data_7HCP
# 
_entry.id   7HCP 
# 
_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   7HCP         pdb_00007hcp 10.2210/pdb7hcp/pdb 
WWPDB D_1001407307 ?            ?                   
# 
_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                        7HCP 
_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 '(8R)-6-(7-fluoro-2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)-6-azaspiro[4.5]decane-8-carboxylic acid' 374.406 
1   ?                      ? ? ?                                                                                    
3 water       nat water                                                                                                    18.015 
408 ?                      ? ? ?                                                                                    
# 
_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 '(8R)-6-(7-fluoro-2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)-6-azaspiro[4.5]decane-8-carboxylic acid' A1A5Y 
3 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 
A1A5Y non-polymer         . 
'(8R)-6-(7-fluoro-2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)-6-azaspiro[4.5]decane-8-carboxylic acid' ? 'C20 H23 F N2 O4' 
374.406 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
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 A1A5Y 1   201 201  A1A5Y LA1 A . 
D 3 HOH   1   301 196  HOH   HOH A . 
D 3 HOH   2   302 292  HOH   HOH A . 
D 3 HOH   3   303 1301 HOH   HOH A . 
D 3 HOH   4   304 93   HOH   HOH A . 
D 3 HOH   5   305 74   HOH   HOH A . 
D 3 HOH   6   306 209  HOH   HOH A . 
D 3 HOH   7   307 278  HOH   HOH A . 
D 3 HOH   8   308 625  HOH   HOH A . 
D 3 HOH   9   309 229  HOH   HOH A . 
D 3 HOH   10  310 39   HOH   HOH A . 
D 3 HOH   11  311 393  HOH   HOH A . 
D 3 HOH   12  312 26   HOH   HOH A . 
D 3 HOH   13  313 86   HOH   HOH A . 
D 3 HOH   14  314 21   HOH   HOH A . 
D 3 HOH   15  315 85   HOH   HOH A . 
D 3 HOH   16  316 76   HOH   HOH A . 
D 3 HOH   17  317 124  HOH   HOH A . 
D 3 HOH   18  318 57   HOH   HOH A . 
D 3 HOH   19  319 105  HOH   HOH A . 
D 3 HOH   20  320 1295 HOH   HOH A . 
D 3 HOH   21  321 96   HOH   HOH A . 
D 3 HOH   22  322 337  HOH   HOH A . 
D 3 HOH   23  323 109  HOH   HOH A . 
D 3 HOH   24  324 225  HOH   HOH A . 
D 3 HOH   25  325 136  HOH   HOH A . 
D 3 HOH   26  326 964  HOH   HOH A . 
D 3 HOH   27  327 192  HOH   HOH A . 
D 3 HOH   28  328 236  HOH   HOH A . 
D 3 HOH   29  329 151  HOH   HOH A . 
D 3 HOH   30  330 15   HOH   HOH A . 
D 3 HOH   31  331 396  HOH   HOH A . 
D 3 HOH   32  332 1290 HOH   HOH A . 
D 3 HOH   33  333 140  HOH   HOH A . 
D 3 HOH   34  334 630  HOH   HOH A . 
D 3 HOH   35  335 661  HOH   HOH A . 
D 3 HOH   36  336 164  HOH   HOH A . 
D 3 HOH   37  337 320  HOH   HOH A . 
D 3 HOH   38  338 469  HOH   HOH A . 
D 3 HOH   39  339 36   HOH   HOH A . 
D 3 HOH   40  340 662  HOH   HOH A . 
D 3 HOH   41  341 153  HOH   HOH A . 
D 3 HOH   42  342 303  HOH   HOH A . 
D 3 HOH   43  343 1289 HOH   HOH A . 
D 3 HOH   44  344 1300 HOH   HOH A . 
D 3 HOH   45  345 49   HOH   HOH A . 
D 3 HOH   46  346 92   HOH   HOH A . 
D 3 HOH   47  347 247  HOH   HOH A . 
D 3 HOH   48  348 139  HOH   HOH A . 
D 3 HOH   49  349 102  HOH   HOH A . 
D 3 HOH   50  350 24   HOH   HOH A . 
D 3 HOH   51  351 42   HOH   HOH A . 
D 3 HOH   52  352 17   HOH   HOH A . 
D 3 HOH   53  353 2    HOH   HOH A . 
D 3 HOH   54  354 81   HOH   HOH A . 
D 3 HOH   55  355 8    HOH   HOH A . 
D 3 HOH   56  356 241  HOH   HOH A . 
D 3 HOH   57  357 354  HOH   HOH A . 
D 3 HOH   58  358 165  HOH   HOH A . 
D 3 HOH   59  359 162  HOH   HOH A . 
D 3 HOH   60  360 138  HOH   HOH A . 
D 3 HOH   61  361 66   HOH   HOH A . 
D 3 HOH   62  362 218  HOH   HOH A . 
D 3 HOH   63  363 939  HOH   HOH A . 
D 3 HOH   64  364 19   HOH   HOH A . 
D 3 HOH   65  365 1283 HOH   HOH A . 
D 3 HOH   66  366 296  HOH   HOH A . 
D 3 HOH   67  367 169  HOH   HOH A . 
D 3 HOH   68  368 1310 HOH   HOH A . 
D 3 HOH   69  369 155  HOH   HOH A . 
D 3 HOH   70  370 5    HOH   HOH A . 
D 3 HOH   71  371 409  HOH   HOH A . 
D 3 HOH   72  372 1    HOH   HOH A . 
D 3 HOH   73  373 27   HOH   HOH A . 
D 3 HOH   74  374 78   HOH   HOH A . 
D 3 HOH   75  375 134  HOH   HOH A . 
D 3 HOH   76  376 45   HOH   HOH A . 
D 3 HOH   77  377 46   HOH   HOH A . 
D 3 HOH   78  378 56   HOH   HOH A . 
D 3 HOH   79  379 159  HOH   HOH A . 
D 3 HOH   80  380 18   HOH   HOH A . 
D 3 HOH   81  381 148  HOH   HOH A . 
D 3 HOH   82  382 405  HOH   HOH A . 
D 3 HOH   83  383 186  HOH   HOH A . 
D 3 HOH   84  384 154  HOH   HOH A . 
D 3 HOH   85  385 1308 HOH   HOH A . 
D 3 HOH   86  386 33   HOH   HOH A . 
D 3 HOH   87  387 35   HOH   HOH A . 
D 3 HOH   88  388 121  HOH   HOH A . 
D 3 HOH   89  389 195  HOH   HOH A . 
D 3 HOH   90  390 58   HOH   HOH A . 
D 3 HOH   91  391 7    HOH   HOH A . 
D 3 HOH   92  392 83   HOH   HOH A . 
D 3 HOH   93  393 34   HOH   HOH A . 
D 3 HOH   94  394 116  HOH   HOH A . 
D 3 HOH   95  395 493  HOH   HOH A . 
D 3 HOH   96  396 12   HOH   HOH A . 
D 3 HOH   97  397 4    HOH   HOH A . 
D 3 HOH   98  398 461  HOH   HOH A . 
D 3 HOH   99  399 199  HOH   HOH A . 
D 3 HOH   100 400 366  HOH   HOH A . 
D 3 HOH   101 401 1309 HOH   HOH A . 
D 3 HOH   102 402 67   HOH   HOH A . 
D 3 HOH   103 403 132  HOH   HOH A . 
D 3 HOH   104 404 6    HOH   HOH A . 
D 3 HOH   105 405 1068 HOH   HOH A . 
D 3 HOH   106 406 3    HOH   HOH A . 
D 3 HOH   107 407 1275 HOH   HOH A . 
D 3 HOH   108 408 381  HOH   HOH A . 
D 3 HOH   109 409 1279 HOH   HOH A . 
D 3 HOH   110 410 281  HOH   HOH A . 
D 3 HOH   111 411 397  HOH   HOH A . 
D 3 HOH   112 412 333  HOH   HOH A . 
D 3 HOH   113 413 351  HOH   HOH A . 
D 3 HOH   114 414 95   HOH   HOH A . 
D 3 HOH   115 415 582  HOH   HOH A . 
D 3 HOH   116 416 123  HOH   HOH A . 
D 3 HOH   117 417 68   HOH   HOH A . 
D 3 HOH   118 418 25   HOH   HOH A . 
D 3 HOH   119 419 125  HOH   HOH A . 
D 3 HOH   120 420 53   HOH   HOH A . 
D 3 HOH   121 421 1222 HOH   HOH A . 
D 3 HOH   122 422 1315 HOH   HOH A . 
D 3 HOH   123 423 115  HOH   HOH A . 
D 3 HOH   124 424 122  HOH   HOH A . 
D 3 HOH   125 425 51   HOH   HOH A . 
D 3 HOH   126 426 212  HOH   HOH A . 
D 3 HOH   127 427 156  HOH   HOH A . 
D 3 HOH   128 428 1286 HOH   HOH A . 
D 3 HOH   129 429 70   HOH   HOH A . 
D 3 HOH   130 430 1296 HOH   HOH A . 
D 3 HOH   131 431 16   HOH   HOH A . 
D 3 HOH   132 432 71   HOH   HOH A . 
D 3 HOH   133 433 944  HOH   HOH A . 
D 3 HOH   134 434 1189 HOH   HOH A . 
D 3 HOH   135 435 40   HOH   HOH A . 
D 3 HOH   136 436 80   HOH   HOH A . 
D 3 HOH   137 437 952  HOH   HOH A . 
D 3 HOH   138 438 94   HOH   HOH A . 
D 3 HOH   139 439 188  HOH   HOH A . 
D 3 HOH   140 440 73   HOH   HOH A . 
D 3 HOH   141 441 1313 HOH   HOH A . 
D 3 HOH   142 442 97   HOH   HOH A . 
D 3 HOH   143 443 1238 HOH   HOH A . 
D 3 HOH   144 444 576  HOH   HOH A . 
D 3 HOH   145 445 104  HOH   HOH A . 
D 3 HOH   146 446 79   HOH   HOH A . 
D 3 HOH   147 447 1094 HOH   HOH A . 
D 3 HOH   148 448 376  HOH   HOH A . 
D 3 HOH   149 449 107  HOH   HOH A . 
D 3 HOH   150 450 1119 HOH   HOH A . 
D 3 HOH   151 451 330  HOH   HOH A . 
D 3 HOH   152 452 509  HOH   HOH A . 
D 3 HOH   153 453 1134 HOH   HOH A . 
D 3 HOH   154 454 408  HOH   HOH A . 
D 3 HOH   155 455 163  HOH   HOH A . 
D 3 HOH   156 456 202  HOH   HOH A . 
D 3 HOH   157 457 726  HOH   HOH A . 
D 3 HOH   158 458 756  HOH   HOH A . 
D 3 HOH   159 459 801  HOH   HOH A . 
D 3 HOH   160 460 361  HOH   HOH A . 
D 3 HOH   161 461 63   HOH   HOH A . 
D 3 HOH   162 462 342  HOH   HOH A . 
D 3 HOH   163 463 126  HOH   HOH A . 
D 3 HOH   164 464 280  HOH   HOH A . 
D 3 HOH   165 465 319  HOH   HOH A . 
D 3 HOH   166 466 556  HOH   HOH A . 
D 3 HOH   167 467 1307 HOH   HOH A . 
D 3 HOH   168 468 1276 HOH   HOH A . 
D 3 HOH   169 469 250  HOH   HOH A . 
D 3 HOH   170 470 370  HOH   HOH A . 
D 3 HOH   171 471 1287 HOH   HOH A . 
D 3 HOH   172 472 1306 HOH   HOH A . 
D 3 HOH   173 473 224  HOH   HOH A . 
D 3 HOH   174 474 711  HOH   HOH A . 
D 3 HOH   175 475 135  HOH   HOH A . 
D 3 HOH   176 476 695  HOH   HOH A . 
D 3 HOH   177 477 674  HOH   HOH A . 
D 3 HOH   178 478 919  HOH   HOH A . 
D 3 HOH   179 479 267  HOH   HOH A . 
D 3 HOH   180 480 326  HOH   HOH A . 
D 3 HOH   181 481 309  HOH   HOH A . 
D 3 HOH   182 482 318  HOH   HOH A . 
D 3 HOH   183 483 805  HOH   HOH A . 
D 3 HOH   184 484 1299 HOH   HOH A . 
D 3 HOH   185 485 331  HOH   HOH A . 
D 3 HOH   186 486 521  HOH   HOH A . 
D 3 HOH   187 487 1314 HOH   HOH A . 
D 3 HOH   188 488 315  HOH   HOH A . 
D 3 HOH   189 489 152  HOH   HOH A . 
D 3 HOH   190 490 263  HOH   HOH A . 
D 3 HOH   191 491 941  HOH   HOH A . 
D 3 HOH   192 492 208  HOH   HOH A . 
D 3 HOH   193 493 1071 HOH   HOH A . 
D 3 HOH   194 494 180  HOH   HOH A . 
D 3 HOH   195 495 356  HOH   HOH A . 
D 3 HOH   196 496 350  HOH   HOH A . 
D 3 HOH   197 497 363  HOH   HOH A . 
D 3 HOH   198 498 313  HOH   HOH A . 
D 3 HOH   199 499 371  HOH   HOH A . 
D 3 HOH   200 500 1284 HOH   HOH A . 
D 3 HOH   201 501 185  HOH   HOH A . 
D 3 HOH   202 502 429  HOH   HOH A . 
D 3 HOH   203 503 772  HOH   HOH A . 
D 3 HOH   204 504 1074 HOH   HOH A . 
D 3 HOH   205 505 346  HOH   HOH A . 
D 3 HOH   206 506 1292 HOH   HOH A . 
D 3 HOH   207 507 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 549  HOH   HOH B . 
E 3 HOH   3   203 240  HOH   HOH B . 
E 3 HOH   4   204 398  HOH   HOH B . 
E 3 HOH   5   205 358  HOH   HOH B . 
E 3 HOH   6   206 758  HOH   HOH B . 
E 3 HOH   7   207 364  HOH   HOH B . 
E 3 HOH   8   208 264  HOH   HOH B . 
E 3 HOH   9   209 353  HOH   HOH B . 
E 3 HOH   10  210 900  HOH   HOH B . 
E 3 HOH   11  211 120  HOH   HOH B . 
E 3 HOH   12  212 1249 HOH   HOH B . 
E 3 HOH   13  213 743  HOH   HOH B . 
E 3 HOH   14  214 654  HOH   HOH B . 
E 3 HOH   15  215 50   HOH   HOH B . 
E 3 HOH   16  216 205  HOH   HOH B . 
E 3 HOH   17  217 232  HOH   HOH B . 
E 3 HOH   18  218 343  HOH   HOH B . 
E 3 HOH   19  219 531  HOH   HOH B . 
E 3 HOH   20  220 54   HOH   HOH B . 
E 3 HOH   21  221 444  HOH   HOH B . 
E 3 HOH   22  222 276  HOH   HOH B . 
E 3 HOH   23  223 272  HOH   HOH B . 
E 3 HOH   24  224 75   HOH   HOH B . 
E 3 HOH   25  225 131  HOH   HOH B . 
E 3 HOH   26  226 133  HOH   HOH B . 
E 3 HOH   27  227 332  HOH   HOH B . 
E 3 HOH   28  228 723  HOH   HOH B . 
E 3 HOH   29  229 128  HOH   HOH B . 
E 3 HOH   30  230 1312 HOH   HOH B . 
E 3 HOH   31  231 300  HOH   HOH B . 
E 3 HOH   32  232 325  HOH   HOH B . 
E 3 HOH   33  233 127  HOH   HOH B . 
E 3 HOH   34  234 452  HOH   HOH B . 
E 3 HOH   35  235 82   HOH   HOH B . 
E 3 HOH   36  236 1140 HOH   HOH B . 
E 3 HOH   37  237 69   HOH   HOH B . 
E 3 HOH   38  238 1    HOH   HOH B . 
E 3 HOH   39  239 110  HOH   HOH B . 
E 3 HOH   40  240 1278 HOH   HOH B . 
E 3 HOH   41  241 30   HOH   HOH B . 
E 3 HOH   42  242 166  HOH   HOH B . 
E 3 HOH   43  243 129  HOH   HOH B . 
E 3 HOH   44  244 14   HOH   HOH B . 
E 3 HOH   45  245 9    HOH   HOH B . 
E 3 HOH   46  246 181  HOH   HOH B . 
E 3 HOH   47  247 144  HOH   HOH B . 
E 3 HOH   48  248 231  HOH   HOH B . 
E 3 HOH   49  249 282  HOH   HOH B . 
E 3 HOH   50  250 72   HOH   HOH B . 
E 3 HOH   51  251 52   HOH   HOH B . 
E 3 HOH   52  252 60   HOH   HOH B . 
E 3 HOH   53  253 47   HOH   HOH B . 
E 3 HOH   54  254 1277 HOH   HOH B . 
E 3 HOH   55  255 172  HOH   HOH B . 
E 3 HOH   56  256 150  HOH   HOH B . 
E 3 HOH   57  257 31   HOH   HOH B . 
E 3 HOH   58  258 103  HOH   HOH B . 
E 3 HOH   59  259 143  HOH   HOH B . 
E 3 HOH   60  260 252  HOH   HOH B . 
E 3 HOH   61  261 10   HOH   HOH B . 
E 3 HOH   62  262 287  HOH   HOH B . 
E 3 HOH   63  263 41   HOH   HOH B . 
E 3 HOH   64  264 271  HOH   HOH B . 
E 3 HOH   65  265 62   HOH   HOH B . 
E 3 HOH   66  266 59   HOH   HOH B . 
E 3 HOH   67  267 77   HOH   HOH B . 
E 3 HOH   68  268 347  HOH   HOH B . 
E 3 HOH   69  269 61   HOH   HOH B . 
E 3 HOH   70  270 20   HOH   HOH B . 
E 3 HOH   71  271 175  HOH   HOH B . 
E 3 HOH   72  272 11   HOH   HOH B . 
E 3 HOH   73  273 391  HOH   HOH B . 
E 3 HOH   74  274 243  HOH   HOH B . 
E 3 HOH   75  275 84   HOH   HOH B . 
E 3 HOH   76  276 147  HOH   HOH B . 
E 3 HOH   77  277 302  HOH   HOH B . 
E 3 HOH   78  278 242  HOH   HOH B . 
E 3 HOH   79  279 114  HOH   HOH B . 
E 3 HOH   80  280 117  HOH   HOH B . 
E 3 HOH   81  281 43   HOH   HOH B . 
E 3 HOH   82  282 1106 HOH   HOH B . 
E 3 HOH   83  283 106  HOH   HOH B . 
E 3 HOH   84  284 22   HOH   HOH B . 
E 3 HOH   85  285 89   HOH   HOH B . 
E 3 HOH   86  286 221  HOH   HOH B . 
E 3 HOH   87  287 416  HOH   HOH B . 
E 3 HOH   88  288 635  HOH   HOH B . 
E 3 HOH   89  289 341  HOH   HOH B . 
E 3 HOH   90  290 99   HOH   HOH B . 
E 3 HOH   91  291 1305 HOH   HOH B . 
E 3 HOH   92  292 13   HOH   HOH B . 
E 3 HOH   93  293 88   HOH   HOH B . 
E 3 HOH   94  294 297  HOH   HOH B . 
E 3 HOH   95  295 160  HOH   HOH B . 
E 3 HOH   96  296 1066 HOH   HOH B . 
E 3 HOH   97  297 137  HOH   HOH B . 
E 3 HOH   98  298 387  HOH   HOH B . 
E 3 HOH   99  299 235  HOH   HOH B . 
E 3 HOH   100 300 112  HOH   HOH B . 
E 3 HOH   101 301 32   HOH   HOH B . 
E 3 HOH   102 302 316  HOH   HOH B . 
E 3 HOH   103 303 216  HOH   HOH B . 
E 3 HOH   104 304 220  HOH   HOH B . 
E 3 HOH   105 305 142  HOH   HOH B . 
E 3 HOH   106 306 215  HOH   HOH B . 
E 3 HOH   107 307 118  HOH   HOH B . 
E 3 HOH   108 308 311  HOH   HOH B . 
E 3 HOH   109 309 299  HOH   HOH B . 
E 3 HOH   110 310 101  HOH   HOH B . 
E 3 HOH   111 311 170  HOH   HOH B . 
E 3 HOH   112 312 1285 HOH   HOH B . 
E 3 HOH   113 313 38   HOH   HOH B . 
E 3 HOH   114 314 91   HOH   HOH B . 
E 3 HOH   115 315 37   HOH   HOH B . 
E 3 HOH   116 316 55   HOH   HOH B . 
E 3 HOH   117 317 48   HOH   HOH B . 
E 3 HOH   118 318 23   HOH   HOH B . 
E 3 HOH   119 319 704  HOH   HOH B . 
E 3 HOH   120 320 44   HOH   HOH B . 
E 3 HOH   121 321 177  HOH   HOH B . 
E 3 HOH   122 322 1291 HOH   HOH B . 
E 3 HOH   123 323 100  HOH   HOH B . 
E 3 HOH   124 324 1126 HOH   HOH B . 
E 3 HOH   125 325 28   HOH   HOH B . 
E 3 HOH   126 326 1294 HOH   HOH B . 
E 3 HOH   127 327 161  HOH   HOH B . 
E 3 HOH   128 328 141  HOH   HOH B . 
E 3 HOH   129 329 29   HOH   HOH B . 
E 3 HOH   130 330 717  HOH   HOH B . 
E 3 HOH   131 331 334  HOH   HOH B . 
E 3 HOH   132 332 98   HOH   HOH B . 
E 3 HOH   133 333 182  HOH   HOH B . 
E 3 HOH   134 334 1274 HOH   HOH B . 
E 3 HOH   135 335 65   HOH   HOH B . 
E 3 HOH   136 336 445  HOH   HOH B . 
E 3 HOH   137 337 619  HOH   HOH B . 
E 3 HOH   138 338 197  HOH   HOH B . 
E 3 HOH   139 339 207  HOH   HOH B . 
E 3 HOH   140 340 362  HOH   HOH B . 
E 3 HOH   141 341 1293 HOH   HOH B . 
E 3 HOH   142 342 960  HOH   HOH B . 
E 3 HOH   143 343 234  HOH   HOH B . 
E 3 HOH   144 344 178  HOH   HOH B . 
E 3 HOH   145 345 339  HOH   HOH B . 
E 3 HOH   146 346 90   HOH   HOH B . 
E 3 HOH   147 347 623  HOH   HOH B . 
E 3 HOH   148 348 87   HOH   HOH B . 
E 3 HOH   149 349 335  HOH   HOH B . 
E 3 HOH   150 350 191  HOH   HOH B . 
E 3 HOH   151 351 463  HOH   HOH B . 
E 3 HOH   152 352 1280 HOH   HOH B . 
E 3 HOH   153 353 203  HOH   HOH B . 
E 3 HOH   154 354 1046 HOH   HOH B . 
E 3 HOH   155 355 1304 HOH   HOH B . 
E 3 HOH   156 356 304  HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 541  HOH   HOH B . 
E 3 HOH   159 359 479  HOH   HOH B . 
E 3 HOH   160 360 1077 HOH   HOH B . 
E 3 HOH   161 361 389  HOH   HOH B . 
E 3 HOH   162 362 718  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 283  HOH   HOH B . 
E 3 HOH   165 365 373  HOH   HOH B . 
E 3 HOH   166 366 1316 HOH   HOH B . 
E 3 HOH   167 367 291  HOH   HOH B . 
E 3 HOH   168 368 898  HOH   HOH B . 
E 3 HOH   169 369 340  HOH   HOH B . 
E 3 HOH   170 370 615  HOH   HOH B . 
E 3 HOH   171 371 667  HOH   HOH B . 
E 3 HOH   172 372 190  HOH   HOH B . 
E 3 HOH   173 373 310  HOH   HOH B . 
E 3 HOH   174 374 1303 HOH   HOH B . 
E 3 HOH   175 375 431  HOH   HOH B . 
E 3 HOH   176 376 149  HOH   HOH B . 
E 3 HOH   177 377 183  HOH   HOH B . 
E 3 HOH   178 378 1173 HOH   HOH B . 
E 3 HOH   179 379 1163 HOH   HOH B . 
E 3 HOH   180 380 1000 HOH   HOH B . 
E 3 HOH   181 381 418  HOH   HOH B . 
E 3 HOH   182 382 1311 HOH   HOH B . 
E 3 HOH   183 383 176  HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 491  HOH   HOH B . 
E 3 HOH   186 386 1298 HOH   HOH B . 
E 3 HOH   187 387 981  HOH   HOH B . 
E 3 HOH   188 388 470  HOH   HOH B . 
E 3 HOH   189 389 248  HOH   HOH B . 
E 3 HOH   190 390 265  HOH   HOH B . 
E 3 HOH   191 391 184  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 355  HOH   HOH B . 
E 3 HOH   194 394 410  HOH   HOH B . 
E 3 HOH   195 395 274  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 157  HOH   HOH B . 
E 3 HOH   198 398 566  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 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           7HCP 
_cell.length_a           88.687 
_cell.length_b           88.687 
_cell.length_c           39.597 
_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                         7HCP 
_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          7HCP 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.67 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2022-07-25 
_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   0.72929 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.pdbx_wavelength_list        0.72929 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HCP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.340 
_reflns.d_resolution_high            0.960 
_reflns.number_obs                   186880 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.049 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.000 
_reflns.B_iso_Wilson_estimate        12.440 
_reflns.pdbx_redundancy              6.700 
_reflns.pdbx_Rrim_I_all              0.054 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1242776 
_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 0.960 0.980  ? 53687 8973 ? 3.511 ? ? ? 6.000 ? 0.500  ? ? ? ? ? ? 96.900 3.846 1.546 0.303 ? 
1 2 5.260 44.340 ? 8412  1225 ? 0.032 ? ? ? 6.900 ? 54.700 ? ? ? ? ? ? 99.400 0.035 0.013 0.998 ? 
# 
_refine.entry_id                                 7HCP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9600 
_refine.ls_d_res_low                             28.0500 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2500 
_refine.ls_number_reflns_obs                     186196 
_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                          0.1525 
_refine.ls_R_factor_R_work                       0.1518 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1658 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  8935 
_refine.ls_number_reflns_R_work                  177261 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.4590 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1700 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                69.560 
_refine.B_iso_min                                8.390 
_refine.pdbx_overall_phase_error                 22.4100 
_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                       0.9600 
_refine_hist.d_res_low                        28.0500 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             408 
_refine_hist.number_atoms_total               2999 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.60 
_refine_hist.pdbx_B_iso_mean_solvent          31.86 
_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 
0.9600 0.9700  30 89.0000  5236 . 0.5331 0.5128 . 281 0.0000 5517 . 'X-RAY DIFFRACTION' . 
0.9700 0.9800  30 98.0000  5845 . 0.4820 0.4426 . 278 0.0000 6123 . 'X-RAY DIFFRACTION' . 
0.9800 0.9900  30 100.0000 5898 . 0.4427 0.4469 . 285 0.0000 6183 . 'X-RAY DIFFRACTION' . 
0.9900 1.0100  30 100.0000 5913 . 0.4034 0.3965 . 286 0.0000 6199 . 'X-RAY DIFFRACTION' . 
1.0100 1.0200  30 100.0000 5951 . 0.3685 0.3417 . 284 0.0000 6235 . 'X-RAY DIFFRACTION' . 
1.0200 1.0300  30 100.0000 5914 . 0.3394 0.3485 . 269 0.0000 6183 . 'X-RAY DIFFRACTION' . 
1.0300 1.0500  30 100.0000 5896 . 0.3058 0.2780 . 314 0.0000 6210 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5847 . 0.2676 0.2977 . 359 0.0000 6206 . 'X-RAY DIFFRACTION' . 
1.0600 1.0800  30 100.0000 5974 . 0.2409 0.2469 . 301 0.0000 6275 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 5920 . 0.2244 0.2400 . 280 0.0000 6200 . 'X-RAY DIFFRACTION' . 
1.1000 1.1200  30 99.0000  5812 . 0.2064 0.2099 . 312 0.0000 6124 . 'X-RAY DIFFRACTION' . 
1.1200 1.1400  30 98.0000  5879 . 0.2020 0.2126 . 244 0.0000 6123 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5937 . 0.1750 0.1964 . 294 0.0000 6231 . 'X-RAY DIFFRACTION' . 
1.1600 1.1800  30 100.0000 5920 . 0.1581 0.1914 . 300 0.0000 6220 . 'X-RAY DIFFRACTION' . 
1.1800 1.2100  30 100.0000 5872 . 0.1454 0.1675 . 331 0.0000 6203 . 'X-RAY DIFFRACTION' . 
1.2100 1.2400  30 100.0000 5981 . 0.1407 0.1549 . 271 0.0000 6252 . 'X-RAY DIFFRACTION' . 
1.2400 1.2700  30 100.0000 5946 . 0.1361 0.1528 . 290 0.0000 6236 . 'X-RAY DIFFRACTION' . 
1.2700 1.3000  30 100.0000 5926 . 0.1295 0.1475 . 297 0.0000 6223 . 'X-RAY DIFFRACTION' . 
1.3000 1.3400  30 100.0000 5906 . 0.1275 0.1451 . 326 0.0000 6232 . 'X-RAY DIFFRACTION' . 
1.3400 1.3800  30 100.0000 5948 . 0.1282 0.1479 . 314 0.0000 6262 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 99.0000  5896 . 0.1253 0.1551 . 283 0.0000 6179 . 'X-RAY DIFFRACTION' . 
1.4300 1.4900  30 100.0000 5946 . 0.1213 0.1261 . 292 0.0000 6238 . 'X-RAY DIFFRACTION' . 
1.4900 1.5600  30 100.0000 5917 . 0.1150 0.1231 . 313 0.0000 6230 . 'X-RAY DIFFRACTION' . 
1.5600 1.6400  30 100.0000 5989 . 0.1164 0.1365 . 306 0.0000 6295 . 'X-RAY DIFFRACTION' . 
1.6400 1.7400  30 100.0000 5982 . 0.1256 0.1424 . 258 0.0000 6240 . 'X-RAY DIFFRACTION' . 
1.7400 1.8800  30 100.0000 5942 . 0.1287 0.1327 . 336 0.0000 6278 . 'X-RAY DIFFRACTION' . 
1.8800 2.0700  30 99.0000  5956 . 0.1341 0.1421 . 294 0.0000 6250 . 'X-RAY DIFFRACTION' . 
2.0700 2.3700  30 100.0000 5967 . 0.1343 0.1366 . 325 0.0000 6292 . 'X-RAY DIFFRACTION' . 
2.3700 2.9800  30 100.0000 6007 . 0.1454 0.1569 . 317 0.0000 6324 . 'X-RAY DIFFRACTION' . 
2.9800 28.0500 30 99.0000  6138 . 0.1484 0.1780 . 295 0.0000 6433 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCP 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000338' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCP 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_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 7HCP A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCP 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 7HCP SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCP MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCP SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCP 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 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N 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                   7HCP 
_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_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OH 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    TYR 
_pdbx_validate_symm_contact.auth_seq_id_1     42 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD1 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     67 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_654 
_pdbx_validate_symm_contact.dist              2.14 
# 
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 ? ? 56.27 -133.58 
2 1 HIS B 86 ? ? 57.60 -127.76 
# 
_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 505 ? 6.08 . 
