CA  A ASP   A 22  ? 0.1746 0.1380 0.1916 0.0111  0.0453  0.0013  22  ASP   A CA  
567  C CA  B ASP   A 22  ? 0.1470 0.1615 0.1849 0.0106  0.0066  0.0031  22  ASP   A CA  
568  C C   A ASP   A 22  ? 0.1592 0.1446 0.1609 0.0090  0.0550  0.0075  22  ASP   A C   
569  C C   B ASP   A 22  ? 0.1453 0.1640 0.1707 0.0032  0.0106  0.0106  22  ASP   A C   
570  O O   A ASP   A 22  ? 0.1624 0.1577 0.1698 0.0093  0.0569  0.0092  22  ASP   A O   
571  O O   B ASP   A 22  ? 0.1467 0.1696 0.1703 -0.0050 0.0171  0.0231  22  ASP   A O   
572  C CB  A ASP   A 22  ? 0.1926 0.1486 0.2290 0.0077  0.0315  -0.0113 22  ASP   A CB  
573  C CB  B ASP   A 22  ? 0.1479 0.1610 0.2156 0.0106  0.0035  0.0059  22  ASP   A CB  
574  C CG  A ASP   A 22  ? 0.2055 0.1631 0.2721 0.0007  0.0163  -0.0181 22  ASP   A CG  
575  C CG  B ASP   A 22  ? 0.1440 0.1576 0.2397 0.0083  -0.0019 0.0137  22  ASP   A CG  
576  O OD1 A ASP   A 22  ? 0.2124 0.1728 0.2812 -0.0069 0.0154  -0.0161 22  ASP   A OD1 
577  O OD1 B ASP   A 22  ? 0.1396 0.1449 0.2409 -0.0060 -0.0036 0.0150  22  ASP   A OD1 
578  O OD2 A ASP   A 22  ? 0.2111 0.1724 0.3058 0.0000  0.0017  -0.0271 22  ASP   A OD2 
579  O OD2 B ASP   A 22  ? 0.1427 0.1680 0.2547 0.0198  0.0085  0.0143  22  ASP   A OD2 
588  N N   A ILE   A 23  ? 0.1503 0.1352 0.1401 0.0070  0.0459  0.0038  23  ILE   A N   
589  N N   B ILE   A 23  ? 0.1469 0.1610 0.1584 0.0038  0.0054  0.0054  23  ILE   A N   
590  C CA  A ILE   A 23  ? 0.1480 0.1314 0.1333 0.0008  0.0351  0.0094  23  ILE   A CA  
591  C CA  B ILE   A 23  ? 0.1488 0.1548 0.1451 0.0005  0.0148  -0.0022 23  ILE   A CA  
592  C C   A ILE   A 23  ? 0.1484 0.1523 0.1285 0.0005  0.0334  0.0048  23  ILE   A C   
593  C C   B ILE   A 23  ? 0.1491 0.1623 0.1414 0.0030  0.0241  -0.0069 23  ILE   A C   
594  O O   A ILE   A 23  ? 0.1515 0.1619 0.1244 0.0001  0.0266  0.0005  23  ILE   A O   
595  O O   B ILE   A 23  ? 0.1518 0.1728 0.1475 0.0021  0.0192  -0.0098 23  ILE   A O   
596  C CB  A ILE   A 23  ? 0.1513 0.1241 0.1199 0.0083  0.0226  0.0149  23  ILE   A CB  
597  C CB  B ILE   A 23  ? 0.1547 0.1538 0.1303 0.0023  0.0106  -0.0035 23  ILE   A CB  
598  C CG1 A ILE   A 23  ? 0.1566 0.1280 0.1238 0.0067  0.0231  0.0131  23  ILE   A CG1 
599  C CG1 B ILE   A 23  ? 0.1597 0.1550 0.1274 0.0109  0.0125  -0.0029 23  ILE   A CG1 
600  C CG2 A ILE   A 23  ? 0.1547 0.1199 0.1247 0.0097  0.0274  0.0197  23  ILE   A CG2 
601  C CG2 B ILE   A 23  ? 0.1563 0.1586 0.1427 0.0021  0.0172  -0.0002 23  ILE   A CG2 
602  C CD1 A ILE   A 23  ? 0.1631 0.1258 0.1187 0.0043  0.0188  0.0098  23  ILE   A CD1 
603  C CD1 B ILE   A 23  ? 0.1656 0.1563 0.1324 0.0114  0.0123  -0.0076 23  ILE   A CD1 
626  N N   A VAL   A 24  ? 0.1505 0.1625 0.1440 -0.0072 0.0261  -0.0003 24  VAL   A N   
627  N N   B VAL   A 24  ? 0.1519 0.1624 0.1436 0.0012  0.0234  -0.0142 24  VAL   A N   
628  C CA  A VAL   A 24  ? 0.1612 0.1774 0.1667 -0.0125 0.0251  -0.0052 24  VAL   A CA  
629  C CA  B VAL   A 24  ? 0.1633 0.1691 0.1529 -0.0039 0.0179  -0.0243 24  VAL   A CA  
630  C C   A VAL   A 24  ? 0.1671 0.1901 0.1699 -0.0100 0.0330  -0.0192 24  VAL   A C   
631  C C   B VAL   A 24  ? 0.1708 0.1800 0.1657 -0.0073 0.0197  -0.0238 24  VAL   A C   
632  O O   A VAL   A 24  ? 0.1734 0.1884 0.1639 -0.0040 0.0336  -0.0158 24  VAL   A O   
633  O O   B VAL   A 24  ? 0.1807 0.1778 0.1606 -0.0035 0.0188  -0.0220 24  VAL   A O   
634  C CB  A VAL   A 24  ? 0.1629 0.1889 0.1983 -0.0213 0.0264  0.0045  24  VAL   A CB  
635  C CB  B VAL   A 24  ? 0.1643 0.1724 0.1635 -0.0046 0.0236  -0.0353 24  VAL   A CB  
636  C CG1 A VAL   A 24  ? 0.1757 0.2022 0.2206 -0.0213 0.0234  0.0029  24  VAL   A CG1 
637  C CG1 B VAL   A 24  ? 0.1756 0.1827 0.1841 -0.0044 0.0260  -0.0385 24  VAL   A CG1 
638  C CG2 A VAL   A 24  ? 0.1651 0.1948 0.2187 -0.0251 0.0318  0.0139  24  VAL   A CG2 
639  C CG2 B VAL   A 24  ? 0.1683 0.1752 0.1799 -0.0021 0.0285  -0.0342 24  VAL   A CG2 
658  N N   A GLU   A 25  ? 0.1722 0.2114 0.1782 -0.0122 0.0511  -0.0296 25  GLU   A N   
659  N N   B GLU   A 25  ? 0.1749 0.2001 0.1796 -0.0136 0.0329  -0.0218 25  GLU   A N   
660  C CA  A GLU   A 25  ? 0.1887 0.2357 0.1900 -0.0120 0.0683  -0.0323 25  GLU   A CA  
661  C CA  B GLU   A 25  ? 0.1899 0.2211 0.1913 -0.0135 0.0494  -0.0202 25  GLU   A CA  
662  C C   A GLU   A 25  ? 0.1843 0.2380 0.1644 -0.0241 0.0654  -0.0322 25  GLU   A C   
663  C C   B GLU   A 25  ? 0.1821 0.2213 0.1632 -0.0190 0.0449  -0.0198 25  GLU   A C   
664  O O   A GLU   A 25  ? 0.1947 0.2471 0.1631 -0.0264 0.0626  -0.0333 25  GLU   A O   
665  O O   B GLU   A 25  ? 0.1931 0.2301 0.1670 -0.0225 0.0400  -0.0210 25  GLU   A O   
666  C CB  A GLU   A 25  ? 0.2063 0.2543 0.2327 -0.0038 0.0848  -0.0307 25  GLU   A CB  
667  C CB  B GLU   A 25  ? 0.2141 0.2416 0.2413 -0.0149 0.0644  -0.0120 25  GLU   A CB  
668  C CG  A GLU   A 25  ? 0.2267 0.2718 0.2840 0.0021  0.0825  -0.0298 25  GLU   A CG  
669  C CG  B GLU   A 25  ? 0.2413 0.2617 0.2997 -0.0165 0.0672  -0.0058 25  GLU   A CG  
670  C CD  A GLU   A 25  ? 0.2412 0.2875 0.3295 0.0045  0.0766  -0.0235 25  GLU   A CD  
671  C CD  B GLU   A 25  ? 0.2616 0.2800 0.3436 -0.0200 0.0715  0.0008  25  GLU   A CD  
672  O OE1 A GLU   A 25  ? 0.2455 0.2942 0.3396 0.0061  0.0624  -0.0222 25  GLU   A OE1 
673  O OE1 B GLU   A 25  ? 0.2689 0.2877 0.3502 -0.0185 0.0730  0.0045  25  GLU   A OE1 
674  O OE2 A GLU   A 25  ? 0.2460 0.2926 0.3461 0.0053  0.0805  -0.0249 25  GLU   A OE2 
675  O OE2 B GLU   A 25  ? 0.2729 0.2842 0.3597 -0.0234 0.0737  -0.0005 25  GLU   A OE2 
688  N N   A GLU   A 26  ? 0.1729 0.2290 0.1702 -0.0381 0.0644  -0.0287 26  GLU   A N   
689  N N   B GLU   A 26  ? 0.1664 0.2126 0.1577 -0.0250 0.0453  -0.0189 26  GLU   A N   
690  C CA  A GLU   A 26  ? 0.1810 0.2274 0.1532 -0.0483 0.0602  -0.0205 26  GLU   A CA  
691  C CA  B GLU   A 26  ? 0.1669 0.2067 0.1236 -0.0351 0.0449  -0.0139 26  GLU   A CA  
692  C C   A GLU   A 26  ? 0.1812 0.2136 0.1319 -0.0491 0.0465  -0.0181 26  GLU   A C   
693  C C   B GLU   A 26  ? 0.1766 0.2033 0.1272 -0.0396 0.0387  -0.0095 26  GLU   A C   
694  O O   A GLU   A 26  ? 0.1884 0.2156 0.1280 -0.0560 0.0466  -0.0217 26  GLU   A O   
695  O O   B GLU   A 26  ? 0.1880 0.2052 0.1481 -0.0414 0.0383  -0.0016 26  GLU   A O   
696  C CB  A GLU   A 26  ? 0.1893 0.2339 0.1736 -0.0538 0.0572  -0.0154 26  GLU   A CB  
697  C CB  B GLU   A 26  ? 0.1579 0.1943 0.1061 -0.0338 0.0438  -0.0115 26  GLU   A CB  
698  C CG  A GLU   A 26  ? 0.1998 0.2357 0.1957 -0.0563 0.0471  -0.0138 26  GLU   A CG  
699  C CG  B GLU   A 26  ? 0.1480 0.1769 0.1095 -0.0327 0.0393  -0.0122 26  GLU   A CG  
700  C CD  A GLU   A 26  ? 0.2018 0.2368 0.2134 -0.0599 0.0484  -0.0137 26  GLU   A CD  
701  C CD  B GLU   A 26  ? 0.1446 0.1663 0.1203 -0.0341 0.0427  -0.0154 26  GLU   A CD  
702  O OE1 A GLU   A 26  ? 0.2063 0.2477 0.2259 -0.0559 0.0483  -0.0078 26  GLU   A OE1 
703  O OE1 B GLU   A 26  ? 0.1454 0.1680 0.1409 -0.0294 0.0516  -0.0119 26  GLU   A OE1 
704  O OE2 A GLU   A 26  ? 0.2002 0.2349 0.2337 -0.0623 0.0536  -0.0180 26  GLU   A OE2 
705  O OE2 B GLU   A 26  ? 0.1452 0.1610 0.1149 -0.0397 0.0432  0.0016  26  GLU   A OE2 
718  N N   . ALA   A 27  ? 0.1667 0.1961 0.1289 -0.0442 0.0437  -0.0112 27  ALA   A N   
719  C CA  . ALA   A 27  ? 0.1770 0.1930 0.1168 -0.0332 0.0417  -0.0071 27  ALA   A CA  
720  C C   . ALA   A 27  ? 0.2055 0.2113 0.1221 -0.0410 0.0457  -0.0263 27  ALA   A C   
721  O O   . ALA   A 27  ? 0.2059 0.2143 0.1174 -0.0477 0.0289  -0.0167 27  ALA   A O   
722  C CB  . ALA   A 27  ? 0.1660 0.1880 0.1182 -0.0321 0.0298  -0.0052 27  ALA   A CB  
729  N N   A LYS   A 28  ? 0.2315 0.2314 0.1395 -0.0366 0.0431  -0.0473 28  LYS   A N   
730  N N   B LYS   A 28  ? 0.2287 0.2256 0.1315 -0.0401 0.0437  -0.0494 28  LYS   A N   
731  C CA  A LYS   A 28  ? 0.2697 0.2632 0.1761 -0.0321 0.0414  -0.0660 28  LYS   A CA  
732  C CA  B LYS   A 28  ? 0.2648 0.2526 0.1594 -0.0389 0.0423  -0.0689 28  LYS   A CA  
733  C C   A LYS   A 28  ? 0.2896 0.2898 0.1680 -0.0383 0.0493  -0.0556 28  LYS   A C   
734  C C   B LYS   A 28  ? 0.2824 0.2752 0.1426 -0.0464 0.0519  -0.0615 28  LYS   A C   
735  O O   A LYS   A 28  ? 0.3007 0.3009 0.2070 -0.0372 0.0306  -0.0515 28  LYS   A O   
736  O O   B LYS   A 28  ? 0.2906 0.2809 0.1798 -0.0487 0.0294  -0.0568 28  LYS   A O   
737  C CB  A LYS   A 28  ? 0.2857 0.2721 0.2262 -0.0209 0.0369  -0.0871 28  LYS   A CB  
738  C CB  B LYS   A 28  ? 0.2806 0.2613 0.2105 -0.0291 0.0377  -0.0866 28  LYS   A CB  
739  C CG  A LYS   A 28  ? 0.3030 0.2823 0.2779 -0.0126 0.0278  -0.0896 28  LYS   A CG  
740  C CG  B LYS   A 28  ? 0.2986 0.2721 0.2600 -0.0226 0.0290  -0.0868 28  LYS   A CG  
741  C CD  A LYS   A 28  ? 0.3187 0.2971 0.3422 -0.0044 0.0174  -0.0812 28  LYS   A CD  
742  C CD  B LYS   A 28  ? 0.3157 0.2887 0.3288 -0.0160 0.0189  -0.0745 28  LYS   A CD  
743  C CE  A LYS   A 28  ? 0.3308 0.3079 0.3833 0.0003  0.0096  -0.0796 28  LYS   A CE  
744  C CE  B LYS   A 28  ? 0.3286 0.3006 0.3719 -0.0134 0.0114  -0.0711 28  LYS   A CE  
745  N NZ  A LYS   A 28  ? 0.3383 0.3140 0.4146 0.0035  0.0071  -0.0810 28  LYS   A NZ  
746  N NZ  B LYS   A 28  ? 0.3368 0.3072 0.4040 -0.0104 0.0098  -0.0710 28  LYS   A NZ  
773  N N   A LYS   A 29  ? 0.2951 0.3060 0.1595 -0.0451 0.0774  -0.0368 29  LYS   A N   
774  N N   B LYS   A 29  ? 0.2888 0.2946 0.1383 -0.0509 0.0830  -0.0434 29  LYS   A N   
775  C CA  A LYS   A 29  ? 0.3065 0.3251 0.1780 -0.0501 0.0906  -0.0224 29  LYS   A CA  
776  C CA  B LYS   A 29  ? 0.3022 0.3176 0.1657 -0.0542 0.0949  -0.0269 29  LYS   A CA  
777  C C   A LYS   A 29  ? 0.2978 0.3169 0.1362 -0.0594 0.0848  -0.0197 29  LYS   A C   
778  C C   B LYS   A 29  ? 0.2954 0.3133 0.1340 -0.0610 0.0856  -0.0219 29  LYS   A C   
779  O O   A LYS   A 29  ? 0.3070 0.3246 0.1464 -0.0532 0.0818  -0.0215 29  LYS   A O   
780  O O   B LYS   A 29  ? 0.3046 0.3214 0.1467 -0.0535 0.0807  -0.0249 29  LYS   A O   
781  C CB  A LYS   A 29  ? 0.3259 0.3524 0.2519 -0.0433 0.1012  -0.0114 29  LYS   A CB  
782  C CB  B LYS   A 29  ? 0.3222 0.3454 0.2449 -0.0477 0.1072  -0.0170 29  LYS   A CB  
783  C CG  A LYS   A 29  ? 0.3469 0.3770 0.3263 -0.0370 0.0994  -0.0037 29  LYS   A CG  
784  C CG  B LYS   A 29  ? 0.3441 0.3703 0.3244 -0.0425 0.1052  -0.0108 29  LYS   A CG  
785  C CD  A LYS   A 29  ? 0.3648 0.3969 0.3970 -0.0319 0.0946  -0.0001 29  LYS   A CD  
786  C CD  B LYS   A 29  ? 0.3626 0.3901 0.3982 -0.0390 0.1004  -0.0093 29  LYS   A CD  
787  C CE  A LYS   A 29  ? 0.3770 0.4111 0.4395 -0.0281 0.0944  0.0005  29  LYS   A CE  
788  C CE  B LYS   A 29  ? 0.3752 0.4042 0.4433 -0.0366 0.0996  -0.0100 29  LYS   A CE  
789  N NZ  A LYS   A 29  ? 0.3834 0.4189 0.4686 -0.0258 0.0939  -0.0007 29  LYS   A NZ  
790  N NZ  B LYS   A 29  ? 0.3819 0.4122 0.4734 -0.0350 0.0993  -0.0129 29  LYS   A NZ  
817  N N   . VAL   A 30  ? 0.2799 0.3002 0.1245 -0.0692 0.0745  -0.0171 30  VAL   A N   
818  C CA  . VAL   A 30  ? 0.2651 0.2823 0.1168 -0.0816 0.0452  0.0058  30  VAL   A CA  
819  C C   . VAL   A 30  ? 0.2621 0.2674 0.0986 -0.0815 0.0314  0.0153  30  VAL   A C   
820  O O   . VAL   A 30  ? 0.2773 0.2777 0.0985 -0.0798 0.0227  0.0220  30  VAL   A O   
821  C CB  . VAL   A 30  ? 0.2560 0.2767 0.1433 -0.0899 0.0220  0.0133  30  VAL   A CB  
822  C CG1 . VAL   A 30  ? 0.2607 0.2757 0.1575 -0.0855 0.0059  0.0149  30  VAL   A CG1 
823  C CG2 . VAL   A 30  ? 0.2527 0.2838 0.1714 -0.0986 0.0163  0.0107  30  VAL   A CG2 
834  N N   . LYS   A 31  ? 0.2557 0.2498 0.0894 -0.0867 0.0200  0.0058  31  LYS   A N   
835  C CA  . LYS   A 31  ? 0.2833 0.2557 0.0885 -0.0793 -0.0039 -0.0038 31  LYS   A CA  
836  C C   . LYS   A 31  ? 0.2545 0.2298 0.0828 -0.0622 0.0011  0.0278  31  LYS   A C   
837  O O   . LYS   A 31  ? 0.2561 0.2407 0.1018 -0.0559 -0.0108 0.0359  31  LYS   A O   
838  C CB  . LYS   A 31  ? 0.3434 0.2998 0.1835 -0.0853 -0.0318 -0.0276 31  LYS   A CB  
839  C CG  . LYS   A 31  ? 0.4163 0.3605 0.3352 -0.0790 -0.0498 -0.0352 31  LYS   A CG  
840  C CD  . LYS   A 31  ? 0.4688 0.4072 0.4563 -0.0726 -0.0635 -0.0400 31  LYS   A CD  
841  C CE  . LYS   A 31  ? 0.4977 0.4367 0.5259 -0.0688 -0.0737 -0.0478 31  LYS   A CE  
842  N NZ  . LYS   A 31  ? 0.5161 0.4610 0.5681 -0.0669 -0.0790 -0.0552 31  LYS   A NZ  
856  N N   . PRO   A 32  ? 0.2179 0.2023 0.0760 -0.0542 0.0055  0.0184  32  PRO   A N   
857  C CA  . PRO   A 32  ? 0.2092 0.1884 0.1058 -0.0473 -0.0048 0.0210  32  PRO   A CA  
858  C C   . PRO   A 32  ? 0.2074 0.1895 0.1078 -0.0335 -0.0167 0.0285  32  PRO   A C   
859  O O   . PRO   A 32  ? 0.1971 0.1840 0.1227 -0.0356 -0.0245 0.0340  32  PRO   A O   
860  C CB  . PRO   A 32  ? 0.2038 0.1976 0.1279 -0.0489 -0.0051 0.0128  32  PRO   A CB  
861  C CG  . PRO   A 32  ? 0.1933 0.1976 0.0845 -0.0438 -0.0094 0.0080  32  PRO   A CG  
862  C CD  . PRO   A 32  ? 0.1950 0.1941 0.0740 -0.0484 0.0013  0.0137  32  PRO   A CD  
870  N N   . THR   A 33  ? 0.2205 0.1897 0.1021 -0.0276 -0.0117 0.0346  33  THR   A N   
871  C CA  . THR   A 33  ? 0.2174 0.1899 0.1129 -0.0186 -0.0265 0.0389  33  THR   A CA  
872  C C   . THR   A 33  ? 0.1846 0.1727 0.1067 -0.0222 -0.0224 0.0285  33  THR   A C   
873  O O   . THR   A 33  ? 0.1771 0.1752 0.1138 -0.0226 -0.0392 0.0309  33  THR   A O   
874  C CB  . THR   A 33  ? 0.2464 0.2142 0.1192 -0.0086 -0.0406 0.0556  33  THR   A CB  
875  O OG1 . THR   A 33  ? 0.2742 0.2331 0.1511 -0.0009 -0.0294 0.0690  33  THR   A OG1 
876  C CG2 . THR   A 33  ? 0.2503 0.2246 0.1487 -0.0011 -0.0429 0.0534  33  THR   A CG2 
884  N N   . VAL   A 34  ? 0.1598 0.1580 0.0925 -0.0270 -0.0228 0.0273  34  VAL   A N   
885  C CA  . VAL   A 34  ? 0.1420 0.1462 0.0886 -0.0216 -0.0103 0.0241  34  VAL   A CA  
886  C C   . VAL   A 34  ? 0.1314 0.1374 0.0734 -0.0187 -0.0000 0.0114  34  VAL   A C   
887  O O   . VAL   A 34  ? 0.1372 0.1371 0.0985 -0.0266 -0.0032 0.0256  34  VAL   A O   
888  C CB  . VAL   A 34  ? 0.1482 0.1469 0.1042 -0.0225 -0.0072 0.0140  34  VAL   A CB  
889  C CG1 . VAL   A 34  ? 0.1518 0.1507 0.1165 -0.0179 0.0056  0.0090  34  VAL   A CG1 
890  C CG2 . VAL   A 34  ? 0.1566 0.1571 0.1407 -0.0055 -0.0071 0.0091  34  VAL   A CG2 
900  N N   . VAL   A 35  ? 0.1209 0.1258 0.0842 -0.0215 -0.0102 0.0170  35  VAL   A N   
901  C CA  . VAL   A 35  ? 0.1130 0.1270 0.0836 -0.0187 0.0037  0.0160  35  VAL   A CA  
902  C C   . VAL   A 35  ? 0.1063 0.1102 0.0852 -0.0178 0.0081  0.0138  35  VAL   A C   
903  O O   . VAL   A 35  ? 0.1069 0.1232 0.0964 -0.0145 0.0104  0.0056  35  VAL   A O   
904  C CB  . VAL   A 35  ? 0.1240 0.1359 0.0827 -0.0114 0.0128  0.0033  35  VAL   A CB  
905  C CG1 . VAL   A 35  ? 0.1303 0.1331 0.1026 -0.0065 0.0023  -0.0022 35  VAL   A CG1 
906  C CG2 . VAL   A 35  ? 0.1248 0.1412 0.1044 -0.0073 0.0155  -0.0017 35  VAL   A CG2 
916  N N   . VAL   A 36  ? 0.0978 0.1199 0.0851 -0.0141 0.0072  0.0147  36  VAL   A N   
917  C CA  . VAL   A 36  ? 0.0934 0.1095 0.0831 -0.0060 0.0102  0.0053  36  VAL   A CA  
918  C C   . VAL   A 36  ? 0.0940 0.1033 0.0908 -0.0090 0.0074  0.0066  36  VAL   A C   
919  O O   . VAL   A 36  ? 0.1008 0.1092 0.1063 -0.0016 0.0174  0.0076  36  VAL   A O   
920  C CB  . VAL   A 36  ? 0.1033 0.0965 0.0918 -0.0101 0.0066  0.0089  36  VAL   A CB  
921  C CG1 . VAL   A 36  ? 0.1163 0.0990 0.0961 -0.0161 0.0126  0.0034  36  VAL   A CG1 
922  C CG2 . VAL   A 36  ? 0.1092 0.0995 0.1092 -0.0072 0.0042  0.0179  36  VAL   A CG2 
932  N N   . ASN   A 37  ? 0.0939 0.0934 0.0975 0.0008  0.0113  0.0136  37  ASN   A N   
933  C CA  . ASN   A 37  ? 0.0944 0.0913 0.0850 0.0031  0.0072  0.0119  37  ASN   A CA  
934  C C   . ASN   A 37  ? 0.0954 0.0940 0.0884 0.0010  0.0165  0.0095  37  ASN   A C   
935  O O   . ASN   A 37  ? 0.1089 0.1051 0.0891 0.0094  0.0141  0.0082  37  ASN   A O   
936  C CB  . ASN   A 37  ? 0.0963 0.0961 0.0913 0.0058  0.0058  0.0091  37  ASN   A CB  
937  C CG  . ASN   A 37  ? 0.0956 0.0966 0.0933 0.0020  0.0078  0.0031  37  ASN   A CG  
938  O OD1 . ASN   A 37  ? 0.0960 0.0967 0.1193 0.0046  0.0051  0.0096  37  ASN   A OD1 
939  N ND2 . ASN   A 37  ? 0.0945 0.0988 0.1083 -0.0039 0.0012  0.0190  37  ASN   A ND2 
946  N N   A ALA   A 38  ? 0.0928 0.1005 0.0870 0.0076  0.0124  -0.0007 38  ALA   A N   
947  N N   B ALA   A 38  ? 0.0973 0.1073 0.0914 -0.0044 0.0104  0.0025  38  ALA   A N   
948  C CA  A ALA   A 38  ? 0.0989 0.1043 0.0920 0.0072  0.0040  -0.0072 38  ALA   A CA  
949  C CA  B ALA   A 38  ? 0.1071 0.1194 0.1003 -0.0140 0.0039  -0.0009 38  ALA   A CA  
950  C C   A ALA   A 38  ? 0.0987 0.1058 0.0904 0.0125  -0.0048 -0.0007 38  ALA   A C   
951  C C   B ALA   A 38  ? 0.1072 0.1162 0.0952 -0.0045 -0.0032 0.0049  38  ALA   A C   
952  O O   A ALA   A 38  ? 0.1036 0.1083 0.1078 0.0165  -0.0052 0.0078  38  ALA   A O   
953  O O   B ALA   A 38  ? 0.1077 0.1146 0.1044 0.0035  -0.0006 -0.0023 38  ALA   A O   
954  C CB  A ALA   A 38  ? 0.1074 0.1246 0.0983 0.0035  -0.0041 -0.0057 38  ALA   A CB  
955  C CB  B ALA   A 38  ? 0.1189 0.1477 0.1174 -0.0203 -0.0010 -0.0024 38  ALA   A CB  
966  N N   A ALA   A 39  ? 0.0927 0.0973 0.0995 0.0128  0.0005  -0.0009 39  ALA   A N   
967  N N   B ALA   A 39  ? 0.1047 0.1063 0.1021 -0.0032 0.0030  0.0190  39  ALA   A N   
968  C CA  A ALA   A 39  ? 0.0960 0.0910 0.0935 0.0071  -0.0013 -0.0045 39  ALA   A CA  
969  C CA  B ALA   A 39  ? 0.1130 0.1093 0.1102 -0.0046 0.0059  0.0131  39  ALA   A CA  
970  C C   A ALA   A 39  ? 0.0992 0.0946 0.0936 0.0077  0.0071  -0.0024 39  ALA   A C   
971  C C   B ALA   A 39  ? 0.1055 0.1042 0.1102 -0.0063 0.0069  0.0051  39  ALA   A C   
972  O O   A ALA   A 39  ? 0.1121 0.0965 0.0924 0.0034  0.0069  -0.0033 39  ALA   A O   
973  O O   B ALA   A 39  ? 0.1038 0.1049 0.1076 -0.0124 0.0165  0.0073  39  ALA   A O   
974  C CB  A ALA   A 39  ? 0.0891 0.0900 0.0882 0.0044  -0.0015 -0.0072 39  ALA   A CB  
975  C CB  B ALA   A 39  ? 0.1267 0.1270 0.1266 -0.0018 0.0070  0.0014  39  ALA   A CB  
986  N N   A ASN   A 40  ? 0.1127 0.1029 0.1033 -0.0008 0.0265  -0.0004 40  ASN   A N   
987  N N   B ASN   A 40  ? 0.1129 0.1055 0.1107 -0.0159 0.0179  0.0020  40  ASN   A N   
988  C CA  A ASN   A 40  ? 0.1178 0.1025 0.1072 0.0041  0.0159  0.0045  40  ASN   A CA  
989  C CA  B ASN   A 40  ? 0.1130 0.1060 0.1038 -0.0082 0.0134  0.0027  40  ASN   A CA  
990  C C   A ASN   A 40  ? 0.1239 0.0961 0.0931 0.0023  0.0260  0.0183  40  ASN   A C   
991  C C   B ASN   A 40  ? 0.1155 0.0954 0.0871 -0.0104 0.0219  0.0092  40  ASN   A C   
992  O O   A ASN   A 40  ? 0.1219 0.0995 0.0989 0.0061  0.0201  0.0164  40  ASN   A O   
993  O O   B ASN   A 40  ? 0.1108 0.0918 0.0916 -0.0077 0.0232  0.0103  40  ASN   A O   
994  C CB  A ASN   A 40  ? 0.1265 0.1017 0.1202 0.0026  0.0004  0.0037  40  ASN   A CB  
995  C CB  B ASN   A 40  ? 0.1199 0.1182 0.1090 -0.0025 0.0066  0.0037  40  ASN   A CB  
996  C CG  A ASN   A 40  ? 0.1333 0.0957 0.1464 0.0005  -0.0122 0.0005  40  ASN   A CG  
997  C CG  B ASN   A 40  ? 0.1233 0.1244 0.1201 -0.0009 0.0147  0.0062  40  ASN   A CG  
998  O OD1 A ASN   A 40  ? 0.1456 0.1004 0.1949 0.0058  -0.0326 -0.0127 40  ASN   A OD1 
999  O OD1 B ASN   A 40  ? 0.1205 0.1312 0.1294 -0.0054 0.0363  0.0156  40  ASN   A OD1 
1000 N ND2 A ASN   A 40  ? 0.1256 0.1041 0.1488 -0.0052 0.0037  -0.0036 40  ASN   A ND2 
1001 N ND2 B ASN   A 40  ? 0.1258 0.1379 0.1446 0.0038  0.0110  -0.0066 40  ASN   A ND2 
1014 N N   A VAL   A 41  ? 0.1341 0.1000 0.0995 0.0026  0.0316  0.0185  41  VAL   A N   
1015 N N   B VAL   A 41  ? 0.1195 0.1003 0.0871 -0.0077 0.0142  0.0035  41  VAL   A N   
1016 C CA  A VAL   A 41  ? 0.1390 0.1054 0.1075 0.0034  0.0457  0.0116  41  VAL   A CA  
1017 C CA  B VAL   A 41  ? 0.1228 0.1061 0.1056 -0.0067 0.0258  0.0048  41  VAL   A CA  
1018 C C   A VAL   A 41  ? 0.1340 0.1074 0.1067 0.0024  0.0440  0.0138  41  VAL   A C   
1019 C C   B VAL   A 41  ? 0.1147 0.1042 0.1114 -0.0000 0.0200  0.0051  41  VAL   A C   
1020 O O   A VAL   A 41  ? 0.1401 0.1046 0.1195 0.0039  0.0302  0.0025  41  VAL   A O   
1021 O O   B VAL   A 41  ? 0.1174 0.0986 0.1372 0.0057  0.0123  0.0073  41  VAL   A O   
1022 C CB  A VAL   A 41  ? 0.1551 0.1176 0.1266 -0.0015 0.0511  0.0034  41  VAL   A CB  
1023 C CB  B VAL   A 41  ? 0.1377 0.1181 0.1166 -0.0171 0.0347  0.0047  41  VAL   A CB  
1024 C CG1 A VAL   A 41  ? 0.1677 0.1241 0.1304 -0.0004 0.0532  -0.0036 41  VAL   A CG1 
1025 C CG1 B VAL   A 41  ? 0.1495 0.1260 0.1155 -0.0154 0.0363  0.0024  41  VAL   A CG1 
1026 C CG2 A VAL   A 41  ? 0.1706 0.1254 0.1242 -0.0089 0.0486  0.0007  41  VAL   A CG2 
1027 C CG2 B VAL   A 41  ? 0.1541 0.1263 0.1062 -0.0217 0.0383  0.0090  41  VAL   A CG2 
1046 N N   A TYR   A 42  ? 0.1213 0.1010 0.1279 0.0009  0.0451  0.0251  42  TYR   A N   
1047 N N   B TYR   A 42  ? 0.1061 0.1007 0.1353 -0.0068 0.0198  0.0102  42  TYR   A N   
1048 C CA  A TYR   A 42  ? 0.1166 0.0980 0.1268 -0.0031 0.0413  0.0271  42  TYR   A CA  
1049 C CA  B TYR   A 42  ? 0.1096 0.1009 0.1363 -0.0084 0.0175  0.0152  42  TYR   A CA  
1050 C C   A TYR   A 42  ? 0.1143 0.0988 0.1252 0.0005  0.0279  0.0266  42  TYR   A C   
1051 C C   B TYR   A 42  ? 0.1023 0.0992 0.1357 -0.0064 0.0127  0.0105  42  TYR   A C   
1052 O O   A TYR   A 42  ? 0.1122 0.1048 0.1388 -0.0073 0.0284  0.0163  42  TYR   A O   
1053 O O   B TYR   A 42  ? 0.1050 0.1017 0.1533 -0.0116 0.0137  -0.0027 42  TYR   A O   
1054 C CB  A TYR   A 42  ? 0.1354 0.1048 0.1272 -0.0026 0.0386  0.0259  42  TYR   A CB  
1055 C CB  B TYR   A 42  ? 0.1373 0.1184 0.1406 -0.0033 0.0225  0.0172  42  TYR   A CB  
1056 C CG  A TYR   A 42  ? 0.1566 0.1161 0.1331 -0.0100 0.0365  0.0324  42  TYR   A CG  
1057 C CG  B TYR   A 42  ? 0.1601 0.1330 0.1426 -0.0064 0.0143  0.0245  42  TYR   A CG  
1058 C CD1 A TYR   A 42  ? 0.1690 0.1285 0.1314 -0.0137 0.0429  0.0276  42  TYR   A CD1 
1059 C CD1 B TYR   A 42  ? 0.1697 0.1453 0.1415 -0.0082 0.0183  0.0190  42  TYR   A CD1 
1060 C CD2 A TYR   A 42  ? 0.1658 0.1368 0.1491 -0.0104 0.0337  0.0219  42  TYR   A CD2 
1061 C CD2 B TYR   A 42  ? 0.1716 0.1511 0.1561 -0.0057 0.0082  0.0156  42  TYR   A CD2 
1062 C CE1 A TYR   A 42  ? 0.1771 0.1456 0.1362 -0.0170 0.0395  0.0281  42  TYR   A CE1 
1063 C CE1 B TYR   A 42  ? 0.1772 0.1571 0.1448 -0.0122 0.0180  0.0166  42  TYR   A CE1 
1064 C CE2 A TYR   A 42  ? 0.1756 0.1510 0.1579 -0.0200 0.0302  0.0233  42  TYR   A CE2 
1065 C CE2 B TYR   A 42  ? 0.1820 0.1642 0.1605 -0.0126 0.0073  0.0144  42  TYR   A CE2 
1066 C CZ  A TYR   A 42  ? 0.1827 0.1553 0.1539 -0.0237 0.0362  0.0256  42  TYR   A CZ  
1067 C CZ  B TYR   A 42  ? 0.1853 0.1684 0.1562 -0.0191 0.0176  0.0147  42  TYR   A CZ  
1068 O OH  A TYR   A 42  ? 0.1934 0.1739 0.1797 -0.0267 0.0347  0.0195  42  TYR   A OH  
1069 O OH  B TYR   A 42  ? 0.1887 0.1874 0.1674 -0.0286 0.0241  0.0116  42  TYR   A OH  
1088 N N   A LEU   A 43  ? 0.1105 0.0972 0.1156 -0.0033 0.0229  0.0141  43  LEU   A N   
1089 N N   B LEU   A 43  ? 0.1001 0.1020 0.1269 -0.0110 0.0117  -0.0027 43  LEU   A N   
1090 C CA  A LEU   A 43  ? 0.1061 0.0939 0.1177 -0.0026 0.0221  0.0107  43  LEU   A CA  
1091 C CA  B LEU   A 43  ? 0.1003 0.1060 0.1257 -0.0106 0.0108  -0.0028 43  LEU   A CA  
1092 C C   A LEU   A 43  ? 0.0994 0.0951 0.1179 0.0025  0.0134  0.0109  43  LEU   A C   
1093 C C   B LEU   A 43  ? 0.0976 0.1114 0.1299 -0.0075 0.0027  -0.0097 43  LEU   A C   
1094 O O   A LEU   A 43  ? 0.1045 0.0981 0.1257 0.0024  0.0033  0.0184  43  LEU   A O   
1095 O O   B LEU   A 43  ? 0.1071 0.1144 0.1467 -0.0016 -0.0065 -0.0130 43  LEU   A O   
1096 C CB  A LEU   A 43  ? 0.1107 0.0916 0.1207 -0.0056 0.0170  0.0086  43  LEU   A CB  
1097 C CB  B LEU   A 43  ? 0.1067 0.1050 0.1274 -0.0099 0.0033  0.0042  43  LEU   A CB  
1098 C CG  A LEU   A 43  ? 0.1129 0.0969 0.1303 0.0008  0.0165  0.0035  43  LEU   A CG  
1099 C CG  B LEU   A 43  ? 0.1118 0.1077 0.1286 0.0000  0.0011  0.0029  43  LEU   A CG  
1100 C CD1 A LEU   A 43  ? 0.1164 0.1037 0.1359 0.0011  0.0135  0.0057  43  LEU   A CD1 
1101 C CD1 B LEU   A 43  ? 0.1152 0.1149 0.1353 0.0048  -0.0036 0.0089  43  LEU   A CD1 
1102 C CD2 A LEU   A 43  ? 0.1246 0.0975 0.1301 -0.0049 0.0126  0.0143  43  LEU   A CD2 
1103 C CD2 B LEU   A 43  ? 0.1226 0.1077 0.1223 -0.0052 0.0040  0.0062  43  LEU   A CD2 
1126 N N   A LYS   A 44  ? 0.1072 0.0918 0.1066 0.0043  0.0086  0.0165  44  LYS   A N   
1127 N N   B LYS   A 44  ? 0.1073 0.1152 0.1245 -0.0131 0.0033  -0.0054 44  LYS   A N   
1128 C CA  A LYS   A 44  ? 0.1181 0.0891 0.1150 0.0055  0.0115  0.0251  44  LYS   A CA  
1129 C CA  B LYS   A 44  ? 0.1212 0.1201 0.1394 -0.0146 0.0106  0.0038  44  LYS   A CA  
1130 C C   A LYS   A 44  ? 0.1059 0.0881 0.1123 0.0115  0.0033  0.0171  44  LYS   A C   
1131 C C   B LYS   A 44  ? 0.1129 0.1098 0.1241 -0.0057 -0.0002 -0.0046 44  LYS   A C   
1132 O O   A LYS   A 44  ? 0.1077 0.0940 0.1254 0.0022  0.0023  0.0046  44  LYS   A O   
1133 O O   B LYS   A 44  ? 0.1182 0.1170 0.1328 -0.0029 -0.0018 -0.0109 44  LYS   A O   
1134 C CB  A LYS   A 44  ? 0.1433 0.0999 0.1538 0.0149  0.0206  0.0354  44  LYS   A CB  
1135 C CB  B LYS   A 44  ? 0.1459 0.1410 0.1794 -0.0155 0.0252  0.0132  44  LYS   A CB  
1136 C CG  A LYS   A 44  ? 0.1708 0.1294 0.2205 0.0120  0.0427  0.0439  44  LYS   A CG  
1137 C CG  B LYS   A 44  ? 0.1740 0.1660 0.2341 -0.0160 0.0418  0.0208  44  LYS   A CG  
1138 C CD  A LYS   A 44  ? 0.2018 0.1776 0.3214 0.0141  0.0278  0.0357  44  LYS   A CD  
1139 C CD  B LYS   A 44  ? 0.2020 0.1992 0.3152 -0.0063 0.0407  0.0144  44  LYS   A CD  
1140 C CE  A LYS   A 44  ? 0.2144 0.2003 0.3805 0.0166  0.0175  0.0386  44  LYS   A CE  
1141 C CE  B LYS   A 44  ? 0.2143 0.2134 0.3701 0.0067  0.0433  0.0114  44  LYS   A CE  
1142 N NZ  A LYS   A 44  ? 0.2223 0.2158 0.4144 0.0133  0.0145  0.0359  44  LYS   A NZ  
1143 N NZ  B LYS   A 44  ? 0.2143 0.2159 0.3902 0.0137  0.0427  0.0109  44  LYS   A NZ  
1170 N N   A HIS   A 45  ? 0.0979 0.0847 0.1115 0.0091  -0.0020 0.0161  45  HIS   A N   
1171 N N   B HIS   A 45  ? 0.1071 0.1061 0.1278 -0.0019 -0.0041 -0.0015 45  HIS   A N   
1172 C CA  A HIS   A 45  ? 0.0927 0.0848 0.1114 0.0042  0.0021  0.0155  45  HIS   A CA  
1173 C CA  B HIS   A 45  ? 0.1117 0.1070 0.1379 -0.0040 -0.0068 -0.0065 45  HIS   A CA  
1174 C C   A HIS   A 45  ? 0.0939 0.0881 0.1190 -0.0003 0.0017  0.0108  45  HIS   A C   
1175 C C   B HIS   A 45  ? 0.1151 0.1137 0.1623 0.0006  -0.0043 -0.0031 45  HIS   A C   
1176 O O   A HIS   A 45  ? 0.1001 0.0858 0.1373 0.0004  -0.0069 -0.0090 45  HIS   A O   
1177 O O   B HIS   A 45  ? 0.1206 0.1198 0.1866 0.0061  -0.0115 -0.0168 45  HIS   A O   
1178 C CB  A HIS   A 45  ? 0.0926 0.0862 0.1019 0.0062  0.0093  0.0044  45  HIS   A CB  
1179 C CB  B HIS   A 45  ? 0.1150 0.1023 0.1213 -0.0038 -0.0052 -0.0104 45  HIS   A CB  
1180 C CG  A HIS   A 45  ? 0.0888 0.0827 0.0959 -0.0042 0.0053  0.0069  45  HIS   A CG  
1181 C CG  B HIS   A 45  ? 0.1095 0.1011 0.1097 -0.0040 0.0024  -0.0071 45  HIS   A CG  
1182 N ND1 A HIS   A 45  ? 0.0793 0.0909 0.0935 -0.0033 -0.0016 0.0021  45  HIS   A ND1 
1183 N ND1 B HIS   A 45  ? 0.1064 0.1102 0.1278 -0.0020 0.0023  0.0010  45  HIS   A ND1 
1184 C CD2 A HIS   A 45  ? 0.0947 0.0939 0.1098 -0.0099 0.0028  0.0119  45  HIS   A CD2 
1185 C CD2 B HIS   A 45  ? 0.1050 0.0955 0.0966 -0.0065 -0.0051 -0.0054 45  HIS   A CD2 
1186 C CE1 A HIS   A 45  ? 0.0887 0.0989 0.0973 -0.0063 0.0010  0.0118  45  HIS   A CE1 
1187 C CE1 B HIS   A 45  ? 0.1022 0.0982 0.0984 -0.0088 0.0010  -0.0054 45  HIS   A CE1 
1188 N NE2 A HIS   A 45  ? 0.0950 0.1047 0.1105 -0.0000 0.0048  0.0125  45  HIS   A NE2 
1189 N NE2 B HIS   A 45  ? 0.0984 0.0961 0.0892 -0.0056 0.0003  -0.0043 45  HIS   A NE2 
1204 N N   A GLY   A 46  ? 0.1096 0.1001 0.1284 0.0076  -0.0133 0.0044  46  GLY   A N   
1205 N N   B GLY   A 46  ? 0.1254 0.1176 0.1648 0.0134  -0.0124 0.0114  46  GLY   A N   
1206 C CA  A GLY   A 46  ? 0.1207 0.1045 0.1477 0.0060  -0.0193 0.0044  46  GLY   A CA  
1207 C CA  B GLY   A 46  ? 0.1269 0.1123 0.1615 0.0162  -0.0188 0.0210  46  GLY   A CA  
1208 C C   A GLY   A 46  ? 0.1236 0.1092 0.1555 0.0118  -0.0322 0.0181  46  GLY   A C   
1209 C C   B GLY   A 46  ? 0.1261 0.1062 0.1362 0.0227  -0.0273 0.0209  46  GLY   A C   
1210 O O   A GLY   A 46  ? 0.1239 0.1198 0.1754 0.0101  -0.0505 0.0021  46  GLY   A O   
1211 O O   B GLY   A 46  ? 0.1280 0.1153 0.1520 0.0235  -0.0263 0.0007  46  GLY   A O   
1218 N N   A GLY   A 47  ? 0.1256 0.1133 0.1538 0.0108  -0.0228 0.0110  47  GLY   A N   
1219 N N   B GLY   A 47  ? 0.1207 0.1020 0.1356 0.0203  -0.0184 0.0167  47  GLY   A N   
1220 C CA  A GLY   A 47  ? 0.1245 0.1197 0.1527 0.0112  -0.0342 0.0032  47  GLY   A CA  
1221 C CA  B GLY   A 47  ? 0.1259 0.1102 0.1545 0.0200  -0.0285 0.0245  47  GLY   A CA  
1222 C C   A GLY   A 47  ? 0.1095 0.1093 0.1277 0.0125  -0.0350 -0.0113 47  GLY   A C   
1223 C C   B GLY   A 47  ? 0.1166 0.1109 0.1423 0.0155  -0.0206 0.0151  47  GLY   A C   
1224 O O   A GLY   A 47  ? 0.1025 0.1012 0.1240 0.0129  -0.0280 -0.0016 47  GLY   A O   
1225 O O   B GLY   A 47  ? 0.1144 0.1044 0.1459 0.0121  -0.0165 0.0211  47  GLY   A O   
1232 N N   A GLY   A 48  ? 0.1094 0.1167 0.1273 0.0125  -0.0409 -0.0119 48  GLY   A N   
1233 N N   B GLY   A 48  ? 0.1108 0.1191 0.1421 0.0127  -0.0201 0.0053  48  GLY   A N   
1234 C CA  A GLY   A 48  ? 0.0989 0.1107 0.1264 0.0125  -0.0345 -0.0227 48  GLY   A CA  
1235 C CA  B GLY   A 48  ? 0.1001 0.1202 0.1430 0.0048  -0.0136 -0.0047 48  GLY   A CA  
1236 C C   A GLY   A 48  ? 0.0882 0.1069 0.1189 0.0062  -0.0160 -0.0182 48  GLY   A C   
1237 C C   B GLY   A 48  ? 0.0904 0.1199 0.1226 0.0054  -0.0025 -0.0068 48  GLY   A C   
1238 O O   A GLY   A 48  ? 0.0984 0.1090 0.1366 0.0147  -0.0151 -0.0257 48  GLY   A O   
1239 O O   B GLY   A 48  ? 0.0981 0.1268 0.1216 0.0017  -0.0053 -0.0095 48  GLY   A O   
1246 N N   A VAL   A 49  ? 0.0904 0.0992 0.1117 0.0023  -0.0089 -0.0208 49  VAL   A N   
1247 N N   B VAL   A 49  ? 0.0938 0.1119 0.1258 -0.0007 -0.0084 0.0015  49  VAL   A N   
1248 C CA  A VAL   A 49  ? 0.1039 0.1001 0.1095 -0.0004 0.0140  -0.0203 49  VAL   A CA  
1249 C CA  B VAL   A 49  ? 0.0966 0.1097 0.1107 -0.0001 -0.0005 0.0107  49  VAL   A CA  
1250 C C   A VAL   A 49  ? 0.0993 0.0981 0.1008 -0.0023 0.0091  -0.0040 49  VAL   A C   
1251 C C   B VAL   A 49  ? 0.0951 0.0979 0.0849 0.0055  0.0058  0.0057  49  VAL   A C   
1252 O O   A VAL   A 49  ? 0.1048 0.1037 0.1111 -0.0108 0.0099  -0.0033 49  VAL   A O   
1253 O O   B VAL   A 49  ? 0.0972 0.0969 0.0849 0.0097  0.0069  -0.0022 49  VAL   A O   
1254 C CB  A VAL   A 49  ? 0.1277 0.1058 0.1271 -0.0111 0.0225  -0.0135 49  VAL   A CB  
1255 C CB  B VAL   A 49  ? 0.1014 0.1116 0.1118 0.0011  -0.0034 0.0132  49  VAL   A CB  
1256 C CG1 A VAL   A 49  ? 0.1320 0.1107 0.1493 -0.0067 0.0235  -0.0167 49  VAL   A CG1 
1257 C CG1 B VAL   A 49  ? 0.0901 0.1085 0.0937 0.0094  0.0072  0.0054  49  VAL   A CG1 
1258 C CG2 A VAL   A 49  ? 0.1391 0.1127 0.1718 -0.0209 0.0143  -0.0089 49  VAL   A CG2 
1259 C CG2 B VAL   A 49  ? 0.1082 0.1176 0.1422 -0.0023 -0.0013 0.0096  49  VAL   A CG2 
1278 N N   A ALA   A 50  ? 0.0939 0.0989 0.1030 -0.0104 -0.0074 0.0060  50  ALA   A N   
1279 N N   B ALA   A 50  ? 0.1000 0.0906 0.0808 0.0066  -0.0027 0.0001  50  ALA   A N   
1280 C CA  A ALA   A 50  ? 0.0847 0.0995 0.1059 -0.0122 -0.0048 0.0096  50  ALA   A CA  
1281 C CA  B ALA   A 50  ? 0.1013 0.0894 0.0810 0.0073  -0.0066 -0.0067 50  ALA   A CA  
1282 C C   A ALA   A 50  ? 0.0743 0.0984 0.1046 -0.0127 -0.0026 0.0085  50  ALA   A C   
1283 C C   B ALA   A 50  ? 0.0972 0.0904 0.0857 0.0068  -0.0066 -0.0101 50  ALA   A C   
1284 O O   A ALA   A 50  ? 0.0846 0.1046 0.1124 -0.0051 -0.0069 0.0081  50  ALA   A O   
1285 O O   B ALA   A 50  ? 0.1005 0.0947 0.0934 0.0090  -0.0057 -0.0132 50  ALA   A O   
1286 C CB  A ALA   A 50  ? 0.0816 0.0994 0.1131 -0.0086 -0.0096 0.0062  50  ALA   A CB  
1287 C CB  B ALA   A 50  ? 0.1048 0.0790 0.0829 0.0080  -0.0037 -0.0080 50  ALA   A CB  
1298 N N   A GLY   A 51  ? 0.0852 0.0934 0.1086 -0.0005 -0.0071 0.0034  51  GLY   A N   
1299 N N   B GLY   A 51  ? 0.1082 0.0896 0.1003 0.0112  -0.0197 -0.0121 51  GLY   A N   
1300 C CA  A GLY   A 51  ? 0.0952 0.0972 0.1223 0.0047  -0.0061 0.0056  51  GLY   A CA  
1301 C CA  B GLY   A 51  ? 0.1156 0.0929 0.1104 0.0122  -0.0198 -0.0087 51  GLY   A CA  
1302 C C   A GLY   A 51  ? 0.0870 0.0955 0.1072 0.0070  -0.0079 -0.0022 51  GLY   A C   
1303 C C   B GLY   A 51  ? 0.1120 0.0946 0.1136 0.0140  -0.0130 -0.0126 51  GLY   A C   
1304 O O   A GLY   A 51  ? 0.0927 0.1007 0.1156 -0.0000 -0.0071 -0.0023 51  GLY   A O   
1305 O O   B GLY   A 51  ? 0.1220 0.1017 0.1254 0.0076  -0.0117 -0.0166 51  GLY   A O   
1312 N N   A ALA   A 52  ? 0.0871 0.1037 0.0968 0.0080  -0.0106 -0.0175 52  ALA   A N   
1313 N N   B ALA   A 52  ? 0.1117 0.1059 0.1106 0.0090  -0.0060 -0.0182 52  ALA   A N   
1314 C CA  A ALA   A 52  ? 0.0904 0.1058 0.1104 0.0059  -0.0098 -0.0121 52  ALA   A CA  
1315 C CA  B ALA   A 52  ? 0.1031 0.1059 0.1250 0.0084  0.0000  -0.0195 52  ALA   A CA  
1316 C C   A ALA   A 52  ? 0.0916 0.1099 0.0935 -0.0039 -0.0002 -0.0187 52  ALA   A C   
1317 C C   B ALA   A 52  ? 0.0986 0.1104 0.1142 0.0003  0.0033  -0.0147 52  ALA   A C   
1318 O O   A ALA   A 52  ? 0.0981 0.1151 0.1105 -0.0056 -0.0058 -0.0300 52  ALA   A O   
1319 O O   B ALA   A 52  ? 0.1053 0.1176 0.1211 0.0055  0.0084  -0.0158 52  ALA   A O   
1320 C CB  A ALA   A 52  ? 0.0976 0.1118 0.1301 0.0024  -0.0105 -0.0081 52  ALA   A CB  
1321 C CB  B ALA   A 52  ? 0.0973 0.1154 0.1500 0.0090  -0.0048 -0.0211 52  ALA   A CB  
1332 N N   A LEU   A 53  ? 0.0913 0.1067 0.0855 -0.0059 -0.0023 -0.0129 53  LEU   A N   
1333 N N   B LEU   A 53  ? 0.0920 0.1095 0.1116 0.0043  -0.0017 -0.0113 53  LEU   A N   
1334 C CA  A LEU   A 53  ? 0.1010 0.1149 0.0916 -0.0071 -0.0031 -0.0064 53  LEU   A CA  
1335 C CA  B LEU   A 53  ? 0.0897 0.1128 0.0968 0.0037  -0.0022 -0.0038 53  LEU   A CA  
1336 C C   A LEU   A 53  ? 0.1063 0.1165 0.0965 0.0014  -0.0089 -0.0034 53  LEU   A C   
1337 C C   B LEU   A 53  ? 0.0904 0.1163 0.0784 0.0025  0.0070  -0.0058 53  LEU   A C   
1338 O O   A LEU   A 53  ? 0.1224 0.1182 0.1127 -0.0058 -0.0128 -0.0004 53  LEU   A O   
1339 O O   B LEU   A 53  ? 0.1055 0.1173 0.0742 -0.0072 0.0026  -0.0122 53  LEU   A O   
1340 C CB  A LEU   A 53  ? 0.1026 0.1217 0.1024 -0.0108 0.0039  0.0010  53  LEU   A CB  
1341 C CB  B LEU   A 53  ? 0.0849 0.1109 0.0948 0.0010  -0.0120 -0.0094 53  LEU   A CB  
1342 C CG  A LEU   A 53  ? 0.1046 0.1248 0.1045 -0.0077 0.0035  0.0129  53  LEU   A CG  
1343 C CG  B LEU   A 53  ? 0.0969 0.1155 0.1036 0.0006  -0.0108 -0.0051 53  LEU   A CG  
1344 C CD1 A LEU   A 53  ? 0.1009 0.1227 0.1106 0.0017  0.0081  0.0156  53  LEU   A CD1 
1345 C CD1 B LEU   A 53  ? 0.1006 0.1238 0.1079 -0.0028 -0.0058 -0.0066 53  LEU   A CD1 
1346 C CD2 A LEU   A 53  ? 0.1220 0.1393 0.1222 -0.0081 0.0130  0.0210  53  LEU   A CD2 
1347 C CD2 B LEU   A 53  ? 0.1119 0.1164 0.1167 0.0003  0.0018  -0.0173 53  LEU   A CD2 
1370 N N   A ASN   A 54  ? 0.1040 0.1078 0.0927 0.0017  -0.0149 -0.0051 54  ASN   A N   
1371 N N   B ASN   A 54  ? 0.0888 0.1108 0.0827 0.0021  0.0090  -0.0029 54  ASN   A N   
1372 C CA  A ASN   A 54  ? 0.0985 0.1033 0.0987 -0.0020 -0.0184 -0.0077 54  ASN   A CA  
1373 C CA  B ASN   A 54  ? 0.0817 0.1104 0.0944 0.0002  0.0059  -0.0009 54  ASN   A CA  
1374 C C   A ASN   A 54  ? 0.1045 0.1064 0.1007 -0.0064 -0.0077 -0.0106 54  ASN   A C   
1375 C C   B ASN   A 54  ? 0.0942 0.1090 0.1054 -0.0062 0.0014  -0.0036 54  ASN   A C   
1376 O O   A ASN   A 54  ? 0.1095 0.1080 0.0883 -0.0065 -0.0077 -0.0182 54  ASN   A O   
1377 O O   B ASN   A 54  ? 0.0952 0.1105 0.1206 -0.0071 -0.0083 -0.0070 54  ASN   A O   
1378 C CB  A ASN   A 54  ? 0.0944 0.0969 0.1076 -0.0060 -0.0165 -0.0165 54  ASN   A CB  
1379 C CB  B ASN   A 54  ? 0.0866 0.1127 0.1131 0.0044  0.0075  0.0013  54  ASN   A CB  
1380 C CG  A ASN   A 54  ? 0.0949 0.0970 0.0943 -0.0060 -0.0136 -0.0128 54  ASN   A CG  
1381 C CG  B ASN   A 54  ? 0.0953 0.1180 0.1337 0.0118  0.0028  0.0059  54  ASN   A CG  
1382 O OD1 A ASN   A 54  ? 0.0913 0.0917 0.0719 -0.0112 -0.0106 -0.0077 54  ASN   A OD1 
1383 O OD1 B ASN   A 54  ? 0.0942 0.1233 0.1464 0.0075  -0.0029 0.0112  54  ASN   A OD1 
1384 N ND2 A ASN   A 54  ? 0.0947 0.1055 0.1220 -0.0122 -0.0276 -0.0033 54  ASN   A ND2 
1385 N ND2 B ASN   A 54  ? 0.1049 0.1186 0.1537 0.0121  -0.0032 0.0139  54  ASN   A ND2 
1398 N N   . LYS   A 55  ? 0.0990 0.1091 0.1146 0.0001  -0.0053 -0.0156 55  LYS   A N   
1399 C CA  . LYS   A 55  ? 0.1107 0.1152 0.1166 0.0089  -0.0098 -0.0170 55  LYS   A CA  
1400 C C   . LYS   A 55  ? 0.1054 0.1202 0.1233 0.0064  -0.0009 -0.0255 55  LYS   A C   
1401 O O   . LYS   A 55  ? 0.1172 0.1351 0.1343 0.0066  -0.0067 -0.0376 55  LYS   A O   
1402 C CB  . LYS   A 55  ? 0.1186 0.1226 0.1375 0.0167  -0.0109 -0.0190 55  LYS   A CB  
1403 C CG  . LYS   A 55  ? 0.1285 0.1496 0.1614 0.0258  -0.0230 -0.0348 55  LYS   A CG  
1404 C CD  . LYS   A 55  ? 0.1382 0.1773 0.1736 0.0365  -0.0070 -0.0348 55  LYS   A CD  
1405 C CE  . LYS   A 55  ? 0.1695 0.2140 0.2020 0.0467  -0.0234 -0.0303 55  LYS   A CE  
1406 N NZ  . LYS   A 55  ? 0.1766 0.2256 0.2012 0.0621  -0.0278 -0.0259 55  LYS   A NZ  
1421 N N   . ALA   A 56  ? 0.1067 0.1356 0.1146 0.0005  0.0058  -0.0323 56  ALA   A N   
1422 C CA  . ALA   A 56  ? 0.1163 0.1582 0.1221 -0.0059 0.0118  -0.0254 56  ALA   A CA  
1423 C C   . ALA   A 56  ? 0.1232 0.1655 0.1050 -0.0045 0.0070  -0.0298 56  ALA   A C   
1424 O O   . ALA   A 56  ? 0.1277 0.1984 0.1246 0.0080  0.0068  -0.0259 56  ALA   A O   
1425 C CB  . ALA   A 56  ? 0.1241 0.1762 0.1356 -0.0181 0.0050  -0.0197 56  ALA   A CB  
1431 N N   . THR   A 57  ? 0.1116 0.1389 0.1001 -0.0036 -0.0017 -0.0249 57  THR   A N   
1432 C CA  . THR   A 57  ? 0.1179 0.1391 0.1046 -0.0017 -0.0113 -0.0215 57  THR   A CA  
1433 C C   . THR   A 57  ? 0.1162 0.1390 0.1108 -0.0016 -0.0088 -0.0290 57  THR   A C   
1434 O O   . THR   A 57  ? 0.1137 0.1470 0.1270 -0.0038 -0.0140 -0.0364 57  THR   A O   
1435 C CB  . THR   A 57  ? 0.1145 0.1344 0.1049 -0.0045 -0.0056 -0.0134 57  THR   A CB  
1436 O OG1 . THR   A 57  ? 0.1058 0.1287 0.1087 0.0002  -0.0046 -0.0109 57  THR   A OG1 
1437 C CG2 . THR   A 57  ? 0.1175 0.1368 0.0975 -0.0040 -0.0011 -0.0061 57  THR   A CG2 
1445 N N   . ASN   A 58  ? 0.1155 0.1392 0.1300 0.0006  -0.0039 -0.0352 58  ASN   A N   
1446 C CA  . ASN   A 58  ? 0.1381 0.1325 0.1558 -0.0075 0.0067  -0.0454 58  ASN   A CA  
1447 C C   . ASN   A 58  ? 0.1184 0.1210 0.1468 0.0019  -0.0075 -0.0319 58  ASN   A C   
1448 O O   . ASN   A 58  ? 0.1245 0.1307 0.1596 -0.0099 -0.0129 -0.0354 58  ASN   A O   
1449 C CB  . ASN   A 58  ? 0.1873 0.1554 0.1832 -0.0178 0.0227  -0.0619 58  ASN   A CB  
1450 C CG  . ASN   A 58  ? 0.2318 0.1815 0.2578 -0.0133 0.0217  -0.0562 58  ASN   A CG  
1451 O OD1 . ASN   A 58  ? 0.2578 0.1802 0.2906 0.0207  0.0491  -0.0488 58  ASN   A OD1 