2 1 O ? A HOH 506 ? 6.11 . 
3 1 O ? A HOH 507 ? 7.47 . 
4 1 O ? B HOH 401 ? 6.31 . 
# 
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 
A1A5Y N2   N N N 1   
A1A5Y C3   C N N 2   
A1A5Y C6   C Y N 3   
A1A5Y C9   C N R 4   
A1A5Y C12  C N N 5   
A1A5Y C14  C N N 6   
A1A5Y C17  C N N 7   
A1A5Y C19  C Y N 8   
A1A5Y C1   C N N 9   
A1A5Y C10  C N N 10  
A1A5Y C11  C N N 11  
A1A5Y C13  C N N 12  
A1A5Y C15  C N N 13  
A1A5Y C16  C N N 14  
A1A5Y C18  C Y N 15  
A1A5Y C2   C N N 16  
A1A5Y C20  C Y N 17  
A1A5Y C4   C Y N 18  
A1A5Y C5   C Y N 19  
A1A5Y C7   C N N 20  
A1A5Y C8   C N N 21  
A1A5Y F1   F N N 22  
A1A5Y N1   N N N 23  
A1A5Y O1   O N N 24  
A1A5Y O2   O N N 25  
A1A5Y O3   O N N 26  
A1A5Y O4   O N N 27  
A1A5Y H22  H N N 28  
A1A5Y H5   H N N 29  
A1A5Y H4   H N N 30  
A1A5Y H1   H N N 31  
A1A5Y H12  H N N 32  
A1A5Y H11  H N N 33  
A1A5Y H13  H N N 34  
A1A5Y H14  H N N 35  
A1A5Y H20  H N N 36  
A1A5Y H19  H N N 37  
A1A5Y H21  H N N 38  
A1A5Y H9   H N N 39  
A1A5Y H10  H N N 40  
A1A5Y H15  H N N 41  
A1A5Y H16  H N N 42  
A1A5Y H17  H N N 43  
A1A5Y H18  H N N 44  
A1A5Y H3   H N N 45  
A1A5Y H2   H N N 46  
A1A5Y H6   H N N 47  
A1A5Y H8   H N N 48  
A1A5Y H7   H N N 49  
A1A5Y H23  H N N 50  
ALA   N    N N N 51  
ALA   CA   C N S 52  
ALA   C    C N N 53  
ALA   O    O N N 54  
ALA   CB   C N N 55  
ALA   OXT  O N N 56  
ALA   H    H N N 57  
ALA   H2   H N N 58  
ALA   HA   H N N 59  
ALA   HB1  H N N 60  
ALA   HB2  H N N 61  
ALA   HB3  H N N 62  
ALA   HXT  H N N 63  
ARG   N    N N N 64  
ARG   CA   C N S 65  
ARG   C    C N N 66  
ARG   O    O N N 67  
ARG   CB   C N N 68  
ARG   CG   C N N 69  
ARG   CD   C N N 70  
ARG   NE   N N N 71  
ARG   CZ   C N N 72  
ARG   NH1  N N N 73  
ARG   NH2  N N N 74  
ARG   OXT  O N N 75  
ARG   H    H N N 76  
ARG   H2   H N N 77  
ARG   HA   H N N 78  
ARG   HB2  H N N 79  
ARG   HB3  H N N 80  
ARG   HG2  H N N 81  
ARG   HG3  H N N 82  
ARG   HD2  H N N 83  
ARG   HD3  H N N 84  
ARG   HE   H N N 85  
ARG   HH11 H N N 86  
ARG   HH12 H N N 87  
ARG   HH21 H N N 88  
ARG   HH22 H N N 89  
ARG   HXT  H N N 90  
ASN   N    N N N 91  
ASN   CA   C N S 92  
ASN   C    C N N 93  
ASN   O    O N N 94  
ASN   CB   C N N 95  
ASN   CG   C N N 96  
ASN   OD1  O N N 97  
ASN   ND2  N N N 98  
ASN   OXT  O N N 99  
ASN   H    H N N 100 
ASN   H2   H N N 101 
ASN   HA   H N N 102 
ASN   HB2  H N N 103 
ASN   HB3  H N N 104 
ASN   HD21 H N N 105 
ASN   HD22 H N N 106 
ASN   HXT  H N N 107 
ASP   N    N N N 108 
ASP   CA   C N S 109 
ASP   C    C N N 110 
ASP   O    O N N 111 
ASP   CB   C N N 112 
ASP   CG   C N N 113 
ASP   OD1  O N N 114 
ASP   OD2  O N N 115 
ASP   OXT  O N N 116 
ASP   H    H N N 117 
ASP   H2   H N N 118 
ASP   HA   H N N 119 
ASP   HB2  H N N 120 
ASP   HB3  H N N 121 
ASP   HD2  H N N 122 
ASP   HXT  H N N 123 
CYS   N    N N N 124 
CYS   CA   C N R 125 
CYS   C    C N N 126 
CYS   O    O N N 127 
CYS   CB   C N N 128 
CYS   SG   S N N 129 
CYS   OXT  O N N 130 
CYS   H    H N N 131 
CYS   H2   H N N 132 
CYS   HA   H N N 133 
CYS   HB2  H N N 134 
CYS   HB3  H N N 135 
CYS   HG   H N N 136 
CYS   HXT  H N N 137 
GLN   N    N N N 138 
GLN   CA   C N S 139 
GLN   C    C N N 140 
GLN   O    O N N 141 
GLN   CB   C N N 142 
GLN   CG   C N N 143 
GLN   CD   C N N 144 
GLN   OE1  O N N 145 
GLN   NE2  N N N 146 
GLN   OXT  O N N 147 
GLN   H    H N N 148 
GLN   H2   H N N 149 
GLN   HA   H N N 150 
GLN   HB2  H N N 151 
GLN   HB3  H N N 152 
GLN   HG2  H N N 153 
GLN   HG3  H N N 154 
GLN   HE21 H N N 155 
GLN   HE22 H N N 156 
GLN   HXT  H N N 157 
GLU   N    N N N 158 
GLU   CA   C N S 159 
GLU   C    C N N 160 
GLU   O    O N N 161 
GLU   CB   C N N 162 
GLU   CG   C N N 163 
GLU   CD   C N N 164 
GLU   OE1  O N N 165 
GLU   OE2  O N N 166 
GLU   OXT  O N N 167 
GLU   H    H N N 168 
GLU   H2   H N N 169 
GLU   HA   H N N 170 
GLU   HB2  H N N 171 
GLU   HB3  H N N 172 
GLU   HG2  H N N 173 
GLU   HG3  H N N 174 
GLU   HE2  H N N 175 
GLU   HXT  H N N 176 
GLY   N    N N N 177 
GLY   CA   C N N 178 
GLY   C    C N N 179 
GLY   O    O N N 180 
GLY   OXT  O N N 181 
GLY   H    H N N 182 
GLY   H2   H N N 183 
GLY   HA2  H N N 184 
GLY   HA3  H N N 185 
GLY   HXT  H N N 186 
HIS   N    N N N 187 
HIS   CA   C N S 188 
HIS   C    C N N 189 
HIS   O    O N N 190 
HIS   CB   C N N 191 
HIS   CG   C Y N 192 
HIS   ND1  N Y N 193 
HIS   CD2  C Y N 194 
HIS   CE1  C Y N 195 
HIS   NE2  N Y N 196 
HIS   OXT  O N N 197 
HIS   H    H N N 198 
HIS   H2   H N N 199 
HIS   HA   H N N 200 
HIS   HB2  H N N 201 
HIS   HB3  H N N 202 
HIS   HD1  H N N 203 
HIS   HD2  H N N 204 
HIS   HE1  H N N 205 
HIS   HE2  H N N 206 
HIS   HXT  H N N 207 
HOH   O    O N N 208 
HOH   H1   H N N 209 
HOH   H2   H N N 210 
ILE   N    N N N 211 
ILE   CA   C N S 212 
ILE   C    C N N 213 
ILE   O    O N N 214 
ILE   CB   C N S 215 
ILE   CG1  C N N 216 
ILE   CG2  C N N 217 
ILE   CD1  C N N 218 
ILE   OXT  O N N 219 
ILE   H    H N N 220 
ILE   H2   H N N 221 
ILE   HA   H N N 222 
ILE   HB   H N N 223 
ILE   HG12 H N N 224 
ILE   HG13 H N N 225 
ILE   HG21 H N N 226 
ILE   HG22 H N N 227 
ILE   HG23 H N N 228 
ILE   HD11 H N N 229 
ILE   HD12 H N N 230 
ILE   HD13 H N N 231 
ILE   HXT  H N N 232 
LEU   N    N N N 233 
LEU   CA   C N S 234 
LEU   C    C N N 235 
LEU   O    O N N 236 
LEU   CB   C N N 237 
LEU   CG   C N N 238 
LEU   CD1  C N N 239 
LEU   CD2  C N N 240 
LEU   OXT  O N N 241 
LEU   H    H N N 242 
LEU   H2   H N N 243 
LEU   HA   H N N 244 
LEU   HB2  H N N 245 
LEU   HB3  H N N 246 
LEU   HG   H N N 247 
LEU   HD11 H N N 248 
LEU   HD12 H N N 249 
LEU   HD13 H N N 250 
LEU   HD21 H N N 251 
LEU   HD22 H N N 252 
LEU   HD23 H N N 253 
LEU   HXT  H N N 254 
LYS   N    N N N 255 
LYS   CA   C N S 256 
LYS   C    C N N 257 
LYS   O    O N N 258 
LYS   CB   C N N 259 
LYS   CG   C N N 260 
LYS   CD   C N N 261 
LYS   CE   C N N 262 
LYS   NZ   N N N 263 
LYS   OXT  O N N 264 
LYS   H    H N N 265 
LYS   H2   H N N 266 
LYS   HA   H N N 267 
LYS   HB2  H N N 268 
LYS   HB3  H N N 269 
LYS   HG2  H N N 270 
LYS   HG3  H N N 271 
LYS   HD2  H N N 272 
LYS   HD3  H N N 273 
LYS   HE2  H N N 274 
LYS   HE3  H N N 275 
LYS   HZ1  H N N 276 
LYS   HZ2  H N N 277 
LYS   HZ3  H N N 278 
LYS   HXT  H N N 279 
MET   N    N N N 280 
MET   CA   C N S 281 
MET   C    C N N 282 
MET   O    O N N 283 
MET   CB   C N N 284 
MET   CG   C N N 285 
MET   SD   S N N 286 
MET   CE   C N N 287 
MET   OXT  O N N 288 
MET   H    H N N 289 
MET   H2   H N N 290 
MET   HA   H N N 291 
MET   HB2  H N N 292 
MET   HB3  H N N 293 
MET   HG2  H N N 294 
MET   HG3  H N N 295 
MET   HE1  H N N 296 
MET   HE2  H N N 297 
MET   HE3  H N N 298 
MET   HXT  H N N 299 
PHE   N    N N N 300 
PHE   CA   C N S 301 
PHE   C    C N N 302 
PHE   O    O N N 303 
PHE   CB   C N N 304 
PHE   CG   C Y N 305 
PHE   CD1  C Y N 306 
PHE   CD2  C Y N 307 
PHE   CE1  C Y N 308 
PHE   CE2  C Y N 309 
PHE   CZ   C Y N 310 
PHE   OXT  O N N 311 
PHE   H    H N N 312 
PHE   H2   H N N 313 
PHE   HA   H N N 314 
PHE   HB2  H N N 315 
PHE   HB3  H N N 316 
PHE   HD1  H N N 317 
PHE   HD2  H N N 318 
PHE   HE1  H N N 319 
PHE   HE2  H N N 320 
PHE   HZ   H N N 321 
PHE   HXT  H N N 322 
PRO   N    N N N 323 
PRO   CA   C N S 324 
PRO   C    C N N 325 
PRO   O    O N N 326 
PRO   CB   C N N 327 
PRO   CG   C N N 328 
PRO   CD   C N N 329 
PRO   OXT  O N N 330 
PRO   H    H N N 331 
PRO   HA   H N N 332 
PRO   HB2  H N N 333 
PRO   HB3  H N N 334 
PRO   HG2  H N N 335 
PRO   HG3  H N N 336 
PRO   HD2  H N N 337 
PRO   HD3  H N N 338 
PRO   HXT  H N N 339 
SER   N    N N N 340 
SER   CA   C N S 341 
SER   C    C N N 342 
SER   O    O N N 343 
SER   CB   C N N 344 
SER   OG   O N N 345 
SER   OXT  O N N 346 
SER   H    H N N 347 
SER   H2   H N N 348 
SER   HA   H N N 349 
SER   HB2  H N N 350 
SER   HB3  H N N 351 
SER   HG   H N N 352 
SER   HXT  H N N 353 
THR   N    N N N 354 
THR   CA   C N S 355 
THR   C    C N N 356 
THR   O    O N N 357 
THR   CB   C N R 358 
THR   OG1  O N N 359 
THR   CG2  C N N 360 
THR   OXT  O N N 361 
THR   H    H N N 362 
THR   H2   H N N 363 
THR   HA   H N N 364 
THR   HB   H N N 365 
THR   HG1  H N N 366 
THR   HG21 H N N 367 
THR   HG22 H N N 368 
THR   HG23 H N N 369 
THR   HXT  H N N 370 
TYR   N    N N N 371 
TYR   CA   C N S 372 
TYR   C    C N N 373 
TYR   O    O N N 374 
TYR   CB   C N N 375 
TYR   CG   C Y N 376 
TYR   CD1  C Y N 377 
TYR   CD2  C Y N 378 
TYR   CE1  C Y N 379 
TYR   CE2  C Y N 380 
TYR   CZ   C Y N 381 
TYR   OH   O N N 382 
TYR   OXT  O N N 383 
TYR   H    H N N 384 
TYR   H2   H N N 385 
TYR   HA   H N N 386 
TYR   HB2  H N N 387 
TYR   HB3  H N N 388 
TYR   HD1  H N N 389 
TYR   HD2  H N N 390 
TYR   HE1  H N N 391 
TYR   HE2  H N N 392 
TYR   HH   H N N 393 
TYR   HXT  H N N 394 
VAL   N    N N N 395 
VAL   CA   C N S 396 
VAL   C    C N N 397 
VAL   O    O N N 398 
VAL   CB   C N N 399 
VAL   CG1  C N N 400 
VAL   CG2  C N N 401 
VAL   OXT  O N N 402 
VAL   H    H N N 403 
VAL   H2   H N N 404 
VAL   HA   H N N 405 
VAL   HB   H N N 406 
VAL   HG11 H N N 407 
VAL   HG12 H N N 408 
VAL   HG13 H N N 409 
VAL   HG21 H N N 410 
VAL   HG22 H N N 411 
VAL   HG23 H N N 412 
VAL   HXT  H N N 413 
# 
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 
A1A5Y C16 C17  sing N N 1   
A1A5Y C16 C15  sing N N 2   
A1A5Y C17 C13  sing N N 3   
A1A5Y C12 C13  sing N N 4   
A1A5Y C12 C11  sing N N 5   
A1A5Y O2  C7   doub N N 6   
A1A5Y C13 N1   sing N N 7   
A1A5Y C13 C14  sing N N 8   
A1A5Y C11 C9   sing N N 9   
A1A5Y C15 C14  sing N N 10  
A1A5Y F1  C18  sing N N 11  
A1A5Y C7  N1   sing N N 12  
A1A5Y C7  C6   sing N N 13  
A1A5Y N1  C8   sing N N 14  
A1A5Y C9  C8   sing N N 15  
A1A5Y C9  C10  sing N N 16  
A1A5Y C18 C6   doub Y N 17  
A1A5Y C18 C19  sing Y N 18  
A1A5Y C6  C5   sing Y N 19  
A1A5Y O3  C10  doub N N 20  
A1A5Y C10 O4   sing N N 21  
A1A5Y C19 C20  doub Y N 22  
A1A5Y C5  C4   doub Y N 23  
A1A5Y C20 C4   sing Y N 24  
A1A5Y C20 N2   sing N N 25  
A1A5Y C4  C3   sing N N 26  
A1A5Y N2  C1   sing N N 27  
A1A5Y C3  C2   sing N N 28  
A1A5Y C1  C2   sing N N 29  
A1A5Y C1  O1   doub N N 30  
A1A5Y N2  H22  sing N N 31  
A1A5Y C3  H5   sing N N 32  
A1A5Y C3  H4   sing N N 33  
A1A5Y C9  H1   sing N N 34  
A1A5Y C12 H12  sing N N 35  
A1A5Y C12 H11  sing N N 36  
A1A5Y C14 H13  sing N N 37  
A1A5Y C14 H14  sing N N 38  
A1A5Y C17 H20  sing N N 39  
A1A5Y C17 H19  sing N N 40  
A1A5Y C19 H21  sing N N 41  
A1A5Y C11 H9   sing N N 42  
A1A5Y C11 H10  sing N N 43  
A1A5Y C15 H15  sing N N 44  
A1A5Y C15 H16  sing N N 45  
A1A5Y C16 H17  sing N N 46  
A1A5Y C16 H18  sing N N 47  
A1A5Y C2  H3   sing N N 48  
A1A5Y C2  H2   sing N N 49  
A1A5Y C5  H6   sing N N 50  
A1A5Y C8  H8   sing N N 51  
A1A5Y C8  H7   sing N N 52  
A1A5Y O4  H23  sing N N 53  
ALA   N   CA   sing N N 54  
ALA   N   H    sing N N 55  
ALA   N   H2   sing N N 56  
ALA   CA  C    sing N N 57  
ALA   CA  CB   sing N N 58  
ALA   CA  HA   sing N N 59  
ALA   C   O    doub N N 60  
ALA   C   OXT  sing N N 61  
ALA   CB  HB1  sing N N 62  
ALA   CB  HB2  sing N N 63  
ALA   CB  HB3  sing N N 64  
ALA   OXT HXT  sing N N 65  
ARG   N   CA   sing N N 66  
ARG   N   H    sing N N 67  
ARG   N   H2   sing N N 68  
ARG   CA  C    sing N N 69  
ARG   CA  CB   sing N N 70  
ARG   CA  HA   sing N N 71  
ARG   C   O    doub N N 72  
ARG   C   OXT  sing N N 73  
ARG   CB  CG   sing N N 74  
ARG   CB  HB2  sing N N 75  
ARG   CB  HB3  sing N N 76  
ARG   CG  CD   sing N N 77  
ARG   CG  HG2  sing N N 78  
ARG   CG  HG3  sing N N 79  
ARG   CD  NE   sing N N 80  
ARG   CD  HD2  sing N N 81  
ARG   CD  HD3  sing N N 82  
ARG   NE  CZ   sing N N 83  
ARG   NE  HE   sing N N 84  
ARG   CZ  NH1  sing N N 85  
ARG   CZ  NH2  doub N N 86  
ARG   NH1 HH11 sing N N 87  
ARG   NH1 HH12 sing N N 88  
ARG   NH2 HH21 sing N N 89  
ARG   NH2 HH22 sing N N 90  
ARG   OXT HXT  sing N N 91  
ASN   N   CA   sing N N 92  
ASN   N   H    sing N N 93  
ASN   N   H2   sing N N 94  
ASN   CA  C    sing N N 95  
ASN   CA  CB   sing N N 96  
ASN   CA  HA   sing N N 97  
ASN   C   O    doub N N 98  
ASN   C   OXT  sing N N 99  
ASN   CB  CG   sing N N 100 
ASN   CB  HB2  sing N N 101 
ASN   CB  HB3  sing N N 102 
ASN   CG  OD1  doub N N 103 
ASN   CG  ND2  sing N N 104 
ASN   ND2 HD21 sing N N 105 
ASN   ND2 HD22 sing N N 106 
ASN   OXT HXT  sing N N 107 
ASP   N   CA   sing N N 108 
ASP   N   H    sing N N 109 
ASP   N   H2   sing N N 110 
ASP   CA  C    sing N N 111 
ASP   CA  CB   sing N N 112 
ASP   CA  HA   sing N N 113 
ASP   C   O    doub N N 114 
ASP   C   OXT  sing N N 115 
ASP   CB  CG   sing N N 116 
ASP   CB  HB2  sing N N 117 
ASP   CB  HB3  sing N N 118 
ASP   CG  OD1  doub N N 119 
ASP   CG  OD2  sing N N 120 
ASP   OD2 HD2  sing N N 121 
ASP   OXT HXT  sing N N 122 
CYS   N   CA   sing N N 123 
CYS   N   H    sing N N 124 
CYS   N   H2   sing N N 125 
CYS   CA  C    sing N N 126 
CYS   CA  CB   sing N N 127 
CYS   CA  HA   sing N N 128 
CYS   C   O    doub N N 129 
CYS   C   OXT  sing N N 130 
CYS   CB  SG   sing N N 131 
CYS   CB  HB2  sing N N 132 
CYS   CB  HB3  sing N N 133 
CYS   SG  HG   sing N N 134 
CYS   OXT HXT  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TYR   N   CA   sing N N 359 
TYR   N   H    sing N N 360 
TYR   N   H2   sing N N 361 
TYR   CA  C    sing N N 362 
TYR   CA  CB   sing N N 363 
TYR   CA  HA   sing N N 364 
TYR   C   O    doub N N 365 
TYR   C   OXT  sing N N 366 
TYR   CB  CG   sing N N 367 
TYR   CB  HB2  sing N N 368 
TYR   CB  HB3  sing N N 369 
TYR   CG  CD1  doub Y N 370 
TYR   CG  CD2  sing Y N 371 
TYR   CD1 CE1  sing Y N 372 
TYR   CD1 HD1  sing N N 373 
TYR   CD2 CE2  doub Y N 374 
TYR   CD2 HD2  sing N N 375 
TYR   CE1 CZ   doub Y N 376 
TYR   CE1 HE1  sing N N 377 
TYR   CE2 CZ   sing Y N 378 
TYR   CE2 HE2  sing N N 379 
TYR   CZ  OH   sing N N 380 
TYR   OH  HH   sing N N 381 
TYR   OXT HXT  sing N N 382 
VAL   N   CA   sing N N 383 
VAL   N   H    sing N N 384 
VAL   N   H2   sing N N 385 
VAL   CA  C    sing N N 386 
VAL   CA  CB   sing N N 387 
VAL   CA  HA   sing N N 388 
VAL   C   O    doub N N 389 
VAL   C   OXT  sing N N 390 
VAL   CB  CG1  sing N N 391 
VAL   CB  CG2  sing N N 392 
VAL   CB  HB   sing N N 393 
VAL   CG1 HG11 sing N N 394 
VAL   CG1 HG12 sing N N 395 
VAL   CG1 HG13 sing N N 396 
VAL   CG2 HG21 sing N N 397 
VAL   CG2 HG22 sing N N 398 
VAL   CG2 HG23 sing N N 399 
VAL   OXT HXT  sing N N 400 
# 
_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                    7HCP 
_atom_sites.fract_transf_matrix[1][1]   0.011276 
_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]   0.011276 
_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]   0.025254 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.713 -16.283 22.307  0.86 56.81 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.666 -16.273 22.342  0.14 55.41 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.740 -15.210 22.475  0.86 56.38 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.714 -15.184 22.522  0.14 55.15 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.388 -13.860 22.191  0.86 54.71 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.377 -13.848 22.212  0.14 54.04 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.497 -13.586 22.651  0.86 55.15 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.484 -13.572 22.675  0.14 54.46 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.103 -15.247 23.879  0.86 57.19 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.116 -15.192 23.941  0.14 55.68 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.081 -14.128 24.033  0.86 57.46 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.098 -14.071 24.096  0.14 55.87 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.456 -16.602 24.131  0.86 57.43 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.482 -16.540 24.243  0.14 55.85 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.028 -15.331 21.832  0.86 67.66 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.983 -15.298 21.898  0.14 66.18 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.794 -15.117 24.547  0.86 68.64 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.826 -15.044 24.585  0.14 66.83 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.570 -14.278 24.844  0.86 68.97 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.617 -14.196 24.929  0.14 67.05 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.546 -13.279 24.091  0.86 68.97 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.562 -13.219 24.108  0.14 67.05 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.489 -14.133 23.265  0.86 68.97 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.479 -14.102 23.350  0.14 67.05 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.000 -16.580 24.987  0.86 68.92 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.042 -16.495 25.106  0.14 67.02 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.820 -16.784 23.422  0.86 68.92 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.833 -16.745 23.551  0.14 67.02 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.145 -17.285 24.140  0.86 68.92 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.174 -17.219 24.259  0.14 67.02 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.693 -13.023 21.423  1.00 52.23 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.154 -11.680 21.095  1.00 47.57 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.016 -10.692 21.337  1.00 43.61 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.890 -11.077 21.668  1.00 43.35 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.706 -11.600 19.664  1.00 46.69 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.696 -12.025 18.620  1.00 45.75 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.539 -11.608 18.653  1.00 45.42 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.133 -12.856 17.679  1.00 45.39 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.933 -13.220 21.069  0.86 62.69 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.937 -13.224 21.062  0.14 62.69 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.879 -11.449 21.691  1.00 57.09 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.965 -10.683 19.477  1.00 56.04 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.477 -12.183 19.590  1.00 56.04 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.600 -13.126 17.060  1.00 54.48 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.950 -13.126 17.689  1.00 54.48 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.314 -9.405  21.165  1.00 39.52 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.407 -8.333  21.555  1.00 35.53 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.499 -7.860  20.423  1.00 30.01 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.809 -6.849  20.584  1.00 30.22 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.193 -7.152  22.134  1.00 36.99 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.110 -6.632  21.189  1.00 37.72 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.047 -9.128  20.813  1.00 47.44 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.835 -8.662  22.263  1.00 42.65 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.571 -6.451  22.389  1.00 44.40 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.685 -7.452  22.916  1.00 44.40 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.531 -5.983  21.524  1.00 45.27 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.511 -8.539  19.275  0.86 26.18 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.448 -8.580  19.309  0.14 27.97 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.624 -8.169  18.177  0.86 22.77 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.508 -8.244  18.252  0.14 25.86 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.187 -8.535  18.532  0.86 23.14 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.098 -8.667  18.648  0.14 24.97 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.909 -9.664  18.945  0.86 24.11 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.902 -9.641  19.380  0.14 25.24 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.041 -8.884  16.892  0.86 20.56 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 15.915 -8.934  16.953  0.14 24.66 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.298 -8.333  16.265  0.86 18.77 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.270 -8.522  16.451  0.14 23.54 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.276 -7.133  15.573  0.86 18.03 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.428 -7.363  15.710  0.14 23.06 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.493 -9.026  16.356  0.86 19.11 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.385 -9.293  16.725  0.14 23.08 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.429 -6.628  14.994  0.86 18.16 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.677 -6.984  15.251  0.14 22.77 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.646 -8.531  15.777  0.86 19.08 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.634 -8.920  16.269  0.14 22.77 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.616 -7.332  15.095  0.86 18.62 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.781 -7.764  15.531  0.14 22.67 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.016 -9.214  19.113  0.86 31.42 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 16.942 -9.263  19.144  0.14 33.58 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.672 -7.215  18.033  0.86 27.34 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.513 -7.286  18.111  0.14 31.04 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.196 -9.823  17.095  0.86 24.68 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 15.933 -9.890  17.103  0.14 29.60 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.324 -8.805  16.246  0.86 24.68 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.263 -8.730  16.271  0.14 29.60 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.479 -6.658  15.504  0.86 21.65 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.688 -6.834  15.519  0.14 27.68 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.521 -9.834  16.815  0.86 22.95 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.290 -10.072 17.221  0.14 27.70 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.405 -5.817  14.532  0.86 21.80 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.773 -6.204  14.753  0.14 27.33 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.445 -9.000  15.847  0.86 22.90 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.376 -9.449  16.460  0.14 27.34 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.390 -6.991  14.706  0.86 22.35 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.621 -7.511  15.223  0.14 27.21 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.269 -7.583  18.361  0.86 22.50 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.108 -7.917  18.162  0.14 23.78 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.900 -7.730  18.835  0.86 23.04 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.720 -8.186  18.513  0.14 22.58 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.904 -7.457  17.716  0.86 21.30 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.807 -7.732  17.382  0.14 21.16 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.122 -6.578  16.878  0.86 21.35 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.164 -6.870  16.574  0.14 21.17 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.635 -6.769  20.003  0.86 25.22 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.323 -7.506  19.830  0.14 22.74 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.292 -6.855  20.435  0.86 27.02 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.773 -8.442  20.741  0.14 22.95 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.423 -6.833  17.964  0.86 27.01 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.217 -7.253  17.625  0.14 28.55 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.761 -8.634  19.150  0.86 27.66 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.602 -9.137  18.626  0.14 27.10 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.219 -7.003  20.745  0.86 30.28 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.110 -7.105  20.228  0.14 27.29 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.820 -5.860  19.715  0.86 30.28 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 10.657 -6.826  19.649  0.14 27.29 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.160 -6.323  21.073  0.86 32.43 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.095 -8.809  20.407  0.14 27.54 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.801  -8.206  17.714  0.86 20.30 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.616  -8.326  17.340  0.14 19.84 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.719  -7.943  16.791  0.86 19.69 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.639  -7.989  16.321  0.14 18.68 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.906  -8.465  15.387  0.86 18.42 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.948  -8.547  14.951  0.14 17.58 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.156  -8.060  14.493  0.86 19.04 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.493  -7.990  13.947  0.14 17.45 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.664  -8.863  18.245  0.86 24.36 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.350  -8.926  17.897  0.14 23.81 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.909  -8.338  17.146  0.86 23.64 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.769  -8.322  16.592  0.14 22.42 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.582  -6.985  16.732  0.86 23.64 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.581  -7.026  16.242  0.14 22.42 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.875  -9.346  15.156  0.86 16.90 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.702  -9.641  14.882  0.14 16.54 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.115 -9.880  13.824  0.86 15.66 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.165 -10.198 13.620  0.14 15.56 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.233  -11.091 13.557  0.86 15.23 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.353  -11.432 13.247  0.14 14.90 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.935  -11.888 14.452  0.86 16.95 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.115  -12.303 14.090  0.14 14.79 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.586 -10.279 13.636  0.86 15.54 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.645 -10.571 13.712  0.14 15.20 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.501 -9.088  13.470  0.86 15.53 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.581 -9.391  13.581  0.14 14.91 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.816 -8.289  14.553  0.86 15.94 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.981 -8.670  14.696  0.14 14.84 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.020 -8.750  12.229  0.86 15.14 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.061 -8.997  12.340  0.14 14.91 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.626 -7.184  14.413  0.86 16.28 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.831 -7.584  14.577  0.14 14.98 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.835 -7.644  12.076  0.86 15.66 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.912 -7.918  12.213  0.14 15.08 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.128 -6.864  13.170  0.86 16.63 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.297 -7.217  13.335  0.14 15.31 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 14.924 -5.762  13.019  0.86 18.02 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 15.147 -6.142  13.213  0.14 15.69 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.411 -9.648  15.758  0.86 20.29 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 9.965  -10.086 15.570  0.14 19.85 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.902  -9.199  13.168  0.86 18.81 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 10.065 -9.542  12.919  0.14 18.68 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.879 -10.785 14.409  0.86 18.66 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.820 -11.003 14.563  0.14 18.25 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.653 -10.826 12.836  0.86 18.66 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.833 -11.183 12.990  0.14 18.25 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.461 -8.502  15.391  0.86 19.14 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.672 -8.920  15.539  0.14 17.82 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.816 -9.273  11.486  0.86 18.18 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 12.806 -9.469  11.580  0.14 17.90 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.824 -6.661  15.153  0.86 19.55 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 14.097 -7.116  15.336  0.14 17.98 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.184 -7.427  11.240  0.86 18.80 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.229 -7.668  11.375  0.14 18.10 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.034 -5.388  13.764  0.86 21.63 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.298 -5.811  13.970  0.14 18.84 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.824  -11.220 12.302  0.86 14.36 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.947  -11.507 11.980  0.14 14.35 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.222  -12.439 11.794  0.86 14.55 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.344  -12.718 11.438  0.14 13.82 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.345  -13.367 11.329  0.86 14.02 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.445  -13.680 11.016  0.14 13.58 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.303 -12.930 10.679  0.86 14.11 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.405 -13.284 10.347  0.14 13.45 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.301  -12.094 10.622  0.86 15.96 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.467  -12.384 10.229  0.14 13.60 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.601  -13.284 9.959   0.86 17.93 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 7.233  -13.496 9.190   0.14 13.17 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.523  -13.874 10.856  0.86 20.07 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 6.393  -14.638 9.750   0.14 13.24 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.036  -12.887 8.603   0.86 20.11 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 6.598  -12.923 7.935   0.14 13.50 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.887  -10.590 11.709  0.86 17.24 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 9.016  -10.869 11.411  0.14 17.23 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.697  -12.868 12.495  0.86 17.46 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.799  -13.147 12.116  0.14 16.59 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.606  -11.488 10.936  0.86 19.16 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.596  -12.115 10.560  0.14 16.33 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.828  -11.649 9.940   0.86 19.16 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.875  -11.639 9.762   0.14 16.33 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.259  -13.978 9.806   0.86 21.53 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 8.086  -13.867 8.919   0.14 15.82 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.138  -14.649 10.419  0.86 24.09 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 6.647  -15.460 9.302   0.14 15.90 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.922  -14.136 11.702  0.86 24.09 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 6.558  -14.715 10.702  0.14 15.90 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.837  -13.205 11.010  0.86 24.09 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 5.458  -14.446 9.588   0.14 15.90 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.600  -13.659 8.212   0.86 24.14 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.460  -13.642 7.299   0.14 16.21 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.400  -12.169 8.726   0.86 24.14 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 5.750  -12.517 8.168   0.14 16.21 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.766  -12.595 8.036   0.86 24.14 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 7.194  -12.257 7.558   0.14 16.21 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.237  -14.643 11.681  0.86 13.70 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.296  -14.944 11.402  0.14 13.65 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.238 -15.635 11.316  0.86 14.08 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.241 -15.992 11.036  0.14 14.02 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.874  -16.207 9.955   0.86 13.88 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.933  -16.467 9.621   0.14 14.04 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.792  -16.779 9.798   0.86 15.84 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.877  -17.058 9.375   0.14 14.47 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.277 -16.735 12.378  0.86 13.54 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.093 -17.158 12.006  0.14 14.39 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.276 -17.851 12.140  0.86 14.26 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.390 -17.809 12.419  0.14 14.92 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.404 -18.688 13.416  0.86 14.67 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.127 -19.080 13.207  0.14 15.45 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.357 -19.871 13.263  0.86 14.74 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.391 -19.587 13.867  0.14 15.79 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.744 -19.411 12.991  0.86 15.61 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.558 -19.498 12.957  0.14 16.01 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.569  -14.959 12.133  0.86 16.45 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.647  -15.222 11.897  0.14 16.39 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.103 -15.204 11.259  0.86 16.90 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.152 -15.653 11.073  0.14 16.83 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.497 -16.317 13.227  0.86 16.26 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 9.654  -16.838 12.807  0.14 17.27 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.395  -17.128 12.432  0.86 16.26 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.545  -17.839 11.582  0.14 17.27 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 10.956 -18.421 11.422  0.86 17.13 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.906 -18.033 11.630  0.14 17.92 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.140 -17.475 11.923  0.86 17.13 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 11.885 -17.199 12.985  0.14 17.92 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.736 -18.124 14.130  0.86 17.61 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 10.474 -18.895 13.901  0.14 18.55 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.529 -19.038 13.651  0.86 17.61 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.798 -19.765 12.608  0.14 18.55 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.364 -20.386 14.086  0.86 17.70 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.573 -19.026 14.632  0.14 18.96 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.068 -20.425 12.522  0.86 17.70 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.276 -20.514 14.141  0.14 18.96 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.267 -20.113 12.821  0.86 18.75 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.216 -20.023 13.247  0.14 19.23 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.751 -18.870 12.285  0.86 18.75 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.319 -19.754 12.139  0.14 19.23 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.065 -18.976 13.695  0.86 18.75 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.850 -18.658 12.921  0.14 19.23 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.761 -16.063 8.974   0.86 13.23 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.858 -16.235 8.692   0.14 13.92 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.500 -16.627 7.654   0.86 13.52 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.722 -16.781 7.347   0.14 13.94 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.078 -18.027 7.494   0.86 13.52 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.329 -18.177 7.252   0.14 14.13 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.446 -18.890 6.876   0.86 14.29 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.712 -19.091 6.696   0.14 14.34 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.069 -15.731 6.554   0.86 14.28 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.382 -15.846 6.332   0.14 14.00 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.401 -14.374 6.378   0.86 15.17 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.689 -14.493 6.162   0.14 14.16 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.136 -13.590 5.302   0.86 16.47 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.573 -13.534 5.386   0.14 14.18 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.937  -14.535 6.028   0.86 15.64 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 9.344  -14.669 5.474   0.14 14.23 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.521 -15.647 9.043   0.86 15.89 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.574 -15.773 8.817   0.14 16.71 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.540  -16.684 7.525   0.86 16.24 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.780  -16.847 7.128   0.14 16.74 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.005 -15.570 6.747   0.86 17.15 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 12.294 -15.677 6.615   0.14 16.81 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 10.991 -16.203 5.710   0.86 17.15 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.386 -16.285 5.466   0.14 16.81 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.465 -13.878 7.207   0.86 18.22 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.531 -14.111 7.039   0.14 17.00 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.714 -12.725 5.191   0.86 19.78 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 11.012 -12.889 4.928   0.14 17.03 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.064 -13.470 5.572   0.86 19.78 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 12.164 -13.077 6.005   0.14 17.03 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.103 -14.084 4.466   0.86 19.78 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 12.091 -14.039 4.740   0.14 17.03 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.586  -13.681 5.739   0.86 18.78 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.976  -13.796 5.271   0.14 17.09 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.854  -15.188 5.314   0.86 18.78 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 9.473  -15.173 4.655   0.14 17.09 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.458  -14.844 6.813   0.86 18.78 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.747  -15.151 6.067   0.14 17.09 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.286 -18.249 8.003   0.86 13.22 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.536 -18.345 7.785   0.14 14.24 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 12.970 -19.528 7.880   0.86 13.63 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 13.190 -19.642 7.894   0.14 14.21 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.759 -19.768 9.160   0.86 13.88 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.803 -19.738 9.286   0.14 14.56 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.683 -18.997 10.122  0.86 14.11 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.511 -18.933 10.175  0.14 14.72 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.935 -19.547 6.688   0.86 14.36 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 14.271 -19.813 6.819   0.14 14.10 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 14.996 -18.631 6.944   0.86 15.28 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 15.321 -18.863 7.042   0.14 13.92 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.247 -19.192 5.376   0.86 15.38 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.697 -19.613 5.431   0.14 14.17 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.741 -17.655 8.424   0.86 15.87 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 13.006 -17.702 8.097   0.14 17.09 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.317 -20.240 7.768   0.86 16.36 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.533 -20.349 7.791   0.14 17.06 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.308 -20.434 6.598   0.86 17.24 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.636 -20.712 6.871   0.14 16.93 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.537 -18.623 6.292   0.86 18.34 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.977 -19.239 7.410   0.14 16.71 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.868 -19.311 4.638   0.86 18.46 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 14.380 -19.792 4.765   0.14 17.02 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.483 -19.775 5.238   0.86 18.46 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.954 -20.218 5.291   0.14 17.02 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 12.947 -18.273 5.392   0.86 18.46 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 13.388 -18.701 5.330   0.14 17.02 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.554 -20.836 9.151   0.86 14.18 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.679 -20.727 9.467   0.14 14.89 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.406 -21.130 10.294  0.86 14.83 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.395 -20.858 10.730  0.14 15.37 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.251 -19.927 10.696  0.86 14.27 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.214 -19.614 11.045  0.14 14.66 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.495 -19.711 11.888  0.86 15.35 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.382 -19.265 12.220  0.14 14.69 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.321 -22.308 9.975   0.86 17.39 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.309 -22.080 10.684  0.14 16.58 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.226 -22.651 11.128  0.86 21.42 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.442 -21.992 11.681  0.14 17.69 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.708 -23.010 12.209  0.86 22.76 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 17.179 -22.108 12.896  0.14 18.27 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.452 -22.559 10.951  0.86 24.22 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.596 -21.799 11.245  0.14 18.07 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.624 -21.389 8.496   0.86 17.03 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.871 -21.322 8.882   0.14 17.88 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.850 -21.376 11.049  0.86 17.80 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.758 -20.998 11.442  0.14 18.45 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.770 -23.092 9.773   0.86 20.88 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.792 -22.870 10.896  0.14 19.90 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.870 -22.093 9.208   0.86 20.88 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.691 -22.158 9.797   0.14 19.90 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.708 -19.128 9.721   0.86 13.63 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.717 -18.925 10.016  0.14 14.01 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.698 -18.095 9.999   0.86 14.13 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.700 -17.864 10.197  0.14 13.51 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.327 -16.694 9.536   0.86 14.77 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.376 -16.592 9.423   0.14 13.35 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 18.088 -15.763 9.814   0.86 15.80 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 18.259 -15.738 9.277   0.14 13.49 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 19.065 -18.478 9.402   0.86 13.90 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 19.084 -18.358 9.765   0.14 13.46 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 19.038 -18.567 7.890   0.86 14.31 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 19.182 -18.559 8.266   0.14 13.32 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.299 -19.374 7.317   0.86 15.35 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 18.587 -19.485 7.712   0.14 13.35 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.840 -17.737 7.233   0.86 14.47 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 19.930 -17.685 7.599   0.14 13.27 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.451 -19.170 8.903   0.86 16.37 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.498 -19.056 9.198   0.14 16.82 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.822 -18.051 10.958  0.86 16.96 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 17.748 -17.636 11.140  0.14 16.22 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.722 -17.802 9.654   0.86 16.68 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.749 -17.701 10.026  0.14 16.16 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.341 -19.342 9.751   0.86 16.68 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.266 -19.206 10.194  0.14 16.16 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.861 -17.751 6.373   0.86 17.37 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 20.016 -17.753 6.745   0.14 15.94 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.345 -17.185 7.663   0.86 17.37 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.332 -17.051 8.020   0.14 15.94 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.202 -16.506 8.851   0.86 14.57 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 16.160 -16.439 8.906   0.14 13.20 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.818 -15.214 8.299   0.86 14.32 