1452 N ND2 . ASN   A 58  ? 0.2431 0.1939 0.2919 -0.0238 0.0076  -0.0594 58  ASN   A ND2 
1459 N N   . ASN   A 59  ? 0.1086 0.1142 0.1274 -0.0024 -0.0169 -0.0241 59  ASN   A N   
1460 C CA  . ASN   A 59  ? 0.1070 0.1026 0.1324 -0.0019 -0.0159 -0.0173 59  ASN   A CA  
1461 C C   . ASN   A 59  ? 0.1034 0.1098 0.1287 -0.0023 -0.0096 -0.0169 59  ASN   A C   
1462 O O   . ASN   A 59  ? 0.1061 0.1108 0.1273 -0.0024 -0.0049 -0.0056 59  ASN   A O   
1463 C CB  . ASN   A 59  ? 0.1106 0.1075 0.1456 0.0025  -0.0238 -0.0200 59  ASN   A CB  
1464 C CG  . ASN   A 59  ? 0.1140 0.1092 0.1437 -0.0010 -0.0272 -0.0090 59  ASN   A CG  
1465 O OD1 . ASN   A 59  ? 0.1258 0.1182 0.1450 -0.0053 -0.0313 0.0004  59  ASN   A OD1 
1466 N ND2 . ASN   A 59  ? 0.1233 0.1141 0.1549 -0.0074 -0.0189 -0.0020 59  ASN   A ND2 
1473 N N   . ALA   A 60  ? 0.0972 0.1136 0.1259 0.0002  -0.0073 -0.0164 60  ALA   A N   
1474 C CA  . ALA   A 60  ? 0.1010 0.1131 0.1337 0.0008  -0.0118 -0.0093 60  ALA   A CA  
1475 C C   . ALA   A 60  ? 0.1003 0.1076 0.1371 0.0017  -0.0096 -0.0083 60  ALA   A C   
1476 O O   . ALA   A 60  ? 0.0963 0.1072 0.1484 -0.0018 -0.0124 -0.0123 60  ALA   A O   
1477 C CB  . ALA   A 60  ? 0.1128 0.1272 0.1366 0.0006  -0.0171 -0.0189 60  ALA   A CB  
1483 N N   . MET   A 61  ? 0.0941 0.1014 0.1289 -0.0049 -0.0029 -0.0118 61  MET   A N   
1484 C CA  . MET   A 61  ? 0.1000 0.1013 0.1228 -0.0067 -0.0009 -0.0021 61  MET   A CA  
1485 C C   . MET   A 61  ? 0.0899 0.0969 0.1248 -0.0045 -0.0092 -0.0100 61  MET   A C   
1486 O O   . MET   A 61  ? 0.1023 0.0963 0.1295 -0.0016 0.0030  -0.0027 61  MET   A O   
1487 C CB  . MET   A 61  ? 0.1051 0.1011 0.1165 -0.0054 -0.0022 -0.0027 61  MET   A CB  
1488 C CG  . MET   A 61  ? 0.1003 0.1062 0.1260 0.0032  -0.0013 -0.0055 61  MET   A CG  
1489 S SD  . MET   A 61  ? 0.1067 0.1131 0.1510 -0.0075 -0.0029 -0.0236 61  MET   A SD  
1490 C CE  . MET   A 61  ? 0.1216 0.1243 0.1732 -0.0124 0.0107  -0.0146 61  MET   A CE  
1500 N N   . GLN   A 62  ? 0.0943 0.0952 0.1205 -0.0018 -0.0022 -0.0080 62  GLN   A N   
1501 C CA  . GLN   A 62  ? 0.0994 0.0945 0.1210 -0.0012 0.0004  -0.0057 62  GLN   A CA  
1502 C C   . GLN   A 62  ? 0.1008 0.0906 0.1355 0.0017  0.0064  -0.0038 62  GLN   A C   
1503 O O   . GLN   A 62  ? 0.1045 0.1067 0.1411 -0.0036 0.0030  -0.0021 62  GLN   A O   
1504 C CB  . GLN   A 62  ? 0.0993 0.0944 0.1277 -0.0000 -0.0026 -0.0024 62  GLN   A CB  
1505 C CG  . GLN   A 62  ? 0.1030 0.0921 0.1342 -0.0020 0.0002  0.0088  62  GLN   A CG  
1506 C CD  . GLN   A 62  ? 0.1121 0.0994 0.1290 -0.0018 0.0049  0.0108  62  GLN   A CD  
1507 O OE1 . GLN   A 62  ? 0.1208 0.1090 0.1394 -0.0044 0.0002  -0.0014 62  GLN   A OE1 
1508 N NE2 . GLN   A 62  ? 0.1186 0.1033 0.1403 0.0022  -0.0029 -0.0045 62  GLN   A NE2 
1517 N N   . VAL   A 63  ? 0.0976 0.0985 0.1467 -0.0061 0.0040  -0.0212 63  VAL   A N   
1518 C CA  . VAL   A 63  ? 0.1026 0.1072 0.1692 -0.0131 0.0001  -0.0204 63  VAL   A CA  
1519 C C   . VAL   A 63  ? 0.0899 0.1092 0.1551 -0.0115 -0.0088 -0.0196 63  VAL   A C   
1520 O O   . VAL   A 63  ? 0.0918 0.1112 0.1752 -0.0119 -0.0018 -0.0171 63  VAL   A O   
1521 C CB  . VAL   A 63  ? 0.1162 0.1244 0.1994 -0.0168 -0.0015 -0.0412 63  VAL   A CB  
1522 C CG1 . VAL   A 63  ? 0.1294 0.1489 0.2284 -0.0162 -0.0109 -0.0618 63  VAL   A CG1 
1523 C CG2 . VAL   A 63  ? 0.1220 0.1173 0.2189 -0.0124 0.0105  -0.0373 63  VAL   A CG2 
1533 N N   . GLU   A 64  ? 0.0950 0.1157 0.1356 -0.0012 -0.0031 -0.0170 64  GLU   A N   
1534 C CA  . GLU   A 64  ? 0.0962 0.1131 0.1469 -0.0054 -0.0089 -0.0131 64  GLU   A CA  
1535 C C   . GLU   A 64  ? 0.0873 0.1101 0.1420 -0.0085 -0.0001 -0.0025 64  GLU   A C   
1536 O O   . GLU   A 64  ? 0.0968 0.1172 0.1460 -0.0003 -0.0023 -0.0060 64  GLU   A O   
1537 C CB  . GLU   A 64  ? 0.1000 0.1174 0.1449 -0.0055 0.0015  -0.0121 64  GLU   A CB  
1538 C CG  . GLU   A 64  ? 0.1158 0.1282 0.1646 -0.0088 0.0077  -0.0142 64  GLU   A CG  
1539 C CD  . GLU   A 64  ? 0.1247 0.1334 0.1716 -0.0148 0.0087  -0.0179 64  GLU   A CD  
1540 O OE1 . GLU   A 64  ? 0.1219 0.1475 0.1869 -0.0181 0.0148  -0.0137 64  GLU   A OE1 
1541 O OE2 . GLU   A 64  ? 0.1447 0.1352 0.1649 -0.0234 0.0023  -0.0018 64  GLU   A OE2 
1548 N N   . SER   A 65  ? 0.0864 0.1077 0.1340 0.0014  0.0061  -0.0107 65  SER   A N   
1549 C CA  . SER   A 65  ? 0.0949 0.1005 0.1308 -0.0011 0.0005  -0.0064 65  SER   A CA  
1550 C C   . SER   A 65  ? 0.0962 0.1101 0.1332 -0.0012 -0.0027 0.0011  65  SER   A C   
1551 O O   . SER   A 65  ? 0.1057 0.1141 0.1500 0.0014  0.0108  -0.0089 65  SER   A O   
1552 C CB  . SER   A 65  ? 0.0966 0.1039 0.1222 -0.0028 0.0070  -0.0018 65  SER   A CB  
1553 O OG  . SER   A 65  ? 0.0975 0.1148 0.1384 -0.0086 -0.0020 0.0067  65  SER   A OG  
1559 N N   . ASP   A 66  ? 0.1019 0.1054 0.1391 -0.0038 0.0132  0.0044  66  ASP   A N   
1560 C CA  . ASP   A 66  ? 0.1136 0.1122 0.1595 -0.0028 0.0133  0.0112  66  ASP   A CA  
1561 C C   . ASP   A 66  ? 0.1096 0.1112 0.1607 -0.0078 0.0207  0.0100  66  ASP   A C   
1562 O O   . ASP   A 66  ? 0.1153 0.1236 0.1750 -0.0042 0.0250  0.0173  66  ASP   A O   
1563 C CB  . ASP   A 66  ? 0.1220 0.1262 0.1825 0.0085  0.0121  0.0217  66  ASP   A CB  
1564 C CG  . ASP   A 66  ? 0.1425 0.1399 0.2166 0.0055  0.0021  0.0399  66  ASP   A CG  
1565 O OD1 . ASP   A 66  ? 0.1399 0.1713 0.1996 -0.0065 -0.0105 0.0419  66  ASP   A OD1 
1566 O OD2 . ASP   A 66  ? 0.1633 0.1556 0.3051 0.0240  -0.0150 0.0241  66  ASP   A OD2 
1571 N N   . ASP   A 67  ? 0.1046 0.1156 0.1706 -0.0025 0.0118  0.0090  67  ASP   A N   
1572 C CA  . ASP   A 67  ? 0.1014 0.1277 0.1795 -0.0052 0.0053  0.0154  67  ASP   A CA  
1573 C C   . ASP   A 67  ? 0.1028 0.1271 0.1677 0.0029  0.0066  0.0212  67  ASP   A C   
1574 O O   . ASP   A 67  ? 0.0981 0.1389 0.1866 0.0003  0.0250  0.0231  67  ASP   A O   
1575 C CB  . ASP   A 67  ? 0.1125 0.1401 0.2187 -0.0067 -0.0122 0.0186  67  ASP   A CB  
1576 C CG  . ASP   A 67  ? 0.1096 0.1497 0.2423 -0.0051 -0.0291 0.0226  67  ASP   A CG  
1577 O OD1 . ASP   A 67  ? 0.1159 0.1613 0.3250 -0.0109 -0.0366 0.0325  67  ASP   A OD1 
1578 O OD2 . ASP   A 67  ? 0.1122 0.1545 0.2249 0.0072  -0.0173 0.0180  67  ASP   A OD2 
1583 N N   . TYR   A 68  ? 0.1033 0.1130 0.1578 0.0040  0.0149  0.0184  68  TYR   A N   
1584 C CA  . TYR   A 68  ? 0.1101 0.1131 0.1600 -0.0008 0.0166  0.0236  68  TYR   A CA  
1585 C C   . TYR   A 68  ? 0.1047 0.1142 0.1587 0.0027  0.0214  0.0134  68  TYR   A C   
1586 O O   . TYR   A 68  ? 0.1121 0.1170 0.1676 0.0070  0.0339  0.0193  68  TYR   A O   
1587 C CB  . TYR   A 68  ? 0.1164 0.1082 0.1723 0.0073  0.0330  0.0193  68  TYR   A CB  
1588 C CG  . TYR   A 68  ? 0.1243 0.1306 0.2075 0.0052  0.0586  0.0264  68  TYR   A CG  
1589 C CD1 . TYR   A 68  ? 0.1365 0.1386 0.2367 -0.0226 0.0474  -0.0089 68  TYR   A CD1 
1590 C CD2 . TYR   A 68  ? 0.1510 0.1255 0.2387 0.0121  0.0610  0.0419  68  TYR   A CD2 
1591 C CE1 . TYR   A 68  ? 0.1432 0.1476 0.2721 -0.0218 0.0560  -0.0182 68  TYR   A CE1 
1592 C CE2 . TYR   A 68  ? 0.1487 0.1330 0.2543 0.0047  0.0651  0.0190  68  TYR   A CE2 
1593 C CZ  . TYR   A 68  ? 0.1492 0.1415 0.2786 -0.0194 0.0574  -0.0124 68  TYR   A CZ  
1594 O OH  . TYR   A 68  ? 0.1750 0.1400 0.3045 -0.0155 0.0281  -0.0320 68  TYR   A OH  
1604 N N   . ILE   A 69  ? 0.1014 0.1075 0.1659 0.0017  0.0205  0.0139  69  ILE   A N   
1605 C CA  . ILE   A 69  ? 0.1123 0.1146 0.1476 0.0039  0.0164  0.0004  69  ILE   A CA  
1606 C C   . ILE   A 69  ? 0.1173 0.1104 0.1455 0.0028  0.0183  0.0097  69  ILE   A C   
1607 O O   . ILE   A 69  ? 0.1270 0.1240 0.1374 -0.0040 0.0236  0.0155  69  ILE   A O   
1608 C CB  . ILE   A 69  ? 0.1207 0.1379 0.1491 0.0065  0.0145  -0.0025 69  ILE   A CB  
1609 C CG1 . ILE   A 69  ? 0.1154 0.1536 0.1610 0.0067  0.0176  -0.0262 69  ILE   A CG1 
1610 C CG2 . ILE   A 69  ? 0.1414 0.1599 0.1705 0.0129  -0.0016 -0.0087 69  ILE   A CG2 
1611 C CD1 . ILE   A 69  ? 0.1201 0.1623 0.1771 -0.0056 0.0161  -0.0327 69  ILE   A CD1 
1623 N N   . ALA   A 70  ? 0.1228 0.1144 0.1494 -0.0068 0.0273  0.0075  70  ALA   A N   
1624 C CA  . ALA   A 70  ? 0.1224 0.1259 0.1748 -0.0117 0.0282  0.0173  70  ALA   A CA  
1625 C C   . ALA   A 70  ? 0.1157 0.1395 0.1674 -0.0143 0.0284  0.0156  70  ALA   A C   
1626 O O   . ALA   A 70  ? 0.1358 0.1727 0.1909 -0.0043 0.0465  0.0287  70  ALA   A O   
1627 C CB  . ALA   A 70  ? 0.1218 0.1189 0.2029 -0.0172 0.0226  0.0107  70  ALA   A CB  
1633 N N   . THR   A 71  ? 0.1137 0.1370 0.1537 -0.0044 0.0190  0.0179  71  THR   A N   
1634 C CA  . THR   A 71  ? 0.1206 0.1553 0.1862 0.0026  0.0220  0.0200  71  THR   A CA  
1635 C C   . THR   A 71  ? 0.1135 0.1508 0.2025 0.0072  0.0367  0.0145  71  THR   A C   
1636 O O   . THR   A 71  ? 0.1211 0.1763 0.2431 0.0078  0.0398  -0.0086 71  THR   A O   
1637 C CB  . THR   A 71  ? 0.1426 0.1795 0.2107 0.0112  -0.0123 0.0224  71  THR   A CB  
1638 O OG1 . THR   A 71  ? 0.1620 0.1946 0.2220 0.0085  -0.0319 0.0126  71  THR   A OG1 
1639 C CG2 . THR   A 71  ? 0.1571 0.1995 0.2362 0.0220  -0.0200 0.0359  71  THR   A CG2 
1647 N N   . ASN   A 72  ? 0.1151 0.1290 0.1816 0.0074  0.0323  0.0171  72  ASN   A N   
1648 C CA  . ASN   A 72  ? 0.1236 0.1332 0.1858 0.0128  0.0362  0.0204  72  ASN   A CA  
1649 C C   . ASN   A 72  ? 0.1313 0.1335 0.1776 0.0078  0.0486  0.0056  72  ASN   A C   
1650 O O   . ASN   A 72  ? 0.1456 0.1380 0.2142 0.0145  0.0395  -0.0068 72  ASN   A O   
1651 C CB  . ASN   A 72  ? 0.1398 0.1373 0.1887 0.0143  0.0350  0.0156  72  ASN   A CB  
1652 C CG  . ASN   A 72  ? 0.1641 0.1487 0.1902 0.0300  0.0325  0.0224  72  ASN   A CG  
1653 O OD1 . ASN   A 72  ? 0.1800 0.1804 0.2070 0.0285  0.0411  0.0212  72  ASN   A OD1 
1654 N ND2 . ASN   A 72  ? 0.1808 0.1550 0.1909 0.0531  0.0137  0.0149  72  ASN   A ND2 
1661 N N   . GLY   A 73  ? 0.1341 0.1325 0.1623 0.0043  0.0355  0.0020  73  GLY   A N   
1662 C CA  . GLY   A 73  ? 0.1377 0.1292 0.1625 -0.0064 0.0387  0.0017  73  GLY   A CA  
1663 C C   . GLY   A 73  ? 0.1378 0.1199 0.1387 0.0002  0.0520  0.0113  73  GLY   A C   
1664 O O   . GLY   A 73  ? 0.1357 0.1243 0.1521 0.0052  0.0434  0.0199  73  GLY   A O   
1668 N N   . PRO   A 74  ? 0.1430 0.1199 0.1405 -0.0125 0.0432  0.0140  74  PRO   A N   
1669 C CA  . PRO   A 74  ? 0.1417 0.1211 0.1492 -0.0076 0.0445  0.0167  74  PRO   A CA  
1670 C C   . PRO   A 74  ? 0.1335 0.1083 0.1428 -0.0019 0.0281  0.0068  74  PRO   A C   
1671 O O   . PRO   A 74  ? 0.1453 0.1128 0.1735 0.0051  0.0352  -0.0130 74  PRO   A O   
1672 C CB  . PRO   A 74  ? 0.1573 0.1512 0.1692 -0.0005 0.0424  0.0292  74  PRO   A CB  
1673 C CG  . PRO   A 74  ? 0.1825 0.1844 0.2147 -0.0147 0.0337  0.0204  74  PRO   A CG  
1674 C CD  . PRO   A 74  ? 0.1640 0.1601 0.1636 -0.0200 0.0388  0.0058  74  PRO   A CD  
1682 N N   . LEU   A 75  ? 0.1286 0.0992 0.1303 -0.0023 0.0246  0.0027  75  LEU   A N   
1683 C CA  . LEU   A 75  ? 0.1345 0.1040 0.1199 0.0013  0.0104  0.0036  75  LEU   A CA  
1684 C C   . LEU   A 75  ? 0.1405 0.1098 0.1279 0.0045  0.0232  0.0056  75  LEU   A C   
1685 O O   . LEU   A 75  ? 0.1718 0.1245 0.1286 0.0090  0.0134  0.0057  75  LEU   A O   
1686 C CB  . LEU   A 75  ? 0.1420 0.1093 0.1090 -0.0115 0.0069  0.0109  75  LEU   A CB  
1687 C CG  . LEU   A 75  ? 0.1596 0.1420 0.1337 -0.0433 0.0048  0.0083  75  LEU   A CG  
1688 C CD1 . LEU   A 75  ? 0.1701 0.1906 0.1496 -0.0387 0.0036  -0.0068 75  LEU   A CD1 
1689 C CD2 . LEU   A 75  ? 0.1864 0.1840 0.1859 -0.0189 0.0097  0.0051  75  LEU   A CD2 
1701 N N   . LYS   A 76  ? 0.1463 0.1159 0.1290 -0.0067 0.0167  -0.0073 76  LYS   A N   
1702 C CA  . LYS   A 76  ? 0.1449 0.1357 0.1333 -0.0056 0.0146  -0.0198 76  LYS   A CA  
1703 C C   . LYS   A 76  ? 0.1340 0.1103 0.1168 -0.0058 0.0171  -0.0006 76  LYS   A C   
1704 O O   . LYS   A 76  ? 0.1409 0.1102 0.1073 -0.0011 0.0231  0.0094  76  LYS   A O   
1705 C CB  . LYS   A 76  ? 0.1490 0.1636 0.1822 0.0061  0.0197  -0.0449 76  LYS   A CB  
1706 C CG  . LYS   A 76  ? 0.1579 0.1588 0.2447 0.0091  0.0132  -0.0483 76  LYS   A CG  
1707 C CD  . LYS   A 76  ? 0.1615 0.1526 0.2959 0.0175  0.0024  -0.0553 76  LYS   A CD  
1708 C CE  . LYS   A 76  ? 0.1752 0.1751 0.3551 0.0134  0.0100  -0.0521 76  LYS   A CE  
1709 N NZ  . LYS   A 76  ? 0.1739 0.1726 0.3932 -0.0002 0.0032  -0.0539 76  LYS   A NZ  
1723 N N   . VAL   A 77  ? 0.1440 0.1202 0.1165 -0.0011 0.0315  0.0083  77  VAL   A N   
1724 C CA  . VAL   A 77  ? 0.1434 0.1208 0.1116 0.0065  0.0270  0.0107  77  VAL   A CA  
1725 C C   . VAL   A 77  ? 0.1310 0.1122 0.1012 0.0077  0.0161  0.0018  77  VAL   A C   
1726 O O   . VAL   A 77  ? 0.1393 0.1217 0.1104 0.0124  0.0337  -0.0048 77  VAL   A O   
1727 C CB  . VAL   A 77  ? 0.1575 0.1404 0.1136 0.0104  0.0159  0.0158  77  VAL   A CB  
1728 C CG1 . VAL   A 77  ? 0.1560 0.1528 0.1352 0.0209  0.0055  0.0026  77  VAL   A CG1 
1729 C CG2 . VAL   A 77  ? 0.1854 0.1582 0.1352 0.0054  0.0041  0.0263  77  VAL   A CG2 
1739 N N   . GLY   A 78  ? 0.1308 0.1126 0.1027 0.0042  0.0242  0.0032  78  GLY   A N   
1740 C CA  . GLY   A 78  ? 0.1265 0.1106 0.1173 0.0007  0.0242  0.0053  78  GLY   A CA  
1741 C C   . GLY   A 78  ? 0.1173 0.1045 0.1142 0.0062  0.0286  0.0050  78  GLY   A C   
1742 O O   . GLY   A 78  ? 0.1188 0.1115 0.1291 0.0034  0.0244  0.0199  78  GLY   A O   
1746 N N   . GLY   A 79  ? 0.1184 0.1032 0.1125 0.0008  0.0233  0.0109  79  GLY   A N   
1747 C CA  . GLY   A 79  ? 0.1171 0.1069 0.1219 0.0034  0.0232  0.0065  79  GLY   A CA  
1748 C C   . GLY   A 79  ? 0.1053 0.1007 0.1198 0.0021  0.0150  0.0023  79  GLY   A C   
1749 O O   . GLY   A 79  ? 0.1124 0.1116 0.1216 0.0196  0.0172  0.0033  79  GLY   A O   
1753 N N   . SER   A 80  ? 0.1000 0.1184 0.1391 0.0043  0.0189  -0.0068 80  SER   A N   
1754 C CA  . SER   A 80  ? 0.1011 0.1075 0.1278 0.0017  0.0058  -0.0034 80  SER   A CA  
1755 C C   . SER   A 80  ? 0.1002 0.1084 0.1288 0.0014  0.0132  0.0072  80  SER   A C   
1756 O O   . SER   A 80  ? 0.1004 0.1325 0.1615 0.0101  0.0186  -0.0092 80  SER   A O   
1757 C CB  . SER   A 80  ? 0.1177 0.1110 0.1465 -0.0025 0.0081  -0.0039 80  SER   A CB  
1758 O OG  . SER   A 80  ? 0.1443 0.1154 0.1757 0.0068  -0.0017 0.0139  80  SER   A OG  
1764 N N   . CYS   A 81  ? 0.0928 0.1029 0.1250 0.0017  -0.0030 0.0023  81  CYS   A N   
1765 C CA  . CYS   A 81  ? 0.0947 0.1124 0.1164 -0.0024 -0.0031 0.0094  81  CYS   A CA  
1766 C C   . CYS   A 81  ? 0.0909 0.1052 0.1202 -0.0058 0.0026  0.0180  81  CYS   A C   
1767 O O   . CYS   A 81  ? 0.0959 0.1353 0.1326 0.0025  0.0046  0.0263  81  CYS   A O   
1768 C CB  . CYS   A 81  ? 0.1065 0.1225 0.1350 -0.0112 0.0011  0.0159  81  CYS   A CB  
1769 S SG  . CYS   A 81  ? 0.1202 0.1118 0.1236 -0.0128 0.0038  0.0081  81  CYS   A SG  
1775 N N   . VAL   A 82  ? 0.0963 0.1161 0.1219 0.0030  -0.0088 0.0084  82  VAL   A N   
1776 C CA  . VAL   A 82  ? 0.1061 0.1166 0.1174 0.0031  -0.0119 0.0169  82  VAL   A CA  
1777 C C   . VAL   A 82  ? 0.1054 0.1261 0.1241 0.0024  -0.0098 0.0159  82  VAL   A C   
1778 O O   . VAL   A 82  ? 0.1009 0.1374 0.1490 0.0030  -0.0071 -0.0046 82  VAL   A O   
1779 C CB  . VAL   A 82  ? 0.1433 0.1300 0.1309 0.0051  -0.0001 0.0171  82  VAL   A CB  
1780 C CG1 . VAL   A 82  ? 0.1643 0.1411 0.1445 0.0076  0.0075  0.0163  82  VAL   A CG1 
1781 C CG2 . VAL   A 82  ? 0.1552 0.1341 0.1649 0.0012  -0.0057 0.0268  82  VAL   A CG2 
1791 N N   . LEU   A 83  ? 0.1010 0.1164 0.1200 -0.0042 -0.0074 0.0118  83  LEU   A N   
1792 C CA  . LEU   A 83  ? 0.1049 0.1227 0.1230 -0.0114 -0.0147 0.0062  83  LEU   A CA  
1793 C C   . LEU   A 83  ? 0.1061 0.1278 0.1096 -0.0083 -0.0176 0.0093  83  LEU   A C   
1794 O O   . LEU   A 83  ? 0.1177 0.1247 0.1209 -0.0075 -0.0078 0.0105  83  LEU   A O   
1795 C CB  . LEU   A 83  ? 0.1147 0.1249 0.1216 -0.0114 -0.0098 0.0055  83  LEU   A CB  
1796 C CG  . LEU   A 83  ? 0.1285 0.1361 0.1285 -0.0069 0.0050  0.0037  83  LEU   A CG  
1797 C CD1 . LEU   A 83  ? 0.1382 0.1470 0.1352 -0.0248 0.0075  0.0123  83  LEU   A CD1 
1798 C CD2 . LEU   A 83  ? 0.1278 0.1498 0.1515 -0.0068 0.0207  0.0117  83  LEU   A CD2 
1810 N N   . SER   A 84  ? 0.1199 0.1328 0.1143 -0.0109 -0.0076 0.0106  84  SER   A N   
1811 C CA  . SER   A 84  ? 0.1328 0.1374 0.1066 -0.0077 -0.0101 0.0010  84  SER   A CA  
1812 C C   . SER   A 84  ? 0.1305 0.1304 0.1069 -0.0148 -0.0021 0.0033  84  SER   A C   
1813 O O   . SER   A 84  ? 0.1245 0.1415 0.1086 -0.0097 -0.0054 -0.0015 84  SER   A O   
1814 C CB  . SER   A 84  ? 0.1329 0.1588 0.1109 -0.0076 -0.0094 -0.0097 84  SER   A CB  
1815 O OG  . SER   A 84  ? 0.1445 0.1722 0.1192 -0.0067 -0.0195 -0.0213 84  SER   A OG  
1821 N N   . GLY   A 85  ? 0.1429 0.1432 0.1056 -0.0179 0.0031  0.0011  85  GLY   A N   
1822 C CA  . GLY   A 85  ? 0.1471 0.1531 0.1166 -0.0237 0.0132  -0.0027 85  GLY   A CA  
1823 C C   . GLY   A 85  ? 0.1405 0.1588 0.0941 -0.0163 0.0037  -0.0041 85  GLY   A C   
1824 O O   . GLY   A 85  ? 0.1402 0.1684 0.1029 -0.0217 0.0118  -0.0169 85  GLY   A O   
1828 N N   . HIS   A 86  ? 0.1459 0.1460 0.0916 -0.0117 -0.0039 -0.0013 86  HIS   A N   
1829 C CA  . HIS   A 86  ? 0.1563 0.1557 0.0966 -0.0168 -0.0013 -0.0036 86  HIS   A CA  
1830 C C   . HIS   A 86  ? 0.1728 0.1700 0.0920 -0.0174 -0.0081 -0.0089 86  HIS   A C   
1831 O O   . HIS   A 86  ? 0.1845 0.1936 0.0939 -0.0111 -0.0005 -0.0056 86  HIS   A O   
1832 C CB  . HIS   A 86  ? 0.1567 0.1500 0.1146 -0.0091 0.0044  -0.0082 86  HIS   A CB  
1833 C CG  . HIS   A 86  ? 0.1535 0.1428 0.1246 -0.0034 0.0042  -0.0002 86  HIS   A CG  
1834 N ND1 . HIS   A 86  ? 0.1572 0.1418 0.1519 -0.0167 0.0100  0.0037  86  HIS   A ND1 
1835 C CD2 . HIS   A 86  ? 0.1526 0.1384 0.1212 0.0004  0.0098  0.0020  86  HIS   A CD2 
1836 C CE1 . HIS   A 86  ? 0.1554 0.1427 0.1435 -0.0129 0.0220  0.0119  86  HIS   A CE1 
1837 N NE2 . HIS   A 86  ? 0.1527 0.1352 0.1273 0.0039  0.0233  0.0182  86  HIS   A NE2 
1845 N N   . ASN   A 87  ? 0.1814 0.1740 0.1026 -0.0117 0.0146  -0.0119 87  ASN   A N   
1846 C CA  . ASN   A 87  ? 0.2013 0.1892 0.1111 -0.0047 0.0370  -0.0163 87  ASN   A CA  
1847 C C   . ASN   A 87  ? 0.2021 0.1992 0.1437 -0.0049 0.0553  -0.0100 87  ASN   A C   
1848 O O   . ASN   A 87  ? 0.2290 0.2181 0.1980 -0.0152 0.0848  -0.0155 87  ASN   A O   
1849 C CB  . ASN   A 87  ? 0.2169 0.1989 0.1222 -0.0014 0.0317  -0.0170 87  ASN   A CB  
1850 C CG  . ASN   A 87  ? 0.2318 0.2052 0.1285 0.0118  0.0369  -0.0171 87  ASN   A CG  
1851 O OD1 . ASN   A 87  ? 0.2470 0.2042 0.1412 0.0344  0.0348  -0.0070 87  ASN   A OD1 
1852 N ND2 . ASN   A 87  ? 0.2382 0.2251 0.1429 0.0126  0.0322  -0.0085 87  ASN   A ND2 
1859 N N   . LEU   A 88  ? 0.1735 0.1947 0.1308 -0.0130 0.0309  0.0049  88  LEU   A N   
1860 C CA  . LEU   A 88  ? 0.1619 0.1974 0.1526 -0.0229 0.0185  0.0224  88  LEU   A CA  
1861 C C   . LEU   A 88  ? 0.1592 0.1956 0.1449 -0.0223 0.0141  0.0290  88  LEU   A C   
1862 O O   . LEU   A 88  ? 0.1629 0.2035 0.1842 -0.0277 0.0213  0.0488  88  LEU   A O   
1863 C CB  . LEU   A 88  ? 0.1714 0.2079 0.1642 -0.0330 -0.0127 0.0339  88  LEU   A CB  
1864 C CG  . LEU   A 88  ? 0.1928 0.2260 0.1957 -0.0302 -0.0247 0.0363  88  LEU   A CG  
1865 C CD1 . LEU   A 88  ? 0.2041 0.2298 0.1890 -0.0318 -0.0234 0.0284  88  LEU   A CD1 
1866 C CD2 . LEU   A 88  ? 0.2103 0.2394 0.2279 -0.0225 -0.0264 0.0312  88  LEU   A CD2 
1878 N N   . ALA   A 89  ? 0.1560 0.1811 0.1221 -0.0238 0.0153  0.0028  89  ALA   A N   
1879 C CA  . ALA   A 89  ? 0.1603 0.1737 0.0948 -0.0235 0.0062  0.0111  89  ALA   A CA  
1880 C C   . ALA   A 89  ? 0.1668 0.1764 0.1013 -0.0185 -0.0109 0.0056  89  ALA   A C   
1881 O O   . ALA   A 89  ? 0.1659 0.1735 0.1432 -0.0208 -0.0202 -0.0159 89  ALA   A O   
1882 C CB  . ALA   A 89  ? 0.1567 0.1792 0.0948 -0.0204 -0.0014 0.0116  89  ALA   A CB  
1888 N N   . LYS   A 90  ? 0.1783 0.1910 0.1075 -0.0239 -0.0248 0.0128  90  LYS   A N   
1889 C CA  . LYS   A 90  ? 0.1913 0.2058 0.1176 -0.0230 -0.0413 0.0126  90  LYS   A CA  
1890 C C   . LYS   A 90  ? 0.1703 0.1850 0.1170 -0.0205 -0.0325 0.0103  90  LYS   A C   
1891 O O   . LYS   A 90  ? 0.1749 0.2033 0.1418 -0.0241 -0.0377 -0.0009 90  LYS   A O   
1892 C CB  . LYS   A 90  ? 0.2217 0.2419 0.1527 -0.0179 -0.0522 0.0325  90  LYS   A CB  
1893 C CG  . LYS   A 90  ? 0.2572 0.2770 0.2511 -0.0157 -0.0559 0.0456  90  LYS   A CG  
1894 C CD  . LYS   A 90  ? 0.2950 0.3100 0.3589 -0.0187 -0.0451 0.0461  90  LYS   A CD  
1895 C CE  . LYS   A 90  ? 0.3338 0.3437 0.4264 -0.0208 -0.0339 0.0409  90  LYS   A CE  
1896 N NZ  . LYS   A 90  ? 0.3483 0.3575 0.4793 -0.0215 -0.0287 0.0359  90  LYS   A NZ  
1910 N N   . HIS   A 91  ? 0.1556 0.1602 0.0942 -0.0203 -0.0305 0.0117  91  HIS   A N   
1911 C CA  . HIS   A 91  ? 0.1402 0.1462 0.0982 -0.0095 -0.0254 0.0109  91  HIS   A CA  
1912 C C   . HIS   A 91  ? 0.1259 0.1318 0.0908 -0.0112 -0.0052 0.0084  91  HIS   A C   
1913 O O   . HIS   A 91  ? 0.1239 0.1484 0.0943 -0.0172 -0.0013 0.0125  91  HIS   A O   
1914 C CB  . HIS   A 91  ? 0.1517 0.1698 0.1412 0.0126  -0.0367 0.0094  91  HIS   A CB  
1915 C CG  . HIS   A 91  ? 0.1950 0.2207 0.2233 0.0195  -0.0713 -0.0029 91  HIS   A CG  
1916 N ND1 . HIS   A 91  ? 0.2079 0.2517 0.2655 0.0191  -0.0797 -0.0218 91  HIS   A ND1 
1917 C CD2 . HIS   A 91  ? 0.2252 0.2427 0.2496 0.0266  -0.0802 0.0078  91  HIS   A CD2 
1918 C CE1 . HIS   A 91  ? 0.2217 0.2597 0.2773 0.0249  -0.0823 -0.0113 91  HIS   A CE1 
1919 N NE2 . HIS   A 91  ? 0.2380 0.2586 0.2698 0.0294  -0.0876 -0.0010 91  HIS   A NE2 
1927 N N   . CYS   A 92  ? 0.1160 0.1269 0.0979 -0.0158 -0.0054 0.0098  92  CYS   A N   
1928 C CA  . CYS   A 92  ? 0.1079 0.1222 0.1015 -0.0123 -0.0009 0.0025  92  CYS   A CA  
1929 C C   . CYS   A 92  ? 0.1018 0.1188 0.0932 -0.0109 0.0022  0.0118  92  CYS   A C   
1930 O O   . CYS   A 92  ? 0.1048 0.1256 0.1104 -0.0111 -0.0028 0.0046  92  CYS   A O   
1931 C CB  . CYS   A 92  ? 0.1179 0.1271 0.1087 -0.0033 -0.0046 0.0081  92  CYS   A CB  
1932 S SG  . CYS   A 92  ? 0.1131 0.1139 0.1093 -0.0076 -0.0030 0.0067  92  CYS   A SG  
1938 N N   . LEU   A 93  ? 0.0998 0.1065 0.1018 -0.0082 0.0085  0.0119  93  LEU   A N   
1939 C CA  . LEU   A 93  ? 0.0966 0.1020 0.0916 -0.0006 0.0087  0.0085  93  LEU   A CA  
1940 C C   . LEU   A 93  ? 0.0914 0.0935 0.0909 -0.0006 0.0046  0.0057  93  LEU   A C   
1941 O O   . LEU   A 93  ? 0.0915 0.1044 0.0938 -0.0007 0.0038  0.0106  93  LEU   A O   
1942 C CB  . LEU   A 93  ? 0.1002 0.1019 0.1049 0.0016  0.0000  0.0172  93  LEU   A CB  
1943 C CG  . LEU   A 93  ? 0.1076 0.1022 0.1163 0.0030  0.0034  0.0189  93  LEU   A CG  
1944 C CD1 . LEU   A 93  ? 0.1160 0.1111 0.1515 0.0011  0.0148  0.0130  93  LEU   A CD1 
1945 C CD2 . LEU   A 93  ? 0.1198 0.1001 0.1335 -0.0025 0.0043  0.0122  93  LEU   A CD2 
1957 N N   . HIS   A 94  ? 0.0877 0.0945 0.0915 -0.0029 0.0050  0.0118  94  HIS   A N   
1958 C CA  . HIS   A 94  ? 0.0885 0.0943 0.0996 -0.0053 -0.0006 0.0101  94  HIS   A CA  
1959 C C   . HIS   A 94  ? 0.0891 0.0923 0.0966 -0.0021 0.0019  0.0040  94  HIS   A C   
1960 O O   . HIS   A 94  ? 0.0938 0.1180 0.1324 0.0008  0.0060  -0.0131 94  HIS   A O   
1961 C CB  . HIS   A 94  ? 0.0908 0.0928 0.1073 0.0001  0.0034  0.0079  94  HIS   A CB  
1962 C CG  . HIS   A 94  ? 0.0953 0.0966 0.0915 -0.0046 -0.0029 0.0112  94  HIS   A CG  
1963 N ND1 . HIS   A 94  ? 0.0955 0.0916 0.1089 -0.0045 -0.0008 0.0132  94  HIS   A ND1 
1964 C CD2 . HIS   A 94  ? 0.1046 0.1056 0.1094 -0.0015 -0.0087 0.0034  94  HIS   A CD2 
1965 C CE1 . HIS   A 94  ? 0.1022 0.0974 0.1045 -0.0094 -0.0058 0.0021  94  HIS   A CE1 
1966 N NE2 . HIS   A 94  ? 0.1051 0.1007 0.1133 -0.0056 -0.0060 0.0069  94  HIS   A NE2 
1974 N N   . VAL   A 95  ? 0.0869 0.0935 0.0849 -0.0001 0.0094  0.0054  95  VAL   A N   
1975 C CA  . VAL   A 95  ? 0.0960 0.0864 0.0894 -0.0031 0.0108  0.0052  95  VAL   A CA  
1976 C C   . VAL   A 95  ? 0.0943 0.0910 0.0831 -0.0081 0.0077  0.0067  95  VAL   A C   
1977 O O   . VAL   A 95  ? 0.1018 0.1028 0.0945 0.0084  0.0087  0.0022  95  VAL   A O   
1978 C CB  . VAL   A 95  ? 0.1038 0.0962 0.1013 -0.0042 0.0051  0.0058  95  VAL   A CB  
1979 C CG1 . VAL   A 95  ? 0.1145 0.1053 0.1184 -0.0097 0.0078  -0.0044 95  VAL   A CG1 
1980 C CG2 . VAL   A 95  ? 0.1058 0.0985 0.1074 -0.0080 0.0118  0.0136  95  VAL   A CG2 
1990 N N   A VAL   A 96  ? 0.0964 0.0926 0.0812 -0.0038 0.0093  0.0052  96  VAL   A N   
1991 N N   B VAL   A 96  ? 0.0974 0.0925 0.0823 -0.0014 0.0086  0.0058  96  VAL   A N   
1992 C CA  A VAL   A 96  ? 0.1078 0.0981 0.0886 -0.0035 0.0106  0.0077  96  VAL   A CA  
1993 C CA  B VAL   A 96  ? 0.1082 0.0985 0.0898 0.0021  0.0121  0.0077  96  VAL   A CA  
1994 C C   A VAL   A 96  ? 0.1109 0.1052 0.0938 -0.0010 0.0195  0.0025  96  VAL   A C   
1995 C C   B VAL   A 96  ? 0.1102 0.1052 0.0864 0.0008  0.0174  0.0072  96  VAL   A C   
1996 O O   A VAL   A 96  ? 0.1180 0.1104 0.1221 -0.0039 0.0267  -0.0145 96  VAL   A O   
1997 O O   B VAL   A 96  ? 0.1171 0.1110 0.0974 -0.0037 0.0191  -0.0057 96  VAL   A O   
1998 C CB  A VAL   A 96  ? 0.1099 0.0977 0.0994 -0.0069 0.0164  0.0130  96  VAL   A CB  
1999 C CB  B VAL   A 96  ? 0.1125 0.1009 0.1064 0.0038  0.0222  0.0081  96  VAL   A CB  
2000 C CG1 A VAL   A 96  ? 0.1111 0.1010 0.0952 -0.0061 0.0107  0.0119  96  VAL   A CG1 
2001 C CG1 B VAL   A 96  ? 0.1223 0.1132 0.1096 0.0030  0.0206  0.0079  96  VAL   A CG1 
2002 C CG2 A VAL   A 96  ? 0.1139 0.1016 0.1078 -0.0156 0.0148  0.0198  96  VAL   A CG2 
2003 C CG2 B VAL   A 96  ? 0.1090 0.1002 0.1187 0.0024  0.0190  0.0077  96  VAL   A CG2 
2022 N N   . GLY   A 97  ? 0.1104 0.1059 0.0966 -0.0048 0.0165  0.0005  97  GLY   A N   
2023 C CA  . GLY   A 97  ? 0.1161 0.1136 0.0863 -0.0008 0.0056  0.0073  97  GLY   A CA  
2024 C C   . GLY   A 97  ? 0.1216 0.1252 0.0793 -0.0019 0.0076  0.0012  97  GLY   A C   
2025 O O   . GLY   A 97  ? 0.1299 0.1281 0.1019 -0.0032 0.0012  0.0126  97  GLY   A O   
2030 N N   . PRO   A 98  ? 0.1280 0.1313 0.0751 0.0019  0.0031  0.0121  98  PRO   A N   
2031 C CA  . PRO   A 98  ? 0.1407 0.1531 0.0935 -0.0037 0.0082  0.0059  98  PRO   A CA  
2032 C C   . PRO   A 98  ? 0.1449 0.1605 0.0873 -0.0131 0.0040  0.0235  98  PRO   A C   
2033 O O   . PRO   A 98  ? 0.1412 0.1448 0.1108 -0.0072 -0.0011 0.0256  98  PRO   A O   
2034 C CB  . PRO   A 98  ? 0.1541 0.1672 0.0758 0.0035  0.0019  -0.0079 98  PRO   A CB  
2035 C CG  . PRO   A 98  ? 0.1501 0.1574 0.0945 0.0054  -0.0050 -0.0108 98  PRO   A CG  
2036 C CD  . PRO   A 98  ? 0.1359 0.1387 0.0806 0.0023  -0.0016 -0.0013 98  PRO   A CD  
2044 N N   A ASN   A 99  ? 0.1497 0.1798 0.0890 -0.0080 0.0133  0.0398  99  ASN   A N   
2045 N N   B ASN   A 99  ? 0.1625 0.1776 0.1024 -0.0057 -0.0069 0.0407  99  ASN   A N   
2046 C CA  A ASN   A 99  ? 0.1581 0.1924 0.0934 -0.0098 0.0171  0.0563  99  ASN   A CA  
2047 C CA  B ASN   A 99  ? 0.1824 0.1889 0.1205 -0.0025 -0.0171 0.0534  99  ASN   A CA  
2048 C C   A ASN   A 99  ? 0.1687 0.2200 0.0902 -0.0208 0.0221  0.0576  99  ASN   A C   
2049 C C   B ASN   A 99  ? 0.1990 0.2093 0.1076 -0.0018 -0.0101 0.0485  99  ASN   A C   
2050 O O   A ASN   A 99  ? 0.1754 0.2216 0.0931 -0.0128 0.0146  0.0657  99  ASN   A O   
2051 O O   B ASN   A 99  ? 0.2011 0.2091 0.1154 0.0167  -0.0146 0.0541  99  ASN   A O   
2052 C CB  A ASN   A 99  ? 0.1600 0.1861 0.1086 -0.0055 0.0054  0.0606  99  ASN   A CB  
2053 C CB  B ASN   A 99  ? 0.1884 0.1886 0.1618 -0.0061 -0.0358 0.0620  99  ASN   A CB  
2054 C CG  A ASN   A 99  ? 0.1633 0.1887 0.1296 -0.0017 -0.0014 0.0396  99  ASN   A CG  
2055 C CG  B ASN   A 99  ? 0.1960 0.1936 0.1934 -0.0087 -0.0424 0.0537  99  ASN   A CG  
2056 O OD1 A ASN   A 99  ? 0.1726 0.1954 0.1343 0.0049  -0.0035 0.0329  99  ASN   A OD1 
2057 O OD1 B ASN   A 99  ? 0.2037 0.1990 0.1872 -0.0076 -0.0458 0.0499  99  ASN   A OD1 
2058 N ND2 A ASN   A 99  ? 0.1693 0.1882 0.1497 0.0006  -0.0051 0.0408  99  ASN   A ND2 
2059 N ND2 B ASN   A 99  ? 0.2019 0.1952 0.2102 -0.0073 -0.0382 0.0511  99  ASN   A ND2 
2072 N N   A VAL   A 100 ? 0.1802 0.2384 0.0968 -0.0322 0.0017  0.0567  100 VAL   A N   
2073 N N   B VAL   A 100 ? 0.2157 0.2233 0.0922 -0.0145 -0.0269 0.0375  100 VAL   A N   
2074 C CA  A VAL   A 100 ? 0.2037 0.2634 0.1279 -0.0371 -0.0114 0.0572  100 VAL   A CA  
2075 C CA  B VAL   A 100 ? 0.2396 0.2395 0.1223 -0.0227 -0.0304 0.0321  100 VAL   A CA  
2076 C C   A VAL   A 100 ? 0.2101 0.2796 0.1297 -0.0454 -0.0136 0.0789  100 VAL   A C   
2077 C C   B VAL   A 100 ? 0.2457 0.2508 0.1058 -0.0320 -0.0330 0.0517  100 VAL   A C   
2078 O O   A VAL   A 100 ? 0.2167 0.2948 0.1498 -0.0401 -0.0074 0.0683  100 VAL   A O   
2079 O O   B VAL   A 100 ? 0.2493 0.2564 0.1159 -0.0266 -0.0149 0.0458  100 VAL   A O   
2080 C CB  A VAL   A 100 ? 0.2232 0.2650 0.1579 -0.0400 -0.0210 0.0462  100 VAL   A CB  
2081 C CB  B VAL   A 100 ? 0.2576 0.2406 0.1639 -0.0299 -0.0305 0.0248  100 VAL   A CB  
2082 C CG1 A VAL   A 100 ? 0.2267 0.2713 0.1800 -0.0442 -0.0182 0.0438  100 VAL   A CG1 
2083 C CG1 B VAL   A 100 ? 0.2615 0.2476 0.1901 -0.0319 -0.0259 0.0212  100 VAL   A CG1 
2084 C CG2 A VAL   A 100 ? 0.2318 0.2649 0.1756 -0.0384 -0.0255 0.0371  100 VAL   A CG2 
2085 C CG2 B VAL   A 100 ? 0.2665 0.2404 0.1808 -0.0338 -0.0284 0.0229  100 VAL   A CG2 
2104 N N   A ASN   A 101 ? 0.2193 0.2802 0.1501 -0.0500 -0.0199 0.1064  101 ASN   A N   
2105 N N   B ASN   A 101 ? 0.2584 0.2666 0.1360 -0.0433 -0.0401 0.0786  101 ASN   A N   
2106 C CA  A ASN   A 101 ? 0.2433 0.2838 0.1700 -0.0572 -0.0294 0.1171  101 ASN   A CA  
2107 C CA  B ASN   A 101 ? 0.2795 0.2887 0.1756 -0.0559 -0.0350 0.0913  101 ASN   A CA  
2108 C C   A ASN   A 101 ? 0.2657 0.3104 0.1921 -0.0558 -0.0076 0.1315  101 ASN   A C   
2109 C C   B ASN   A 101 ? 0.2983 0.3156 0.2162 -0.0704 -0.0078 0.1060  101 ASN   A C   
2110 O O   A ASN   A 101 ? 0.2793 0.3201 0.2061 -0.0586 -0.0140 0.1404  101 ASN   A O   
2111 O O   B ASN   A 101 ? 0.3103 0.3220 0.2490 -0.0721 -0.0088 0.1005  101 ASN   A O   
2112 C CB  A ASN   A 101 ? 0.2455 0.2609 0.1702 -0.0630 -0.0568 0.1091  101 ASN   A CB  
2113 C CB  B ASN   A 101 ? 0.2825 0.2888 0.1878 -0.0495 -0.0531 0.0834  101 ASN   A CB  
2114 C CG  A ASN   A 101 ? 0.2480 0.2436 0.1564 -0.0710 -0.0773 0.0744  101 ASN   A CG  
2115 C CG  B ASN   A 101 ? 0.2852 0.2892 0.1798 -0.0454 -0.0646 0.0683  101 ASN   A CG  
2116 O OD1 A ASN   A 101 ? 0.2453 0.2373 0.1548 -0.0723 -0.0672 0.0447  101 ASN   A OD1 
2117 O OD1 B ASN   A 101 ? 0.2828 0.2949 0.1771 -0.0375 -0.0624 0.0466  101 ASN   A OD1 
2118 N ND2 A ASN   A 101 ? 0.2552 0.2304 0.1506 -0.0826 -0.0869 0.0721  101 ASN   A ND2 
2119 N ND2 B ASN   A 101 ? 0.2914 0.2835 0.1748 -0.0486 -0.0731 0.0761  101 ASN   A ND2 
2132 N N   A LYS   A 102 ? 0.2739 0.3366 0.2156 -0.0591 0.0089  0.1394  102 LYS   A N   
2133 N N   B LYS   A 102 ? 0.3002 0.3398 0.2385 -0.0769 0.0052  0.1018  102 LYS   A N   
2134 C CA  A LYS   A 102 ? 0.2876 0.3588 0.2353 -0.0579 0.0107  0.1246  102 LYS   A CA  
2135 C CA  B LYS   A 102 ? 0.3080 0.3658 0.2537 -0.0736 0.0057  0.0834  102 LYS   A CA  
2136 C C   A LYS   A 102 ? 0.2952 0.3785 0.2115 -0.0513 0.0135  0.1182  102 LYS   A C   
2137 C C   B LYS   A 102 ? 0.3134 0.3861 0.2490 -0.0674 0.0174  0.0706  102 LYS   A C   
2138 O O   A LYS   A 102 ? 0.2981 0.3901 0.2091 -0.0507 0.0246  0.1175  102 LYS   A O   
2139 O O   B LYS   A 102 ? 0.3162 0.3965 0.2445 -0.0676 0.0241  0.0673  102 LYS   A O   
2140 C CB  A LYS   A 102 ? 0.2952 0.3637 0.2699 -0.0635 0.0033  0.1086  102 LYS   A CB  
2141 C CB  B LYS   A 102 ? 0.3125 0.3715 0.2722 -0.0731 -0.0116 0.0722  102 LYS   A CB  
2142 C CG  A LYS   A 102 ? 0.3052 0.3677 0.2966 -0.0658 -0.0068 0.0902  102 LYS   A CG  
2143 C CG  B LYS   A 102 ? 0.3186 0.3759 0.2813 -0.0712 -0.0299 0.0623  102 LYS   A CG  
2144 C CD  A LYS   A 102 ? 0.3188 0.3755 0.3162 -0.0643 -0.0149 0.0687  102 LYS   A CD  
2145 C CD  B LYS   A 102 ? 0.3260 0.3818 0.2811 -0.0679 -0.0464 0.0503  102 LYS   A CD  
2146 C CE  A LYS   A 102 ? 0.3312 0.3827 0.3341 -0.0601 -0.0201 0.0521  102 LYS   A CE  
2147 C CE  B LYS   A 102 ? 0.3338 0.3860 0.2885 -0.0637 -0.0590 0.0414  102 LYS   A CE  
2148 N NZ  A LYS   A 102 ? 0.3388 0.3864 0.3423 -0.0587 -0.0221 0.0403  102 LYS   A NZ  
2149 N NZ  B LYS   A 102 ? 0.3367 0.3871 0.2844 -0.0635 -0.0651 0.0346  102 LYS   A NZ  
2176 N N   A GLY   A 103 ? 0.2974 0.3876 0.2110 -0.0391 -0.0030 0.0907  103 GLY   A N   
2177 N N   B GLY   A 103 ? 0.3135 0.3949 0.2497 -0.0583 0.0150  0.0494  103 GLY   A N   
2178 C CA  A GLY   A 103 ? 0.2978 0.3897 0.2013 -0.0309 -0.0049 0.0689  103 GLY   A CA  
2179 C CA  B GLY   A 103 ? 0.3111 0.3998 0.2342 -0.0504 0.0167  0.0355  103 GLY   A CA  
2180 C C   A GLY   A 103 ? 0.2928 0.3917 0.1907 -0.0273 0.0001  0.0453  103 GLY   A C   
2181 C C   B GLY   A 103 ? 0.3049 0.4042 0.2309 -0.0439 0.0248  0.0244  103 GLY   A C   
2182 O O   A GLY   A 103 ? 0.2966 0.3965 0.2006 -0.0278 0.0012  0.0377  103 GLY   A O   
2183 O O   B GLY   A 103 ? 0.3114 0.4118 0.2349 -0.0454 0.0238  0.0164  103 GLY   A O   
2190 N N   A GLU   A 104 ? 0.2814 0.3858 0.1468 -0.0249 0.0052  0.0324  104 GLU   A N   
2191 N N   B GLU   A 104 ? 0.2881 0.3956 0.1908 -0.0386 0.0349  0.0244  104 GLU   A N   
2192 C CA  A GLU   A 104 ? 0.2654 0.3760 0.1201 -0.0271 0.0058  0.0175  104 GLU   A CA  
2193 C CA  B GLU   A 104 ? 0.2669 0.3836 0.1655 -0.0393 0.0396  0.0232  104 GLU   A CA  
2194 C C   A GLU   A 104 ? 0.2591 0.3793 0.1037 -0.0315 0.0188  -0.0081 104 GLU   A C   
2195 C C   B GLU   A 104 ? 0.2670 0.3962 0.1754 -0.0395 0.0312  -0.0022 104 GLU   A C   
2196 O O   A GLU   A 104 ? 0.2521 0.3810 0.1128 -0.0320 0.0149  -0.0214 104 GLU   A O   
2197 O O   B GLU   A 104 ? 0.2656 0.4042 0.1888 -0.0412 0.0295  -0.0102 104 GLU   A O   
2198 C CB  A GLU   A 104 ? 0.2518 0.3631 0.1190 -0.0262 -0.0079 0.0346  104 GLU   A CB  
2199 C CB  B GLU   A 104 ? 0.2430 0.3593 0.1390 -0.0426 0.0528  0.0469  104 GLU   A CB  
2200 C CG  A GLU   A 104 ? 0.2444 0.3531 0.1417 -0.0227 -0.0198 0.0451  104 GLU   A CG  
2201 C CG  B GLU   A 104 ? 0.2251 0.3364 0.1390 -0.0425 0.0528  0.0596  104 GLU   A CG  
2202 C CD  A GLU   A 104 ? 0.2384 0.3442 0.1549 -0.0195 -0.0267 0.0561  104 GLU   A CD  
2203 C CD  B GLU   A 104 ? 0.2101 0.3081 0.1351 -0.0407 0.0504  0.0652  104 GLU   A CD  
2204 O OE1 A GLU   A 104 ? 0.2314 0.3382 0.1383 -0.0152 -0.0337 0.0649  104 GLU   A OE1 
2205 O OE1 B GLU   A 104 ? 0.1948 0.2877 0.1175 -0.0376 0.0430  0.0556  104 GLU   A OE1 
2206 O OE2 A GLU   A 104 ? 0.2480 0.3439 0.1920 -0.0208 -0.0194 0.0573  104 GLU   A OE2 
2207 O OE2 B GLU   A 104 ? 0.2201 0.3044 0.1498 -0.0427 0.0460  0.0841  104 GLU   A OE2 
2220 N N   A ASP   A 105 ? 0.2617 0.3825 0.1245 -0.0338 0.0344  -0.0266 105 ASP   A N   
2221 N N   B ASP   A 105 ? 0.2665 0.4000 0.1690 -0.0369 0.0324  -0.0237 105 ASP   A N   
2222 C CA  A ASP   A 105 ? 0.2556 0.3805 0.1664 -0.0348 0.0426  -0.0464 105 ASP   A CA  
2223 C CA  B ASP   A 105 ? 0.2633 0.4003 0.1875 -0.0314 0.0258  -0.0469 105 ASP   A CA  
2224 C C   A ASP   A 105 ? 0.2261 0.3606 0.1477 -0.0417 0.0342  -0.0562 105 ASP   A C   
2225 C C   B ASP   A 105 ? 0.2431 0.3834 0.1501 -0.0378 0.0122  -0.0626 105 ASP   A C   
2226 O O   A ASP   A 105 ? 0.2059 0.3432 0.1200 -0.0402 0.0360  -0.0703 105 ASP   A O   
2227 O O   B ASP   A 105 ? 0.2271 0.3675 0.1245 -0.0387 -0.0027 -0.0788 105 ASP   A O   
2228 C CB  A ASP   A 105 ? 0.2730 0.3951 0.2209 -0.0303 0.0563  -0.0515 105 ASP   A CB  
2229 C CB  B ASP   A 105 ? 0.2779 0.4135 0.2461 -0.0188 0.0282  -0.0472 105 ASP   A CB  
2230 C CG  A ASP   A 105 ? 0.2867 0.4053 0.2764 -0.0263 0.0567  -0.0592 105 ASP   A CG  
2231 C CG  B ASP   A 105 ? 0.2946 0.4266 0.3045 -0.0065 0.0245  -0.0492 105 ASP   A CG  
2232 O OD1 A ASP   A 105 ? 0.2870 0.4098 0.2840 -0.0252 0.0459  -0.0732 105 ASP   A OD1 
2233 O OD1 B ASP   A 105 ? 0.2987 0.4328 0.3288 -0.0001 0.0231  -0.0472 105 ASP   A OD1 
2234 O OD2 A ASP   A 105 ? 0.2942 0.4101 0.3040 -0.0264 0.0678  -0.0564 105 ASP   A OD2 
2235 O OD2 B ASP   A 105 ? 0.3051 0.4306 0.3263 -0.0027 0.0234  -0.0499 105 ASP   A OD2 
2244 N N   A ILE   A 106 ? 0.2131 0.3581 0.1626 -0.0525 0.0080  -0.0562 106 ILE   A N   
2245 N N   B ILE   A 106 ? 0.2374 0.3792 0.1629 -0.0448 0.0061  -0.0617 106 ILE   A N   
2246 C CA  A ILE   A 106 ? 0.1900 0.3461 0.1766 -0.0649 -0.0153 -0.0700 106 ILE   A CA  
2247 C CA  B ILE   A 106 ? 0.2265 0.3670 0.1824 -0.0488 0.0033  -0.0707 106 ILE   A CA  
2248 C C   A ILE   A 106 ? 0.1699 0.3213 0.1879 -0.0812 -0.0095 -0.0937 106 ILE   A C   
2249 C C   B ILE   A 106 ? 0.2166 0.3386 0.1965 -0.0524 0.0076  -0.0933 106 ILE   A C   
2250 O O   A ILE   A 106 ? 0.1519 0.3078 0.1831 -0.0792 0.0067  -0.1010 106 ILE   A O   
2251 O O   B ILE   A 106 ? 0.2096 0.3289 0.2009 -0.0473 0.0245  -0.1067 106 ILE   A O   
2252 C CB  A ILE   A 106 ? 0.1922 0.3568 0.2080 -0.0561 -0.0404 -0.0499 106 ILE   A CB  
2253 C CB  B ILE   A 106 ? 0.2286 0.3791 0.2196 -0.0444 -0.0024 -0.0538 106 ILE   A CB  
2254 C CG1 A ILE   A 106 ? 0.1867 0.3545 0.2266 -0.0474 -0.0525 -0.0335 106 ILE   A CG1 
2255 C CG1 B ILE   A 106 ? 0.2275 0.3779 0.2426 -0.0412 0.0014  -0.0406 106 ILE   A CG1 
2256 C CG2 A ILE   A 106 ? 0.1967 0.3645 0.2170 -0.0554 -0.0425 -0.0508 106 ILE   A CG2 
2257 C CG2 B ILE   A 106 ? 0.2327 0.3871 0.2408 -0.0440 -0.0067 -0.0472 106 ILE   A CG2 
2258 C CD1 A ILE   A 106 ? 0.1865 0.3507 0.2417 -0.0371 -0.0464 -0.0240 106 ILE   A CD1 
2259 C CD1 B ILE   A 106 ? 0.2299 0.3750 0.2519 -0.0358 0.0082  -0.0339 106 ILE   A CD1 
2282 N N   A GLN   A 107 ? 0.1856 0.3092 0.2165 -0.0824 0.0033  -0.1035 107 GLN   A N   
2283 N N   B GLN   A 107 ? 0.2237 0.3213 0.2378 -0.0533 0.0087  -0.0957 107 GLN   A N   
2284 C CA  A GLN   A 107 ? 0.2090 0.2966 0.2859 -0.0684 0.0306  -0.0980 107 GLN   A CA  
2285 C CA  B GLN   A 107 ? 0.2302 0.3003 0.2882 -0.0462 0.0269  -0.0946 107 GLN   A CA  
2286 C C   A GLN   A 107 ? 0.1956 0.2545 0.2751 -0.0589 0.0485  -0.0779 107 GLN   A C   
2287 C C   B GLN   A 107 ? 0.2047 0.2558 0.2771 -0.0480 0.0444  -0.0772 107 GLN   A C   
2288 O O   A GLN   A 107 ? 0.2073 0.2504 0.3292 -0.0510 0.0553  -0.0712 107 GLN   A O   
2289 O O   B GLN   A 107 ? 0.2138 0.2500 0.3228 -0.0402 0.0524  -0.0749 107 GLN   A O   
2290 C CB  A GLN   A 107 ? 0.2421 0.3227 0.3664 -0.0706 0.0336  -0.0953 107 GLN   A CB  
2291 C CB  B GLN   A 107 ? 0.2597 0.3220 0.3620 -0.0436 0.0154  -0.0925 107 GLN   A CB  
2292 C CG  A GLN   A 107 ? 0.2751 0.3473 0.4510 -0.0667 0.0328  -0.0874 107 GLN   A CG  
2293 C CG  B GLN   A 107 ? 0.2855 0.3412 0.4431 -0.0403 0.0065  -0.0826 107 GLN   A CG  
2294 C CD  A GLN   A 107 ? 0.3006 0.3654 0.5176 -0.0639 0.0327  -0.0783 107 GLN   A CD  
2295 C CD  B GLN   A 107 ? 0.3075 0.3531 0.5063 -0.0359 -0.0019 -0.0698 107 GLN   A CD  
2296 O OE1 A GLN   A 107 ? 0.3084 0.3700 0.5448 -0.0632 0.0333  -0.0788 107 GLN   A OE1 
2297 O OE1 B GLN   A 107 ? 0.3166 0.3564 0.5303 -0.0357 -0.0048 -0.0636 107 GLN   A OE1 
2298 N NE2 A GLN   A 107 ? 0.3117 0.3720 0.5413 -0.0630 0.0305  -0.0761 107 GLN   A NE2 
2299 N NE2 B GLN   A 107 ? 0.3135 0.3552 0.5207 -0.0334 -0.0032 -0.0683 107 GLN   A NE2 