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.756 -15.227 8.199   0.14 13.25 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.541 -14.732 8.976   0.86 13.90 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.517 -14.669 8.885   0.14 13.32 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.543 -15.463 9.055   0.86 13.78 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.463 -15.318 8.904   0.14 13.22 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.653 -15.260 6.771   0.86 14.96 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.510 -15.478 6.702   0.14 13.41 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.223 -13.890 6.240   0.86 15.56 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 15.095 -14.187 6.011   0.14 13.62 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 16.938 -15.718 6.102   0.86 16.14 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.760 -16.048 6.043   0.14 13.51 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.633 -17.129 8.703   0.86 17.49 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.541 -17.035 8.950   0.14 15.85 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.521 -14.572 8.499   0.86 17.19 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.458 -14.564 8.275   0.14 15.90 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 14.960 -15.901 6.554   0.86 17.96 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.793 -16.122 6.596   0.14 16.10 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.315 -13.889 5.276   0.86 18.68 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 15.099 -14.326 5.051   0.14 16.35 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.296 -13.735 6.483   0.86 18.68 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.206 -13.941 6.305   0.14 16.35 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.789 -13.209 6.630   0.86 18.68 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.727 -13.488 6.244   0.14 16.35 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 16.852 -15.606 5.143   0.86 19.38 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.596 -16.150 5.092   0.14 16.22 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.676 -15.181 6.432   0.86 19.38 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.500 -15.435 6.184   0.14 16.22 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 17.092 -16.651 6.316   0.86 19.38 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 16.963 -16.909 6.438   0.14 16.22 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.571 -13.471 9.400   0.86 13.54 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.648 -13.466 9.440   0.14 13.35 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.496 -12.794 10.104  0.86 13.53 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.585 -12.784 10.162  0.14 13.52 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.221 -11.476 9.396   0.86 13.89 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.330 -11.434 9.505   0.14 13.45 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.120 -10.919 8.765   0.86 13.99 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.239 -10.839 8.918   0.14 13.51 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.923 -12.529 11.550  0.86 14.42 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 13.987 -12.566 11.626  0.14 14.09 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 14.113 -13.793 12.354  0.86 14.91 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 14.369 -13.831 12.365  0.14 14.72 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.287 -14.536 12.269  0.86 15.72 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 15.652 -14.355 12.267  0.14 15.10 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 13.109 -14.258 13.189  0.86 15.33 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 13.450 -14.495 13.168  0.14 15.11 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.452 -15.708 12.998  0.86 15.78 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 16.007 -15.509 12.942  0.14 15.51 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.265 -15.431 13.922  0.86 15.60 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 13.798 -15.647 13.850  0.14 15.41 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.440 -16.150 13.826  0.86 15.76 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 15.075 -16.150 13.730  0.14 15.70 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.596 -17.307 14.558  0.86 16.31 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 15.424 -17.297 14.405  0.14 16.18 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.251 -12.953 9.268   0.86 16.25 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.374 -13.005 9.403   0.14 16.02 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.693 -13.340 10.092  0.86 16.25 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.771 -13.307 10.131  0.14 16.23 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.767 -12.053 11.544  0.86 17.31 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 14.744 -11.962 11.658  0.14 16.91 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.243 -12.000 11.984  0.86 17.31 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 13.241 -12.177 12.094  0.14 16.91 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 15.974 -14.249 11.711  0.86 18.88 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 16.283 -13.926 11.737  0.14 18.13 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.314 -13.786 13.260  0.86 18.40 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 12.587 -14.160 13.249  0.14 18.14 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.250 -16.195 12.933  0.86 18.95 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 16.870 -15.852 12.866  0.14 18.62 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.583 -15.729 14.483  0.86 18.73 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 13.171 -16.088 14.381  0.14 18.50 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 13.859 -17.531 14.901  0.86 19.58 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 16.227 -17.495 14.246  0.14 19.43 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 11.992 -10.961 9.490   0.86 13.98 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 12.093 -10.944 9.603   0.14 13.39 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.613 -9.754  8.762   0.86 14.59 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.694 -9.723  8.908   0.14 13.37 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.654 -8.905  9.588   0.86 15.05 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.768 -8.895  9.791   0.14 13.60 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.816  -9.422  10.335  0.86 15.64 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 9.953  -9.440  10.543  0.14 13.56 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 11.030 -10.119 7.380   0.86 15.04 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 11.043 -10.043 7.545   0.14 13.02 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 10.986 -8.904  6.458   0.86 15.61 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 10.785 -8.759  6.753   0.14 12.89 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.669  -10.797 7.517   0.86 15.65 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.763  -10.849 7.732   0.14 13.09 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.763 -9.280  5.021   0.86 17.02 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.336 -9.006  5.331   0.14 12.82 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.360 -11.314 9.958   0.86 16.79 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.462 -11.308 10.065  0.14 16.07 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.422 -9.234  8.609   0.86 17.52 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.486 -9.194  8.736   0.14 16.05 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.631 -10.760 6.974   0.86 18.06 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.665 -10.584 7.039   0.14 15.64 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.264 -8.321  6.731   0.86 18.74 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 10.091 -8.248  7.195   0.14 15.48 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.834 -8.432  6.511   0.86 18.74 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.605 -8.241  6.718   0.14 15.48 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.410  -11.160 6.654   0.86 18.79 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.456  -11.158 6.864   0.14 15.71 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.736  -11.510 8.168   0.86 18.79 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.949  -11.609 8.304   0.14 15.71 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 9.014  -10.142 7.807   0.86 18.79 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 9.088  -10.285 8.140   0.14 15.71 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.802 -8.476  4.475   0.86 20.44 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.280 -8.158  4.866   0.14 15.39 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.451 -9.901  4.744   0.86 20.44 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 10.984 -9.582  4.892   0.14 15.39 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.888  -9.692  4.935   0.86 20.44 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.467  -9.436  5.344   0.14 15.39 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.771 -7.585  9.424   0.86 15.37 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 10.895 -7.570  9.687   0.14 14.26 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 9.960  -6.632  10.171  0.86 16.64 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 10.080 -6.633  10.449  0.14 15.32 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.755  -5.378  9.330   0.86 16.84 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.828  -5.396  9.598   0.14 15.59 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.643 -4.977  8.576   0.86 17.08 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.678 -4.994  8.799   0.14 15.61 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.674 -6.272  11.481  0.86 17.74 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.783 -6.223  11.748  0.14 16.10 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.940  -5.346  12.429  0.86 19.44 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 9.965  -5.323  12.659  0.14 16.99 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.842 -5.066  13.624  0.86 20.67 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 10.794 -4.846  13.838  0.14 17.70 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.212 -4.152  14.657  0.86 21.32 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 9.996  -3.922  14.741  0.14 18.08 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 11.124 -3.969  15.827  0.86 21.65 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 10.820 -3.403  15.865  0.14 18.23 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.337 -7.211  8.884   0.86 18.46 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.465 -7.183  9.170   0.14 17.12 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.102  -7.032  10.376  0.86 19.98 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.230  -7.042  10.669  0.14 18.39 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.847 -7.094  11.967  0.86 21.30 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 11.001 -7.023  12.248  0.14 19.32 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.517 -5.847  11.260  0.86 21.30 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.598 -5.746  11.524  0.14 19.32 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.739  -4.508  11.984  0.86 23.33 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 9.666  -4.544  12.165  0.14 20.39 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.125  -5.773  12.743  0.86 23.33 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 9.204  -5.818  13.002  0.14 20.39 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 11.052 -5.906  14.059  0.86 24.81 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 11.079 -5.612  14.361  0.14 21.25 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.655 -4.644  13.308  0.86 24.81 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.567 -4.359  13.510  0.14 21.25 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 10.046 -3.281  14.261  0.86 25.60 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 9.679  -3.166  14.222  0.14 21.71 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.383  -4.541  14.975  0.86 25.60 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 9.246  -4.410  15.114  0.14 21.71 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.733 -3.461  16.443  0.86 25.99 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.296 -3.032  16.481  0.14 21.88 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.321 -4.760  16.184  0.86 25.99 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 11.279 -4.069  16.238  0.14 21.88 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.878 -3.576  15.565  0.86 25.99 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 11.393 -2.791  15.566  0.14 21.88 ?  19  LYS   A HZ3  1 
ATOM   531  N N    A ASN   A 1 20  ? 8.573  -4.767  9.455   0.86 17.43 ?  20  ASN   A N    1 
ATOM   532  N N    B ASN   A 1 20  ? 8.652  -4.791  9.778   0.14 15.94 ?  20  ASN   A N    1 
ATOM   533  C CA   A ASN   A 1 20  ? 8.338  -3.439  8.902   0.86 18.85 ?  20  ASN   A CA   1 
ATOM   534  C CA   B ASN   A 1 20  ? 8.279  -3.574  9.055   0.14 16.40 ?  20  ASN   A CA   1 
ATOM   535  C C    A ASN   A 1 20  ? 8.960  -2.446  9.870   0.86 19.18 ?  20  ASN   A C    1 
ATOM   536  C C    B ASN   A 1 20  ? 8.721  -2.380  9.892   0.14 16.65 ?  20  ASN   A C    1 
ATOM   537  O O    A ASN   A 1 20  ? 8.448  -2.242  10.976  0.86 20.39 ?  20  ASN   A O    1 
ATOM   538  O O    B ASN   A 1 20  ? 7.963  -1.844  10.702  0.14 16.69 ?  20  ASN   A O    1 
ATOM   539  C CB   A ASN   A 1 20  ? 6.838  -3.202  8.731   0.86 19.64 ?  20  ASN   A CB   1 
ATOM   540  C CB   B ASN   A 1 20  ? 6.778  -3.552  8.784   0.14 16.58 ?  20  ASN   A CB   1 
ATOM   541  C CG   A ASN   A 1 20  ? 6.497  -1.769  8.336   0.86 21.19 ?  20  ASN   A CG   1 
ATOM   542  C CG   B ASN   A 1 20  ? 6.320  -2.279  8.087   0.14 16.79 ?  20  ASN   A CG   1 
ATOM   543  O OD1  A ASN   A 1 20  ? 5.507  -1.212  8.807   0.86 23.29 ?  20  ASN   A OD1  1 
ATOM   544  O OD1  B ASN   A 1 20  ? 5.225  -1.774  8.349   0.14 16.73 ?  20  ASN   A OD1  1 
ATOM   545  N ND2  A ASN   A 1 20  ? 7.306  -1.174  7.468   0.86 21.22 ?  20  ASN   A ND2  1 
ATOM   546  N ND2  B ASN   A 1 20  ? 7.156  -1.752  7.199   0.14 17.18 ?  20  ASN   A ND2  1 
ATOM   547  H H    A ASN   A 1 20  ? 7.895  -5.105  9.864   0.86 20.92 ?  20  ASN   A H    1 
ATOM   548  H H    B ASN   A 1 20  ? 8.045  -5.071  10.319  0.14 19.14 ?  20  ASN   A H    1 
ATOM   549  H HA   A ASN   A 1 20  ? 8.775  -3.360  8.043   0.86 22.63 ?  20  ASN   A HA   1 
ATOM   550  H HA   B ASN   A 1 20  ? 8.747  -3.550  8.207   0.14 19.69 ?  20  ASN   A HA   1 
ATOM   551  H HB2  A ASN   A 1 20  ? 6.510  -3.790  8.035   0.86 23.58 ?  20  ASN   A HB2  1 
ATOM   552  H HB2  B ASN   A 1 20  ? 6.541  -4.304  8.224   0.14 19.90 ?  20  ASN   A HB2  1 
ATOM   553  H HB3  A ASN   A 1 20  ? 6.395  -3.400  9.569   0.86 23.58 ?  20  ASN   A HB3  1 
ATOM   554  H HB3  B ASN   A 1 20  ? 6.306  -3.613  9.625   0.14 19.90 ?  20  ASN   A HB3  1 
ATOM   555  H HD21 A ASN   A 1 20  ? 7.148  -0.368  7.223   0.86 25.47 ?  20  ASN   A HD21 1 
ATOM   556  H HD21 B ASN   A 1 20  ? 6.939  -1.032  6.783   0.14 20.63 ?  20  ASN   A HD21 1 
ATOM   557  H HD22 A ASN   A 1 20  ? 7.992  -1.593  7.159   0.86 25.47 ?  20  ASN   A HD22 1 
ATOM   558  H HD22 B ASN   A 1 20  ? 7.913  -2.127  7.038   0.14 20.63 ?  20  ASN   A HD22 1 
ATOM   559  N N    A ALA   A 1 21  ? 10.091 -1.862  9.484   0.86 19.06 ?  21  ALA   A N    1 
ATOM   560  N N    B ALA   A 1 21  ? 9.965  -1.949  9.688   0.14 16.88 ?  21  ALA   A N    1 
ATOM   561  C CA   A ALA   A 1 21  ? 10.785 -0.965  10.392  0.86 18.88 ?  21  ALA   A CA   1 
ATOM   562  C CA   B ALA   A 1 21  ? 10.536 -0.895  10.516  0.14 17.09 ?  21  ALA   A CA   1 
ATOM   563  C C    A ALA   A 1 21  ? 11.749 -0.097  9.609   0.86 18.35 ?  21  ALA   A C    1 
ATOM   564  C C    B ALA   A 1 21  ? 11.724 -0.268  9.804   0.14 16.90 ?  21  ALA   A C    1 
ATOM   565  O O    A ALA   A 1 21  ? 12.187 -0.459  8.513   0.86 18.36 ?  21  ALA   A O    1 
ATOM   566  O O    B ALA   A 1 21  ? 12.290 -0.843  8.871   0.14 16.53 ?  21  ALA   A O    1 
ATOM   567  C CB   A ALA   A 1 21  ? 11.543 -1.738  11.474  0.86 19.74 ?  21  ALA   A CB   1 
ATOM   568  C CB   B ALA   A 1 21  ? 10.965 -1.437  11.883  0.14 17.24 ?  21  ALA   A CB   1 
ATOM   569  H H    A ALA   A 1 21  ? 10.466 -1.963  8.716   0.86 22.88 ?  21  ALA   A H    1 
ATOM   570  H H    B ALA   A 1 21  ? 10.491 -2.246  9.074   0.14 20.26 ?  21  ALA   A H    1 
ATOM   571  H HA   A ALA   A 1 21  ? 10.132 -0.385  10.827  0.86 22.67 ?  21  ALA   A HA   1 
ATOM   572  H HA   B ALA   A 1 21  ? 9.869  -0.207  10.657  0.14 20.51 ?  21  ALA   A HA   1 
ATOM   573  H HB1  A ALA   A 1 21  ? 11.950 -1.103  12.079  0.86 23.70 ?  21  ALA   A HB1  1 
ATOM   574  H HB1  B ALA   A 1 21  ? 11.377 -0.722  12.390  0.14 20.70 ?  21  ALA   A HB1  1 
ATOM   575  H HB2  A ALA   A 1 21  ? 10.912 -2.298  11.955  0.86 23.70 ?  21  ALA   A HB2  1 
ATOM   576  H HB2  B ALA   A 1 21  ? 10.183 -1.769  12.349  0.14 20.70 ?  21  ALA   A HB2  1 
ATOM   577  H HB3  A ALA   A 1 21  ? 12.218 -2.284  11.050  0.86 23.70 ?  21  ALA   A HB3  1 
ATOM   578  H HB3  B ALA   A 1 21  ? 11.602 -2.156  11.749  0.14 20.70 ?  21  ALA   A HB3  1 
ATOM   579  N N    A ASP   A 1 22  ? 12.041 1.064   10.189  0.86 18.21 ?  22  ASP   A N    1 
ATOM   580  N N    B ASP   A 1 22  ? 12.089 0.929   10.262  0.14 17.13 ?  22  ASP   A N    1 
ATOM   581  C CA   A ASP   A 1 22  ? 13.077 1.962   9.705   0.86 18.27 ?  22  ASP   A CA   1 
ATOM   582  C CA   B ASP   A 1 22  ? 13.260 1.625   9.747   0.14 17.39 ?  22  ASP   A CA   1 
ATOM   583  C C    A ASP   A 1 22  ? 14.408 1.457   10.249  0.86 16.80 ?  22  ASP   A C    1 
ATOM   584  C C    B ASP   A 1 22  ? 14.526 0.981   10.300  0.14 16.91 ?  22  ASP   A C    1 
ATOM   585  O O    A ASP   A 1 22  ? 14.609 1.425   11.468  0.86 17.24 ?  22  ASP   A O    1 
ATOM   586  O O    B ASP   A 1 22  ? 14.636 0.744   11.507  0.14 16.90 ?  22  ASP   A O    1 
ATOM   587  C CB   A ASP   A 1 22  ? 12.774 3.366   10.224  0.86 20.65 ?  22  ASP   A CB   1 
ATOM   588  C CB   B ASP   A 1 22  ? 13.210 3.095   10.162  0.14 17.90 ?  22  ASP   A CB   1 
ATOM   589  C CG   A ASP   A 1 22  ? 13.778 4.404   9.760   0.86 22.83 ?  22  ASP   A CG   1 
ATOM   590  C CG   B ASP   A 1 22  ? 14.493 3.835   9.837   0.14 18.55 ?  22  ASP   A CG   1 
ATOM   591  O OD1  A ASP   A 1 22  ? 14.855 4.047   9.250   0.86 23.06 ?  22  ASP   A OD1  1 
ATOM   592  O OD1  B ASP   A 1 22  ? 15.177 3.444   8.867   0.14 18.56 ?  22  ASP   A OD1  1 
ATOM   593  O OD2  A ASP   A 1 22  ? 13.481 5.604   9.916   0.86 24.98 -1 22  ASP   A OD2  1 
ATOM   594  O OD2  B ASP   A 1 22  ? 14.825 4.797   10.558  0.14 19.17 -1 22  ASP   A OD2  1 
ATOM   595  H H    A ASP   A 1 22  ? 11.625 1.367   10.887  0.86 21.86 ?  22  ASP   A H    1 
ATOM   596  H H    B ASP   A 1 22  ? 11.663 1.366   10.873  0.14 20.56 ?  22  ASP   A H    1 
ATOM   597  H HA   A ASP   A 1 22  ? 13.096 1.967   8.735   0.86 21.93 ?  22  ASP   A HA   1 
ATOM   598  H HA   B ASP   A 1 22  ? 13.276 1.573   8.779   0.14 20.88 ?  22  ASP   A HA   1 
ATOM   599  H HB2  A ASP   A 1 22  ? 11.887 3.631   9.923   0.86 24.78 ?  22  ASP   A HB2  1 
ATOM   600  H HB2  B ASP   A 1 22  ? 12.490 3.534   9.684   0.14 21.49 ?  22  ASP   A HB2  1 
ATOM   601  H HB3  A ASP   A 1 22  ? 12.800 3.356   11.194  0.86 24.78 ?  22  ASP   A HB3  1 
ATOM   602  H HB3  B ASP   A 1 22  ? 13.050 3.147   11.119  0.14 21.49 ?  22  ASP   A HB3  1 
ATOM   603  N N    A ILE   A 1 23  ? 15.302 1.028   9.353   0.86 16.55 ?  23  ILE   A N    1 
ATOM   604  N N    B ILE   A 1 23  ? 15.486 0.702   9.414   0.14 16.62 ?  23  ILE   A N    1 
ATOM   605  C CA   A ILE   A 1 23  ? 16.563 0.423   9.780   0.86 15.80 ?  23  ILE   A CA   1 
ATOM   606  C CA   B ILE   A 1 23  ? 16.715 0.044   9.850   0.14 16.56 ?  23  ILE   A CA   1 
ATOM   607  C C    A ILE   A 1 23  ? 17.367 1.371   10.659  0.86 15.97 ?  23  ILE   A C    1 
ATOM   608  C C    B ILE   A 1 23  ? 17.528 0.956   10.762  0.14 16.80 ?  23  ILE   A C    1 
ATOM   609  O O    A ILE   A 1 23  ? 18.085 0.924   11.563  0.86 16.47 ?  23  ILE   A O    1 
ATOM   610  O O    B ILE   A 1 23  ? 18.242 0.477   11.652  0.14 16.42 ?  23  ILE   A O    1 
ATOM   611  C CB   A ILE   A 1 23  ? 17.365 -0.086  8.561   0.86 15.56 ?  23  ILE   A CB   1 
ATOM   612  C CB   B ILE   A 1 23  ? 17.528 -0.464  8.643   0.14 16.20 ?  23  ILE   A CB   1 
ATOM   613  C CG1  A ILE   A 1 23  ? 18.526 -0.978  9.004   0.86 15.81 ?  23  ILE   A CG1  1 
ATOM   614  C CG1  B ILE   A 1 23  ? 18.661 -1.381  9.113   0.14 16.08 ?  23  ILE   A CG1  1 
ATOM   615  C CG2  A ILE   A 1 23  ? 17.849 1.072   7.700   0.86 15.80 ?  23  ILE   A CG2  1 
ATOM   616  C CG2  B ILE   A 1 23  ? 18.082 0.697   7.827   0.14 16.11 ?  23  ILE   A CG2  1 
ATOM   617  C CD1  A ILE   A 1 23  ? 19.233 -1.675  7.848   0.86 15.67 ?  23  ILE   A CD1  1 
ATOM   618  C CD1  B ILE   A 1 23  ? 19.463 -1.987  7.984   0.14 16.00 ?  23  ILE   A CD1  1 
ATOM   619  H H    A ILE   A 1 23  ? 15.195 1.069   8.506   0.86 19.87 ?  23  ILE   A H    1 
ATOM   620  H H    B ILE   A 1 23  ? 15.447 0.880   8.574   0.14 19.95 ?  23  ILE   A H    1 
ATOM   621  H HA   A ILE   A 1 23  ? 16.359 -0.348  10.326  0.86 18.96 ?  23  ILE   A HA   1 
ATOM   622  H HA   B ILE   A 1 23  ? 16.470 -0.733  10.371  0.14 19.88 ?  23  ILE   A HA   1 
ATOM   623  H HB   A ILE   A 1 23  ? 16.768 -0.625  8.022   0.86 18.68 ?  23  ILE   A HB   1 
ATOM   624  H HB   B ILE   A 1 23  ? 16.939 -0.981  8.074   0.14 19.44 ?  23  ILE   A HB   1 
ATOM   625  H HG12 A ILE   A 1 23  ? 19.183 -0.440  9.469   0.86 18.98 ?  23  ILE   A HG12 1 
ATOM   626  H HG12 B ILE   A 1 23  ? 19.272 -0.870  9.666   0.14 19.30 ?  23  ILE   A HG12 1 
ATOM   627  H HG13 A ILE   A 1 23  ? 18.185 -1.668  9.597   0.86 18.98 ?  23  ILE   A HG13 1 
ATOM   628  H HG13 B ILE   A 1 23  ? 18.280 -2.109  9.628   0.14 19.30 ?  23  ILE   A HG13 1 
ATOM   629  H HG21 A ILE   A 1 23  ? 18.200 0.723   6.864   0.86 18.97 ?  23  ILE   A HG21 1 
ATOM   630  H HG21 B ILE   A 1 23  ? 18.417 0.358   6.980   0.14 19.34 ?  23  ILE   A HG21 1 
ATOM   631  H HG22 A ILE   A 1 23  ? 17.102 1.666   7.518   0.86 18.97 ?  23  ILE   A HG22 1 
ATOM   632  H HG22 B ILE   A 1 23  ? 17.372 1.336   7.668   0.14 19.34 ?  23  ILE   A HG22 1 
ATOM   633  H HG23 A ILE   A 1 23  ? 18.545 1.555   8.172   0.86 18.97 ?  23  ILE   A HG23 1 
ATOM   634  H HG23 B ILE   A 1 23  ? 18.802 1.118   8.322   0.14 19.34 ?  23  ILE   A HG23 1 
ATOM   635  H HD11 A ILE   A 1 23  ? 19.891 -2.289  8.204   0.86 18.81 ?  23  ILE   A HD11 1 
ATOM   636  H HD11 B ILE   A 1 23  ? 20.071 -2.649  8.350   0.14 19.21 ?  23  ILE   A HD11 1 
ATOM   637  H HD12 A ILE   A 1 23  ? 18.575 -2.160  7.325   0.86 18.81 ?  23  ILE   A HD12 1 
ATOM   638  H HD12 B ILE   A 1 23  ? 18.855 -2.407  7.357   0.14 19.21 ?  23  ILE   A HD12 1 
ATOM   639  H HD13 A ILE   A 1 23  ? 19.665 -1.005  7.296   0.86 18.81 ?  23  ILE   A HD13 1 
ATOM   640  H HD13 B ILE   A 1 23  ? 19.965 -1.286  7.541   0.14 19.21 ?  23  ILE   A HD13 1 
ATOM   641  N N    A VAL   A 1 24  ? 17.243 2.682   10.435  0.86 16.85 ?  24  VAL   A N    1 
ATOM   642  N N    B VAL   A 1 24  ? 17.432 2.272   10.570  0.14 17.69 ?  24  VAL   A N    1 
ATOM   643  C CA   A VAL   A 1 24  ? 17.930 3.652   11.286  0.86 18.08 ?  24  VAL   A CA   1 
ATOM   644  C CA   B VAL   A 1 24  ? 18.129 3.206   11.449  0.14 18.66 ?  24  VAL   A CA   1 
ATOM   645  C C    A VAL   A 1 24  ? 17.421 3.554   12.717  0.86 18.91 ?  24  VAL   A C    1 
ATOM   646  C C    B VAL   A 1 24  ? 17.529 3.162   12.850  0.14 19.52 ?  24  VAL   A C    1 
ATOM   647  O O    A VAL   A 1 24  ? 18.203 3.474   13.673  0.86 19.25 ?  24  VAL   A O    1 
ATOM   648  O O    B VAL   A 1 24  ? 18.252 3.106   13.852  0.14 19.55 ?  24  VAL   A O    1 
ATOM   649  C CB   A VAL   A 1 24  ? 17.763 5.075   10.724  0.86 19.16 ?  24  VAL   A CB   1 
ATOM   650  C CB   B VAL   A 1 24  ? 18.100 4.625   10.854  0.14 18.83 ?  24  VAL   A CB   1 
ATOM   651  C CG1  A VAL   A 1 24  ? 18.296 6.111   11.711  0.86 20.11 ?  24  VAL   A CG1  1 
ATOM   652  C CG1  B VAL   A 1 24  ? 18.704 5.622   11.830  0.14 18.95 ?  24  VAL   A CG1  1 
ATOM   653  C CG2  A VAL   A 1 24  ? 18.465 5.200   9.381   0.86 20.46 ?  24  VAL   A CG2  1 
ATOM   654  C CG2  B VAL   A 1 24  ? 18.841 4.657   9.525   0.14 18.94 ?  24  VAL   A CG2  1 
ATOM   655  H H    A VAL   A 1 24  ? 16.775 3.033   9.805   0.86 20.23 ?  24  VAL   A H    1 
ATOM   656  H H    B VAL   A 1 24  ? 16.980 2.644   9.944   0.14 21.24 ?  24  VAL   A H    1 
ATOM   657  H HA   A VAL   A 1 24  ? 18.877 3.451   11.298  0.86 21.71 ?  24  VAL   A HA   1 
ATOM   658  H HA   B VAL   A 1 24  ? 19.057 2.938   11.519  0.14 22.40 ?  24  VAL   A HA   1 
ATOM   659  H HB   A VAL   A 1 24  ? 16.821 5.256   10.583  0.86 23.00 ?  24  VAL   A HB   1 
ATOM   660  H HB   B VAL   A 1 24  ? 17.181 4.885   10.690  0.14 22.60 ?  24  VAL   A HB   1 
ATOM   661  H HG11 A VAL   A 1 24  ? 18.438 6.948   11.242  0.86 24.15 ?  24  VAL   A HG11 1 
ATOM   662  H HG11 B VAL   A 1 24  ? 18.898 6.445   11.355  0.14 22.75 ?  24  VAL   A HG11 1 
ATOM   663  H HG12 A VAL   A 1 24  ? 17.646 6.235   12.419  0.86 24.15 ?  24  VAL   A HG12 1 
ATOM   664  H HG12 B VAL   A 1 24  ? 18.066 5.794   12.540  0.14 22.75 ?  24  VAL   A HG12 1 
ATOM   665  H HG13 A VAL   A 1 24  ? 19.135 5.792   12.078  0.86 24.15 ?  24  VAL   A HG13 1 
ATOM   666  H HG13 B VAL   A 1 24  ? 19.521 5.251   12.196  0.14 22.75 ?  24  VAL   A HG13 1 
ATOM   667  H HG21 A VAL   A 1 24  ? 18.288 6.080   9.009   0.86 24.56 ?  24  VAL   A HG21 1 
ATOM   668  H HG21 B VAL   A 1 24  ? 18.442 5.337   8.961   0.14 22.73 ?  24  VAL   A HG21 1 
ATOM   669  H HG22 A VAL   A 1 24  ? 19.421 5.086   9.511   0.86 24.56 ?  24  VAL   A HG22 1 
ATOM   670  H HG22 B VAL   A 1 24  ? 19.772 4.871   9.690   0.14 22.73 ?  24  VAL   A HG22 1 
ATOM   671  H HG23 A VAL   A 1 24  ? 18.129 4.516   8.781   0.86 24.56 ?  24  VAL   A HG23 1 
ATOM   672  H HG23 B VAL   A 1 24  ? 18.768 3.790   9.095   0.14 22.73 ?  24  VAL   A HG23 1 
ATOM   673  N N    A GLU   A 1 25  ? 16.097 3.562   12.886  0.86 19.96 ?  25  GLU   A N    1 
ATOM   674  N N    B GLU   A 1 25  ? 16.198 3.189   12.941  0.14 20.38 ?  25  GLU   A N    1 
ATOM   675  C CA   A GLU   A 1 25  ? 15.527 3.484   14.227  0.86 21.73 ?  25  GLU   A CA   1 
ATOM   676  C CA   B GLU   A 1 25  ? 15.551 3.107   14.246  0.14 21.38 ?  25  GLU   A CA   1 
ATOM   677  C C    A GLU   A 1 25  ? 15.775 2.117   14.856  0.86 20.33 ?  25  GLU   A C    1 
ATOM   678  C C    B GLU   A 1 25  ? 15.749 1.734   14.879  0.14 20.97 ?  25  GLU   A C    1 
ATOM   679  O O    A GLU   A 1 25  ? 16.029 2.021   16.062  0.86 21.03 ?  25  GLU   A O    1 
ATOM   680  O O    B GLU   A 1 25  ? 15.891 1.626   16.103  0.14 20.94 ?  25  GLU   A O    1 
ATOM   681  C CB   A GLU   A 1 25  ? 14.034 3.820   14.181  0.86 24.65 ?  25  GLU   A CB   1 
ATOM   682  C CB   B GLU   A 1 25  ? 14.068 3.463   14.124  0.14 22.69 ?  25  GLU   A CB   1 
ATOM   683  C CG   A GLU   A 1 25  ? 13.754 5.253   13.735  0.86 28.24 ?  25  GLU   A CG   1 
ATOM   684  C CG   B GLU   A 1 25  ? 13.822 4.892   13.668  0.14 24.04 ?  25  GLU   A CG   1 
ATOM   685  C CD   A GLU   A 1 25  ? 14.511 6.283   14.558  0.86 31.53 ?  25  GLU   A CD   1 
ATOM   686  C CD   B GLU   A 1 25  ? 14.441 5.913   14.600  0.14 25.16 ?  25  GLU   A CD   1 
ATOM   687  O OE1  A GLU   A 1 25  ? 14.585 6.127   15.796  0.86 32.63 ?  25  GLU   A OE1  1 
ATOM   688  O OE1  B GLU   A 1 25  ? 14.533 5.629   15.814  0.14 25.48 ?  25  GLU   A OE1  1 
ATOM   689  O OE2  A GLU   A 1 25  ? 15.052 7.238   13.962  0.86 32.96 -1 25  GLU   A OE2  1 
ATOM   690  O OE2  B GLU   A 1 25  ? 14.842 6.993   14.121  0.14 25.62 -1 25  GLU   A OE2  1 
ATOM   691  H H    A GLU   A 1 25  ? 15.516 3.616   12.251  0.86 23.96 ?  25  GLU   A H    1 
ATOM   692  H H    B GLU   A 1 25  ? 15.659 3.263   12.274  0.14 24.46 ?  25  GLU   A H    1 
ATOM   693  H HA   A GLU   A 1 25  ? 15.957 4.143   14.788  0.86 26.08 ?  25  GLU   A HA   1 
ATOM   694  H HA   B GLU   A 1 25  ? 15.962 3.752   14.837  0.14 25.66 ?  25  GLU   A HA   1 
ATOM   695  H HB2  A GLU   A 1 25  ? 13.589 3.226   13.555  0.86 29.59 ?  25  GLU   A HB2  1 
ATOM   696  H HB2  B GLU   A 1 25  ? 13.651 2.873   13.479  0.14 27.23 ?  25  GLU   A HB2  1 
ATOM   697  H HB3  A GLU   A 1 25  ? 13.652 3.709   15.067  0.86 29.59 ?  25  GLU   A HB3  1 
ATOM   698  H HB3  B GLU   A 1 25  ? 13.646 3.356   14.991  0.14 27.23 ?  25  GLU   A HB3  1 
ATOM   699  H HG2  A GLU   A 1 25  ? 14.033 5.357   12.813  0.86 33.90 ?  25  GLU   A HG2  1 
ATOM   700  H HG2  B GLU   A 1 25  ? 14.204 5.014   12.784  0.14 28.85 ?  25  GLU   A HG2  1 
ATOM   701  H HG3  A GLU   A 1 25  ? 12.801 5.431   13.815  0.86 33.90 ?  25  GLU   A HG3  1 
ATOM   702  H HG3  B GLU   A 1 25  ? 12.868 5.061   13.642  0.14 28.85 ?  25  GLU   A HG3  1 
ATOM   703  N N    A GLU   A 1 26  ? 15.735 1.051   14.053  0.86 19.56 ?  26  GLU   A N    1 
ATOM   704  N N    B GLU   A 1 26  ? 15.766 0.673   14.068  0.14 20.73 ?  26  GLU   A N    1 
ATOM   705  C CA   A GLU   A 1 26  ? 16.042 -0.279  14.574  0.86 19.49 ?  26  GLU   A CA   1 
ATOM   706  C CA   B GLU   A 1 26  ? 16.128 -0.637  14.600  0.14 20.59 ?  26  GLU   A CA   1 
ATOM   707  C C    A GLU   A 1 26  ? 17.472 -0.339  15.101  0.86 18.31 ?  26  GLU   A C    1 
ATOM   708  C C    B GLU   A 1 26  ? 17.581 -0.669  15.053  0.14 20.26 ?  26  GLU   A C    1 
ATOM   709  O O    A GLU   A 1 26  ? 17.724 -0.859  16.195  0.86 18.52 ?  26  GLU   A O    1 
ATOM   710  O O    B GLU   A 1 26  ? 17.915 -1.376  16.011  0.14 20.21 ?  26  GLU   A O    1 
ATOM   711  C CB   A GLU   A 1 26  ? 15.847 -1.326  13.476  0.86 21.33 ?  26  GLU   A CB   1 
ATOM   712  C CB   B GLU   A 1 26  ? 15.875 -1.725  13.555  0.14 20.85 ?  26  GLU   A CB   1 
ATOM   713  C CG   A GLU   A 1 26  ? 14.458 -1.918  13.367  0.86 23.81 ?  26  GLU   A CG   1 
ATOM   714  C CG   B GLU   A 1 26  ? 14.406 -1.992  13.284  0.14 21.11 ?  26  GLU   A CG   1 
ATOM   715  C CD   A GLU   A 1 26  ? 14.047 -2.723  14.592  0.86 24.78 ?  26  GLU   A CD   1 
ATOM   716  C CD   B GLU   A 1 26  ? 13.678 -2.526  14.497  0.14 21.13 ?  26  GLU   A CD   1 
ATOM   717  O OE1  A GLU   A 1 26  ? 14.480 -3.894  14.782  0.86 25.16 ?  26  GLU   A OE1  1 
ATOM   718  O OE1  B GLU   A 1 26  ? 14.285 -3.296  15.270  0.14 21.25 ?  26  GLU   A OE1  1 
ATOM   719  O OE2  A GLU   A 1 26  ? 13.266 -2.163  15.370  0.86 26.18 -1 26  GLU   A OE2  1 
ATOM   720  O OE2  B GLU   A 1 26  ? 12.499 -2.161  14.682  0.14 21.02 -1 26  GLU   A OE2  1 
ATOM   721  H H    A GLU   A 1 26  ? 15.543 1.076   13.216  0.86 23.48 ?  26  GLU   A H    1 
ATOM   722  H H    B GLU   A 1 26  ? 15.573 0.681   13.230  0.14 24.89 ?  26  GLU   A H    1 
ATOM   723  H HA   A GLU   A 1 26  ? 15.438 -0.480  15.304  0.86 23.39 ?  26  GLU   A HA   1 
ATOM   724  H HA   B GLU   A 1 26  ? 15.572 -0.828  15.371  0.14 24.72 ?  26  GLU   A HA   1 
ATOM   725  H HB2  A GLU   A 1 26  ? 16.055 -0.915  12.621  0.86 25.60 ?  26  GLU   A HB2  1 
ATOM   726  H HB2  B GLU   A 1 26  ? 16.284 -1.457  12.717  0.14 25.02 ?  26  GLU   A HB2  1 
ATOM   727  H HB3  A GLU   A 1 26  ? 16.461 -2.056  13.642  0.86 25.60 ?  26  GLU   A HB3  1 
ATOM   728  H HB3  B GLU   A 1 26  ? 16.275 -2.555  13.863  0.14 25.02 ?  26  GLU   A HB3  1 
ATOM   729  H HG2  A GLU   A 1 26  ? 13.820 -1.191  13.250  0.86 28.59 ?  26  GLU   A HG2  1 
ATOM   730  H HG2  B GLU   A 1 26  ? 13.974 -1.164  13.032  0.14 25.34 ?  26  GLU   A HG2  1 
ATOM   731  H HG3  A GLU   A 1 26  ? 14.423 -2.510  12.604  0.86 28.59 ?  26  GLU   A HG3  1 
ATOM   732  H HG3  B GLU   A 1 26  ? 14.327 -2.643  12.570  0.14 25.34 ?  26  GLU   A HG3  1 
ATOM   733  N N    A ALA   A 1 27  ? 18.424 0.188   14.331  0.86 17.03 ?  27  ALA   A N    1 
ATOM   734  N N    B ALA   A 1 27  ? 18.455 0.087   14.386  0.14 20.11 ?  27  ALA   A N    1 
ATOM   735  C CA   A ALA   A 1 27  ? 19.818 0.146   14.760  0.86 17.19 ?  27  ALA   A CA   1 
ATOM   736  C CA   B ALA   A 1 27  ? 19.856 0.125   14.792  0.14 20.12 ?  27  ALA   A CA   1 
ATOM   737  C C    A ALA   A 1 27  ? 20.016 0.932   16.050  0.86 18.58 ?  27  ALA   A C    1 
ATOM   738  C C    B ALA   A 1 27  ? 20.034 0.936   16.069  0.14 20.40 ?  27  ALA   A C    1 
ATOM   739  O O    A ALA   A 1 27  ? 20.694 0.470   16.974  0.86 18.88 ?  27  ALA   A O    1 
ATOM   740  O O    B ALA   A 1 27  ? 20.728 0.505   16.997  0.14 20.39 ?  27  ALA   A O    1 
ATOM   741  C CB   A ALA   A 1 27  ? 20.722 0.686   13.653  0.86 17.00 ?  27  ALA   A CB   1 
ATOM   742  C CB   B ALA   A 1 27  ? 20.718 0.693   13.665  0.14 20.03 ?  27  ALA   A CB   1 
ATOM   743  H H    A ALA   A 1 27  ? 18.287 0.570   13.570  0.86 20.45 ?  27  ALA   A H    1 
ATOM   744  H H    B ALA   A 1 27  ? 18.264 0.575   13.703  0.14 24.14 ?  27  ALA   A H    1 
ATOM   745  H HA   A ALA   A 1 27  ? 20.064 -0.775  14.925  0.86 20.64 ?  27  ALA   A HA   1 
ATOM   746  H HA   B ALA   A 1 27  ? 20.153 -0.781  14.968  0.14 24.15 ?  27  ALA   A HA   1 
ATOM   747  H HB1  A ALA   A 1 27  ? 21.645 0.650   13.955  0.86 20.41 ?  27  ALA   A HB1  1 
ATOM   748  H HB1  B ALA   A 1 27  ? 21.644 0.708   13.956  0.14 24.05 ?  27  ALA   A HB1  1 
ATOM   749  H HB2  A ALA   A 1 27  ? 20.614 0.138   12.859  0.86 20.41 ?  27  ALA   A HB2  1 
ATOM   750  H HB2  B ALA   A 1 27  ? 20.627 0.129   12.882  0.14 24.05 ?  27  ALA   A HB2  1 
ATOM   751  H HB3  A ALA   A 1 27  ? 20.475 1.603   13.458  0.86 20.41 ?  27  ALA   A HB3  1 
ATOM   752  H HB3  B ALA   A 1 27  ? 20.421 1.593   13.463  0.14 24.05 ?  27  ALA   A HB3  1 
ATOM   753  N N    . LYS   A 1 28  ? 19.414 2.118   16.139  1.00 20.84 ?  28  LYS   A N    1 
ATOM   754  C CA   . LYS   A 1 28  ? 19.553 2.937   17.340  1.00 24.27 ?  28  LYS   A CA   1 
ATOM   755  C C    . LYS   A 1 28  ? 19.010 2.225   18.572  1.00 25.68 ?  28  LYS   A C    1 
ATOM   756  O O    . LYS   A 1 28  ? 19.547 2.396   19.673  1.00 27.32 ?  28  LYS   A O    1 
ATOM   757  C CB   . LYS   A 1 28  ? 18.871 4.293   17.142  1.00 26.85 ?  28  LYS   A CB   1 
ATOM   758  C CG   . LYS   A 1 28  ? 19.668 5.242   16.258  1.00 29.29 ?  28  LYS   A CG   1 
ATOM   759  C CD   . LYS   A 1 28  ? 19.179 6.678   16.358  1.00 32.01 ?  28  LYS   A CD   1 
ATOM   760  C CE   . LYS   A 1 28  ? 17.905 6.891   15.568  1.00 33.93 ?  28  LYS   A CE   1 
ATOM   761  N NZ   . LYS   A 1 28  ? 17.552 8.336   15.477  1.00 35.10 ?  28  LYS   A NZ   1 
ATOM   762  H H    A LYS   A 1 28  ? 18.925 2.464   15.526  0.86 25.02 ?  28  LYS   A H    1 
ATOM   763  H H    B LYS   A 1 28  ? 18.922 2.455   15.524  0.14 25.02 ?  28  LYS   A H    1 
ATOM   764  H HA   . LYS   A 1 28  ? 20.491 3.102   17.499  1.00 29.13 ?  28  LYS   A HA   1 
ATOM   765  H HB2  . LYS   A 1 28  ? 18.008 4.156   16.723  1.00 32.22 ?  28  LYS   A HB2  1 
ATOM   766  H HB3  . LYS   A 1 28  ? 18.757 4.719   18.005  1.00 32.22 ?  28  LYS   A HB3  1 
ATOM   767  H HG2  . LYS   A 1 28  ? 20.600 5.223   16.529  1.00 35.16 ?  28  LYS   A HG2  1 
ATOM   768  H HG3  . LYS   A 1 28  ? 19.586 4.961   15.333  1.00 35.16 ?  28  LYS   A HG3  1 
ATOM   769  H HD2  . LYS   A 1 28  ? 18.998 6.891   17.288  1.00 38.41 ?  28  LYS   A HD2  1 
ATOM   770  H HD3  . LYS   A 1 28  ? 19.858 7.274   16.005  1.00 38.41 ?  28  LYS   A HD3  1 
ATOM   771  H HE2  . LYS   A 1 28  ? 18.027 6.551   14.668  1.00 40.72 ?  28  LYS   A HE2  1 
ATOM   772  H HE3  . LYS   A 1 28  ? 17.175 6.427   16.005  1.00 40.72 ?  28  LYS   A HE3  1 
ATOM   773  H HZ1  . LYS   A 1 28  ? 16.803 8.437   15.008  1.00 42.13 ?  28  LYS   A HZ1  1 
ATOM   774  H HZ2  . LYS   A 1 28  ? 17.432 8.671   16.292  1.00 42.13 ?  28  LYS   A HZ2  1 
ATOM   775  H HZ3  . LYS   A 1 28  ? 18.208 8.784   15.073  1.00 42.13 ?  28  LYS   A HZ3  1 
ATOM   776  N N    . LYS   A 1 29  ? 17.965 1.414   18.408  1.00 26.27 ?  29  LYS   A N    1 
ATOM   777  C CA   . LYS   A 1 29  ? 17.374 0.700   19.536  1.00 28.32 ?  29  LYS   A CA   1 
ATOM   778  C C    . LYS   A 1 29  ? 18.203 -0.522  19.920  1.00 27.00 ?  29  LYS   A C    1 
ATOM   779  O O    . LYS   A 1 29  ? 18.497 -0.739  21.102  1.00 27.77 ?  29  LYS   A O    1 
ATOM   780  C CB   . LYS   A 1 29  ? 15.949 0.272   19.176  1.00 31.92 ?  29  LYS   A CB   1 
ATOM   781  C CG   . LYS   A 1 29  ? 15.193 -0.418  20.301  1.00 35.80 ?  29  LYS   A CG   1 
ATOM   782  C CD   . LYS   A 1 29  ? 14.800 0.570   21.384  1.00 39.44 ?  29  LYS   A CD   1 
ATOM   783  C CE   . LYS   A 1 29  ? 13.890 -0.071  22.417  1.00 41.94 ?  29  LYS   A CE   1 
ATOM   784  N NZ   . LYS   A 1 29  ? 13.439 0.912   23.439  1.00 43.25 ?  29  LYS   A NZ   1 
ATOM   785  H H    . LYS   A 1 29  ? 17.583 1.257   17.654  1.00 31.54 ?  29  LYS   A H    1 
ATOM   786  H HA   . LYS   A 1 29  ? 17.327 1.288   20.304  1.00 33.99 ?  29  LYS   A HA   1 
ATOM   787  H HB2  . LYS   A 1 29  ? 15.440 1.060   18.927  1.00 38.31 ?  29  LYS   A HB2  1 
ATOM   788  H HB3  . LYS   A 1 29  ? 15.985 -0.344  18.429  1.00 38.31 ?  29  LYS   A HB3  1 
ATOM   789  H HG2  . LYS   A 1 29  ? 14.383 -0.816  19.945  1.00 42.97 ?  29  LYS   A HG2  1 
ATOM   790  H HG3  . LYS   A 1 29  ? 15.753 -1.104  20.701  1.00 42.97 ?  29  LYS   A HG3  1 
ATOM   791  H HD2  . LYS   A 1 29  ? 15.599 0.886   21.835  1.00 47.33 ?  29  LYS   A HD2  1 
ATOM   792  H HD3  . LYS   A 1 29  ? 14.327 1.315   20.980  1.00 47.33 ?  29  LYS   A HD3  1 
ATOM   793  H HE2  . LYS   A 1 29  ? 13.105 -0.428  21.972  1.00 50.33 ?  29  LYS   A HE2  1 
ATOM   794  H HE3  . LYS   A 1 29  ? 14.371 -0.781  22.869  1.00 50.33 ?  29  LYS   A HE3  1 
ATOM   795  H HZ1  . LYS   A 1 29  ? 12.908 0.513   24.031  1.00 51.91 ?  29  LYS   A HZ1  1 
ATOM   796  H HZ2  . LYS   A 1 29  ? 14.143 1.252   23.865  1.00 51.91 ?  29  LYS   A HZ2  1 
ATOM   797  H HZ3  . LYS   A 1 29  ? 12.990 1.573   23.048  1.00 51.91 ?  29  LYS   A HZ3  1 
ATOM   798  N N    . VAL   A 1 30  ? 18.570 -1.339  18.934  1.00 25.43 ?  30  VAL   A N    1 
ATOM   799  C CA   . VAL   A 1 30  ? 19.218 -2.615  19.215  1.00 24.79 ?  30  VAL   A CA   1 
ATOM   800  C C    . VAL   A 1 30  ? 20.725 -2.460  19.428  1.00 23.07 ?  30  VAL   A C    1 
ATOM   801  O O    . VAL   A 1 30  ? 21.317 -3.182  20.237  1.00 23.60 ?  30  VAL   A O    1 
ATOM   802  C CB   . VAL   A 1 30  ? 18.896 -3.605  18.081  1.00 25.24 ?  30  VAL   A CB   1 
ATOM   803  C CG1  . VAL   A 1 30  ? 19.660 -4.907  18.264  1.00 25.64 ?  30  VAL   A CG1  1 
ATOM   804  C CG2  . VAL   A 1 30  ? 17.395 -3.868  18.014  1.00 25.84 ?  30  VAL   A CG2  1 
ATOM   805  H H    . VAL   A 1 30  ? 18.435 -1.188  18.098  1.00 30.53 ?  30  VAL   A H    1 
ATOM   806  H HA   . VAL   A 1 30  ? 18.839 -2.981  20.029  1.00 29.75 ?  30  VAL   A HA   1 
ATOM   807  H HB   . VAL   A 1 30  ? 19.168 -3.218  17.235  1.00 30.29 ?  30  VAL   A HB   1 
ATOM   808  H HG11 . VAL   A 1 30  ? 19.272 -5.582  17.684  1.00 30.78 ?  30  VAL   A HG11 1 
ATOM   809  H HG12 . VAL   A 1 30  ? 20.589 -4.765  18.029  1.00 30.78 ?  30  VAL   A HG12 1 
ATOM   810  H HG13 . VAL   A 1 30  ? 19.586 -5.187  19.189  1.00 30.78 ?  30  VAL   A HG13 1 
ATOM   811  H HG21 . VAL   A 1 30  ? 17.220 -4.532  17.328  1.00 31.02 ?  30  VAL   A HG21 1 
ATOM   812  H HG22 . VAL   A 1 30  ? 17.094 -4.198  18.876  1.00 31.02 ?  30  VAL   A HG22 1 
ATOM   813  H HG23 . VAL   A 1 30  ? 16.939 -3.041  17.798  1.00 31.02 ?  30  VAL   A HG23 1 
ATOM   814  N N    . LYS   A 1 31  ? 21.363 -1.520  18.740  1.00 21.83 ?  31  LYS   A N    1 
ATOM   815  C CA   . LYS   A 1 31  ? 22.817 -1.423  18.689  1.00 23.10 ?  31  LYS   A CA   1 
ATOM   816  C C    . LYS   A 1 31  ? 23.416 -2.778  18.303  1.00 19.55 ?  31  LYS   A C    1 
ATOM   817  O O    . LYS   A 1 31  ? 24.197 -3.360  19.063  1.00 20.69 ?  31  LYS   A O    1 
ATOM   818  C CB   . LYS   A 1 31  ? 23.407 -0.918  19.998  1.00 28.62 ?  31  LYS   A CB   1 
ATOM   819  C CG   . LYS   A 1 31  ? 22.739 0.339   20.537  1.00 35.20 ?  31  LYS   A CG   1 
ATOM   820  C CD   . LYS   A 1 31  ? 23.744 1.458   20.775  1.00 40.19 ?  31  LYS   A CD   1 
ATOM   821  C CE   . LYS   A 1 31  ? 23.190 2.511   21.727  1.00 43.55 ?  31  LYS   A CE   1 
ATOM   822  N NZ   . LYS   A 1 31  ? 21.912 3.107   21.246  1.00 45.41 ?  31  LYS   A NZ   1 
ATOM   823  H H    . LYS   A 1 31  ? 20.966 -0.905  18.292  1.00 26.21 ?  31  LYS   A H    1 
ATOM   824  H HA   . LYS   A 1 31  ? 23.055 -0.790  18.000  1.00 27.73 ?  31  LYS   A HA   1 
ATOM   825  H HB2  . LYS   A 1 31  ? 23.324 -1.610  20.670  1.00 34.35 ?  31  LYS   A HB2  1 
ATOM   826  H HB3  . LYS   A 1 31  ? 24.348 -0.714  19.854  1.00 34.35 ?  31  LYS   A HB3  1 
ATOM   827  H HG2  . LYS   A 1 31  ? 22.084 0.654   19.895  1.00 42.24 ?  31  LYS   A HG2  1 
ATOM   828  H HG3  . LYS   A 1 31  ? 22.308 0.134   21.382  1.00 42.24 ?  31  LYS   A HG3  1 
ATOM   829  H HD2  . LYS   A 1 31  ? 24.550 1.089   21.168  1.00 48.24 ?  31  LYS   A HD2  1 
ATOM   830  H HD3  . LYS   A 1 31  ? 23.949 1.889   19.930  1.00 48.24 ?  31  LYS   A HD3  1 
ATOM   831  H HE2  . LYS   A 1 31  ? 23.024 2.100   22.590  1.00 52.27 ?  31  LYS   A HE2  1 
ATOM   832  H HE3  . LYS   A 1 31  ? 23.839 3.226   21.819  1.00 52.27 ?  31  LYS   A HE3  1 
ATOM   833  H HZ1  . LYS   A 1 31  ? 21.628 3.723   21.822  1.00 54.50 ?  31  LYS   A HZ1  1 
ATOM   834  H HZ2  . LYS   A 1 31  ? 22.035 3.489   20.452  1.00 54.50 ?  31  LYS   A HZ2  1 
ATOM   835  H HZ3  . LYS   A 1 31  ? 21.291 2.474   21.169  1.00 54.50 ?  31  LYS   A HZ3  1 
ATOM   836  N N    . PRO   A 1 32  ? 23.058 -3.307  17.140  1.00 17.12 ?  32  PRO   A N    1 
ATOM   837  C CA   . PRO   A 1 32  ? 23.542 -4.632  16.756  1.00 18.01 ?  32  PRO   A CA   1 
ATOM   838  C C    . PRO   A 1 32  ? 25.041 -4.631  16.537  1.00 17.90 ?  32  PRO   A C    1 
ATOM   839  O O    . PRO   A 1 32  ? 25.670 -3.594  16.321  1.00 17.82 ?  32  PRO   A O    1 
ATOM   840  C CB   . PRO   A 1 32  ? 22.805 -4.901  15.441  1.00 17.93 ?  32  PRO   A CB   1 
ATOM   841  C CG   . PRO   A 1 32  ? 22.594 -3.529  14.869  1.00 16.30 ?  32  PRO   A CG   1 
ATOM   842  C CD   . PRO   A 1 32  ? 22.304 -2.664  16.052  1.00 16.57 ?  32  PRO   A CD   1 
ATOM   843  H HA   . PRO   A 1 32  ? 23.308 -5.301  17.415  1.00 21.62 ?  32  PRO   A HA   1 
ATOM   844  H HB2  . PRO   A 1 32  ? 23.358 -5.444  14.851  1.00 21.53 ?  32  PRO   A HB2  1 
ATOM   845  H HB3  . PRO   A 1 32  ? 21.960 -5.341  15.621  1.00 21.53 ?  32  PRO   A HB3  1 
ATOM   846  H HG2  . PRO   A 1 32  ? 23.397 -3.242  14.411  1.00 19.57 ?  32  PRO   A HG2  1 
ATOM   847  H HG3  . PRO   A 1 32  ? 21.838 -3.550  14.257  1.00 19.57 ?  32  PRO   A HG3  1 
ATOM   848  H HD2  . PRO   A 1 32  ? 22.627 -1.765  15.894  1.00 19.89 ?  32  PRO   A HD2  1 
ATOM   849  H HD3  . PRO   A 1 32  ? 21.357 -2.677  16.254  1.00 19.89 ?  32  PRO   A HD3  1 
ATOM   850  N N    . THR   A 1 33  ? 25.612 -5.834  16.575  1.00 17.81 ?  33  THR   A N    1 
ATOM   851  C CA   . THR   A 1 33  ? 27.019 -5.984  16.237  1.00 18.17 ?  33  THR   A CA   1 
ATOM   852  C C    . THR   A 1 33  ? 27.288 -5.516  14.816  1.00 16.55 ?  33  THR   A C    1 
ATOM   853  O O    . THR   A 1 33  ? 28.311 -4.871  14.553  1.00 16.40 ?  33  THR   A O    1 
ATOM   854  C CB   . THR   A 1 33  ? 27.443 -7.439  16.429  1.00 19.79 ?  33  THR   A CB   1 
ATOM   855  O OG1  . THR   A 1 33  ? 27.139 -7.840  17.767  1.00 21.72 ?  33  THR   A OG1  1 
ATOM   856  C CG2  . THR   A 1 33  ? 28.938 -7.610  16.181  1.00 20.71 ?  33  THR   A CG2  1 
ATOM   857  H H    . THR   A 1 33  ? 25.216 -6.569  16.775  1.00 21.38 ?  33  THR   A H    1 
ATOM   858  H HA   . THR   A 1 33  ? 27.556 -5.441  16.832  1.00 21.82 ?  33  THR   A HA   1 
ATOM   859  H HB   . THR   A 1 33  ? 26.967 -8.012  15.804  1.00 23.76 ?  33  THR   A HB   1 
ATOM   860  H HG1  . THR   A 1 33  ? 27.562 -7.362  18.316  1.00 26.07 ?  33  THR   A HG1  1 
ATOM   861  H HG21 . THR   A 1 33  ? 29.222 -8.501  16.448  1.00 24.86 ?  33  THR   A HG21 1 
ATOM   862  H HG22 . THR   A 1 33  ? 29.138 -7.489  15.240  1.00 24.86 ?  33  THR   A HG22 1 
ATOM   863  H HG23 . THR   A 1 33  ? 29.436 -6.957  16.697  1.00 24.86 ?  33  THR   A HG23 1 
ATOM   864  N N    . VAL   A 1 34  ? 26.376 -5.815  13.891  1.00 14.69 ?  34  VAL   A N    1 
ATOM   865  C CA   . VAL   A 1 34  ? 26.546 -5.481  12.481  1.00 13.73 ?  34  VAL   A CA   1 
ATOM   866  C C    . VAL   A 1 34  ? 25.237 -4.923  11.934  1.00 13.03 ?  34  VAL   A C    1 
ATOM   867  O O    . VAL   A 1 34  ? 24.198 -5.592  11.994  1.00 13.88 ?  34  VAL   A O    1 
ATOM   868  C CB   . VAL   A 1 34  ? 26.990 -6.689  11.635  1.00 14.28 ?  34  VAL   A CB   1 
ATOM   869  C CG1  . VAL   A 1 34  ? 27.160 -6.281  10.179  1.00 14.93 ?  34  VAL   A CG1  1 
ATOM   870  C CG2  . VAL   A 1 34  ? 28.282 -7.296  12.180  1.00 15.49 ?  34  VAL   A CG2  1 
ATOM   871  H H    . VAL   A 1 34  ? 25.636 -6.219  14.058  1.00 17.64 ?  34  VAL   A H    1 
ATOM   872  H HA   . VAL   A 1 34  ? 27.224 -4.789  12.392  1.00 16.48 ?  34  VAL   A HA   1 
ATOM   873  H HB   . VAL   A 1 34  ? 26.302 -7.368  11.672  1.00 17.15 ?  34  VAL   A HB   1 
ATOM   874  H HG11 . VAL   A 1 34  ? 27.647 -6.978  9.710   1.00 17.92 ?  34  VAL   A HG11 1 
ATOM   875  H HG12 . VAL   A 1 34  ? 26.289 -6.159  9.775   1.00 17.92 ?  34  VAL   A HG12 1 
ATOM   876  H HG13 . VAL   A 1 34  ? 27.664 -5.449  10.139  1.00 17.92 ?  34  VAL   A HG13 1 
ATOM   877  H HG21 . VAL   A 1 34  ? 28.558 -8.029  11.605  1.00 18.60 ?  34  VAL   A HG21 1 
ATOM   878  H HG22 . VAL   A 1 34  ? 28.973 -6.615  12.198  1.00 18.60 ?  34  VAL   A HG22 1 
ATOM   879  H HG23 . VAL   A 1 34  ? 28.123 -7.627  13.079  1.00 18.60 ?  34  VAL   A HG23 1 
ATOM   880  N N    . VAL   A 1 35  ? 25.289 -3.709  11.385  1.00 12.32 ?  35  VAL   A N    1 
ATOM   881  C CA   . VAL   A 1 35  ? 24.247 -3.193  10.507  1.00 12.26 ?  35  VAL   A CA   1 
ATOM   882  C C    . VAL   A 1 35  ? 24.788 -3.181  9.086   1.00 11.66 ?  35  VAL   A C    1 
ATOM   883  O O    . VAL   A 1 35  ? 25.931 -2.777  8.852   1.00 12.32 ?  35  VAL   A O    1 
ATOM   884  C CB   . VAL   A 1 35  ? 23.711 -1.805  10.929  1.00 13.06 ?  35  VAL   A CB   1 
ATOM   885  C CG1  . VAL   A 1 35  ? 24.778 -0.707  10.811  1.00 13.73 ?  35  VAL   A CG1  1 
ATOM   886  C CG2  . VAL   A 1 35  ? 22.477 -1.449  10.108  1.00 13.78 ?  35  VAL   A CG2  1 
ATOM   887  H H    . VAL   A 1 35  ? 25.934 -3.151  11.507  1.00 14.79 ?  35  VAL   A H    1 
ATOM   888  H HA   . VAL   A 1 35  ? 23.497 -3.809  10.525  1.00 14.73 ?  35  VAL   A HA   1 
ATOM   889  H HB   . VAL   A 1 35  ? 23.438 -1.847  11.855  1.00 15.68 ?  35  VAL   A HB   1 
ATOM   890  H HG11 . VAL   A 1 35  ? 24.426 0.120   11.181  1.00 16.49 ?  35  VAL   A HG11 1 