2316 N N   . LEU   A 108 ? 0.1721 0.2138 0.2168 -0.0552 0.0493  -0.0793 108 LEU   A N   
2317 C CA  . LEU   A 108 ? 0.1546 0.1623 0.1878 -0.0213 0.0471  -0.0313 108 LEU   A CA  
2318 C C   . LEU   A 108 ? 0.1283 0.1252 0.1873 -0.0065 0.0300  0.0060  108 LEU   A C   
2319 O O   . LEU   A 108 ? 0.1208 0.1279 0.1954 -0.0028 0.0346  0.0161  108 LEU   A O   
2320 C CB  . LEU   A 108 ? 0.1603 0.1704 0.1502 -0.0294 0.0471  -0.0225 108 LEU   A CB  
2321 C CG  . LEU   A 108 ? 0.1808 0.1982 0.1668 -0.0274 0.0553  -0.0194 108 LEU   A CG  
2322 C CD1 . LEU   A 108 ? 0.2027 0.2096 0.1679 -0.0386 0.0622  -0.0183 108 LEU   A CD1 
2323 C CD2 . LEU   A 108 ? 0.1854 0.2227 0.2144 -0.0111 0.0513  -0.0044 108 LEU   A CD2 
2336 N N   . LEU   A 109 ? 0.1209 0.1257 0.1728 0.0036  0.0239  0.0216  109 LEU   A N   
2337 C CA  . LEU   A 109 ? 0.1201 0.1162 0.1473 0.0007  0.0183  0.0224  109 LEU   A CA  
2338 C C   . LEU   A 109 ? 0.1084 0.1107 0.1400 -0.0055 0.0135  0.0051  109 LEU   A C   
2339 O O   . LEU   A 109 ? 0.1187 0.0954 0.1567 -0.0028 0.0007  -0.0014 109 LEU   A O   
2340 C CB  . LEU   A 109 ? 0.1270 0.1273 0.1547 0.0091  0.0074  0.0348  109 LEU   A CB  
2341 C CG  . LEU   A 109 ? 0.1215 0.1302 0.1526 0.0073  0.0195  0.0325  109 LEU   A CG  
2342 C CD1 . LEU   A 109 ? 0.1244 0.1229 0.1835 0.0124  0.0244  0.0061  109 LEU   A CD1 
2343 C CD2 . LEU   A 109 ? 0.1265 0.1522 0.1719 0.0091  0.0117  0.0360  109 LEU   A CD2 
2355 N N   . LYS   A 110 ? 0.1077 0.1074 0.1256 -0.0015 0.0097  0.0044  110 LYS   A N   
2356 C CA  . LYS   A 110 ? 0.1046 0.1050 0.1291 -0.0036 0.0110  0.0066  110 LYS   A CA  
2357 C C   . LYS   A 110 ? 0.1090 0.1045 0.1167 -0.0061 0.0097  -0.0045 110 LYS   A C   
2358 O O   . LYS   A 110 ? 0.1051 0.1043 0.1277 -0.0060 0.0128  -0.0023 110 LYS   A O   
2359 C CB  . LYS   A 110 ? 0.1151 0.1098 0.1420 -0.0032 -0.0016 -0.0036 110 LYS   A CB  
2360 C CG  . LYS   A 110 ? 0.1172 0.1091 0.1484 -0.0041 -0.0022 -0.0045 110 LYS   A CG  
2361 C CD  . LYS   A 110 ? 0.1191 0.1159 0.1607 -0.0075 -0.0022 -0.0051 110 LYS   A CD  
2362 C CE  . LYS   A 110 ? 0.1299 0.1176 0.1850 -0.0063 0.0100  -0.0076 110 LYS   A CE  
2363 N NZ  . LYS   A 110 ? 0.1348 0.1177 0.2076 -0.0131 0.0123  -0.0017 110 LYS   A NZ  
2377 N N   . SER   A 111 ? 0.1103 0.1073 0.1221 -0.0015 0.0083  0.0034  111 SER   A N   
2378 C CA  . SER   A 111 ? 0.1038 0.1170 0.1347 -0.0003 0.0112  0.0017  111 SER   A CA  
2379 C C   . SER   A 111 ? 0.0977 0.1026 0.1314 -0.0067 0.0113  0.0089  111 SER   A C   
2380 O O   . SER   A 111 ? 0.1098 0.0984 0.1447 -0.0056 0.0118  0.0068  111 SER   A O   
2381 C CB  . SER   A 111 ? 0.1223 0.1323 0.1455 -0.0027 0.0271  -0.0061 111 SER   A CB  
2382 O OG  . SER   A 111 ? 0.1653 0.1525 0.1635 -0.0001 0.0307  -0.0128 111 SER   A OG  
2388 N N   . ALA   A 112 ? 0.1006 0.0966 0.1333 0.0022  0.0172  0.0085  112 ALA   A N   
2389 C CA  . ALA   A 112 ? 0.1091 0.0948 0.1250 -0.0007 0.0198  0.0028  112 ALA   A CA  
2390 C C   . ALA   A 112 ? 0.1018 0.0887 0.1298 -0.0002 0.0115  0.0000  112 ALA   A C   
2391 O O   . ALA   A 112 ? 0.1041 0.0904 0.1355 -0.0102 0.0129  0.0012  112 ALA   A O   
2392 C CB  . ALA   A 112 ? 0.1196 0.0966 0.1326 -0.0044 0.0159  0.0027  112 ALA   A CB  
2398 N N   . TYR   A 113 ? 0.0910 0.0980 0.1389 -0.0052 0.0107  0.0088  113 TYR   A N   
2399 C CA  . TYR   A 113 ? 0.0906 0.0906 0.1341 0.0003  0.0173  0.0104  113 TYR   A CA  
2400 C C   . TYR   A 113 ? 0.0879 0.0948 0.1219 -0.0083 0.0117  0.0028  113 TYR   A C   
2401 O O   . TYR   A 113 ? 0.0951 0.0991 0.1311 -0.0041 0.0146  0.0020  113 TYR   A O   
2402 C CB  . TYR   A 113 ? 0.0971 0.1024 0.1334 -0.0016 0.0007  0.0171  113 TYR   A CB  
2403 C CG  . TYR   A 113 ? 0.0960 0.1065 0.1246 -0.0066 0.0081  0.0199  113 TYR   A CG  
2404 C CD1 . TYR   A 113 ? 0.0988 0.1189 0.1114 -0.0003 0.0056  0.0210  113 TYR   A CD1 
2405 C CD2 . TYR   A 113 ? 0.1025 0.1076 0.1230 -0.0094 0.0013  0.0128  113 TYR   A CD2 
2406 C CE1 . TYR   A 113 ? 0.1027 0.1255 0.1246 0.0013  0.0105  0.0259  113 TYR   A CE1 
2407 C CE2 . TYR   A 113 ? 0.0989 0.1191 0.1314 -0.0069 0.0032  0.0187  113 TYR   A CE2 
2408 C CZ  . TYR   A 113 ? 0.0989 0.1216 0.1266 0.0035  0.0111  0.0266  113 TYR   A CZ  
2409 O OH  . TYR   A 113 ? 0.1007 0.1324 0.1407 0.0112  0.0101  0.0304  113 TYR   A OH  
2419 N N   . GLU   A 114 ? 0.0966 0.0886 0.1345 -0.0045 0.0138  0.0078  114 GLU   A N   
2420 C CA  . GLU   A 114 ? 0.0966 0.0890 0.1351 0.0052  0.0114  0.0098  114 GLU   A CA  
2421 C C   . GLU   A 114 ? 0.0940 0.0950 0.1366 0.0075  0.0095  0.0069  114 GLU   A C   
2422 O O   . GLU   A 114 ? 0.1036 0.0950 0.1335 0.0019  0.0047  0.0066  114 GLU   A O   
2423 C CB  . GLU   A 114 ? 0.1014 0.0936 0.1366 -0.0003 0.0047  0.0104  114 GLU   A CB  
2424 C CG  . GLU   A 114 ? 0.1043 0.0946 0.1419 0.0052  0.0075  -0.0004 114 GLU   A CG  
2425 C CD  . GLU   A 114 ? 0.1114 0.0949 0.1580 -0.0025 0.0070  0.0054  114 GLU   A CD  
2426 O OE1 . GLU   A 114 ? 0.1182 0.1007 0.1572 -0.0060 0.0153  -0.0061 114 GLU   A OE1 
2427 O OE2 . GLU   A 114 ? 0.1270 0.1005 0.1834 -0.0071 0.0084  -0.0122 114 GLU   A OE2 
2434 N N   . ASN   A 115 ? 0.0981 0.0918 0.1323 -0.0025 0.0099  0.0082  115 ASN   A N   
2435 C CA  . ASN   A 115 ? 0.0964 0.0971 0.1314 -0.0082 0.0120  0.0054  115 ASN   A CA  
2436 C C   . ASN   A 115 ? 0.0984 0.0927 0.1256 -0.0103 0.0054  -0.0010 115 ASN   A C   
2437 O O   . ASN   A 115 ? 0.1013 0.1090 0.1236 -0.0076 0.0093  0.0073  115 ASN   A O   
2438 C CB  . ASN   A 115 ? 0.1060 0.1042 0.1224 -0.0140 0.0153  0.0016  115 ASN   A CB  
2439 C CG  . ASN   A 115 ? 0.1065 0.1279 0.1310 -0.0200 0.0214  -0.0004 115 ASN   A CG  
2440 O OD1 . ASN   A 115 ? 0.1143 0.2285 0.1579 -0.0224 0.0272  0.0193  115 ASN   A OD1 
2441 N ND2 . ASN   A 115 ? 0.1118 0.1122 0.1303 -0.0105 0.0241  0.0096  115 ASN   A ND2 
2448 N N   . PHE   A 116 ? 0.0966 0.0947 0.1261 -0.0003 0.0148  0.0099  116 PHE   A N   
2449 C CA  . PHE   A 116 ? 0.0991 0.1029 0.1192 -0.0038 0.0158  0.0094  116 PHE   A CA  
2450 C C   . PHE   A 116 ? 0.0929 0.1088 0.1275 -0.0037 0.0148  0.0139  116 PHE   A C   
2451 O O   . PHE   A 116 ? 0.1037 0.1129 0.1302 0.0034  0.0109  0.0172  116 PHE   A O   
2452 C CB  . PHE   A 116 ? 0.0984 0.0991 0.1289 -0.0022 0.0166  0.0053  116 PHE   A CB  
2453 C CG  . PHE   A 116 ? 0.0977 0.1002 0.1111 -0.0020 0.0189  0.0045  116 PHE   A CG  
2454 C CD1 . PHE   A 116 ? 0.1005 0.0997 0.1252 -0.0053 0.0210  0.0111  116 PHE   A CD1 
2455 C CD2 . PHE   A 116 ? 0.1009 0.1065 0.1299 0.0010  0.0188  0.0133  116 PHE   A CD2 
2456 C CE1 . PHE   A 116 ? 0.1039 0.0954 0.1333 -0.0099 0.0170  0.0049  116 PHE   A CE1 
2457 C CE2 . PHE   A 116 ? 0.1031 0.1038 0.1360 -0.0023 0.0182  0.0052  116 PHE   A CE2 
2458 C CZ  . PHE   A 116 ? 0.1044 0.0942 0.1296 0.0001  0.0098  0.0073  116 PHE   A CZ  
2468 N N   . ASN   A 117 ? 0.0959 0.1013 0.1381 0.0005  0.0134  0.0158  117 ASN   A N   
2469 C CA  . ASN   A 117 ? 0.0976 0.1016 0.1353 0.0006  0.0133  0.0187  117 ASN   A CA  
2470 C C   . ASN   A 117 ? 0.1013 0.1089 0.1378 0.0011  0.0123  0.0152  117 ASN   A C   
2471 O O   . ASN   A 117 ? 0.1083 0.1139 0.1603 -0.0031 -0.0032 0.0308  117 ASN   A O   
2472 C CB  . ASN   A 117 ? 0.0998 0.1037 0.1452 0.0001  0.0072  0.0226  117 ASN   A CB  
2473 C CG  . ASN   A 117 ? 0.0977 0.1018 0.1444 0.0003  0.0127  0.0212  117 ASN   A CG  
2474 O OD1 . ASN   A 117 ? 0.0990 0.1248 0.1560 -0.0107 0.0152  0.0148  117 ASN   A OD1 
2475 N ND2 . ASN   A 117 ? 0.0984 0.1077 0.1421 -0.0009 0.0087  0.0196  117 ASN   A ND2 
2482 N N   . GLN   A 118 ? 0.0999 0.1097 0.1454 -0.0046 0.0030  0.0170  118 GLN   A N   
2483 C CA  . GLN   A 118 ? 0.1052 0.1187 0.1503 -0.0005 -0.0046 0.0117  118 GLN   A CA  
2484 C C   . GLN   A 118 ? 0.1076 0.1211 0.1397 -0.0010 -0.0037 0.0134  118 GLN   A C   
2485 O O   . GLN   A 118 ? 0.1092 0.1589 0.1642 0.0068  -0.0135 -0.0080 118 GLN   A O   
2486 C CB  . GLN   A 118 ? 0.0997 0.1195 0.1642 -0.0036 0.0016  0.0134  118 GLN   A CB  
2487 C CG  . GLN   A 118 ? 0.0986 0.1224 0.1718 -0.0029 0.0060  0.0153  118 GLN   A CG  
2488 C CD  . GLN   A 118 ? 0.0935 0.1291 0.1791 -0.0021 0.0116  0.0114  118 GLN   A CD  
2489 O OE1 . GLN   A 118 ? 0.1033 0.1416 0.1881 0.0092  -0.0004 0.0056  118 GLN   A OE1 
2490 N NE2 . GLN   A 118 ? 0.1100 0.1184 0.1842 0.0010  0.0026  0.0173  118 GLN   A NE2 
2499 N N   . HIS   A 119 ? 0.1112 0.1209 0.1268 -0.0044 0.0015  0.0167  119 HIS   A N   
2500 C CA  . HIS   A 119 ? 0.1175 0.1245 0.1317 -0.0045 -0.0034 0.0212  119 HIS   A CA  
2501 C C   . HIS   A 119 ? 0.1223 0.1318 0.1255 0.0033  -0.0001 0.0208  119 HIS   A C   
2502 O O   . HIS   A 119 ? 0.1292 0.1383 0.1281 -0.0224 0.0039  0.0210  119 HIS   A O   
2503 C CB  . HIS   A 119 ? 0.1208 0.1250 0.1470 -0.0032 0.0183  0.0221  119 HIS   A CB  
2504 C CG  . HIS   A 119 ? 0.1278 0.1281 0.1869 0.0010  0.0150  0.0292  119 HIS   A CG  
2505 N ND1 . HIS   A 119 ? 0.1354 0.1490 0.2414 -0.0080 0.0115  0.0172  119 HIS   A ND1 
2506 C CD2 . HIS   A 119 ? 0.1375 0.1338 0.2068 0.0132  0.0330  0.0480  119 HIS   A CD2 
2507 C CE1 . HIS   A 119 ? 0.1364 0.1464 0.2607 -0.0097 0.0309  0.0322  119 HIS   A CE1 
2508 N NE2 . HIS   A 119 ? 0.1517 0.1380 0.2489 0.0096  0.0476  0.0527  119 HIS   A NE2 
2516 N N   . GLU   A 120 ? 0.1271 0.1457 0.1287 0.0053  -0.0005 0.0413  120 GLU   A N   
2517 C CA  . GLU   A 120 ? 0.1484 0.1767 0.1626 0.0172  0.0000  0.0712  120 GLU   A CA  
2518 C C   . GLU   A 120 ? 0.1294 0.1575 0.1342 -0.0012 -0.0029 0.0598  120 GLU   A C   
2519 O O   . GLU   A 120 ? 0.1348 0.1506 0.1408 -0.0061 -0.0014 0.0563  120 GLU   A O   
2520 C CB  . GLU   A 120 ? 0.2163 0.2541 0.2151 0.0471  -0.0202 0.1248  120 GLU   A CB  
2521 C CG  . GLU   A 120 ? 0.3268 0.3480 0.3496 0.0655  -0.0305 0.1407  120 GLU   A CG  
2522 C CD  . GLU   A 120 ? 0.4325 0.4360 0.4869 0.0735  -0.0173 0.1234  120 GLU   A CD  
2523 O OE1 . GLU   A 120 ? 0.4564 0.4511 0.5302 0.0754  -0.0142 0.1156  120 GLU   A OE1 
2524 O OE2 . GLU   A 120 ? 0.4963 0.4963 0.5496 0.0751  -0.0096 0.1168  120 GLU   A OE2 
2531 N N   . VAL   A 121 ? 0.1275 0.1568 0.1176 -0.0024 -0.0006 0.0454  121 VAL   A N   
2532 C CA  . VAL   A 121 ? 0.1335 0.1646 0.1070 -0.0018 0.0112  0.0442  121 VAL   A CA  
2533 C C   . VAL   A 121 ? 0.1192 0.1474 0.0966 -0.0094 0.0045  0.0312  121 VAL   A C   
2534 O O   . VAL   A 121 ? 0.1230 0.1560 0.1152 -0.0158 -0.0088 0.0278  121 VAL   A O   
2535 C CB  . VAL   A 121 ? 0.1720 0.2056 0.1408 0.0132  0.0249  0.0557  121 VAL   A CB  
2536 C CG1 . VAL   A 121 ? 0.1809 0.2282 0.1334 0.0219  0.0367  0.0619  121 VAL   A CG1 
2537 C CG2 . VAL   A 121 ? 0.1940 0.2270 0.1798 0.0085  0.0240  0.0440  121 VAL   A CG2 
2547 N N   . LEU   A 122 ? 0.1140 0.1269 0.1062 -0.0118 0.0060  0.0340  122 LEU   A N   
2548 C CA  . LEU   A 122 ? 0.1210 0.1203 0.1144 -0.0155 0.0246  0.0236  122 LEU   A CA  
2549 C C   . LEU   A 122 ? 0.1113 0.1179 0.1007 -0.0148 0.0058  0.0251  122 LEU   A C   
2550 O O   . LEU   A 122 ? 0.1147 0.1234 0.1431 -0.0213 0.0034  0.0255  122 LEU   A O   
2551 C CB  . LEU   A 122 ? 0.1406 0.1273 0.1521 -0.0061 0.0180  0.0356  122 LEU   A CB  
2552 C CG  . LEU   A 122 ? 0.1445 0.1334 0.1309 -0.0051 0.0204  0.0230  122 LEU   A CG  
2553 C CD1 . LEU   A 122 ? 0.1676 0.1329 0.1537 -0.0136 0.0217  0.0271  122 LEU   A CD1 
2554 C CD2 . LEU   A 122 ? 0.1405 0.1244 0.1273 0.0008  0.0276  0.0138  122 LEU   A CD2 
2566 N N   . LEU   A 123 ? 0.1106 0.1180 0.0980 -0.0135 0.0057  0.0228  123 LEU   A N   
2567 C CA  . LEU   A 123 ? 0.1114 0.1156 0.0970 -0.0153 0.0152  0.0207  123 LEU   A CA  
2568 C C   . LEU   A 123 ? 0.1040 0.1115 0.0874 -0.0084 0.0139  0.0200  123 LEU   A C   
2569 O O   . LEU   A 123 ? 0.1027 0.1296 0.1027 -0.0176 0.0072  0.0227  123 LEU   A O   
2570 C CB  . LEU   A 123 ? 0.1174 0.1277 0.0984 -0.0168 0.0182  0.0200  123 LEU   A CB  
2571 C CG  . LEU   A 123 ? 0.1215 0.1332 0.1121 -0.0120 0.0225  0.0096  123 LEU   A CG  
2572 C CD1 . LEU   A 123 ? 0.1258 0.1396 0.1318 0.0012  0.0204  0.0022  123 LEU   A CD1 
2573 C CD2 . LEU   A 123 ? 0.1362 0.1394 0.1254 -0.0040 0.0186  -0.0024 123 LEU   A CD2 
2585 N N   . ALA   A 124 ? 0.1063 0.1072 0.0854 -0.0116 0.0088  0.0174  124 ALA   A N   
2586 C CA  . ALA   A 124 ? 0.1050 0.1035 0.0945 -0.0078 0.0066  0.0183  124 ALA   A CA  
2587 C C   . ALA   A 124 ? 0.1012 0.1076 0.0945 -0.0084 0.0092  0.0195  124 ALA   A C   
2588 O O   . ALA   A 124 ? 0.0996 0.1150 0.1054 -0.0062 0.0123  0.0222  124 ALA   A O   
2589 C CB  . ALA   A 124 ? 0.1069 0.1055 0.1116 -0.0036 0.0081  0.0179  124 ALA   A CB  
2595 N N   A PRO   A 125 ? 0.0953 0.0987 0.0960 -0.0101 0.0043  0.0232  125 PRO   A N   
2596 N N   B PRO   A 125 ? 0.1110 0.1140 0.0877 -0.0056 0.0132  0.0214  125 PRO   A N   
2597 C CA  A PRO   A 125 ? 0.0995 0.1011 0.1012 -0.0025 0.0014  0.0182  125 PRO   A CA  
2598 C CA  B PRO   A 125 ? 0.1182 0.1169 0.0834 -0.0012 0.0056  0.0095  125 PRO   A CA  
2599 C C   A PRO   A 125 ? 0.0925 0.1001 0.1018 -0.0036 0.0056  0.0183  125 PRO   A C   
2600 C C   B PRO   A 125 ? 0.1120 0.1195 0.0753 -0.0023 0.0102  0.0126  125 PRO   A C   
2601 O O   A PRO   A 125 ? 0.0930 0.1004 0.1127 0.0019  0.0056  0.0126  125 PRO   A O   
2602 O O   B PRO   A 125 ? 0.1151 0.1236 0.0943 0.0001  0.0092  0.0086  125 PRO   A O   
2603 C CB  A PRO   A 125 ? 0.1155 0.0902 0.0881 -0.0082 0.0088  0.0168  125 PRO   A CB  
2604 C CB  B PRO   A 125 ? 0.1331 0.1120 0.0870 -0.0002 0.0158  0.0114  125 PRO   A CB  
2605 C CG  A PRO   A 125 ? 0.1105 0.0785 0.0861 -0.0090 0.0184  0.0105  125 PRO   A CG  
2606 C CG  B PRO   A 125 ? 0.1426 0.1172 0.1012 -0.0055 0.0131  0.0128  125 PRO   A CG  
2607 C CD  A PRO   A 125 ? 0.0942 0.0871 0.0878 -0.0113 0.0098  0.0078  125 PRO   A CD  
2608 C CD  B PRO   A 125 ? 0.1235 0.1198 0.0997 -0.0063 0.0164  0.0113  125 PRO   A CD  
2623 N N   A LEU   A 126 ? 0.0920 0.1057 0.0982 -0.0045 0.0083  0.0133  126 LEU   A N   
2624 N N   B LEU   A 126 ? 0.1132 0.1197 0.0932 -0.0013 0.0028  0.0122  126 LEU   A N   
2625 C CA  A LEU   A 126 ? 0.0975 0.1036 0.1023 -0.0037 0.0118  0.0124  126 LEU   A CA  
2626 C CA  B LEU   A 126 ? 0.1091 0.1121 0.0943 -0.0054 0.0106  0.0082  126 LEU   A CA  
2627 C C   A LEU   A 126 ? 0.1052 0.1059 0.1072 0.0031  -0.0060 0.0130  126 LEU   A C   
2628 C C   B LEU   A 126 ? 0.1094 0.1038 0.0948 0.0002  0.0062  0.0039  126 LEU   A C   
2629 O O   A LEU   A 126 ? 0.1101 0.1108 0.1224 0.0150  0.0076  0.0208  126 LEU   A O   
2630 O O   B LEU   A 126 ? 0.1177 0.1065 0.0996 -0.0016 0.0104  0.0112  126 LEU   A O   
2631 C CB  A LEU   A 126 ? 0.1012 0.1034 0.1025 -0.0029 0.0077  0.0060  126 LEU   A CB  
2632 C CB  B LEU   A 126 ? 0.1134 0.1255 0.1113 -0.0104 0.0099  0.0001  126 LEU   A CB  
2633 C CG  A LEU   A 126 ? 0.1053 0.1132 0.1231 0.0014  0.0162  0.0077  126 LEU   A CG  
2634 C CG  B LEU   A 126 ? 0.1180 0.1329 0.1352 -0.0087 0.0134  -0.0065 126 LEU   A CG  
2635 C CD1 A LEU   A 126 ? 0.1076 0.1203 0.1493 -0.0003 0.0116  0.0081  126 LEU   A CD1 
2636 C CD1 B LEU   A 126 ? 0.1188 0.1368 0.1606 -0.0095 0.0173  -0.0196 126 LEU   A CD1 
2637 C CD2 A LEU   A 126 ? 0.1093 0.1087 0.1144 -0.0113 0.0205  0.0129  126 LEU   A CD2 
2638 C CD2 B LEU   A 126 ? 0.1182 0.1402 0.1342 -0.0073 0.0038  -0.0028 126 LEU   A CD2 
2661 N N   A LEU   A 127 ? 0.1074 0.1073 0.1063 0.0006  -0.0097 -0.0010 127 LEU   A N   
2662 N N   B LEU   A 127 ? 0.1022 0.0952 0.1022 -0.0009 0.0172  -0.0025 127 LEU   A N   
2663 C CA  A LEU   A 127 ? 0.1041 0.1031 0.0964 -0.0027 -0.0093 0.0010  127 LEU   A CA  
2664 C CA  B LEU   A 127 ? 0.1000 0.1112 0.1048 0.0007  0.0134  0.0059  127 LEU   A CA  
2665 C C   A LEU   A 127 ? 0.0985 0.0989 0.0934 -0.0036 -0.0053 0.0046  127 LEU   A C   
2666 C C   B LEU   A 127 ? 0.1009 0.1064 0.1059 0.0014  0.0118  0.0007  127 LEU   A C   
2667 O O   A LEU   A 127 ? 0.1090 0.0977 0.0863 -0.0105 -0.0037 0.0035  127 LEU   A O   
2668 O O   B LEU   A 127 ? 0.1157 0.1089 0.1019 0.0019  0.0147  0.0013  127 LEU   A O   
2669 C CB  A LEU   A 127 ? 0.1070 0.1002 0.0911 0.0008  -0.0016 -0.0000 127 LEU   A CB  
2670 C CB  B LEU   A 127 ? 0.1039 0.1352 0.1176 0.0015  0.0083  0.0051  127 LEU   A CB  
2671 C CG  A LEU   A 127 ? 0.1081 0.0870 0.0989 0.0019  -0.0044 -0.0016 127 LEU   A CG  
2672 C CG  B LEU   A 127 ? 0.1188 0.1617 0.1390 0.0024  -0.0022 0.0097  127 LEU   A CG  
2673 C CD1 A LEU   A 127 ? 0.1108 0.0841 0.0995 0.0007  -0.0003 0.0007  127 LEU   A CD1 
2674 C CD1 B LEU   A 127 ? 0.1214 0.1703 0.1588 0.0107  0.0063  0.0158  127 LEU   A CD1 
2675 C CD2 A LEU   A 127 ? 0.1234 0.0764 0.0956 0.0062  -0.0165 0.0015  127 LEU   A CD2 
2676 C CD2 B LEU   A 127 ? 0.1333 0.1764 0.1369 -0.0045 -0.0110 -0.0073 127 LEU   A CD2 
2699 N N   A SER   A 128 ? 0.1063 0.1110 0.0919 -0.0018 -0.0025 0.0105  128 SER   A N   
2700 N N   B SER   A 128 ? 0.1062 0.1043 0.1147 -0.0059 0.0052  0.0028  128 SER   A N   
2701 C CA  A SER   A 128 ? 0.1154 0.1230 0.0911 0.0014  0.0015  0.0114  128 SER   A CA  
2702 C CA  B SER   A 128 ? 0.1045 0.1000 0.1084 -0.0062 -0.0065 -0.0006 128 SER   A CA  
2703 C C   A SER   A 128 ? 0.1205 0.1244 0.0955 0.0041  0.0010  0.0084  128 SER   A C   
2704 C C   B SER   A 128 ? 0.1090 0.0935 0.1026 0.0002  -0.0185 0.0126  128 SER   A C   
2705 O O   A SER   A 128 ? 0.1254 0.1440 0.1031 -0.0067 0.0174  0.0152  128 SER   A O   
2706 O O   B SER   A 128 ? 0.1094 0.1043 0.1190 -0.0070 -0.0229 0.0120  128 SER   A O   
2707 C CB  A SER   A 128 ? 0.1186 0.1273 0.0849 0.0065  0.0042  0.0238  128 SER   A CB  
2708 C CB  B SER   A 128 ? 0.1033 0.1102 0.0990 -0.0132 -0.0097 0.0051  128 SER   A CB  
2709 O OG  A SER   A 128 ? 0.1299 0.1311 0.1019 0.0078  0.0036  0.0202  128 SER   A OG  
2710 O OG  B SER   A 128 ? 0.0981 0.1127 0.1047 -0.0150 -0.0054 0.0102  128 SER   A OG  
2721 N N   A ALA   A 129 ? 0.1185 0.1264 0.0973 0.0059  0.0012  0.0039  129 ALA   A N   
2722 N N   B ALA   A 129 ? 0.1099 0.1032 0.1222 0.0030  -0.0172 0.0136  129 ALA   A N   
2723 C CA  A ALA   A 129 ? 0.1129 0.1232 0.0834 -0.0005 -0.0016 0.0029  129 ALA   A CA  
2724 C CA  B ALA   A 129 ? 0.1124 0.1075 0.1243 0.0058  -0.0145 0.0085  129 ALA   A CA  
2725 C C   A ALA   A 129 ? 0.1136 0.1180 0.0691 -0.0048 -0.0017 0.0064  129 ALA   A C   
2726 C C   B ALA   A 129 ? 0.1206 0.1083 0.1083 0.0089  -0.0114 0.0045  129 ALA   A C   
2727 O O   A ALA   A 129 ? 0.1180 0.1228 0.0746 -0.0096 0.0051  0.0039  129 ALA   A O   
2728 O O   B ALA   A 129 ? 0.1203 0.1169 0.1003 0.0039  -0.0049 0.0202  129 ALA   A O   
2729 C CB  A ALA   A 129 ? 0.1153 0.1282 0.0955 0.0102  0.0014  0.0109  129 ALA   A CB  
2730 C CB  B ALA   A 129 ? 0.1152 0.1147 0.1464 0.0025  -0.0105 0.0044  129 ALA   A CB  
2741 N N   A GLY   A 130 ? 0.1125 0.1180 0.1085 -0.0081 0.0137  -0.0004 130 GLY   A N   
2742 N N   B GLY   A 130 ? 0.1259 0.1106 0.1199 0.0162  -0.0086 0.0088  130 GLY   A N   
2743 C CA  A GLY   A 130 ? 0.1207 0.1208 0.1140 -0.0060 0.0182  -0.0061 130 GLY   A CA  
2744 C CA  B GLY   A 130 ? 0.1333 0.1079 0.1141 0.0129  -0.0032 0.0078  130 GLY   A CA  
2745 C C   A GLY   A 130 ? 0.1215 0.1228 0.1046 -0.0017 0.0174  -0.0051 130 GLY   A C   
2746 C C   B GLY   A 130 ? 0.1351 0.1062 0.1087 0.0145  -0.0147 0.0129  130 GLY   A C   
2747 O O   A GLY   A 130 ? 0.1281 0.1214 0.1088 -0.0093 0.0232  -0.0040 130 GLY   A O   
2748 O O   B GLY   A 130 ? 0.1378 0.1050 0.1179 0.0142  -0.0243 0.0125  130 GLY   A O   
2755 N N   A ILE   A 131 ? 0.1241 0.1266 0.0996 -0.0026 0.0051  0.0010  131 ILE   A N   
2756 N N   B ILE   A 131 ? 0.1392 0.1057 0.1123 0.0044  -0.0108 0.0239  131 ILE   A N   
2757 C CA  A ILE   A 131 ? 0.1276 0.1298 0.0796 -0.0019 -0.0084 -0.0097 131 ILE   A CA  
2758 C CA  B ILE   A 131 ? 0.1363 0.1027 0.1072 -0.0038 -0.0174 0.0224  131 ILE   A CA  
2759 C C   A ILE   A 131 ? 0.1240 0.1318 0.0795 0.0005  -0.0117 -0.0005 131 ILE   A C   
2760 C C   B ILE   A 131 ? 0.1366 0.1050 0.1169 -0.0064 -0.0046 0.0219  131 ILE   A C   
2761 O O   A ILE   A 131 ? 0.1273 0.1354 0.0933 0.0094  -0.0051 0.0068  131 ILE   A O   
2762 O O   B ILE   A 131 ? 0.1480 0.1099 0.1382 -0.0032 0.0077  0.0259  131 ILE   A O   
2763 C CB  A ILE   A 131 ? 0.1259 0.1372 0.0922 0.0009  -0.0087 -0.0149 131 ILE   A CB  
2764 C CB  B ILE   A 131 ? 0.1400 0.1122 0.1175 -0.0005 -0.0228 0.0087  131 ILE   A CB  
2765 C CG1 A ILE   A 131 ? 0.1328 0.1550 0.0921 0.0017  -0.0079 -0.0123 131 ILE   A CG1 
2766 C CG1 B ILE   A 131 ? 0.1420 0.1386 0.1136 -0.0027 -0.0271 0.0049  131 ILE   A CG1 
2767 C CG2 A ILE   A 131 ? 0.1296 0.1305 0.1149 0.0077  -0.0156 -0.0159 131 ILE   A CG2 
2768 C CG2 B ILE   A 131 ? 0.1376 0.1028 0.1330 -0.0040 -0.0156 -0.0073 131 ILE   A CG2 
2769 C CD1 A ILE   A 131 ? 0.1368 0.1612 0.1261 0.0008  -0.0176 -0.0082 131 ILE   A CD1 
2770 C CD1 B ILE   A 131 ? 0.1482 0.1492 0.1440 -0.0014 -0.0332 -0.0095 131 ILE   A CD1 
2793 N N   A PHE   A 132 ? 0.1249 0.1317 0.0783 0.0056  -0.0040 0.0059  132 PHE   A N   
2794 N N   B PHE   A 132 ? 0.1267 0.1031 0.1048 0.0047  -0.0036 0.0107  132 PHE   A N   
2795 C CA  A PHE   A 132 ? 0.1244 0.1405 0.0794 0.0079  0.0037  0.0043  132 PHE   A CA  
2796 C CA  B PHE   A 132 ? 0.1280 0.1057 0.1090 0.0050  -0.0008 0.0079  132 PHE   A CA  
2797 C C   A PHE   A 132 ? 0.1227 0.1571 0.0674 0.0102  0.0078  0.0043  132 PHE   A C   
2798 C C   B PHE   A 132 ? 0.1421 0.1143 0.1193 0.0080  -0.0076 0.0041  132 PHE   A C   
2799 O O   A PHE   A 132 ? 0.1239 0.1691 0.0649 0.0179  -0.0045 0.0018  132 PHE   A O   
2800 O O   B PHE   A 132 ? 0.1556 0.1183 0.1499 0.0122  -0.0125 -0.0022 132 PHE   A O   
2801 C CB  A PHE   A 132 ? 0.1297 0.1385 0.0967 0.0088  -0.0033 0.0027  132 PHE   A CB  
2802 C CB  B PHE   A 132 ? 0.1151 0.1057 0.1019 0.0018  -0.0048 0.0189  132 PHE   A CB  
2803 C CG  A PHE   A 132 ? 0.1310 0.1371 0.0903 0.0091  0.0052  0.0069  132 PHE   A CG  
2804 C CG  B PHE   A 132 ? 0.1138 0.1097 0.0960 0.0002  -0.0167 0.0107  132 PHE   A CG  
2805 C CD1 A PHE   A 132 ? 0.1393 0.1420 0.1105 0.0087  0.0067  0.0014  132 PHE   A CD1 
2806 C CD1 B PHE   A 132 ? 0.1183 0.1183 0.1072 0.0039  -0.0099 -0.0005 132 PHE   A CD1 
2807 C CD2 A PHE   A 132 ? 0.1314 0.1431 0.1002 0.0034  0.0138  0.0041  132 PHE   A CD2 
2808 C CD2 B PHE   A 132 ? 0.1145 0.1299 0.1358 0.0028  -0.0202 -0.0040 132 PHE   A CD2 
2809 C CE1 A PHE   A 132 ? 0.1442 0.1449 0.1119 0.0080  0.0136  -0.0007 132 PHE   A CE1 
2810 C CE1 B PHE   A 132 ? 0.1219 0.1241 0.1185 0.0049  -0.0163 -0.0132 132 PHE   A CE1 
2811 C CE2 A PHE   A 132 ? 0.1340 0.1448 0.0993 0.0019  0.0183  0.0090  132 PHE   A CE2 
2812 C CE2 B PHE   A 132 ? 0.1146 0.1391 0.1498 0.0069  -0.0158 -0.0070 132 PHE   A CE2 
2813 C CZ  A PHE   A 132 ? 0.1404 0.1460 0.1072 0.0027  0.0097  0.0060  132 PHE   A CZ  
2814 C CZ  B PHE   A 132 ? 0.1168 0.1325 0.1348 -0.0027 -0.0250 -0.0110 132 PHE   A CZ  
2833 N N   A GLY   A 133 ? 0.1227 0.1628 0.0660 0.0086  0.0003  0.0030  133 GLY   A N   
2834 N N   B GLY   A 133 ? 0.1474 0.1188 0.1126 0.0066  -0.0182 0.0092  133 GLY   A N   
2835 C CA  A GLY   A 133 ? 0.1371 0.1687 0.0793 0.0041  -0.0100 -0.0022 133 GLY   A CA  
2836 C CA  B GLY   A 133 ? 0.1523 0.1268 0.1200 0.0063  -0.0161 0.0020  133 GLY   A CA  
2837 C C   A GLY   A 133 ? 0.1464 0.1776 0.0788 -0.0047 -0.0255 -0.0062 133 GLY   A C   
2838 C C   B GLY   A 133 ? 0.1571 0.1387 0.1278 0.0025  -0.0269 -0.0030 133 GLY   A C   
2839 O O   A GLY   A 133 ? 0.1700 0.1947 0.0957 -0.0063 -0.0435 -0.0164 133 GLY   A O   
2840 O O   B GLY   A 133 ? 0.1836 0.1634 0.1567 -0.0010 -0.0342 -0.0149 133 GLY   A O   
2847 N N   A ALA   A 134 ? 0.1386 0.1694 0.0835 -0.0156 -0.0142 -0.0086 134 ALA   A N   
2848 N N   B ALA   A 134 ? 0.1449 0.1273 0.1235 -0.0081 -0.0234 -0.0047 134 ALA   A N   
2849 C CA  A ALA   A 134 ? 0.1411 0.1689 0.1167 -0.0093 -0.0144 -0.0099 134 ALA   A CA  
2850 C CA  B ALA   A 134 ? 0.1410 0.1271 0.1363 -0.0131 -0.0129 -0.0097 134 ALA   A CA  
2851 C C   A ALA   A 134 ? 0.1437 0.1656 0.1176 -0.0073 -0.0216 -0.0077 134 ALA   A C   
2852 C C   B ALA   A 134 ? 0.1404 0.1336 0.1142 -0.0092 -0.0071 -0.0076 134 ALA   A C   
2853 O O   A ALA   A 134 ? 0.1540 0.1687 0.1438 -0.0098 -0.0183 -0.0158 134 ALA   A O   
2854 O O   B ALA   A 134 ? 0.1488 0.1391 0.1276 -0.0111 0.0105  -0.0042 134 ALA   A O   
2855 C CB  A ALA   A 134 ? 0.1498 0.1736 0.1486 -0.0042 -0.0123 -0.0089 134 ALA   A CB  
2856 C CB  B ALA   A 134 ? 0.1476 0.1262 0.1672 -0.0155 -0.0123 -0.0121 134 ALA   A CB  
2867 N N   A ASP   A 135 ? 0.1448 0.1609 0.1312 -0.0077 -0.0207 0.0026  135 ASP   A N   
2868 N N   B ASP   A 135 ? 0.1432 0.1369 0.1133 -0.0118 -0.0124 0.0029  135 ASP   A N   
2869 C CA  A ASP   A 135 ? 0.1432 0.1591 0.1512 -0.0055 -0.0320 0.0098  135 ASP   A CA  
2870 C CA  B ASP   A 135 ? 0.1440 0.1404 0.1359 -0.0115 -0.0211 0.0113  135 ASP   A CA  
2871 C C   A ASP   A 135 ? 0.1342 0.1508 0.1417 -0.0049 -0.0156 0.0278  135 ASP   A C   
2872 C C   B ASP   A 135 ? 0.1290 0.1320 0.1393 -0.0079 -0.0069 0.0058  135 ASP   A C   
2873 O O   A ASP   A 135 ? 0.1304 0.1490 0.1448 0.0008  -0.0200 0.0289  135 ASP   A O   
2874 O O   B ASP   A 135 ? 0.1259 0.1326 0.1324 -0.0076 -0.0082 0.0057  135 ASP   A O   
2875 C CB  A ASP   A 135 ? 0.1585 0.1746 0.1795 -0.0165 -0.0471 -0.0068 135 ASP   A CB  
2876 C CB  B ASP   A 135 ? 0.1633 0.1614 0.1577 -0.0183 -0.0367 0.0063  135 ASP   A CB  
2877 C CG  A ASP   A 135 ? 0.1696 0.1884 0.2121 -0.0286 -0.0511 -0.0126 135 ASP   A CG  
2878 C CG  B ASP   A 135 ? 0.1794 0.1865 0.1937 -0.0215 -0.0469 0.0029  135 ASP   A CG  
2879 O OD1 A ASP   A 135 ? 0.1643 0.1922 0.2099 -0.0372 -0.0563 -0.0034 135 ASP   A OD1 
2880 O OD1 B ASP   A 135 ? 0.1799 0.1913 0.2185 -0.0146 -0.0442 0.0141  135 ASP   A OD1 
2881 O OD2 A ASP   A 135 ? 0.1889 0.1995 0.2526 -0.0294 -0.0316 -0.0129 135 ASP   A OD2 
2882 O OD2 B ASP   A 135 ? 0.1980 0.2058 0.2349 -0.0277 -0.0497 -0.0059 135 ASP   A OD2 
2891 N N   A PRO   A 136 ? 0.1303 0.1497 0.1361 -0.0017 -0.0082 0.0389  136 PRO   A N   
2892 N N   B PRO   A 136 ? 0.1220 0.1251 0.1499 0.0007  -0.0033 0.0024  136 PRO   A N   
2893 C CA  A PRO   A 136 ? 0.1263 0.1504 0.1425 -0.0045 -0.0038 0.0331  136 PRO   A CA  
2894 C CA  B PRO   A 136 ? 0.1212 0.1342 0.1598 -0.0008 0.0005  -0.0031 136 PRO   A CA  
2895 C C   A PRO   A 136 ? 0.1111 0.1445 0.1469 -0.0038 -0.0051 0.0311  136 PRO   A C   
2896 C C   B PRO   A 136 ? 0.1045 0.1353 0.1496 0.0011  0.0006  -0.0013 136 PRO   A C   
2897 O O   A PRO   A 136 ? 0.1096 0.1438 0.1568 -0.0079 -0.0074 0.0272  136 PRO   A O   
2898 O O   B PRO   A 136 ? 0.1006 0.1247 0.1376 0.0026  0.0130  0.0039  136 PRO   A O   
2899 C CB  A PRO   A 136 ? 0.1398 0.1503 0.1540 -0.0020 0.0064  0.0307  136 PRO   A CB  
2900 C CB  B PRO   A 136 ? 0.1365 0.1342 0.1776 0.0013  -0.0013 -0.0097 136 PRO   A CB  
2901 C CG  A PRO   A 136 ? 0.1477 0.1554 0.1670 0.0030  0.0032  0.0265  136 PRO   A CG  
2902 C CG  B PRO   A 136 ? 0.1451 0.1348 0.1956 0.0109  0.0040  -0.0070 136 PRO   A CG  
2903 C CD  A PRO   A 136 ? 0.1408 0.1515 0.1493 0.0050  -0.0029 0.0446  136 PRO   A CD  
2904 C CD  B PRO   A 136 ? 0.1319 0.1223 0.1751 0.0100  0.0062  0.0075  136 PRO   A CD  
2919 N N   A ILE   A 137 ? 0.1082 0.1449 0.1489 -0.0022 -0.0146 0.0333  137 ILE   A N   
2920 N N   B ILE   A 137 ? 0.1030 0.1389 0.1680 -0.0026 -0.0059 -0.0013 137 ILE   A N   
2921 C CA  A ILE   A 137 ? 0.1093 0.1533 0.1583 -0.0133 -0.0210 0.0298  137 ILE   A CA  
2922 C CA  B ILE   A 137 ? 0.1070 0.1482 0.1687 -0.0048 -0.0056 -0.0072 137 ILE   A CA  
2923 C C   A ILE   A 137 ? 0.1073 0.1501 0.1517 -0.0180 -0.0302 0.0272  137 ILE   A C   
2924 C C   B ILE   A 137 ? 0.1081 0.1439 0.1571 -0.0099 0.0027  -0.0013 137 ILE   A C   
2925 O O   A ILE   A 137 ? 0.1179 0.1479 0.1575 -0.0163 -0.0241 0.0272  137 ILE   A O   
2926 O O   B ILE   A 137 ? 0.1095 0.1376 0.1592 -0.0107 0.0136  0.0023  137 ILE   A O   
2927 C CB  A ILE   A 137 ? 0.1174 0.1703 0.1820 -0.0153 -0.0332 0.0218  137 ILE   A CB  
2928 C CB  B ILE   A 137 ? 0.1175 0.1619 0.1894 -0.0013 -0.0172 -0.0159 137 ILE   A CB  
2929 C CG1 A ILE   A 137 ? 0.1249 0.1960 0.2254 -0.0123 -0.0387 0.0203  137 ILE   A CG1 
2930 C CG1 B ILE   A 137 ? 0.1322 0.1856 0.2305 0.0041  -0.0306 -0.0135 137 ILE   A CG1 
2931 C CG2 A ILE   A 137 ? 0.1242 0.1696 0.1822 -0.0228 -0.0363 0.0079  137 ILE   A CG2 
2932 C CG2 B ILE   A 137 ? 0.1232 0.1596 0.1993 -0.0030 -0.0259 -0.0219 137 ILE   A CG2 
2933 C CD1 A ILE   A 137 ? 0.1415 0.2169 0.2550 -0.0024 -0.0327 0.0234  137 ILE   A CD1 
2934 C CD1 B ILE   A 137 ? 0.1478 0.2033 0.2520 0.0078  -0.0321 -0.0082 137 ILE   A CD1 
2957 N N   A HIS   A 138 ? 0.1070 0.1585 0.1440 -0.0109 -0.0241 0.0262  138 HIS   A N   
2958 N N   B HIS   A 138 ? 0.1166 0.1576 0.1566 -0.0088 0.0171  0.0007  138 HIS   A N   
2959 C CA  A HIS   A 138 ? 0.1081 0.1642 0.1350 -0.0103 -0.0183 0.0246  138 HIS   A CA  
2960 C CA  B HIS   A 138 ? 0.1225 0.1580 0.1447 -0.0080 0.0180  0.0064  138 HIS   A CA  
2961 C C   A HIS   A 138 ? 0.1036 0.1603 0.1338 -0.0051 -0.0075 0.0262  138 HIS   A C   
2962 C C   B HIS   A 138 ? 0.1138 0.1553 0.1401 -0.0038 0.0173  0.0179  138 HIS   A C   
2963 O O   A HIS   A 138 ? 0.1092 0.1632 0.1315 -0.0069 -0.0140 0.0216  138 HIS   A O   
2964 O O   B HIS   A 138 ? 0.1222 0.1566 0.1492 -0.0044 0.0167  0.0122  138 HIS   A O   
2965 C CB  A HIS   A 138 ? 0.1232 0.1794 0.1361 -0.0104 -0.0247 0.0169  138 HIS   A CB  
2966 C CB  B HIS   A 138 ? 0.1328 0.1670 0.1344 0.0007  0.0159  -0.0097 138 HIS   A CB  
2967 C CG  A HIS   A 138 ? 0.1416 0.1900 0.1417 -0.0116 -0.0213 0.0093  138 HIS   A CG  
2968 C CG  B HIS   A 138 ? 0.1486 0.1726 0.1387 -0.0005 0.0088  -0.0217 138 HIS   A CG  
2969 N ND1 A HIS   A 138 ? 0.1549 0.2031 0.1718 -0.0139 -0.0202 -0.0023 138 HIS   A ND1 
2970 N ND1 B HIS   A 138 ? 0.1603 0.1826 0.1686 -0.0006 0.0018  -0.0314 138 HIS   A ND1 
2971 C CD2 A HIS   A 138 ? 0.1450 0.1914 0.1443 -0.0023 -0.0126 0.0094  138 HIS   A CD2 
2972 C CD2 B HIS   A 138 ? 0.1526 0.1736 0.1405 0.0049  0.0150  -0.0177 138 HIS   A CD2 
2973 C CE1 A HIS   A 138 ? 0.1595 0.2073 0.1670 -0.0042 -0.0153 -0.0055 138 HIS   A CE1 
2974 C CE1 B HIS   A 138 ? 0.1630 0.1855 0.1588 0.0084  0.0030  -0.0323 138 HIS   A CE1 
2975 N NE2 A HIS   A 138 ? 0.1529 0.2027 0.1493 0.0031  -0.0065 0.0022  138 HIS   A NE2 
2976 N NE2 B HIS   A 138 ? 0.1598 0.1827 0.1448 0.0112  0.0118  -0.0215 138 HIS   A NE2 
2991 N N   . SER   A 139 ? 0.1035 0.1490 0.1373 -0.0037 -0.0002 0.0306  139 SER   A N   
2992 C CA  . SER   A 139 ? 0.1009 0.1462 0.1313 -0.0062 0.0011  0.0310  139 SER   A CA  
2993 C C   . SER   A 139 ? 0.0963 0.1370 0.1371 -0.0064 0.0061  0.0229  139 SER   A C   
2994 O O   . SER   A 139 ? 0.0926 0.1300 0.1475 -0.0083 0.0037  0.0252  139 SER   A O   
2995 C CB  . SER   A 139 ? 0.1039 0.1488 0.1413 -0.0110 -0.0067 0.0364  139 SER   A CB  
2996 O OG  . SER   A 139 ? 0.1117 0.1407 0.1480 -0.0159 -0.0101 0.0410  139 SER   A OG  
3003 N N   . LEU   A 140 ? 0.0947 0.1405 0.1359 -0.0066 0.0013  0.0338  140 LEU   A N   
3004 C CA  . LEU   A 140 ? 0.0940 0.1376 0.1331 -0.0068 0.0018  0.0355  140 LEU   A CA  
3005 C C   . LEU   A 140 ? 0.0890 0.1443 0.1355 -0.0055 0.0030  0.0333  140 LEU   A C   
3006 O O   . LEU   A 140 ? 0.0995 0.1424 0.1480 -0.0029 -0.0024 0.0306  140 LEU   A O   
3007 C CB  . LEU   A 140 ? 0.0999 0.1438 0.1306 -0.0069 0.0045  0.0290  140 LEU   A CB  
3008 C CG  . LEU   A 140 ? 0.0996 0.1563 0.1368 -0.0148 0.0021  0.0354  140 LEU   A CG  
3009 C CD1 . LEU   A 140 ? 0.1073 0.1565 0.1417 -0.0107 0.0005  0.0357  140 LEU   A CD1 
3010 C CD2 . LEU   A 140 ? 0.1037 0.1718 0.1589 -0.0070 0.0072  0.0451  140 LEU   A CD2 
3022 N N   . ARG   A 141 ? 0.0953 0.1437 0.1458 -0.0099 -0.0006 0.0340  141 ARG   A N   
3023 C CA  . ARG   A 141 ? 0.1075 0.1508 0.1591 -0.0184 -0.0048 0.0125  141 ARG   A CA  
3024 C C   . ARG   A 141 ? 0.1121 0.1344 0.1505 -0.0132 -0.0100 0.0146  141 ARG   A C   
3025 O O   . ARG   A 141 ? 0.1075 0.1350 0.1713 -0.0122 0.0006  0.0068  141 ARG   A O   
3026 C CB  . ARG   A 141 ? 0.1209 0.1697 0.1871 -0.0219 -0.0119 0.0028  141 ARG   A CB  
3027 C CG  . ARG   A 141 ? 0.1605 0.2027 0.2351 -0.0207 -0.0121 -0.0118 141 ARG   A CG  
3028 C CD  . ARG   A 141 ? 0.1832 0.2168 0.2617 -0.0283 -0.0130 -0.0225 141 ARG   A CD  
3029 N NE  . ARG   A 141 ? 0.1719 0.2266 0.2781 -0.0254 -0.0187 -0.0194 141 ARG   A NE  
3030 C CZ  . ARG   A 141 ? 0.1683 0.2463 0.2921 -0.0326 -0.0073 -0.0068 141 ARG   A CZ  
3031 N NH1 . ARG   A 141 ? 0.1665 0.2577 0.2869 -0.0383 0.0056  -0.0219 141 ARG   A NH1 
3032 N NH2 . ARG   A 141 ? 0.1640 0.2543 0.3102 -0.0263 -0.0147 0.0143  141 ARG   A NH2 
3046 N N   . VAL   A 142 ? 0.1068 0.1304 0.1466 -0.0109 -0.0033 0.0127  142 VAL   A N   
3047 C CA  . VAL   A 142 ? 0.1086 0.1305 0.1437 -0.0061 0.0103  0.0134  142 VAL   A CA  
3048 C C   . VAL   A 142 ? 0.0935 0.1260 0.1440 -0.0096 0.0096  0.0128  142 VAL   A C   
3049 O O   . VAL   A 142 ? 0.0994 0.1231 0.1460 0.0027  0.0107  0.0124  142 VAL   A O   
3050 C CB  . VAL   A 142 ? 0.1149 0.1352 0.1464 -0.0058 0.0145  0.0136  142 VAL   A CB  
3051 C CG1 . VAL   A 142 ? 0.1191 0.1317 0.1451 -0.0091 0.0143  0.0117  142 VAL   A CG1 
3052 C CG2 . VAL   A 142 ? 0.1265 0.1536 0.1569 0.0014  0.0077  0.0169  142 VAL   A CG2 
3062 N N   . CYS   A 143 ? 0.0975 0.1221 0.1389 -0.0090 0.0065  0.0180  143 CYS   A N   
3063 C CA  . CYS   A 143 ? 0.0956 0.1210 0.1481 -0.0073 0.0068  0.0145  143 CYS   A CA  
3064 C C   . CYS   A 143 ? 0.0965 0.1169 0.1421 -0.0048 0.0072  0.0198  143 CYS   A C   
3065 O O   . CYS   A 143 ? 0.0949 0.1155 0.1459 -0.0024 0.0047  0.0209  143 CYS   A O   
3066 C CB  . CYS   A 143 ? 0.1090 0.1225 0.1440 -0.0035 0.0103  0.0224  143 CYS   A CB  
3067 S SG  . CYS   A 143 ? 0.1268 0.1328 0.1298 0.0084  0.0142  0.0122  143 CYS   A SG  
3073 N N   . VAL   A 144 ? 0.0945 0.1254 0.1529 -0.0095 0.0090  0.0322  144 VAL   A N   
3074 C CA  . VAL   A 144 ? 0.1029 0.1304 0.1779 -0.0145 0.0148  0.0274  144 VAL   A CA  
3075 C C   . VAL   A 144 ? 0.1071 0.1238 0.1750 -0.0183 -0.0056 0.0230  144 VAL   A C   
3076 O O   . VAL   A 144 ? 0.1213 0.1304 0.1846 -0.0033 -0.0056 0.0268  144 VAL   A O   
3077 C CB  . VAL   A 144 ? 0.1224 0.1551 0.2339 -0.0081 0.0274  0.0319  144 VAL   A CB  
3078 C CG1 . VAL   A 144 ? 0.1264 0.1755 0.2726 -0.0152 0.0136  0.0329  144 VAL   A CG1 
3079 C CG2 . VAL   A 144 ? 0.1136 0.1596 0.2391 -0.0018 0.0340  0.0430  144 VAL   A CG2 
3089 N N   . ASP   A 145 ? 0.1058 0.1226 0.1877 -0.0145 -0.0014 0.0133  145 ASP   A N   
3090 C CA  . ASP   A 145 ? 0.1170 0.1254 0.1948 -0.0221 -0.0038 0.0065  145 ASP   A CA  
3091 C C   . ASP   A 145 ? 0.1203 0.1164 0.1833 -0.0123 0.0025  -0.0045 145 ASP   A C   
3092 O O   . ASP   A 145 ? 0.1360 0.1317 0.2350 -0.0126 0.0011  -0.0377 145 ASP   A O   
3093 C CB  . ASP   A 145 ? 0.1318 0.1498 0.2110 -0.0260 -0.0158 -0.0006 145 ASP   A CB  
3094 C CG  . ASP   A 145 ? 0.1529 0.1865 0.2426 -0.0437 -0.0312 0.0175  145 ASP   A CG  
3095 O OD1 . ASP   A 145 ? 0.1439 0.2020 0.2512 -0.0517 -0.0279 0.0248  145 ASP   A OD1 
3096 O OD2 . ASP   A 145 ? 0.1719 0.2094 0.2555 -0.0516 -0.0487 0.0193  145 ASP   A OD2 
3101 N N   . THR   A 146 ? 0.1076 0.1102 0.1608 -0.0126 0.0044  0.0050  146 THR   A N   
3102 C CA  . THR   A 146 ? 0.0996 0.1125 0.1461 -0.0045 0.0053  0.0033  146 THR   A CA  
3103 C C   . THR   A 146 ? 0.0958 0.1089 0.1496 -0.0019 0.0078  0.0135  146 THR   A C   
3104 O O   . THR   A 146 ? 0.1143 0.1207 0.1516 0.0057  -0.0009 0.0104  146 THR   A O   
3105 C CB  . THR   A 146 ? 0.1026 0.1144 0.1416 -0.0027 0.0108  0.0060  146 THR   A CB  
3106 O OG1 . THR   A 146 ? 0.1009 0.1298 0.1472 -0.0015 -0.0010 0.0033  146 THR   A OG1 
3107 C CG2 . THR   A 146 ? 0.1067 0.1183 0.1657 -0.0081 0.0115  0.0071  146 THR   A CG2 
3115 N N   . VAL   A 147 ? 0.0954 0.1112 0.1481 -0.0022 0.0093  0.0160  147 VAL   A N   
3116 C CA  . VAL   A 147 ? 0.0990 0.1138 0.1454 -0.0064 0.0204  0.0182  147 VAL   A CA  
3117 C C   . VAL   A 147 ? 0.1026 0.1074 0.1518 -0.0086 0.0147  0.0214  147 VAL   A C   
3118 O O   . VAL   A 147 ? 0.1041 0.1137 0.1736 -0.0130 0.0112  0.0252  147 VAL   A O   
3119 C CB  . VAL   A 147 ? 0.1083 0.1117 0.1419 -0.0110 0.0172  0.0205  147 VAL   A CB  
3120 C CG1 . VAL   A 147 ? 0.1408 0.1150 0.1536 -0.0067 0.0187  0.0310  147 VAL   A CG1 
3121 C CG2 . VAL   A 147 ? 0.1115 0.1153 0.1321 -0.0097 0.0057  0.0191  147 VAL   A CG2 
3131 N N   . ARG   A 148 ? 0.0969 0.1062 0.1586 -0.0094 0.0121  0.0281  148 ARG   A N   
3132 C CA  . ARG   A 148 ? 0.1047 0.1110 0.1606 -0.0081 0.0044  0.0363  148 ARG   A CA  
3133 C C   . ARG   A 148 ? 0.1215 0.1140 0.1635 -0.0114 0.0081  0.0497  148 ARG   A C   
3134 O O   . ARG   A 148 ? 0.1514 0.1292 0.1703 -0.0172 0.0120  0.0429  148 ARG   A O   
3135 C CB  . ARG   A 148 ? 0.1102 0.1147 0.1708 -0.0052 0.0172  0.0315  148 ARG   A CB  
3136 C CG  . ARG   A 148 ? 0.1334 0.1119 0.1952 -0.0063 0.0249  0.0167  148 ARG   A CG  
3137 C CD  . ARG   A 148 ? 0.1529 0.1150 0.2092 -0.0006 0.0351  0.0328  148 ARG   A CD  
3138 N NE  . ARG   A 148 ? 0.1427 0.1228 0.2083 0.0077  0.0420  0.0393  148 ARG   A NE  
3139 C CZ  . ARG   A 148 ? 0.1397 0.1127 0.2025 0.0059  0.0473  0.0296  148 ARG   A CZ  
3140 N NH1 . ARG   A 148 ? 0.1512 0.1151 0.2221 -0.0054 0.0392  0.0105  148 ARG   A NH1 
3141 N NH2 . ARG   A 148 ? 0.1379 0.1337 0.2071 0.0148  0.0500  0.0422  148 ARG   A NH2 
3155 N N   . THR   A 149 ? 0.1204 0.1221 0.1416 -0.0159 0.0018  0.0365  149 THR   A N   
3156 C CA  . THR   A 149 ? 0.1220 0.1233 0.1439 -0.0116 0.0028  0.0387  149 THR   A CA  
3157 C C   . THR   A 149 ? 0.1188 0.1199 0.1304 -0.0142 0.0009  0.0407  149 THR   A C   
3158 O O   . THR   A 149 ? 0.1174 0.1272 0.1484 -0.0173 0.0043  0.0361  149 THR   A O   
3159 C CB  . THR   A 149 ? 0.1164 0.1393 0.1477 -0.0137 0.0073  0.0295  149 THR   A CB  
3160 O OG1 . THR   A 149 ? 0.1166 0.1300 0.1582 -0.0216 0.0046  0.0249  149 THR   A OG1 
3161 C CG2 . THR   A 149 ? 0.1172 0.1506 0.1598 -0.0071 -0.0007 0.0319  149 THR   A CG2 
3169 N N   . ASN   A 150 ? 0.1231 0.1216 0.1423 -0.0026 -0.0006 0.0367  150 ASN   A N   
3170 C CA  . ASN   A 150 ? 0.1293 0.1292 0.1419 -0.0049 0.0070  0.0363  150 ASN   A CA  
3171 C C   . ASN   A 150 ? 0.1104 0.1221 0.1469 -0.0112 0.0056  0.0373  150 ASN   A C   
3172 O O   . ASN   A 150 ? 0.1270 0.1340 0.1869 -0.0068 -0.0196 0.0315  150 ASN   A O   
3173 C CB  . ASN   A 150 ? 0.1758 0.1598 0.1629 -0.0074 0.0294  0.0576  150 ASN   A CB  
3174 C CG  . ASN   A 150 ? 0.2352 0.2002 0.2424 -0.0094 0.0114  0.0681  150 ASN   A CG  
3175 O OD1 . ASN   A 150 ? 0.2600 0.2086 0.2690 -0.0205 0.0145  0.0936  150 ASN   A OD1 
3176 N ND2 . ASN   A 150 ? 0.2606 0.2253 0.2767 0.0005  -0.0033 0.0689  150 ASN   A ND2 
3183 N N   . VAL   A 151 ? 0.1109 0.1162 0.1398 -0.0112 0.0028  0.0327  151 VAL   A N   
3184 C CA  . VAL   A 151 ? 0.1130 0.1142 0.1300 -0.0137 0.0062  0.0292  151 VAL   A CA  
3185 C C   . VAL   A 151 ? 0.1086 0.1087 0.1331 -0.0188 0.0089  0.0322  151 VAL   A C   