ATOM   891  H HG12 . VAL   A 1 35  ? 25.567 -0.978  11.307  1.00 16.49 ?  35  VAL   A HG12 1 
ATOM   892  H HG13 . VAL   A 1 35  ? 25.006 -0.577  9.876   1.00 16.49 ?  35  VAL   A HG13 1 
ATOM   893  H HG21 . VAL   A 1 35  ? 22.112 -0.614  10.429  1.00 16.55 ?  35  VAL   A HG21 1 
ATOM   894  H HG22 . VAL   A 1 35  ? 22.732 -1.363  9.173   1.00 16.55 ?  35  VAL   A HG22 1 
ATOM   895  H HG23 . VAL   A 1 35  ? 21.822 -2.159  10.204  1.00 16.55 ?  35  VAL   A HG23 1 
ATOM   896  N N    . VAL   A 1 36  ? 23.969 -3.630  8.141   1.00 11.12 ?  36  VAL   A N    1 
ATOM   897  C CA   . VAL   A 1 36  ? 24.340 -3.641  6.734   1.00 10.93 ?  36  VAL   A CA   1 
ATOM   898  C C    . VAL   A 1 36  ? 23.885 -2.349  6.076   1.00 11.16 ?  36  VAL   A C    1 
ATOM   899  O O    . VAL   A 1 36  ? 22.728 -1.936  6.228   1.00 11.80 ?  36  VAL   A O    1 
ATOM   900  C CB   . VAL   A 1 36  ? 23.727 -4.852  6.019   1.00 10.86 ?  36  VAL   A CB   1 
ATOM   901  C CG1  . VAL   A 1 36  ? 23.991 -4.780  4.541   1.00 11.45 ?  36  VAL   A CG1  1 
ATOM   902  C CG2  . VAL   A 1 36  ? 24.273 -6.137  6.607   1.00 11.96 ?  36  VAL   A CG2  1 
ATOM   903  H H    . VAL   A 1 36  ? 23.177 -3.941  8.293   1.00 13.36 ?  36  VAL   A H    1 
ATOM   904  H HA   . VAL   A 1 36  ? 25.309 -3.707  6.658   1.00 13.12 ?  36  VAL   A HA   1 
ATOM   905  H HB   . VAL   A 1 36  ? 22.767 -4.842  6.153   1.00 13.04 ?  36  VAL   A HB   1 
ATOM   906  H HG11 . VAL   A 1 36  ? 23.847 -5.659  4.153   1.00 13.74 ?  36  VAL   A HG11 1 
ATOM   907  H HG12 . VAL   A 1 36  ? 23.382 -4.142  4.137   1.00 13.74 ?  36  VAL   A HG12 1 
ATOM   908  H HG13 . VAL   A 1 36  ? 24.908 -4.504  4.395   1.00 13.74 ?  36  VAL   A HG13 1 
ATOM   909  H HG21 . VAL   A 1 36  ? 23.892 -6.894  6.129   1.00 14.36 ?  36  VAL   A HG21 1 
ATOM   910  H HG22 . VAL   A 1 36  ? 25.239 -6.146  6.517   1.00 14.36 ?  36  VAL   A HG22 1 
ATOM   911  H HG23 . VAL   A 1 36  ? 24.030 -6.190  7.547   1.00 14.36 ?  36  VAL   A HG23 1 
ATOM   912  N N    . ASN   A 1 37  ? 24.792 -1.723  5.335   1.00 10.46 ?  37  ASN   A N    1 
ATOM   913  C CA   . ASN   A 1 37  ? 24.456 -0.593  4.485   1.00 10.30 ?  37  ASN   A CA   1 
ATOM   914  C C    . ASN   A 1 37  ? 24.318 -1.048  3.047   1.00 10.12 ?  37  ASN   A C    1 
ATOM   915  O O    . ASN   A 1 37  ? 25.097 -1.880  2.569   1.00 11.05 ?  37  ASN   A O    1 
ATOM   916  C CB   . ASN   A 1 37  ? 25.533 0.482   4.565   1.00 10.54 ?  37  ASN   A CB   1 
ATOM   917  C CG   . ASN   A 1 37  ? 25.206 1.681   3.720   1.00 11.21 ?  37  ASN   A CG   1 
ATOM   918  O OD1  . ASN   A 1 37  ? 24.030 2.026   3.552   1.00 11.77 ?  37  ASN   A OD1  1 
ATOM   919  N ND2  . ASN   A 1 37  ? 26.232 2.339   3.195   1.00 11.46 ?  37  ASN   A ND2  1 
ATOM   920  H H    . ASN   A 1 37  ? 25.628 -1.940  5.312   1.00 12.56 ?  37  ASN   A H    1 
ATOM   921  H HA   . ASN   A 1 37  ? 23.619 -0.209  4.777   1.00 12.37 ?  37  ASN   A HA   1 
ATOM   922  H HB2  . ASN   A 1 37  ? 25.624 0.778   5.486   1.00 12.66 ?  37  ASN   A HB2  1 
ATOM   923  H HB3  . ASN   A 1 37  ? 26.379 0.113   4.254   1.00 12.66 ?  37  ASN   A HB3  1 
ATOM   924  H HD21 . ASN   A 1 37  ? 26.091 3.030   2.699   1.00 13.77 ?  37  ASN   A HD21 1 
ATOM   925  H HD22 . ASN   A 1 37  ? 27.033 2.076   3.333   1.00 13.77 ?  37  ASN   A HD22 1 
ATOM   926  N N    A ALA   A 1 38  ? 23.307 -0.498  2.371   0.86 10.88 ?  38  ALA   A N    1 
ATOM   927  N N    B ALA   A 1 38  ? 23.309 -0.518  2.361   0.14 10.57 ?  38  ALA   A N    1 
ATOM   928  C CA   A ALA   A 1 38  ? 23.100 -0.639  0.928   0.86 11.42 ?  38  ALA   A CA   1 
ATOM   929  C CA   B ALA   A 1 38  ? 23.121 -0.780  0.936   0.14 11.11 ?  38  ALA   A CA   1 
ATOM   930  C C    A ALA   A 1 38  ? 24.015 0.348   0.206   0.86 11.09 ?  38  ALA   A C    1 
ATOM   931  C C    B ALA   A 1 38  ? 23.881 0.300   0.177   0.14 10.99 ?  38  ALA   A C    1 
ATOM   932  O O    A ALA   A 1 38  ? 23.610 1.434   -0.220  0.86 11.54 ?  38  ALA   A O    1 
ATOM   933  O O    B ALA   A 1 38  ? 23.335 1.347   -0.175  0.14 10.93 ?  38  ALA   A O    1 
ATOM   934  C CB   A ALA   A 1 38  ? 21.641 -0.377  0.581   0.86 13.03 ?  38  ALA   A CB   1 
ATOM   935  C CB   B ALA   A 1 38  ? 21.640 -0.794  0.588   0.14 11.74 ?  38  ALA   A CB   1 
ATOM   936  H H    A ALA   A 1 38  ? 22.709 -0.007  2.747   0.86 13.07 ?  38  ALA   A H    1 
ATOM   937  H H    B ALA   A 1 38  ? 22.714 0.003   2.704   0.14 12.69 ?  38  ALA   A H    1 
ATOM   938  H HA   A ALA   A 1 38  ? 23.332 -1.542  0.652   0.86 13.72 ?  38  ALA   A HA   1 
ATOM   939  H HA   B ALA   A 1 38  ? 23.501 -1.646  0.713   0.14 13.34 ?  38  ALA   A HA   1 
ATOM   940  H HB1  A ALA   A 1 38  ? 21.520 -0.487  -0.376  0.86 15.64 ?  38  ALA   A HB1  1 
ATOM   941  H HB1  B ALA   A 1 38  ? 21.547 -0.863  -0.373  0.14 14.09 ?  38  ALA   A HB1  1 
ATOM   942  H HB2  A ALA   A 1 38  ? 21.084 -1.017  1.057   0.86 15.64 ?  38  ALA   A HB2  1 
ATOM   943  H HB2  B ALA   A 1 38  ? 21.218 -1.554  1.020   0.14 14.09 ?  38  ALA   A HB2  1 
ATOM   944  H HB3  A ALA   A 1 38  ? 21.410 0.523   0.846   0.86 15.64 ?  38  ALA   A HB3  1 
ATOM   945  H HB3  B ALA   A 1 38  ? 21.237 0.031   0.899   0.14 14.09 ?  38  ALA   A HB3  1 
ATOM   946  N N    A ALA   A 1 39  ? 25.277 -0.040  0.066   0.86 10.77 ?  39  ALA   A N    1 
ATOM   947  N N    B ALA   A 1 39  ? 25.160 0.043   -0.074  0.14 10.98 ?  39  ALA   A N    1 
ATOM   948  C CA   A ALA   A 1 39  ? 26.322 0.841   -0.421  0.86 10.57 ?  39  ALA   A CA   1 
ATOM   949  C CA   B ALA   A 1 39  ? 26.073 1.052   -0.588  0.14 11.26 ?  39  ALA   A CA   1 
ATOM   950  C C    A ALA   A 1 39  ? 26.438 0.790   -1.937  0.86 10.53 ?  39  ALA   A C    1 
ATOM   951  C C    B ALA   A 1 39  ? 26.342 0.852   -2.076  0.14 11.41 ?  39  ALA   A C    1 
ATOM   952  O O    A ALA   A 1 39  ? 25.944 -0.123  -2.601  0.86 11.28 ?  39  ALA   A O    1 
ATOM   953  O O    B ALA   A 1 39  ? 25.958 -0.151  -2.682  0.14 11.57 ?  39  ALA   A O    1 
ATOM   954  C CB   A ALA   A 1 39  ? 27.649 0.439   0.218   0.86 11.48 ?  39  ALA   A CB   1 
ATOM   955  C CB   B ALA   A 1 39  ? 27.389 1.010   0.192   0.14 11.41 ?  39  ALA   A CB   1 
ATOM   956  H H    A ALA   A 1 39  ? 25.553 -0.836  0.252   0.86 12.93 ?  39  ALA   A H    1 
ATOM   957  H H    B ALA   A 1 39  ? 25.525 -0.727  0.049   0.14 13.18 ?  39  ALA   A H    1 
ATOM   958  H HA   A ALA   A 1 39  ? 26.113 1.751   -0.159  0.86 12.70 ?  39  ALA   A HA   1 
ATOM   959  H HA   B ALA   A 1 39  ? 25.674 1.926   -0.456  0.14 13.52 ?  39  ALA   A HA   1 
ATOM   960  H HB1  A ALA   A 1 39  ? 28.342 1.035   -0.108  0.86 13.79 ?  39  ALA   A HB1  1 
ATOM   961  H HB1  B ALA   A 1 39  ? 27.975 1.703   -0.150  0.14 13.70 ?  39  ALA   A HB1  1 
ATOM   962  H HB2  A ALA   A 1 39  ? 27.571 0.522   1.183   0.86 13.79 ?  39  ALA   A HB2  1 
ATOM   963  H HB2  B ALA   A 1 39  ? 27.204 1.163   1.131   0.14 13.70 ?  39  ALA   A HB2  1 
ATOM   964  H HB3  A ALA   A 1 39  ? 27.852 -0.474  -0.023  0.86 13.79 ?  39  ALA   A HB3  1 
ATOM   965  H HB3  B ALA   A 1 39  ? 27.797 0.139   0.072   0.14 13.70 ?  39  ALA   A HB3  1 
ATOM   966  N N    A ASN   A 1 40  ? 27.123 1.793   -2.482  0.86 11.09 ?  40  ASN   A N    1 
ATOM   967  N N    B ASN   A 1 40  ? 27.014 1.839   -2.663  0.14 11.56 ?  40  ASN   A N    1 
ATOM   968  C CA   A ASN   A 1 40  ? 27.643 1.744   -3.841  0.86 11.15 ?  40  ASN   A CA   1 
ATOM   969  C CA   B ASN   A 1 40  ? 27.522 1.766   -4.024  0.14 11.66 ?  40  ASN   A CA   1 
ATOM   970  C C    A ASN   A 1 40  ? 29.166 1.630   -3.783  0.86 10.47 ?  40  ASN   A C    1 
ATOM   971  C C    B ASN   A 1 40  ? 29.039 1.601   -3.983  0.14 11.72 ?  40  ASN   A C    1 
ATOM   972  O O    A ASN   A 1 40  ? 29.766 1.732   -2.711  0.86 10.92 ?  40  ASN   A O    1 
ATOM   973  O O    B ASN   A 1 40  ? 29.664 1.643   -2.921  0.14 11.70 ?  40  ASN   A O    1 
ATOM   974  C CB   A ASN   A 1 40  ? 27.152 2.929   -4.687  0.86 12.16 ?  40  ASN   A CB   1 
ATOM   975  C CB   B ASN   A 1 40  ? 27.101 2.995   -4.835  0.14 11.74 ?  40  ASN   A CB   1 
ATOM   976  C CG   A ASN   A 1 40  ? 27.532 4.269   -4.110  0.86 13.66 ?  40  ASN   A CG   1 
ATOM   977  C CG   B ASN   A 1 40  ? 27.479 4.298   -4.164  0.14 11.84 ?  40  ASN   A CG   1 
ATOM   978  O OD1  A ASN   A 1 40  ? 28.708 4.542   -3.848  0.86 14.67 ?  40  ASN   A OD1  1 
ATOM   979  O OD1  B ASN   A 1 40  ? 28.620 4.489   -3.740  0.14 12.25 ?  40  ASN   A OD1  1 
ATOM   980  N ND2  A ASN   A 1 40  ? 26.531 5.127   -3.917  0.86 14.52 ?  40  ASN   A ND2  1 
ATOM   981  N ND2  B ASN   A 1 40  ? 26.513 5.205   -4.057  0.14 11.87 ?  40  ASN   A ND2  1 
ATOM   982  H H    A ASN   A 1 40  ? 27.307 2.525   -2.073  0.86 13.31 ?  40  ASN   A H    1 
ATOM   983  H H    B ASN   A 1 40  ? 27.194 2.583   -2.271  0.14 13.88 ?  40  ASN   A H    1 
ATOM   984  H HA   A ASN   A 1 40  ? 27.315 0.936   -4.266  0.86 13.38 ?  40  ASN   A HA   1 
ATOM   985  H HA   B ASN   A 1 40  ? 27.140 0.985   -4.457  0.14 14.00 ?  40  ASN   A HA   1 
ATOM   986  H HB2  A ASN   A 1 40  ? 27.537 2.861   -5.578  0.86 14.60 ?  40  ASN   A HB2  1 
ATOM   987  H HB2  B ASN   A 1 40  ? 27.540 2.965   -5.701  0.14 14.09 ?  40  ASN   A HB2  1 
ATOM   988  H HB3  A ASN   A 1 40  ? 26.184 2.891   -4.749  0.86 14.60 ?  40  ASN   A HB3  1 
ATOM   989  H HB3  B ASN   A 1 40  ? 26.139 2.985   -4.954  0.14 14.09 ?  40  ASN   A HB3  1 
ATOM   990  H HD21 A ASN   A 1 40  ? 26.692 5.912   -3.595  0.86 17.43 ?  40  ASN   A HD21 1 
ATOM   991  H HD21 B ASN   A 1 40  ? 26.673 5.963   -3.683  0.14 14.26 ?  40  ASN   A HD21 1 
ATOM   992  H HD22 A ASN   A 1 40  ? 25.725 4.906   -4.114  0.86 17.43 ?  40  ASN   A HD22 1 
ATOM   993  H HD22 B ASN   A 1 40  ? 25.727 5.033   -4.361  0.14 14.26 ?  40  ASN   A HD22 1 
ATOM   994  N N    A VAL   A 1 41  ? 29.780 1.391   -4.945  0.86 10.98 ?  41  VAL   A N    1 
ATOM   995  N N    B VAL   A 1 41  ? 29.636 1.417   -5.162  0.14 12.02 ?  41  VAL   A N    1 
ATOM   996  C CA   A VAL   A 1 41  ? 31.207 1.079   -4.979  0.86 12.03 ?  41  VAL   A CA   1 
ATOM   997  C CA   B VAL   A 1 41  ? 31.052 1.063   -5.216  0.14 12.10 ?  41  VAL   A CA   1 
ATOM   998  C C    A VAL   A 1 41  ? 32.069 2.229   -4.506  0.86 11.99 ?  41  VAL   A C    1 
ATOM   999  C C    B VAL   A 1 41  ? 31.942 2.195   -4.715  0.14 12.08 ?  41  VAL   A C    1 
ATOM   1000 O O    A VAL   A 1 41  ? 33.215 2.009   -4.106  0.86 12.52 ?  41  VAL   A O    1 
ATOM   1001 O O    B VAL   A 1 41  ? 33.066 1.949   -4.261  0.14 11.88 ?  41  VAL   A O    1 
ATOM   1002 C CB   A VAL   A 1 41  ? 31.686 0.606   -6.369  0.86 12.77 ?  41  VAL   A CB   1 
ATOM   1003 C CB   B VAL   A 1 41  ? 31.454 0.595   -6.626  0.14 12.42 ?  41  VAL   A CB   1 
ATOM   1004 C CG1  A VAL   A 1 41  ? 31.009 -0.689  -6.762  0.86 13.70 ?  41  VAL   A CG1  1 
ATOM   1005 C CG1  B VAL   A 1 41  ? 30.702 -0.671  -6.991  0.14 12.83 ?  41  VAL   A CG1  1 
ATOM   1006 C CG2  A VAL   A 1 41  ? 31.494 1.683   -7.430  0.86 14.06 ?  41  VAL   A CG2  1 
ATOM   1007 C CG2  B VAL   A 1 41  ? 31.205 1.690   -7.649  0.14 12.55 ?  41  VAL   A CG2  1 
ATOM   1008 H H    A VAL   A 1 41  ? 29.396 1.396   -5.717  0.86 13.18 ?  41  VAL   A H    1 
ATOM   1009 H H    B VAL   A 1 41  ? 29.243 1.484   -5.923  0.14 14.43 ?  41  VAL   A H    1 
ATOM   1010 H HA   A VAL   A 1 41  ? 31.365 0.342   -4.368  0.86 14.45 ?  41  VAL   A HA   1 
ATOM   1011 H HA   B VAL   A 1 41  ? 31.190 0.313   -4.619  0.14 14.53 ?  41  VAL   A HA   1 
ATOM   1012 H HB   A VAL   A 1 41  ? 32.639 0.421   -6.319  0.86 15.34 ?  41  VAL   A HB   1 
ATOM   1013 H HB   B VAL   A 1 41  ? 32.402 0.389   -6.626  0.14 14.91 ?  41  VAL   A HB   1 
ATOM   1014 H HG11 A VAL   A 1 41  ? 31.345 -0.975  -7.626  0.86 16.45 ?  41  VAL   A HG11 1 
ATOM   1015 H HG11 B VAL   A 1 41  ? 30.934 -0.921  -7.896  0.14 15.40 ?  41  VAL   A HG11 1 
ATOM   1016 H HG12 A VAL   A 1 41  ? 31.200 -1.363  -6.092  0.86 16.45 ?  41  VAL   A HG12 1 
ATOM   1017 H HG12 B VAL   A 1 41  ? 30.956 -1.376  -6.375  0.14 15.40 ?  41  VAL   A HG12 1 
ATOM   1018 H HG13 A VAL   A 1 41  ? 30.050 -0.538  -6.815  0.86 16.45 ?  41  VAL   A HG13 1 
ATOM   1019 H HG13 B VAL   A 1 41  ? 29.750 -0.503  -6.926  0.14 15.40 ?  41  VAL   A HG13 1 
ATOM   1020 H HG21 A VAL   A 1 41  ? 31.730 1.317   -8.298  0.86 16.88 ?  41  VAL   A HG21 1 
ATOM   1021 H HG21 B VAL   A 1 41  ? 31.483 1.369   -8.520  0.14 15.06 ?  41  VAL   A HG21 1 
ATOM   1022 H HG22 A VAL   A 1 41  ? 30.567 1.962   -7.431  0.86 16.88 ?  41  VAL   A HG22 1 
ATOM   1023 H HG22 B VAL   A 1 41  ? 30.261 1.905   -7.660  0.14 15.06 ?  41  VAL   A HG22 1 
ATOM   1024 H HG23 A VAL   A 1 41  ? 32.069 2.436   -7.224  0.86 16.88 ?  41  VAL   A HG23 1 
ATOM   1025 H HG23 B VAL   A 1 41  ? 31.723 2.472   -7.405  0.14 15.06 ?  41  VAL   A HG23 1 
ATOM   1026 N N    A TYR   A 1 42  ? 31.558 3.455   -4.568  0.86 11.75 ?  42  TYR   A N    1 
ATOM   1027 N N    B TYR   A 1 42  ? 31.477 3.440   -4.788  0.14 12.41 ?  42  TYR   A N    1 
ATOM   1028 C CA   A TYR   A 1 42  ? 32.291 4.643   -4.156  0.86 11.91 ?  42  TYR   A CA   1 
ATOM   1029 C CA   B TYR   A 1 42  ? 32.275 4.576   -4.346  0.14 12.60 ?  42  TYR   A CA   1 
ATOM   1030 C C    A TYR   A 1 42  ? 32.037 5.007   -2.705  0.86 11.66 ?  42  TYR   A C    1 
ATOM   1031 C C    B TYR   A 1 42  ? 31.986 4.984   -2.908  0.14 12.37 ?  42  TYR   A C    1 
ATOM   1032 O O    A TYR   A 1 42  ? 32.601 5.995   -2.216  0.86 12.30 ?  42  TYR   A O    1 
ATOM   1033 O O    B TYR   A 1 42  ? 32.539 5.987   -2.443  0.14 12.40 ?  42  TYR   A O    1 
ATOM   1034 C CB   A TYR   A 1 42  ? 31.938 5.828   -5.071  0.86 13.28 ?  42  TYR   A CB   1 
ATOM   1035 C CB   B TYR   A 1 42  ? 32.066 5.774   -5.277  0.14 13.11 ?  42  TYR   A CB   1 
ATOM   1036 C CG   A TYR   A 1 42  ? 32.108 5.517   -6.546  0.86 14.31 ?  42  TYR   A CG   1 
ATOM   1037 C CG   B TYR   A 1 42  ? 32.336 5.453   -6.725  0.14 13.55 ?  42  TYR   A CG   1 
ATOM   1038 C CD1  A TYR   A 1 42  ? 33.363 5.317   -7.096  0.86 14.96 ?  42  TYR   A CD1  1 
ATOM   1039 C CD1  B TYR   A 1 42  ? 33.635 5.333   -7.201  0.14 13.98 ?  42  TYR   A CD1  1 
ATOM   1040 C CD2  A TYR   A 1 42  ? 31.008 5.405   -7.382  0.86 15.52 ?  42  TYR   A CD2  1 
ATOM   1041 C CD2  B TYR   A 1 42  ? 31.292 5.260   -7.616  0.14 13.72 ?  42  TYR   A CD2  1 
ATOM   1042 C CE1  A TYR   A 1 42  ? 33.518 5.019   -8.442  0.86 15.56 ?  42  TYR   A CE1  1 
ATOM   1043 C CE1  B TYR   A 1 42  ? 33.885 5.034   -8.527  0.14 14.24 ?  42  TYR   A CE1  1 
ATOM   1044 C CE2  A TYR   A 1 42  ? 31.156 5.117   -8.729  0.86 16.55 ?  42  TYR   A CE2  1 
ATOM   1045 C CE2  B TYR   A 1 42  ? 31.531 4.961   -8.942  0.14 13.94 ?  42  TYR   A CE2  1 
ATOM   1046 C CZ   A TYR   A 1 42  ? 32.413 4.922   -9.254  0.86 16.38 ?  42  TYR   A CZ   1 
ATOM   1047 C CZ   B TYR   A 1 42  ? 32.828 4.849   -9.393  0.14 14.19 ?  42  TYR   A CZ   1 
ATOM   1048 O OH   A TYR   A 1 42  ? 32.555 4.631   -10.592 0.86 18.14 ?  42  TYR   A OH   1 
ATOM   1049 O OH   B TYR   A 1 42  ? 33.062 4.551   -10.716 0.14 14.58 ?  42  TYR   A OH   1 
ATOM   1050 H H    A TYR   A 1 42  ? 30.769 3.629   -4.857  0.86 14.11 ?  42  TYR   A H    1 
ATOM   1051 H H    B TYR   A 1 42  ? 30.698 3.653   -5.091  0.14 14.90 ?  42  TYR   A H    1 
ATOM   1052 H HA   A TYR   A 1 42  ? 33.243 4.476   -4.255  0.86 14.31 ?  42  TYR   A HA   1 
ATOM   1053 H HA   B TYR   A 1 42  ? 33.210 4.330   -4.400  0.14 15.13 ?  42  TYR   A HA   1 
ATOM   1054 H HB2  A TYR   A 1 42  ? 31.010 6.078   -4.924  0.86 15.94 ?  42  TYR   A HB2  1 
ATOM   1055 H HB2  B TYR   A 1 42  ? 31.148 6.074   -5.204  0.14 15.75 ?  42  TYR   A HB2  1 
ATOM   1056 H HB3  A TYR   A 1 42  ? 32.516 6.581   -4.857  0.86 15.94 ?  42  TYR   A HB3  1 
ATOM   1057 H HB3  B TYR   A 1 42  ? 32.670 6.486   -5.010  0.14 15.75 ?  42  TYR   A HB3  1 
ATOM   1058 H HD1  A TYR   A 1 42  ? 34.116 5.380   -6.552  0.86 17.96 ?  42  TYR   A HD1  1 
ATOM   1059 H HD1  B TYR   A 1 42  ? 34.350 5.456   -6.616  0.14 16.78 ?  42  TYR   A HD1  1 
ATOM   1060 H HD2  A TYR   A 1 42  ? 30.156 5.542   -7.034  0.86 18.64 ?  42  TYR   A HD2  1 
ATOM   1061 H HD2  B TYR   A 1 42  ? 30.416 5.336   -7.314  0.14 16.47 ?  42  TYR   A HD2  1 
ATOM   1062 H HE1  A TYR   A 1 42  ? 34.370 4.886   -8.797  0.86 18.68 ?  42  TYR   A HE1  1 
ATOM   1063 H HE1  B TYR   A 1 42  ? 34.761 4.958   -8.831  0.14 17.10 ?  42  TYR   A HE1  1 
ATOM   1064 H HE2  A TYR   A 1 42  ? 30.406 5.050   -9.276  0.86 19.87 ?  42  TYR   A HE2  1 
ATOM   1065 H HE2  B TYR   A 1 42  ? 30.820 4.838   -9.526  0.14 16.74 ?  42  TYR   A HE2  1 
ATOM   1066 H HH   A TYR   A 1 42  ? 33.371 4.529   -10.779 0.86 21.78 ?  42  TYR   A HH   1 
ATOM   1067 H HH   B TYR   A 1 42  ? 32.329 4.467   -11.119 0.14 17.51 ?  42  TYR   A HH   1 
ATOM   1068 N N    A LEU   A 1 43  ? 31.179 4.250   -2.021  0.86 11.11 ?  43  LEU   A N    1 
ATOM   1069 N N    B LEU   A 1 43  ? 31.136 4.238   -2.202  0.14 12.52 ?  43  LEU   A N    1 
ATOM   1070 C CA   A LEU   A 1 43  ? 30.729 4.582   -0.671  0.86 11.09 ?  43  LEU   A CA   1 
ATOM   1071 C CA   B LEU   A 1 43  ? 30.772 4.546   -0.819  0.14 12.77 ?  43  LEU   A CA   1 
ATOM   1072 C C    A LEU   A 1 43  ? 30.258 6.032   -0.576  0.86 11.05 ?  43  LEU   A C    1 
ATOM   1073 C C    B LEU   A 1 43  ? 30.297 5.990   -0.675  0.14 13.32 ?  43  LEU   A C    1 
ATOM   1074 O O    A LEU   A 1 43  ? 30.515 6.729   0.407   0.86 12.21 ?  43  LEU   A O    1 
ATOM   1075 O O    B LEU   A 1 43  ? 30.617 6.681   0.293   0.14 13.38 ?  43  LEU   A O    1 
ATOM   1076 C CB   A LEU   A 1 43  ? 31.778 4.265   0.393   0.86 11.44 ?  43  LEU   A CB   1 
ATOM   1077 C CB   B LEU   A 1 43  ? 31.903 4.226   0.161   0.14 12.78 ?  43  LEU   A CB   1 
ATOM   1078 C CG   A LEU   A 1 43  ? 32.289 2.822   0.458   0.86 11.66 ?  43  LEU   A CG   1 
ATOM   1079 C CG   B LEU   A 1 43  ? 32.235 2.745   0.363   0.14 12.69 ?  43  LEU   A CG   1 
ATOM   1080 C CD1  A LEU   A 1 43  ? 33.332 2.701   1.551   0.86 13.00 ?  43  LEU   A CD1  1 
ATOM   1081 C CD1  B LEU   A 1 43  ? 33.294 2.582   1.441   0.14 12.84 ?  43  LEU   A CD1  1 
ATOM   1082 C CD2  A LEU   A 1 43  ? 31.164 1.821   0.678   0.86 12.25 ?  43  LEU   A CD2  1 
ATOM   1083 C CD2  B LEU   A 1 43  ? 30.986 1.943   0.710   0.14 12.64 ?  43  LEU   A CD2  1 
ATOM   1084 H H    A LEU   A 1 43  ? 30.834 3.519   -2.325  0.86 13.34 ?  43  LEU   A H    1 
ATOM   1085 H H    B LEU   A 1 43  ? 30.741 3.541   -2.510  0.14 15.04 ?  43  LEU   A H    1 
ATOM   1086 H HA   A LEU   A 1 43  ? 29.955 4.023   -0.476  0.86 13.31 ?  43  LEU   A HA   1 
ATOM   1087 H HA   B LEU   A 1 43  ? 30.022 3.981   -0.582  0.14 15.34 ?  43  LEU   A HA   1 
ATOM   1088 H HB2  A LEU   A 1 43  ? 32.543 4.835   0.241   0.86 13.73 ?  43  LEU   A HB2  1 
ATOM   1089 H HB2  B LEU   A 1 43  ? 32.711 4.664   -0.146  0.14 15.34 ?  43  LEU   A HB2  1 
ATOM   1090 H HB3  A LEU   A 1 43  ? 31.391 4.467   1.261   0.86 13.73 ?  43  LEU   A HB3  1 
ATOM   1091 H HB3  B LEU   A 1 43  ? 31.655 4.579   1.030   0.14 15.34 ?  43  LEU   A HB3  1 
ATOM   1092 H HG   A LEU   A 1 43  ? 32.719 2.604   -0.384  0.86 14.00 ?  43  LEU   A HG   1 
ATOM   1093 H HG   B LEU   A 1 43  ? 32.596 2.390   -0.463  0.14 15.23 ?  43  LEU   A HG   1 
ATOM   1094 H HD11 A LEU   A 1 43  ? 33.650 1.784   1.584   0.86 15.61 ?  43  LEU   A HD11 1 
ATOM   1095 H HD11 B LEU   A 1 43  ? 33.494 1.638   1.547   0.14 15.42 ?  43  LEU   A HD11 1 
ATOM   1096 H HD12 A LEU   A 1 43  ? 34.067 3.300   1.355   0.86 15.61 ?  43  LEU   A HD12 1 
ATOM   1097 H HD12 B LEU   A 1 43  ? 34.093 3.061   1.175   0.14 15.42 ?  43  LEU   A HD12 1 
ATOM   1098 H HD13 A LEU   A 1 43  ? 32.927 2.938   2.401   0.86 15.61 ?  43  LEU   A HD13 1 
ATOM   1099 H HD13 B LEU   A 1 43  ? 32.954 2.942   2.276   0.14 15.42 ?  43  LEU   A HD13 1 
ATOM   1100 H HD21 A LEU   A 1 43  ? 31.549 0.934   0.788   0.86 14.71 ?  43  LEU   A HD21 1 
ATOM   1101 H HD21 B LEU   A 1 43  ? 31.251 1.077   1.054   0.14 15.18 ?  43  LEU   A HD21 1 
ATOM   1102 H HD22 A LEU   A 1 43  ? 30.673 2.068   1.475   0.86 14.71 ?  43  LEU   A HD22 1 
ATOM   1103 H HD22 B LEU   A 1 43  ? 30.478 2.426   1.381   0.14 15.18 ?  43  LEU   A HD22 1 
ATOM   1104 H HD23 A LEU   A 1 43  ? 30.577 1.831   -0.093  0.86 14.71 ?  43  LEU   A HD23 1 
ATOM   1105 H HD23 B LEU   A 1 43  ? 30.450 1.831   -0.092  0.14 15.18 ?  43  LEU   A HD23 1 
ATOM   1106 N N    A LYS   A 1 44  ? 29.526 6.475   -1.600  0.86 11.23 ?  44  LYS   A N    1 
ATOM   1107 N N    B LYS   A 1 44  ? 29.523 6.447   -1.655  0.14 13.95 ?  44  LYS   A N    1 
ATOM   1108 C CA   A LYS   A 1 44  ? 28.886 7.788   -1.599  0.86 11.92 ?  44  LYS   A CA   1 
ATOM   1109 C CA   B LYS   A 1 44  ? 28.875 7.752   -1.606  0.14 14.70 ?  44  LYS   A CA   1 
ATOM   1110 C C    A LYS   A 1 44  ? 27.465 7.598   -1.092  0.86 10.93 ?  44  LYS   A C    1 
ATOM   1111 C C    B LYS   A 1 44  ? 27.448 7.548   -1.114  0.14 13.77 ?  44  LYS   A C    1 
ATOM   1112 O O    A LYS   A 1 44  ? 26.598 7.083   -1.806  0.86 12.33 ?  44  LYS   A O    1 
ATOM   1113 O O    B LYS   A 1 44  ? 26.599 7.027   -1.844  0.14 13.85 ?  44  LYS   A O    1 
ATOM   1114 C CB   A LYS   A 1 44  ? 28.919 8.399   -2.993  0.86 14.26 ?  44  LYS   A CB   1 
ATOM   1115 C CB   B LYS   A 1 44  ? 28.900 8.421   -2.978  0.14 16.49 ?  44  LYS   A CB   1 
ATOM   1116 C CG   A LYS   A 1 44  ? 30.296 8.875   -3.431  0.86 18.07 ?  44  LYS   A CG   1 
ATOM   1117 C CG   B LYS   A 1 44  ? 30.273 8.936   -3.383  0.14 18.27 ?  44  LYS   A CG   1 
ATOM   1118 C CD   A LYS   A 1 44  ? 30.949 9.814   -2.415  0.86 23.40 ?  44  LYS   A CD   1 
ATOM   1119 C CD   B LYS   A 1 44  ? 30.832 9.900   -2.343  0.14 20.04 ?  44  LYS   A CD   1 
ATOM   1120 C CE   A LYS   A 1 44  ? 32.285 10.326  -2.915  0.86 26.49 ?  44  LYS   A CE   1 
ATOM   1121 C CE   B LYS   A 1 44  ? 32.118 10.550  -2.814  0.14 21.17 ?  44  LYS   A CE   1 
ATOM   1122 N NZ   A LYS   A 1 44  ? 33.116 10.900  -1.821  0.86 28.12 ?  44  LYS   A NZ   1 
ATOM   1123 N NZ   B LYS   A 1 44  ? 32.658 11.504  -1.808  0.14 21.80 ?  44  LYS   A NZ   1 
ATOM   1124 H H    A LYS   A 1 44  ? 29.380 6.023   -2.319  0.86 13.48 ?  44  LYS   A H    1 
ATOM   1125 H H    B LYS   A 1 44  ? 29.359 6.011   -2.377  0.14 16.75 ?  44  LYS   A H    1 
ATOM   1126 H HA   A LYS   A 1 44  ? 29.345 8.374   -0.976  0.86 14.31 ?  44  LYS   A HA   1 
ATOM   1127 H HA   B LYS   A 1 44  ? 29.328 8.316   -0.962  0.14 17.65 ?  44  LYS   A HA   1 
ATOM   1128 H HB2  A LYS   A 1 44  ? 28.616 7.734   -3.632  0.86 17.12 ?  44  LYS   A HB2  1 
ATOM   1129 H HB2  B LYS   A 1 44  ? 28.616 7.776   -3.645  0.14 19.80 ?  44  LYS   A HB2  1 
ATOM   1130 H HB3  A LYS   A 1 44  ? 28.320 9.164   -3.012  0.86 17.12 ?  44  LYS   A HB3  1 
ATOM   1131 H HB3  B LYS   A 1 44  ? 28.291 9.176   -2.970  0.14 19.80 ?  44  LYS   A HB3  1 
ATOM   1132 H HG2  A LYS   A 1 44  ? 30.873 8.107   -3.551  0.86 21.69 ?  44  LYS   A HG2  1 
ATOM   1133 H HG2  B LYS   A 1 44  ? 30.883 8.187   -3.467  0.14 21.94 ?  44  LYS   A HG2  1 
ATOM   1134 H HG3  A LYS   A 1 44  ? 30.209 9.359   -4.272  0.86 21.69 ?  44  LYS   A HG3  1 
ATOM   1135 H HG3  B LYS   A 1 44  ? 30.200 9.408   -4.228  0.14 21.94 ?  44  LYS   A HG3  1 
ATOM   1136 H HD2  A LYS   A 1 44  ? 30.357 10.566  -2.253  0.86 28.09 ?  44  LYS   A HD2  1 
ATOM   1137 H HD2  B LYS   A 1 44  ? 30.177 10.594  -2.166  0.14 24.06 ?  44  LYS   A HD2  1 
ATOM   1138 H HD3  A LYS   A 1 44  ? 31.106 9.326   -1.589  0.86 28.09 ?  44  LYS   A HD3  1 
ATOM   1139 H HD3  B LYS   A 1 44  ? 31.031 9.412   -1.527  0.14 24.06 ?  44  LYS   A HD3  1 
ATOM   1140 H HE2  A LYS   A 1 44  ? 32.777 9.590   -3.312  0.86 31.80 ?  44  LYS   A HE2  1 