3186 O O   . VAL   A 151 ? 0.1188 0.1185 0.1638 -0.0174 0.0061  0.0284  151 VAL   A O   
3187 C CB  . VAL   A 151 ? 0.1438 0.1318 0.1280 -0.0013 0.0145  0.0251  151 VAL   A CB  
3188 C CG1 . VAL   A 151 ? 0.1363 0.1629 0.1597 -0.0053 0.0080  0.0316  151 VAL   A CG1 
3189 C CG2 . VAL   A 151 ? 0.1541 0.1380 0.1255 0.0057  0.0203  0.0247  151 VAL   A CG2 
3199 N N   . TYR   A 152 ? 0.1074 0.1124 0.1246 -0.0101 0.0120  0.0316  152 TYR   A N   
3200 C CA  . TYR   A 152 ? 0.1069 0.1170 0.1079 -0.0114 0.0100  0.0294  152 TYR   A CA  
3201 C C   . TYR   A 152 ? 0.0991 0.1140 0.1051 -0.0100 0.0157  0.0245  152 TYR   A C   
3202 O O   . TYR   A 152 ? 0.1143 0.1139 0.1176 -0.0209 0.0118  0.0226  152 TYR   A O   
3203 C CB  . TYR   A 152 ? 0.1127 0.1255 0.1125 -0.0081 0.0145  0.0259  152 TYR   A CB  
3204 C CG  . TYR   A 152 ? 0.1261 0.1462 0.1098 -0.0146 0.0188  0.0336  152 TYR   A CG  
3205 C CD1 . TYR   A 152 ? 0.1409 0.1665 0.1285 0.0015  0.0161  0.0409  152 TYR   A CD1 
3206 C CD2 . TYR   A 152 ? 0.1341 0.1576 0.0973 -0.0293 0.0131  0.0262  152 TYR   A CD2 
3207 C CE1 . TYR   A 152 ? 0.1711 0.1792 0.1392 0.0051  0.0012  0.0459  152 TYR   A CE1 
3208 C CE2 . TYR   A 152 ? 0.1596 0.1718 0.1148 -0.0299 0.0163  0.0343  152 TYR   A CE2 
3209 C CZ  . TYR   A 152 ? 0.1849 0.1752 0.1261 -0.0139 0.0018  0.0543  152 TYR   A CZ  
3210 O OH  . TYR   A 152 ? 0.2153 0.1960 0.1609 -0.0075 0.0125  0.0658  152 TYR   A OH  
3220 N N   A LEU   A 153 ? 0.0995 0.1136 0.1103 -0.0137 0.0102  0.0295  153 LEU   A N   
3221 N N   B LEU   A 153 ? 0.0977 0.1132 0.1112 -0.0093 0.0155  0.0267  153 LEU   A N   
3222 C CA  A LEU   A 153 ? 0.0970 0.1100 0.1154 -0.0073 0.0123  0.0237  153 LEU   A CA  
3223 C CA  B LEU   A 153 ? 0.1010 0.1119 0.1216 -0.0030 0.0082  0.0246  153 LEU   A CA  
3224 C C   A LEU   A 153 ? 0.0973 0.1148 0.1192 -0.0115 0.0243  0.0207  153 LEU   A C   
3225 C C   B LEU   A 153 ? 0.1049 0.1094 0.1155 -0.0019 0.0144  0.0229  153 LEU   A C   
3226 O O   A LEU   A 153 ? 0.0983 0.1263 0.1483 -0.0144 0.0308  0.0221  153 LEU   A O   
3227 O O   B LEU   A 153 ? 0.1101 0.1174 0.1299 0.0073  0.0167  0.0165  153 LEU   A O   
3228 C CB  A LEU   A 153 ? 0.0940 0.1067 0.1196 -0.0021 0.0112  0.0281  153 LEU   A CB  
3229 C CB  B LEU   A 153 ? 0.1016 0.1096 0.1331 -0.0066 0.0077  0.0242  153 LEU   A CB  
3230 C CG  A LEU   A 153 ? 0.0993 0.1095 0.1186 0.0033  0.0110  0.0296  153 LEU   A CG  
3231 C CG  B LEU   A 153 ? 0.1064 0.1151 0.1380 -0.0027 0.0147  0.0143  153 LEU   A CG  
3232 C CD1 A LEU   A 153 ? 0.1033 0.1211 0.1250 0.0015  0.0142  0.0186  153 LEU   A CD1 
3233 C CD1 B LEU   A 153 ? 0.1153 0.1201 0.1422 -0.0043 0.0127  0.0120  153 LEU   A CD1 
3234 C CD2 A LEU   A 153 ? 0.0978 0.1094 0.1123 0.0062  0.0132  0.0199  153 LEU   A CD2 
3235 C CD2 B LEU   A 153 ? 0.1091 0.1139 0.1295 0.0022  0.0127  0.0086  153 LEU   A CD2 
3258 N N   A ALA   A 154 ? 0.1005 0.1127 0.1004 -0.0050 0.0212  0.0192  154 ALA   A N   
3259 N N   B ALA   A 154 ? 0.1045 0.1035 0.0993 -0.0037 0.0131  0.0207  154 ALA   A N   
3260 C CA  A ALA   A 154 ? 0.1202 0.1177 0.1185 0.0034  0.0218  0.0190  154 ALA   A CA  
3261 C CA  B ALA   A 154 ? 0.1118 0.1082 0.1112 0.0001  0.0049  0.0085  154 ALA   A CA  
3262 C C   A ALA   A 154 ? 0.1188 0.1151 0.1232 0.0023  0.0172  0.0331  154 ALA   A C   
3263 C C   B ALA   A 154 ? 0.1086 0.0999 0.1124 -0.0013 0.0063  0.0118  154 ALA   A C   
3264 O O   A ALA   A 154 ? 0.1108 0.1177 0.1058 -0.0110 0.0119  0.0224  154 ALA   A O   
3265 O O   B ALA   A 154 ? 0.1112 0.1116 0.1297 0.0062  -0.0020 0.0029  154 ALA   A O   
3266 C CB  A ALA   A 154 ? 0.1371 0.1190 0.1303 0.0069  0.0137  0.0021  154 ALA   A CB  
3267 C CB  B ALA   A 154 ? 0.1191 0.1164 0.1294 0.0097  -0.0033 -0.0028 154 ALA   A CB  
3278 N N   A VAL   A 155 ? 0.1289 0.1249 0.1423 0.0124  0.0183  0.0452  155 VAL   A N   
3279 N N   B VAL   A 155 ? 0.1090 0.1143 0.1138 0.0012  0.0138  0.0201  155 VAL   A N   
3280 C CA  A VAL   A 155 ? 0.1338 0.1295 0.1648 0.0146  0.0218  0.0553  155 VAL   A CA  
3281 C CA  B VAL   A 155 ? 0.1052 0.1271 0.1314 -0.0032 0.0133  0.0251  155 VAL   A CA  
3282 C C   A VAL   A 155 ? 0.1464 0.1257 0.1912 0.0168  0.0215  0.0637  155 VAL   A C   
3283 C C   B VAL   A 155 ? 0.1130 0.1334 0.1478 0.0133  0.0064  0.0228  155 VAL   A C   
3284 O O   A VAL   A 155 ? 0.1447 0.1295 0.1927 0.0195  0.0280  0.0497  155 VAL   A O   
3285 O O   B VAL   A 155 ? 0.1106 0.1302 0.1667 0.0191  0.0162  0.0240  155 VAL   A O   
3286 C CB  A VAL   A 155 ? 0.1338 0.1486 0.1596 0.0150  0.0178  0.0462  155 VAL   A CB  
3287 C CB  B VAL   A 155 ? 0.1103 0.1424 0.1397 -0.0096 0.0054  0.0187  155 VAL   A CB  
3288 C CG1 A VAL   A 155 ? 0.1424 0.1624 0.1668 0.0140  0.0156  0.0495  155 VAL   A CG1 
3289 C CG1 B VAL   A 155 ? 0.1206 0.1607 0.1516 -0.0066 -0.0004 0.0293  155 VAL   A CG1 
3290 C CG2 A VAL   A 155 ? 0.1400 0.1562 0.1568 0.0166  0.0144  0.0444  155 VAL   A CG2 
3291 C CG2 B VAL   A 155 ? 0.1247 0.1467 0.1470 -0.0092 0.0057  0.0110  155 VAL   A CG2 
3310 N N   A PHE   A 156 ? 0.1654 0.1274 0.2197 0.0139  0.0181  0.0714  156 PHE   A N   
3311 N N   B PHE   A 156 ? 0.1173 0.1405 0.1599 0.0138  0.0086  0.0179  156 PHE   A N   
3312 C CA  A PHE   A 156 ? 0.1787 0.1302 0.2483 0.0163  0.0162  0.0729  156 PHE   A CA  
3313 C CA  B PHE   A 156 ? 0.1266 0.1468 0.1757 0.0106  0.0097  0.0243  156 PHE   A CA  
3314 C C   A PHE   A 156 ? 0.1818 0.1320 0.2511 0.0159  0.0271  0.0779  156 PHE   A C   
3315 C C   B PHE   A 156 ? 0.1297 0.1477 0.1803 0.0136  0.0146  0.0267  156 PHE   A C   
3316 O O   A PHE   A 156 ? 0.1911 0.1390 0.2614 0.0138  0.0244  0.0569  156 PHE   A O   
3317 O O   B PHE   A 156 ? 0.1323 0.1538 0.1838 0.0200  0.0126  0.0241  156 PHE   A O   
3318 C CB  A PHE   A 156 ? 0.1932 0.1398 0.2595 0.0142  0.0030  0.0753  156 PHE   A CB  
3319 C CB  B PHE   A 156 ? 0.1285 0.1495 0.1867 0.0145  0.0013  0.0268  156 PHE   A CB  
3320 C CG  A PHE   A 156 ? 0.2131 0.1496 0.2673 0.0230  -0.0111 0.0684  156 PHE   A CG  
3321 C CG  B PHE   A 156 ? 0.1400 0.1478 0.1977 0.0216  -0.0063 0.0159  156 PHE   A CG  
3322 C CD1 A PHE   A 156 ? 0.2262 0.1643 0.2849 0.0231  -0.0163 0.0571  156 PHE   A CD1 
3323 C CD1 B PHE   A 156 ? 0.1494 0.1492 0.2007 0.0283  -0.0103 0.0131  156 PHE   A CD1 
3324 C CD2 A PHE   A 156 ? 0.2254 0.1574 0.2742 0.0261  -0.0153 0.0725  156 PHE   A CD2 
3325 C CD2 B PHE   A 156 ? 0.1527 0.1523 0.2033 0.0228  0.0013  0.0149  156 PHE   A CD2 
3326 C CE1 A PHE   A 156 ? 0.2376 0.1696 0.2964 0.0240  -0.0156 0.0501  156 PHE   A CE1 
3327 C CE1 B PHE   A 156 ? 0.1603 0.1539 0.2114 0.0251  -0.0055 0.0120  156 PHE   A CE1 
3328 C CE2 A PHE   A 156 ? 0.2367 0.1659 0.2855 0.0313  -0.0187 0.0583  156 PHE   A CE2 
3329 C CE2 B PHE   A 156 ? 0.1631 0.1529 0.2160 0.0257  0.0043  0.0167  156 PHE   A CE2 
3330 C CZ  A PHE   A 156 ? 0.2405 0.1710 0.2936 0.0285  -0.0187 0.0444  156 PHE   A CZ  
3331 C CZ  B PHE   A 156 ? 0.1629 0.1577 0.2104 0.0261  0.0044  0.0122  156 PHE   A CZ  
3350 N N   A ASP   A 157 ? 0.1876 0.1388 0.2376 0.0171  0.0323  0.0881  157 ASP   A N   
3351 N N   B ASP   A 157 ? 0.1322 0.1514 0.1761 0.0044  0.0223  0.0401  157 ASP   A N   
3352 C CA  A ASP   A 157 ? 0.1919 0.1542 0.2298 0.0201  0.0243  0.0878  157 ASP   A CA  
3353 C CA  B ASP   A 157 ? 0.1393 0.1609 0.1873 -0.0051 0.0110  0.0500  157 ASP   A CA  
3354 C C   A ASP   A 157 ? 0.1787 0.1506 0.2197 0.0253  0.0404  0.0773  157 ASP   A C   
3355 C C   B ASP   A 157 ? 0.1334 0.1530 0.1962 -0.0075 0.0099  0.0468  157 ASP   A C   
3356 O O   A ASP   A 157 ? 0.1731 0.1409 0.2022 0.0295  0.0522  0.0795  157 ASP   A O   
3357 O O   B ASP   A 157 ? 0.1381 0.1486 0.1937 -0.0018 -0.0008 0.0456  157 ASP   A O   
3358 C CB  A ASP   A 157 ? 0.2039 0.1740 0.2389 0.0153  0.0034  0.0960  157 ASP   A CB  
3359 C CB  B ASP   A 157 ? 0.1601 0.1808 0.2074 -0.0139 0.0025  0.0569  157 ASP   A CB  
3360 C CG  A ASP   A 157 ? 0.2211 0.1829 0.2666 0.0113  -0.0172 0.1035  157 ASP   A CG  
3361 C CG  B ASP   A 157 ? 0.1880 0.1932 0.2327 -0.0144 -0.0061 0.0588  157 ASP   A CG  
3362 O OD1 A ASP   A 157 ? 0.2487 0.1963 0.3063 0.0050  -0.0417 0.0842  157 ASP   A OD1 
3363 O OD1 B ASP   A 157 ? 0.1890 0.1928 0.2493 -0.0143 -0.0082 0.0706  157 ASP   A OD1 
3364 O OD2 A ASP   A 157 ? 0.2057 0.1892 0.2905 0.0137  -0.0157 0.1017  157 ASP   A OD2 
3365 O OD2 B ASP   A 157 ? 0.2042 0.1994 0.2505 -0.0141 -0.0131 0.0505  157 ASP   A OD2 
3374 N N   A LYS   A 158 ? 0.1808 0.1568 0.2342 0.0239  0.0400  0.0642  158 LYS   A N   
3375 N N   B LYS   A 158 ? 0.1299 0.1576 0.2066 -0.0088 0.0206  0.0437  158 LYS   A N   
3376 C CA  A LYS   A 158 ? 0.1857 0.1658 0.2412 0.0237  0.0421  0.0618  158 LYS   A CA  
3377 C CA  B LYS   A 158 ? 0.1431 0.1669 0.2145 -0.0074 0.0332  0.0373  158 LYS   A CA  
3378 C C   A LYS   A 158 ? 0.1741 0.1619 0.2215 0.0333  0.0373  0.0635  158 LYS   A C   
3379 C C   B LYS   A 158 ? 0.1297 0.1530 0.1914 -0.0105 0.0122  0.0299  158 LYS   A C   
3380 O O   A LYS   A 158 ? 0.1772 0.1583 0.2087 0.0322  0.0484  0.0516  158 LYS   A O   
3381 O O   B LYS   A 158 ? 0.1356 0.1450 0.1934 -0.0145 0.0106  0.0350  158 LYS   A O   
3382 C CB  A LYS   A 158 ? 0.2018 0.1750 0.2616 0.0206  0.0513  0.0639  158 LYS   A CB  
3383 C CB  B LYS   A 158 ? 0.1713 0.1941 0.2536 -0.0021 0.0645  0.0333  158 LYS   A CB  
3384 C CG  A LYS   A 158 ? 0.2196 0.1878 0.2878 0.0169  0.0622  0.0589  158 LYS   A CG  
3385 C CG  B LYS   A 158 ? 0.1959 0.2159 0.2872 0.0023  0.0927  0.0437  158 LYS   A CG  
3386 C CD  A LYS   A 158 ? 0.2390 0.2063 0.3148 0.0170  0.0717  0.0557  158 LYS   A CD  
3387 C CD  B LYS   A 158 ? 0.2179 0.2309 0.3073 0.0018  0.1135  0.0573  158 LYS   A CD  
3388 C CE  A LYS   A 158 ? 0.2520 0.2202 0.3389 0.0148  0.0744  0.0557  158 LYS   A CE  
3389 C CE  B LYS   A 158 ? 0.2301 0.2415 0.3159 0.0062  0.1257  0.0657  158 LYS   A CE  
3390 N NZ  A LYS   A 158 ? 0.2571 0.2270 0.3426 0.0124  0.0730  0.0542  158 LYS   A NZ  
3391 N NZ  B LYS   A 158 ? 0.2385 0.2482 0.3237 0.0115  0.1341  0.0730  158 LYS   A NZ  
3418 N N   A ASN   A 159 ? 0.1641 0.1625 0.2075 0.0397  0.0159  0.0684  159 ASN   A N   
3419 N N   B ASN   A 159 ? 0.1236 0.1601 0.1841 -0.0052 -0.0046 0.0324  159 ASN   A N   
3420 C CA  A ASN   A 159 ? 0.1622 0.1727 0.2164 0.0326  0.0064  0.0680  159 ASN   A CA  
3421 C CA  B ASN   A 159 ? 0.1259 0.1763 0.1974 -0.0039 -0.0169 0.0406  159 ASN   A CA  
3422 C C   A ASN   A 159 ? 0.1523 0.1747 0.2036 0.0237  0.0154  0.0635  159 ASN   A C   
3423 C C   B ASN   A 159 ? 0.1197 0.1670 0.1784 -0.0102 -0.0203 0.0388  159 ASN   A C   
3424 O O   A ASN   A 159 ? 0.1420 0.1689 0.1878 0.0268  0.0124  0.0321  159 ASN   A O   
3425 O O   B ASN   A 159 ? 0.1179 0.1736 0.1778 -0.0122 -0.0160 0.0278  159 ASN   A O   
3426 C CB  A ASN   A 159 ? 0.1718 0.1866 0.2438 0.0285  -0.0003 0.0734  159 ASN   A CB  
3427 C CB  B ASN   A 159 ? 0.1448 0.2046 0.2297 0.0086  -0.0163 0.0456  159 ASN   A CB  
3428 C CG  A ASN   A 159 ? 0.1857 0.2042 0.2887 0.0261  0.0018  0.0735  159 ASN   A CG  
3429 C CG  B ASN   A 159 ? 0.1713 0.2377 0.2625 0.0121  -0.0172 0.0405  159 ASN   A CG  
3430 O OD1 A ASN   A 159 ? 0.1909 0.2142 0.3129 0.0301  0.0006  0.0790  159 ASN   A OD1 
3431 O OD1 B ASN   A 159 ? 0.1831 0.2552 0.2816 0.0075  -0.0306 0.0314  159 ASN   A OD1 
3432 N ND2 A ASN   A 159 ? 0.1934 0.2087 0.3036 0.0205  0.0035  0.0700  159 ASN   A ND2 
3433 N ND2 B ASN   A 159 ? 0.1827 0.2458 0.2757 0.0134  -0.0122 0.0442  159 ASN   A ND2 
3446 N N   A LEU   A 160 ? 0.1443 0.1772 0.1936 0.0214  0.0163  0.0817  160 LEU   A N   
3447 N N   B LEU   A 160 ? 0.1187 0.1610 0.1813 -0.0144 -0.0279 0.0525  160 LEU   A N   
3448 C CA  A LEU   A 160 ? 0.1452 0.1869 0.1918 0.0142  0.0267  0.0928  160 LEU   A CA  
3449 C CA  B LEU   A 160 ? 0.1223 0.1706 0.1867 -0.0084 -0.0090 0.0694  160 LEU   A CA  
3450 C C   A LEU   A 160 ? 0.1334 0.1880 0.1923 0.0166  0.0340  0.0978  160 LEU   A C   
3451 C C   B LEU   A 160 ? 0.1199 0.1751 0.1742 0.0033  0.0104  0.0740  160 LEU   A C   
3452 O O   A LEU   A 160 ? 0.1355 0.1903 0.1879 0.0198  0.0303  0.1111  160 LEU   A O   
3453 O O   B LEU   A 160 ? 0.1219 0.1773 0.1614 0.0028  -0.0013 0.0891  160 LEU   A O   
3454 C CB  A LEU   A 160 ? 0.1497 0.2010 0.1858 0.0062  0.0323  0.0883  160 LEU   A CB  
3455 C CB  B LEU   A 160 ? 0.1310 0.1863 0.1865 -0.0130 -0.0130 0.0724  160 LEU   A CB  
3456 C CG  A LEU   A 160 ? 0.1556 0.2126 0.1836 -0.0030 0.0390  0.0783  160 LEU   A CG  
3457 C CG  B LEU   A 160 ? 0.1359 0.2036 0.1941 -0.0200 -0.0004 0.0641  160 LEU   A CG  
3458 C CD1 A LEU   A 160 ? 0.1639 0.2208 0.1874 -0.0092 0.0474  0.0699  160 LEU   A CD1 
3459 C CD1 B LEU   A 160 ? 0.1457 0.2122 0.1958 -0.0199 0.0068  0.0592  160 LEU   A CD1 
3460 C CD2 A LEU   A 160 ? 0.1557 0.2202 0.1752 -0.0048 0.0412  0.0698  160 LEU   A CD2 
3461 C CD2 B LEU   A 160 ? 0.1388 0.2118 0.2039 -0.0209 0.0036  0.0532  160 LEU   A CD2 
3484 N N   A TYR   A 161 ? 0.1285 0.1832 0.1954 0.0147  0.0333  0.0878  161 TYR   A N   
3485 N N   B TYR   A 161 ? 0.1186 0.1713 0.1780 0.0176  0.0255  0.0648  161 TYR   A N   
3486 C CA  A TYR   A 161 ? 0.1257 0.1781 0.1911 0.0074  0.0252  0.0804  161 TYR   A CA  
3487 C CA  B TYR   A 161 ? 0.1241 0.1622 0.1702 0.0226  0.0384  0.0623  161 TYR   A CA  
3488 C C   A TYR   A 161 ? 0.1194 0.1927 0.1771 0.0023  0.0134  0.0849  161 TYR   A C   
3489 C C   B TYR   A 161 ? 0.1230 0.1796 0.1669 0.0354  0.0335  0.0662  161 TYR   A C   
3490 O O   A TYR   A 161 ? 0.1147 0.1967 0.1483 -0.0024 0.0080  0.0837  161 TYR   A O   
3491 O O   B TYR   A 161 ? 0.1202 0.1836 0.1404 0.0347  0.0351  0.0609  161 TYR   A O   
3492 C CB  A TYR   A 161 ? 0.1312 0.1617 0.2013 0.0083  0.0139  0.0689  161 TYR   A CB  
3493 C CB  B TYR   A 161 ? 0.1340 0.1411 0.1706 0.0122  0.0403  0.0534  161 TYR   A CB  
3494 C CG  A TYR   A 161 ? 0.1261 0.1483 0.1935 0.0047  0.0056  0.0475  161 TYR   A CG  
3495 C CG  B TYR   A 161 ? 0.1342 0.1234 0.1615 0.0012  0.0367  0.0305  161 TYR   A CG  
3496 C CD1 A TYR   A 161 ? 0.1235 0.1343 0.1885 0.0040  0.0062  0.0320  161 TYR   A CD1 
3497 C CD1 B TYR   A 161 ? 0.1324 0.1085 0.1454 -0.0068 0.0339  0.0121  161 TYR   A CD1 
3498 C CD2 A TYR   A 161 ? 0.1247 0.1494 0.1857 0.0104  0.0031  0.0312  161 TYR   A CD2 
3499 C CD2 B TYR   A 161 ? 0.1410 0.1305 0.1653 0.0030  0.0387  0.0238  161 TYR   A CD2 
3500 C CE1 A TYR   A 161 ? 0.1282 0.1157 0.1676 0.0062  0.0034  0.0223  161 TYR   A CE1 
3501 C CE1 B TYR   A 161 ? 0.1467 0.1155 0.1453 -0.0095 0.0269  0.0042  161 TYR   A CE1 
3502 C CE2 A TYR   A 161 ? 0.1284 0.1308 0.1678 0.0043  0.0053  0.0244  161 TYR   A CE2 
3503 C CE2 B TYR   A 161 ? 0.1516 0.1285 0.1625 -0.0087 0.0415  0.0218  161 TYR   A CE2 
3504 C CZ  A TYR   A 161 ? 0.1309 0.1083 0.1492 0.0035  0.0035  0.0228  161 TYR   A CZ  
3505 C CZ  B TYR   A 161 ? 0.1614 0.1254 0.1558 -0.0145 0.0340  0.0205  161 TYR   A CZ  
3506 O OH  A TYR   A 161 ? 0.1412 0.0990 0.1374 0.0017  -0.0026 0.0188  161 TYR   A OH  
3507 O OH  B TYR   A 161 ? 0.1837 0.1365 0.1767 -0.0171 0.0237  0.0197  161 TYR   A OH  
3526 N N   A ASP   A 162 ? 0.1182 0.2060 0.1898 -0.0008 0.0174  0.0902  162 ASP   A N   
3527 N N   B ASP   A 162 ? 0.1247 0.1970 0.1815 0.0382  0.0316  0.0714  162 ASP   A N   
3528 C CA  A ASP   A 162 ? 0.1118 0.2249 0.2062 -0.0103 0.0265  0.0914  162 ASP   A CA  
3529 C CA  B ASP   A 162 ? 0.1201 0.2219 0.1977 0.0295  0.0304  0.0821  162 ASP   A CA  
3530 C C   A ASP   A 162 ? 0.1064 0.2480 0.2015 -0.0154 0.0178  0.0951  162 ASP   A C   
3531 C C   B ASP   A 162 ? 0.1122 0.2475 0.1909 0.0202  0.0248  0.0834  162 ASP   A C   
3532 O O   A ASP   A 162 ? 0.1080 0.2476 0.2218 -0.0187 0.0144  0.0869  162 ASP   A O   
3533 O O   B ASP   A 162 ? 0.1123 0.2476 0.2067 0.0171  0.0181  0.0746  162 ASP   A O   
3534 C CB  A ASP   A 162 ? 0.1172 0.2264 0.2406 -0.0095 0.0458  0.0738  162 ASP   A CB  
3535 C CB  B ASP   A 162 ? 0.1275 0.2243 0.2145 0.0341  0.0351  0.0885  162 ASP   A CB  
3536 C CG  A ASP   A 162 ? 0.1256 0.2321 0.2721 -0.0061 0.0567  0.0491  162 ASP   A CG  
3537 C CG  B ASP   A 162 ? 0.1359 0.2325 0.2440 0.0355  0.0342  0.0890  162 ASP   A CG  
3538 O OD1 A ASP   A 162 ? 0.1424 0.2381 0.2844 -0.0121 0.0604  0.0506  162 ASP   A OD1 
3539 O OD1 B ASP   A 162 ? 0.1534 0.2412 0.2466 0.0270  0.0440  0.0885  162 ASP   A OD1 
3540 O OD2 A ASP   A 162 ? 0.1229 0.2335 0.2908 -0.0017 0.0633  0.0303  162 ASP   A OD2 
3541 O OD2 B ASP   A 162 ? 0.1379 0.2374 0.2792 0.0352  0.0265  0.0857  162 ASP   A OD2 
3550 N N   A LYS   A 163 ? 0.1171 0.2738 0.2128 -0.0144 0.0009  0.0890  163 LYS   A N   
3551 N N   B LYS   A 163 ? 0.1233 0.2740 0.2019 0.0135  0.0115  0.0796  163 LYS   A N   
3552 C CA  A LYS   A 163 ? 0.1314 0.2934 0.2019 -0.0193 -0.0069 0.0874  163 LYS   A CA  
3553 C CA  B LYS   A 163 ? 0.1399 0.2949 0.1987 0.0032  0.0027  0.0771  163 LYS   A CA  
3554 C C   A LYS   A 163 ? 0.1254 0.2816 0.1805 -0.0268 0.0045  0.0816  163 LYS   A C   
3555 C C   B LYS   A 163 ? 0.1300 0.2889 0.1740 -0.0047 0.0093  0.0643  163 LYS   A C   
3556 O O   A LYS   A 163 ? 0.1225 0.3004 0.1895 -0.0345 -0.0007 0.0656  163 LYS   A O   
3557 O O   B LYS   A 163 ? 0.1339 0.3073 0.1858 -0.0147 0.0151  0.0465  163 LYS   A O   
3558 C CB  A LYS   A 163 ? 0.1642 0.3191 0.2426 -0.0082 -0.0244 0.0828  163 LYS   A CB  
3559 C CB  B LYS   A 163 ? 0.1730 0.3154 0.2409 0.0071  -0.0046 0.0819  163 LYS   A CB  
3560 C CG  A LYS   A 163 ? 0.2010 0.3392 0.3075 -0.0076 -0.0176 0.0747  163 LYS   A CG  
3561 C CG  B LYS   A 163 ? 0.2052 0.3332 0.3036 0.0060  0.0032  0.0796  163 LYS   A CG  
3562 C CD  A LYS   A 163 ? 0.2286 0.3544 0.3686 -0.0088 -0.0187 0.0663  163 LYS   A CD  
3563 C CD  B LYS   A 163 ? 0.2320 0.3477 0.3626 0.0056  0.0079  0.0748  163 LYS   A CD  
3564 C CE  A LYS   A 163 ? 0.2579 0.3640 0.4124 -0.0103 -0.0188 0.0635  163 LYS   A CE  
3565 C CE  B LYS   A 163 ? 0.2537 0.3573 0.4089 0.0067  0.0117  0.0705  163 LYS   A CE  
3566 N NZ  A LYS   A 163 ? 0.2649 0.3685 0.4358 -0.0105 -0.0215 0.0650  163 LYS   A NZ  
3567 N NZ  B LYS   A 163 ? 0.2589 0.3617 0.4313 0.0080  0.0148  0.0731  163 LYS   A NZ  
3594 N N   A LEU   A 164 ? 0.1154 0.2471 0.1650 -0.0365 0.0005  0.0695  164 LEU   A N   
3595 N N   B LEU   A 164 ? 0.1121 0.2595 0.1447 -0.0082 0.0018  0.0529  164 LEU   A N   
3596 C CA  A LEU   A 164 ? 0.1169 0.2191 0.1637 -0.0415 0.0098  0.0553  164 LEU   A CA  
3597 C CA  B LEU   A 164 ? 0.1116 0.2325 0.1370 -0.0103 0.0148  0.0401  164 LEU   A CA  
3598 C C   A LEU   A 164 ? 0.1236 0.2153 0.1538 -0.0354 0.0090  0.0504  164 LEU   A C   
3599 C C   B LEU   A 164 ? 0.1154 0.2280 0.1334 -0.0166 0.0162  0.0442  164 LEU   A C   
3600 O O   A LEU   A 164 ? 0.1322 0.2215 0.1604 -0.0364 0.0187  0.0370  164 LEU   A O   
3601 O O   B LEU   A 164 ? 0.1205 0.2332 0.1370 -0.0287 0.0249  0.0379  164 LEU   A O   
3602 C CB  A LEU   A 164 ? 0.1132 0.2010 0.1640 -0.0421 0.0140  0.0535  164 LEU   A CB  
3603 C CB  B LEU   A 164 ? 0.1064 0.2128 0.1178 0.0018  0.0218  0.0230  164 LEU   A CB  
3604 C CG  A LEU   A 164 ? 0.1193 0.1936 0.1726 -0.0370 0.0024  0.0463  164 LEU   A CG  
3605 C CG  B LEU   A 164 ? 0.1179 0.2037 0.1320 0.0056  0.0136  0.0157  164 LEU   A CG  
3606 C CD1 A LEU   A 164 ? 0.1155 0.1877 0.1764 -0.0317 -0.0045 0.0452  164 LEU   A CD1 
3607 C CD1 B LEU   A 164 ? 0.1174 0.1977 0.1427 0.0153  0.0088  0.0143  164 LEU   A CD1 
3608 C CD2 A LEU   A 164 ? 0.1253 0.1967 0.1700 -0.0422 0.0127  0.0455  164 LEU   A CD2 
3609 C CD2 B LEU   A 164 ? 0.1242 0.2058 0.1352 -0.0087 0.0290  0.0138  164 LEU   A CD2 
3632 N N   A VAL   A 165 ? 0.1223 0.2076 0.1509 -0.0264 0.0105  0.0541  165 VAL   A N   
3633 N N   B VAL   A 165 ? 0.1144 0.2178 0.1364 -0.0119 0.0135  0.0496  165 VAL   A N   
3634 C CA  A VAL   A 165 ? 0.1221 0.2083 0.1526 -0.0249 0.0203  0.0576  165 VAL   A CA  
3635 C CA  B VAL   A 165 ? 0.1190 0.2151 0.1524 -0.0163 0.0182  0.0572  165 VAL   A CA  
3636 C C   A VAL   A 165 ? 0.1154 0.2198 0.1520 -0.0188 0.0239  0.0629  165 VAL   A C   
3637 C C   B VAL   A 165 ? 0.1142 0.2231 0.1559 -0.0125 0.0189  0.0598  165 VAL   A C   
3638 O O   A VAL   A 165 ? 0.1174 0.2208 0.1644 -0.0212 0.0192  0.0623  165 VAL   A O   
3639 O O   B VAL   A 165 ? 0.1154 0.2236 0.1651 -0.0112 0.0086  0.0547  165 VAL   A O   
3640 C CB  A VAL   A 165 ? 0.1346 0.2024 0.1524 -0.0214 0.0216  0.0450  165 VAL   A CB  
3641 C CB  B VAL   A 165 ? 0.1352 0.2089 0.1595 -0.0165 0.0149  0.0528  165 VAL   A CB  
3642 C CG1 A VAL   A 165 ? 0.1366 0.2030 0.1558 -0.0202 0.0258  0.0394  165 VAL   A CG1 
3643 C CG1 B VAL   A 165 ? 0.1390 0.2094 0.1672 -0.0187 0.0163  0.0503  165 VAL   A CG1 
3644 C CG2 A VAL   A 165 ? 0.1424 0.2002 0.1635 -0.0223 0.0227  0.0430  165 VAL   A CG2 
3645 C CG2 B VAL   A 165 ? 0.1425 0.2051 0.1654 -0.0160 0.0132  0.0554  165 VAL   A CG2 
3664 N N   . SER   A 166 ? 0.1082 0.2331 0.1724 -0.0126 0.0161  0.0554  166 SER   A N   
3665 C CA  . SER   A 166 ? 0.1103 0.2648 0.1763 -0.0122 0.0126  0.0447  166 SER   A CA  
3666 C C   . SER   A 166 ? 0.1105 0.2925 0.1872 -0.0183 -0.0035 0.0337  166 SER   A C   
3667 O O   . SER   A 166 ? 0.1327 0.3121 0.2396 -0.0370 0.0105  -0.0037 166 SER   A O   
3668 C CB  . SER   A 166 ? 0.1238 0.2751 0.2153 -0.0087 -0.0018 0.0321  166 SER   A CB  
3669 O OG  . SER   A 166 ? 0.1573 0.2843 0.2690 -0.0132 0.0054  0.0401  166 SER   A OG  
3676 N N   . SER   A 167 ? 0.1148 0.2980 0.1530 -0.0009 -0.0112 0.0472  167 SER   A N   
3677 C CA  . SER   A 167 ? 0.1397 0.3130 0.1623 0.0058  -0.0092 0.0410  167 SER   A CA  
3678 C C   . SER   A 167 ? 0.1454 0.3088 0.1555 0.0156  0.0069  0.0376  167 SER   A C   
3679 O O   . SER   A 167 ? 0.1667 0.3130 0.1719 0.0219  -0.0062 0.0284  167 SER   A O   
3680 C CB  . SER   A 167 ? 0.1576 0.3327 0.1670 0.0135  -0.0023 0.0541  167 SER   A CB  
3681 O OG  . SER   A 167 ? 0.1659 0.3438 0.1729 0.0122  0.0212  0.0754  167 SER   A OG  
3687 N N   A PHE   A 168 ? 0.1357 0.3055 0.1538 0.0257  0.0149  0.0415  168 PHE   A N   
3688 N N   B PHE   A 168 ? 0.1453 0.3029 0.1546 0.0150  0.0047  0.0345  168 PHE   A N   
3689 C CA  A PHE   A 168 ? 0.1343 0.3044 0.1723 0.0267  0.0279  0.0414  168 PHE   A CA  
3690 C CA  B PHE   A 168 ? 0.1523 0.2992 0.1733 0.0059  0.0068  0.0260  168 PHE   A CA  
3691 C C   A PHE   A 168 ? 0.1499 0.3293 0.2217 0.0188  0.0532  0.0270  168 PHE   A C   
3692 C C   B PHE   A 168 ? 0.1746 0.3250 0.2231 -0.0051 0.0325  0.0150  168 PHE   A C   
3693 O O   A PHE   A 168 ? 0.1496 0.3342 0.2516 0.0072  0.0637  0.0363  168 PHE   A O   
3694 O O   B PHE   A 168 ? 0.1767 0.3297 0.2532 -0.0144 0.0529  0.0229  168 PHE   A O   
3695 C CB  A PHE   A 168 ? 0.1338 0.2823 0.1639 0.0236  0.0154  0.0458  168 PHE   A CB  
3696 C CB  B PHE   A 168 ? 0.1482 0.2732 0.1594 -0.0024 -0.0161 0.0185  168 PHE   A CB  
3697 C CG  A PHE   A 168 ? 0.1306 0.2628 0.1515 0.0163  0.0151  0.0580  168 PHE   A CG  
3698 C CG  B PHE   A 168 ? 0.1407 0.2512 0.1485 -0.0110 -0.0267 0.0153  168 PHE   A CG  
3699 C CD1 A PHE   A 168 ? 0.1367 0.2593 0.1656 0.0059  0.0139  0.0677  168 PHE   A CD1 
3700 C CD1 B PHE   A 168 ? 0.1368 0.2441 0.1644 -0.0182 -0.0300 0.0188  168 PHE   A CD1 
3701 C CD2 A PHE   A 168 ? 0.1236 0.2538 0.1529 0.0140  0.0292  0.0592  168 PHE   A CD2 
3702 C CD2 B PHE   A 168 ? 0.1382 0.2440 0.1452 -0.0124 -0.0217 0.0097  168 PHE   A CD2 
3703 C CE1 A PHE   A 168 ? 0.1301 0.2537 0.1678 0.0032  0.0208  0.0754  168 PHE   A CE1 
3704 C CE1 B PHE   A 168 ? 0.1270 0.2405 0.1627 -0.0228 -0.0313 0.0152  168 PHE   A CE1 
3705 C CE2 A PHE   A 168 ? 0.1256 0.2478 0.1616 0.0102  0.0281  0.0718  168 PHE   A CE2 
3706 C CE2 B PHE   A 168 ? 0.1398 0.2388 0.1558 -0.0143 -0.0217 0.0132  168 PHE   A CE2 
3707 C CZ  A PHE   A 168 ? 0.1259 0.2480 0.1650 0.0064  0.0251  0.0778  168 PHE   A CZ  
3708 C CZ  B PHE   A 168 ? 0.1324 0.2381 0.1608 -0.0178 -0.0317 0.0149  168 PHE   A CZ  
3727 N N   A LEU   A 169 ? 0.1925 0.3477 0.2795 0.0146  0.0505  0.0042  169 LEU   A N   
3728 N N   B LEU   A 169 ? 0.2148 0.3447 0.2735 -0.0120 0.0257  -0.0042 169 LEU   A N   
3729 C CA  A LEU   A 169 ? 0.2419 0.3675 0.3606 0.0158  0.0212  -0.0096 169 LEU   A CA  
3730 C CA  B LEU   A 169 ? 0.2643 0.3676 0.3526 -0.0137 0.0028  -0.0166 169 LEU   A CA  
3731 C C   A LEU   A 169 ? 0.2498 0.3712 0.3948 0.0178  0.0100  -0.0057 169 LEU   A C   
3732 C C   B LEU   A 169 ? 0.2745 0.3733 0.3879 -0.0175 -0.0021 -0.0105 169 LEU   A C   
3733 O O   A LEU   A 169 ? 0.2548 0.3743 0.4014 0.0193  0.0068  -0.0060 169 LEU   A O   
3734 O O   B LEU   A 169 ? 0.2827 0.3778 0.3970 -0.0190 0.0008  -0.0079 169 LEU   A O   
3735 C CB  A LEU   A 169 ? 0.2743 0.3808 0.3880 0.0122  0.0055  -0.0236 169 LEU   A CB  
3736 C CB  B LEU   A 169 ? 0.2969 0.3825 0.3822 -0.0132 -0.0125 -0.0302 169 LEU   A CB  
3737 C CG  A LEU   A 169 ? 0.3009 0.3918 0.4149 0.0075  -0.0071 -0.0380 169 LEU   A CG  
3738 C CG  B LEU   A 169 ? 0.3223 0.3939 0.4074 -0.0154 -0.0255 -0.0424 169 LEU   A CG  
3739 C CD1 A LEU   A 169 ? 0.3083 0.3950 0.4226 0.0060  -0.0118 -0.0416 169 LEU   A CD1 
3740 C CD1 B LEU   A 169 ? 0.3299 0.3971 0.4144 -0.0172 -0.0305 -0.0447 169 LEU   A CD1 
3741 C CD2 A LEU   A 169 ? 0.3094 0.3962 0.4187 0.0054  -0.0089 -0.0433 169 LEU   A CD2 
3742 C CD2 B LEU   A 169 ? 0.3307 0.3987 0.4116 -0.0163 -0.0295 -0.0474 169 LEU   A CD2 
3743 O OXT A LEU   A 169 ? 0.2406 0.3706 0.4002 0.0207  0.0092  -0.0061 169 LEU   A OXT 
3744 O OXT B LEU   A 169 ? 0.2676 0.3722 0.3879 -0.0182 -0.0067 -0.0108 169 LEU   A OXT 
3767 N N   A SER   B 1   ? 0.3428 0.3439 0.3671 -0.0945 -0.0705 0.0399  1   SER   B N   
3768 N N   B SER   B 1   ? 0.3281 0.3122 0.3148 -0.0967 -0.0693 0.0140  1   SER   B N   
3769 C CA  A SER   B 1   ? 0.3343 0.3408 0.3633 -0.0988 -0.0701 0.0374  1   SER   B CA  
3770 C CA  B SER   B 1   ? 0.3197 0.3155 0.3214 -0.1008 -0.0726 0.0091  1   SER   B CA  
3771 C C   A SER   B 1   ? 0.3131 0.3334 0.3446 -0.0994 -0.0725 0.0567  1   SER   B C   
3772 C C   B SER   B 1   ? 0.2998 0.3191 0.3110 -0.0969 -0.0834 0.0291  1   SER   B C   
3773 O O   A SER   B 1   ? 0.3202 0.3347 0.3239 -0.0934 -0.0708 0.0559  1   SER   B O   
3774 O O   B SER   B 1   ? 0.2990 0.3180 0.2802 -0.0966 -0.0953 0.0260  1   SER   B O   
3775 C CB  A SER   B 1   ? 0.3431 0.3426 0.3647 -0.1026 -0.0635 0.0207  1   SER   B CB  
3776 C CB  B SER   B 1   ? 0.3278 0.3131 0.3220 -0.1078 -0.0615 -0.0126 1   SER   B CB  
3777 O OG  A SER   B 1   ? 0.3524 0.3488 0.3986 -0.1036 -0.0571 0.0160  1   SER   B OG  
3778 O OG  B SER   B 1   ? 0.3369 0.3186 0.3560 -0.1099 -0.0528 -0.0191 1   SER   B OG  
3793 N N   A MET   B 2   ? 0.2889 0.3237 0.3418 -0.1005 -0.0711 0.0878  2   MET   B N   
3794 N N   B MET   B 2   ? 0.2888 0.3238 0.3237 -0.0846 -0.0771 0.0600  2   MET   B N   
3795 C CA  A MET   B 2   ? 0.2700 0.3156 0.3475 -0.0892 -0.0704 0.1089  2   MET   B CA  
3796 C CA  B MET   B 2   ? 0.2827 0.3268 0.3345 -0.0640 -0.0694 0.0829  2   MET   B CA  
3797 C C   A MET   B 2   ? 0.2265 0.2803 0.2931 -0.0843 -0.0866 0.1376  2   MET   B C   
3798 C C   B MET   B 2   ? 0.2570 0.3028 0.2924 -0.0528 -0.0678 0.1044  2   MET   B C   
3799 O O   A MET   B 2   ? 0.2115 0.2850 0.2863 -0.0801 -0.0951 0.1478  2   MET   B O   
3800 O O   B MET   B 2   ? 0.2569 0.3133 0.3044 -0.0481 -0.0682 0.1036  2   MET   B O   
3801 C CB  A MET   B 2   ? 0.2997 0.3477 0.4239 -0.0702 -0.0523 0.0853  2   MET   B CB  
3802 C CB  B MET   B 2   ? 0.3068 0.3552 0.3995 -0.0470 -0.0629 0.0750  2   MET   B CB  
3803 C CG  A MET   B 2   ? 0.3258 0.3739 0.4891 -0.0508 -0.0372 0.0703  2   MET   B CG  
3804 C CG  B MET   B 2   ? 0.3271 0.3779 0.4484 -0.0314 -0.0582 0.0753  2   MET   B CG  
3805 S SD  A MET   B 2   ? 0.3491 0.3958 0.5496 -0.0342 -0.0259 0.0614  2   MET   B SD  
3806 S SD  B MET   B 2   ? 0.3443 0.3981 0.4975 -0.0185 -0.0573 0.0778  2   MET   B SD  
3807 C CE  A MET   B 2   ? 0.3543 0.3998 0.5558 -0.0310 -0.0205 0.0634  2   MET   B CE  
3808 C CE  B MET   B 2   ? 0.3474 0.4019 0.5012 -0.0174 -0.0531 0.0768  2   MET   B CE  
3827 N N   A VAL   B 3   ? 0.2021 0.2424 0.2680 -0.0869 -0.0849 0.1338  3   VAL   B N   
3828 N N   B VAL   B 3   ? 0.2326 0.2674 0.2599 -0.0512 -0.0597 0.1109  3   VAL   B N   
3829 C CA  A VAL   B 3   ? 0.1970 0.2085 0.2592 -0.0778 -0.0688 0.1165  3   VAL   B CA  
3830 C CA  B VAL   B 3   ? 0.2182 0.2349 0.2441 -0.0439 -0.0430 0.0957  3   VAL   B CA  
3831 C C   A VAL   B 3   ? 0.1780 0.1928 0.2278 -0.0644 -0.0632 0.0977  3   VAL   B C   
3832 C C   B VAL   B 3   ? 0.1927 0.2106 0.2064 -0.0397 -0.0386 0.0878  3   VAL   B C   
3833 O O   A VAL   B 3   ? 0.1714 0.1894 0.2351 -0.0628 -0.0688 0.1017  3   VAL   B O   
3834 O O   B VAL   B 3   ? 0.1902 0.2159 0.1916 -0.0220 -0.0364 0.0879  3   VAL   B O   
3835 C CB  A VAL   B 3   ? 0.2140 0.2087 0.2951 -0.0785 -0.0616 0.0926  3   VAL   B CB  
3836 C CB  B VAL   B 3   ? 0.2316 0.2318 0.2693 -0.0414 -0.0343 0.0821  3   VAL   B CB  
3837 C CG1 A VAL   B 3   ? 0.2214 0.2087 0.3093 -0.0777 -0.0611 0.0853  3   VAL   B CG1 
3838 C CG1 B VAL   B 3   ? 0.2367 0.2306 0.2810 -0.0446 -0.0335 0.0759  3   VAL   B CG1 
3839 C CG2 A VAL   B 3   ? 0.2193 0.2137 0.3145 -0.0750 -0.0536 0.0920  3   VAL   B CG2 
3840 C CG2 B VAL   B 3   ? 0.2358 0.2329 0.2774 -0.0350 -0.0320 0.0822  3   VAL   B CG2 
3859 N N   . ASN   B 4   ? 0.1737 0.1836 0.1990 -0.0504 -0.0514 0.0719  4   ASN   B N   
3860 C CA  . ASN   B 4   ? 0.1721 0.1770 0.1648 -0.0509 -0.0319 0.0343  4   ASN   B CA  
3861 C C   . ASN   B 4   ? 0.1854 0.1946 0.1568 -0.0551 -0.0115 0.0189  4   ASN   B C   
3862 O O   . ASN   B 4   ? 0.1859 0.2082 0.1918 -0.0541 -0.0159 0.0018  4   ASN   B O   
3863 C CB  . ASN   B 4   ? 0.1610 0.1752 0.1603 -0.0407 -0.0416 0.0230  4   ASN   B CB  
3864 C CG  . ASN   B 4   ? 0.1581 0.1637 0.1512 -0.0388 -0.0384 0.0237  4   ASN   B CG  
3865 O OD1 . ASN   B 4   ? 0.1582 0.1490 0.1544 -0.0354 -0.0391 0.0219  4   ASN   B OD1 
3866 N ND2 . ASN   B 4   ? 0.1684 0.1722 0.1489 -0.0232 -0.0235 0.0185  4   ASN   B ND2 
3874 N N   . SER   B 5   ? 0.2076 0.2143 0.1656 -0.0551 0.0108  0.0218  5   SER   B N   
3875 C CA  . SER   B 5   ? 0.2376 0.2468 0.2061 -0.0408 0.0322  0.0257  5   SER   B CA  
3876 C C   . SER   B 5   ? 0.2508 0.2484 0.2302 -0.0558 0.0465  0.0272  5   SER   B C   
3877 O O   . SER   B 5   ? 0.2631 0.2489 0.2975 -0.0527 0.0578  0.0229  5   SER   B O   
3878 C CB  . SER   B 5   ? 0.2521 0.2708 0.2481 -0.0290 0.0459  0.0388  5   SER   B CB  
3879 O OG  . SER   B 5   ? 0.2715 0.2918 0.3063 -0.0208 0.0540  0.0459  5   SER   B OG  
3885 N N   . PHE   B 6   ? 0.2620 0.2600 0.2026 -0.0593 0.0572  0.0370  6   PHE   B N   
3886 C CA  . PHE   B 6   ? 0.2637 0.2614 0.1808 -0.0705 0.0519  0.0164  6   PHE   B CA  
3887 C C   . PHE   B 6   ? 0.3109 0.2920 0.2130 -0.0718 0.0666  -0.0084 6   PHE   B C   
3888 O O   . PHE   B 6   ? 0.3253 0.3262 0.2512 -0.0640 0.0401  -0.0228 6   PHE   B O   
3889 C CB  . PHE   B 6   ? 0.2256 0.2382 0.1600 -0.0677 0.0309  0.0126  6   PHE   B CB  
3890 C CG  . PHE   B 6   ? 0.1927 0.2102 0.1524 -0.0591 0.0135  0.0092  6   PHE   B CG  
3891 C CD1 . PHE   B 6   ? 0.1922 0.1820 0.1354 -0.0566 -0.0007 0.0071  6   PHE   B CD1 
3892 C CD2 . PHE   B 6   ? 0.1711 0.2110 0.1607 -0.0490 0.0104  0.0292  6   PHE   B CD2 
3893 C CE1 . PHE   B 6   ? 0.1834 0.1643 0.1490 -0.0491 -0.0070 0.0023  6   PHE   B CE1 
3894 C CE2 . PHE   B 6   ? 0.1737 0.1940 0.1926 -0.0411 0.0059  0.0269  6   PHE   B CE2 
3895 C CZ  . PHE   B 6   ? 0.1742 0.1715 0.1705 -0.0406 0.0023  0.0056  6   PHE   B CZ  
3905 N N   A SER   B 7   ? 0.3264 0.2790 0.2247 -0.0823 0.0866  -0.0273 7   SER   B N   
3906 N N   B SER   B 7   ? 0.3255 0.2814 0.2214 -0.0757 0.0794  -0.0183 7   SER   B N   
3907 C CA  A SER   B 7   ? 0.3376 0.2745 0.2612 -0.0823 0.1012  -0.0376 7   SER   B CA  
3908 C CA  B SER   B 7   ? 0.3359 0.2784 0.2520 -0.0701 0.0857  -0.0193 7   SER   B CA  
3909 C C   A SER   B 7   ? 0.3303 0.2601 0.2499 -0.0848 0.1130  -0.0447 7   SER   B C   
3910 C C   B SER   B 7   ? 0.3292 0.2632 0.2282 -0.0710 0.0802  -0.0196 7   SER   B C   
3911 O O   A SER   B 7   ? 0.3310 0.2593 0.2725 -0.0873 0.1076  -0.0414 7   SER   B O   
3912 O O   B SER   B 7   ? 0.3287 0.2653 0.2419 -0.0710 0.0777  -0.0140 7   SER   B O   
3913 C CB  A SER   B 7   ? 0.3491 0.2835 0.3013 -0.0770 0.1069  -0.0367 7   SER   B CB  
3914 C CB  B SER   B 7   ? 0.3468 0.2895 0.2968 -0.0620 0.0966  -0.0165 7   SER   B CB  
3915 O OG  A SER   B 7   ? 0.3565 0.2928 0.3370 -0.0719 0.1038  -0.0317 7   SER   B OG  
3916 O OG  B SER   B 7   ? 0.3539 0.3003 0.3303 -0.0545 0.0959  -0.0107 7   SER   B OG  
3927 N N   A GLY   B 8   ? 0.3253 0.2481 0.2450 -0.0750 0.1225  -0.0584 8   GLY   B N   
3928 N N   B GLY   B 8   ? 0.3246 0.2467 0.2250 -0.0646 0.0705  -0.0265 8   GLY   B N   
3929 C CA  A GLY   B 8   ? 0.3130 0.2325 0.2350 -0.0699 0.1284  -0.0649 8   GLY   B CA  
3930 C CA  B GLY   B 8   ? 0.3149 0.2288 0.2114 -0.0635 0.0624  -0.0310 8   GLY   B CA  
3931 C C   A GLY   B 8   ? 0.2971 0.2113 0.2236 -0.0675 0.1274  -0.0642 8   GLY   B C   
3932 C C   B GLY   B 8   ? 0.3037 0.2068 0.2027 -0.0659 0.0517  -0.0309 8   GLY   B C   
3933 O O   A GLY   B 8   ? 0.2994 0.2135 0.2522 -0.0687 0.1276  -0.0640 8   GLY   B O   
3934 O O   B GLY   B 8   ? 0.3035 0.2135 0.2087 -0.0610 0.0493  -0.0338 8   GLY   B O   
3941 N N   A TYR   B 9   ? 0.2865 0.1936 0.2070 -0.0555 0.1084  -0.0656 9   TYR   B N   
3942 N N   B TYR   B 9   ? 0.2981 0.1878 0.2021 -0.0584 0.0404  -0.0322 9   TYR   B N   
3943 C CA  A TYR   B 9   ? 0.2729 0.1788 0.1911 -0.0466 0.0850  -0.0439 9   TYR   B CA  
3944 C CA  B TYR   B 9   ? 0.2889 0.1673 0.1865 -0.0493 0.0380  -0.0234 9   TYR   B CA  
3945 C C   A TYR   B 9   ? 0.2738 0.1786 0.1810 -0.0452 0.0579  -0.0348 9   TYR   B C   
3946 C C   B TYR   B 9   ? 0.2821 0.1707 0.1718 -0.0509 0.0310  -0.0207 9   TYR   B C   
3947 O O   A TYR   B 9   ? 0.2837 0.1939 0.2148 -0.0397 0.0594  -0.0288 9   TYR   B O   
3948 O O   B TYR   B 9   ? 0.2946 0.1837 0.1963 -0.0528 0.0277  -0.0151 9   TYR   B O   
3949 C CB  A TYR   B 9   ? 0.2632 0.1653 0.1908 -0.0401 0.0826  -0.0413 9   TYR   B CB  
3950 C CB  B TYR   B 9   ? 0.2897 0.1489 0.1928 -0.0393 0.0417  -0.0181 9   TYR   B CB  
3951 C CG  A TYR   B 9   ? 0.2500 0.1481 0.1888 -0.0468 0.0803  -0.0463 9   TYR   B CG  
3952 C CG  B TYR   B 9   ? 0.2858 0.1310 0.1965 -0.0425 0.0474  -0.0205 9   TYR   B CG  
3953 C CD1 A TYR   B 9   ? 0.2501 0.1394 0.1966 -0.0561 0.0786  -0.0448 9   TYR   B CD1 
3954 C CD1 B TYR   B 9   ? 0.2875 0.1229 0.2067 -0.0513 0.0484  -0.0224 9   TYR   B CD1 
3955 C CD2 A TYR   B 9   ? 0.2378 0.1452 0.1918 -0.0499 0.0709  -0.0494 9   TYR   B CD2 
3956 C CD2 B TYR   B 9   ? 0.2775 0.1226 0.1940 -0.0360 0.0511  -0.0269 9   TYR   B CD2 
3957 C CE1 A TYR   B 9   ? 0.2452 0.1466 0.2106 -0.0653 0.0736  -0.0504 9   TYR   B CE1 
3958 C CE1 B TYR   B 9   ? 0.2843 0.1237 0.2108 -0.0514 0.0514  -0.0337 9   TYR   B CE1 
3959 C CE2 A TYR   B 9   ? 0.2354 0.1465 0.2026 -0.0515 0.0645  -0.0533 9   TYR   B CE2 
3960 C CE2 B TYR   B 9   ? 0.2769 0.1195 0.2061 -0.0341 0.0520  -0.0339 9   TYR   B CE2 
3961 C CZ  A TYR   B 9   ? 0.2391 0.1522 0.2144 -0.0640 0.0692  -0.0557 9   TYR   B CZ  
3962 C CZ  B TYR   B 9   ? 0.2800 0.1235 0.2193 -0.0427 0.0560  -0.0439 9   TYR   B CZ  
3963 O OH  A TYR   B 9   ? 0.2369 0.1675 0.2325 -0.0742 0.0690  -0.0534 9   TYR   B OH  
3964 O OH  B TYR   B 9   ? 0.2776 0.1325 0.2305 -0.0460 0.0591  -0.0590 9   TYR   B OH  
3983 N N   . LEU   B 10  ? 0.2628 0.1590 0.1551 -0.0491 0.0275  -0.0337 10  LEU   B N   
3984 C CA  . LEU   B 10  ? 0.2504 0.1564 0.1587 -0.0533 -0.0034 -0.0312 10  LEU   B CA  
3985 C C   . LEU   B 10  ? 0.2267 0.1498 0.1580 -0.0519 -0.0202 -0.0287 10  LEU   B C   
3986 O O   . LEU   B 10  ? 0.2121 0.1524 0.1704 -0.0399 -0.0137 -0.0220 10  LEU   B O   
3987 C CB  . LEU   B 10  ? 0.2620 0.1561 0.1804 -0.0538 -0.0226 -0.0181 10  LEU   B CB  
3988 C CG  . LEU   B 10  ? 0.2784 0.1643 0.2230 -0.0463 -0.0451 -0.0080 10  LEU   B CG  
3989 C CD1 . LEU   B 10  ? 0.2902 0.1804 0.2511 -0.0453 -0.0471 -0.0091 10  LEU   B CD1 
3990 C CD2 . LEU   B 10  ? 0.2897 0.1700 0.2610 -0.0470 -0.0432 0.0111  10  LEU   B CD2 
4003 N N   . LYS   B 11  ? 0.2395 0.1761 0.1550 -0.0418 -0.0240 -0.0196 11  LYS   B N   
4004 C CA  . LYS   B 11  ? 0.2563 0.2069 0.1838 -0.0322 -0.0445 -0.0228 11  LYS   B CA  
4005 C C   . LYS   B 11  ? 0.2417 0.1885 0.1901 -0.0578 -0.0421 -0.0379 11  LYS   B C   
4006 O O   . LYS   B 11  ? 0.2621 0.2130 0.2420 -0.0713 -0.0357 -0.0722 11  LYS   B O   
4007 C CB  . LYS   B 11  ? 0.2894 0.2577 0.2412 -0.0058 -0.0550 -0.0155 11  LYS   B CB  
4008 C CG  . LYS   B 11  ? 0.3185 0.2908 0.3041 0.0097  -0.0542 -0.0162 11  LYS   B CG  
4009 C CD  . LYS   B 11  ? 0.3408 0.3138 0.3704 0.0184  -0.0456 -0.0177 11  LYS   B CD  
4010 C CE  . LYS   B 11  ? 0.3592 0.3269 0.4197 0.0182  -0.0414 -0.0163 11  LYS   B CE  
4011 N NZ  . LYS   B 11  ? 0.3667 0.3342 0.4475 0.0160  -0.0400 -0.0111 11  LYS   B NZ  
4025 N N   . LEU   B 12  ? 0.2143 0.1636 0.1922 -0.0528 -0.0352 -0.0360 12  LEU   B N   
4026 C CA  . LEU   B 12  ? 0.2029 0.1469 0.2170 -0.0495 -0.0329 -0.0284 12  LEU   B CA  
4027 C C   . LEU   B 12  ? 0.1943 0.1465 0.2191 -0.0510 -0.0375 -0.0254 12  LEU   B C   
4028 O O   . LEU   B 12  ? 0.1972 0.1538 0.2340 -0.0622 -0.0479 -0.0181 12  LEU   B O   
4029 C CB  . LEU   B 12  ? 0.1990 0.1278 0.2214 -0.0379 -0.0238 -0.0251 12  LEU   B CB  
4030 C CG  . LEU   B 12  ? 0.1920 0.1259 0.2161 -0.0361 -0.0174 -0.0219 12  LEU   B CG  
4031 C CD1 . LEU   B 12  ? 0.2032 0.1305 0.2085 -0.0232 -0.0112 -0.0082 12  LEU   B CD1 
4032 C CD2 . LEU   B 12  ? 0.1992 0.1387 0.2443 -0.0288 -0.0130 -0.0363 12  LEU   B CD2 
4044 N N   . THR   B 13  ? 0.1850 0.1549 0.2269 -0.0488 -0.0430 -0.0336 13  THR   B N   
4045 C CA  . THR   B 13  ? 0.1838 0.1637 0.2150 -0.0525 -0.0501 -0.0223 13  THR   B CA  
4046 C C   . THR   B 13  ? 0.2171 0.1741 0.2241 -0.0591 -0.0603 -0.0207 13  THR   B C   
4047 O O   . THR   B 13  ? 0.2305 0.1725 0.2430 -0.0578 -0.0255 -0.0214 13  THR   B O   
4048 C CB  . THR   B 13  ? 0.1642 0.1680 0.2172 -0.0477 -0.0437 -0.0131 13  THR   B CB  
4049 O OG1 . THR   B 13  ? 0.1580 0.1567 0.2288 -0.0425 -0.0363 -0.0130 13  THR   B OG1 
4050 C CG2 . THR   B 13  ? 0.1672 0.1749 0.2273 -0.0402 -0.0279 -0.0047 13  THR   B CG2 
4058 N N   A ASP   B 14  ? 0.2253 0.1807 0.2403 -0.0631 -0.0846 -0.0149 14  ASP   B N   
4059 N N   B ASP   B 14  ? 0.2271 0.1818 0.2377 -0.0604 -0.0770 -0.0079 14  ASP   B N   
4060 C CA  A ASP   B 14  ? 0.2331 0.1942 0.2633 -0.0590 -0.0939 0.0037  14  ASP   B CA  
4061 C CA  B ASP   B 14  ? 0.2364 0.1952 0.2555 -0.0549 -0.0820 0.0142  14  ASP   B CA  
4062 C C   A ASP   B 14  ? 0.2208 0.1774 0.2328 -0.0568 -0.0778 0.0052  14  ASP   B C   
4063 C C   B ASP   B 14  ? 0.2226 0.1790 0.2265 -0.0526 -0.0754 0.0149  14  ASP   B C   
4064 O O   A ASP   B 14  ? 0.2372 0.1863 0.2414 -0.0518 -0.0692 0.0137  14  ASP   B O   
4065 O O   B ASP   B 14  ? 0.2394 0.1884 0.2292 -0.0444 -0.0756 0.0293  14  ASP   B O   