ATOM   1141 H HE2  B LYS   A 1 44  ? 32.784 9.859   -2.967  0.14 25.41 ?  44  LYS   A HE2  1 
ATOM   1142 H HE3  A LYS   A 1 44  ? 32.130 11.018  -3.574  0.86 31.80 ?  44  LYS   A HE3  1 
ATOM   1143 H HE3  B LYS   A 1 44  ? 31.945 11.036  -3.634  0.14 25.41 ?  44  LYS   A HE3  1 
ATOM   1144 H HZ1  A LYS   A 1 44  ? 33.889 11.191  -2.149  0.86 33.75 ?  44  LYS   A HZ1  1 
ATOM   1145 H HZ1  B LYS   A 1 44  ? 33.411 11.868  -2.110  0.14 26.17 ?  44  LYS   A HZ1  1 
ATOM   1146 H HZ2  A LYS   A 1 44  ? 32.686 11.583  -1.442  0.86 33.75 ?  44  LYS   A HZ2  1 
ATOM   1147 H HZ2  B LYS   A 1 44  ? 32.065 12.149  -1.653  0.14 26.17 ?  44  LYS   A HZ2  1 
ATOM   1148 H HZ3  A LYS   A 1 44  ? 33.276 10.282  -1.203  0.86 33.75 ?  44  LYS   A HZ3  1 
ATOM   1149 H HZ3  B LYS   A 1 44  ? 32.829 11.077  -1.045  0.14 26.17 ?  44  LYS   A HZ3  1 
ATOM   1150 N N    A HIS   A 1 45  ? 27.233 7.987   0.156   0.86 10.69 ?  45  HIS   A N    1 
ATOM   1151 N N    B HIS   A 1 45  ? 27.192 7.961   0.124   0.14 13.02 ?  45  HIS   A N    1 
ATOM   1152 C CA   A HIS   A 1 45  ? 25.996 7.636   0.850   0.86 10.89 ?  45  HIS   A CA   1 
ATOM   1153 C CA   B HIS   A 1 45  ? 25.915 7.705   0.787   0.14 12.34 ?  45  HIS   A CA   1 
ATOM   1154 C C    A HIS   A 1 45  ? 24.969 8.758   0.700   0.86 11.75 ?  45  HIS   A C    1 
ATOM   1155 C C    B HIS   A 1 45  ? 25.007 8.899   0.530   0.14 12.23 ?  45  HIS   A C    1 
ATOM   1156 O O    A HIS   A 1 45  ? 24.624 9.468   1.645   0.86 12.77 ?  45  HIS   A O    1 
ATOM   1157 O O    B HIS   A 1 45  ? 25.021 9.890   1.262   0.14 12.33 ?  45  HIS   A O    1 
ATOM   1158 C CB   A HIS   A 1 45  ? 26.293 7.363   2.310   0.86 11.04 ?  45  HIS   A CB   1 
ATOM   1159 C CB   B HIS   A 1 45  ? 26.140 7.462   2.273   0.14 11.74 ?  45  HIS   A CB   1 
ATOM   1160 C CG   A HIS   A 1 45  ? 27.410 6.396   2.525   0.86 10.83 ?  45  HIS   A CG   1 
ATOM   1161 C CG   B HIS   A 1 45  ? 27.288 6.547   2.560   0.14 11.05 ?  45  HIS   A CG   1 
ATOM   1162 N ND1  A HIS   A 1 45  ? 27.393 5.108   2.031   0.86 11.34 ?  45  HIS   A ND1  1 
ATOM   1163 N ND1  B HIS   A 1 45  ? 27.362 5.266   2.055   0.14 10.93 ?  45  HIS   A ND1  1 
ATOM   1164 C CD2  A HIS   A 1 45  ? 28.583 6.543   3.184   0.86 11.26 ?  45  HIS   A CD2  1 
ATOM   1165 C CD2  B HIS   A 1 45  ? 28.413 6.731   3.290   0.14 10.58 ?  45  HIS   A CD2  1 
ATOM   1166 C CE1  A HIS   A 1 45  ? 28.515 4.506   2.385   0.86 11.09 ?  45  HIS   A CE1  1 
ATOM   1167 C CE1  B HIS   A 1 45  ? 28.482 4.699   2.467   0.14 10.48 ?  45  HIS   A CE1  1 
ATOM   1168 N NE2  A HIS   A 1 45  ? 29.255 5.353   3.082   0.86 11.33 ?  45  HIS   A NE2  1 
ATOM   1169 N NE2  B HIS   A 1 45  ? 29.138 5.566   3.218   0.14 10.42 ?  45  HIS   A NE2  1 
ATOM   1170 H H    A HIS   A 1 45  ? 27.776 8.463   0.627   0.86 12.83 ?  45  HIS   A H    1 
ATOM   1171 H H    B HIS   A 1 45  ? 27.748 8.405   0.607   0.14 15.63 ?  45  HIS   A H    1 
ATOM   1172 H HA   A HIS   A 1 45  ? 25.629 6.827   0.459   0.86 13.08 ?  45  HIS   A HA   1 
ATOM   1173 H HA   B HIS   A 1 45  ? 25.505 6.916   0.407   0.14 14.82 ?  45  HIS   A HA   1 
ATOM   1174 H HB2  A HIS   A 1 45  ? 26.526 8.197   2.747   0.86 13.26 ?  45  HIS   A HB2  1 
ATOM   1175 H HB2  B HIS   A 1 45  ? 26.321 8.310   2.709   0.14 14.10 ?  45  HIS   A HB2  1 
ATOM   1176 H HB3  A HIS   A 1 45  ? 25.494 6.991   2.727   0.86 13.26 ?  45  HIS   A HB3  1 
ATOM   1177 H HB3  B HIS   A 1 45  ? 25.340 7.063   2.652   0.14 14.10 ?  45  HIS   A HB3  1 
ATOM   1178 H HD2  A HIS   A 1 45  ? 28.887 7.315   3.618   0.86 13.52 ?  45  HIS   A HD2  1 
ATOM   1179 H HD2  B HIS   A 1 45  ? 28.649 7.503   3.756   0.14 12.71 ?  45  HIS   A HD2  1 
ATOM   1180 H HE1  A HIS   A 1 45  ? 28.740 3.628   2.191   0.86 13.31 ?  45  HIS   A HE1  1 
ATOM   1181 H HE1  B HIS   A 1 45  ? 28.761 3.837   2.265   0.14 12.58 ?  45  HIS   A HE1  1 
ATOM   1182 H HE2  A HIS   A 1 45  ? 30.031 5.183   3.417   0.86 13.61 ?  45  HIS   A HE2  1 
ATOM   1183 H HE2  B HIS   A 1 45  ? 29.895 5.427   3.600   0.14 12.51 ?  45  HIS   A HE2  1 
ATOM   1184 N N    A GLY   A 1 46  ? 24.465 8.901   -0.518  0.86 13.42 ?  46  GLY   A N    1 
ATOM   1185 N N    B GLY   A 1 46  ? 24.213 8.806   -0.533  0.14 12.15 ?  46  GLY   A N    1 
ATOM   1186 C CA   A GLY   A 1 46  ? 23.659 10.062  -0.842  0.86 14.02 ?  46  GLY   A CA   1 
ATOM   1187 C CA   B GLY   A 1 46  ? 23.349 9.901   -0.925  0.14 11.78 ?  46  GLY   A CA   1 
ATOM   1188 C C    A GLY   A 1 46  ? 22.176 9.926   -0.585  0.86 13.88 ?  46  GLY   A C    1 
ATOM   1189 C C    B GLY   A 1 46  ? 21.908 9.739   -0.494  0.14 11.55 ?  46  GLY   A C    1 
ATOM   1190 O O    A GLY   A 1 46  ? 21.501 10.920  -0.298  0.86 15.26 ?  46  GLY   A O    1 
ATOM   1191 O O    B GLY   A 1 46  ? 21.296 10.694  -0.005  0.14 11.80 ?  46  GLY   A O    1 
ATOM   1192 H H    A GLY   A 1 46  ? 24.560 8.339   -1.162  0.86 16.11 ?  46  GLY   A H    1 
ATOM   1193 H H    B GLY   A 1 46  ? 24.161 8.118   -1.048  0.14 14.59 ?  46  GLY   A H    1 
ATOM   1194 H HA2  A GLY   A 1 46  ? 23.977 10.818  -0.325  0.86 16.84 ?  46  GLY   A HA2  1 
ATOM   1195 H HA2  B GLY   A 1 46  ? 23.674 10.725  -0.538  0.14 14.15 ?  46  GLY   A HA2  1 
ATOM   1196 H HA3  A GLY   A 1 46  ? 23.771 10.270  -1.779  0.86 16.84 ?  46  GLY   A HA3  1 
ATOM   1197 H HA3  B GLY   A 1 46  ? 23.362 9.990   -1.889  0.14 14.15 ?  46  GLY   A HA3  1 
ATOM   1198 N N    A GLY   A 1 47  ? 21.648 8.718   -0.723  0.86 14.06 ?  47  GLY   A N    1 
ATOM   1199 N N    B GLY   A 1 47  ? 21.352 8.542   -0.663  0.14 11.42 ?  47  GLY   A N    1 
ATOM   1200 C CA   A GLY   A 1 47  ? 20.213 8.528   -0.686  0.86 14.37 ?  47  GLY   A CA   1 
ATOM   1201 C CA   B GLY   A 1 47  ? 19.940 8.337   -0.428  0.14 11.15 ?  47  GLY   A CA   1 
ATOM   1202 C C    A GLY   A 1 47  ? 19.886 7.089   -0.354  0.86 13.15 ?  47  GLY   A C    1 
ATOM   1203 C C    B GLY   A 1 47  ? 19.659 6.931   0.051   0.14 10.28 ?  47  GLY   A C    1 
ATOM   1204 O O    A GLY   A 1 47  ? 20.767 6.259   -0.124  0.86 13.67 ?  47  GLY   A O    1 
ATOM   1205 O O    B GLY   A 1 47  ? 20.568 6.117   0.228   0.14 10.25 ?  47  GLY   A O    1 
ATOM   1206 H H    A GLY   A 1 47  ? 22.097 7.997   -0.818  0.86 16.89 ?  47  GLY   A H    1 
ATOM   1207 H H    B GLY   A 1 47  ? 21.779 7.829   -0.900  0.14 13.72 ?  47  GLY   A H    1 
ATOM   1208 H HA2  A GLY   A 1 47  ? 19.809 9.103   -0.013  0.86 17.25 ?  47  GLY   A HA2  1 
ATOM   1209 H HA2  B GLY   A 1 47  ? 19.623 8.959   0.243   0.14 13.39 ?  47  GLY   A HA2  1 
ATOM   1210 H HA3  A GLY   A 1 47  ? 19.831 8.749   -1.553  0.86 17.25 ?  47  GLY   A HA3  1 
ATOM   1211 H HA3  B GLY   A 1 47  ? 19.448 8.490   -1.251  0.14 13.39 ?  47  GLY   A HA3  1 
ATOM   1212 N N    A GLY   A 1 48  ? 18.594 6.793   -0.346  0.86 13.27 ?  48  GLY   A N    1 
ATOM   1213 N N    B GLY   A 1 48  ? 18.373 6.651   0.260   0.14 9.65  ?  48  GLY   A N    1 
ATOM   1214 C CA   A GLY   A 1 48  ? 18.166 5.469   0.028   0.86 13.15 ?  48  GLY   A CA   1 
ATOM   1215 C CA   B GLY   A 1 48  ? 17.973 5.335   0.707   0.14 8.84  ?  48  GLY   A CA   1 
ATOM   1216 C C    A GLY   A 1 48  ? 18.568 5.145   1.454   0.86 12.08 ?  48  GLY   A C    1 
ATOM   1217 C C    B GLY   A 1 48  ? 18.499 5.032   2.099   0.14 8.55  ?  48  GLY   A C    1 
ATOM   1218 O O    A GLY   A 1 48  ? 18.707 6.024   2.313   0.86 12.52 ?  48  GLY   A O    1 
ATOM   1219 O O    B GLY   A 1 48  ? 18.618 5.908   2.961   0.14 8.40  ?  48  GLY   A O    1 
ATOM   1220 H H    A GLY   A 1 48  ? 17.961 7.337   -0.538  0.86 15.93 ?  48  GLY   A H    1 
ATOM   1221 H H    B GLY   A 1 48  ? 17.721 7.203   0.147   0.14 11.59 ?  48  GLY   A H    1 
ATOM   1222 H HA2  A GLY   A 1 48  ? 17.208 5.395   -0.049  0.86 15.78 ?  48  GLY   A HA2  1 
ATOM   1223 H HA2  B GLY   A 1 48  ? 17.004 5.276   0.705   0.14 10.62 ?  48  GLY   A HA2  1 
ATOM   1224 H HA3  A GLY   A 1 48  ? 18.581 4.812   -0.558  0.86 15.78 ?  48  GLY   A HA3  1 
ATOM   1225 H HA3  B GLY   A 1 48  ? 18.324 4.668   0.099   0.14 10.62 ?  48  GLY   A HA3  1 
ATOM   1226 N N    A VAL   A 1 49  ? 18.782 3.853   1.704   0.86 11.83 ?  49  VAL   A N    1 
ATOM   1227 N N    B VAL   A 1 49  ? 18.824 3.757   2.316   0.14 8.39  ?  49  VAL   A N    1 
ATOM   1228 C CA   A VAL   A 1 49  ? 19.244 3.402   3.011   0.86 12.18 ?  49  VAL   A CA   1 
ATOM   1229 C CA   B VAL   A 1 49  ? 19.400 3.348   3.593   0.14 8.99  ?  49  VAL   A CA   1 
ATOM   1230 C C    A VAL   A 1 49  ? 20.562 4.071   3.384   0.86 11.07 ?  49  VAL   A C    1 
ATOM   1231 C C    B VAL   A 1 49  ? 20.746 4.026   3.812   0.14 9.41  ?  49  VAL   A C    1 
ATOM   1232 O O    A VAL   A 1 49  ? 20.753 4.480   4.533   0.86 11.38 ?  49  VAL   A O    1 
ATOM   1233 O O    B VAL   A 1 49  ? 21.085 4.416   4.937   0.14 9.83  ?  49  VAL   A O    1 
ATOM   1234 C CB   A VAL   A 1 49  ? 19.360 1.865   3.024   0.86 13.25 ?  49  VAL   A CB   1 
ATOM   1235 C CB   B VAL   A 1 49  ? 19.508 1.813   3.664   0.14 9.27  ?  49  VAL   A CB   1 
ATOM   1236 C CG1  A VAL   A 1 49  ? 20.112 1.386   4.263   0.86 14.33 ?  49  VAL   A CG1  1 
ATOM   1237 C CG1  B VAL   A 1 49  ? 20.409 1.399   4.817   0.14 9.25  ?  49  VAL   A CG1  1 
ATOM   1238 C CG2  A VAL   A 1 49  ? 17.987 1.223   2.948   0.86 15.25 ?  49  VAL   A CG2  1 
ATOM   1239 C CG2  B VAL   A 1 49  ? 18.125 1.191   3.808   0.14 9.53  ?  49  VAL   A CG2  1 
ATOM   1240 H H    A VAL   A 1 49  ? 18.672 3.219   1.135   0.86 14.21 ?  49  VAL   A H    1 
ATOM   1241 H H    B VAL   A 1 49  ? 18.723 3.122   1.745   0.14 10.07 ?  49  VAL   A H    1 
ATOM   1242 H HA   A VAL   A 1 49  ? 18.589 3.646   3.683   0.86 14.62 ?  49  VAL   A HA   1 
ATOM   1243 H HA   B VAL   A 1 49  ? 18.810 3.631   4.308   0.14 10.80 ?  49  VAL   A HA   1 
ATOM   1244 H HB   A VAL   A 1 49  ? 19.871 1.580   2.249   0.86 15.91 ?  49  VAL   A HB   1 
ATOM   1245 H HB   B VAL   A 1 49  ? 19.905 1.483   2.841   0.14 11.13 ?  49  VAL   A HB   1 
ATOM   1246 H HG11 A VAL   A 1 49  ? 19.933 0.441   4.395   0.86 17.21 ?  49  VAL   A HG11 1 
ATOM   1247 H HG11 B VAL   A 1 49  ? 20.244 0.466   5.019   0.14 11.11 ?  49  VAL   A HG11 1 
ATOM   1248 H HG12 A VAL   A 1 49  ? 21.062 1.527   4.140   0.86 17.21 ?  49  VAL   A HG12 1 
ATOM   1249 H HG12 B VAL   A 1 49  ? 21.334 1.523   4.557   0.14 11.11 ?  49  VAL   A HG12 1 
ATOM   1250 H HG13 A VAL   A 1 49  ? 19.798 1.887   5.035   0.86 17.21 ?  49  VAL   A HG13 1 
ATOM   1251 H HG13 B VAL   A 1 49  ? 20.199 1.947   5.588   0.14 11.11 ?  49  VAL   A HG13 1 
ATOM   1252 H HG21 A VAL   A 1 49  ? 18.091 0.256   2.954   0.86 18.30 ?  49  VAL   A HG21 1 
ATOM   1253 H HG21 B VAL   A 1 49  ? 18.219 0.232   3.907   0.14 11.44 ?  49  VAL   A HG21 1 
ATOM   1254 H HG22 A VAL   A 1 49  ? 17.467 1.502   3.717   0.86 18.30 ?  49  VAL   A HG22 1 
ATOM   1255 H HG22 B VAL   A 1 49  ? 17.693 1.565   4.591   0.14 11.44 ?  49  VAL   A HG22 1 
ATOM   1256 H HG23 A VAL   A 1 49  ? 17.556 1.505   2.131   0.86 18.30 ?  49  VAL   A HG23 1 
ATOM   1257 H HG23 B VAL   A 1 49  ? 17.607 1.394   3.014   0.14 11.44 ?  49  VAL   A HG23 1 
ATOM   1258 N N    A ALA   A 1 50  ? 21.506 4.136   2.443   0.86 10.92 ?  50  ALA   A N    1 
ATOM   1259 N N    B ALA   A 1 50  ? 21.532 4.178   2.743   0.14 9.40  ?  50  ALA   A N    1 
ATOM   1260 C CA   A ALA   A 1 50  ? 22.821 4.688   2.752   0.86 10.76 ?  50  ALA   A CA   1 
ATOM   1261 C CA   B ALA   A 1 50  ? 22.853 4.782   2.874   0.14 9.54  ?  50  ALA   A CA   1 
ATOM   1262 C C    A ALA   A 1 50  ? 22.727 6.144   3.176   0.86 10.61 ?  50  ALA   A C    1 
ATOM   1263 C C    B ALA   A 1 50  ? 22.752 6.213   3.385   0.14 9.69  ?  50  ALA   A C    1 
ATOM   1264 O O    A ALA   A 1 50  ? 23.358 6.560   4.154   0.86 11.49 ?  50  ALA   A O    1 
ATOM   1265 O O    B ALA   A 1 50  ? 23.420 6.588   4.356   0.14 9.63  ?  50  ALA   A O    1 
ATOM   1266 C CB   A ALA   A 1 50  ? 23.744 4.565   1.544   0.86 10.92 ?  50  ALA   A CB   1 
ATOM   1267 C CB   B ALA   A 1 50  ? 23.593 4.729   1.536   0.14 9.49  ?  50  ALA   A CB   1 
ATOM   1268 H H    A ALA   A 1 50  ? 21.406 3.879   1.632   0.86 13.11 ?  50  ALA   A H    1 
ATOM   1269 H H    B ALA   A 1 50  ? 21.319 3.950   1.939   0.14 11.29 ?  50  ALA   A H    1 
ATOM   1270 H HA   A ALA   A 1 50  ? 23.209 4.191   3.488   0.86 12.92 ?  50  ALA   A HA   1 
ATOM   1271 H HA   B ALA   A 1 50  ? 23.366 4.278   3.518   0.14 11.46 ?  50  ALA   A HA   1 
ATOM   1272 H HB1  A ALA   A 1 50  ? 24.607 4.940   1.771   0.86 13.12 ?  50  ALA   A HB1  1 
ATOM   1273 H HB1  B ALA   A 1 50  ? 24.471 5.130   1.643   0.14 11.39 ?  50  ALA   A HB1  1 
ATOM   1274 H HB2  A ALA   A 1 50  ? 23.832 3.632   1.310   0.86 13.12 ?  50  ALA   A HB2  1 
ATOM   1275 H HB2  B ALA   A 1 50  ? 23.685 3.802   1.262   0.14 11.39 ?  50  ALA   A HB2  1 
ATOM   1276 H HB3  A ALA   A 1 50  ? 23.353 5.060   0.803   0.86 13.12 ?  50  ALA   A HB3  1 
ATOM   1277 H HB3  B ALA   A 1 50  ? 23.085 5.220   0.871   0.14 11.39 ?  50  ALA   A HB3  1 
ATOM   1278 N N    A GLY   A 1 51  ? 21.951 6.940   2.443   0.86 10.74 ?  51  GLY   A N    1 
ATOM   1279 N N    B GLY   A 1 51  ? 21.912 7.027   2.745   0.14 9.96  ?  51  GLY   A N    1 
ATOM   1280 C CA   A GLY   A 1 51  ? 21.800 8.332   2.816   0.86 11.52 ?  51  GLY   A CA   1 
ATOM   1281 C CA   B GLY   A 1 51  ? 21.742 8.396   3.200   0.14 10.13 ?  51  GLY   A CA   1 
ATOM   1282 C C    A GLY   A 1 51  ? 21.196 8.483   4.196   0.86 11.46 ?  51  GLY   A C    1 
ATOM   1283 C C    B GLY   A 1 51  ? 21.173 8.471   4.603   0.14 10.58 ?  51  GLY   A C    1 
ATOM   1284 O O    A GLY   A 1 51  ? 21.589 9.367   4.959   0.86 12.17 ?  51  GLY   A O    1 
ATOM   1285 O O    B GLY   A 1 51  ? 21.577 9.317   5.405   0.14 11.04 ?  51  GLY   A O    1 
ATOM   1286 H H    A GLY   A 1 51  ? 21.517 6.704   1.742   0.86 12.89 ?  51  GLY   A H    1 
ATOM   1287 H H    B GLY   A 1 51  ? 21.438 6.811   2.060   0.14 11.97 ?  51  GLY   A H    1 
ATOM   1288 H HA2  A GLY   A 1 51  ? 22.666 8.770   2.810   0.86 13.83 ?  51  GLY   A HA2  1 
ATOM   1289 H HA2  B GLY   A 1 51  ? 22.600 8.849   3.187   0.14 12.17 ?  51  GLY   A HA2  1 
ATOM   1290 H HA3  A GLY   A 1 51  ? 21.223 8.782   2.179   0.86 13.83 ?  51  GLY   A HA3  1 
ATOM   1291 H HA3  B GLY   A 1 51  ? 21.141 8.863   2.597   0.14 12.17 ?  51  GLY   A HA3  1 
ATOM   1292 N N    A ALA   A 1 52  ? 20.227 7.624   4.530   0.86 11.91 ?  52  ALA   A N    1 
ATOM   1293 N N    B ALA   A 1 52  ? 20.236 7.577   4.923   0.14 10.71 ?  52  ALA   A N    1 
ATOM   1294 C CA   A ALA   A 1 52  ? 19.591 7.688   5.840   0.86 12.49 ?  52  ALA   A CA   1 
ATOM   1295 C CA   B ALA   A 1 52  ? 19.617 7.595   6.244   0.14 10.98 ?  52  ALA   A CA   1 
ATOM   1296 C C    A ALA   A 1 52  ? 20.547 7.266   6.952   0.86 11.71 ?  52  ALA   A C    1 
ATOM   1297 C C    B ALA   A 1 52  ? 20.604 7.170   7.323   0.14 10.78 ?  52  ALA   A C    1 
ATOM   1298 O O    A ALA   A 1 52  ? 20.618 7.916   7.999   0.86 12.33 ?  52  ALA   A O    1 
ATOM   1299 O O    B ALA   A 1 52  ? 20.680 7.798   8.385   0.14 11.07 ?  52  ALA   A O    1 
ATOM   1300 C CB   A ALA   A 1 52  ? 18.328 6.830   5.843   0.86 13.78 ?  52  ALA   A CB   1 
ATOM   1301 C CB   B ALA   A 1 52  ? 18.384 6.696   6.251   0.14 11.61 ?  52  ALA   A CB   1 
ATOM   1302 H H    A ALA   A 1 52  ? 19.941 6.993   4.025   0.86 14.30 ?  52  ALA   A H    1 
ATOM   1303 H H    B ALA   A 1 52  ? 19.954 6.956   4.402   0.14 12.86 ?  52  ALA   A H    1 
ATOM   1304 H HA   A ALA   A 1 52  ? 19.329 8.601   6.014   0.86 14.99 ?  52  ALA   A HA   1 
ATOM   1305 H HA   B ALA   A 1 52  ? 19.331 8.499   6.443   0.14 13.18 ?  52  ALA   A HA   1 
ATOM   1306 H HB1  A ALA   A 1 52  ? 17.911 6.883   6.720   0.86 16.54 ?  52  ALA   A HB1  1 
ATOM   1307 H HB1  B ALA   A 1 52  ? 17.961 6.748   7.122   0.14 13.94 ?  52  ALA   A HB1  1 
ATOM   1308 H HB2  A ALA   A 1 52  ? 17.718 7.168   5.169   0.86 16.54 ?  52  ALA   A HB2  1 
ATOM   1309 H HB2  B ALA   A 1 52  ? 17.771 7.005   5.565   0.14 13.94 ?  52  ALA   A HB2  1 
ATOM   1310 H HB3  A ALA   A 1 52  ? 18.564 5.911   5.646   0.86 16.54 ?  52  ALA   A HB3  1 
ATOM   1311 H HB3  B ALA   A 1 52  ? 18.656 5.784   6.066   0.14 13.94 ?  52  ALA   A HB3  1 
ATOM   1312 N N    A LEU   A 1 53  ? 21.278 6.162   6.763   0.86 11.56 ?  53  LEU   A N    1 
ATOM   1313 N N    B LEU   A 1 53  ? 21.364 6.099   7.076   0.14 10.45 ?  53  LEU   A N    1 
ATOM   1314 C CA   A LEU   A 1 53  ? 22.239 5.738   7.782   0.86 11.89 ?  53  LEU   A CA   1 
ATOM   1315 C CA   B LEU   A 1 53  ? 22.407 5.706   8.019   0.14 10.58 ?  53  LEU   A CA   1 
ATOM   1316 C C    A LEU   A 1 53  ? 23.299 6.806   7.988   0.86 10.85 ?  53  LEU   A C    1 
ATOM   1317 C C    B LEU   A 1 53  ? 23.419 6.830   8.196   0.14 11.07 ?  53  LEU   A C    1 
ATOM   1318 O O    A LEU   A 1 53  ? 23.640 7.146   9.124   0.86 12.29 ?  53  LEU   A O    1 
ATOM   1319 O O    B LEU   A 1 53  ? 23.764 7.200   9.324   0.14 11.59 ?  53  LEU   A O    1 
ATOM   1320 C CB   A LEU   A 1 53  ? 22.891 4.403   7.401   0.86 12.21 ?  53  LEU   A CB   1 
ATOM   1321 C CB   B LEU   A 1 53  ? 23.110 4.433   7.539   0.14 10.13 ?  53  LEU   A CB   1 
ATOM   1322 C CG   A LEU   A 1 53  ? 22.004 3.155   7.462   0.86 12.91 ?  53  LEU   A CG   1 
ATOM   1323 C CG   B LEU   A 1 53  ? 22.383 3.085   7.609   0.14 10.16 ?  53  LEU   A CG   1 
ATOM   1324 C CD1  A LEU   A 1 53  ? 22.717 1.966   6.837   0.86 13.08 ?  53  LEU   A CD1  1 
ATOM   1325 C CD1  B LEU   A 1 53  ? 23.280 1.991   7.045   0.14 10.12 ?  53  LEU   A CD1  1 
ATOM   1326 C CD2  A LEU   A 1 53  ? 21.588 2.822   8.888   0.86 14.71 ?  53  LEU   A CD2  1 
ATOM   1327 C CD2  B LEU   A 1 53  ? 21.971 2.742   9.028   0.14 10.25 ?  53  LEU   A CD2  1 
ATOM   1328 H H    A LEU   A 1 53  ? 21.232 5.648   6.074   0.86 13.88 ?  53  LEU   A H    1 
ATOM   1329 H H    B LEU   A 1 53  ? 21.296 5.595   6.382   0.14 12.55 ?  53  LEU   A H    1 
ATOM   1330 H HA   A LEU   A 1 53  ? 21.776 5.613   8.624   0.86 14.28 ?  53  LEU   A HA   1 
ATOM   1331 H HA   B LEU   A 1 53  ? 22.006 5.526   8.881   0.14 12.71 ?  53  LEU   A HA   1 
ATOM   1332 H HB2  A LEU   A 1 53  ? 23.223 4.473   6.493   0.86 14.66 ?  53  LEU   A HB2  1 
ATOM   1333 H HB2  B LEU   A 1 53  ? 23.353 4.564   6.611   0.14 12.16 ?  53  LEU   A HB2  1 
ATOM   1334 H HB3  A LEU   A 1 53  ? 23.639 4.246   8.002   0.86 14.66 ?  53  LEU   A HB3  1 
ATOM   1335 H HB3  B LEU   A 1 53  ? 23.920 4.333   8.063   0.14 12.16 ?  53  LEU   A HB3  1 
ATOM   1336 H HG   A LEU   A 1 53  ? 21.200 3.319   6.945   0.86 15.50 ?  53  LEU   A HG   1 
ATOM   1337 H HG   B LEU   A 1 53  ? 21.586 3.124   7.062   0.14 12.20 ?  53  LEU   A HG   1 
ATOM   1338 H HD11 A LEU   A 1 53  ? 22.134 1.190   6.885   0.86 15.70 ?  53  LEU   A HD11 1 
ATOM   1339 H HD11 B LEU   A 1 53  ? 22.814 1.141   7.094   0.14 12.15 ?  53  LEU   A HD11 1 
ATOM   1340 H HD12 A LEU   A 1 53  ? 22.917 2.169   5.909   0.86 15.70 ?  53  LEU   A HD12 1 
ATOM   1341 H HD12 B LEU   A 1 53  ? 23.492 2.198   6.122   0.14 12.15 ?  53  LEU   A HD12 1 
ATOM   1342 H HD13 A LEU   A 1 53  ? 23.536 1.796   7.325   0.86 15.70 ?  53  LEU   A HD13 1 
ATOM   1343 H HD13 B LEU   A 1 53  ? 24.097 1.948   7.569   0.14 12.15 ?  53  LEU   A HD13 1 
ATOM   1344 H HD21 A LEU   A 1 53  ? 21.060 2.004   8.882   0.86 17.66 ?  53  LEU   A HD21 1 
ATOM   1345 H HD21 B LEU   A 1 53  ? 21.487 1.900   9.021   0.14 12.30 ?  53  LEU   A HD21 1 
ATOM   1346 H HD22 A LEU   A 1 53  ? 22.382 2.694   9.431   0.86 17.66 ?  53  LEU   A HD22 1 
ATOM   1347 H HD22 B LEU   A 1 53  ? 22.764 2.663   9.578   0.14 12.30 ?  53  LEU   A HD22 1 
ATOM   1348 H HD23 A LEU   A 1 53  ? 21.057 3.550   9.244   0.86 17.66 ?  53  LEU   A HD23 1 
ATOM   1349 H HD23 B LEU   A 1 53  ? 21.398 3.446   9.369   0.14 12.30 ?  53  LEU   A HD23 1 
ATOM   1350 N N    A ASN   A 1 54  ? 23.823 7.354   6.895   0.86 10.86 ?  54  ASN   A N    1 
ATOM   1351 N N    B ASN   A 1 54  ? 23.897 7.395   7.085   0.14 11.47 ?  54  ASN   A N    1 
ATOM   1352 C CA   A ASN   A 1 54  ? 24.882 8.342   7.033   0.86 10.85 ?  54  ASN   A CA   1 
ATOM   1353 C CA   B ASN   A 1 54  ? 24.926 8.425   7.168   0.14 11.82 ?  54  ASN   A CA   1 
ATOM   1354 C C    A ASN   A 1 54  ? 24.383 9.584   7.765   0.86 11.40 ?  54  ASN   A C    1 
ATOM   1355 C C    B ASN   A 1 54  ? 24.400 9.671   7.868   0.14 12.05 ?  54  ASN   A C    1 
ATOM   1356 O O    A ASN   A 1 54  ? 25.085 10.131  8.626   0.86 12.38 ?  54  ASN   A O    1 
ATOM   1357 O O    B ASN   A 1 54  ? 25.065 10.228  8.749   0.14 11.98 ?  54  ASN   A O    1 
ATOM   1358 C CB   A ASN   A 1 54  ? 25.444 8.716   5.674   0.86 11.27 ?  54  ASN   A CB   1 
ATOM   1359 C CB   B ASN   A 1 54  ? 25.460 8.760   5.776   0.14 11.95 ?  54  ASN   A CB   1 
ATOM   1360 C CG   A ASN   A 1 54  ? 26.466 9.803   5.788   0.86 11.37 ?  54  ASN   A CG   1 
ATOM   1361 C CG   B ASN   A 1 54  ? 26.456 9.900   5.802   0.14 11.90 ?  54  ASN   A CG   1 
ATOM   1362 O OD1  A ASN   A 1 54  ? 27.462 9.657   6.513   0.86 11.35 ?  54  ASN   A OD1  1 
ATOM   1363 O OD1  B ASN   A 1 54  ? 27.567 9.753   6.310   0.14 12.09 ?  54  ASN   A OD1  1 
ATOM   1364 N ND2  A ASN   A 1 54  ? 26.232 10.915  5.111   0.86 11.98 ?  54  ASN   A ND2  1 
ATOM   1365 N ND2  B ASN   A 1 54  ? 26.063 11.046  5.260   0.14 11.77 ?  54  ASN   A ND2  1 
ATOM   1366 H H    A ASN   A 1 54  ? 23.581 7.179   6.087   0.86 13.04 ?  54  ASN   A H    1 
ATOM   1367 H H    B ASN   A 1 54  ? 23.640 7.207   6.287   0.14 13.78 ?  54  ASN   A H    1 
ATOM   1368 H HA   A ASN   A 1 54  ? 25.596 7.957   7.556   0.86 13.03 ?  54  ASN   A HA   1 
ATOM   1369 H HA   B ASN   A 1 54  ? 25.664 8.087   7.693   0.14 14.19 ?  54  ASN   A HA   1 
ATOM   1370 H HB2  A ASN   A 1 54  ? 25.868 7.932   5.277   0.86 13.53 ?  54  ASN   A HB2  1 
ATOM   1371 H HB2  B ASN   A 1 54  ? 25.910 7.980   5.413   0.14 14.35 ?  54  ASN   A HB2  1 
ATOM   1372 H HB3  A ASN   A 1 54  ? 24.726 9.027   5.099   0.86 13.53 ?  54  ASN   A HB3  1 
ATOM   1373 H HB3  B ASN   A 1 54  ? 24.723 9.017   5.203   0.14 14.35 ?  54  ASN   A HB3  1 
ATOM   1374 H HD21 A ASN   A 1 54  ? 26.793 11.563  5.153   0.86 14.39 ?  54  ASN   A HD21 1 
ATOM   1375 H HD21 B ASN   A 1 54  ? 26.593 11.724  5.255   0.14 14.14 ?  54  ASN   A HD21 1 
ATOM   1376 H HD22 A ASN   A 1 54  ? 25.527 10.981  4.628   0.86 14.39 ?  54  ASN   A HD22 1 
ATOM   1377 H HD22 B ASN   A 1 54  ? 25.280 11.111  4.912   0.14 14.14 ?  54  ASN   A HD22 1 
ATOM   1378 N N    A LYS   A 1 55  ? 23.168 10.042  7.436   0.86 11.65 ?  55  LYS   A N    1 
ATOM   1379 N N    B LYS   A 1 55  ? 23.202 10.126  7.491   0.14 12.44 ?  55  LYS   A N    1 
ATOM   1380 C CA   A LYS   A 1 55  ? 22.587 11.196  8.110   0.86 12.34 ?  55  LYS   A CA   1 
ATOM   1381 C CA   B LYS   A 1 55  ? 22.626 11.278  8.174   0.14 13.17 ?  55  LYS   A CA   1 
ATOM   1382 C C    A LYS   A 1 55  ? 22.513 10.961  9.613   0.86 12.28 ?  55  LYS   A C    1 
ATOM   1383 C C    B LYS   A 1 55  ? 22.443 10.998  9.658   0.14 13.03 ?  55  LYS   A C    1 
ATOM   1384 O O    A LYS   A 1 55  ? 22.814 11.859  10.407  0.86 13.27 ?  55  LYS   A O    1 
ATOM   1385 O O    B LYS   A 1 55  ? 22.602 11.905  10.484  0.14 12.99 ?  55  LYS   A O    1 
ATOM   1386 C CB   A LYS   A 1 55  ? 21.210 11.489  7.506   0.86 12.96 ?  55  LYS   A CB   1 
ATOM   1387 C CB   B LYS   A 1 55  ? 21.300 11.688  7.527   0.14 13.98 ?  55  LYS   A CB   1 
ATOM   1388 C CG   A LYS   A 1 55  ? 20.453 12.642  8.141   0.86 14.34 ?  55  LYS   A CG   1 
ATOM   1389 C CG   B LYS   A 1 55  ? 20.779 13.040  8.010   0.14 14.82 ?  55  LYS   A CG   1 
ATOM   1390 C CD   A LYS   A 1 55  ? 19.140 12.891  7.398   0.86 15.44 ?  55  LYS   A CD   1 