4066 C CB  A ASP   B 14  ? 0.2506 0.2224 0.3228 -0.0564 -0.1120 0.0058  14  ASP   B CB  
4067 C CB  B ASP   B 14  ? 0.2573 0.2227 0.3090 -0.0503 -0.0864 0.0223  14  ASP   B CB  
4068 C CG  A ASP   B 14  ? 0.2726 0.2465 0.3887 -0.0503 -0.1073 -0.0014 14  ASP   B CG  
4069 C CG  B ASP   B 14  ? 0.2794 0.2469 0.3672 -0.0444 -0.0766 0.0211  14  ASP   B CG  
4070 O OD1 A ASP   B 14  ? 0.2859 0.2512 0.4018 -0.0542 -0.1027 -0.0149 14  ASP   B OD1 
4071 O OD1 B ASP   B 14  ? 0.2897 0.2548 0.3774 -0.0453 -0.0628 0.0204  14  ASP   B OD1 
4072 O OD2 A ASP   B 14  ? 0.2740 0.2571 0.4182 -0.0480 -0.1070 0.0007  14  ASP   B OD2 
4073 O OD2 B ASP   B 14  ? 0.2836 0.2554 0.3872 -0.0469 -0.0816 0.0191  14  ASP   B OD2 
4082 N N   . ASN   B 15  ? 0.1909 0.1583 0.2093 -0.0444 -0.0705 0.0068  15  ASN   B N   
4083 C CA  . ASN   B 15  ? 0.1523 0.1379 0.1922 -0.0312 -0.0454 -0.0047 15  ASN   B CA  
4084 C C   . ASN   B 15  ? 0.1342 0.1257 0.1735 -0.0191 -0.0302 -0.0091 15  ASN   B C   
4085 O O   . ASN   B 15  ? 0.1380 0.1219 0.2000 -0.0197 -0.0360 -0.0197 15  ASN   B O   
4086 C CB  . ASN   B 15  ? 0.1443 0.1338 0.2029 -0.0132 -0.0435 -0.0028 15  ASN   B CB  
4087 C CG  . ASN   B 15  ? 0.1379 0.1356 0.2010 -0.0172 -0.0188 -0.0049 15  ASN   B CG  
4088 O OD1 . ASN   B 15  ? 0.1447 0.1553 0.2367 -0.0367 -0.0246 0.0058  15  ASN   B OD1 
4089 N ND2 . ASN   B 15  ? 0.1385 0.1160 0.2056 -0.0141 0.0087  -0.0139 15  ASN   B ND2 
4097 N N   . VAL   B 16  ? 0.1399 0.1222 0.1772 -0.0243 -0.0386 -0.0069 16  VAL   B N   
4098 C CA  . VAL   B 16  ? 0.1376 0.1198 0.1655 -0.0224 -0.0321 -0.0261 16  VAL   B CA  
4099 C C   . VAL   B 16  ? 0.1381 0.1248 0.1685 -0.0340 -0.0305 -0.0162 16  VAL   B C   
4100 O O   . VAL   B 16  ? 0.1504 0.1386 0.1918 -0.0316 -0.0190 -0.0276 16  VAL   B O   
4101 C CB  . VAL   B 16  ? 0.1443 0.1268 0.1762 -0.0115 -0.0152 -0.0224 16  VAL   B CB  
4102 C CG1 . VAL   B 16  ? 0.1576 0.1201 0.1699 0.0023  -0.0174 -0.0141 16  VAL   B CG1 
4103 C CG2 . VAL   B 16  ? 0.1422 0.1322 0.2000 -0.0069 -0.0092 -0.0242 16  VAL   B CG2 
4113 N N   . TYR   B 17  ? 0.1448 0.1276 0.1646 -0.0278 -0.0275 -0.0177 17  TYR   B N   
4114 C CA  . TYR   B 17  ? 0.1521 0.1411 0.1641 -0.0320 -0.0217 -0.0071 17  TYR   B CA  
4115 C C   . TYR   B 17  ? 0.1466 0.1228 0.1592 -0.0343 -0.0125 -0.0092 17  TYR   B C   
4116 O O   . TYR   B 17  ? 0.1445 0.1286 0.1659 -0.0230 -0.0244 -0.0312 17  TYR   B O   
4117 C CB  . TYR   B 17  ? 0.1784 0.1772 0.1676 -0.0182 -0.0161 0.0243  17  TYR   B CB  
4118 C CG  . TYR   B 17  ? 0.2082 0.2192 0.2077 -0.0156 -0.0245 0.0321  17  TYR   B CG  
4119 C CD1 . TYR   B 17  ? 0.2249 0.2275 0.2267 -0.0111 -0.0298 0.0493  17  TYR   B CD1 
4120 C CD2 . TYR   B 17  ? 0.2281 0.2474 0.2326 -0.0083 -0.0335 0.0263  17  TYR   B CD2 
4121 C CE1 . TYR   B 17  ? 0.2433 0.2505 0.2351 -0.0046 -0.0406 0.0431  17  TYR   B CE1 
4122 C CE2 . TYR   B 17  ? 0.2422 0.2630 0.2565 0.0007  -0.0452 0.0346  17  TYR   B CE2 
4123 C CZ  . TYR   B 17  ? 0.2550 0.2691 0.2563 0.0027  -0.0510 0.0425  17  TYR   B CZ  
4124 O OH  . TYR   B 17  ? 0.2703 0.2845 0.2783 0.0115  -0.0572 0.0447  17  TYR   B OH  
4134 N N   . ILE   B 18  ? 0.1602 0.1196 0.1447 -0.0290 -0.0043 -0.0204 18  ILE   B N   
4135 C CA  . ILE   B 18  ? 0.1591 0.1177 0.1434 -0.0268 -0.0104 -0.0173 18  ILE   B CA  
4136 C C   . ILE   B 18  ? 0.1740 0.1229 0.1413 -0.0331 -0.0014 -0.0275 18  ILE   B C   
4137 O O   . ILE   B 18  ? 0.2005 0.1370 0.1558 -0.0293 0.0041  -0.0340 18  ILE   B O   
4138 C CB  . ILE   B 18  ? 0.1628 0.1214 0.1563 -0.0369 -0.0079 -0.0117 18  ILE   B CB  
4139 C CG1 . ILE   B 18  ? 0.1622 0.1286 0.1670 -0.0369 -0.0047 0.0003  18  ILE   B CG1 
4140 C CG2 . ILE   B 18  ? 0.1658 0.1272 0.1690 -0.0366 -0.0072 -0.0131 18  ILE   B CG2 
4141 C CD1 . ILE   B 18  ? 0.1713 0.1577 0.1940 -0.0349 -0.0216 0.0143  18  ILE   B CD1 
4153 N N   A LYS   B 19  ? 0.1722 0.1288 0.1499 -0.0219 0.0159  -0.0326 19  LYS   B N   
4154 N N   B LYS   B 19  ? 0.1710 0.1271 0.1477 -0.0203 0.0142  -0.0293 19  LYS   B N   
4155 C CA  A LYS   B 19  ? 0.1768 0.1360 0.1641 -0.0247 0.0259  -0.0347 19  LYS   B CA  
4156 C CA  B LYS   B 19  ? 0.1748 0.1329 0.1587 -0.0211 0.0210  -0.0281 19  LYS   B CA  
4157 C C   A LYS   B 19  ? 0.1621 0.1314 0.1745 -0.0227 0.0298  -0.0363 19  LYS   B C   
4158 C C   B LYS   B 19  ? 0.1613 0.1301 0.1733 -0.0180 0.0268  -0.0309 19  LYS   B C   
4159 O O   A LYS   B 19  ? 0.1572 0.1323 0.1702 -0.0199 0.0232  -0.0365 19  LYS   B O   
4160 O O   B LYS   B 19  ? 0.1576 0.1315 0.1745 -0.0100 0.0179  -0.0280 19  LYS   B O   
4161 C CB  A LYS   B 19  ? 0.1970 0.1559 0.1790 -0.0278 0.0350  -0.0226 19  LYS   B CB  
4162 C CB  B LYS   B 19  ? 0.1924 0.1494 0.1654 -0.0226 0.0250  -0.0116 19  LYS   B CB  
4163 C CG  A LYS   B 19  ? 0.2164 0.1749 0.2011 -0.0287 0.0462  -0.0242 19  LYS   B CG  
4164 C CG  B LYS   B 19  ? 0.2102 0.1680 0.1804 -0.0216 0.0266  -0.0093 19  LYS   B CG  
4165 C CD  A LYS   B 19  ? 0.2361 0.2003 0.2105 -0.0335 0.0510  -0.0203 19  LYS   B CD  
4166 C CD  B LYS   B 19  ? 0.2302 0.1952 0.1909 -0.0255 0.0265  -0.0041 19  LYS   B CD  
4167 C CE  A LYS   B 19  ? 0.2537 0.2212 0.2336 -0.0333 0.0493  -0.0169 19  LYS   B CE  
4168 C CE  B LYS   B 19  ? 0.2477 0.2182 0.2177 -0.0248 0.0212  -0.0019 19  LYS   B CE  
4169 N NZ  A LYS   B 19  ? 0.2646 0.2328 0.2428 -0.0367 0.0470  -0.0111 19  LYS   B NZ  
4170 N NZ  B LYS   B 19  ? 0.2590 0.2307 0.2265 -0.0253 0.0169  0.0032  19  LYS   B NZ  
4197 N N   . ASN   B 20  ? 0.1606 0.1361 0.1932 -0.0157 0.0305  -0.0470 20  ASN   B N   
4198 C CA  . ASN   B 20  ? 0.1595 0.1504 0.2157 -0.0074 0.0335  -0.0585 20  ASN   B CA  
4199 C C   . ASN   B 20  ? 0.1570 0.1673 0.2218 -0.0202 0.0483  -0.0667 20  ASN   B C   
4200 O O   . ASN   B 20  ? 0.1760 0.2037 0.2499 -0.0330 0.0524  -0.0698 20  ASN   B O   
4201 C CB  . ASN   B 20  ? 0.1830 0.1537 0.2428 0.0092  0.0258  -0.0590 20  ASN   B CB  
4202 C CG  . ASN   B 20  ? 0.2063 0.1587 0.2688 0.0353  0.0215  -0.0612 20  ASN   B CG  
4203 O OD1 . ASN   B 20  ? 0.2363 0.1929 0.3054 0.0511  0.0182  -0.0671 20  ASN   B OD1 
4204 N ND2 . ASN   B 20  ? 0.1968 0.1563 0.2560 0.0335  0.0142  -0.0597 20  ASN   B ND2 
4212 N N   . ALA   B 21  ? 0.1603 0.1491 0.2309 -0.0259 0.0420  -0.0529 21  ALA   B N   
4213 C CA  . ALA   B 21  ? 0.1684 0.1534 0.2460 -0.0317 0.0340  -0.0399 21  ALA   B CA  
4214 C C   . ALA   B 21  ? 0.1643 0.1358 0.2363 -0.0220 0.0306  -0.0256 21  ALA   B C   
4215 O O   . ALA   B 21  ? 0.1743 0.1306 0.2359 -0.0296 0.0307  -0.0174 21  ALA   B O   
4216 C CB  . ALA   B 21  ? 0.1897 0.1759 0.2602 -0.0431 0.0342  -0.0196 21  ALA   B CB  
4222 N N   . ASP   B 22  ? 0.1593 0.1345 0.2387 -0.0220 0.0218  -0.0258 22  ASP   B N   
4223 C CA  . ASP   B 22  ? 0.1548 0.1315 0.2336 -0.0140 0.0171  -0.0166 22  ASP   B CA  
4224 C C   . ASP   B 22  ? 0.1508 0.1262 0.1919 -0.0145 0.0201  -0.0093 22  ASP   B C   
4225 O O   . ASP   B 22  ? 0.1587 0.1296 0.1959 -0.0114 0.0162  -0.0029 22  ASP   B O   
4226 C CB  . ASP   B 22  ? 0.1642 0.1397 0.2782 -0.0114 0.0114  0.0019  22  ASP   B CB  
4227 C CG  . ASP   B 22  ? 0.1676 0.1563 0.3299 -0.0073 -0.0120 -0.0035 22  ASP   B CG  
4228 O OD1 . ASP   B 22  ? 0.1867 0.1526 0.3252 -0.0032 -0.0363 -0.0110 22  ASP   B OD1 
4229 O OD2 . ASP   B 22  ? 0.1745 0.1861 0.3827 0.0028  -0.0269 -0.0159 22  ASP   B OD2 
4234 N N   . ILE   B 23  ? 0.1530 0.1191 0.1751 -0.0119 0.0119  0.0126  23  ILE   B N   
4235 C CA  . ILE   B 23  ? 0.1436 0.1176 0.1590 -0.0112 0.0020  0.0064  23  ILE   B CA  
4236 C C   . ILE   B 23  ? 0.1377 0.1177 0.1706 -0.0057 -0.0038 -0.0010 23  ILE   B C   
4237 O O   . ILE   B 23  ? 0.1331 0.1138 0.1556 -0.0094 0.0037  -0.0009 23  ILE   B O   
4238 C CB  . ILE   B 23  ? 0.1371 0.1239 0.1802 -0.0222 -0.0021 0.0182  23  ILE   B CB  
4239 C CG1 . ILE   B 23  ? 0.1431 0.1360 0.1889 -0.0206 0.0092  0.0232  23  ILE   B CG1 
4240 C CG2 . ILE   B 23  ? 0.1449 0.1450 0.1976 -0.0157 0.0036  0.0121  23  ILE   B CG2 
4241 C CD1 . ILE   B 23  ? 0.1466 0.1514 0.1972 -0.0140 0.0088  0.0156  23  ILE   B CD1 
4253 N N   . VAL   B 24  ? 0.1389 0.1150 0.1767 -0.0044 -0.0075 -0.0031 24  VAL   B N   
4254 C CA  . VAL   B 24  ? 0.1347 0.1186 0.1937 -0.0054 -0.0102 -0.0056 24  VAL   B CA  
4255 C C   . VAL   B 24  ? 0.1322 0.1239 0.1996 -0.0064 -0.0031 0.0009  24  VAL   B C   
4256 O O   . VAL   B 24  ? 0.1318 0.1308 0.2097 -0.0139 -0.0087 0.0105  24  VAL   B O   
4257 C CB  . VAL   B 24  ? 0.1426 0.1418 0.2047 0.0026  -0.0217 -0.0004 24  VAL   B CB  
4258 C CG1 . VAL   B 24  ? 0.1408 0.1480 0.2223 -0.0070 -0.0275 0.0078  24  VAL   B CG1 
4259 C CG2 . VAL   B 24  ? 0.1558 0.1711 0.2080 0.0064  -0.0161 -0.0117 24  VAL   B CG2 
4269 N N   . GLU   B 25  ? 0.1486 0.1352 0.2029 -0.0052 0.0052  -0.0013 25  GLU   B N   
4270 C CA  . GLU   B 25  ? 0.1582 0.1598 0.2154 -0.0001 0.0202  -0.0010 25  GLU   B CA  
4271 C C   . GLU   B 25  ? 0.1587 0.1467 0.1959 -0.0080 0.0136  0.0020  25  GLU   B C   
4272 O O   . GLU   B 25  ? 0.1629 0.1666 0.2045 -0.0040 0.0212  0.0134  25  GLU   B O   
4273 C CB  . GLU   B 25  ? 0.1909 0.2032 0.2636 0.0185  0.0346  -0.0146 25  GLU   B CB  
4274 C CG  . GLU   B 25  ? 0.2242 0.2634 0.3565 0.0245  0.0332  -0.0168 25  GLU   B CG  
4275 C CD  . GLU   B 25  ? 0.2589 0.3292 0.4469 0.0212  0.0262  -0.0179 25  GLU   B CD  
4276 O OE1 . GLU   B 25  ? 0.2813 0.3519 0.4721 0.0239  0.0283  -0.0130 25  GLU   B OE1 
4277 O OE2 . GLU   B 25  ? 0.2820 0.3479 0.4756 0.0203  0.0194  -0.0255 25  GLU   B OE2 
4284 N N   . GLU   B 26  ? 0.1590 0.1393 0.1793 -0.0238 0.0087  0.0048  26  GLU   B N   
4285 C CA  . GLU   B 26  ? 0.1567 0.1576 0.1754 -0.0335 0.0005  0.0116  26  GLU   B CA  
4286 C C   . GLU   B 26  ? 0.1368 0.1541 0.1775 -0.0216 0.0118  0.0241  26  GLU   B C   
4287 O O   . GLU   B 26  ? 0.1559 0.1783 0.1847 -0.0170 0.0110  0.0339  26  GLU   B O   
4288 C CB  . GLU   B 26  ? 0.1841 0.1806 0.1951 -0.0482 -0.0012 0.0111  26  GLU   B CB  
4289 C CG  . GLU   B 26  ? 0.2234 0.2109 0.2504 -0.0549 0.0102  -0.0086 26  GLU   B CG  
4290 C CD  . GLU   B 26  ? 0.2491 0.2348 0.2586 -0.0726 0.0188  -0.0442 26  GLU   B CD  
4291 O OE1 . GLU   B 26  ? 0.2710 0.2217 0.2659 -0.0777 0.0498  -0.0449 26  GLU   B OE1 
4292 O OE2 . GLU   B 26  ? 0.2486 0.2760 0.2923 -0.0707 0.0154  -0.0328 26  GLU   B OE2 
4299 N N   . ALA   B 27  ? 0.1213 0.1363 0.1852 -0.0176 0.0127  0.0172  27  ALA   B N   
4300 C CA  . ALA   B 27  ? 0.1292 0.1374 0.1969 -0.0114 0.0112  0.0302  27  ALA   B CA  
4301 C C   . ALA   B 27  ? 0.1333 0.1465 0.2147 -0.0054 0.0168  0.0391  27  ALA   B C   
4302 O O   . ALA   B 27  ? 0.1419 0.1512 0.2206 0.0063  0.0220  0.0468  27  ALA   B O   
4303 C CB  . ALA   B 27  ? 0.1444 0.1229 0.2024 -0.0172 0.0079  0.0170  27  ALA   B CB  
4309 N N   . LYS   B 28  ? 0.1221 0.1663 0.2517 -0.0156 0.0250  0.0625  28  LYS   B N   
4310 C CA  . LYS   B 28  ? 0.1477 0.2094 0.2841 -0.0038 0.0608  0.0844  28  LYS   B CA  
4311 C C   . LYS   B 28  ? 0.1742 0.2265 0.2711 0.0080  0.0797  0.0722  28  LYS   B C   
4312 O O   . LYS   B 28  ? 0.1981 0.2240 0.2883 0.0007  0.0763  0.0759  28  LYS   B O   
4313 C CB  . LYS   B 28  ? 0.1753 0.2520 0.3452 0.0062  0.0943  0.1131  28  LYS   B CB  
4314 C CG  . LYS   B 28  ? 0.2119 0.3020 0.3798 0.0161  0.1028  0.1319  28  LYS   B CG  
4315 C CD  . LYS   B 28  ? 0.2740 0.3623 0.4310 0.0210  0.1190  0.1377  28  LYS   B CD  
4316 C CE  . LYS   B 28  ? 0.3345 0.4101 0.4862 0.0243  0.1156  0.1395  28  LYS   B CE  
4317 N NZ  . LYS   B 28  ? 0.3638 0.4312 0.5044 0.0260  0.1106  0.1436  28  LYS   B NZ  
4331 N N   A LYS   B 29  ? 0.1868 0.2462 0.2691 0.0241  0.0782  0.0627  29  LYS   B N   
4332 N N   B LYS   B 29  ? 0.1868 0.2461 0.2693 0.0236  0.0779  0.0636  29  LYS   B N   
4333 C CA  A LYS   B 29  ? 0.2209 0.2733 0.2849 0.0270  0.0724  0.0559  29  LYS   B CA  
4334 C CA  B LYS   B 29  ? 0.2204 0.2728 0.2844 0.0267  0.0730  0.0574  29  LYS   B CA  
4335 C C   A LYS   B 29  ? 0.2189 0.2712 0.2479 0.0277  0.0655  0.0662  29  LYS   B C   
4336 C C   B LYS   B 29  ? 0.2184 0.2709 0.2477 0.0275  0.0658  0.0669  29  LYS   B C   
4337 O O   A LYS   B 29  ? 0.2328 0.2842 0.2541 0.0306  0.0607  0.0660  29  LYS   B O   
4338 O O   B LYS   B 29  ? 0.2320 0.2839 0.2541 0.0305  0.0609  0.0666  29  LYS   B O   
4339 C CB  A LYS   B 29  ? 0.2629 0.3035 0.3511 0.0243  0.0576  0.0392  29  LYS   B CB  
4340 C CB  B LYS   B 29  ? 0.2620 0.3025 0.3502 0.0240  0.0589  0.0421  29  LYS   B CB  
4341 C CG  A LYS   B 29  ? 0.2949 0.3270 0.4176 0.0202  0.0491  0.0296  29  LYS   B CG  
4342 C CG  B LYS   B 29  ? 0.2931 0.3254 0.4156 0.0201  0.0512  0.0336  29  LYS   B CG  
4343 C CD  A LYS   B 29  ? 0.3178 0.3429 0.4711 0.0151  0.0488  0.0214  29  LYS   B CD  
4344 C CD  B LYS   B 29  ? 0.3144 0.3408 0.4681 0.0150  0.0512  0.0261  29  LYS   B CD  
4345 C CE  A LYS   B 29  ? 0.3328 0.3522 0.5067 0.0120  0.0497  0.0153  29  LYS   B CE  
4346 C CE  B LYS   B 29  ? 0.3280 0.3497 0.5037 0.0114  0.0530  0.0209  29  LYS   B CE  
4347 N NZ  A LYS   B 29  ? 0.3407 0.3571 0.5324 0.0109  0.0490  0.0103  29  LYS   B NZ  
4348 N NZ  B LYS   B 29  ? 0.3348 0.3546 0.5288 0.0108  0.0520  0.0168  29  LYS   B NZ  
4375 N N   . VAL   B 30  ? 0.2017 0.2567 0.2293 0.0190  0.0538  0.0735  30  VAL   B N   
4376 C CA  . VAL   B 30  ? 0.1851 0.2420 0.2462 0.0006  0.0185  0.0744  30  VAL   B CA  
4377 C C   . VAL   B 30  ? 0.1627 0.2275 0.2428 -0.0093 0.0263  0.0891  30  VAL   B C   
4378 O O   . VAL   B 30  ? 0.1824 0.2504 0.2475 0.0017  0.0216  0.1021  30  VAL   B O   
4379 C CB  . VAL   B 30  ? 0.1897 0.2379 0.2759 -0.0176 -0.0148 0.0673  30  VAL   B CB  
4380 C CG1 . VAL   B 30  ? 0.1941 0.2439 0.2716 -0.0183 -0.0088 0.0607  30  VAL   B CG1 
4381 C CG2 . VAL   B 30  ? 0.1975 0.2372 0.2995 -0.0263 -0.0298 0.0556  30  VAL   B CG2 
4392 N N   A LYS   B 31  ? 0.1502 0.2009 0.2632 -0.0220 0.0240  0.0948  31  LYS   B N   
4393 N N   B LYS   B 31  ? 0.1550 0.2032 0.2592 -0.0212 0.0171  0.0873  31  LYS   B N   
4394 C CA  A LYS   B 31  ? 0.1398 0.1940 0.2864 -0.0349 0.0137  0.0919  31  LYS   B CA  
4395 C CA  B LYS   B 31  ? 0.1494 0.1980 0.2772 -0.0332 0.0017  0.0766  31  LYS   B CA  
4396 C C   A LYS   B 31  ? 0.1291 0.1606 0.2567 -0.0312 -0.0081 0.0789  31  LYS   B C   
4397 C C   B LYS   B 31  ? 0.1390 0.1653 0.2460 -0.0314 -0.0206 0.0596  31  LYS   B C   
4398 O O   A LYS   B 31  ? 0.1362 0.1638 0.2776 -0.0217 0.0004  0.1019  31  LYS   B O   
4399 O O   B LYS   B 31  ? 0.1517 0.1711 0.2543 -0.0258 -0.0240 0.0639  31  LYS   B O   
4400 C CB  A LYS   B 31  ? 0.1594 0.2293 0.3262 -0.0336 0.0300  0.1022  31  LYS   B CB  
4401 C CB  B LYS   B 31  ? 0.1709 0.2334 0.3146 -0.0309 0.0125  0.0817  31  LYS   B CB  
4402 C CG  A LYS   B 31  ? 0.1817 0.2625 0.3621 -0.0296 0.0383  0.0990  31  LYS   B CG  
4403 C CG  B LYS   B 31  ? 0.1936 0.2657 0.3466 -0.0272 0.0170  0.0733  31  LYS   B CG  
4404 C CD  A LYS   B 31  ? 0.2017 0.2933 0.3936 -0.0233 0.0328  0.0870  31  LYS   B CD  
4405 C CD  B LYS   B 31  ? 0.2112 0.2942 0.3775 -0.0242 0.0128  0.0613  31  LYS   B CD  
4406 C CE  A LYS   B 31  ? 0.2203 0.3175 0.4227 -0.0190 0.0187  0.0745  31  LYS   B CE  
4407 C CE  B LYS   B 31  ? 0.2259 0.3176 0.4062 -0.0222 0.0021  0.0511  31  LYS   B CE  
4408 N NZ  A LYS   B 31  ? 0.2312 0.3308 0.4371 -0.0149 0.0058  0.0655  31  LYS   B NZ  
4409 N NZ  B LYS   B 31  ? 0.2338 0.3286 0.4207 -0.0194 -0.0113 0.0432  31  LYS   B NZ  
4436 N N   . PRO   B 32  ? 0.1341 0.1367 0.2080 -0.0307 -0.0269 0.0466  32  PRO   B N   
4437 C CA  . PRO   B 32  ? 0.1394 0.1273 0.1617 -0.0266 -0.0259 0.0256  32  PRO   B CA  
4438 C C   . PRO   B 32  ? 0.1517 0.1187 0.1647 -0.0300 -0.0386 0.0289  32  PRO   B C   
4439 O O   . PRO   B 32  ? 0.1634 0.1229 0.1986 -0.0328 -0.0646 0.0250  32  PRO   B O   
4440 C CB  . PRO   B 32  ? 0.1583 0.1220 0.1659 -0.0260 -0.0202 0.0124  32  PRO   B CB  
4441 C CG  . PRO   B 32  ? 0.1739 0.1137 0.1751 -0.0244 -0.0371 0.0153  32  PRO   B CG  
4442 C CD  . PRO   B 32  ? 0.1619 0.1197 0.1907 -0.0203 -0.0409 0.0248  32  PRO   B CD  
4450 N N   . THR   B 33  ? 0.1536 0.1124 0.1443 -0.0210 -0.0376 0.0212  33  THR   B N   
4451 C CA  . THR   B 33  ? 0.1595 0.1159 0.1406 -0.0258 -0.0326 0.0206  33  THR   B CA  
4452 C C   . THR   B 33  ? 0.1650 0.1035 0.1420 -0.0265 -0.0378 0.0161  33  THR   B C   
4453 O O   . THR   B 33  ? 0.1871 0.1087 0.1586 -0.0349 -0.0423 0.0152  33  THR   B O   
4454 C CB  . THR   B 33  ? 0.1683 0.1251 0.1533 -0.0100 -0.0367 0.0238  33  THR   B CB  
4455 O OG1 . THR   B 33  ? 0.1601 0.1364 0.1528 -0.0143 -0.0395 0.0299  33  THR   B OG1 
4456 C CG2 . THR   B 33  ? 0.1896 0.1322 0.1775 -0.0031 -0.0377 0.0191  33  THR   B CG2 
4464 N N   . VAL   B 34  ? 0.1549 0.1053 0.1317 -0.0289 -0.0308 0.0136  34  VAL   B N   
4465 C CA  . VAL   B 34  ? 0.1408 0.1088 0.1221 -0.0224 -0.0273 0.0076  34  VAL   B CA  
4466 C C   . VAL   B 34  ? 0.1231 0.1026 0.1140 -0.0267 -0.0124 0.0086  34  VAL   B C   
4467 O O   . VAL   B 34  ? 0.1418 0.1007 0.1250 -0.0221 -0.0277 0.0031  34  VAL   B O   
4468 C CB  . VAL   B 34  ? 0.1479 0.1207 0.1464 -0.0106 -0.0290 0.0018  34  VAL   B CB  
4469 C CG1 . VAL   B 34  ? 0.1446 0.1283 0.1552 -0.0099 -0.0167 0.0007  34  VAL   B CG1 
4470 C CG2 . VAL   B 34  ? 0.1534 0.1215 0.1786 -0.0073 -0.0250 0.0038  34  VAL   B CG2 
4480 N N   . VAL   B 35  ? 0.1158 0.0996 0.1117 -0.0260 -0.0062 0.0049  35  VAL   B N   
4481 C CA  . VAL   B 35  ? 0.1097 0.0989 0.1156 -0.0200 -0.0047 0.0042  35  VAL   B CA  
4482 C C   . VAL   B 35  ? 0.1013 0.0929 0.1206 -0.0136 -0.0039 0.0012  35  VAL   B C   
4483 O O   . VAL   B 35  ? 0.1098 0.0961 0.1243 -0.0222 0.0014  -0.0051 35  VAL   B O   
4484 C CB  . VAL   B 35  ? 0.1157 0.1119 0.1168 -0.0155 0.0045  0.0080  35  VAL   B CB  
4485 C CG1 . VAL   B 35  ? 0.1092 0.1258 0.1350 -0.0199 0.0034  0.0065  35  VAL   B CG1 
4486 C CG2 . VAL   B 35  ? 0.1151 0.1170 0.1395 -0.0073 0.0029  -0.0007 35  VAL   B CG2 
4496 N N   . VAL   B 36  ? 0.1044 0.0921 0.1014 -0.0161 -0.0039 0.0038  36  VAL   B N   
4497 C CA  . VAL   B 36  ? 0.1042 0.0898 0.1079 -0.0087 0.0027  0.0017  36  VAL   B CA  
4498 C C   . VAL   B 36  ? 0.0969 0.0903 0.1039 -0.0087 -0.0034 0.0000  36  VAL   B C   
4499 O O   . VAL   B 36  ? 0.1051 0.1018 0.1270 -0.0073 0.0006  -0.0064 36  VAL   B O   
4500 C CB  . VAL   B 36  ? 0.1042 0.0972 0.1117 -0.0163 -0.0004 0.0038  36  VAL   B CB  
4501 C CG1 . VAL   B 36  ? 0.1054 0.1054 0.1276 -0.0168 -0.0013 0.0014  36  VAL   B CG1 
4502 C CG2 . VAL   B 36  ? 0.1094 0.1024 0.1200 -0.0092 -0.0060 0.0028  36  VAL   B CG2 
4512 N N   . ASN   B 37  ? 0.1058 0.1004 0.1074 0.0008  -0.0006 0.0010  37  ASN   B N   
4513 C CA  . ASN   B 37  ? 0.1069 0.1025 0.1181 0.0033  -0.0061 0.0061  37  ASN   B CA  
4514 C C   . ASN   B 37  ? 0.1042 0.0983 0.1101 0.0044  -0.0054 0.0006  37  ASN   B C   
4515 O O   . ASN   B 37  ? 0.1134 0.1096 0.1178 0.0059  0.0011  0.0065  37  ASN   B O   
4516 C CB  . ASN   B 37  ? 0.1067 0.1061 0.1132 0.0010  -0.0069 0.0073  37  ASN   B CB  
4517 C CG  . ASN   B 37  ? 0.1086 0.1023 0.1241 -0.0002 -0.0080 0.0018  37  ASN   B CG  
4518 O OD1 . ASN   B 37  ? 0.1180 0.1073 0.1430 0.0073  -0.0116 0.0024  37  ASN   B OD1 
4519 N ND2 . ASN   B 37  ? 0.1210 0.1028 0.1328 0.0014  -0.0207 0.0062  37  ASN   B ND2 
4526 N N   . ALA   B 38  ? 0.1057 0.0972 0.1119 0.0067  0.0050  0.0010  38  ALA   B N   
4527 C CA  . ALA   B 38  ? 0.1243 0.1018 0.1183 -0.0023 0.0064  0.0054  38  ALA   B CA  
4528 C C   . ALA   B 38  ? 0.1175 0.1005 0.1183 0.0030  0.0062  0.0081  38  ALA   B C   
4529 O O   . ALA   B 38  ? 0.1243 0.1086 0.1321 0.0073  0.0073  0.0080  38  ALA   B O   
4530 C CB  . ALA   B 38  ? 0.1490 0.1089 0.1362 -0.0063 0.0095  0.0001  38  ALA   B CB  
4536 N N   . ALA   B 39  ? 0.1119 0.1032 0.1164 0.0082  -0.0025 0.0031  39  ALA   B N   
4537 C CA  . ALA   B 39  ? 0.1248 0.1104 0.1163 0.0051  -0.0100 0.0058  39  ALA   B CA  
4538 C C   . ALA   B 39  ? 0.1252 0.1152 0.1071 0.0021  -0.0056 -0.0016 39  ALA   B C   
4539 O O   . ALA   B 39  ? 0.1257 0.1222 0.1303 0.0020  -0.0028 0.0104  39  ALA   B O   
4540 C CB  . ALA   B 39  ? 0.1334 0.1111 0.1316 -0.0009 0.0016  0.0009  39  ALA   B CB  
4546 N N   . ASN   B 40  ? 0.1312 0.1387 0.1141 -0.0055 0.0021  -0.0063 40  ASN   B N   
4547 C CA  . ASN   B 40  ? 0.1356 0.1457 0.1224 0.0002  -0.0034 -0.0045 40  ASN   B CA  
4548 C C   . ASN   B 40  ? 0.1393 0.1480 0.1036 0.0077  -0.0053 -0.0039 40  ASN   B C   
4549 O O   . ASN   B 40  ? 0.1367 0.1376 0.1229 0.0105  -0.0046 -0.0008 40  ASN   B O   
4550 C CB  . ASN   B 40  ? 0.1551 0.1440 0.1416 0.0101  -0.0083 -0.0004 40  ASN   B CB  
4551 C CG  . ASN   B 40  ? 0.1577 0.1488 0.1738 0.0076  -0.0203 0.0084  40  ASN   B CG  
4552 O OD1 . ASN   B 40  ? 0.1501 0.1483 0.2484 0.0080  -0.0283 0.0091  40  ASN   B OD1 
4553 N ND2 . ASN   B 40  ? 0.1622 0.1499 0.1667 0.0037  -0.0090 0.0073  40  ASN   B ND2 
4560 N N   . VAL   B 41  ? 0.1475 0.1545 0.1083 0.0120  0.0024  -0.0040 41  VAL   B N   
4561 C CA  . VAL   B 41  ? 0.1485 0.1661 0.1149 0.0135  0.0018  -0.0160 41  VAL   B CA  
4562 C C   . VAL   B 41  ? 0.1483 0.1650 0.1070 0.0185  -0.0050 -0.0163 41  VAL   B C   
4563 O O   . VAL   B 41  ? 0.1514 0.1615 0.1194 0.0117  -0.0120 -0.0184 41  VAL   B O   
4564 C CB  . VAL   B 41  ? 0.1611 0.1795 0.1410 0.0008  0.0217  -0.0231 41  VAL   B CB  
4565 C CG1 . VAL   B 41  ? 0.1575 0.1845 0.1594 -0.0009 0.0278  -0.0280 41  VAL   B CG1 
4566 C CG2 . VAL   B 41  ? 0.1743 0.1930 0.1566 -0.0026 0.0204  -0.0199 41  VAL   B CG2 
4576 N N   . TYR   B 42  ? 0.1529 0.1629 0.1191 0.0155  -0.0184 -0.0076 42  TYR   B N   
4577 C CA  . TYR   B 42  ? 0.1608 0.1679 0.1372 0.0141  -0.0252 -0.0119 42  TYR   B CA  
4578 C C   . TYR   B 42  ? 0.1455 0.1459 0.1376 0.0166  -0.0221 -0.0183 42  TYR   B C   
4579 O O   . TYR   B 42  ? 0.1495 0.1559 0.1583 0.0128  -0.0248 -0.0284 42  TYR   B O   
4580 C CB  . TYR   B 42  ? 0.1881 0.2062 0.1558 0.0109  -0.0371 -0.0017 42  TYR   B CB  
4581 C CG  . TYR   B 42  ? 0.1943 0.2249 0.1432 -0.0010 -0.0292 0.0079  42  TYR   B CG  
4582 C CD1 . TYR   B 42  ? 0.1938 0.2263 0.1138 -0.0074 -0.0139 -0.0014 42  TYR   B CD1 
4583 C CD2 . TYR   B 42  ? 0.2070 0.2387 0.1938 -0.0035 -0.0070 0.0150  42  TYR   B CD2 
4584 C CE1 . TYR   B 42  ? 0.2068 0.2401 0.1239 -0.0015 -0.0028 0.0002  42  TYR   B CE1 
4585 C CE2 . TYR   B 42  ? 0.2176 0.2514 0.1863 0.0017  0.0113  0.0286  42  TYR   B CE2 
4586 C CZ  . TYR   B 42  ? 0.2273 0.2622 0.1671 0.0161  0.0204  0.0152  42  TYR   B CZ  
4587 O OH  . TYR   B 42  ? 0.2593 0.2842 0.2076 0.0370  0.0323  0.0241  42  TYR   B OH  
4597 N N   . LEU   B 43  ? 0.1357 0.1325 0.1287 0.0092  -0.0139 -0.0158 43  LEU   B N   
4598 C CA  . LEU   B 43  ? 0.1375 0.1283 0.1201 0.0082  -0.0115 -0.0035 43  LEU   B CA  
4599 C C   . LEU   B 43  ? 0.1419 0.1354 0.1275 0.0065  -0.0150 -0.0016 43  LEU   B C   
4600 O O   . LEU   B 43  ? 0.1348 0.1380 0.1609 0.0086  -0.0200 0.0058  43  LEU   B O   
4601 C CB  . LEU   B 43  ? 0.1402 0.1230 0.1316 0.0028  -0.0205 -0.0062 43  LEU   B CB  
4602 C CG  . LEU   B 43  ? 0.1388 0.1221 0.1351 0.0033  -0.0220 -0.0099 43  LEU   B CG  
4603 C CD1 . LEU   B 43  ? 0.1442 0.1277 0.1714 0.0040  -0.0339 -0.0075 43  LEU   B CD1 
4604 C CD2 . LEU   B 43  ? 0.1421 0.1240 0.1444 -0.0048 -0.0181 -0.0105 43  LEU   B CD2 
4616 N N   . LYS   B 44  ? 0.1403 0.1306 0.1194 0.0128  -0.0079 -0.0062 44  LYS   B N   
4617 C CA  . LYS   B 44  ? 0.1457 0.1395 0.1222 0.0096  -0.0137 0.0086  44  LYS   B CA  
4618 C C   . LYS   B 44  ? 0.1359 0.1368 0.1338 0.0126  -0.0068 -0.0011 44  LYS   B C   
4619 O O   . LYS   B 44  ? 0.1574 0.1380 0.1556 0.0027  -0.0012 0.0008  44  LYS   B O   
4620 C CB  . LYS   B 44  ? 0.1754 0.1617 0.1467 0.0174  -0.0190 0.0052  44  LYS   B CB  
4621 C CG  . LYS   B 44  ? 0.2128 0.1933 0.1832 0.0153  -0.0446 0.0031  44  LYS   B CG  
4622 C CD  . LYS   B 44  ? 0.2439 0.2155 0.2445 0.0065  -0.0475 -0.0013 44  LYS   B CD  
4623 C CE  . LYS   B 44  ? 0.2711 0.2411 0.2913 0.0042  -0.0534 0.0068  44  LYS   B CE  
4624 N NZ  . LYS   B 44  ? 0.2808 0.2501 0.3187 0.0059  -0.0602 0.0195  44  LYS   B NZ  
4638 N N   . HIS   B 45  ? 0.1348 0.1362 0.1278 0.0097  -0.0068 0.0048  45  HIS   B N   
4639 C CA  . HIS   B 45  ? 0.1382 0.1322 0.1324 0.0114  -0.0063 -0.0060 45  HIS   B CA  
4640 C C   . HIS   B 45  ? 0.1656 0.1487 0.1691 0.0202  -0.0169 -0.0095 45  HIS   B C   
4641 O O   . HIS   B 45  ? 0.1719 0.1760 0.2149 0.0457  0.0096  -0.0048 45  HIS   B O   
4642 C CB  . HIS   B 45  ? 0.1313 0.1328 0.1347 -0.0003 -0.0097 -0.0041 45  HIS   B CB  
4643 C CG  . HIS   B 45  ? 0.1316 0.1299 0.1260 -0.0033 -0.0095 0.0014  45  HIS   B CG  
4644 N ND1 . HIS   B 45  ? 0.1400 0.1257 0.1343 0.0029  -0.0124 -0.0065 45  HIS   B ND1 
4645 C CD2 . HIS   B 45  ? 0.1379 0.1303 0.1519 -0.0094 -0.0116 -0.0031 45  HIS   B CD2 
4646 C CE1 . HIS   B 45  ? 0.1431 0.1198 0.1190 0.0012  -0.0186 -0.0078 45  HIS   B CE1 
4647 N NE2 . HIS   B 45  ? 0.1440 0.1247 0.1334 -0.0036 -0.0206 -0.0056 45  HIS   B NE2 
4655 N N   A GLY   B 46  ? 0.1764 0.1435 0.1906 0.0226  -0.0296 -0.0025 46  GLY   B N   
4656 N N   B GLY   B 46  ? 0.1782 0.1493 0.1814 0.0201  -0.0244 0.0013  46  GLY   B N   
4657 C CA  A GLY   B 46  ? 0.1830 0.1520 0.2299 0.0249  -0.0381 0.0012  46  GLY   B CA  
4658 C CA  B GLY   B 46  ? 0.1873 0.1621 0.2129 0.0194  -0.0306 0.0085  46  GLY   B CA  
4659 C C   A GLY   B 46  ? 0.1794 0.1637 0.2605 0.0332  -0.0379 -0.0016 46  GLY   B C   
4660 C C   B GLY   B 46  ? 0.1878 0.1773 0.2397 0.0234  -0.0292 0.0129  46  GLY   B C   
4661 O O   A GLY   B 46  ? 0.1849 0.1774 0.3284 0.0408  -0.0301 -0.0199 46  GLY   B O   
4662 O O   B GLY   B 46  ? 0.2009 0.1995 0.2664 0.0221  -0.0211 0.0268  46  GLY   B O   
4669 N N   . GLY   B 47  ? 0.1779 0.1735 0.2296 0.0178  -0.0185 -0.0015 47  GLY   B N   
4670 C CA  . GLY   B 47  ? 0.1628 0.1525 0.1946 0.0104  -0.0128 -0.0035 47  GLY   B CA  
4671 C C   . GLY   B 47  ? 0.1429 0.1332 0.1648 0.0066  0.0015  0.0054  47  GLY   B C   
4672 O O   . GLY   B 47  ? 0.1539 0.1270 0.1680 0.0072  -0.0002 0.0147  47  GLY   B O   
4677 N N   . GLY   B 48  ? 0.1283 0.1239 0.1629 0.0034  -0.0077 0.0161  48  GLY   B N   
4678 C CA  . GLY   B 48  ? 0.1297 0.1215 0.1694 -0.0022 -0.0060 0.0101  48  GLY   B CA  
4679 C C   . GLY   B 48  ? 0.1251 0.1191 0.1587 0.0023  0.0063  0.0013  48  GLY   B C   
4680 O O   . GLY   B 48  ? 0.1277 0.1198 0.1710 0.0048  -0.0076 0.0078  48  GLY   B O   
4684 N N   . VAL   B 49  ? 0.1270 0.1245 0.1426 0.0103  0.0025  0.0088  49  VAL   B N   
4685 C CA  . VAL   B 49  ? 0.1276 0.1325 0.1344 0.0104  -0.0113 -0.0012 49  VAL   B CA  
4686 C C   . VAL   B 49  ? 0.1200 0.1224 0.1213 0.0133  -0.0032 0.0059  49  VAL   B C   
4687 O O   . VAL   B 49  ? 0.1270 0.1281 0.1369 0.0077  0.0001  0.0085  49  VAL   B O   
4688 C CB  . VAL   B 49  ? 0.1302 0.1550 0.1642 0.0056  -0.0221 -0.0020 49  VAL   B CB  
4689 C CG1 . VAL   B 49  ? 0.1334 0.1649 0.1577 0.0061  -0.0228 -0.0031 49  VAL   B CG1 
4690 C CG2 . VAL   B 49  ? 0.1481 0.1684 0.1941 -0.0029 -0.0372 -0.0066 49  VAL   B CG2 
4700 N N   . ALA   B 50  ? 0.1128 0.1164 0.1285 0.0023  -0.0022 0.0027  50  ALA   B N   
4701 C CA  . ALA   B 50  ? 0.1172 0.1156 0.1235 0.0072  -0.0056 0.0080  50  ALA   B CA  
4702 C C   . ALA   B 50  ? 0.1233 0.1124 0.1275 0.0057  -0.0031 0.0046  50  ALA   B C   
4703 O O   . ALA   B 50  ? 0.1242 0.1137 0.1304 0.0071  -0.0025 0.0043  50  ALA   B O   
4704 C CB  . ALA   B 50  ? 0.1161 0.1176 0.1292 0.0037  0.0044  0.0101  50  ALA   B CB  
4710 N N   . GLY   B 51  ? 0.1230 0.1198 0.1382 0.0097  -0.0071 0.0108  51  GLY   B N   
4711 C CA  . GLY   B 51  ? 0.1149 0.1265 0.1602 0.0166  -0.0135 0.0165  51  GLY   B CA  
4712 C C   . GLY   B 51  ? 0.1165 0.1242 0.1596 0.0199  -0.0056 0.0093  51  GLY   B C   
4713 O O   . GLY   B 51  ? 0.1234 0.1364 0.1718 0.0119  -0.0080 0.0044  51  GLY   B O   
4717 N N   . ALA   B 52  ? 0.1185 0.1156 0.1624 0.0152  0.0034  0.0177  52  ALA   B N   
4718 C CA  . ALA   B 52  ? 0.1230 0.1261 0.1626 0.0206  0.0053  0.0075  52  ALA   B CA  
4719 C C   . ALA   B 52  ? 0.1163 0.1287 0.1419 0.0112  0.0080  0.0054  52  ALA   B C   
4720 O O   . ALA   B 52  ? 0.1191 0.1313 0.1573 0.0119  0.0090  0.0032  52  ALA   B O   
4721 C CB  . ALA   B 52  ? 0.1431 0.1314 0.1669 0.0084  0.0134  0.0050  52  ALA   B CB  
4727 N N   . LEU   B 53  ? 0.1108 0.1227 0.1354 0.0164  0.0054  0.0127  53  LEU   B N   
4728 C CA  . LEU   B 53  ? 0.1127 0.1344 0.1370 0.0132  -0.0008 0.0119  53  LEU   B CA  
4729 C C   . LEU   B 53  ? 0.1183 0.1259 0.1338 0.0136  0.0086  0.0104  53  LEU   B C   
4730 O O   . LEU   B 53  ? 0.1258 0.1334 0.1404 0.0028  0.0085  0.0176  53  LEU   B O   
4731 C CB  . LEU   B 53  ? 0.1124 0.1410 0.1455 0.0127  -0.0011 0.0173  53  LEU   B CB  
4732 C CG  . LEU   B 53  ? 0.1124 0.1516 0.1511 0.0069  -0.0007 0.0262  53  LEU   B CG  
4733 C CD1 . LEU   B 53  ? 0.1181 0.1738 0.1776 0.0133  -0.0013 0.0047  53  LEU   B CD1 
4734 C CD2 . LEU   B 53  ? 0.1274 0.1799 0.1746 -0.0089 -0.0041 -0.0067 53  LEU   B CD2 
4746 N N   . ASN   B 54  ? 0.1167 0.1151 0.1373 0.0057  0.0025  0.0088  54  ASN   B N   
4747 C CA  . ASN   B 54  ? 0.1245 0.1247 0.1449 0.0045  0.0036  0.0090  54  ASN   B CA  
4748 C C   . ASN   B 54  ? 0.1201 0.1248 0.1541 0.0035  0.0021  0.0089  54  ASN   B C   
4749 O O   . ASN   B 54  ? 0.1209 0.1314 0.1597 0.0001  0.0005  0.0082  54  ASN   B O   
4750 C CB  . ASN   B 54  ? 0.1245 0.1359 0.1569 0.0062  0.0024  0.0141  54  ASN   B CB  
4751 C CG  . ASN   B 54  ? 0.1166 0.1436 0.1520 0.0073  -0.0013 0.0026  54  ASN   B CG  
4752 O OD1 . ASN   B 54  ? 0.1206 0.1460 0.1631 0.0052  -0.0102 -0.0095 54  ASN   B OD1 
4753 N ND2 . ASN   B 54  ? 0.1324 0.1675 0.1814 -0.0005 -0.0313 0.0166  54  ASN   B ND2 
4760 N N   . LYS   B 55  ? 0.1147 0.1336 0.1662 0.0105  -0.0008 0.0097  55  LYS   B N   
4761 C CA  . LYS   B 55  ? 0.1207 0.1512 0.1869 0.0184  -0.0034 0.0104  55  LYS   B CA  
4762 C C   . LYS   B 55  ? 0.1146 0.1504 0.1814 0.0157  0.0045  0.0040  55  LYS   B C   
4763 O O   . LYS   B 55  ? 0.1106 0.1636 0.1963 0.0127  0.0063  -0.0026 55  LYS   B O   
4764 C CB  . LYS   B 55  ? 0.1338 0.1559 0.2154 0.0315  0.0029  0.0181  55  LYS   B CB  
4765 C CG  . LYS   B 55  ? 0.1779 0.1807 0.2978 0.0393  0.0180  0.0316  55  LYS   B CG  
4766 C CD  . LYS   B 55  ? 0.2178 0.2058 0.3620 0.0484  0.0411  0.0403  55  LYS   B CD  
4767 C CE  . LYS   B 55  ? 0.2424 0.2318 0.4288 0.0531  0.0553  0.0423  55  LYS   B CE  
4768 N NZ  . LYS   B 55  ? 0.2479 0.2506 0.4590 0.0540  0.0471  0.0459  55  LYS   B NZ  
4782 N N   . ALA   B 56  ? 0.1170 0.1534 0.1653 0.0142  0.0092  -0.0019 56  ALA   B N   
4783 C CA  . ALA   B 56  ? 0.1338 0.1665 0.1601 0.0052  0.0085  0.0032  56  ALA   B CA  
4784 C C   . ALA   B 56  ? 0.1297 0.1615 0.1607 0.0063  0.0133  0.0111  56  ALA   B C   
4785 O O   . ALA   B 56  ? 0.1408 0.1713 0.1795 0.0091  0.0293  0.0111  56  ALA   B O   
4786 C CB  . ALA   B 56  ? 0.1464 0.1868 0.1743 -0.0033 0.0157  -0.0023 56  ALA   B CB  
4792 N N   . THR   B 57  ? 0.1281 0.1531 0.1659 0.0061  0.0140  0.0148  57  THR   B N   
4793 C CA  . THR   B 57  ? 0.1320 0.1495 0.1656 0.0083  0.0186  0.0227  57  THR   B CA  
4794 C C   . THR   B 57  ? 0.1305 0.1575 0.1793 0.0043  0.0254  0.0223  57  THR   B C   
4795 O O   . THR   B 57  ? 0.1364 0.1561 0.1982 -0.0081 0.0263  0.0249  57  THR   B O   
4796 C CB  . THR   B 57  ? 0.1320 0.1391 0.1547 0.0019  0.0161  0.0220  57  THR   B CB  
4797 O OG1 . THR   B 57  ? 0.1292 0.1356 0.1613 0.0002  0.0176  0.0097  57  THR   B OG1 
4798 C CG2 . THR   B 57  ? 0.1309 0.1466 0.1533 0.0015  0.0167  0.0222  57  THR   B CG2 
4806 N N   . ASN   B 58  ? 0.1166 0.1790 0.2079 -0.0094 0.0108  0.0086  58  ASN   B N   
4807 C CA  . ASN   B 58  ? 0.1375 0.2259 0.2471 -0.0204 0.0316  0.0184  58  ASN   B CA  
4808 C C   . ASN   B 58  ? 0.1164 0.2014 0.2071 -0.0114 0.0039  0.0134  58  ASN   B C   
4809 O O   . ASN   B 58  ? 0.1264 0.2091 0.2148 -0.0175 0.0036  0.0100  58  ASN   B O   
4810 C CB  . ASN   B 58  ? 0.2496 0.3175 0.3809 -0.0312 0.0516  0.0377  58  ASN   B CB  
4811 C CG  . ASN   B 58  ? 0.3755 0.4080 0.5232 -0.0336 0.0656  0.0542  58  ASN   B CG  
4812 O OD1 . ASN   B 58  ? 0.4176 0.4352 0.5725 -0.0345 0.0707  0.0596  58  ASN   B OD1 
4813 N ND2 . ASN   B 58  ? 0.4155 0.4342 0.5737 -0.0345 0.0706  0.0560  58  ASN   B ND2 
4820 N N   . ASN   B 59  ? 0.1129 0.1823 0.1913 -0.0058 -0.0048 0.0209  59  ASN   B N   
4821 C CA  . ASN   B 59  ? 0.1177 0.1849 0.1845 -0.0089 -0.0120 0.0248  59  ASN   B CA  
4822 C C   . ASN   B 59  ? 0.1125 0.1732 0.1770 -0.0148 -0.0085 0.0182  59  ASN   B C   
4823 O O   . ASN   B 59  ? 0.1164 0.1758 0.1731 -0.0116 -0.0113 0.0100  59  ASN   B O   
4824 C CB  . ASN   B 59  ? 0.1335 0.2024 0.1933 -0.0058 -0.0240 0.0238  59  ASN   B CB  
4825 C CG  . ASN   B 59  ? 0.1432 0.2225 0.2082 -0.0009 -0.0366 0.0161  59  ASN   B CG  
4826 O OD1 . ASN   B 59  ? 0.1487 0.2265 0.2085 0.0030  -0.0272 0.0262  59  ASN   B OD1 
4827 N ND2 . ASN   B 59  ? 0.1489 0.2329 0.2160 -0.0112 -0.0312 0.0122  59  ASN   B ND2 
4834 N N   . ALA   B 60  ? 0.1215 0.1609 0.1839 -0.0102 -0.0026 0.0122  60  ALA   B N   
4835 C CA  . ALA   B 60  ? 0.1309 0.1481 0.1794 -0.0143 -0.0042 0.0132  60  ALA   B CA  
4836 C C   . ALA   B 60  ? 0.1275 0.1344 0.1595 -0.0083 -0.0092 0.0119  60  ALA   B C   
4837 O O   . ALA   B 60  ? 0.1324 0.1381 0.1734 -0.0118 -0.0059 -0.0009 60  ALA   B O   
4838 C CB  . ALA   B 60  ? 0.1436 0.1504 0.1963 -0.0127 0.0056  0.0102  60  ALA   B CB  
4844 N N   . MET   B 61  ? 0.1169 0.1287 0.1681 -0.0087 -0.0036 0.0059  61  MET   B N   
4845 C CA  . MET   B 61  ? 0.1169 0.1244 0.1604 -0.0062 -0.0103 0.0031  61  MET   B CA  
4846 C C   . MET   B 61  ? 0.1194 0.1234 0.1572 -0.0065 -0.0108 0.0045  61  MET   B C   
4847 O O   . MET   B 61  ? 0.1281 0.1274 0.1474 0.0001  -0.0078 -0.0078 61  MET   B O   
4848 C CB  . MET   B 61  ? 0.1176 0.1317 0.1443 -0.0026 -0.0119 0.0052  61  MET   B CB  
4849 C CG  . MET   B 61  ? 0.1208 0.1351 0.1360 0.0020  -0.0071 0.0018  61  MET   B CG  
4850 S SD  . MET   B 61  ? 0.1171 0.1296 0.1693 -0.0021 -0.0021 -0.0051 61  MET   B SD  
4851 C CE  . MET   B 61  ? 0.1274 0.1501 0.1950 0.0026  -0.0010 -0.0173 61  MET   B CE  
4861 N N   . GLN   B 62  ? 0.1218 0.1275 0.1487 -0.0019 -0.0119 0.0095  62  GLN   B N   
4862 C CA  . GLN   B 62  ? 0.1270 0.1307 0.1568 -0.0004 -0.0172 -0.0006 62  GLN   B CA  
4863 C C   . GLN   B 62  ? 0.1268 0.1378 0.1648 -0.0038 -0.0246 -0.0029 62  GLN   B C   
4864 O O   . GLN   B 62  ? 0.1386 0.1388 0.1642 -0.0060 -0.0301 -0.0139 62  GLN   B O   
4865 C CB  . GLN   B 62  ? 0.1323 0.1392 0.1558 0.0006  -0.0195 0.0068  62  GLN   B CB  
4866 C CG  . GLN   B 62  ? 0.1305 0.1488 0.1547 0.0028  -0.0228 0.0020  62  GLN   B CG  
4867 C CD  . GLN   B 62  ? 0.1272 0.1428 0.1450 0.0031  -0.0277 0.0071  62  GLN   B CD  
4868 O OE1 . GLN   B 62  ? 0.1332 0.1408 0.1599 0.0000  -0.0219 -0.0050 62  GLN   B OE1 
4869 N NE2 . GLN   B 62  ? 0.1274 0.1501 0.1593 0.0038  -0.0223 -0.0031 62  GLN   B NE2 
4878 N N   . VAL   B 63  ? 0.1251 0.1427 0.1776 -0.0084 -0.0225 -0.0071 63  VAL   B N   
4879 C CA  . VAL   B 63  ? 0.1314 0.1479 0.1933 -0.0148 -0.0312 -0.0077 63  VAL   B CA  
4880 C C   . VAL   B 63  ? 0.1377 0.1362 0.1794 -0.0158 -0.0345 -0.0160 63  VAL   B C   
4881 O O   . VAL   B 63  ? 0.1512 0.1398 0.1955 -0.0097 -0.0442 -0.0159 63  VAL   B O   
4882 C CB  . VAL   B 63  ? 0.1410 0.1671 0.2211 -0.0180 -0.0330 -0.0084 63  VAL   B CB  
4883 C CG1 . VAL   B 63  ? 0.1487 0.1744 0.2340 -0.0257 -0.0266 -0.0020 63  VAL   B CG1 
4884 C CG2 . VAL   B 63  ? 0.1401 0.1799 0.2345 -0.0065 -0.0309 -0.0100 63  VAL   B CG2 
4894 N N   . GLU   B 64  ? 0.1326 0.1310 0.1805 -0.0070 -0.0237 -0.0114 64  GLU   B N   
4895 C CA  . GLU   B 64  ? 0.1372 0.1223 0.1684 -0.0099 -0.0230 -0.0069 64  GLU   B CA  
4896 C C   . GLU   B 64  ? 0.1306 0.1203 0.1562 -0.0055 -0.0231 -0.0133 64  GLU   B C   
4897 O O   . GLU   B 64  ? 0.1438 0.1296 0.1676 -0.0059 -0.0196 -0.0194 64  GLU   B O   
4898 C CB  . GLU   B 64  ? 0.1394 0.1257 0.1637 -0.0153 -0.0198 -0.0046 64  GLU   B CB  
4899 C CG  . GLU   B 64  ? 0.1453 0.1324 0.1692 -0.0220 -0.0247 -0.0156 64  GLU   B CG  
4900 C CD  . GLU   B 64  ? 0.1489 0.1471 0.1737 -0.0284 -0.0260 -0.0108 64  GLU   B CD  
4901 O OE1 . GLU   B 64  ? 0.1485 0.1624 0.1921 -0.0259 -0.0222 -0.0280 64  GLU   B OE1 
4902 O OE2 . GLU   B 64  ? 0.1633 0.1631 0.1821 -0.0285 -0.0456 -0.0108 64  GLU   B OE2 
4909 N N   . SER   B 65  ? 0.1308 0.1172 0.1595 -0.0055 -0.0133 -0.0147 65  SER   B N   
4910 C CA  . SER   B 65  ? 0.1318 0.1205 0.1620 -0.0008 -0.0184 -0.0193 65  SER   B CA  
4911 C C   . SER   B 65  ? 0.1344 0.1276 0.1571 -0.0006 -0.0220 -0.0200 65  SER   B C   
4912 O O   . SER   B 65  ? 0.1357 0.1349 0.1603 -0.0024 -0.0182 -0.0213 65  SER   B O   
4913 C CB  . SER   B 65  ? 0.1323 0.1265 0.1536 -0.0068 -0.0177 -0.0133 65  SER   B CB  
4914 O OG  . SER   B 65  ? 0.1330 0.1263 0.1609 -0.0053 -0.0185 -0.0191 65  SER   B OG  
4920 N N   . ASP   B 66  ? 0.1400 0.1359 0.1541 0.0012  -0.0235 -0.0245 66  ASP   B N   
4921 C CA  . ASP   B 66  ? 0.1492 0.1446 0.1553 0.0080  -0.0305 -0.0148 66  ASP   B CA  
4922 C C   . ASP   B 66  ? 0.1569 0.1458 0.1520 0.0019  -0.0271 -0.0214 66  ASP   B C   
4923 O O   . ASP   B 66  ? 0.1596 0.1433 0.1621 0.0045  -0.0326 -0.0256 66  ASP   B O   
4924 C CB  . ASP   B 66  ? 0.1628 0.1589 0.1768 0.0158  -0.0438 -0.0202 66  ASP   B CB  
4925 C CG  . ASP   B 66  ? 0.1929 0.1813 0.1997 0.0227  -0.0585 -0.0038 66  ASP   B CG  
4926 O OD1 . ASP   B 66  ? 0.2209 0.1752 0.2022 0.0140  -0.0560 0.0022  66  ASP   B OD1 
4927 O OD2 . ASP   B 66  ? 0.2081 0.2043 0.2623 0.0388  -0.0529 -0.0081 66  ASP   B OD2 
4932 N N   . ASP   B 67  ? 0.1527 0.1390 0.1535 -0.0046 -0.0245 -0.0176 67  ASP   B N   
4933 C CA  . ASP   B 67  ? 0.1652 0.1355 0.1571 -0.0099 -0.0248 -0.0116 67  ASP   B CA  
4934 C C   . ASP   B 67  ? 0.1589 0.1330 0.1651 -0.0030 -0.0203 -0.0202 67  ASP   B C   
4935 O O   . ASP   B 67  ? 0.1633 0.1434 0.1758 -0.0028 -0.0137 -0.0292 67  ASP   B O   
4936 C CB  . ASP   B 67  ? 0.1924 0.1455 0.1803 -0.0181 -0.0377 -0.0063 67  ASP   B CB  
4937 C CG  . ASP   B 67  ? 0.2280 0.1557 0.1866 -0.0101 -0.0668 -0.0128 67  ASP   B CG  
4938 O OD1 . ASP   B 67  ? 0.2465 0.1622 0.1959 -0.0108 -0.0731 -0.0061 67  ASP   B OD1 
4939 O OD2 . ASP   B 67  ? 0.2452 0.1633 0.2062 -0.0018 -0.0697 -0.0154 67  ASP   B OD2 
4944 N N   . TYR   B 68  ? 0.1520 0.1314 0.1553 0.0027  -0.0308 -0.0260 68  TYR   B N   
4945 C CA  . TYR   B 68  ? 0.1523 0.1515 0.1697 0.0076  -0.0355 -0.0355 68  TYR   B CA  
4946 C C   . TYR   B 68  ? 0.1466 0.1524 0.1550 0.0032  -0.0355 -0.0445 68  TYR   B C   
4947 O O   . TYR   B 68  ? 0.1521 0.1598 0.1590 0.0040  -0.0329 -0.0558 68  TYR   B O   
4948 C CB  . TYR   B 68  ? 0.1577 0.1729 0.1675 0.0106  -0.0447 -0.0475 68  TYR   B CB  
4949 C CG  . TYR   B 68  ? 0.1714 0.1893 0.1877 0.0152  -0.0385 -0.0723 68  TYR   B CG  
4950 C CD1 . TYR   B 68  ? 0.1753 0.1903 0.2225 -0.0051 -0.0392 -0.0799 68  TYR   B CD1 
4951 C CD2 . TYR   B 68  ? 0.1755 0.2111 0.2110 0.0232  -0.0488 -0.0656 68  TYR   B CD2 
4952 C CE1 . TYR   B 68  ? 0.1804 0.2070 0.2445 -0.0016 -0.0415 -0.0740 68  TYR   B CE1 
4953 C CE2 . TYR   B 68  ? 0.1765 0.2187 0.2189 0.0204  -0.0417 -0.0747 68  TYR   B CE2 
4954 C CZ  . TYR   B 68  ? 0.1719 0.2165 0.2300 0.0075  -0.0430 -0.0816 68  TYR   B CZ  
4955 O OH  . TYR   B 68  ? 0.1671 0.2409 0.2516 0.0038  -0.0381 -0.0648 68  TYR   B OH  
4965 N N   . ILE   B 69  ? 0.1434 0.1388 0.1642 0.0054  -0.0294 -0.0362 69  ILE   B N   
4966 C CA  . ILE   B 69  ? 0.1504 0.1445 0.1737 -0.0018 -0.0253 -0.0367 69  ILE   B CA  
4967 C C   . ILE   B 69  ? 0.1515 0.1469 0.1642 0.0087  -0.0374 -0.0325 69  ILE   B C   
4968 O O   . ILE   B 69  ? 0.1543 0.1595 0.1704 0.0078  -0.0218 -0.0396 69  ILE   B O   
4969 C CB  . ILE   B 69  ? 0.1547 0.1477 0.1978 -0.0034 0.0039  -0.0332 69  ILE   B CB  
4970 C CG1 . ILE   B 69  ? 0.1602 0.1497 0.2020 -0.0037 0.0126  -0.0373 69  ILE   B CG1 
4971 C CG2 . ILE   B 69  ? 0.1698 0.1569 0.2191 -0.0070 0.0044  -0.0215 69  ILE   B CG2 
4972 C CD1 . ILE   B 69  ? 0.1612 0.1572 0.2045 -0.0127 0.0084  -0.0402 69  ILE   B CD1 
4984 N N   . ALA   B 70  ? 0.1491 0.1425 0.1678 0.0084  -0.0420 -0.0240 70  ALA   B N   
4985 C CA  . ALA   B 70  ? 0.1546 0.1456 0.1564 0.0031  -0.0412 -0.0247 70  ALA   B CA  
4986 C C   . ALA   B 70  ? 0.1564 0.1408 0.1594 -0.0022 -0.0446 -0.0330 70  ALA   B C   
4987 O O   . ALA   B 70  ? 0.1621 0.1453 0.1685 0.0003  -0.0345 -0.0376 70  ALA   B O   
4988 C CB  . ALA   B 70  ? 0.1563 0.1627 0.1677 -0.0030 -0.0411 -0.0246 70  ALA   B CB  
4994 N N   . THR   B 71  ? 0.1611 0.1409 0.1687 0.0051  -0.0492 -0.0351 71  THR   B N   
4995 C CA  . THR   B 71  ? 0.1741 0.1469 0.1844 0.0106  -0.0616 -0.0393 71  THR   B CA  
4996 C C   . THR   B 71  ? 0.1642 0.1529 0.2047 0.0291  -0.0624 -0.0546 71  THR   B C   
4997 O O   . THR   B 71  ? 0.1743 0.1649 0.2414 0.0286  -0.0566 -0.0741 71  THR   B O   
4998 C CB  . THR   B 71  ? 0.2011 0.1710 0.2143 -0.0025 -0.0760 -0.0128 71  THR   B CB  
4999 O OG1 . THR   B 71  ? 0.2143 0.1993 0.2530 -0.0194 -0.0717 0.0127  71  THR   B OG1 
5000 C CG2 . THR   B 71  ? 0.2211 0.1691 0.2383 0.0010  -0.0673 0.0011  71  THR   B CG2 
5008 N N   . ASN   B 72  ? 0.1524 0.1595 0.2036 0.0219  -0.0593 -0.0724 72  ASN   B N   
5009 C CA  . ASN   B 72  ? 0.1613 0.1770 0.2044 0.0216  -0.0509 -0.0823 72  ASN   B CA  
5010 C C   . ASN   B 72  ? 0.1633 0.1915 0.2039 0.0040  -0.0245 -0.0777 72  ASN   B C   
5011 O O   . ASN   B 72  ? 0.1661 0.2080 0.2241 0.0064  -0.0090 -0.0774 72  ASN   B O   
5012 C CB  . ASN   B 72  ? 0.1690 0.1969 0.2148 0.0220  -0.0585 -0.0721 72  ASN   B CB  
5013 C CG  . ASN   B 72  ? 0.1785 0.2075 0.2314 0.0320  -0.0623 -0.0469 72  ASN   B CG  
5014 O OD1 . ASN   B 72  ? 0.1960 0.2236 0.2437 0.0219  -0.0484 -0.0415 72  ASN   B OD1 
5015 N ND2 . ASN   B 72  ? 0.1931 0.2118 0.2669 0.0427  -0.0489 -0.0114 72  ASN   B ND2 
5022 N N   . GLY   B 73  ? 0.1641 0.1912 0.1801 -0.0007 -0.0264 -0.0703 73  GLY   B N   
5023 C CA  . GLY   B 73  ? 0.1581 0.1972 0.1663 -0.0042 -0.0256 -0.0562 73  GLY   B CA  
5024 C C   . GLY   B 73  ? 0.1537 0.1925 0.1339 0.0068  -0.0181 -0.0581 73  GLY   B C   
5025 O O   . GLY   B 73  ? 0.1484 0.1780 0.1459 0.0078  -0.0182 -0.0454 73  GLY   B O   
5029 N N   . PRO   B 74  ? 0.1565 0.2002 0.1319 0.0049  -0.0264 -0.0469 74  PRO   B N   
5030 C CA  . PRO   B 74  ? 0.1533 0.1981 0.1173 0.0098  -0.0230 -0.0350 74  PRO   B CA  
5031 C C   . PRO   B 74  ? 0.1405 0.1762 0.1203 0.0113  -0.0241 -0.0317 74  PRO   B C   
5032 O O   . PRO   B 74  ? 0.1416 0.1778 0.1648 0.0114  -0.0111 -0.0386 74  PRO   B O   
5033 C CB  . PRO   B 74  ? 0.1676 0.2161 0.1261 0.0061  -0.0185 -0.0244 74  PRO   B CB  
5034 C CG  . PRO   B 74  ? 0.1818 0.2238 0.1553 0.0049  -0.0146 -0.0196 74  PRO   B CG  
5035 C CD  . PRO   B 74  ? 0.1802 0.2158 0.1506 0.0057  -0.0162 -0.0376 74  PRO   B CD  
5043 N N   . LEU   B 75  ? 0.1337 0.1660 0.1151 0.0102  -0.0202 -0.0256 75  LEU   B N   
5044 C CA  . LEU   B 75  ? 0.1347 0.1684 0.1138 0.0025  -0.0156 -0.0097 75  LEU   B CA  
5045 C C   . LEU   B 75  ? 0.1410 0.1781 0.1146 0.0041  -0.0076 -0.0130 75  LEU   B C   
5046 O O   . LEU   B 75  ? 0.1595 0.1915 0.1191 0.0026  -0.0034 -0.0079 75  LEU   B O   
5047 C CB  . LEU   B 75  ? 0.1465 0.1722 0.1108 -0.0058 -0.0216 0.0053  75  LEU   B CB  
5048 C CG  . LEU   B 75  ? 0.1806 0.1802 0.1287 -0.0276 -0.0056 -0.0045 75  LEU   B CG  
5049 C CD1 . LEU   B 75  ? 0.2186 0.1935 0.1391 -0.0363 0.0137  -0.0138 75  LEU   B CD1 
5050 C CD2 . LEU   B 75  ? 0.2164 0.1992 0.2069 -0.0157 0.0042  0.0019  75  LEU   B CD2 
5062 N N   . LYS   B 76  ? 0.1379 0.1950 0.1421 0.0012  -0.0044 -0.0090 76  LYS   B N   
5063 C CA  . LYS   B 76  ? 0.1487 0.2003 0.1732 -0.0069 0.0195  -0.0097 76  LYS   B CA  
5064 C C   . LYS   B 76  ? 0.1381 0.1810 0.1423 -0.0003 0.0086  0.0089  76  LYS   B C   
5065 O O   . LYS   B 76  ? 0.1424 0.1666 0.1357 0.0006  0.0012  0.0071  76  LYS   B O   
5066 C CB  . LYS   B 76  ? 0.1695 0.2108 0.2486 -0.0069 0.0428  -0.0477 76  LYS   B CB  
5067 C CG  . LYS   B 76  ? 0.1804 0.2255 0.3057 0.0031  0.0323  -0.0623 76  LYS   B CG  
5068 C CD  . LYS   B 76  ? 0.1771 0.2356 0.3617 0.0099  0.0117  -0.0752 76  LYS   B CD  
5069 C CE  . LYS   B 76  ? 0.1769 0.2548 0.4170 0.0137  -0.0039 -0.0800 76  LYS   B CE  
5070 N NZ  . LYS   B 76  ? 0.1776 0.2652 0.4372 0.0107  -0.0231 -0.0993 76  LYS   B NZ  
5084 N N   . VAL   B 77  ? 0.1503 0.1905 0.1321 0.0147  0.0120  0.0112  77  VAL   B N   
5085 C CA  . VAL   B 77  ? 0.1474 0.1779 0.1443 0.0198  0.0236  0.0329  77  VAL   B CA  
5086 C C   . VAL   B 77  ? 0.1357 0.1593 0.1389 0.0228  0.0109  0.0296  77  VAL   B C   
5087 O O   . VAL   B 77  ? 0.1389 0.1621 0.1414 0.0270  0.0212  0.0212  77  VAL   B O   
5088 C CB  . VAL   B 77  ? 0.1538 0.1851 0.1678 0.0233  0.0276  0.0441  77  VAL   B CB  
5089 C CG1 . VAL   B 77  ? 0.1610 0.1750 0.2023 0.0124  0.0281  0.0601  77  VAL   B CG1 
5090 C CG2 . VAL   B 77  ? 0.1708 0.2043 0.1881 0.0242  0.0057  0.0459  77  VAL   B CG2 
5100 N N   . GLY   B 78  ? 0.1360 0.1516 0.1250 0.0171  0.0108  0.0183  78  GLY   B N   
5101 C CA  . GLY   B 78  ? 0.1302 0.1455 0.1351 0.0119  0.0169  0.0103  78  GLY   B CA  
5102 C C   . GLY   B 78  ? 0.1232 0.1389 0.1209 0.0115  0.0146  0.0050  78  GLY   B C   
5103 O O   . GLY   B 78  ? 0.1300 0.1345 0.1401 0.0191  0.0152  0.0100  78  GLY   B O   
5107 N N   . GLY   B 79  ? 0.1200 0.1437 0.1281 0.0143  0.0182  0.0062  79  GLY   B N   
5108 C CA  . GLY   B 79  ? 0.1268 0.1309 0.1290 0.0139  0.0085  0.0029  79  GLY   B CA  
5109 C C   . GLY   B 79  ? 0.1137 0.1233 0.1261 0.0139  0.0046  -0.0032 79  GLY   B C   
5110 O O   . GLY   B 79  ? 0.1215 0.1233 0.1317 0.0121  0.0180  0.0095  79  GLY   B O   
5114 N N   . SER   B 80  ? 0.1189 0.1183 0.1363 0.0090  0.0156  -0.0040 80  SER   B N   
5115 C CA  . SER   B 80  ? 0.1168 0.1176 0.1347 0.0073  0.0078  -0.0002 80  SER   B CA  
5116 C C   . SER   B 80  ? 0.1178 0.1116 0.1318 0.0080  -0.0033 -0.0069 80  SER   B C   
5117 O O   . SER   B 80  ? 0.1278 0.1145 0.1691 0.0109  0.0063  -0.0143 80  SER   B O   
5118 C CB  . SER   B 80  ? 0.1182 0.1218 0.1534 -0.0015 0.0043  0.0024  80  SER   B CB  
5119 O OG  . SER   B 80  ? 0.1200 0.1354 0.1732 0.0030  -0.0140 0.0073  80  SER   B OG  
5125 N N   . CYS   B 81  ? 0.1131 0.1020 0.1454 0.0030  -0.0017 -0.0044 81  CYS   B N   
5126 C CA  . CYS   B 81  ? 0.1181 0.1027 0.1486 0.0080  -0.0068 -0.0076 81  CYS   B CA  
5127 C C   . CYS   B 81  ? 0.1136 0.0989 0.1236 0.0048  -0.0166 -0.0071 81  CYS   B C   
5128 O O   . CYS   B 81  ? 0.1397 0.1029 0.1291 0.0094  -0.0040 -0.0080 81  CYS   B O   
5129 C CB  . CYS   B 81  ? 0.1367 0.1157 0.1509 -0.0061 -0.0135 -0.0083 81  CYS   B CB  
5130 S SG  . CYS   B 81  ? 0.1337 0.1335 0.1454 -0.0025 -0.0235 -0.0130 81  CYS   B SG  
5136 N N   . VAL   B 82  ? 0.1202 0.0988 0.1384 0.0003  -0.0087 -0.0098 82  VAL   B N   
5137 C CA  . VAL   B 82  ? 0.1243 0.1018 0.1372 -0.0031 -0.0064 -0.0085 82  VAL   B CA  
5138 C C   . VAL   B 82  ? 0.1320 0.0977 0.1466 -0.0006 -0.0029 -0.0031 82  VAL   B C   
5139 O O   . VAL   B 82  ? 0.1422 0.0989 0.1755 0.0001  -0.0108 -0.0176 82  VAL   B O   
5140 C CB  . VAL   B 82  ? 0.1327 0.1261 0.1518 0.0006  -0.0114 0.0022  82  VAL   B CB  
5141 C CG1 . VAL   B 82  ? 0.1594 0.1458 0.1576 0.0065  -0.0062 0.0130  82  VAL   B CG1 
5142 C CG2 . VAL   B 82  ? 0.1398 0.1419 0.1664 -0.0018 -0.0251 0.0030  82  VAL   B CG2 
5152 N N   . LEU   B 83  ? 0.1210 0.0997 0.1428 -0.0115 -0.0176 -0.0091 83  LEU   B N   
5153 C CA  . LEU   B 83  ? 0.1219 0.1016 0.1376 -0.0099 -0.0149 -0.0041 83  LEU   B CA  
5154 C C   . LEU   B 83  ? 0.1191 0.1014 0.1397 -0.0177 -0.0166 -0.0018 83  LEU   B C   
5155 O O   . LEU   B 83  ? 0.1242 0.1112 0.1335 -0.0213 -0.0089 0.0073  83  LEU   B O   
5156 C CB  . LEU   B 83  ? 0.1301 0.1191 0.1342 -0.0132 -0.0224 -0.0073 83  LEU   B CB  
5157 C CG  . LEU   B 83  ? 0.1488 0.1378 0.1497 -0.0179 -0.0069 -0.0122 83  LEU   B CG  
5158 C CD1 . LEU   B 83  ? 0.1552 0.1475 0.1393 -0.0079 -0.0149 -0.0040 83  LEU   B CD1 
5159 C CD2 . LEU   B 83  ? 0.1699 0.1405 0.1612 -0.0092 -0.0106 -0.0265 83  LEU   B CD2 
5171 N N   . SER   B 84  ? 0.1267 0.1102 0.1600 -0.0178 -0.0134 0.0005  84  SER   B N   
5172 C CA  . SER   B 84  ? 0.1295 0.1298 0.1554 -0.0189 -0.0096 0.0130  84  SER   B CA  
5173 C C   . SER   B 84  ? 0.1178 0.1514 0.1212 -0.0183 -0.0104 0.0212  84  SER   B C   
5174 O O   . SER   B 84  ? 0.1269 0.1334 0.1230 -0.0194 -0.0114 0.0054  84  SER   B O   
5175 C CB  . SER   B 84  ? 0.1435 0.1326 0.2064 -0.0193 0.0084  0.0149  84  SER   B CB  
5176 O OG  . SER   B 84  ? 0.1461 0.1464 0.2579 -0.0288 0.0156  0.0209  84  SER   B OG  
5182 N N   . GLY   B 85  ? 0.1243 0.1734 0.1348 -0.0248 -0.0127 0.0167  85  GLY   B N   
5183 C CA  . GLY   B 85  ? 0.1266 0.1826 0.1411 -0.0345 0.0001  -0.0057 85  GLY   B CA  
5184 C C   . GLY   B 85  ? 0.1239 0.1625 0.1404 -0.0394 0.0016  0.0081  85  GLY   B C   
5185 O O   . GLY   B 85  ? 0.1317 0.1667 0.1378 -0.0500 0.0181  -0.0032 85  GLY   B O   
5189 N N   . HIS   B 86  ? 0.1230 0.1422 0.1456 -0.0304 -0.0150 0.0209  86  HIS   B N   
5190 C CA  . HIS   B 86  ? 0.1216 0.1408 0.1411 -0.0301 -0.0156 0.0222  86  HIS   B CA  
5191 C C   . HIS   B 86  ? 0.1207 0.1530 0.1370 -0.0388 -0.0137 0.0409  86  HIS   B C   
5192 O O   . HIS   B 86  ? 0.1375 0.1660 0.1465 -0.0306 -0.0005 0.0402  86  HIS   B O   
5193 C CB  . HIS   B 86  ? 0.1314 0.1414 0.1446 -0.0176 -0.0171 0.0135  86  HIS   B CB  
5194 C CG  . HIS   B 86  ? 0.1358 0.1472 0.1454 -0.0087 -0.0240 0.0205  86  HIS   B CG  
5195 N ND1 . HIS   B 86  ? 0.1482 0.1692 0.1642 -0.0180 -0.0300 0.0001  86  HIS   B ND1 
5196 C CD2 . HIS   B 86  ? 0.1383 0.1524 0.1452 -0.0089 -0.0192 0.0106  86  HIS   B CD2 
5197 C CE1 . HIS   B 86  ? 0.1529 0.1722 0.1564 -0.0139 -0.0102 -0.0145 86  HIS   B CE1 
5198 N NE2 . HIS   B 86  ? 0.1464 0.1661 0.1402 0.0005  -0.0089 -0.0033 86  HIS   B NE2 
5206 N N   . ASN   B 87  ? 0.1259 0.1563 0.1430 -0.0327 -0.0025 0.0377  87  ASN   B N   
5207 C CA  . ASN   B 87  ? 0.1300 0.1729 0.1521 -0.0291 0.0202  0.0260  87  ASN   B CA  
5208 C C   . ASN   B 87  ? 0.1416 0.1605 0.1450 -0.0232 0.0313  0.0203  87  ASN   B C   
5209 O O   . ASN   B 87  ? 0.1642 0.1691 0.1782 -0.0246 0.0480  0.0179  87  ASN   B O   
5210 C CB  . ASN   B 87  ? 0.1369 0.2128 0.1760 -0.0206 0.0250  0.0192  87  ASN   B CB  
5211 C CG  . ASN   B 87  ? 0.1513 0.2339 0.1895 0.0123  0.0254  0.0404  87  ASN   B CG  
5212 O OD1 . ASN   B 87  ? 0.1403 0.2176 0.1720 0.0094  0.0426  0.0626  87  ASN   B OD1 
5213 N ND2 . ASN   B 87  ? 0.1805 0.2483 0.2285 0.0166  0.0268  0.0407  87  ASN   B ND2 
5220 N N   . LEU   B 88  ? 0.1360 0.1462 0.1272 -0.0311 0.0165  0.0190  88  LEU   B N   
5221 C CA  . LEU   B 88  ? 0.1439 0.1417 0.1320 -0.0274 0.0076  0.0084  88  LEU   B CA  
5222 C C   . LEU   B 88  ? 0.1420 0.1316 0.1258 -0.0293 0.0031  0.0067  88  LEU   B C   
5223 O O   . LEU   B 88  ? 0.1668 0.1438 0.1581 -0.0122 -0.0237 -0.0022 88  LEU   B O   
5224 C CB  . LEU   B 88  ? 0.1555 0.1487 0.1508 -0.0329 -0.0053 0.0173  88  LEU   B CB  
5225 C CG  . LEU   B 88  ? 0.1927 0.1778 0.1649 -0.0343 -0.0234 0.0419  88  LEU   B CG  
5226 C CD1 . LEU   B 88  ? 0.2094 0.2110 0.1874 -0.0440 -0.0127 0.0529  88  LEU   B CD1 
5227 C CD2 . LEU   B 88  ? 0.2291 0.2043 0.2217 0.0074  -0.0572 0.0193  88  LEU   B CD2 
5239 N N   . ALA   B 89  ? 0.1366 0.1284 0.1282 -0.0310 0.0181  0.0051  89  ALA   B N   
5240 C CA  . ALA   B 89  ? 0.1349 0.1256 0.1079 -0.0345 0.0082  0.0100  89  ALA   B CA  
5241 C C   . ALA   B 89  ? 0.1401 0.1271 0.1128 -0.0359 0.0177  0.0047  89  ALA   B C   
5242 O O   . ALA   B 89  ? 0.1247 0.1412 0.1534 -0.0357 0.0141  -0.0269 89  ALA   B O   
5243 C CB  . ALA   B 89  ? 0.1253 0.1269 0.1268 -0.0322 0.0060  0.0147  89  ALA   B CB  
5249 N N   . LYS   B 90  ? 0.1745 0.1181 0.1276 -0.0366 -0.0032 0.0087  90  LYS   B N   
5250 C CA  . LYS   B 90  ? 0.1890 0.1147 0.1345 -0.0412 -0.0062 0.0117  90  LYS   B CA  
5251 C C   . LYS   B 90  ? 0.1751 0.1052 0.1454 -0.0438 -0.0077 -0.0019 90  LYS   B C   
5252 O O   . LYS   B 90  ? 0.1891 0.1298 0.1666 -0.0650 0.0043  0.0011  90  LYS   B O   
5253 C CB  . LYS   B 90  ? 0.2082 0.1191 0.1634 -0.0331 0.0060  0.0181  90  LYS   B CB  
5254 C CG  . LYS   B 90  ? 0.2073 0.1339 0.1603 -0.0163 0.0351  0.0214  90  LYS   B CG  
5255 C CD  . LYS   B 90  ? 0.2335 0.1579 0.2139 -0.0105 0.0533  -0.0017 90  LYS   B CD  
5256 C CE  . LYS   B 90  ? 0.2436 0.1778 0.2614 -0.0149 0.0642  -0.0032 90  LYS   B CE  
5257 N NZ  . LYS   B 90  ? 0.2510 0.1759 0.2700 -0.0215 0.0703  0.0026  90  LYS   B NZ  
5271 N N   . HIS   B 91  ? 0.1471 0.1006 0.1166 -0.0292 -0.0128 0.0017  91  HIS   B N   
5272 C CA  . HIS   B 91  ? 0.1352 0.1023 0.1235 -0.0183 -0.0141 -0.0010 91  HIS   B CA  
5273 C C   . HIS   B 91  ? 0.1205 0.1065 0.1139 -0.0261 -0.0087 -0.0022 91  HIS   B C   
5274 O O   . HIS   B 91  ? 0.1371 0.1098 0.1175 -0.0207 -0.0144 0.0057  91  HIS   B O   
5275 C CB  . HIS   B 91  ? 0.1551 0.1061 0.1663 0.0001  -0.0082 0.0078  91  HIS   B CB  
5276 C CG  . HIS   B 91  ? 0.1969 0.1233 0.2417 0.0103  0.0291  0.0320  91  HIS   B CG  
5277 N ND1 . HIS   B 91  ? 0.2313 0.1366 0.3027 0.0049  0.0368  0.0176  91  HIS   B ND1 
5278 C CD2 . HIS   B 91  ? 0.2100 0.1560 0.2913 0.0229  0.0135  0.0615  91  HIS   B CD2 
5279 C CE1 . HIS   B 91  ? 0.2345 0.1526 0.3226 0.0216  0.0320  0.0295  91  HIS   B CE1 
5280 N NE2 . HIS   B 91  ? 0.2228 0.1673 0.3219 0.0353  0.0265  0.0676  91  HIS   B NE2 
5288 N N   . CYS   B 92  ? 0.1160 0.1036 0.1175 -0.0287 -0.0130 -0.0009 92  CYS   B N   
5289 C CA  . CYS   B 92  ? 0.1166 0.0976 0.1102 -0.0216 -0.0071 0.0028  92  CYS   B CA  
5290 C C   . CYS   B 92  ? 0.1124 0.0927 0.1054 -0.0109 -0.0037 0.0019  92  CYS   B C   
5291 O O   . CYS   B 92  ? 0.1178 0.1021 0.1337 -0.0155 -0.0034 -0.0073 92  CYS   B O   
5292 C CB  . CYS   B 92  ? 0.1133 0.1139 0.1163 -0.0113 -0.0008 0.0041  92  CYS   B CB  
5293 S SG  . CYS   B 92  ? 0.1184 0.1138 0.1197 -0.0063 -0.0089 0.0057  92  CYS   B SG  
5299 N N   . LEU   B 93  ? 0.1033 0.0986 0.1088 -0.0111 -0.0050 -0.0067 93  LEU   B N   
5300 C CA  . LEU   B 93  ? 0.1055 0.0994 0.1133 -0.0040 -0.0036 -0.0002 93  LEU   B CA  
5301 C C   . LEU   B 93  ? 0.0983 0.0937 0.1091 -0.0001 -0.0049 -0.0007 93  LEU   B C   
5302 O O   . LEU   B 93  ? 0.1070 0.0994 0.1111 -0.0041 -0.0027 0.0021  93  LEU   B O   
5303 C CB  . LEU   B 93  ? 0.1046 0.1023 0.1180 -0.0023 -0.0016 -0.0052 93  LEU   B CB  
5304 C CG  . LEU   B 93  ? 0.1066 0.1127 0.1397 -0.0030 -0.0008 0.0080  93  LEU   B CG  
5305 C CD1 . LEU   B 93  ? 0.1134 0.1220 0.1447 0.0037  -0.0006 -0.0012 93  LEU   B CD1 
5306 C CD2 . LEU   B 93  ? 0.1028 0.1199 0.1519 0.0039  -0.0022 -0.0005 93  LEU   B CD2 
5318 N N   . HIS   B 94  ? 0.1022 0.0930 0.1079 -0.0050 -0.0086 -0.0007 94  HIS   B N   
5319 C CA  . HIS   B 94  ? 0.1030 0.0929 0.1143 -0.0002 -0.0032 0.0010  94  HIS   B CA  
5320 C C   . HIS   B 94  ? 0.1016 0.0994 0.1253 0.0018  0.0023  0.0021  94  HIS   B C   
5321 O O   . HIS   B 94  ? 0.1083 0.1086 0.1644 -0.0003 0.0162  -0.0081 94  HIS   B O   
5322 C CB  . HIS   B 94  ? 0.1091 0.0992 0.1169 0.0008  -0.0028 0.0044  94  HIS   B CB  
5323 C CG  . HIS   B 94  ? 0.1114 0.1003 0.1138 -0.0058 -0.0169 0.0016  94  HIS   B CG  
5324 N ND1 . HIS   B 94  ? 0.1101 0.1065 0.1209 -0.0029 -0.0173 0.0001  94  HIS   B ND1 
5325 C CD2 . HIS   B 94  ? 0.1200 0.1048 0.1232 -0.0015 -0.0179 0.0030  94  HIS   B CD2 
5326 C CE1 . HIS   B 94  ? 0.1128 0.1058 0.1216 -0.0118 -0.0146 0.0016  94  HIS   B CE1 
5327 N NE2 . HIS   B 94  ? 0.1109 0.1089 0.1367 -0.0132 -0.0133 0.0043  94  HIS   B NE2 
5335 N N   . VAL   B 95  ? 0.0954 0.0913 0.1258 0.0026  0.0010  0.0021  95  VAL   B N   
5336 C CA  . VAL   B 95  ? 0.1014 0.1002 0.1234 0.0024  -0.0002 0.0054  95  VAL   B CA  
5337 C C   . VAL   B 95  ? 0.1074 0.1050 0.1233 -0.0012 0.0082  0.0001  95  VAL   B C   
5338 O O   . VAL   B 95  ? 0.1103 0.1000 0.1423 0.0062  0.0068  0.0107  95  VAL   B O   
5339 C CB  . VAL   B 95  ? 0.1103 0.1006 0.1215 0.0006  -0.0050 -0.0008 95  VAL   B CB  
5340 C CG1 . VAL   B 95  ? 0.1197 0.1220 0.1391 -0.0092 0.0030  0.0134  95  VAL   B CG1 
5341 C CG2 . VAL   B 95  ? 0.1162 0.1046 0.1255 0.0064  -0.0098 0.0014  95  VAL   B CG2 
5351 N N   . VAL   B 96  ? 0.1141 0.1139 0.1123 0.0092  0.0034  0.0091  96  VAL   B N   
5352 C CA  . VAL   B 96  ? 0.1245 0.1288 0.1119 0.0098  0.0007  0.0142  96  VAL   B CA  
5353 C C   . VAL   B 96  ? 0.1228 0.1271 0.1127 0.0060  0.0076  0.0113  96  VAL   B C   
5354 O O   . VAL   B 96  ? 0.1216 0.1277 0.1399 0.0050  0.0170  0.0003  96  VAL   B O   
5355 C CB  . VAL   B 96  ? 0.1306 0.1400 0.1150 0.0111  0.0071  0.0020  96  VAL   B CB  
5356 C CG1 . VAL   B 96  ? 0.1289 0.1539 0.1373 0.0141  0.0102  0.0007  96  VAL   B CG1 
5357 C CG2 . VAL   B 96  ? 0.1362 0.1506 0.1273 0.0102  0.0098  -0.0020 96  VAL   B CG2 
5367 N N   . GLY   B 97  ? 0.1282 0.1232 0.1234 0.0050  0.0046  0.0181  97  GLY   B N   
5368 C CA  . GLY   B 97  ? 0.1382 0.1226 0.1285 -0.0006 0.0084  0.0156  97  GLY   B CA  
5369 C C   . GLY   B 97  ? 0.1507 0.1322 0.1274 0.0067  0.0006  0.0143  97  GLY   B C   
5370 O O   . GLY   B 97  ? 0.1592 0.1439 0.1322 0.0026  0.0054  0.0124  97  GLY   B O   
5374 N N   . PRO   B 98  ? 0.1624 0.1372 0.1331 0.0066  0.0172  0.0235  98  PRO   B N   
5375 C CA  . PRO   B 98  ? 0.1707 0.1498 0.1395 0.0130  0.0293  0.0142  98  PRO   B CA  
5376 C C   . PRO   B 98  ? 0.1829 0.1538 0.1103 0.0225  0.0278  0.0303  98  PRO   B C   
5377 O O   . PRO   B 98  ? 0.1788 0.1505 0.1366 0.0200  0.0251  0.0298  98  PRO   B O   
5378 C CB  . PRO   B 98  ? 0.1623 0.1532 0.1555 0.0055  0.0337  0.0157  98  PRO   B CB  
5379 C CG  . PRO   B 98  ? 0.1574 0.1483 0.1558 0.0035  0.0225  0.0244  98  PRO   B CG  
5380 C CD  . PRO   B 98  ? 0.1438 0.1358 0.1498 0.0062  0.0151  0.0248  98  PRO   B CD  
5388 N N   . ASN   B 99  ? 0.1891 0.1662 0.1284 0.0345  0.0235  0.0208  99  ASN   B N   
5389 C CA  . ASN   B 99  ? 0.2029 0.1722 0.1335 0.0384  0.0137  0.0285  99  ASN   B CA  
5390 C C   . ASN   B 99  ? 0.2296 0.1991 0.1506 0.0309  0.0314  0.0448  99  ASN   B C   
5391 O O   . ASN   B 99  ? 0.2434 0.2027 0.1577 0.0326  0.0254  0.0450  99  ASN   B O   
5392 C CB  . ASN   B 99  ? 0.2133 0.1665 0.1409 0.0381  0.0038  0.0316  99  ASN   B CB  
5393 C CG  . ASN   B 99  ? 0.2183 0.1756 0.1719 0.0342  -0.0072 0.0323  99  ASN   B CG  
5394 O OD1 . ASN   B 99  ? 0.2239 0.1787 0.1992 0.0360  -0.0128 0.0372  99  ASN   B OD1 
5395 N ND2 . ASN   B 99  ? 0.2203 0.1785 0.1961 0.0343  -0.0219 0.0248  99  ASN   B ND2 
5402 N N   A VAL   B 100 ? 0.2459 0.2133 0.1830 0.0211  0.0360  0.0624  100 VAL   B N   
5403 N N   B VAL   B 100 ? 0.2447 0.2120 0.1815 0.0196  0.0369  0.0629  100 VAL   B N   
5404 C CA  A VAL   B 100 ? 0.2726 0.2310 0.2289 0.0164  0.0393  0.0760  100 VAL   B CA  
5405 C CA  B VAL   B 100 ? 0.2707 0.2285 0.2263 0.0135  0.0405  0.0766  100 VAL   B CA  
5406 C C   A VAL   B 100 ? 0.2910 0.2382 0.2286 0.0264  0.0402  0.0945  100 VAL   B C   
5407 C C   B VAL   B 100 ? 0.2897 0.2359 0.2257 0.0246  0.0404  0.0941  100 VAL   B C   
5408 O O   A VAL   B 100 ? 0.2981 0.2473 0.2337 0.0245  0.0481  0.0927  100 VAL   B O   
5409 O O   B VAL   B 100 ? 0.2964 0.2428 0.2280 0.0221  0.0481  0.0911  100 VAL   B O   
5410 C CB  A VAL   B 100 ? 0.2862 0.2478 0.2910 0.0002  0.0349  0.0739  100 VAL   B CB  
5411 C CB  B VAL   B 100 ? 0.2833 0.2438 0.2871 -0.0048 0.0370  0.0760  100 VAL   B CB  
5412 C CG1 A VAL   B 100 ? 0.2931 0.2530 0.3165 -0.0010 0.0353  0.0726  100 VAL   B CG1 
5413 C CG1 B VAL   B 100 ? 0.2904 0.2487 0.3128 -0.0059 0.0370  0.0751  100 VAL   B CG1 
5414 C CG2 A VAL   B 100 ? 0.2891 0.2539 0.3118 -0.0077 0.0341  0.0807  100 VAL   B CG2 
5415 C CG2 B VAL   B 100 ? 0.2853 0.2484 0.3064 -0.0147 0.0372  0.0842  100 VAL   B CG2 
5434 N N   . ASN   B 101 ? 0.3039 0.2411 0.2352 0.0364  0.0282  0.1051  101 ASN   B N   
5435 C CA  . ASN   B 101 ? 0.3465 0.2610 0.2579 0.0479  0.0043  0.1191  101 ASN   B CA  
5436 C C   . ASN   B 101 ? 0.3893 0.3074 0.2521 0.0470  -0.0117 0.1222  101 ASN   B C   
5437 O O   . ASN   B 101 ? 0.4005 0.3243 0.2661 0.0537  -0.0217 0.1045  101 ASN   B O   
5438 C CB  . ASN   B 101 ? 0.3507 0.2447 0.2791 0.0468  0.0134  0.1178  101 ASN   B CB  
5439 C CG  . ASN   B 101 ? 0.3557 0.2327 0.2970 0.0476  0.0282  0.1157  101 ASN   B CG  
5440 O OD1 . ASN   B 101 ? 0.3669 0.2292 0.3278 0.0408  0.0494  0.1068  101 ASN   B OD1 
5441 N ND2 . ASN   B 101 ? 0.3525 0.2340 0.2970 0.0479  0.0244  0.1055  101 ASN   B ND2 
5449 N N   A LYS   B 102 ? 0.4062 0.3296 0.2696 0.0390  -0.0036 0.1086  102 LYS   B N   
5450 N N   B LYS   B 102 ? 0.4024 0.3267 0.2688 0.0376  -0.0028 0.1107  102 LYS   B N   
5451 C CA  A LYS   B 102 ? 0.4218 0.3569 0.2939 0.0295  0.0080  0.0834  102 LYS   B CA  
5452 C CA  B LYS   B 102 ? 0.4144 0.3514 0.2920 0.0270  0.0096  0.0866  102 LYS   B CA  
5453 C C   A LYS   B 102 ? 0.4207 0.3611 0.2771 0.0320  0.0203  0.0880  102 LYS   B C   
5454 C C   B LYS   B 102 ? 0.4103 0.3524 0.2762 0.0279  0.0205  0.0915  102 LYS   B C   
5455 O O   A LYS   B 102 ? 0.4280 0.3664 0.2817 0.0330  0.0143  0.0829  102 LYS   B O   
5456 O O   B LYS   B 102 ? 0.4163 0.3576 0.2839 0.0296  0.0148  0.0839  102 LYS   B O   
5457 C CB  A LYS   B 102 ? 0.4375 0.3780 0.3463 0.0190  0.0111  0.0504  102 LYS   B CB  
5458 C CB  B LYS   B 102 ? 0.4293 0.3733 0.3429 0.0167  0.0137  0.0533  102 LYS   B CB  
5459 C CG  A LYS   B 102 ? 0.4518 0.3961 0.3920 0.0111  0.0159  0.0222  102 LYS   B CG  
5460 C CG  B LYS   B 102 ? 0.4430 0.3921 0.3873 0.0093  0.0187  0.0238  102 LYS   B CG  
5461 C CD  A LYS   B 102 ? 0.4654 0.4105 0.4364 0.0054  0.0204  0.0018  102 LYS   B CD  
5462 C CD  B LYS   B 102 ? 0.4559 0.4071 0.4291 0.0037  0.0231  0.0027  102 LYS   B CD  
5463 C CE  A LYS   B 102 ? 0.4767 0.4205 0.4717 0.0016  0.0237  -0.0126 102 LYS   B CE  
5464 C CE  B LYS   B 102 ? 0.4663 0.4176 0.4633 0.0001  0.0266  -0.0120 102 LYS   B CE  
5465 N NZ  A LYS   B 102 ? 0.4831 0.4260 0.4904 -0.0001 0.0241  -0.0203 102 LYS   B NZ  
5466 N NZ  B LYS   B 102 ? 0.4723 0.4237 0.4809 -0.0013 0.0271  -0.0195 102 LYS   B NZ  
5493 N N   A GLY   B 103 ? 0.4096 0.3581 0.2652 0.0324  0.0382  0.0922  103 GLY   B N   
5494 N N   B GLY   B 103 ? 0.3973 0.3460 0.2608 0.0259  0.0375  0.0991  103 GLY   B N   
5495 C CA  A GLY   B 103 ? 0.3977 0.3547 0.2752 0.0342  0.0547  0.0834  103 GLY   B CA  
5496 C CA  B GLY   B 103 ? 0.3836 0.3392 0.2661 0.0241  0.0526  0.0906  103 GLY   B CA  
5497 C C   A GLY   B 103 ? 0.3834 0.3483 0.2721 0.0353  0.0699  0.0733  103 GLY   B C   
5498 C C   B GLY   B 103 ? 0.3672 0.3293 0.2554 0.0205  0.0664  0.0794  103 GLY   B C   
5499 O O   A GLY   B 103 ? 0.3868 0.3542 0.2771 0.0354  0.0725  0.0758  103 GLY   B O   
5500 O O   B GLY   B 103 ? 0.3706 0.3356 0.2606 0.0223  0.0725  0.0796  103 GLY   B O   
5507 N N   A GLU   B 104 ? 0.3635 0.3336 0.2566 0.0368  0.0788  0.0560  104 GLU   B N   
5508 N N   B GLU   B 104 ? 0.3449 0.3100 0.2280 0.0147  0.0692  0.0636  104 GLU   B N   
5509 C CA  A GLU   B 104 ? 0.3446 0.3202 0.2405 0.0393  0.0820  0.0360  104 GLU   B CA  
5510 C CA  B GLU   B 104 ? 0.3237 0.2927 0.2025 0.0084  0.0669  0.0445  104 GLU   B CA  
5511 C C   A GLU   B 104 ? 0.3476 0.3216 0.2505 0.0267  0.1037  0.0289  104 GLU   B C   
5512 C C   B GLU   B 104 ? 0.3227 0.2925 0.2069 -0.0023 0.0885  0.0367  104 GLU   B C   
5513 O O   A GLU   B 104 ? 0.3517 0.3255 0.2633 0.0229  0.0995  0.0238  104 GLU   B O   
5514 O O   B GLU   B 104 ? 0.3281 0.2974 0.2252 -0.0057 0.0831  0.0311  104 GLU   B O   
5515 C CB  A GLU   B 104 ? 0.3272 0.3050 0.2369 0.0551  0.0536  0.0160  104 GLU   B CB  
5516 C CB  B GLU   B 104 ? 0.3081 0.2750 0.1978 0.0115  0.0339  0.0235  104 GLU   B CB  
5517 C CG  A GLU   B 104 ? 0.3138 0.2949 0.2340 0.0682  0.0241  -0.0075 104 GLU   B CG  
5518 C CG  B GLU   B 104 ? 0.2968 0.2624 0.1923 0.0134  0.0004  -0.0024 104 GLU   B CG  
5519 C CD  A GLU   B 104 ? 0.2998 0.2836 0.2196 0.0829  -0.0037 -0.0190 104 GLU   B CD  
5520 C CD  B GLU   B 104 ? 0.2869 0.2477 0.1712 0.0126  -0.0303 -0.0114 104 GLU   B CD  
5521 O OE1 A GLU   B 104 ? 0.2841 0.2694 0.1862 0.0970  0.0001  -0.0173 104 GLU   B OE1 
5522 O OE1 B GLU   B 104 ? 0.2750 0.2341 0.1438 0.0131  -0.0282 -0.0057 104 GLU   B OE1 
5523 O OE2 A GLU   B 104 ? 0.3050 0.2920 0.2363 0.0785  -0.0285 -0.0276 104 GLU   B OE2 
5524 O OE2 B GLU   B 104 ? 0.2907 0.2522 0.1766 0.0061  -0.0574 -0.0211 104 GLU   B OE2 
5537 N N   A ASP   B 105 ? 0.3442 0.3199 0.2519 0.0150  0.1220  0.0278  105 ASP   B N   
5538 N N   B ASP   B 105 ? 0.3141 0.2884 0.1967 -0.0132 0.1092  0.0328  105 ASP   B N   
5539 C CA  A ASP   B 105 ? 0.3445 0.3178 0.2698 0.0037  0.1333  0.0192  105 ASP   B CA  
5540 C CA  B ASP   B 105 ? 0.3096 0.2837 0.2098 -0.0247 0.1235  0.0188  105 ASP   B CA  
5541 C C   A ASP   B 105 ? 0.3353 0.2970 0.2521 -0.0056 0.1344  0.0164  105 ASP   B C   
5542 C C   B ASP   B 105 ? 0.2991 0.2601 0.1944 -0.0365 0.1165  0.0122  105 ASP   B C   
5543 O O   A ASP   B 105 ? 0.3309 0.2934 0.2468 -0.0043 0.1381  0.0164  105 ASP   B O   
5544 O O   B ASP   B 105 ? 0.2865 0.2482 0.1797 -0.0420 0.1126  0.0089  105 ASP   B O   
5545 C CB  A ASP   B 105 ? 0.3552 0.3353 0.3243 0.0061  0.1324  0.0075  105 ASP   B CB  
5546 C CB  B ASP   B 105 ? 0.3180 0.3013 0.2656 -0.0199 0.1272  0.0029  105 ASP   B CB  
5547 C CG  A ASP   B 105 ? 0.3634 0.3495 0.3789 0.0044  0.1367  0.0016  105 ASP   B CG  
5548 C CG  B ASP   B 105 ? 0.3247 0.3136 0.3211 -0.0221 0.1334  -0.0020 105 ASP   B CG  
5549 O OD1 A ASP   B 105 ? 0.3641 0.3549 0.3888 -0.0003 0.1420  0.0033  105 ASP   B OD1 
5550 O OD1 B ASP   B 105 ? 0.3233 0.3204 0.3273 -0.0294 0.1391  -0.0012 105 ASP   B OD1 
5551 O OD2 A ASP   B 105 ? 0.3674 0.3565 0.4069 0.0070  0.1321  -0.0030 105 ASP   B OD2 
5552 O OD2 B ASP   B 105 ? 0.3265 0.3167 0.3307 -0.0212 0.1391  -0.0011 105 ASP   B OD2 
5561 N N   A ILE   B 106 ? 0.3281 0.2780 0.2565 -0.0148 0.1216  0.0181  106 ILE   B N   
5562 N N   B ILE   B 106 ? 0.2982 0.2467 0.2093 -0.0435 0.1013  0.0136  106 ILE   B N   
5563 C CA  A ILE   B 106 ? 0.3114 0.2562 0.2555 -0.0255 0.1212  0.0161  106 ILE   B CA  
5564 C CA  B ILE   B 106 ? 0.2841 0.2293 0.2179 -0.0566 0.1003  0.0100  106 ILE   B CA  
5565 C C   A ILE   B 106 ? 0.2818 0.2446 0.2483 -0.0226 0.1182  0.0031  106 ILE   B C   
5566 C C   B ILE   B 106 ? 0.2542 0.2226 0.2098 -0.0571 0.0915  -0.0147 106 ILE   B C   
5567 O O   A ILE   B 106 ? 0.2762 0.2317 0.2480 -0.0202 0.1139  0.0006  106 ILE   B O   
5568 O O   B ILE   B 106 ? 0.2405 0.2057 0.1914 -0.0650 0.0764  -0.0275 106 ILE   B O   
5569 C CB  A ILE   B 106 ? 0.3264 0.2517 0.2752 -0.0337 0.1163  0.0225  106 ILE   B CB  
5570 C CB  B ILE   B 106 ? 0.3038 0.2285 0.2475 -0.0586 0.0993  0.0218  106 ILE   B CB  
5571 C CG1 A ILE   B 106 ? 0.3306 0.2480 0.2827 -0.0264 0.1117  0.0169  106 ILE   B CG1 
5572 C CG1 B ILE   B 106 ? 0.3107 0.2291 0.2617 -0.0438 0.0948  0.0167  106 ILE   B CG1 
5573 C CG2 A ILE   B 106 ? 0.3333 0.2556 0.2923 -0.0414 0.1162  0.0275  106 ILE   B CG2 
5574 C CG2 B ILE   B 106 ? 0.3121 0.2329 0.2690 -0.0667 0.1004  0.0274  106 ILE   B CG2 
5575 C CD1 A ILE   B 106 ? 0.3321 0.2468 0.2860 -0.0207 0.1088  0.0164  106 ILE   B CD1 
5576 C CD1 B ILE   B 106 ? 0.3133 0.2306 0.2692 -0.0343 0.0926  0.0170  106 ILE   B CD1 
5599 N N   A GLN   B 107 ? 0.2644 0.2506 0.2658 -0.0244 0.1093  0.0013  107 GLN   B N   
5600 N N   B GLN   B 107 ? 0.2471 0.2402 0.2391 -0.0466 0.0856  -0.0189 107 GLN   B N   
5601 C CA  A GLN   B 107 ? 0.2466 0.2577 0.2796 -0.0234 0.1005  0.0031  107 GLN   B CA  
5602 C CA  B GLN   B 107 ? 0.2407 0.2589 0.2630 -0.0304 0.0799  -0.0139 107 GLN   B CA  
5603 C C   A GLN   B 107 ? 0.2155 0.2385 0.2511 -0.0129 0.0820  0.0006  107 GLN   B C   
5604 C C   B GLN   B 107 ? 0.2168 0.2459 0.2349 -0.0137 0.0519  -0.0167 107 GLN   B C   
5605 O O   A GLN   B 107 ? 0.2155 0.2433 0.2818 -0.0056 0.0622  -0.0085 107 GLN   B O   
5606 O O   B GLN   B 107 ? 0.2179 0.2550 0.2649 -0.0064 0.0371  -0.0248 107 GLN   B O   
5607 C CB  A GLN   B 107 ? 0.2726 0.2860 0.3401 -0.0227 0.0874  0.0064  107 GLN   B CB  
5608 C CB  B GLN   B 107 ? 0.2694 0.2899 0.3281 -0.0247 0.0761  -0.0064 107 GLN   B CB  
5609 C CG  A GLN   B 107 ? 0.3001 0.3136 0.4042 -0.0185 0.0575  0.0068  107 GLN   B CG  
5610 C CG  B GLN   B 107 ? 0.2997 0.3195 0.3960 -0.0175 0.0535  -0.0022 107 GLN   B CG  
5611 C CD  A GLN   B 107 ? 0.3200 0.3356 0.4560 -0.0184 0.0377  0.0097  107 GLN   B CD  
5612 C CD  B GLN   B 107 ? 0.3229 0.3432 0.4498 -0.0151 0.0369  0.0029  107 GLN   B CD  
5613 O OE1 A GLN   B 107 ? 0.3273 0.3446 0.4749 -0.0187 0.0362  0.0061  107 GLN   B OE1 
5614 O OE1 B GLN   B 107 ? 0.3319 0.3525 0.4686 -0.0165 0.0362  0.0015  107 GLN   B OE1 
5615 N NE2 A GLN   B 107 ? 0.3278 0.3424 0.4732 -0.0149 0.0282  0.0161  107 GLN   B NE2 
5616 N NE2 B GLN   B 107 ? 0.3318 0.3509 0.4675 -0.0103 0.0297  0.0086  107 GLN   B NE2 
5633 N N   A LEU   B 108 ? 0.1880 0.2142 0.2159 0.0021  0.0741  0.0024  108 LEU   B N   
5634 N N   B LEU   B 108 ? 0.1942 0.2210 0.2009 0.0025  0.0337  -0.0150 108 LEU   B N   
5635 C CA  A LEU   B 108 ? 0.1776 0.1950 0.1886 0.0140  0.0601  0.0094  108 LEU   B CA  
5636 C CA  B LEU   B 108 ? 0.1860 0.1989 0.1785 0.0159  0.0280  -0.0014 108 LEU   B CA  
5637 C C   A LEU   B 108 ? 0.1594 0.1613 0.1827 0.0188  0.0418  0.0192  108 LEU   B C   
5638 C C   B LEU   B 108 ? 0.1643 0.1633 0.1753 0.0225  0.0221  0.0146  108 LEU   B C   
5639 O O   A LEU   B 108 ? 0.1629 0.1512 0.1853 0.0157  0.0317  0.0161  108 LEU   B O   
5640 O O   B LEU   B 108 ? 0.1670 0.1527 0.1676 0.0246  0.0092  0.0132  108 LEU   B O   
5641 C CB  A LEU   B 108 ? 0.1917 0.2109 0.1833 0.0143  0.0569  0.0109  108 LEU   B CB  
5642 C CB  B LEU   B 108 ? 0.1992 0.2116 0.1706 0.0150  0.0269  -0.0019 108 LEU   B CB  
5643 C CG  A LEU   B 108 ? 0.2084 0.2328 0.1898 0.0120  0.0498  -0.0037 108 LEU   B CG  
5644 C CG  B LEU   B 108 ? 0.2159 0.2307 0.1733 0.0120  0.0223  -0.0181 108 LEU   B CG  
5645 C CD1 A LEU   B 108 ? 0.2175 0.2447 0.1835 0.0052  0.0476  -0.0044 108 LEU   B CD1 
5646 C CD1 B LEU   B 108 ? 0.2228 0.2419 0.1707 0.0045  0.0220  -0.0180 108 LEU   B CD1 
5647 C CD2 A LEU   B 108 ? 0.2162 0.2403 0.1947 0.0130  0.0496  -0.0092 108 LEU   B CD2 
5648 C CD2 B LEU   B 108 ? 0.2268 0.2383 0.1844 0.0138  0.0208  -0.0218 108 LEU   B CD2 
5671 N N   . LEU   B 109 ? 0.1534 0.1460 0.1741 0.0196  0.0365  0.0214  109 LEU   B N   
5672 C CA  . LEU   B 109 ? 0.1328 0.1214 0.1817 0.0132  0.0304  0.0214  109 LEU   B CA  
5673 C C   . LEU   B 109 ? 0.1234 0.1117 0.1682 0.0017  0.0283  0.0159  109 LEU   B C   
5674 O O   . LEU   B 109 ? 0.1209 0.1088 0.1724 0.0046  0.0262  0.0233  109 LEU   B O   
5675 C CB  . LEU   B 109 ? 0.1365 0.1131 0.1868 0.0130  0.0269  0.0337  109 LEU   B CB  
5676 C CG  . LEU   B 109 ? 0.1417 0.1162 0.1828 0.0072  0.0158  0.0203  109 LEU   B CG  
5677 C CD1 . LEU   B 109 ? 0.1392 0.1264 0.1827 0.0150  0.0239  0.0190  109 LEU   B CD1 
5678 C CD2 . LEU   B 109 ? 0.1530 0.1234 0.2010 0.0072  0.0196  0.0180  109 LEU   B CD2 
5691 N N   . LYS   B 110 ? 0.1184 0.1161 0.1688 0.0033  0.0294  0.0225  110 LYS   B N   
5692 C CA  . LYS   B 110 ? 0.1183 0.1100 0.1735 0.0009  0.0223  0.0111  110 LYS   B CA  
5693 C C   . LYS   B 110 ? 0.1140 0.1080 0.1589 0.0033  0.0236  0.0091  110 LYS   B C   
5694 O O   . LYS   B 110 ? 0.1124 0.1117 0.1534 -0.0024 0.0186  0.0046  110 LYS   B O   
5695 C CB  . LYS   B 110 ? 0.1192 0.1112 0.1846 -0.0069 0.0258  -0.0011 110 LYS   B CB  
5696 C CG  . LYS   B 110 ? 0.1194 0.1124 0.2033 -0.0072 0.0135  0.0092  110 LYS   B CG  
5697 C CD  . LYS   B 110 ? 0.1187 0.1131 0.2170 -0.0071 0.0145  0.0046  110 LYS   B CD  
5698 C CE  . LYS   B 110 ? 0.1217 0.1281 0.2330 -0.0055 0.0132  0.0016  110 LYS   B CE  
5699 N NZ  . LYS   B 110 ? 0.1248 0.1415 0.2282 -0.0007 0.0062  -0.0100 110 LYS   B NZ  
5713 N N   . SER   B 111 ? 0.1199 0.1107 0.1703 0.0004  0.0285  0.0131  111 SER   B N   
5714 C CA  . SER   B 111 ? 0.1271 0.1117 0.1633 0.0046  0.0246  0.0108  111 SER   B CA  
5715 C C   . SER   B 111 ? 0.1230 0.1083 0.1530 0.0020  0.0139  0.0068  111 SER   B C   
5716 O O   . SER   B 111 ? 0.1241 0.1134 0.1617 0.0022  0.0059  0.0137  111 SER   B O   
5717 C CB  . SER   B 111 ? 0.1432 0.1347 0.1746 0.0049  0.0341  0.0209  111 SER   B CB  
5718 O OG  . SER   B 111 ? 0.1625 0.1754 0.1877 0.0078  0.0435  0.0170  111 SER   B OG  
5724 N N   . ALA   B 112 ? 0.1102 0.1081 0.1536 0.0045  0.0163  0.0141  112 ALA   B N   
5725 C CA  . ALA   B 112 ? 0.1112 0.1204 0.1501 0.0055  0.0055  0.0041  112 ALA   B CA  
5726 C C   . ALA   B 112 ? 0.0973 0.1099 0.1382 0.0074  0.0059  0.0050  112 ALA   B C   
5727 O O   . ALA   B 112 ? 0.1029 0.1069 0.1531 -0.0008 0.0085  -0.0001 112 ALA   B O   
5728 C CB  . ALA   B 112 ? 0.1138 0.1290 0.1564 0.0133  0.0042  0.0106  112 ALA   B CB  
5734 N N   . TYR   B 113 ? 0.0976 0.1021 0.1495 -0.0008 0.0091  0.0066  113 TYR   B N   
5735 C CA  . TYR   B 113 ? 0.0960 0.0957 0.1420 0.0000  0.0108  0.0024  113 TYR   B CA  
5736 C C   . TYR   B 113 ? 0.0955 0.0934 0.1464 -0.0025 0.0049  0.0006  113 TYR   B C   
5737 O O   . TYR   B 113 ? 0.1048 0.0927 0.1424 -0.0027 0.0062  -0.0014 113 TYR   B O   
5738 C CB  . TYR   B 113 ? 0.1022 0.0918 0.1557 -0.0010 0.0130  0.0031  113 TYR   B CB  
5739 C CG  . TYR   B 113 ? 0.1037 0.0963 0.1719 -0.0073 0.0060  0.0053  113 TYR   B CG  
5740 C CD1 . TYR   B 113 ? 0.1149 0.0969 0.1765 -0.0020 0.0210  0.0070  113 TYR   B CD1 
5741 C CD2 . TYR   B 113 ? 0.1148 0.0913 0.1665 -0.0051 0.0041  0.0080  113 TYR   B CD2 
5742 C CE1 . TYR   B 113 ? 0.1126 0.1024 0.1705 -0.0004 0.0221  0.0018  113 TYR   B CE1 
5743 C CE2 . TYR   B 113 ? 0.1241 0.0884 0.1790 0.0017  0.0080  0.0141  113 TYR   B CE2 
5744 C CZ  . TYR   B 113 ? 0.1101 0.0952 0.1810 0.0045  0.0061  0.0014  113 TYR   B CZ  
5745 O OH  . TYR   B 113 ? 0.1153 0.0973 0.1970 0.0126  0.0167  0.0029  113 TYR   B OH  
5755 N N   . GLU   B 114 ? 0.0993 0.0919 0.1490 0.0037  0.0112  0.0026  114 GLU   B N   
5756 C CA  . GLU   B 114 ? 0.0976 0.0890 0.1511 0.0032  0.0069  0.0003  114 GLU   B CA  
5757 C C   . GLU   B 114 ? 0.0938 0.0955 0.1403 0.0053  0.0086  -0.0074 114 GLU   B C   
5758 O O   . GLU   B 114 ? 0.0980 0.0988 0.1528 0.0053  0.0064  0.0076  114 GLU   B O   
5759 C CB  . GLU   B 114 ? 0.0989 0.0988 0.1636 0.0008  0.0124  0.0058  114 GLU   B CB  
5760 C CG  . GLU   B 114 ? 0.1039 0.1003 0.1646 0.0019  0.0137  0.0012  114 GLU   B CG  
5761 C CD  . GLU   B 114 ? 0.1010 0.1045 0.1645 -0.0042 0.0083  0.0029  114 GLU   B CD  
5762 O OE1 . GLU   B 114 ? 0.0993 0.1192 0.1681 -0.0060 0.0217  0.0029  114 GLU   B OE1 
5763 O OE2 . GLU   B 114 ? 0.1041 0.1206 0.1764 -0.0154 0.0112  0.0052  114 GLU   B OE2 
5770 N N   . ASN   B 115 ? 0.1024 0.0898 0.1407 -0.0011 0.0054  0.0007  115 ASN   B N   
5771 C CA  . ASN   B 115 ? 0.1003 0.0973 0.1352 -0.0059 0.0055  -0.0019 115 ASN   B CA  
5772 C C   . ASN   B 115 ? 0.0934 0.0905 0.1366 -0.0088 -0.0037 -0.0013 115 ASN   B C   
5773 O O   . ASN   B 115 ? 0.1089 0.0966 0.1468 -0.0122 -0.0025 -0.0046 115 ASN   B O   
5774 C CB  . ASN   B 115 ? 0.1106 0.1101 0.1358 -0.0047 0.0044  0.0004  115 ASN   B CB  
5775 C CG  . ASN   B 115 ? 0.1210 0.1132 0.1456 0.0019  -0.0033 -0.0008 115 ASN   B CG  
5776 O OD1 . ASN   B 115 ? 0.1645 0.1267 0.1745 0.0010  0.0130  -0.0177 115 ASN   B OD1 
5777 N ND2 . ASN   B 115 ? 0.1177 0.1248 0.1423 -0.0017 0.0104  0.0000  115 ASN   B ND2 
5784 N N   . PHE   B 116 ? 0.0973 0.0910 0.1320 -0.0012 0.0074  -0.0015 116 PHE   B N   
5785 C CA  . PHE   B 116 ? 0.0993 0.0980 0.1394 -0.0051 0.0038  0.0029  116 PHE   B CA  
5786 C C   . PHE   B 116 ? 0.1027 0.0874 0.1365 -0.0067 -0.0012 0.0045  116 PHE   B C   
5787 O O   . PHE   B 116 ? 0.1019 0.1003 0.1393 0.0007  -0.0003 0.0047  116 PHE   B O   
5788 C CB  . PHE   B 116 ? 0.0983 0.0951 0.1380 -0.0028 -0.0052 0.0006  116 PHE   B CB  
5789 C CG  . PHE   B 116 ? 0.0954 0.0978 0.1359 -0.0022 0.0041  -0.0005 116 PHE   B CG  
5790 C CD1 . PHE   B 116 ? 0.1011 0.1010 0.1520 -0.0035 0.0038  -0.0034 116 PHE   B CD1 
5791 C CD2 . PHE   B 116 ? 0.1074 0.1023 0.1355 0.0024  0.0082  -0.0061 116 PHE   B CD2 
5792 C CE1 . PHE   B 116 ? 0.1061 0.1065 0.1518 0.0022  -0.0063 0.0021  116 PHE   B CE1 
5793 C CE2 . PHE   B 116 ? 0.1030 0.1026 0.1391 0.0039  0.0019  0.0006  116 PHE   B CE2 
5794 C CZ  . PHE   B 116 ? 0.0952 0.1038 0.1540 0.0038  -0.0050 0.0043  116 PHE   B CZ  
5804 N N   . ASN   B 117 ? 0.0968 0.0929 0.1409 -0.0023 -0.0044 0.0015  117 ASN   B N   
5805 C CA  . ASN   B 117 ? 0.1078 0.0963 0.1335 0.0014  0.0000  -0.0016 117 ASN   B CA  
5806 C C   . ASN   B 117 ? 0.1081 0.0976 0.1500 0.0026  0.0003  0.0025  117 ASN   B C   
5807 O O   . ASN   B 117 ? 0.1186 0.0984 0.1810 -0.0004 -0.0178 0.0051  117 ASN   B O   
5808 C CB  . ASN   B 117 ? 0.1135 0.0988 0.1390 0.0009  -0.0031 -0.0054 117 ASN   B CB  
5809 C CG  . ASN   B 117 ? 0.1091 0.0961 0.1491 0.0061  -0.0001 -0.0072 117 ASN   B CG  
5810 O OD1 . ASN   B 117 ? 0.1262 0.0932 0.1695 -0.0109 0.0090  -0.0100 117 ASN   B OD1 
5811 N ND2 . ASN   B 117 ? 0.1100 0.0973 0.1552 -0.0008 0.0041  -0.0081 117 ASN   B ND2 
5818 N N   . GLN   B 118 ? 0.1066 0.0930 0.1521 -0.0016 -0.0110 -0.0043 118 GLN   B N   
5819 C CA  . GLN   B 118 ? 0.1155 0.0937 0.1593 0.0013  -0.0101 -0.0016 118 GLN   B CA  
5820 C C   . GLN   B 118 ? 0.1189 0.0947 0.1630 -0.0019 0.0002  -0.0024 118 GLN   B C   
5821 O O   . GLN   B 118 ? 0.1392 0.0926 0.1971 -0.0061 0.0098  0.0006  118 GLN   B O   
5822 C CB  . GLN   B 118 ? 0.1232 0.0997 0.1715 0.0030  -0.0150 -0.0010 118 GLN   B CB  
5823 C CG  . GLN   B 118 ? 0.1270 0.0998 0.1633 0.0070  -0.0081 -0.0126 118 GLN   B CG  
5824 C CD  . GLN   B 118 ? 0.1301 0.0977 0.1602 0.0020  -0.0057 -0.0166 118 GLN   B CD  
5825 O OE1 . GLN   B 118 ? 0.1379 0.0986 0.1786 0.0081  0.0150  0.0009  118 GLN   B OE1 
5826 N NE2 . GLN   B 118 ? 0.1414 0.1001 0.1671 0.0038  -0.0105 -0.0051 118 GLN   B NE2 
5835 N N   . HIS   B 119 ? 0.1116 0.0971 0.1320 -0.0055 -0.0012 0.0062  119 HIS   B N   
5836 C CA  . HIS   B 119 ? 0.1194 0.1076 0.1377 -0.0044 -0.0077 0.0020  119 HIS   B CA  
5837 C C   . HIS   B 119 ? 0.1243 0.1041 0.1346 -0.0039 -0.0100 0.0036  119 HIS   B C   
5838 O O   . HIS   B 119 ? 0.1378 0.1068 0.1465 -0.0195 -0.0071 0.0048  119 HIS   B O   
5839 C CB  . HIS   B 119 ? 0.1223 0.1202 0.1463 -0.0031 -0.0131 -0.0044 119 HIS   B CB  
5840 C CG  . HIS   B 119 ? 0.1326 0.1439 0.1631 0.0113  -0.0253 -0.0145 119 HIS   B CG  
5841 N ND1 . HIS   B 119 ? 0.1443 0.1613 0.1944 0.0004  -0.0372 -0.0386 119 HIS   B ND1 
5842 C CD2 . HIS   B 119 ? 0.1482 0.1626 0.1793 0.0392  -0.0330 -0.0190 119 HIS   B CD2 
5843 C CE1 . HIS   B 119 ? 0.1651 0.1746 0.2107 0.0158  -0.0446 -0.0561 119 HIS   B CE1 
5844 N NE2 . HIS   B 119 ? 0.1673 0.1861 0.1999 0.0322  -0.0437 -0.0457 119 HIS   B NE2 
5852 N N   . GLU   B 120 ? 0.1411 0.1072 0.1400 -0.0099 -0.0173 0.0042  120 GLU   B N   
5853 C CA  . GLU   B 120 ? 0.1698 0.1223 0.1514 0.0012  -0.0338 0.0181  120 GLU   B CA  
5854 C C   . GLU   B 120 ? 0.1449 0.1102 0.1437 -0.0087 -0.0218 0.0229  120 GLU   B C   
5855 O O   . GLU   B 120 ? 0.1441 0.1209 0.1422 -0.0091 -0.0184 0.0115  120 GLU   B O   
5856 C CB  . GLU   B 120 ? 0.2413 0.1617 0.2074 0.0233  -0.0663 0.0455  120 GLU   B CB  
5857 C CG  . GLU   B 120 ? 0.3012 0.2438 0.3114 0.0305  -0.0929 0.0698  120 GLU   B CG  
5858 C CD  . GLU   B 120 ? 0.3608 0.3342 0.4222 0.0318  -0.1015 0.0796  120 GLU   B CD  
5859 O OE1 . GLU   B 120 ? 0.3892 0.3687 0.4545 0.0288  -0.1001 0.0909  120 GLU   B OE1 
5860 O OE2 . GLU   B 120 ? 0.3800 0.3614 0.4695 0.0317  -0.1004 0.0709  120 GLU   B OE2 
5867 N N   . VAL   B 121 ? 0.1350 0.1101 0.1369 -0.0132 -0.0095 0.0148  121 VAL   B N   
5868 C CA  . VAL   B 121 ? 0.1361 0.1203 0.1271 -0.0127 -0.0104 0.0095  121 VAL   B CA  
5869 C C   . VAL   B 121 ? 0.1274 0.1132 0.1195 -0.0197 -0.0105 0.0040  121 VAL   B C   
5870 O O   . VAL   B 121 ? 0.1331 0.1068 0.1462 -0.0244 -0.0145 0.0048  121 VAL   B O   
5871 C CB  . VAL   B 121 ? 0.1591 0.1547 0.1316 -0.0016 -0.0127 0.0191  121 VAL   B CB  
5872 C CG1 . VAL   B 121 ? 0.1645 0.1653 0.1630 -0.0094 0.0019  0.0087  121 VAL   B CG1 
5873 C CG2 . VAL   B 121 ? 0.1755 0.1823 0.1340 0.0099  -0.0050 0.0029  121 VAL   B CG2 
5883 N N   . LEU   B 122 ? 0.1202 0.1044 0.1187 -0.0125 -0.0178 0.0039  122 LEU   B N   
5884 C CA  . LEU   B 122 ? 0.1114 0.1130 0.1134 -0.0169 -0.0107 0.0045  122 LEU   B CA  
5885 C C   . LEU   B 122 ? 0.1084 0.1023 0.1162 -0.0227 -0.0098 0.0042  122 LEU   B C   
5886 O O   . LEU   B 122 ? 0.1216 0.1066 0.1499 -0.0247 -0.0178 -0.0023 122 LEU   B O   
5887 C CB  . LEU   B 122 ? 0.1332 0.1216 0.1516 -0.0031 -0.0154 0.0062  122 LEU   B CB  
5888 C CG  . LEU   B 122 ? 0.1285 0.1221 0.1524 -0.0102 -0.0065 0.0038  122 LEU   B CG  
5889 C CD1 . LEU   B 122 ? 0.1313 0.1453 0.1632 -0.0121 -0.0071 -0.0015 122 LEU   B CD1 
5890 C CD2 . LEU   B 122 ? 0.1330 0.1286 0.1285 -0.0077 -0.0058 -0.0057 122 LEU   B CD2 
5902 N N   . LEU   B 123 ? 0.1134 0.0968 0.1206 -0.0183 -0.0055 0.0028  123 LEU   B N   
5903 C CA  . LEU   B 123 ? 0.1204 0.0979 0.1206 -0.0177 -0.0118 -0.0024 123 LEU   B CA  
5904 C C   . LEU   B 123 ? 0.1086 0.0959 0.1159 -0.0192 -0.0080 -0.0022 123 LEU   B C   
5905 O O   . LEU   B 123 ? 0.1211 0.1013 0.1334 -0.0251 -0.0116 0.0026  123 LEU   B O   
5906 C CB  . LEU   B 123 ? 0.1228 0.0998 0.1279 -0.0188 -0.0055 -0.0041 123 LEU   B CB  
5907 C CG  . LEU   B 123 ? 0.1179 0.1062 0.1488 -0.0120 0.0011  0.0074  123 LEU   B CG  
5908 C CD1 . LEU   B 123 ? 0.1255 0.1110 0.1527 -0.0102 0.0078  -0.0020 123 LEU   B CD1 
5909 C CD2 . LEU   B 123 ? 0.1208 0.1102 0.1760 -0.0133 0.0015  0.0215  123 LEU   B CD2 
5921 N N   . ALA   B 124 ? 0.1123 0.0904 0.1172 -0.0203 0.0024  -0.0018 124 ALA   B N   
5922 C CA  . ALA   B 124 ? 0.1042 0.0914 0.1285 -0.0156 -0.0005 -0.0082 124 ALA   B CA  
5923 C C   . ALA   B 124 ? 0.1023 0.0967 0.1303 -0.0114 -0.0039 -0.0078 124 ALA   B C   
5924 O O   . ALA   B 124 ? 0.1151 0.1005 0.1294 -0.0086 -0.0067 0.0033  124 ALA   B O   
5925 C CB  . ALA   B 124 ? 0.1165 0.1016 0.1289 -0.0019 0.0069  0.0028  124 ALA   B CB  
5931 N N   . PRO   B 125 ? 0.1120 0.0972 0.1260 -0.0137 -0.0121 0.0105  125 PRO   B N   
5932 C CA  . PRO   B 125 ? 0.1231 0.0985 0.1370 -0.0092 -0.0104 0.0174  125 PRO   B CA  
5933 C C   . PRO   B 125 ? 0.1151 0.0948 0.1495 -0.0085 -0.0071 0.0041  125 PRO   B C   
5934 O O   . PRO   B 125 ? 0.1202 0.0938 0.1642 -0.0057 0.0027  0.0095  125 PRO   B O   
5935 C CB  . PRO   B 125 ? 0.1271 0.1222 0.1535 -0.0170 -0.0087 0.0288  125 PRO   B CB  
5936 C CG  . PRO   B 125 ? 0.1331 0.1285 0.1424 -0.0264 -0.0141 0.0156  125 PRO   B CG  
5937 C CD  . PRO   B 125 ? 0.1242 0.1111 0.1253 -0.0258 -0.0117 0.0065  125 PRO   B CD  
5945 N N   . LEU   B 126 ? 0.1153 0.0947 0.1681 -0.0127 0.0095  0.0116  126 LEU   B N   
5946 C CA  . LEU   B 126 ? 0.1237 0.1023 0.1740 -0.0091 0.0174  0.0139  126 LEU   B CA  
5947 C C   . LEU   B 126 ? 0.1217 0.1131 0.1770 -0.0003 0.0186  0.0182  126 LEU   B C   
5948 O O   . LEU   B 126 ? 0.1419 0.1350 0.1977 0.0178  -0.0018 -0.0040 126 LEU   B O   
5949 C CB  . LEU   B 126 ? 0.1392 0.1086 0.2020 -0.0108 0.0284  0.0062  126 LEU   B CB  
5950 C CG  . LEU   B 126 ? 0.1552 0.1169 0.2069 -0.0237 0.0246  -0.0116 126 LEU   B CG  
5951 C CD1 . LEU   B 126 ? 0.1713 0.1300 0.2562 -0.0278 0.0112  -0.0250 126 LEU   B CD1 
5952 C CD2 . LEU   B 126 ? 0.1572 0.1233 0.1985 -0.0341 0.0156  -0.0101 126 LEU   B CD2 
5964 N N   . LEU   B 127 ? 0.1203 0.1004 0.1773 0.0020  0.0195  0.0117  127 LEU   B N   
5965 C CA  . LEU   B 127 ? 0.1179 0.1101 0.1764 -0.0060 0.0236  0.0174  127 LEU   B CA  
5966 C C   . LEU   B 127 ? 0.1126 0.1055 0.1720 -0.0029 0.0193  0.0142  127 LEU   B C   
5967 O O   . LEU   B 127 ? 0.1200 0.1110 0.1783 -0.0105 0.0117  0.0158  127 LEU   B O   
5968 C CB  . LEU   B 127 ? 0.1292 0.1092 0.1786 -0.0007 0.0227  0.0157  127 LEU   B CB  
5969 C CG  . LEU   B 127 ? 0.1439 0.1072 0.1921 0.0039  0.0198  0.0151  127 LEU   B CG  
5970 C CD1 . LEU   B 127 ? 0.1561 0.1060 0.1957 -0.0014 0.0132  0.0054  127 LEU   B CD1 
5971 C CD2 . LEU   B 127 ? 0.1468 0.1161 0.2071 -0.0125 0.0194  0.0277  127 LEU   B CD2 
5983 N N   . SER   B 128 ? 0.1213 0.1053 0.1763 -0.0023 0.0039  0.0127  128 SER   B N   
5984 C CA  . SER   B 128 ? 0.1289 0.1125 0.1789 0.0066  -0.0040 0.0176  128 SER   B CA  
5985 C C   . SER   B 128 ? 0.1415 0.1146 0.1951 0.0096  -0.0208 0.0134  128 SER   B C   
5986 O O   . SER   B 128 ? 0.1553 0.1229 0.2266 0.0057  -0.0180 0.0277  128 SER   B O   
5987 C CB  . SER   B 128 ? 0.1424 0.1167 0.1735 0.0065  0.0069  0.0217  128 SER   B CB  
5988 O OG  . SER   B 128 ? 0.1532 0.1310 0.1711 0.0134  0.0128  0.0257  128 SER   B OG  
5994 N N   . ALA   B 129 ? 0.1525 0.1245 0.2096 0.0261  -0.0124 0.0037  129 ALA   B N   
5995 C CA  . ALA   B 129 ? 0.1643 0.1291 0.2163 0.0306  -0.0162 -0.0108 129 ALA   B CA  
5996 C C   . ALA   B 129 ? 0.1494 0.1197 0.2120 0.0199  0.0030  -0.0052 129 ALA   B C   
5997 O O   . ALA   B 129 ? 0.1409 0.1245 0.2173 0.0173  -0.0018 0.0058  129 ALA   B O   
5998 C CB  . ALA   B 129 ? 0.1839 0.1504 0.2443 0.0360  -0.0118 -0.0180 129 ALA   B CB  
6004 N N   . GLY   B 130 ? 0.1530 0.1187 0.2181 0.0206  0.0070  -0.0067 130 GLY   B N   
6005 C CA  . GLY   B 130 ? 0.1575 0.1273 0.2160 0.0188  0.0218  -0.0081 130 GLY   B CA  
6006 C C   . GLY   B 130 ? 0.1616 0.1272 0.2129 0.0153  0.0078  0.0052  130 GLY   B C   
6007 O O   . GLY   B 130 ? 0.1813 0.1403 0.2149 0.0141  0.0089  0.0145  130 GLY   B O   
6011 N N   . ILE   B 131 ? 0.1542 0.1413 0.2237 0.0277  0.0070  0.0002  131 ILE   B N   
6012 C CA  . ILE   B 131 ? 0.1668 0.1558 0.2216 0.0255  -0.0099 0.0134  131 ILE   B CA  
6013 C C   . ILE   B 131 ? 0.1801 0.1516 0.1874 0.0172  -0.0065 0.0147  131 ILE   B C   
6014 O O   . ILE   B 131 ? 0.2075 0.1681 0.2012 0.0238  -0.0202 0.0186  131 ILE   B O   
6015 C CB  . ILE   B 131 ? 0.1686 0.1911 0.2593 0.0220  -0.0197 0.0219  131 ILE   B CB  
6016 C CG1 . ILE   B 131 ? 0.1660 0.2090 0.2743 -0.0019 -0.0086 0.0252  131 ILE   B CG1 
6017 C CG2 . ILE   B 131 ? 0.1718 0.2049 0.2815 0.0324  -0.0172 0.0160  131 ILE   B CG2 
6018 C CD1 . ILE   B 131 ? 0.1730 0.2304 0.2887 -0.0201 -0.0040 0.0273  131 ILE   B CD1 
6030 N N   . PHE   B 132 ? 0.1645 0.1351 0.1734 0.0136  0.0104  0.0172  132 PHE   B N   
6031 C CA  . PHE   B 132 ? 0.1772 0.1423 0.1616 0.0090  0.0302  0.0117  132 PHE   B CA  
6032 C C   . PHE   B 132 ? 0.1903 0.1532 0.1778 0.0104  0.0323  0.0115  132 PHE   B C   
6033 O O   . PHE   B 132 ? 0.2114 0.1736 0.2089 0.0049  0.0455  0.0193  132 PHE   B O   
6034 C CB  . PHE   B 132 ? 0.1606 0.1382 0.1542 0.0100  0.0209  0.0202  132 PHE   B CB  
6035 C CG  . PHE   B 132 ? 0.1618 0.1428 0.1660 0.0143  0.0225  0.0187  132 PHE   B CG  
6036 C CD1 . PHE   B 132 ? 0.1691 0.1444 0.2082 0.0152  0.0252  0.0191  132 PHE   B CD1 
6037 C CD2 . PHE   B 132 ? 0.1545 0.1408 0.1450 0.0232  0.0192  0.0186  132 PHE   B CD2 
6038 C CE1 . PHE   B 132 ? 0.1710 0.1457 0.2127 0.0113  0.0191  0.0159  132 PHE   B CE1 
6039 C CE2 . PHE   B 132 ? 0.1614 0.1451 0.1656 0.0186  0.0079  0.0141  132 PHE   B CE2 
6040 C CZ  . PHE   B 132 ? 0.1673 0.1429 0.2035 0.0098  -0.0005 0.0154  132 PHE   B CZ  
6050 N N   . GLY   B 133 ? 0.1898 0.1443 0.1751 0.0099  0.0205  0.0284  133 GLY   B N   
6051 C CA  . GLY   B 133 ? 0.2002 0.1539 0.1904 -0.0106 0.0178  0.0337  133 GLY   B CA  
6052 C C   . GLY   B 133 ? 0.2038 0.1610 0.1937 -0.0221 0.0204  0.0333  133 GLY   B C   
6053 O O   . GLY   B 133 ? 0.2213 0.1732 0.2306 -0.0375 0.0206  0.0504  133 GLY   B O   
6057 N N   . ALA   B 134 ? 0.1865 0.1611 0.1819 -0.0213 0.0225  0.0204  134 ALA   B N   
6058 C CA  . ALA   B 134 ? 0.1776 0.1597 0.1978 -0.0161 0.0293  0.0056  134 ALA   B CA  
6059 C C   . ALA   B 134 ? 0.1790 0.1482 0.2058 -0.0021 0.0276  0.0164  134 ALA   B C   
6060 O O   . ALA   B 134 ? 0.1823 0.1711 0.2248 0.0055  0.0300  0.0076  134 ALA   B O   
6061 C CB  . ALA   B 134 ? 0.1754 0.1592 0.2252 -0.0066 0.0168  -0.0037 134 ALA   B CB  
6067 N N   . ASP   B 135 ? 0.1916 0.1384 0.2002 -0.0087 0.0112  0.0261  135 ASP   B N   
6068 C CA  . ASP   B 135 ? 0.2087 0.1321 0.2208 -0.0096 -0.0020 0.0285  135 ASP   B CA  
6069 C C   . ASP   B 135 ? 0.1951 0.1254 0.2106 -0.0002 0.0028  0.0201  135 ASP   B C   
6070 O O   . ASP   B 135 ? 0.1884 0.1210 0.2190 0.0013  0.0112  0.0286  135 ASP   B O   
6071 C CB  . ASP   B 135 ? 0.2382 0.1458 0.2526 -0.0322 0.0001  0.0302  135 ASP   B CB  
6072 C CG  . ASP   B 135 ? 0.2708 0.1504 0.2938 -0.0500 0.0017  0.0257  135 ASP   B CG  
6073 O OD1 . ASP   B 135 ? 0.2815 0.1365 0.2827 -0.0342 -0.0031 0.0230  135 ASP   B OD1 
6074 O OD2 . ASP   B 135 ? 0.2956 0.1875 0.3436 -0.0638 -0.0070 0.0062  135 ASP   B OD2 
6079 N N   . PRO   B 136 ? 0.1901 0.1262 0.2153 0.0166  -0.0028 0.0161  136 PRO   B N   
6080 C CA  . PRO   B 136 ? 0.1714 0.1190 0.2079 0.0147  -0.0072 0.0027  136 PRO   B CA  
6081 C C   . PRO   B 136 ? 0.1522 0.1087 0.2191 0.0121  -0.0011 0.0004  136 PRO   B C   
6082 O O   . PRO   B 136 ? 0.1381 0.1068 0.2105 0.0110  0.0073  0.0034  136 PRO   B O   
6083 C CB  . PRO   B 136 ? 0.1806 0.1440 0.2223 0.0233  -0.0148 -0.0075 136 PRO   B CB  
6084 C CG  . PRO   B 136 ? 0.1994 0.1482 0.2422 0.0295  -0.0133 -0.0054 136 PRO   B CG  
6085 C CD  . PRO   B 136 ? 0.1974 0.1394 0.2312 0.0329  -0.0041 0.0043  136 PRO   B CD  
6093 N N   . ILE   B 137 ? 0.1585 0.1045 0.2297 0.0127  -0.0076 0.0070  137 ILE   B N   
6094 C CA  . ILE   B 137 ? 0.1681 0.1035 0.2337 -0.0010 0.0003  -0.0000 137 ILE   B CA  
6095 C C   . ILE   B 137 ? 0.1589 0.1071 0.2179 -0.0079 0.0096  0.0106  137 ILE   B C   
6096 O O   . ILE   B 137 ? 0.1485 0.1096 0.2253 -0.0077 0.0013  0.0052  137 ILE   B O   
6097 C CB  . ILE   B 137 ? 0.1963 0.1113 0.2779 -0.0035 0.0015  0.0003  137 ILE   B CB  
6098 C CG1 . ILE   B 137 ? 0.2289 0.1258 0.3267 0.0058  0.0057  -0.0166 137 ILE   B CG1 
6099 C CG2 . ILE   B 137 ? 0.2002 0.1111 0.2947 -0.0266 -0.0021 0.0047  137 ILE   B CG2 
6100 C CD1 . ILE   B 137 ? 0.2526 0.1517 0.3722 0.0228  0.0044  -0.0064 137 ILE   B CD1 
6112 N N   . HIS   B 138 ? 0.1686 0.1066 0.2147 -0.0037 0.0156  0.0159  138 HIS   B N   
6113 C CA  . HIS   B 138 ? 0.1768 0.1156 0.2172 -0.0043 0.0258  0.0083  138 HIS   B CA  
6114 C C   . HIS   B 138 ? 0.1592 0.1133 0.2002 -0.0008 0.0283  0.0125  138 HIS   B C   
6115 O O   . HIS   B 138 ? 0.1498 0.1200 0.2232 0.0087  0.0327  0.0283  138 HIS   B O   
6116 C CB  . HIS   B 138 ? 0.1983 0.1260 0.2243 -0.0034 0.0340  0.0106  138 HIS   B CB  
6117 C CG  . HIS   B 138 ? 0.2156 0.1493 0.2165 -0.0091 0.0521  0.0268  138 HIS   B CG  
6118 N ND1 . HIS   B 138 ? 0.2222 0.1696 0.2420 -0.0081 0.0642  0.0173  138 HIS   B ND1 
6119 C CD2 . HIS   B 138 ? 0.2312 0.1606 0.2146 -0.0090 0.0586  0.0182  138 HIS   B CD2 
6120 C CE1 . HIS   B 138 ? 0.2307 0.1681 0.2351 -0.0064 0.0712  0.0167  138 HIS   B CE1 
6121 N NE2 . HIS   B 138 ? 0.2394 0.1570 0.2274 0.0002  0.0655  0.0102  138 HIS   B NE2 
6129 N N   . SER   B 139 ? 0.1539 0.1012 0.1990 0.0032  0.0195  0.0041  139 SER   B N   
6130 C CA  . SER   B 139 ? 0.1453 0.1001 0.1987 -0.0000 0.0203  0.0002  139 SER   B CA  
6131 C C   . SER   B 139 ? 0.1238 0.0950 0.1865 0.0008  0.0155  -0.0020 139 SER   B C   
6132 O O   . SER   B 139 ? 0.1281 0.0951 0.1893 0.0014  0.0079  0.0014  139 SER   B O   
6133 C CB  . SER   B 139 ? 0.1522 0.1022 0.2055 0.0028  0.0147  0.0015  139 SER   B CB  
6134 O OG  . SER   B 139 ? 0.1621 0.1010 0.2112 0.0030  -0.0010 0.0088  139 SER   B OG  
6140 N N   . LEU   B 140 ? 0.1270 0.0899 0.1894 -0.0061 0.0208  -0.0064 140 LEU   B N   
6141 C CA  . LEU   B 140 ? 0.1236 0.0927 0.1973 0.0006  0.0140  0.0003  140 LEU   B CA  
6142 C C   . LEU   B 140 ? 0.1233 0.0919 0.2020 0.0000  0.0063  -0.0052 140 LEU   B C   
6143 O O   . LEU   B 140 ? 0.1203 0.0980 0.1978 -0.0017 0.0037  0.0012  140 LEU   B O   
6144 C CB  . LEU   B 140 ? 0.1197 0.0937 0.2058 -0.0072 0.0192  -0.0067 140 LEU   B CB  
6145 C CG  . LEU   B 140 ? 0.1322 0.0966 0.1893 -0.0083 0.0060  0.0020  140 LEU   B CG  
6146 C CD1 . LEU   B 140 ? 0.1406 0.1033 0.1993 -0.0123 0.0105  -0.0027 140 LEU   B CD1 
6147 C CD2 . LEU   B 140 ? 0.1530 0.1045 0.2060 -0.0109 -0.0019 -0.0098 140 LEU   B CD2 
6159 N N   . ARG   B 141 ? 0.1137 0.0976 0.2108 -0.0034 0.0127  -0.0075 141 ARG   B N   
6160 C CA  . ARG   B 141 ? 0.1159 0.1001 0.2466 -0.0120 0.0239  -0.0063 141 ARG   B CA  
6161 C C   . ARG   B 141 ? 0.1112 0.1045 0.2251 -0.0144 0.0112  -0.0006 141 ARG   B C   
6162 O O   . ARG   B 141 ? 0.1201 0.1026 0.2191 -0.0140 0.0050  -0.0107 141 ARG   B O   
6163 C CB  . ARG   B 141 ? 0.1307 0.1088 0.2776 -0.0171 0.0343  -0.0076 141 ARG   B CB  
6164 C CG  . ARG   B 141 ? 0.1672 0.1419 0.3113 -0.0230 0.0349  -0.0039 141 ARG   B CG  
6165 C CD  . ARG   B 141 ? 0.2088 0.1577 0.3147 -0.0160 0.0221  -0.0128 141 ARG   B CD  
6166 N NE  . ARG   B 141 ? 0.2306 0.1569 0.3127 -0.0378 0.0297  -0.0135 141 ARG   B NE  
6167 C CZ  . ARG   B 141 ? 0.2438 0.1459 0.2977 -0.0269 0.0428  -0.0275 141 ARG   B CZ  
6168 N NH1 . ARG   B 141 ? 0.2512 0.1356 0.3016 -0.0307 0.0437  -0.0300 141 ARG   B NH1 
6169 N NH2 . ARG   B 141 ? 0.2538 0.1566 0.3021 -0.0102 0.0329  -0.0225 141 ARG   B NH2 
6183 N N   . VAL   B 142 ? 0.1126 0.0977 0.2121 -0.0092 0.0168  -0.0055 142 VAL   B N   
6184 C CA  . VAL   B 142 ? 0.1106 0.0981 0.2079 -0.0015 0.0230  -0.0058 142 VAL   B CA  
6185 C C   . VAL   B 142 ? 0.1057 0.0994 0.2095 -0.0015 0.0146  -0.0084 142 VAL   B C   
6186 O O   . VAL   B 142 ? 0.1146 0.0991 0.2172 0.0039  0.0177  -0.0054 142 VAL   B O   
6187 C CB  . VAL   B 142 ? 0.1224 0.1077 0.2132 0.0038  0.0224  0.0060  142 VAL   B CB  
6188 C CG1 . VAL   B 142 ? 0.1265 0.1084 0.2143 0.0094  0.0257  0.0002  142 VAL   B CG1 
6189 C CG2 . VAL   B 142 ? 0.1433 0.1123 0.2085 -0.0031 0.0237  0.0083  142 VAL   B CG2 
6199 N N   . CYS   B 143 ? 0.1072 0.0948 0.1990 0.0014  0.0064  0.0022  143 CYS   B N   
6200 C CA  . CYS   B 143 ? 0.1090 0.0958 0.2046 -0.0025 0.0045  0.0035  143 CYS   B CA  
6201 C C   . CYS   B 143 ? 0.1043 0.0923 0.1996 -0.0033 0.0106  -0.0053 143 CYS   B C   
6202 O O   . CYS   B 143 ? 0.1047 0.1018 0.2006 -0.0057 0.0026  -0.0058 143 CYS   B O   
6203 C CB  . CYS   B 143 ? 0.1096 0.1074 0.1958 0.0001  0.0021  -0.0080 143 CYS   B CB  
6204 S SG  . CYS   B 143 ? 0.1156 0.1198 0.1915 -0.0032 0.0105  0.0024  143 CYS   B SG  
6210 N N   . VAL   B 144 ? 0.1139 0.0983 0.1939 -0.0053 0.0081  -0.0153 144 VAL   B N   
6211 C CA  . VAL   B 144 ? 0.1182 0.1080 0.2200 -0.0114 -0.0010 -0.0213 144 VAL   B CA  
6212 C C   . VAL   B 144 ? 0.1148 0.1055 0.2216 -0.0104 -0.0054 -0.0104 144 VAL   B C   
6213 O O   . VAL   B 144 ? 0.1268 0.1261 0.2448 0.0044  0.0000  0.0105  144 VAL   B O   
6214 C CB  . VAL   B 144 ? 0.1454 0.1164 0.2821 -0.0099 -0.0115 -0.0338 144 VAL   B CB  
6215 C CG1 . VAL   B 144 ? 0.1667 0.1518 0.3284 -0.0055 -0.0224 -0.0326 144 VAL   B CG1 
6216 C CG2 . VAL   B 144 ? 0.1593 0.1107 0.2784 0.0093  -0.0310 -0.0454 144 VAL   B CG2 
6226 N N   . ASP   B 145 ? 0.1164 0.1023 0.2313 -0.0059 -0.0034 -0.0085 145 ASP   B N   
6227 C CA  . ASP   B 145 ? 0.1091 0.1070 0.2544 -0.0055 0.0035  -0.0131 145 ASP   B CA  
6228 C C   . ASP   B 145 ? 0.1038 0.1105 0.2390 -0.0033 0.0097  -0.0124 145 ASP   B C   
6229 O O   . ASP   B 145 ? 0.1084 0.1269 0.3005 -0.0075 0.0142  -0.0329 145 ASP   B O   
6230 C CB  . ASP   B 145 ? 0.1236 0.1125 0.2982 -0.0163 0.0173  -0.0114 145 ASP   B CB  
6231 C CG  . ASP   B 145 ? 0.1393 0.1215 0.3457 -0.0193 0.0310  -0.0010 145 ASP   B CG  
6232 O OD1 . ASP   B 145 ? 0.1470 0.1252 0.3568 -0.0156 -0.0047 -0.0189 145 ASP   B OD1 
6233 O OD2 . ASP   B 145 ? 0.1660 0.1345 0.3911 -0.0242 0.0490  0.0094  145 ASP   B OD2 
6238 N N   . THR   B 146 ? 0.1033 0.1056 0.1933 -0.0044 0.0088  -0.0022 146 THR   B N   
6239 C CA  . THR   B 146 ? 0.1115 0.1018 0.1833 -0.0063 0.0104  -0.0054 146 THR   B CA  
6240 C C   . THR   B 146 ? 0.1097 0.0957 0.1798 0.0006  0.0080  -0.0018 146 THR   B C   
6241 O O   . THR   B 146 ? 0.1122 0.1016 0.1860 -0.0009 0.0044  0.0002  146 THR   B O   
6242 C CB  . THR   B 146 ? 0.1187 0.0975 0.1948 -0.0002 0.0215  0.0001  146 THR   B CB  
6243 O OG1 . THR   B 146 ? 0.1213 0.0963 0.2114 -0.0024 0.0247  0.0064  146 THR   B OG1 
6244 C CG2 . THR   B 146 ? 0.1260 0.1046 0.1868 -0.0027 0.0184  0.0030  146 THR   B CG2 
6252 N N   . VAL   B 147 ? 0.1132 0.0999 0.1810 -0.0029 0.0132  0.0023  147 VAL   B N   
6253 C CA  . VAL   B 147 ? 0.1162 0.0952 0.1695 -0.0091 0.0063  -0.0043 147 VAL   B CA  
6254 C C   . VAL   B 147 ? 0.1100 0.0983 0.1763 -0.0130 -0.0025 -0.0085 147 VAL   B C   
6255 O O   . VAL   B 147 ? 0.1195 0.1108 0.1876 -0.0181 -0.0217 -0.0132 147 VAL   B O   
6256 C CB  . VAL   B 147 ? 0.1167 0.1071 0.1585 -0.0031 -0.0054 -0.0044 147 VAL   B CB  
6257 C CG1 . VAL   B 147 ? 0.1175 0.1229 0.1579 -0.0074 -0.0050 -0.0021 147 VAL   B CG1 
6258 C CG2 . VAL   B 147 ? 0.1225 0.1090 0.1567 -0.0096 0.0056  -0.0023 147 VAL   B CG2 
6268 N N   . ARG   B 148 ? 0.1105 0.1012 0.1718 -0.0091 -0.0118 -0.0158 148 ARG   B N   
6269 C CA  . ARG   B 148 ? 0.1151 0.1107 0.1677 -0.0095 -0.0200 -0.0129 148 ARG   B CA  
6270 C C   . ARG   B 148 ? 0.1205 0.1171 0.1651 -0.0075 -0.0179 -0.0065 148 ARG   B C   
6271 O O   . ARG   B 148 ? 0.1403 0.1424 0.1642 -0.0205 -0.0252 0.0000  148 ARG   B O   
6272 C CB  . ARG   B 148 ? 0.1174 0.1188 0.1700 -0.0005 -0.0221 -0.0178 148 ARG   B CB  
6273 C CG  . ARG   B 148 ? 0.1173 0.1355 0.1857 -0.0094 -0.0134 -0.0361 148 ARG   B CG  
6274 C CD  . ARG   B 148 ? 0.1241 0.1527 0.1999 0.0076  -0.0190 -0.0344 148 ARG   B CD  
6275 N NE  . ARG   B 148 ? 0.1300 0.1474 0.1865 0.0240  -0.0171 -0.0332 148 ARG   B NE  
6276 C CZ  . ARG   B 148 ? 0.1233 0.1407 0.1633 0.0120  -0.0098 -0.0265 148 ARG   B CZ  
6277 N NH1 . ARG   B 148 ? 0.1180 0.1479 0.1748 -0.0025 0.0089  -0.0220 148 ARG   B NH1 
6278 N NH2 . ARG   B 148 ? 0.1514 0.1261 0.1586 0.0158  -0.0130 -0.0150 148 ARG   B NH2 
6292 N N   . THR   B 149 ? 0.1201 0.1127 0.1616 -0.0091 -0.0171 -0.0073 149 THR   B N   
6293 C CA  . THR   B 149 ? 0.1251 0.1147 0.1590 -0.0140 -0.0136 0.0053  149 THR   B CA  
6294 C C   . THR   B 149 ? 0.1211 0.1117 0.1448 -0.0121 -0.0238 0.0023  149 THR   B C   
6295 O O   . THR   B 149 ? 0.1289 0.1059 0.1602 -0.0158 -0.0133 0.0000  149 THR   B O   
6296 C CB  . THR   B 149 ? 0.1261 0.1141 0.1626 -0.0139 -0.0209 0.0028  149 THR   B CB  
6297 O OG1 . THR   B 149 ? 0.1296 0.1202 0.1516 -0.0192 -0.0212 -0.0012 149 THR   B OG1 
6298 C CG2 . THR   B 149 ? 0.1327 0.1161 0.1738 -0.0061 -0.0118 0.0061  149 THR   B CG2 
6306 N N   . ASN   B 150 ? 0.1284 0.1140 0.1495 -0.0109 -0.0235 -0.0029 150 ASN   B N   
6307 C CA  . ASN   B 150 ? 0.1374 0.1234 0.1455 -0.0128 -0.0191 -0.0088 150 ASN   B CA  
6308 C C   . ASN   B 150 ? 0.1235 0.1179 0.1495 -0.0132 -0.0197 -0.0038 150 ASN   B C   
6309 O O   . ASN   B 150 ? 0.1379 0.1151 0.1686 -0.0221 -0.0359 -0.0027 150 ASN   B O   
6310 C CB  . ASN   B 150 ? 0.1586 0.1591 0.1461 -0.0122 -0.0264 0.0049  150 ASN   B CB  
6311 C CG  . ASN   B 150 ? 0.1854 0.2006 0.1767 -0.0153 -0.0337 0.0163  150 ASN   B CG  
6312 O OD1 . ASN   B 150 ? 0.1935 0.2142 0.1993 -0.0256 -0.0513 0.0014  150 ASN   B OD1 
6313 N ND2 . ASN   B 150 ? 0.1961 0.2186 0.2217 -0.0054 -0.0381 0.0533  150 ASN   B ND2 
6320 N N   . VAL   B 151 ? 0.1161 0.1143 0.1465 -0.0126 -0.0180 -0.0011 151 VAL   B N   
6321 C CA  . VAL   B 151 ? 0.1156 0.1156 0.1493 -0.0187 -0.0124 0.0008  151 VAL   B CA  
6322 C C   . VAL   B 151 ? 0.1261 0.1026 0.1420 -0.0246 -0.0181 -0.0021 151 VAL   B C   
6323 O O   . VAL   B 151 ? 0.1309 0.1160 0.1660 -0.0235 -0.0174 -0.0084 151 VAL   B O   
6324 C CB  . VAL   B 151 ? 0.1380 0.1358 0.1666 -0.0049 -0.0119 -0.0059 151 VAL   B CB  
6325 C CG1 . VAL   B 151 ? 0.1502 0.1369 0.1937 -0.0122 0.0014  -0.0135 151 VAL   B CG1 
6326 C CG2 . VAL   B 151 ? 0.1478 0.1461 0.1695 0.0028  -0.0133 -0.0013 151 VAL   B CG2 
6336 N N   . TYR   B 152 ? 0.1219 0.0981 0.1373 -0.0197 -0.0112 -0.0041 152 TYR   B N   
6337 C CA  . TYR   B 152 ? 0.1243 0.1132 0.1360 -0.0234 -0.0064 -0.0074 152 TYR   B CA  
6338 C C   . TYR   B 152 ? 0.1159 0.1010 0.1275 -0.0185 -0.0073 -0.0070 152 TYR   B C   
6339 O O   . TYR   B 152 ? 0.1226 0.1060 0.1349 -0.0207 -0.0080 -0.0043 152 TYR   B O   
6340 C CB  . TYR   B 152 ? 0.1356 0.1227 0.1465 -0.0195 -0.0110 0.0027  152 TYR   B CB  
6341 C CG  . TYR   B 152 ? 0.1516 0.1338 0.1360 -0.0298 -0.0151 0.0029  152 TYR   B CG  
6342 C CD1 . TYR   B 152 ? 0.1611 0.1454 0.1311 -0.0216 -0.0201 0.0032  152 TYR   B CD1 
6343 C CD2 . TYR   B 152 ? 0.1736 0.1470 0.1368 -0.0257 -0.0127 0.0033  152 TYR   B CD2 
6344 C CE1 . TYR   B 152 ? 0.1794 0.1624 0.1396 -0.0184 -0.0203 0.0166  152 TYR   B CE1 
6345 C CE2 . TYR   B 152 ? 0.1835 0.1635 0.1432 -0.0261 -0.0149 -0.0028 152 TYR   B CE2 
6346 C CZ  . TYR   B 152 ? 0.1859 0.1813 0.1392 -0.0240 -0.0305 0.0197  152 TYR   B CZ  
6347 O OH  . TYR   B 152 ? 0.2071 0.2189 0.1686 -0.0171 -0.0332 0.0207  152 TYR   B OH  
6357 N N   . LEU   B 153 ? 0.1197 0.1015 0.1338 -0.0241 -0.0103 -0.0042 153 LEU   B N   
6358 C CA  . LEU   B 153 ? 0.1254 0.0975 0.1278 -0.0152 -0.0032 -0.0085 153 LEU   B CA  
6359 C C   . LEU   B 153 ? 0.1240 0.0976 0.1376 -0.0191 -0.0043 -0.0090 153 LEU   B C   
6360 O O   . LEU   B 153 ? 0.1304 0.1147 0.1570 -0.0086 -0.0059 -0.0284 153 LEU   B O   
6361 C CB  . LEU   B 153 ? 0.1248 0.1015 0.1435 -0.0195 0.0004  -0.0061 153 LEU   B CB  
6362 C CG  . LEU   B 153 ? 0.1216 0.1101 0.1615 -0.0193 0.0004  -0.0053 153 LEU   B CG  
6363 C CD1 . LEU   B 153 ? 0.1297 0.1243 0.1695 -0.0211 0.0048  -0.0021 153 LEU   B CD1 
6364 C CD2 . LEU   B 153 ? 0.1300 0.1249 0.1702 -0.0201 0.0162  -0.0033 153 LEU   B CD2 
6376 N N   . ALA   B 154 ? 0.1203 0.1005 0.1511 -0.0072 -0.0083 -0.0071 154 ALA   B N   
6377 C CA  . ALA   B 154 ? 0.1298 0.1115 0.1666 0.0007  -0.0129 -0.0152 154 ALA   B CA  
6378 C C   . ALA   B 154 ? 0.1427 0.1125 0.1658 0.0055  -0.0147 -0.0203 154 ALA   B C   
6379 O O   . ALA   B 154 ? 0.1729 0.1154 0.1831 0.0065  -0.0018 -0.0047 154 ALA   B O   
6380 C CB  . ALA   B 154 ? 0.1275 0.1273 0.1931 -0.0019 -0.0109 -0.0210 154 ALA   B CB  
6386 N N   . VAL   B 155 ? 0.1159 0.1054 0.1765 -0.0008 0.0003  -0.0130 155 VAL   B N   
6387 C CA  . VAL   B 155 ? 0.1138 0.1073 0.1913 0.0010  -0.0072 -0.0034 155 VAL   B CA  
6388 C C   . VAL   B 155 ? 0.1131 0.1034 0.1829 0.0004  -0.0106 -0.0132 155 VAL   B C   
6389 O O   . VAL   B 155 ? 0.1315 0.1221 0.2113 0.0004  -0.0032 -0.0230 155 VAL   B O   
6390 C CB  . VAL   B 155 ? 0.1200 0.1178 0.2283 -0.0046 -0.0188 0.0039  155 VAL   B CB  
6391 C CG1 . VAL   B 155 ? 0.1226 0.1167 0.2313 -0.0097 -0.0137 0.0005  155 VAL   B CG1 
6392 C CG2 . VAL   B 155 ? 0.1161 0.1306 0.2606 -0.0120 -0.0126 0.0255  155 VAL   B CG2 
6402 N N   . PHE   B 156 ? 0.1065 0.1165 0.1926 0.0030  -0.0030 -0.0097 156 PHE   B N   
6403 C CA  . PHE   B 156 ? 0.1071 0.1237 0.2293 0.0054  -0.0008 -0.0098 156 PHE   B CA  
6404 C C   . PHE   B 156 ? 0.1069 0.1305 0.2563 0.0102  -0.0083 -0.0270 156 PHE   B C   
6405 O O   . PHE   B 156 ? 0.1308 0.1472 0.2843 0.0237  0.0016  -0.0306 156 PHE   B O   
6406 C CB  . PHE   B 156 ? 0.1169 0.1214 0.2414 -0.0004 -0.0142 -0.0069 156 PHE   B CB  
6407 C CG  . PHE   B 156 ? 0.1157 0.1328 0.2563 -0.0030 -0.0122 0.0137  156 PHE   B CG  
6408 C CD1 . PHE   B 156 ? 0.1170 0.1595 0.2936 0.0004  -0.0034 0.0444  156 PHE   B CD1 
6409 C CD2 . PHE   B 156 ? 0.1212 0.1427 0.2577 0.0115  -0.0220 0.0193  156 PHE   B CD2 
6410 C CE1 . PHE   B 156 ? 0.1239 0.1779 0.3101 0.0052  -0.0022 0.0450  156 PHE   B CE1 
6411 C CE2 . PHE   B 156 ? 0.1322 0.1633 0.2765 0.0125  -0.0158 0.0256  156 PHE   B CE2 
6412 C CZ  . PHE   B 156 ? 0.1233 0.1788 0.3052 0.0144  -0.0196 0.0344  156 PHE   B CZ  
6422 N N   . ASP   B 157 ? 0.1117 0.1150 0.2712 0.0105  -0.0167 -0.0135 157 ASP   B N   
6423 C CA  . ASP   B 157 ? 0.1182 0.1233 0.3001 0.0063  -0.0268 -0.0212 157 ASP   B CA  
6424 C C   . ASP   B 157 ? 0.1193 0.1174 0.3036 0.0079  -0.0197 -0.0428 157 ASP   B C   
6425 O O   . ASP   B 157 ? 0.1162 0.1229 0.2858 0.0036  -0.0180 -0.0361 157 ASP   B O   
6426 C CB  . ASP   B 157 ? 0.1455 0.1435 0.3198 0.0048  -0.0407 -0.0059 157 ASP   B CB  
6427 C CG  . ASP   B 157 ? 0.1712 0.1565 0.3478 -0.0028 -0.0217 -0.0109 157 ASP   B CG  
6428 O OD1 . ASP   B 157 ? 0.1797 0.1471 0.3660 0.0029  -0.0179 -0.0127 157 ASP   B OD1 
6429 O OD2 . ASP   B 157 ? 0.1976 0.1799 0.3760 -0.0061 -0.0016 -0.0077 157 ASP   B OD2 
6434 N N   . LYS   B 158 ? 0.1233 0.1378 0.3190 0.0062  -0.0009 -0.0608 158 LYS   B N   
6435 C CA  . LYS   B 158 ? 0.1390 0.1561 0.3293 0.0048  0.0057  -0.0715 158 LYS   B CA  
6436 C C   . LYS   B 158 ? 0.1366 0.1408 0.3290 0.0098  0.0033  -0.0670 158 LYS   B C   
6437 O O   . LYS   B 158 ? 0.1454 0.1396 0.3289 -0.0035 -0.0035 -0.0683 158 LYS   B O   
6438 C CB  . LYS   B 158 ? 0.1621 0.1897 0.3378 0.0048  0.0135  -0.0904 158 LYS   B CB  
6439 C CG  . LYS   B 158 ? 0.1939 0.2177 0.3479 0.0097  0.0214  -0.0971 158 LYS   B CG  
6440 C CD  . LYS   B 158 ? 0.2222 0.2556 0.3653 0.0074  0.0299  -0.0924 158 LYS   B CD  
6441 C CE  . LYS   B 158 ? 0.2392 0.2822 0.3857 0.0071  0.0279  -0.0816 158 LYS   B CE  
6442 N NZ  . LYS   B 158 ? 0.2340 0.2924 0.3866 0.0062  0.0292  -0.0779 158 LYS   B NZ  
6456 N N   . ASN   B 159 ? 0.1427 0.1303 0.3491 0.0089  -0.0022 -0.0525 159 ASN   B N   
6457 C CA  . ASN   B 159 ? 0.1533 0.1304 0.3744 0.0178  -0.0141 -0.0414 159 ASN   B CA  
6458 C C   . ASN   B 159 ? 0.1385 0.1173 0.3555 0.0125  -0.0290 -0.0366 159 ASN   B C   
6459 O O   . ASN   B 159 ? 0.1406 0.1210 0.3726 -0.0058 -0.0289 -0.0293 159 ASN   B O   
6460 C CB  . ASN   B 159 ? 0.1700 0.1436 0.4150 0.0265  -0.0220 -0.0405 159 ASN   B CB  
6461 C CG  . ASN   B 159 ? 0.1951 0.1638 0.4481 0.0248  -0.0370 -0.0596 159 ASN   B CG  
6462 O OD1 . ASN   B 159 ? 0.2088 0.1784 0.4500 0.0319  -0.0390 -0.0812 159 ASN   B OD1 
6463 N ND2 . ASN   B 159 ? 0.1988 0.1747 0.4611 0.0383  -0.0430 -0.0505 159 ASN   B ND2 
6470 N N   . LEU   B 160 ? 0.1256 0.1180 0.3297 0.0046  -0.0317 -0.0297 160 LEU   B N   
6471 C CA  . LEU   B 160 ? 0.1193 0.1228 0.2905 0.0046  -0.0299 -0.0154 160 LEU   B CA  
6472 C C   . LEU   B 160 ? 0.1193 0.1130 0.2728 -0.0001 -0.0184 -0.0303 160 LEU   B C   
6473 O O   . LEU   B 160 ? 0.1137 0.1182 0.2562 -0.0039 -0.0172 -0.0182 160 LEU   B O   
6474 C CB  . LEU   B 160 ? 0.1201 0.1316 0.2778 0.0035  -0.0295 -0.0067 160 LEU   B CB  
6475 C CG  . LEU   B 160 ? 0.1266 0.1456 0.2633 0.0071  -0.0314 -0.0048 160 LEU   B CG  
6476 C CD1 . LEU   B 160 ? 0.1384 0.1663 0.2477 -0.0062 -0.0180 -0.0111 160 LEU   B CD1 
6477 C CD2 . LEU   B 160 ? 0.1307 0.1466 0.2670 0.0206  -0.0255 -0.0175 160 LEU   B CD2 
6489 N N   . TYR   B 161 ? 0.1122 0.1201 0.2831 -0.0054 -0.0020 -0.0354 161 TYR   B N   
6490 C CA  . TYR   B 161 ? 0.1251 0.1195 0.2677 -0.0103 0.0116  -0.0373 161 TYR   B CA  
6491 C C   . TYR   B 161 ? 0.1263 0.1208 0.2491 -0.0082 0.0121  -0.0334 161 TYR   B C   
6492 O O   . TYR   B 161 ? 0.1321 0.1238 0.2374 -0.0139 0.0008  -0.0310 161 TYR   B O   
6493 C CB  . TYR   B 161 ? 0.1419 0.1255 0.2725 -0.0172 0.0246  -0.0346 161 TYR   B CB  
6494 C CG  . TYR   B 161 ? 0.1592 0.1320 0.2638 -0.0230 0.0339  -0.0460 161 TYR   B CG  
6495 C CD1 . TYR   B 161 ? 0.1680 0.1286 0.2534 -0.0326 0.0444  -0.0380 161 TYR   B CD1 
6496 C CD2 . TYR   B 161 ? 0.1821 0.1427 0.2595 -0.0216 0.0319  -0.0518 161 TYR   B CD2 
6497 C CE1 . TYR   B 161 ? 0.1875 0.1433 0.2675 -0.0354 0.0329  -0.0414 161 TYR   B CE1 
6498 C CE2 . TYR   B 161 ? 0.2005 0.1604 0.2780 -0.0281 0.0279  -0.0471 161 TYR   B CE2 
6499 C CZ  . TYR   B 161 ? 0.1994 0.1586 0.2746 -0.0411 0.0237  -0.0371 161 TYR   B CZ  
6500 O OH  . TYR   B 161 ? 0.2243 0.1807 0.2917 -0.0357 0.0216  -0.0296 161 TYR   B OH  
6510 N N   . ASP   B 162 ? 0.1296 0.1191 0.2764 -0.0068 0.0037  -0.0420 162 ASP   B N   
6511 C CA  . ASP   B 162 ? 0.1430 0.1254 0.2811 -0.0043 -0.0062 -0.0506 162 ASP   B CA  
6512 C C   . ASP   B 162 ? 0.1376 0.1166 0.2718 -0.0071 -0.0115 -0.0440 162 ASP   B C   
6513 O O   . ASP   B 162 ? 0.1471 0.1264 0.2649 -0.0140 -0.0194 -0.0320 162 ASP   B O   
6514 C CB  . ASP   B 162 ? 0.1652 0.1464 0.3027 0.0063  -0.0104 -0.0697 162 ASP   B CB  
6515 C CG  . ASP   B 162 ? 0.1723 0.1721 0.3216 0.0111  -0.0060 -0.0797 162 ASP   B CG  
6516 O OD1 . ASP   B 162 ? 0.1724 0.1914 0.3111 0.0075  0.0063  -0.0763 162 ASP   B OD1 
6517 O OD2 . ASP   B 162 ? 0.1848 0.1926 0.3480 0.0249  -0.0003 -0.0721 162 ASP   B OD2 
6522 N N   . LYS   B 163 ? 0.1312 0.1077 0.2661 -0.0096 -0.0191 -0.0218 163 LYS   B N   
6523 C CA  . LYS   B 163 ? 0.1433 0.1205 0.2726 -0.0180 -0.0186 -0.0070 163 LYS   B CA  
6524 C C   . LYS   B 163 ? 0.1224 0.1139 0.2603 -0.0186 -0.0167 -0.0009 163 LYS   B C   
6525 O O   . LYS   B 163 ? 0.1235 0.1251 0.2851 -0.0196 -0.0178 -0.0040 163 LYS   B O   
6526 C CB  . LYS   B 163 ? 0.1862 0.1638 0.3269 -0.0248 -0.0268 0.0045  163 LYS   B CB  
6527 C CG  . LYS   B 163 ? 0.2709 0.2542 0.4074 -0.0332 -0.0259 0.0101  163 LYS   B CG  
6528 C CD  . LYS   B 163 ? 0.3541 0.3429 0.4838 -0.0420 -0.0300 0.0045  163 LYS   B CD  
6529 C CE  . LYS   B 163 ? 0.4196 0.4116 0.5271 -0.0466 -0.0268 0.0013  163 LYS   B CE  
6530 N NZ  . LYS   B 163 ? 0.4581 0.4527 0.5595 -0.0482 -0.0258 -0.0036 163 LYS   B NZ  
6544 N N   . LEU   B 164 ? 0.1119 0.1109 0.2332 -0.0146 -0.0132 -0.0008 164 LEU   B N   
6545 C CA  . LEU   B 164 ? 0.1158 0.1056 0.2179 -0.0101 -0.0154 -0.0052 164 LEU   B CA  
6546 C C   . LEU   B 164 ? 0.1211 0.1066 0.2176 -0.0113 -0.0244 -0.0102 164 LEU   B C   
6547 O O   . LEU   B 164 ? 0.1270 0.1278 0.2383 -0.0101 -0.0278 -0.0104 164 LEU   B O   
6548 C CB  . LEU   B 164 ? 0.1091 0.1077 0.2119 -0.0071 -0.0146 -0.0058 164 LEU   B CB  
6549 C CG  . LEU   B 164 ? 0.1195 0.1236 0.2192 -0.0091 -0.0055 -0.0067 164 LEU   B CG  
6550 C CD1 . LEU   B 164 ? 0.1251 0.1220 0.2229 -0.0053 -0.0163 -0.0104 164 LEU   B CD1 
6551 C CD2 . LEU   B 164 ? 0.1400 0.1603 0.2346 -0.0057 0.0004  -0.0180 164 LEU   B CD2 
6563 N N   . VAL   B 165 ? 0.1430 0.1130 0.2369 -0.0098 -0.0254 -0.0173 165 VAL   B N   
6564 C CA  . VAL   B 165 ? 0.1721 0.1234 0.2353 -0.0202 -0.0419 -0.0127 165 VAL   B CA  
6565 C C   . VAL   B 165 ? 0.1932 0.1352 0.2545 -0.0286 -0.0566 -0.0128 165 VAL   B C   
6566 O O   . VAL   B 165 ? 0.2088 0.1492 0.2562 -0.0331 -0.0610 -0.0041 165 VAL   B O   
6567 C CB  . VAL   B 165 ? 0.1932 0.1410 0.2391 -0.0105 -0.0155 -0.0221 165 VAL   B CB  
6568 C CG1 . VAL   B 165 ? 0.2066 0.1532 0.2555 -0.0170 -0.0019 -0.0228 165 VAL   B CG1 
6569 C CG2 . VAL   B 165 ? 0.1897 0.1471 0.2379 -0.0095 -0.0057 -0.0118 165 VAL   B CG2 
6579 N N   . SER   B 166 ? 0.1986 0.1275 0.2767 -0.0274 -0.0621 -0.0320 166 SER   B N   
6580 C CA  . SER   B 166 ? 0.1892 0.1299 0.3246 -0.0299 -0.0599 -0.0380 166 SER   B CA  
6581 C C   . SER   B 166 ? 0.1804 0.1336 0.3296 -0.0316 -0.0643 -0.0186 166 SER   B C   
6582 O O   . SER   B 166 ? 0.1822 0.1599 0.3625 -0.0458 -0.0731 -0.0298 166 SER   B O   
6583 C CB  . SER   B 166 ? 0.1943 0.1380 0.3515 -0.0252 -0.0499 -0.0490 166 SER   B CB  
6584 O OG  . SER   B 166 ? 0.1836 0.1329 0.3680 -0.0221 -0.0493 -0.0288 166 SER   B OG  
6590 N N   . SER   B 167 ? 0.1674 0.1256 0.3042 -0.0295 -0.0593 0.0109  167 SER   B N   
6591 C CA  . SER   B 167 ? 0.1559 0.1295 0.2951 -0.0290 -0.0345 0.0187  167 SER   B CA  
6592 C C   . SER   B 167 ? 0.1492 0.1365 0.2876 -0.0333 -0.0364 0.0311  167 SER   B C   
6593 O O   . SER   B 167 ? 0.1561 0.1472 0.2795 -0.0319 -0.0336 0.0201  167 SER   B O   
6594 C CB  . SER   B 167 ? 0.1482 0.1400 0.2946 -0.0255 -0.0091 0.0202  167 SER   B CB  
6595 O OG  . SER   B 167 ? 0.1437 0.1494 0.2904 -0.0137 -0.0012 0.0157  167 SER   B OG  
6601 N N   . PHE   B 168 ? 0.1473 0.1347 0.2918 -0.0310 -0.0261 0.0383  168 PHE   B N   
6602 C CA  . PHE   B 168 ? 0.1566 0.1367 0.2648 -0.0341 -0.0215 0.0268  168 PHE   B CA  
6603 C C   . PHE   B 168 ? 0.1425 0.1305 0.2374 -0.0171 -0.0010 0.0070  168 PHE   B C   
6604 O O   . PHE   B 168 ? 0.1691 0.1314 0.2374 0.0048  -0.0070 -0.0032 168 PHE   B O   
6605 C CB  . PHE   B 168 ? 0.1761 0.1398 0.2621 -0.0416 -0.0472 0.0457  168 PHE   B CB  
6606 C CG  . PHE   B 168 ? 0.2058 0.1279 0.2606 -0.0439 -0.0560 0.0229  168 PHE   B CG  
6607 C CD1 . PHE   B 168 ? 0.2393 0.1332 0.2728 -0.0348 -0.0627 0.0175  168 PHE   B CD1 
6608 C CD2 . PHE   B 168 ? 0.1938 0.1276 0.2620 -0.0358 -0.0575 0.0260  168 PHE   B CD2 
6609 C CE1 . PHE   B 168 ? 0.2514 0.1471 0.2753 -0.0230 -0.0566 0.0108  168 PHE   B CE1 
6610 C CE2 . PHE   B 168 ? 0.2153 0.1340 0.2619 -0.0266 -0.0634 0.0124  168 PHE   B CE2 
6611 C CZ  . PHE   B 168 ? 0.2369 0.1368 0.2767 -0.0162 -0.0625 0.0181  168 PHE   B CZ  
6621 N N   A LEU   B 169 ? 0.1532 0.1496 0.2474 -0.0017 -0.0020 -0.0055 169 LEU   B N   
6622 N N   B LEU   B 169 ? 0.1507 0.1503 0.2437 -0.0005 0.0017  -0.0040 169 LEU   B N   
6623 C CA  A LEU   B 169 ? 0.1742 0.1724 0.2814 -0.0029 -0.0077 -0.0232 169 LEU   B CA  
6624 C CA  B LEU   B 169 ? 0.1712 0.1746 0.2760 -0.0005 -0.0009 -0.0203 169 LEU   B CA  
6625 C C   A LEU   B 169 ? 0.1878 0.1870 0.3282 0.0015  -0.0104 -0.0486 169 LEU   B C   
6626 C C   B LEU   B 169 ? 0.1888 0.1902 0.3198 0.0110  -0.0013 -0.0406 169 LEU   B C   
6627 O O   A LEU   B 169 ? 0.2003 0.2006 0.3658 -0.0082 -0.0140 -0.0674 169 LEU   B O   
6628 O O   B LEU   B 169 ? 0.2031 0.2067 0.3480 0.0069  0.0056  -0.0542 169 LEU   B O   
6629 C CB  A LEU   B 169 ? 0.1920 0.1978 0.2910 -0.0057 -0.0144 -0.0053 169 LEU   B CB  
6630 C CB  B LEU   B 169 ? 0.1866 0.2010 0.2869 -0.0086 -0.0067 -0.0052 169 LEU   B CB  
6631 C CG  A LEU   B 169 ? 0.2182 0.2221 0.3153 -0.0014 -0.0165 0.0014  169 LEU   B CG  
6632 C CG  B LEU   B 169 ? 0.2127 0.2271 0.3127 -0.0073 -0.0087 0.0002  169 LEU   B CG  
6633 C CD1 A LEU   B 169 ? 0.2245 0.2356 0.3224 -0.0052 -0.0194 0.0098  169 LEU   B CD1 
6634 C CD1 B LEU   B 169 ? 0.2247 0.2395 0.3152 -0.0075 -0.0134 0.0050  169 LEU   B CD1 
6635 C CD2 A LEU   B 169 ? 0.2198 0.2271 0.3154 0.0034  -0.0099 -0.0032 169 LEU   B CD2 
6636 C CD2 B LEU   B 169 ? 0.2133 0.2356 0.3144 -0.0044 -0.0005 -0.0058 169 LEU   B CD2 
6637 O OXT A LEU   B 169 ? 0.1982 0.1975 0.3360 0.0192  -0.0048 -0.0502 169 LEU   B OXT 
6638 O OXT B LEU   B 169 ? 0.2017 0.1988 0.3324 0.0296  -0.0029 -0.0419 169 LEU   B OXT 
6661 S S   B DMS   C .   ? 0.1918 0.1575 0.2252 0.0093  0.0081  0.0435  301 DMS   A S   
6662 O O   B DMS   C .   ? 0.2041 0.1789 0.2602 0.0128  0.0090  0.0315  301 DMS   A O   
6663 C C1  B DMS   C .   ? 0.1690 0.1436 0.1917 -0.0025 0.0140  0.0460  301 DMS   A C1  
6664 C C2  B DMS   C .   ? 0.2031 0.1647 0.2448 -0.0012 0.0060  0.0376  301 DMS   A C2  
6671 N N2  B A1A47 D .   ? 0.1485 0.1118 0.1292 -0.0003 -0.0112 0.0121  302 A1A47 A N2  
6672 C C3  B A1A47 D .   ? 0.1553 0.1725 0.1831 0.0070  -0.0055 0.0209  302 A1A47 A C3  
6673 C C6  B A1A47 D .   ? 0.1198 0.1205 0.1323 0.0161  0.0060  -0.0027 302 A1A47 A C6  
6674 C C9  B A1A47 D .   ? 0.1559 0.1069 0.1448 0.0059  0.0072  0.0046  302 A1A47 A C9  
6675 C C1  B A1A47 D .   ? 0.1342 0.1502 0.1727 0.0190  0.0198  0.0426  302 A1A47 A C1  
6676 C C10 B A1A47 D .   ? 0.1457 0.1070 0.1276 0.0084  -0.0064 0.0116  302 A1A47 A C10 
6677 C C11 B A1A47 D .   ? 0.1298 0.1092 0.1257 0.0115  -0.0055 0.0030  302 A1A47 A C11 
6678 C C2  B A1A47 D .   ? 0.1349 0.1527 0.1630 0.0119  0.0058  0.0338  302 A1A47 A C2  
6679 C C4  B A1A47 D .   ? 0.1634 0.1708 0.1867 -0.0051 -0.0065 0.0125  302 A1A47 A C4  
6680 C C5  B A1A47 D .   ? 0.1405 0.1555 0.1762 -0.0062 -0.0028 0.0045  302 A1A47 A C5  
6681 C C7  B A1A47 D .   ? 0.1361 0.1251 0.1362 0.0091  0.0064  0.0135  302 A1A47 A C7  
6682 C C8  B A1A47 D .   ? 0.1541 0.1208 0.1497 0.0028  0.0045  0.0116  302 A1A47 A C8  
6683 N N1  B A1A47 D .   ? 0.1272 0.1413 0.1539 0.0029  0.0114  0.0214  302 A1A47 A N1  
6684 N N3  B A1A47 D .   ? 0.1303 0.1094 0.1354 -0.0044 0.0023  0.0112  302 A1A47 A N3  
6685 O O1  B A1A47 D .   ? 0.1342 0.1539 0.1811 0.0167  0.0241  0.0577  302 A1A47 A O1  
6686 O O2  B A1A47 D .   ? 0.1078 0.1221 0.1389 -0.0004 0.0072  0.0169  302 A1A47 A O2  
6687 O O3  B A1A47 D .   ? 0.1074 0.1339 0.1554 -0.0070 0.0216  0.0013  302 A1A47 A O3  
6688 O O4  B A1A47 D .   ? 0.1467 0.1472 0.1962 0.0301  0.0146  0.0393  302 A1A47 A O4  
6689 S S1  B A1A47 D .   ? 0.1134 0.1340 0.1317 0.0122  -0.0016 0.0197  302 A1A47 A S1  
6690 S S2  B A1A47 D .   ? 0.1472 0.1172 0.1178 -0.0014 0.0048  0.0098  302 A1A47 A S2  
6701 O O   . HOH   E .   ? 0.4175 0.1882 0.3244 -0.0185 0.0412  0.0367  401 HOH   A O   
6702 O O   . HOH   E .   ? 0.3910 0.6300 0.3825 -0.1273 0.0475  0.0608  402 HOH   A O   
6703 O O   . HOH   E .   ? 0.4435 0.6649 0.3542 -0.1010 -0.0838 -0.0910 403 HOH   A O   
6704 O O   . HOH   E .   ? 0.3128 0.3017 0.3275 0.0166  0.0885  -0.0407 404 HOH   A O   
6705 O O   . HOH   E .   ? 0.7128 0.3175 0.5623 -0.0707 -0.1353 0.0575  405 HOH   A O   
6706 O O   . HOH   E .   ? 0.5519 0.4130 0.3083 0.1532  -0.1087 0.0461  406 HOH   A O   
6707 O O   . HOH   E .   ? 0.4130 0.2701 0.4070 -0.0165 0.0990  0.0850  407 HOH   A O   
6708 O O   . HOH   E .   ? 0.2421 0.5840 0.5627 0.0076  -0.0554 0.1636  408 HOH   A O   
6709 O O   . HOH   E .   ? 0.2757 0.2007 0.4228 -0.0342 -0.1413 0.0969  409 HOH   A O   
6710 O O   B HOH   E .   ? 0.3321 0.2734 0.2270 0.0532  0.0482  -0.0392 410 HOH   A O   
6711 O O   . HOH   E .   ? 0.1950 0.2486 0.2314 -0.0461 0.0513  0.0087  411 HOH   A O   
6712 O O   . HOH   E .   ? 0.1895 0.1567 0.2229 0.0259  -0.0420 -0.0113 412 HOH   A O   
6713 O O   . HOH   E .   ? 0.1881 0.1657 0.3452 -0.0447 -0.0056 -0.0260 413 HOH   A O   
6714 O O   . HOH   E .   ? 0.1891 0.5051 0.3648 0.0073  -0.0417 0.0992  414 HOH   A O   
6715 O O   . HOH   E .   ? 0.2695 0.2982 0.1505 -0.0201 0.0429  0.0630  415 HOH   A O   
6716 O O   . HOH   E .   ? 0.3169 0.3120 0.3555 -0.1034 0.1541  -0.0524 416 HOH   A O   
6717 O O   . HOH   E .   ? 0.1551 0.1383 0.1839 0.0165  -0.0255 0.0172  417 HOH   A O   
6718 O O   . HOH   E .   ? 0.4531 0.4815 0.3308 0.1633  0.0800  -0.1288 418 HOH   A O   
6719 O O   . HOH   E .   ? 0.2835 0.4215 0.3079 0.0157  0.0742  0.0869  419 HOH   A O   
6720 O O   . HOH   E .   ? 0.2234 0.1644 0.1996 -0.0288 -0.0075 0.0007  420 HOH   A O   
6721 O O   . HOH   E .   ? 0.1267 0.1327 0.1988 -0.0196 0.0109  0.0037  421 HOH   A O   
6722 O O   . HOH   E .   ? 0.2936 0.2582 0.2022 -0.0909 0.0217  0.0485  422 HOH   A O   
6723 O O   . HOH   E .   ? 0.1428 0.3378 0.2926 0.0385  -0.0016 0.0417  423 HOH   A O   
6724 O O   . HOH   E .   ? 0.1575 0.3185 0.3708 -0.0208 0.0321  -0.1250 424 HOH   A O   
6725 O O   . HOH   E .   ? 0.5808 0.5026 0.2847 -0.0003 0.0161  0.1026  425 HOH   A O   
6726 O O   . HOH   E .   ? 0.2835 0.6470 0.5554 0.1535  0.0631  0.0788  426 HOH   A O   
6727 O O   . HOH   E .   ? 0.4326 0.4553 0.2433 -0.0972 0.1276  0.0804  427 HOH   A O   
6728 O O   . HOH   E .   ? 0.2575 0.2098 0.2390 0.0568  0.0464  0.0400  428 HOH   A O   
6729 O O   . HOH   E .   ? 0.3106 0.3422 0.2318 -0.0515 -0.0457 -0.0582 429 HOH   A O   
6730 O O   . HOH   E .   ? 0.5494 0.4155 0.4198 -0.1303 -0.0658 -0.1157 430 HOH   A O   
6731 O O   . HOH   E .   ? 0.5376 0.4044 0.4891 0.0566  0.2527  -0.0779 431 HOH   A O   
6732 O O   . HOH   E .   ? 0.1285 0.1263 0.2016 0.0009  -0.0177 -0.0381 432 HOH   A O   
6733 O O   . HOH   E .   ? 0.4471 0.1677 0.4259 0.0346  0.0570  0.0246  433 HOH   A O   
6734 O O   . HOH   E .   ? 0.3622 0.3473 0.4106 0.1009  0.0619  -0.0872 434 HOH   A O   
6735 O O   . HOH   E .   ? 0.4162 0.2118 0.4171 0.0301  -0.1343 0.0685  435 HOH   A O   
6736 O O   . HOH   E .   ? 0.4470 0.4235 0.3810 -0.1642 -0.0914 0.2087  436 HOH   A O   
6737 O O   . HOH   E .   ? 0.1135 0.3576 0.2037 0.0054  0.0194  0.0846  437 HOH   A O   
6738 O O   A HOH   E .   ? 0.2926 0.3282 0.3435 -0.0692 0.0985  0.1357  438 HOH   A O   
6739 O O   B HOH   E .   ? 0.2418 0.1711 0.2662 0.0394  0.0957  0.0586  439 HOH   A O   
6740 O O   B HOH   E .   ? 0.1411 0.0709 0.1244 0.0151  0.0190  0.0443  440 HOH   A O   
6741 O O   . HOH   E .   ? 0.2031 0.3647 0.3069 0.0210  -0.0557 0.0647  441 HOH   A O   
6742 O O   A HOH   E .   ? 0.1813 0.1331 0.1614 0.0295  0.0219  0.0230  442 HOH   A O   
6743 O O   . HOH   E .   ? 0.3126 0.3984 0.3620 0.1691  0.0668  0.0451  443 HOH   A O   
6744 O O   . HOH   E .   ? 0.4703 0.2732 0.3412 -0.1251 0.0810  0.0594  444 HOH   A O   
6745 O O   A HOH   E .   ? 0.2601 0.2034 0.4387 0.0574  0.1155  -0.0279 445 HOH   A O   
6746 O O   . HOH   E .   ? 0.1746 0.1508 0.2148 0.0025  -0.0549 -0.0195 446 HOH   A O   
6747 O O   . HOH   E .   ? 0.5594 0.4503 0.3464 -0.1120 0.1377  0.1513  447 HOH   A O   
6748 O O   . HOH   E .   ? 0.2124 0.3370 0.3602 0.0810  -0.0667 -0.0215 448 HOH   A O   
6749 O O   . HOH   E .   ? 0.3452 0.1931 0.4150 -0.1047 0.1025  0.0118  449 HOH   A O   
6750 O O   . HOH   E .   ? 0.2349 0.3746 0.2874 -0.0252 0.0688  0.0106  450 HOH   A O   
6751 O O   . HOH   E .   ? 0.1274 0.1680 0.2350 0.0112  -0.0110 0.0049  451 HOH   A O   
6752 O O   A HOH   E .   ? 0.2643 0.3035 0.3098 0.1610  0.0222  0.0174  452 HOH   A O   
6753 O O   . HOH   E .   ? 0.2805 0.3023 0.2346 -0.0548 -0.0249 -0.0840 453 HOH   A O   
6754 O O   . HOH   E .   ? 0.3486 0.1875 0.1778 0.1166  0.0466  0.0103  454 HOH   A O   
6755 O O   . HOH   E .   ? 0.2038 0.1978 0.1941 0.0209  -0.0009 0.0512  455 HOH   A O   
6756 O O   . HOH   E .   ? 0.4631 0.3783 0.2258 0.0524  0.0454  0.1089  456 HOH   A O   
6757 O O   . HOH   E .   ? 0.1264 0.1896 0.2058 0.0094  -0.0050 0.0441  457 HOH   A O   
6758 O O   . HOH   E .   ? 0.1606 0.1892 0.3506 0.0138  0.0818  -0.0235 458 HOH   A O   
6759 O O   . HOH   E .   ? 0.4537 0.3407 0.6746 0.0970  -0.1341 0.0150  459 HOH   A O   
6760 O O   . HOH   E .   ? 0.3085 0.2707 0.3245 -0.0962 -0.0211 -0.0229 460 HOH   A O   
6761 O O   . HOH   E .   ? 0.2486 0.2962 0.4467 -0.0414 -0.0823 -0.0757 461 HOH   A O   
6762 O O   . HOH   E .   ? 0.6169 0.5951 0.3869 0.1794  -0.0711 -0.0659 462 HOH   A O   
6763 O O   B HOH   E .   ? 0.2472 0.2192 0.3780 -0.0542 0.1628  -0.1051 463 HOH   A O   
6764 O O   B HOH   E .   ? 0.1563 0.1073 0.0842 0.0038  -0.0034 0.0094  464 HOH   A O   
6765 O O   B HOH   E .   ? 0.1234 0.1917 0.2738 -0.0275 -0.0694 0.0089  465 HOH   A O   
6766 O O   . HOH   E .   ? 0.1157 0.1085 0.1144 -0.0028 0.0135  0.0016  466 HOH   A O   
6767 O O   . HOH   E .   ? 0.2690 0.3399 0.3653 -0.1211 -0.0788 -0.0018 467 HOH   A O   
6768 O O   . HOH   E .   ? 0.1671 0.1675 0.2086 -0.0346 0.0040  0.0318  468 HOH   A O   
6769 O O   A HOH   E .   ? 0.1347 0.1862 0.2523 0.0315  0.0482  -0.0832 469 HOH   A O   
6770 O O   . HOH   E .   ? 0.3825 0.2392 0.3342 -0.1449 0.1131  -0.0712 470 HOH   A O   
6771 O O   . HOH   E .   ? 0.3313 0.6239 0.4303 -0.0178 -0.1681 0.0955  471 HOH   A O   
6772 O O   . HOH   E .   ? 0.1192 0.1306 0.1230 -0.0026 -0.0135 -0.0087 472 HOH   A O   
6773 O O   . HOH   E .   ? 0.1265 0.1091 0.1834 -0.0018 0.0138  -0.0122 473 HOH   A O   
6774 O O   . HOH   E .   ? 0.1402 0.1445 0.1752 -0.0139 0.0065  0.0271  474 HOH   A O   
6775 O O   . HOH   E .   ? 0.2299 0.2696 0.2696 -0.0180 0.0574  -0.0732 475 HOH   A O   
6776 O O   . HOH   E .   ? 0.2021 0.1917 0.2456 -0.0011 -0.0522 0.0374  476 HOH   A O   
6777 O O   . HOH   E .   ? 0.1950 0.1694 0.1448 0.0117  -0.0034 0.0141  477 HOH   A O   
6778 O O   B HOH   E .   ? 0.1364 0.2758 0.2140 -0.0380 0.0523  -0.0549 478 HOH   A O   
6779 O O   B HOH   E .   ? 0.2928 0.2992 0.4000 -0.0171 0.1113  -0.1186 479 HOH   A O   
6780 O O   . HOH   E .   ? 0.1641 0.1875 0.1973 -0.0122 -0.0414 0.0299  480 HOH   A O   
6781 O O   . HOH   E .   ? 0.2028 0.2450 0.2225 0.0138  -0.0117 -0.0499 481 HOH   A O   
6782 O O   . HOH   E .   ? 0.1531 0.1778 0.2359 -0.0108 -0.0222 0.0792  482 HOH   A O   
6783 O O   . HOH   E .   ? 0.1655 0.1186 0.1321 -0.0232 0.0147  -0.0071 483 HOH   A O   
6784 O O   B HOH   E .   ? 0.1508 0.2833 0.2597 -0.0092 0.0062  -0.0653 484 HOH   A O   
6785 O O   . HOH   E .   ? 0.2785 0.2530 0.1803 0.0479  0.0860  0.0172  485 HOH   A O   
6786 O O   . HOH   E .   ? 0.4749 0.5229 0.4543 0.0814  -0.0896 0.1158  486 HOH   A O   
6787 O O   . HOH   E .   ? 0.1987 0.1428 0.2185 -0.0108 -0.0024 0.0093  487 HOH   A O   
6788 O O   . HOH   E .   ? 0.1152 0.1222 0.1585 0.0059  -0.0200 0.0028  488 HOH   A O   
6789 O O   . HOH   E .   ? 0.2743 0.1906 0.4832 -0.0557 -0.0477 0.0289  489 HOH   A O   
6790 O O   A HOH   E .   ? 0.1838 0.1727 0.2344 -0.0571 0.0363  0.0577  490 HOH   A O   
6791 O O   . HOH   E .   ? 0.1524 0.1759 0.1568 -0.0019 0.0168  0.0489  491 HOH   A O   
6792 O O   A HOH   E .   ? 0.0785 0.1106 0.0699 -0.0111 -0.0041 0.0083  492 HOH   A O   
6793 O O   . HOH   E .   ? 0.2228 0.1710 0.1404 -0.0398 0.0267  0.0201  493 HOH   A O   
6794 O O   . HOH   E .   ? 0.3067 0.2182 0.2991 0.0157  -0.0370 0.0728  494 HOH   A O   
6795 O O   . HOH   E .   ? 0.2343 0.4242 0.2761 0.0270  0.0637  0.1706  495 HOH   A O   
6796 O O   . HOH   E .   ? 0.3654 0.3267 0.1886 0.0484  -0.0985 0.0158  496 HOH   A O   
6797 O O   . HOH   E .   ? 0.2792 0.5453 0.3483 0.0796  0.0730  -0.1077 497 HOH   A O   
6798 O O   A HOH   E .   ? 0.2371 0.2798 0.3008 -0.0043 0.1017  -0.0260 498 HOH   A O   
6799 O O   . HOH   E .   ? 0.4367 0.3225 0.1622 -0.0195 0.0878  0.0401  499 HOH   A O   
6800 O O   . HOH   E .   ? 0.2171 0.2302 0.4275 0.0312  -0.0807 -0.1039 500 HOH   A O   
6801 O O   . HOH   E .   ? 0.3253 0.5930 0.4090 -0.0242 0.0319  0.1400  501 HOH   A O   
6802 O O   B HOH   E .   ? 0.2318 0.2144 0.3650 0.0472  -0.0681 0.0220  502 HOH   A O   
6803 O O   . HOH   E .   ? 0.1153 0.1426 0.1257 0.0046  -0.0168 -0.0230 503 HOH   A O   
6804 O O   A HOH   E .   ? 0.4847 0.3281 0.4132 -0.0829 0.0765  -0.0335 504 HOH   A O   
6805 O O   . HOH   E .   ? 0.1637 0.1613 0.3290 0.0344  0.1013  0.0908  505 HOH   A O   
6806 O O   . HOH   E .   ? 0.5935 0.3618 0.4165 0.1384  -0.0909 0.1269  506 HOH   A O   
6807 O O   . HOH   E .   ? 0.1811 0.1408 0.1236 -0.0018 0.0168  0.0139  507 HOH   A O   
6808 O O   . HOH   E .   ? 0.4357 0.4120 0.4933 -0.0598 -0.0416 0.0857  508 HOH   A O   
6809 O O   . HOH   E .   ? 0.2359 0.3451 0.3198 -0.0398 0.1051  -0.0817 509 HOH   A O   
6810 O O   . HOH   E .   ? 0.2488 0.2255 0.1620 -0.0411 -0.0624 0.0190  510 HOH   A O   
6811 O O   . HOH   E .   ? 0.2266 0.2887 0.3350 -0.0336 -0.0354 0.0382  511 HOH   A O   
6812 O O   A HOH   E .   ? 0.1120 0.1496 0.2477 0.0052  0.0364  0.0467  512 HOH   A O   
6813 O O   . HOH   E .   ? 0.6624 0.4333 0.4023 -0.0536 0.0215  0.1780  513 HOH   A O   
6814 O O   . HOH   E .   ? 0.1822 0.1412 0.2356 0.0051  -0.0316 -0.0046 514 HOH   A O   
6815 O O   . HOH   E .   ? 0.1236 0.1441 0.2439 0.0013  0.0036  0.0145  515 HOH   A O   
6816 O O   A HOH   E .   ? 0.1207 0.0852 0.1472 0.0027  0.0248  0.0571  516 HOH   A O   
6817 O O   B HOH   E .   ? 0.3202 0.3363 0.4210 -0.0908 0.1057  -0.1293 517 HOH   A O   
6818 O O   . HOH   E .   ? 0.2309 0.1887 0.2105 -0.0560 0.0018  0.0512  518 HOH   A O   
6819 O O   . HOH   E .   ? 0.1642 0.2304 0.2829 -0.0011 -0.0296 -0.0020 519 HOH   A O   
6820 O O   . HOH   E .   ? 0.5787 0.5960 0.4968 -0.0929 0.0913  0.0680  520 HOH   A O   
6821 O O   . HOH   E .   ? 0.5656 0.2481 0.3449 0.0910  -0.0826 -0.0446 521 HOH   A O   
6822 O O   A HOH   E .   ? 0.3485 0.2039 0.2349 -0.1300 -0.0434 0.0654  522 HOH   A O   
6823 O O   . HOH   E .   ? 0.6144 0.6477 0.5829 0.0225  -0.1132 0.0238  523 HOH   A O   
6824 O O   . HOH   E .   ? 0.4224 0.5403 0.3100 -0.0934 -0.0431 0.1184  524 HOH   A O   
6825 O O   . HOH   E .   ? 0.1686 0.2590 0.2173 0.0046  -0.0458 0.0299  525 HOH   A O   
6826 O O   . HOH   E .   ? 0.2128 0.3907 0.2040 0.1567  -0.0039 0.0114  526 HOH   A O   
6827 O O   . HOH   E .   ? 0.4538 0.6003 0.4008 0.1137  0.0733  0.1144  527 HOH   A O   
6828 O O   A HOH   E .   ? 0.1193 0.1006 0.2300 0.0088  -0.0585 0.0474  528 HOH   A O   
6829 O O   . HOH   E .   ? 0.4559 0.6077 0.3506 0.0501  0.2246  -0.0614 529 HOH   A O   
6830 O O   . HOH   E .   ? 0.3109 0.1104 0.1839 0.0001  -0.0465 0.0076  530 HOH   A O   
6831 O O   B HOH   E .   ? 0.1450 0.1289 0.1438 -0.0108 0.0138  0.0315  531 HOH   A O   
6832 O O   . HOH   E .   ? 0.3770 0.2040 0.4229 -0.0649 -0.1928 0.0972  532 HOH   A O   
6833 O O   . HOH   E .   ? 0.2588 0.4873 0.1360 -0.0580 0.0372  -0.0090 533 HOH   A O   
6834 O O   . HOH   E .   ? 0.3538 0.3557 0.2918 0.1496  -0.0811 -0.1275 534 HOH   A O   
6835 O O   . HOH   E .   ? 0.4742 0.4223 0.4557 -0.1306 -0.1353 -0.1075 535 HOH   A O   
6836 O O   . HOH   E .   ? 0.1331 0.1734 0.2225 -0.0102 0.0063  0.0384  536 HOH   A O   
6837 O O   . HOH   E .   ? 0.3091 0.3380 0.6765 -0.0207 0.1188  -0.0379 537 HOH   A O   
6838 O O   . HOH   E .   ? 0.5458 0.6553 0.5683 0.0620  0.0721  0.0185  538 HOH   A O   
6839 O O   B HOH   E .   ? 0.1939 0.2341 0.2884 0.0325  -0.0810 -0.1315 539 HOH   A O   
6840 O O   . HOH   E .   ? 0.4867 0.4211 0.2916 0.0332  -0.1325 0.0540  540 HOH   A O   
6841 O O   . HOH   E .   ? 0.4600 0.4499 0.3700 -0.0650 -0.0167 0.2282  541 HOH   A O   
6842 O O   A HOH   E .   ? 0.0683 0.1125 0.1269 0.0188  -0.0255 -0.0039 542 HOH   A O   
6843 O O   . HOH   E .   ? 0.4856 0.5201 0.4809 0.0926  0.0815  -0.0943 543 HOH   A O   
6844 O O   . HOH   E .   ? 0.3903 0.3632 0.4945 -0.1238 -0.0922 -0.1203 544 HOH   A O   
6845 O O   . HOH   E .   ? 0.3414 0.2254 0.1340 -0.0912 0.0482  0.0308  545 HOH   A O   
6846 O O   . HOH   E .   ? 0.5692 0.6153 0.3156 0.1540  -0.0991 0.1291  546 HOH   A O   
6847 O O   B HOH   E .   ? 0.0824 0.1557 0.1615 0.0110  0.0343  -0.0068 547 HOH   A O   
6848 O O   . HOH   E .   ? 0.2582 0.2479 0.1989 0.0115  -0.0179 0.0051  548 HOH   A O   
6849 O O   . HOH   E .   ? 0.2147 0.1351 0.2260 0.0157  0.0051  0.0092  549 HOH   A O   
6850 O O   . HOH   E .   ? 0.4658 0.3843 0.6752 0.0366  -0.1553 0.0926  550 HOH   A O   
6851 O O   . HOH   E .   ? 0.3856 0.4872 0.5151 -0.1547 -0.0241 -0.0801 551 HOH   A O   
6852 O O   B HOH   E .   ? 0.1206 0.1548 0.1525 -0.0153 0.0090  -0.0005 552 HOH   A O   
6853 O O   . HOH   E .   ? 0.3130 0.2549 0.2988 0.1440  -0.0533 -0.0551 553 HOH   A O   
6854 O O   . HOH   E .   ? 0.2748 0.1581 0.4859 0.0161  0.1101  0.0188  554 HOH   A O   
6855 O O   . HOH   E .   ? 0.1989 0.2358 0.2201 0.0126  -0.0088 -0.0601 555 HOH   A O   
6856 O O   A HOH   E .   ? 0.0741 0.1030 0.0954 0.0067  -0.0111 -0.0041 556 HOH   A O   
6857 O O   A HOH   E .   ? 0.4091 0.2295 0.2358 0.0121  0.1099  0.0427  557 HOH   A O   
6858 O O   . HOH   E .   ? 0.1616 0.1970 0.5370 -0.0269 -0.0789 0.0647  558 HOH   A O   
6859 O O   . HOH   E .   ? 0.2496 0.1797 0.2415 0.0142  0.0475  0.0186  559 HOH   A O   
6860 O O   . HOH   E .   ? 0.3845 0.4672 0.4331 0.0335  -0.0264 0.1607  560 HOH   A O   
6861 O O   . HOH   E .   ? 0.5343 0.2471 0.4005 0.0193  -0.0605 0.1070  561 HOH   A O   
6862 O O   . HOH   E .   ? 0.7230 0.7688 0.4407 -0.0561 -0.0405 -0.0844 562 HOH   A O   
6863 O O   B HOH   E .   ? 0.2484 0.2084 0.3516 0.0828  0.1479  0.0860  563 HOH   A O   
6864 O O   A HOH   E .   ? 0.6962 0.3835 0.4075 0.1674  0.1635  0.0720  564 HOH   A O   
6865 O O   . HOH   E .   ? 0.6234 0.5431 0.4369 -0.1052 0.0907  0.0752  565 HOH   A O   
6866 O O   . HOH   E .   ? 0.2073 0.2330 0.3564 0.0374  -0.0193 0.0524  566 HOH   A O   
6867 O O   . HOH   E .   ? 0.4594 0.3581 0.5349 0.0211  0.0406  0.0773  567 HOH   A O   
6868 O O   . HOH   E .   ? 0.6391 0.6768 0.4312 0.0774  -0.0931 -0.0024 568 HOH   A O   
6869 O O   . HOH   E .   ? 0.2378 0.2488 0.3066 -0.0484 0.0373  -0.0602 569 HOH   A O   
6870 O O   . HOH   E .   ? 0.3154 0.4126 0.3966 0.0833  -0.1020 0.0951  570 HOH   A O   
6871 O O   . HOH   E .   ? 0.2305 0.3449 0.4532 -0.0238 -0.0335 -0.0503 571 HOH   A O   
6872 O O   . HOH   E .   ? 0.4000 0.5158 0.3388 -0.0933 -0.0925 0.1559  572 HOH   A O   
6873 O O   A HOH   E .   ? 0.3241 0.2885 0.3450 0.0977  0.1615  0.1064  573 HOH   A O   
6874 O O   . HOH   E .   ? 0.2500 0.4591 0.5298 -0.1336 0.0844  -0.1900 574 HOH   A O   
6875 O O   . HOH   E .   ? 0.2146 0.2449 0.2944 -0.0738 0.0390  -0.0299 575 HOH   A O   
6876 O O   . HOH   E .   ? 0.5479 0.2933 0.7021 0.0487  0.0812  0.2081  576 HOH   A O   
6877 O O   . HOH   E .   ? 0.2520 0.2095 0.4272 0.0436  -0.1391 -0.0449 577 HOH   A O   
6878 O O   . HOH   E .   ? 0.2528 0.1522 0.2408 0.0425  -0.0958 -0.0407 578 HOH   A O   
6879 O O   . HOH   E .   ? 0.2650 0.3654 0.4672 0.0514  0.0325  -0.2050 579 HOH   A O   
6880 O O   . HOH   E .   ? 0.3477 0.5155 0.3129 0.0213  0.0116  -0.0631 580 HOH   A O   
6881 O O   . HOH   E .   ? 0.5465 0.5422 0.4176 0.1256  0.1320  0.0957  581 HOH   A O   
6882 O O   . HOH   E .   ? 0.2610 0.2037 0.4416 0.0049  0.0869  0.0094  582 HOH   A O   
6883 O O   . HOH   E .   ? 0.4434 0.5279 0.4212 0.1463  -0.0400 -0.0550 583 HOH   A O   
6884 O O   . HOH   E .   ? 0.5161 0.6365 0.6134 -0.1509 -0.1232 0.1219  584 HOH   A O   
6885 O O   . HOH   E .   ? 0.3594 0.2505 0.3314 -0.0728 -0.1360 0.0693  585 HOH   A O   
6886 O O   . HOH   E .   ? 0.3821 0.4677 0.2364 -0.0612 -0.0098 0.0400  586 HOH   A O   
6887 O O   . HOH   E .   ? 0.3841 0.4080 0.5364 -0.1734 -0.0406 -0.0284 587 HOH   A O   
6888 O O   . HOH   E .   ? 0.5741 0.4439 0.6231 -0.0030 0.0678  -0.0354 588 HOH   A O   
6889 O O   . HOH   E .   ? 0.3744 0.3852 0.2493 -0.0498 -0.0634 0.0060  589 HOH   A O   
6890 O O   . HOH   E .   ? 0.2069 0.1889 0.2198 0.0158  0.0075  -0.0016 590 HOH   A O   
6891 O O   B HOH   E .   ? 0.3024 0.1267 0.3507 0.0380  0.0645  0.0707  591 HOH   A O   
6892 O O   . HOH   E .   ? 0.5597 0.3595 0.3732 -0.0173 0.0522  -0.1164 592 HOH   A O   
6893 O O   . HOH   E .   ? 0.6913 0.3295 0.3035 -0.0410 -0.1188 0.0294  593 HOH   A O   
6894 O O   . HOH   E .   ? 0.5357 0.5632 0.6145 0.1174  0.1232  -0.1156 594 HOH   A O   
6895 O O   B HOH   E .   ? 0.1262 0.2159 0.2521 0.0080  -0.0286 -0.0326 595 HOH   A O   
6896 O O   . HOH   E .   ? 0.2550 0.4305 0.3618 0.1070  0.1150  0.2138  596 HOH   A O   
6897 O O   . HOH   E .   ? 0.2608 0.3544 0.4556 -0.0082 0.1255  0.0715  597 HOH   A O   
6898 O O   . HOH   E .   ? 0.4122 0.4181 0.3046 -0.0446 0.1134  -0.0055 598 HOH   A O   
6899 O O   . HOH   E .   ? 0.4476 0.4846 0.4083 -0.0993 -0.0781 -0.0409 599 HOH   A O   
6900 O O   . HOH   E .   ? 0.5226 0.6083 0.3732 -0.0574 0.1241  0.0809  600 HOH   A O   
6901 O O   . HOH   E .   ? 0.4686 0.3311 0.4319 -0.0325 0.2585  0.0001  601 HOH   A O   
6902 O O   . HOH   E .   ? 0.4129 0.3554 0.5547 0.0135  -0.1243 0.0068  602 HOH   A O   
6903 O O   . HOH   E .   ? 0.3626 0.2382 0.3967 -0.0778 0.0356  0.0851  603 HOH   A O   
6904 O O   . HOH   E .   ? 0.2242 0.1959 0.4539 -0.0033 0.0259  0.0716  604 HOH   A O   
6905 O O   . HOH   E .   ? 0.3103 0.3103 0.2175 -0.0333 0.0989  0.0031  605 HOH   A O   
6906 O O   . HOH   E .   ? 0.2337 0.2721 0.4548 0.0052  0.1075  -0.0504 606 HOH   A O   
6907 O O   . HOH   E .   ? 0.2545 0.2280 0.5922 -0.0034 -0.1150 0.0211  607 HOH   A O   
6908 O O   . HOH   E .   ? 0.6376 0.2337 0.4717 -0.0626 0.0362  0.0708  608 HOH   A O   
6909 O O   B HOH   E .   ? 0.3040 0.3430 0.3349 -0.0382 -0.0830 0.1353  609 HOH   A O   
6910 O O   B HOH   E .   ? 0.3267 0.3219 0.3948 0.0060  -0.1165 0.0400  610 HOH   A O   
6911 O O   B HOH   E .   ? 0.2067 0.1903 0.2446 0.0466  -0.0187 0.0721  611 HOH   A O   
6912 O O   . HOH   E .   ? 0.2216 0.2606 0.3349 0.0320  -0.0486 0.0691  612 HOH   A O   
6913 O O   B HOH   E .   ? 0.1620 0.2810 0.2145 0.0164  -0.0757 0.0845  613 HOH   A O   
6914 O O   . HOH   E .   ? 0.3398 0.7955 0.5322 -0.0705 0.0254  0.1927  614 HOH   A O   
6915 O O   . HOH   E .   ? 0.4361 0.2001 0.4402 -0.1135 0.0035  0.0363  615 HOH   A O   
6916 O O   B HOH   E .   ? 0.3930 0.2089 0.2666 -0.0068 0.0013  -0.0237 616 HOH   A O   
6917 O O   . HOH   E .   ? 0.4972 0.6258 0.4638 0.0837  -0.0246 0.0989  617 HOH   A O   
6918 O O   . HOH   E .   ? 0.2390 0.3644 0.4263 0.0494  -0.0153 0.0230  618 HOH   A O   
6919 O O   . HOH   E .   ? 0.6297 0.3891 0.5551 0.0553  0.0936  -0.0141 619 HOH   A O   
6920 O O   . HOH   E .   ? 0.2738 0.4358 0.2787 -0.0287 -0.0012 -0.0725 620 HOH   A O   
6921 O O   . HOH   E .   ? 0.3957 0.6725 0.4171 0.0705  -0.1163 0.1284  621 HOH   A O   
6922 O O   . HOH   E .   ? 0.2441 0.1943 0.4568 0.0124  0.0425  0.0520  622 HOH   A O   
6923 O O   . HOH   E .   ? 0.4845 0.5950 0.4919 0.2894  -0.0073 0.0840  623 HOH   A O   
6924 O O   . HOH   E .   ? 0.3404 0.4563 0.3586 0.0299  0.0066  -0.1408 624 HOH   A O   
6925 O O   A HOH   E .   ? 0.3356 0.5905 0.2957 0.0280  0.0831  -0.0138 625 HOH   A O   
6926 O O   . HOH   E .   ? 0.2194 0.5984 0.3676 0.0185  -0.0014 -0.0567 626 HOH   A O   
6927 O O   . HOH   E .   ? 0.3665 0.4957 0.3656 0.1090  -0.0708 0.1175  627 HOH   A O   
6928 O O   B HOH   E .   ? 0.1725 0.1771 0.2102 -0.0012 -0.0027 0.0713  628 HOH   A O   
6929 O O   . HOH   E .   ? 0.3908 0.5885 0.4296 -0.0356 -0.0934 -0.0238 629 HOH   A O   
6930 O O   B HOH   E .   ? 0.4224 0.2056 0.2119 0.0861  -0.0134 0.0400  630 HOH   A O   
6931 O O   B HOH   E .   ? 0.3537 0.3126 0.3245 -0.0753 0.0591  0.0217  631 HOH   A O   
6932 O O   . HOH   E .   ? 0.3957 0.3882 0.5166 -0.0601 -0.1252 0.2469  632 HOH   A O   
6933 O O   . HOH   F .   ? 0.2278 0.2007 0.2758 0.0264  0.0795  0.0335  201 HOH   B O   
6934 O O   . HOH   F .   ? 0.4837 0.4916 0.2021 0.0766  -0.0726 -0.1154 202 HOH   B O   
6935 O O   . HOH   F .   ? 0.6774 0.3608 0.5042 0.0087  0.1509  -0.0202 203 HOH   B O   
6936 O O   . HOH   F .   ? 0.4241 0.3650 0.5844 0.0149  -0.1182 0.2341  204 HOH   B O   
6937 O O   . HOH   F .   ? 0.3184 0.6453 0.3122 0.1134  0.0172  0.1840  205 HOH   B O   
6938 O O   . HOH   F .   ? 0.6128 0.4843 0.5529 0.1567  -0.0012 -0.0258 206 HOH   B O   
6939 O O   . HOH   F .   ? 0.4474 0.5092 0.4465 0.2518  -0.1347 -0.0201 207 HOH   B O   
6940 O O   . HOH   F .   ? 0.4388 0.2361 0.3466 -0.0580 0.0135  -0.0904 208 HOH   B O   
6941 O O   . HOH   F .   ? 0.3703 0.4677 0.5919 -0.1150 -0.0500 -0.1424 209 HOH   B O   
6942 O O   . HOH   F .   ? 0.2699 0.2960 0.6501 0.0776  -0.1161 0.0454  210 HOH   B O   
6943 O O   . HOH   F .   ? 0.2753 0.3721 0.5346 -0.0313 0.0186  -0.0294 211 HOH   B O   
6944 O O   . HOH   F .   ? 0.1709 0.1963 0.2572 0.0006  0.0449  -0.0113 212 HOH   B O   
6945 O O   . HOH   F .   ? 0.5037 0.4451 0.3475 -0.0194 -0.0947 0.1047  213 HOH   B O   
6946 O O   . HOH   F .   ? 0.3043 0.4647 0.4949 -0.0163 0.1830  -0.1574 214 HOH   B O   
6947 O O   . HOH   F .   ? 0.3799 0.5453 0.4205 0.2528  -0.0477 0.0293  215 HOH   B O   
6948 O O   . HOH   F .   ? 0.4191 0.1819 0.4077 -0.0146 -0.1219 0.0175  216 HOH   B O   
6949 O O   . HOH   F .   ? 0.3623 0.3963 0.3543 0.0075  0.0512  -0.1341 217 HOH   B O   
6950 O O   . HOH   F .   ? 0.5784 0.2996 0.3652 -0.1994 0.0417  0.0504  218 HOH   B O   
6951 O O   . HOH   F .   ? 0.1490 0.1457 0.2485 -0.0131 -0.0027 0.0077  219 HOH   B O   
6952 O O   . HOH   F .   ? 0.2407 0.2153 0.5732 -0.0303 0.0401  0.0150  220 HOH   B O   
6953 O O   . HOH   F .   ? 0.2657 0.4221 0.5659 0.0258  -0.0580 0.0447  221 HOH   B O   
6954 O O   . HOH   F .   ? 0.3313 0.5331 0.4202 0.2270  -0.0179 -0.0971 222 HOH   B O   
6955 O O   . HOH   F .   ? 0.3682 0.4267 0.4607 -0.1934 -0.0219 0.1222  223 HOH   B O   
6956 O O   . HOH   F .   ? 0.2523 0.1652 0.2465 -0.0391 0.1247  -0.0081 224 HOH   B O   
6957 O O   . HOH   F .   ? 0.3545 0.3541 0.6085 -0.0310 -0.1487 -0.0572 225 HOH   B O   
6958 O O   . HOH   F .   ? 0.3688 0.6497 0.4022 0.2410  -0.0118 -0.0098 226 HOH   B O   
6959 O O   . HOH   F .   ? 0.2599 0.2917 0.4081 -0.0796 0.0783  -0.0427 227 HOH   B O   
6960 O O   . HOH   F .   ? 0.2833 0.1981 0.3154 -0.0039 0.1034  -0.0107 228 HOH   B O   
6961 O O   . HOH   F .   ? 0.5108 0.5483 0.3195 0.0048  -0.0486 -0.0026 229 HOH   B O   
6962 O O   . HOH   F .   ? 0.2232 0.2372 0.2947 0.0397  0.0187  -0.0836 230 HOH   B O   
6963 O O   . HOH   F .   ? 0.6228 0.4521 0.5995 0.1807  0.0741  -0.0277 231 HOH   B O   
6964 O O   . HOH   F .   ? 0.3892 0.3173 0.2212 0.0488  0.0983  0.0469  232 HOH   B O   
6965 O O   . HOH   F .   ? 0.1850 0.1167 0.3162 0.0185  -0.0579 -0.0190 233 HOH   B O   
6966 O O   . HOH   F .   ? 0.1187 0.1264 0.1616 -0.0126 -0.0062 0.0023  234 HOH   B O   
6967 O O   . HOH   F .   ? 0.3448 0.2819 0.3748 0.0509  -0.1314 -0.1554 235 HOH   B O   
6968 O O   . HOH   F .   ? 0.1827 0.1895 0.3917 -0.0275 -0.0187 -0.0609 236 HOH   B O   
6969 O O   . HOH   F .   ? 0.1383 0.1625 0.2535 -0.0103 0.0036  -0.0017 237 HOH   B O   
6970 O O   . HOH   F .   ? 0.1911 0.3750 0.2684 -0.0530 -0.0314 -0.0566 238 HOH   B O   
6971 O O   . HOH   F .   ? 0.1170 0.1134 0.1462 -0.0039 -0.0033 0.0025  239 HOH   B O   
6972 O O   . HOH   F .   ? 0.1778 0.4072 0.2268 -0.0676 -0.0235 0.0838  240 HOH   B O   
6973 O O   . HOH   F .   ? 0.5366 0.3186 0.2269 0.0742  0.1002  0.0010  241 HOH   B O   
6974 O O   . HOH   F .   ? 0.3985 0.2840 0.3930 -0.1947 0.0329  -0.0099 242 HOH   B O   
6975 O O   . HOH   F .   ? 0.1858 0.1916 0.2811 -0.0390 0.0043  -0.0299 243 HOH   B O   
6976 O O   . HOH   F .   ? 0.3979 0.2610 0.4263 -0.0341 -0.1166 -0.0602 244 HOH   B O   
6977 O O   . HOH   F .   ? 0.1902 0.2034 0.1657 0.0085  -0.0115 -0.0019 245 HOH   B O   
6978 O O   . HOH   F .   ? 0.3207 0.1824 0.4587 0.0248  0.1964  0.0736  246 HOH   B O   
6979 O O   . HOH   F .   ? 0.3365 0.4000 0.2679 0.0743  -0.0157 -0.1582 247 HOH   B O   
6980 O O   . HOH   F .   ? 0.2549 0.4240 0.4874 0.0105  0.0960  -0.1517 248 HOH   B O   
6981 O O   . HOH   F .   ? 0.1394 0.1269 0.2375 -0.0073 0.0133  -0.0190 249 HOH   B O   
6982 O O   . HOH   F .   ? 0.1953 0.1775 0.1942 -0.0269 -0.0344 0.0084  250 HOH   B O   
6983 O O   . HOH   F .   ? 0.2380 0.4842 0.3606 -0.0994 -0.0392 -0.0864 251 HOH   B O   
6984 O O   . HOH   F .   ? 0.3407 0.1576 0.2033 0.0010  -0.0658 -0.0067 252 HOH   B O   
6985 O O   . HOH   F .   ? 0.2916 0.3038 0.1735 0.0579  0.0547  0.0198  253 HOH   B O   
6986 O O   . HOH   F .   ? 0.4021 0.2392 0.3984 0.1009  -0.0486 -0.0941 254 HOH   B O   
6987 O O   . HOH   F .   ? 0.2022 0.2876 0.2273 -0.0342 0.0174  0.0592  255 HOH   B O   
6988 O O   . HOH   F .   ? 0.2746 0.1548 0.5533 -0.0185 -0.1182 -0.0117 256 HOH   B O   
6989 O O   . HOH   F .   ? 0.1411 0.1430 0.2486 -0.0181 -0.0177 0.0082  257 HOH   B O   
6990 O O   . HOH   F .   ? 0.2233 0.1850 0.1824 0.0210  -0.0072 0.0068  258 HOH   B O   
6991 O O   . HOH   F .   ? 0.1552 0.2488 0.2533 0.0440  0.0425  0.0978  259 HOH   B O   
6992 O O   . HOH   F .   ? 0.2143 0.2899 0.5376 0.0799  -0.0469 -0.1107 260 HOH   B O   
6993 O O   . HOH   F .   ? 0.2706 0.4741 0.3747 -0.0292 -0.0954 0.1211  261 HOH   B O   
6994 O O   . HOH   F .   ? 0.1866 0.1206 0.1930 -0.0188 -0.0231 0.0212  262 HOH   B O   
6995 O O   . HOH   F .   ? 0.2089 0.2042 0.2395 0.0850  -0.0734 -0.0793 263 HOH   B O   
6996 O O   . HOH   F .   ? 0.2741 0.2025 0.2907 0.0850  0.1102  0.0214  264 HOH   B O   
6997 O O   . HOH   F .   ? 0.2630 0.2080 0.2673 -0.0222 0.0113  -0.0550 265 HOH   B O   
6998 O O   . HOH   F .   ? 0.1147 0.1429 0.1695 -0.0037 0.0065  -0.0013 266 HOH   B O   
6999 O O   . HOH   F .   ? 0.3764 0.2953 0.3627 -0.0650 0.0793  -0.0916 267 HOH   B O   
7000 O O   . HOH   F .   ? 0.2300 0.2781 0.2022 -0.0280 -0.0761 0.0030  268 HOH   B O   
7001 O O   . HOH   F .   ? 0.2282 0.1786 0.2829 -0.0600 0.0028  0.0007  269 HOH   B O   
7002 O O   . HOH   F .   ? 0.2138 0.1626 0.3676 0.0018  -0.0660 -0.0402 270 HOH   B O   
7003 O O   . HOH   F .   ? 0.1535 0.1611 0.1547 -0.0370 -0.0316 0.0053  271 HOH   B O   
7004 O O   . HOH   F .   ? 0.1739 0.1334 0.2037 -0.0248 -0.0131 0.0114  272 HOH   B O   
7005 O O   . HOH   F .   ? 0.1593 0.1245 0.4417 -0.0101 -0.0288 -0.0031 273 HOH   B O   
7006 O O   . HOH   F .   ? 0.2827 0.2528 0.4436 -0.0132 -0.0521 -0.1265 274 HOH   B O   
7007 O O   . HOH   F .   ? 0.2240 0.2284 0.2294 -0.0407 -0.0560 -0.0333 275 HOH   B O   
7008 O O   . HOH   F .   ? 0.2223 0.3759 0.3621 0.0395  0.1077  0.0264  276 HOH   B O   
7009 O O   . HOH   F .   ? 0.1403 0.1392 0.2843 -0.0115 0.0139  -0.0049 277 HOH   B O   
7010 O O   . HOH   F .   ? 0.2661 0.3531 0.3239 -0.0869 0.1035  -0.1559 278 HOH   B O   
7011 O O   . HOH   F .   ? 0.3149 0.6236 0.3067 0.1358  -0.0847 0.0865  279 HOH   B O   
7012 O O   . HOH   F .   ? 0.2147 0.2503 0.1906 0.0792  -0.0125 0.0099  280 HOH   B O   
7013 O O   . HOH   F .   ? 0.5051 0.3469 0.2767 0.2297  0.0996  0.0933  281 HOH   B O   
7014 O O   . HOH   F .   ? 0.1349 0.1250 0.1607 -0.0013 0.0087  -0.0031 282 HOH   B O   
7015 O O   . HOH   F .   ? 0.2467 0.2069 0.5382 0.0102  0.0983  0.0394  283 HOH   B O   
7016 O O   . HOH   F .   ? 0.2661 0.6170 0.7244 0.1144  -0.0219 -0.1223 284 HOH   B O   
7017 O O   . HOH   F .   ? 0.2334 0.4090 0.4690 -0.0903 -0.1064 0.1077  285 HOH   B O   
7018 O O   . HOH   F .   ? 0.3352 0.1793 0.4056 -0.0689 -0.2069 0.0690  286 HOH   B O   
7019 O O   . HOH   F .   ? 0.3181 0.3178 0.4159 0.0758  -0.1005 -0.0844 287 HOH   B O   
7020 O O   . HOH   F .   ? 0.1998 0.5057 0.4480 -0.0671 -0.0483 -0.1429 288 HOH   B O   
7021 O O   . HOH   F .   ? 0.1345 0.1717 0.2404 0.0178  -0.0101 0.0045  289 HOH   B O   
7022 O O   . HOH   F .   ? 0.3765 0.3538 0.6879 0.0655  -0.0126 0.0627  290 HOH   B O   
7023 O O   . HOH   F .   ? 0.1446 0.2736 0.4777 0.0157  0.0023  -0.1232 291 HOH   B O   
7024 O O   . HOH   F .   ? 0.1338 0.1897 0.1362 -0.0129 -0.0141 0.0017  292 HOH   B O   
7025 O O   . HOH   F .   ? 0.2211 0.2328 0.2617 0.0272  -0.0669 0.0158  293 HOH   B O   
7026 O O   . HOH   F .   ? 0.2368 0.5964 0.2480 0.0339  -0.0196 -0.0251 294 HOH   B O   
7027 O O   . HOH   F .   ? 0.1831 0.1459 0.2331 -0.0155 -0.0177 -0.0137 295 HOH   B O   
7028 O O   . HOH   F .   ? 0.2805 0.2496 0.2404 -0.0073 0.0128  -0.1146 296 HOH   B O   
7029 O O   . HOH   F .   ? 0.4164 0.5590 0.4911 0.0925  -0.1136 -0.0298 297 HOH   B O   
7030 O O   . HOH   F .   ? 0.2467 0.2577 0.5180 -0.0288 -0.0718 0.1504  298 HOH   B O   
7031 O O   . HOH   F .   ? 0.5772 0.4415 0.2379 0.0965  -0.0924 -0.0581 299 HOH   B O   
7032 O O   . HOH   F .   ? 0.1522 0.1421 0.2127 0.0032  0.0018  0.0106  300 HOH   B O   
7033 O O   . HOH   F .   ? 0.4436 0.3642 0.2309 0.1277  -0.0842 0.0403  301 HOH   B O   
7034 O O   . HOH   F .   ? 0.3555 0.2637 0.1958 0.0599  -0.0761 -0.0203 302 HOH   B O   
7035 O O   . HOH   F .   ? 0.3835 0.2924 0.4387 -0.0853 -0.0095 0.0581  303 HOH   B O   
7036 O O   . HOH   F .   ? 0.4843 0.2974 0.2395 -0.1954 0.0928  -0.0188 304 HOH   B O   
7037 O O   . HOH   F .   ? 0.3517 0.1632 0.3446 0.0781  0.1670  0.0544  305 HOH   B O   
7038 O O   . HOH   F .   ? 0.2511 0.2756 0.4006 -0.0788 0.1015  -0.0563 306 HOH   B O   
7039 O O   . HOH   F .   ? 0.2444 0.2769 0.3254 -0.0557 0.0953  -0.0840 307 HOH   B O   
7040 O O   . HOH   F .   ? 0.2112 0.1253 0.2341 -0.0117 -0.0012 0.0266  308 HOH   B O   
7041 O O   . HOH   F .   ? 0.1370 0.1234 0.2623 0.0073  0.0018  -0.0107 309 HOH   B O   
7042 O O   . HOH   F .   ? 0.1413 0.1691 0.2266 -0.0217 -0.0104 0.0110  310 HOH   B O   
7043 O O   . HOH   F .   ? 0.1829 0.2174 0.5796 0.0331  -0.0386 -0.0899 311 HOH   B O   
7044 O O   . HOH   F .   ? 0.3737 0.2360 0.2582 0.1582  0.0958  0.0442  312 HOH   B O   
7045 O O   . HOH   F .   ? 0.2049 0.1284 0.3259 0.0273  -0.1133 -0.0126 313 HOH   B O   
7046 O O   . HOH   F .   ? 0.5875 0.4777 0.4073 -0.1160 -0.0029 0.0611  314 HOH   B O   
7047 O O   . HOH   F .   ? 0.3917 0.4036 0.1652 -0.0403 0.0270  0.0254  315 HOH   B O   
7048 O O   . HOH   F .   ? 0.6225 0.4565 0.5084 0.1713  0.0680  -0.0249 316 HOH   B O   
7049 O O   . HOH   F .   ? 0.4276 0.2148 0.2911 0.0317  0.0833  0.0775  317 HOH   B O   
7050 O O   . HOH   F .   ? 0.2739 0.3724 0.6726 -0.0102 -0.0618 0.1944  318 HOH   B O   
7051 O O   . HOH   F .   ? 0.4218 0.4587 0.2262 0.0749  -0.0473 -0.0836 319 HOH   B O   
7052 O O   . HOH   F .   ? 0.1883 0.1902 0.1598 -0.0134 0.0229  0.0117  320 HOH   B O   
7053 O O   . HOH   F .   ? 0.6798 0.1757 0.2514 -0.0143 -0.0635 -0.0049 321 HOH   B O   
7054 O O   . HOH   F .   ? 0.2585 0.2838 0.4058 -0.0495 -0.1346 0.1080  322 HOH   B O   
7055 O O   . HOH   F .   ? 0.2021 0.3121 0.4531 -0.0320 -0.0193 0.0294  323 HOH   B O   
7056 O O   . HOH   F .   ? 0.2351 0.2015 0.2205 0.0127  -0.0048 0.0380  324 HOH   B O   
7057 O O   . HOH   F .   ? 0.4544 0.4818 0.2923 -0.0406 -0.0838 0.0305  325 HOH   B O   
7058 O O   . HOH   F .   ? 0.1379 0.1430 0.2590 -0.0089 -0.0069 -0.0171 326 HOH   B O   
7059 O O   . HOH   F .   ? 0.5713 0.3308 0.3695 -0.0318 0.0808  0.1310  327 HOH   B O   
7060 O O   . HOH   F .   ? 0.1915 0.5944 0.5444 -0.0104 0.0600  -0.0566 328 HOH   B O   
7061 O O   . HOH   F .   ? 0.1424 0.2539 0.2183 -0.0123 -0.0250 0.0616  329 HOH   B O   
7062 O O   . HOH   F .   ? 0.3865 0.5347 0.2227 0.0482  -0.0301 0.0750  330 HOH   B O   
7063 O O   . HOH   F .   ? 0.3925 0.3224 0.4876 0.0895  0.2105  0.1820  331 HOH   B O   
7064 O O   . HOH   F .   ? 0.1655 0.1863 0.2546 0.0320  0.0402  0.0279  332 HOH   B O   
7065 O O   . HOH   F .   ? 0.5368 0.4104 0.5791 0.1098  -0.0883 0.1380  333 HOH   B O   
7066 O O   . HOH   F .   ? 0.1575 0.5431 0.5863 -0.0162 -0.0452 -0.0059 334 HOH   B O   
7067 O O   . HOH   F .   ? 0.2325 0.1744 0.5138 -0.0083 0.0241  0.0297  335 HOH   B O   
7068 O O   . HOH   F .   ? 0.6830 0.5605 0.5392 0.2927  -0.0090 -0.0547 336 HOH   B O   
7069 O O   . HOH   F .   ? 0.4989 0.3056 0.3865 0.0376  0.0537  -0.1451 337 HOH   B O   
7070 O O   . HOH   F .   ? 0.2023 0.2100 0.5020 -0.0445 0.0163  0.1162  338 HOH   B O   
7071 O O   . HOH   F .   ? 0.1443 0.2387 0.2737 0.0148  -0.0064 -0.0541 339 HOH   B O   
7072 O O   . HOH   F .   ? 0.1462 0.1243 0.2125 0.0063  -0.0179 0.0048  340 HOH   B O   
7073 O O   . HOH   F .   ? 0.4816 0.3875 0.5863 -0.0110 -0.0126 -0.1148 341 HOH   B O   
7074 O O   . HOH   F .   ? 0.3937 0.5751 0.3566 -0.0057 -0.0563 0.0275  342 HOH   B O   
7075 O O   . HOH   F .   ? 0.4601 0.3533 0.3021 0.0714  -0.0978 -0.0855 343 HOH   B O   
7076 O O   . HOH   F .   ? 0.1850 0.1717 0.2723 -0.0079 0.0525  -0.0052 344 HOH   B O   
7077 O O   . HOH   F .   ? 0.6583 0.6471 0.2754 0.0396  -0.0473 0.1394  345 HOH   B O   
7078 O O   . HOH   F .   ? 0.4465 0.5912 0.3861 -0.1253 -0.0941 -0.0876 346 HOH   B O   
7079 O O   . HOH   F .   ? 0.3748 0.4169 0.4438 0.0066  -0.0636 0.0684  347 HOH   B O   
7080 O O   . HOH   F .   ? 0.3929 0.5843 0.6319 0.0678  0.0051  -0.0657 348 HOH   B O   
7081 O O   . HOH   F .   ? 0.5170 0.5796 0.5069 -0.1234 0.0988  0.1282  349 HOH   B O   
7082 O O   . HOH   F .   ? 0.2512 0.2019 0.5092 -0.0085 -0.1044 -0.0579 350 HOH   B O   
7083 O O   . HOH   F .   ? 0.1919 0.3294 0.5346 0.0236  0.0561  0.0221  351 HOH   B O   
7084 O O   . HOH   F .   ? 0.2296 0.5343 0.3361 0.1536  -0.0425 -0.1327 352 HOH   B O   
7085 O O   . HOH   F .   ? 0.3053 0.5288 0.4510 -0.1743 0.0075  0.0042  353 HOH   B O   
7086 O O   . HOH   F .   ? 0.4187 0.2570 0.5192 -0.0691 0.1654  0.0530  354 HOH   B O   
7087 O O   . HOH   F .   ? 0.4591 0.3448 0.3833 0.0813  0.1233  -0.0558 355 HOH   B O   
7088 O O   . HOH   F .   ? 0.3418 0.2324 0.3385 -0.0906 0.0213  -0.1079 356 HOH   B O   
7089 O O   . HOH   F .   ? 0.2928 0.1681 0.3488 0.0422  -0.1206 -0.0414 357 HOH   B O   
7090 O O   . HOH   F .   ? 0.3323 0.2501 0.4207 -0.0815 0.0094  -0.0656 358 HOH   B O   
7091 O O   . HOH   F .   ? 0.4503 0.5047 0.5721 0.2022  -0.1316 0.1495  359 HOH   B O   
7092 O O   . HOH   F .   ? 0.4472 0.3283 0.4412 0.0301  -0.1700 -0.0189 360 HOH   B O   
7093 O O   . HOH   F .   ? 0.4964 0.5433 0.5403 -0.1002 -0.0471 0.0422  361 HOH   B O   
7094 O O   . HOH   F .   ? 0.4233 0.3747 0.5497 0.0212  0.1099  0.0803  362 HOH   B O   
7095 O O   . HOH   F .   ? 0.4608 0.6096 0.2711 0.2319  -0.0292 0.0333  363 HOH   B O   
7096 O O   . HOH   F .   ? 0.1847 0.3353 0.5684 -0.0616 -0.0419 -0.0912 364 HOH   B O   
7097 O O   . HOH   F .   ? 0.6255 0.3898 0.4178 0.0570  0.1056  0.0520  365 HOH   B O   
7098 O O   . HOH   F .   ? 0.4726 0.3050 0.4707 0.0710  -0.1613 0.0047  366 HOH   B O   
7099 O O   . HOH   F .   ? 0.4706 0.2965 0.4862 -0.1490 -0.0035 0.0068  367 HOH   B O   
7100 O O   . HOH   F .   ? 0.6247 0.4810 0.3464 0.1624  -0.1265 0.0438  368 HOH   B O   
7101 O O   . HOH   F .   ? 0.4560 0.4968 0.5943 0.2535  0.1097  0.1462  369 HOH   B O   
7102 O O   . HOH   F .   ? 0.4761 0.4192 0.4249 0.0479  -0.1050 -0.0839 370 HOH   B O   
7103 O O   . HOH   F .   ? 0.4321 0.3117 0.5035 0.0858  -0.1483 -0.0584 371 HOH   B O   
7104 O O   . HOH   F .   ? 0.7311 0.6205 0.4337 0.2164  -0.1328 0.0728  372 HOH   B O   
7105 O O   . HOH   F .   ? 0.6311 0.3765 0.2929 -0.1454 -0.0725 -0.0576 373 HOH   B O   
7106 O O   . HOH   F .   ? 0.5311 0.1800 0.2902 0.0307  0.0381  0.0369  374 HOH   B O   
7107 O O   . HOH   F .   ? 0.4057 0.4858 0.4459 -0.1278 -0.0612 0.0933  375 HOH   B O   
7108 O O   . HOH   F .   ? 0.2747 0.3817 0.1939 0.0726  0.0214  -0.0039 376 HOH   B O   
7109 O O   . HOH   F .   ? 0.2184 0.3689 0.4696 0.0702  -0.0947 -0.0710 377 HOH   B O   
7110 O O   . HOH   F .   ? 0.4850 0.6058 0.6099 0.1293  0.0544  0.2794  378 HOH   B O   
7111 O O   . HOH   F .   ? 0.6351 0.3554 0.5638 -0.0325 -0.0735 -0.0389 379 HOH   B O   
7112 O O   . HOH   F .   ? 0.5250 0.7019 0.3884 -0.1338 0.0591  -0.1433 380 HOH   B O   
7113 O O   . HOH   F .   ? 0.3541 0.4177 0.4508 0.1381  -0.0170 0.0360  381 HOH   B O   
7114 O O   . HOH   F .   ? 0.2965 0.2259 0.3154 -0.0114 0.0048  0.0513  382 HOH   B O   
7115 O O   . HOH   F .   ? 0.5070 0.6574 0.5558 0.0714  0.1829  0.1447  383 HOH   B O   
7116 O O   . HOH   F .   ? 0.3835 0.6919 0.5932 0.0471  0.2250  0.1210  384 HOH   B O   
7117 O O   . HOH   F .   ? 0.4045 0.3330 0.2614 0.0294  0.0214  -0.0306 385 HOH   B O   
7118 O O   . HOH   F .   ? 0.6962 0.3920 0.4220 0.0760  0.0495  -0.1328 386 HOH   B O   
7119 O O   . HOH   F .   ? 0.5573 0.4253 0.4601 -0.0956 -0.0084 -0.0364 387 HOH   B O   
7120 O O   . HOH   F .   ? 0.2242 0.3848 0.3454 -0.0620 -0.0823 -0.0516 388 HOH   B O   
7121 O O   . HOH   F .   ? 0.6529 0.5781 0.4007 0.1983  0.0009  0.1014  389 HOH   B O   
7122 O O   . HOH   F .   ? 0.4656 0.4456 0.4079 -0.0412 -0.0869 -0.0532 390 HOH   B O   
7123 O O   . HOH   F .   ? 0.3755 0.3750 0.3071 -0.0680 -0.0070 0.0471  391 HOH   B O   
7124 O O   . HOH   F .   ? 0.3673 0.1946 0.3028 0.0618  -0.0320 0.0002  392 HOH   B O   
7125 O O   . HOH   F .   ? 0.2167 0.4452 0.5913 -0.1286 -0.0595 0.0325  393 HOH   B O   
7126 O O   . HOH   F .   ? 0.3858 0.2054 0.5224 -0.0492 0.0658  0.0515  394 HOH   B O   
7127 O O   . HOH   F .   ? 0.5478 0.6432 0.6599 0.1264  -0.0710 0.2730  395 HOH   B O   
7128 O O   . HOH   F .   ? 0.4042 0.5597 0.3918 0.1690  0.0084  -0.1008 396 HOH   B O   
7129 O O   . HOH   F .   ? 0.3192 0.3783 0.3434 0.0609  -0.0088 -0.0637 397 HOH   B O   
7130 O O   . HOH   F .   ? 0.4161 0.4399 0.3400 -0.0379 0.0891  0.0191  398 HOH   B O   
7131 O O   . HOH   F .   ? 0.1901 0.2776 0.5215 -0.0538 -0.0930 0.0114  399 HOH   B O   
7132 O O   . HOH   F .   ? 0.5834 0.3906 0.3242 -0.1928 0.0395  0.1146  400 HOH   B O   
7133 O O   . HOH   F .   ? 0.5603 0.5629 0.3631 0.1552  -0.0042 0.0340  401 HOH   B O   
# 