ATOM   1391 C CD   B LYS   A 1 55  ? 19.392 13.344  7.469   0.14 15.74 ?  55  LYS   A CD   1 
ATOM   1392 C CE   A LYS   A 1 55  ? 18.307 13.987  8.047   0.86 16.79 ?  55  LYS   A CE   1 
ATOM   1393 C CE   B LYS   A 1 55  ? 18.891 14.694  7.956   0.14 16.54 ?  55  LYS   A CE   1 
ATOM   1394 N NZ   A LYS   A 1 55  ? 16.998 14.177  7.358   0.86 17.72 ?  55  LYS   A NZ   1 
ATOM   1395 N NZ   B LYS   A 1 55  ? 17.484 14.962  7.551   0.14 16.90 ?  55  LYS   A NZ   1 
ATOM   1396 H H    A LYS   A 1 55  ? 22.657 9.688   6.835   0.86 13.99 ?  55  LYS   A H    1 
ATOM   1397 H H    B LYS   A 1 55  ? 22.715 9.793   6.864   0.14 14.93 ?  55  LYS   A H    1 
ATOM   1398 H HA   A LYS   A 1 55  ? 23.152 11.964  7.955   0.86 14.82 ?  55  LYS   A HA   1 
ATOM   1399 H HA   B LYS   A 1 55  ? 23.235 12.026  8.091   0.14 15.82 ?  55  LYS   A HA   1 
ATOM   1400 H HB2  A LYS   A 1 55  ? 21.326 11.699  6.567   0.86 15.56 ?  55  LYS   A HB2  1 
ATOM   1401 H HB2  B LYS   A 1 55  ? 21.424 11.747  6.567   0.14 16.78 ?  55  LYS   A HB2  1 
ATOM   1402 H HB3  A LYS   A 1 55  ? 20.660 10.694  7.595   0.86 15.56 ?  55  LYS   A HB3  1 
ATOM   1403 H HB3  B LYS   A 1 55  ? 20.627 11.023  7.733   0.14 16.78 ?  55  LYS   A HB3  1 
ATOM   1404 H HG2  A LYS   A 1 55  ? 20.245 12.423  9.064   0.86 17.21 ?  55  LYS   A HG2  1 
ATOM   1405 H HG2  B LYS   A 1 55  ? 20.729 13.038  8.977   0.14 17.80 ?  55  LYS   A HG2  1 
ATOM   1406 H HG3  A LYS   A 1 55  ? 20.989 13.446  8.095   0.86 17.21 ?  55  LYS   A HG3  1 
ATOM   1407 H HG3  B LYS   A 1 55  ? 21.379 13.740  7.706   0.14 17.80 ?  55  LYS   A HG3  1 
ATOM   1408 H HD2  A LYS   A 1 55  ? 19.337 13.158  6.487   0.86 18.54 ?  55  LYS   A HD2  1 
ATOM   1409 H HD2  B LYS   A 1 55  ? 19.437 13.384  6.505   0.14 18.89 ?  55  LYS   A HD2  1 
ATOM   1410 H HD3  A LYS   A 1 55  ? 18.616 12.072  7.398   0.86 18.54 ?  55  LYS   A HD3  1 
ATOM   1411 H HD3  B LYS   A 1 55  ? 18.767 12.656  7.753   0.14 18.89 ?  55  LYS   A HD3  1 
ATOM   1412 H HE2  A LYS   A 1 55  ? 18.130 13.747  8.971   0.86 20.16 ?  55  LYS   A HE2  1 
ATOM   1413 H HE2  B LYS   A 1 55  ? 18.937 14.717  8.923   0.14 19.85 ?  55  LYS   A HE2  1 
ATOM   1414 H HE3  A LYS   A 1 55  ? 18.796 14.823  8.007   0.86 20.16 ?  55  LYS   A HE3  1 
ATOM   1415 H HE3  B LYS   A 1 55  ? 19.451 15.393  7.581   0.14 19.85 ?  55  LYS   A HE3  1 
ATOM   1416 H HZ1  A LYS   A 1 55  ? 16.421 14.579  7.907   0.86 21.28 ?  55  LYS   A HZ1  1 
ATOM   1417 H HZ1  B LYS   A 1 55  ? 17.260 15.797  7.763   0.14 20.29 ?  55  LYS   A HZ1  1 
ATOM   1418 H HZ2  A LYS   A 1 55  ? 17.104 14.685  6.635   0.86 21.28 ?  55  LYS   A HZ2  1 
ATOM   1419 H HZ2  B LYS   A 1 55  ? 17.393 14.853  6.672   0.14 20.29 ?  55  LYS   A HZ2  1 
ATOM   1420 H HZ3  A LYS   A 1 55  ? 16.661 13.390  7.116   0.86 21.28 ?  55  LYS   A HZ3  1 
ATOM   1421 H HZ3  B LYS   A 1 55  ? 16.935 14.400  7.970   0.14 20.29 ?  55  LYS   A HZ3  1 
ATOM   1422 N N    . ALA   A 1 56  ? 22.121 9.754   10.022  1.00 13.00 ?  56  ALA   A N    1 
ATOM   1423 C CA   . ALA   A 1 56  ? 22.009 9.420   11.434  1.00 13.87 ?  56  ALA   A CA   1 
ATOM   1424 C C    . ALA   A 1 56  ? 23.351 9.447   12.155  1.00 13.65 ?  56  ALA   A C    1 
ATOM   1425 O O    . ALA   A 1 56  ? 23.375 9.625   13.376  1.00 14.99 ?  56  ALA   A O    1 
ATOM   1426 C CB   . ALA   A 1 56  ? 21.338 8.054   11.600  1.00 15.13 ?  56  ALA   A CB   1 
ATOM   1427 H H    A ALA   A 1 56  ? 21.909 9.113   9.492   0.86 15.61 ?  56  ALA   A H    1 
ATOM   1428 H H    B ALA   A 1 56  ? 21.960 9.108   9.480   0.14 15.61 ?  56  ALA   A H    1 
ATOM   1429 H HA   . ALA   A 1 56  ? 21.442 10.074  11.864  1.00 16.66 ?  56  ALA   A HA   1 
ATOM   1430 H HB1  . ALA   A 1 56  ? 21.270 7.848   12.547  1.00 18.17 ?  56  ALA   A HB1  1 
ATOM   1431 H HB2  . ALA   A 1 56  ? 20.455 8.088   11.204  1.00 18.17 ?  56  ALA   A HB2  1 
ATOM   1432 H HB3  . ALA   A 1 56  ? 21.876 7.379   11.154  1.00 18.17 ?  56  ALA   A HB3  1 
ATOM   1433 N N    . THR   A 1 57  ? 24.461 9.268   11.437  1.00 12.63 ?  57  THR   A N    1 
ATOM   1434 C CA   . THR   A 1 57  ? 25.801 9.392   12.013  1.00 12.90 ?  57  THR   A CA   1 
ATOM   1435 C C    . THR   A 1 57  ? 26.349 10.811  11.941  1.00 13.04 ?  57  THR   A C    1 
ATOM   1436 O O    . THR   A 1 57  ? 27.533 11.026  12.233  1.00 13.81 ?  57  THR   A O    1 
ATOM   1437 C CB   . THR   A 1 57  ? 26.812 8.447   11.335  1.00 12.70 ?  57  THR   A CB   1 
ATOM   1438 O OG1  . THR   A 1 57  ? 27.180 8.942   10.037  1.00 12.53 ?  57  THR   A OG1  1 
ATOM   1439 C CG2  . THR   A 1 57  ? 26.277 7.026   11.223  1.00 12.25 ?  57  THR   A CG2  1 
ATOM   1440 H H    . THR   A 1 57  ? 24.466 9.054   10.600  1.00 15.17 ?  57  THR   A H    1 
ATOM   1441 H HA   . THR   A 1 57  ? 25.756 9.133   12.950  1.00 15.49 ?  57  THR   A HA   1 
ATOM   1442 H HB   . THR   A 1 57  ? 27.613 8.402   11.887  1.00 15.25 ?  57  THR   A HB   1 
ATOM   1443 H HG1  . THR   A 1 57  ? 26.497 9.003   9.552   1.00 15.05 ?  57  THR   A HG1  1 
ATOM   1444 H HG21 . THR   A 1 57  ? 26.765 6.539   10.538  1.00 14.71 ?  57  THR   A HG21 1 
ATOM   1445 H HG22 . THR   A 1 57  ? 26.381 6.560   12.067  1.00 14.71 ?  57  THR   A HG22 1 
ATOM   1446 H HG23 . THR   A 1 57  ? 25.338 7.028   10.986  1.00 14.71 ?  57  THR   A HG23 1 
ATOM   1447 N N    . ASN   A 1 58  ? 25.532 11.778  11.537  1.00 13.44 ?  58  ASN   A N    1 
ATOM   1448 C CA   . ASN   A 1 58  ? 25.993 13.158  11.434  1.00 14.55 ?  58  ASN   A CA   1 
ATOM   1449 C C    . ASN   A 1 58  ? 27.133 13.291  10.421  1.00 13.20 ?  58  ASN   A C    1 
ATOM   1450 O O    . ASN   A 1 58  ? 28.026 14.124  10.577  1.00 14.02 ?  58  ASN   A O    1 
ATOM   1451 C CB   . ASN   A 1 58  ? 26.383 13.703  12.822  1.00 17.24 ?  58  ASN   A CB   1 
ATOM   1452 C CG   . ASN   A 1 58  ? 26.753 15.170  12.811  1.00 21.03 ?  58  ASN   A CG   1 
ATOM   1453 O OD1  . ASN   A 1 58  ? 26.089 15.974  12.168  1.00 22.52 ?  58  ASN   A OD1  1 
ATOM   1454 N ND2  . ASN   A 1 58  ? 27.812 15.531  13.543  1.00 22.50 ?  58  ASN   A ND2  1 
ATOM   1455 H H    . ASN   A 1 58  ? 24.713 11.652  11.306  1.00 16.14 ?  58  ASN   A H    1 
ATOM   1456 H HA   . ASN   A 1 58  ? 25.253 13.690  11.113  1.00 17.47 ?  58  ASN   A HA   1 
ATOM   1457 H HB2  . ASN   A 1 58  ? 25.628 13.587  13.428  1.00 20.69 ?  58  ASN   A HB2  1 
ATOM   1458 H HB3  . ASN   A 1 58  ? 27.146 13.211  13.157  1.00 20.69 ?  58  ASN   A HB3  1 
ATOM   1459 H HD21 . ASN   A 1 58  ? 28.055 16.357  13.569  1.00 27.01 ?  58  ASN   A HD21 1 
ATOM   1460 H HD22 . ASN   A 1 58  ? 28.248 14.939  13.984  1.00 27.01 ?  58  ASN   A HD22 1 
ATOM   1461 N N    . ASN   A 1 59  ? 27.108 12.478  9.365   1.00 12.33 ?  59  ASN   A N    1 
ATOM   1462 C CA   . ASN   A 1 59  ? 28.078 12.457  8.263   1.00 11.98 ?  59  ASN   A CA   1 
ATOM   1463 C C    . ASN   A 1 59  ? 29.391 11.778  8.644   1.00 11.71 ?  59  ASN   A C    1 
ATOM   1464 O O    . ASN   A 1 59  ? 30.308 11.741  7.816   1.00 12.01 ?  59  ASN   A O    1 
ATOM   1465 C CB   . ASN   A 1 59  ? 28.375 13.841  7.661   1.00 12.04 ?  59  ASN   A CB   1 
ATOM   1466 C CG   . ASN   A 1 59  ? 28.716 13.775  6.193   1.00 12.55 ?  59  ASN   A CG   1 
ATOM   1467 O OD1  . ASN   A 1 59  ? 28.006 13.152  5.408   1.00 12.75 ?  59  ASN   A OD1  1 
ATOM   1468 N ND2  . ASN   A 1 59  ? 29.808 14.437  5.807   1.00 13.16 ?  59  ASN   A ND2  1 
ATOM   1469 H H    . ASN   A 1 59  ? 26.493 11.884  9.252   1.00 14.81 ?  59  ASN   A H    1 
ATOM   1470 H HA   . ASN   A 1 59  ? 27.693 11.931  7.549   1.00 14.39 ?  59  ASN   A HA   1 
ATOM   1471 H HB2  . ASN   A 1 59  ? 27.595 14.409  7.754   1.00 14.46 ?  59  ASN   A HB2  1 
ATOM   1472 H HB3  . ASN   A 1 59  ? 29.131 14.237  8.120   1.00 14.46 ?  59  ASN   A HB3  1 
ATOM   1473 H HD21 . ASN   A 1 59  ? 30.047 14.429  4.978   1.00 15.80 ?  59  ASN   A HD21 1 
ATOM   1474 H HD22 . ASN   A 1 59  ? 30.284 14.860  6.384   1.00 15.80 ?  59  ASN   A HD22 1 
ATOM   1475 N N    . ALA   A 1 60  ? 29.520 11.237  9.853   1.00 11.50 ?  60  ALA   A N    1 
ATOM   1476 C CA   . ALA   A 1 60  ? 30.758 10.548  10.206  1.00 11.93 ?  60  ALA   A CA   1 
ATOM   1477 C C    . ALA   A 1 60  ? 30.985 9.308   9.347   1.00 11.89 ?  60  ALA   A C    1 
ATOM   1478 O O    . ALA   A 1 60  ? 32.130 8.990   9.007   1.00 12.55 ?  60  ALA   A O    1 
ATOM   1479 C CB   . ALA   A 1 60  ? 30.755 10.189  11.688  1.00 12.51 ?  60  ALA   A CB   1 
ATOM   1480 H H    . ALA   A 1 60  ? 28.924 11.257  10.468  1.00 13.81 ?  60  ALA   A H    1 
ATOM   1481 H HA   . ALA   A 1 60  ? 31.503 11.153  10.050  1.00 14.33 ?  60  ALA   A HA   1 
ATOM   1482 H HB1  . ALA   A 1 60  ? 31.580 9.737   11.905  1.00 15.02 ?  60  ALA   A HB1  1 
ATOM   1483 H HB2  . ALA   A 1 60  ? 30.677 11.009  12.207  1.00 15.02 ?  60  ALA   A HB2  1 
ATOM   1484 H HB3  . ALA   A 1 60  ? 29.996 9.614   11.869  1.00 15.02 ?  60  ALA   A HB3  1 
ATOM   1485 N N    . MET   A 1 61  ? 29.911 8.614   8.967   1.00 11.49 ?  61  MET   A N    1 
ATOM   1486 C CA   . MET   A 1 61  ? 30.050 7.481   8.057   1.00 11.43 ?  61  MET   A CA   1 
ATOM   1487 C C    . MET   A 1 61  ? 30.689 7.912   6.738   1.00 11.22 ?  61  MET   A C    1 
ATOM   1488 O O    . MET   A 1 61  ? 31.582 7.231   6.224   1.00 11.69 ?  61  MET   A O    1 
ATOM   1489 C CB   . MET   A 1 61  ? 28.687 6.831   7.831   1.00 11.63 ?  61  MET   A CB   1 
ATOM   1490 C CG   . MET   A 1 61  ? 28.701 5.667   6.863   1.00 12.46 ?  61  MET   A CG   1 
ATOM   1491 S SD   . MET   A 1 61  ? 27.080 4.932   6.644   1.00 13.49 ?  61  MET   A SD   1 
ATOM   1492 C CE   . MET   A 1 61  ? 26.909 4.042   8.190   1.00 15.34 ?  61  MET   A CE   1 
ATOM   1493 H H    . MET   A 1 61  ? 29.103 8.780   9.213   1.00 13.80 ?  61  MET   A H    1 
ATOM   1494 H HA   . MET   A 1 61  ? 30.619 6.819   8.474   1.00 13.72 ?  61  MET   A HA   1 
ATOM   1495 H HB2  . MET   A 1 61  ? 28.354 6.503   8.677   1.00 13.97 ?  61  MET   A HB2  1 
ATOM   1496 H HB3  . MET   A 1 61  ? 28.078 7.498   7.475   1.00 13.97 ?  61  MET   A HB3  1 
ATOM   1497 H HG2  . MET   A 1 61  ? 29.002 5.969   5.991   1.00 14.96 ?  61  MET   A HG2  1 
ATOM   1498 H HG3  . MET   A 1 61  ? 29.292 4.976   7.198   1.00 14.96 ?  61  MET   A HG3  1 
ATOM   1499 H HE1  . MET   A 1 61  ? 26.081 3.534   8.178   1.00 18.42 ?  61  MET   A HE1  1 
ATOM   1500 H HE2  . MET   A 1 61  ? 27.663 3.440   8.289   1.00 18.42 ?  61  MET   A HE2  1 
ATOM   1501 H HE3  . MET   A 1 61  ? 26.895 4.678   8.922   1.00 18.42 ?  61  MET   A HE3  1 
ATOM   1502 N N    . GLN   A 1 62  ? 30.245 9.042   6.179   1.00 11.29 ?  62  GLN   A N    1 
ATOM   1503 C CA   . GLN   A 1 62  ? 30.802 9.516   4.915   1.00 11.51 ?  62  GLN   A CA   1 
ATOM   1504 C C    . GLN   A 1 62  ? 32.271 9.896   5.057   1.00 11.39 ?  62  GLN   A C    1 
ATOM   1505 O O    . GLN   A 1 62  ? 33.078 9.583   4.177   1.00 12.10 ?  62  GLN   A O    1 
ATOM   1506 C CB   . GLN   A 1 62  ? 29.996 10.701  4.388   1.00 11.38 ?  62  GLN   A CB   1 
ATOM   1507 C CG   . GLN   A 1 62  ? 30.375 11.071  2.972   1.00 11.68 ?  62  GLN   A CG   1 
ATOM   1508 C CD   . GLN   A 1 62  ? 30.043 9.946   2.023   1.00 11.92 ?  62  GLN   A CD   1 
ATOM   1509 O OE1  . GLN   A 1 62  ? 28.869 9.648   1.811   1.00 12.59 ?  62  GLN   A OE1  1 
ATOM   1510 N NE2  . GLN   A 1 62  ? 31.058 9.269   1.500   1.00 12.70 ?  62  GLN   A NE2  1 
ATOM   1511 H H    . GLN   A 1 62  ? 29.630 9.538   6.507   1.00 13.56 ?  62  GLN   A H    1 
ATOM   1512 H HA   . GLN   A 1 62  ? 30.746 8.795   4.264   1.00 13.83 ?  62  GLN   A HA   1 
ATOM   1513 H HB2  . GLN   A 1 62  ? 29.055 10.474  4.400   1.00 13.67 ?  62  GLN   A HB2  1 
ATOM   1514 H HB3  . GLN   A 1 62  ? 30.163 11.470  4.954   1.00 13.67 ?  62  GLN   A HB3  1 
ATOM   1515 H HG2  . GLN   A 1 62  ? 29.869 11.852  2.700   1.00 14.02 ?  62  GLN   A HG2  1 
ATOM   1516 H HG3  . GLN   A 1 62  ? 31.325 11.246  2.922   1.00 14.02 ?  62  GLN   A HG3  1 
ATOM   1517 H HE21 . GLN   A 1 62  ? 31.866 9.497   1.682   1.00 15.25 ?  62  GLN   A HE21 1 
ATOM   1518 H HE22 . GLN   A 1 62  ? 30.906 8.614   0.962   1.00 15.25 ?  62  GLN   A HE22 1 
ATOM   1519 N N    . VAL   A 1 63  ? 32.638 10.565  6.153   1.00 11.75 ?  63  VAL   A N    1 
ATOM   1520 C CA   . VAL   A 1 63  ? 34.031 10.956  6.365   1.00 12.86 ?  63  VAL   A CA   1 
ATOM   1521 C C    . VAL   A 1 63  ? 34.923 9.719   6.426   1.00 12.03 ?  63  VAL   A C    1 
ATOM   1522 O O    . VAL   A 1 63  ? 35.973 9.648   5.772   1.00 12.52 ?  63  VAL   A O    1 
ATOM   1523 C CB   . VAL   A 1 63  ? 34.149 11.832  7.626   1.00 14.71 ?  63  VAL   A CB   1 
ATOM   1524 C CG1  . VAL   A 1 63  ? 35.600 12.077  7.982   1.00 16.38 ?  63  VAL   A CG1  1 
ATOM   1525 C CG2  . VAL   A 1 63  ? 33.428 13.162  7.416   1.00 15.06 ?  63  VAL   A CG2  1 
ATOM   1526 H H    . VAL   A 1 63  ? 32.096 10.805  6.778   1.00 14.11 ?  63  VAL   A H    1 
ATOM   1527 H HA   . VAL   A 1 63  ? 34.316 11.489  5.607   1.00 15.45 ?  63  VAL   A HA   1 
ATOM   1528 H HB   . VAL   A 1 63  ? 33.727 11.376  8.371   1.00 17.66 ?  63  VAL   A HB   1 
ATOM   1529 H HG11 . VAL   A 1 63  ? 35.647 12.808  8.614   1.00 19.66 ?  63  VAL   A HG11 1 
ATOM   1530 H HG12 . VAL   A 1 63  ? 35.969 11.272  8.376   1.00 19.66 ?  63  VAL   A HG12 1 
ATOM   1531 H HG13 . VAL   A 1 63  ? 36.085 12.306  7.173   1.00 19.66 ?  63  VAL   A HG13 1 
ATOM   1532 H HG21 . VAL   A 1 63  ? 33.520 13.703  8.218   1.00 18.08 ?  63  VAL   A HG21 1 
ATOM   1533 H HG22 . VAL   A 1 63  ? 33.827 13.624  6.661   1.00 18.08 ?  63  VAL   A HG22 1 
ATOM   1534 H HG23 . VAL   A 1 63  ? 32.489 12.993  7.240   1.00 18.08 ?  63  VAL   A HG23 1 
ATOM   1535 N N    . GLU   A 1 64  ? 34.498 8.708   7.185   1.00 12.21 ?  64  GLU   A N    1 
ATOM   1536 C CA   . GLU   A 1 64  ? 35.260 7.471   7.273   1.00 12.44 ?  64  GLU   A CA   1 
ATOM   1537 C C    . GLU   A 1 64  ? 35.342 6.787   5.917   1.00 12.02 ?  64  GLU   A C    1 
ATOM   1538 O O    . GLU   A 1 64  ? 36.388 6.241   5.538   1.00 12.64 ?  64  GLU   A O    1 
ATOM   1539 C CB   . GLU   A 1 64  ? 34.576 6.560   8.287   1.00 13.38 ?  64  GLU   A CB   1 
ATOM   1540 C CG   . GLU   A 1 64  ? 35.237 5.226   8.443   1.00 14.38 ?  64  GLU   A CG   1 
ATOM   1541 C CD   . GLU   A 1 64  ? 34.376 4.235   9.189   1.00 15.06 ?  64  GLU   A CD   1 
ATOM   1542 O OE1  . GLU   A 1 64  ? 33.136 4.329   9.079   1.00 16.31 ?  64  GLU   A OE1  1 
ATOM   1543 O OE2  . GLU   A 1 64  ? 34.938 3.346   9.872   1.00 15.49 -1 64  GLU   A OE2  1 
ATOM   1544 H H    . GLU   A 1 64  ? 33.774 8.715   7.646   1.00 14.67 ?  64  GLU   A H    1 
ATOM   1545 H HA   . GLU   A 1 64  ? 36.160 7.669   7.584   1.00 14.94 ?  64  GLU   A HA   1 
ATOM   1546 H HB2  . GLU   A 1 64  ? 34.586 7.004   9.155   1.00 16.07 ?  64  GLU   A HB2  1 
ATOM   1547 H HB3  . GLU   A 1 64  ? 33.660 6.422   8.004   1.00 16.07 ?  64  GLU   A HB3  1 
ATOM   1548 H HG2  . GLU   A 1 64  ? 35.424 4.850   7.566   1.00 17.27 ?  64  GLU   A HG2  1 
ATOM   1549 H HG3  . GLU   A 1 64  ? 36.061 5.338   8.936   1.00 17.27 ?  64  GLU   A HG3  1 
ATOM   1550 N N    . SER   A 1 65  ? 34.227 6.781   5.189   1.00 11.48 ?  65  SER   A N    1 
ATOM   1551 C CA   . SER   A 1 65  ? 34.169 6.132   3.885   1.00 11.52 ?  65  SER   A CA   1 
ATOM   1552 C C    . SER   A 1 65  ? 35.092 6.802   2.876   1.00 11.85 ?  65  SER   A C    1 
ATOM   1553 O O    . SER   A 1 65  ? 35.738 6.124   2.069   1.00 12.52 ?  65  SER   A O    1 
ATOM   1554 C CB   . SER   A 1 65  ? 32.740 6.152   3.359   1.00 11.63 ?  65  SER   A CB   1 
ATOM   1555 O OG   . SER   A 1 65  ? 31.891 5.330   4.144   1.00 12.41 ?  65  SER   A OG   1 
ATOM   1556 H H    . SER   A 1 65  ? 33.489 7.148   5.431   1.00 13.78 ?  65  SER   A H    1 
ATOM   1557 H HA   . SER   A 1 65  ? 34.446 5.209   3.975   1.00 13.83 ?  65  SER   A HA   1 
ATOM   1558 H HB2  . SER   A 1 65  ? 32.405 7.061   3.384   1.00 13.97 ?  65  SER   A HB2  1 
ATOM   1559 H HB3  . SER   A 1 65  ? 32.739 5.826   2.446   1.00 13.97 ?  65  SER   A HB3  1 
ATOM   1560 H HG   . SER   A 1 65  ? 31.890 5.603   4.945   1.00 14.90 ?  65  SER   A HG   1 
ATOM   1561 N N    . ASP   A 1 66  ? 35.160 8.133   2.893   1.00 11.89 ?  66  ASP   A N    1 
ATOM   1562 C CA   . ASP   A 1 66  ? 36.021 8.835   1.947   1.00 12.91 ?  66  ASP   A CA   1 
ATOM   1563 C C    . ASP   A 1 66  ? 37.483 8.476   2.184   1.00 12.55 ?  66  ASP   A C    1 
ATOM   1564 O O    . ASP   A 1 66  ? 38.258 8.309   1.232   1.00 13.65 ?  66  ASP   A O    1 
ATOM   1565 C CB   . ASP   A 1 66  ? 35.801 10.340  2.061   1.00 14.41 ?  66  ASP   A CB   1 
ATOM   1566 C CG   . ASP   A 1 66  ? 34.472 10.804  1.454   1.00 16.23 ?  66  ASP   A CG   1 
ATOM   1567 O OD1  . ASP   A 1 66  ? 33.749 10.016  0.801   1.00 16.66 ?  66  ASP   A OD1  1 
ATOM   1568 O OD2  . ASP   A 1 66  ? 34.171 12.000  1.621   1.00 19.36 -1 66  ASP   A OD2  1 
ATOM   1569 H H    . ASP   A 1 66  ? 34.723 8.646   3.430   1.00 14.27 ?  66  ASP   A H    1 
ATOM   1570 H HA   . ASP   A 1 66  ? 35.784 8.563   1.046   1.00 15.50 ?  66  ASP   A HA   1 
ATOM   1571 H HB2  . ASP   A 1 66  ? 35.796 10.589  2.996   1.00 17.30 ?  66  ASP   A HB2  1 
ATOM   1572 H HB3  . ASP   A 1 66  ? 36.522 10.798  1.598   1.00 17.30 ?  66  ASP   A HB3  1 
ATOM   1573 N N    . ASP   A 1 67  ? 37.877 8.348   3.449   1.00 12.85 ?  67  ASP   A N    1 
ATOM   1574 C CA   . ASP   A 1 67  ? 39.232 7.903   3.748   1.00 13.63 ?  67  ASP   A CA   1 
ATOM   1575 C C    . ASP   A 1 67  ? 39.459 6.476   3.266   1.00 13.50 ?  67  ASP   A C    1 
ATOM   1576 O O    . ASP   A 1 67  ? 40.517 6.160   2.714   1.00 14.36 ?  67  ASP   A O    1 
ATOM   1577 C CB   . ASP   A 1 67  ? 39.494 8.020   5.244   1.00 15.54 ?  67  ASP   A CB   1 
ATOM   1578 C CG   . ASP   A 1 67  ? 40.802 7.371   5.656   1.00 16.93 ?  67  ASP   A CG   1 
ATOM   1579 O OD1  . ASP   A 1 67  ? 41.870 8.009   5.496   1.00 19.47 ?  67  ASP   A OD1  1 
ATOM   1580 O OD2  . ASP   A 1 67  ? 40.759 6.211   6.127   1.00 16.94 -1 67  ASP   A OD2  1 
ATOM   1581 H H    . ASP   A 1 67  ? 37.390 8.505   4.133   1.00 15.43 ?  67  ASP   A H    1 
ATOM   1582 H HA   . ASP   A 1 67  ? 39.862 8.476   3.283   1.00 16.36 ?  67  ASP   A HA   1 
ATOM   1583 H HB2  . ASP   A 1 67  ? 39.530 8.957   5.479   1.00 18.65 ?  67  ASP   A HB2  1 
ATOM   1584 H HB3  . ASP   A 1 67  ? 38.770 7.582   5.722   1.00 18.65 ?  67  ASP   A HB3  1 
ATOM   1585 N N    . TYR   A 1 68  ? 38.476 5.592   3.462   1.00 13.10 ?  68  TYR   A N    1 
ATOM   1586 C CA   . TYR   A 1 68  ? 38.601 4.215   2.986   1.00 13.14 ?  68  TYR   A CA   1 
ATOM   1587 C C    . TYR   A 1 68  ? 38.836 4.172   1.477   1.00 12.67 ?  68  TYR   A C    1 
ATOM   1588 O O    . TYR   A 1 68  ? 39.711 3.442   0.993   1.00 13.26 ?  68  TYR   A O    1 
ATOM   1589 C CB   . TYR   A 1 68  ? 37.355 3.390   3.365   1.00 13.61 ?  68  TYR   A CB   1 
ATOM   1590 C CG   . TYR   A 1 68  ? 37.383 2.005   2.735   1.00 15.11 ?  68  TYR   A CG   1 
ATOM   1591 C CD1  . TYR   A 1 68  ? 36.923 1.811   1.436   1.00 16.93 ?  68  TYR   A CD1  1 
ATOM   1592 C CD2  . TYR   A 1 68  ? 37.927 0.923   3.401   1.00 17.50 ?  68  TYR   A CD2  1 
ATOM   1593 C CE1  . TYR   A 1 68  ? 36.984 0.594   0.823   1.00 18.42 ?  68  TYR   A CE1  1 
ATOM   1594 C CE2  . TYR   A 1 68  ? 37.979 -0.336  2.793   1.00 17.87 ?  68  TYR   A CE2  1 
ATOM   1595 C CZ   . TYR   A 1 68  ? 37.523 -0.471  1.502   1.00 18.74 ?  68  TYR   A CZ   1 
ATOM   1596 O OH   . TYR   A 1 68  ? 37.602 -1.686  0.884   1.00 20.67 ?  68  TYR   A OH   1 
ATOM   1597 H H    . TYR   A 1 68  ? 37.731 5.761   3.865   1.00 15.73 ?  68  TYR   A H    1 
ATOM   1598 H HA   . TYR   A 1 68  ? 39.366 3.805   3.414   1.00 15.78 ?  68  TYR   A HA   1 
ATOM   1599 H HB2  . TYR   A 1 68  ? 37.325 3.279   4.328   1.00 16.34 ?  68  TYR   A HB2  1 
ATOM   1600 H HB3  . TYR   A 1 68  ? 36.558 3.848   3.055   1.00 16.34 ?  68  TYR   A HB3  1 
ATOM   1601 H HD1  . TYR   A 1 68  ? 36.572 2.539   0.969   1.00 20.33 ?  68  TYR   A HD1  1 
ATOM   1602 H HD2  . TYR   A 1 68  ? 38.252 1.024   4.261   1.00 21.01 ?  68  TYR   A HD2  1 
ATOM   1603 H HE1  . TYR   A 1 68  ? 36.665 0.488   -0.046  1.00 22.11 ?  68  TYR   A HE1  1 
ATOM   1604 H HE2  . TYR   A 1 68  ? 38.349 -1.067  3.234   1.00 21.46 ?  68  TYR   A HE2  1 
ATOM   1605 H HH   . TYR   A 1 68  ? 37.933 -2.257  1.406   1.00 24.81 ?  68  TYR   A HH   1 
ATOM   1606 N N    . ILE   A 1 69  ? 38.048 4.932   0.714   1.00 12.56 ?  69  ILE   A N    1 
ATOM   1607 C CA   . ILE   A 1 69  ? 38.176 4.918   -0.740  1.00 12.90 ?  69  ILE   A CA   1 
ATOM   1608 C C    . ILE   A 1 69  ? 39.499 5.535   -1.174  1.00 12.78 ?  69  ILE   A C    1 
ATOM   1609 O O    . ILE   A 1 69  ? 40.134 5.068   -2.122  1.00 13.03 ?  69  ILE   A O    1 
ATOM   1610 C CB   . ILE   A 1 69  ? 36.971 5.623   -1.392  1.00 13.75 ?  69  ILE   A CB   1 
ATOM   1611 C CG1  . ILE   A 1 69  ? 35.666 4.878   -1.110  1.00 14.43 ?  69  ILE   A CG1  1 
ATOM   1612 C CG2  . ILE   A 1 69  ? 37.201 5.817   -2.897  1.00 15.56 ?  69  ILE   A CG2  1 
ATOM   1613 C CD1  . ILE   A 1 69  ? 35.490 3.601   -1.903  1.00 15.36 ?  69  ILE   A CD1  1 
ATOM   1614 H H    . ILE   A 1 69  ? 37.445 5.469   1.014   1.00 15.08 ?  69  ILE   A H    1 
ATOM   1615 H HA   . ILE   A 1 69  ? 38.175 3.997   -1.038  1.00 15.49 ?  69  ILE   A HA   1 
ATOM   1616 H HB   . ILE   A 1 69  ? 36.892 6.498   -0.992  1.00 16.51 ?  69  ILE   A HB   1 
ATOM   1617 H HG12 . ILE   A 1 69  ? 35.640 4.644   -0.167  1.00 17.32 ?  69  ILE   A HG12 1 
ATOM   1618 H HG13 . ILE   A 1 69  ? 34.922 5.462   -1.320  1.00 17.32 ?  69  ILE   A HG13 1 
ATOM   1619 H HG21 . ILE   A 1 69  ? 36.356 6.054   -3.317  1.00 18.68 ?  69  ILE   A HG21 1 
ATOM   1620 H HG22 . ILE   A 1 69  ? 37.840 6.540   -3.032  1.00 18.68 ?  69  ILE   A HG22 1 
ATOM   1621 H HG23 . ILE   A 1 69  ? 37.541 4.998   -3.279  1.00 18.68 ?  69  ILE   A HG23 1 
ATOM   1622 H HD11 . ILE   A 1 69  ? 34.706 3.132   -1.573  1.00 18.44 ?  69  ILE   A HD11 1 
ATOM   1623 H HD12 . ILE   A 1 69  ? 35.366 3.824   -2.840  1.00 18.44 ?  69  ILE   A HD12 1 
ATOM   1624 H HD13 . ILE   A 1 69  ? 36.276 3.046   -1.795  1.00 18.44 ?  69  ILE   A HD13 1 
ATOM   1625 N N    . ALA   A 1 70  ? 39.916 6.615   -0.514  1.00 12.93 ?  70  ALA   A N    1 
ATOM   1626 C CA   . ALA   A 1 70  ? 41.189 7.237   -0.861  1.00 14.05 ?  70  ALA   A CA   1 
ATOM   1627 C C    . ALA   A 1 70  ? 42.344 6.258   -0.701  1.00 14.26 ?  70  ALA   A C    1 
ATOM   1628 O O    . ALA   A 1 70  ? 43.316 6.309   -1.460  1.00 16.16 ?  70  ALA   A O    1 
ATOM   1629 C CB   . ALA   A 1 70  ? 41.426 8.476   0.005   1.00 14.52 ?  70  ALA   A CB   1 
ATOM   1630 H H    . ALA   A 1 70  ? 39.485 7.008   0.113   1.00 15.52 ?  70  ALA   A H    1 
ATOM   1631 H HA   . ALA   A 1 70  ? 41.163 7.529   -1.789  1.00 16.87 ?  70  ALA   A HA   1 
ATOM   1632 H HB1  . ALA   A 1 70  ? 42.283 8.871   -0.237  1.00 17.43 ?  70  ALA   A HB1  1 
ATOM   1633 H HB2  . ALA   A 1 70  ? 40.715 9.113   -0.145  1.00 17.43 ?  70  ALA   A HB2  1 
ATOM   1634 H HB3  . ALA   A 1 70  ? 41.445 8.208   0.938   1.00 17.43 ?  70  ALA   A HB3  1 
ATOM   1635 N N    . THR   A 1 71  ? 42.245 5.351   0.264   1.00 13.73 ?  71  THR   A N    1 
ATOM   1636 C CA   . THR   A 1 71  ? 43.305 4.384   0.519   1.00 15.15 ?  71  THR   A CA   1 
ATOM   1637 C C    . THR   A 1 71  ? 43.192 3.159   -0.376  1.00 15.23 ?  71  THR   A C    1 
ATOM   1638 O O    . THR   A 1 71  ? 44.206 2.655   -0.872  1.00 17.44 ?  71  THR   A O    1 
ATOM   1639 C CB   . THR   A 1 71  ? 43.234 3.939   1.976   1.00 16.95 ?  71  THR   A CB   1 
ATOM   1640 O OG1  . THR   A 1 71  ? 43.480 5.066   2.823   1.00 18.50 ?  71  THR   A OG1  1 
ATOM   1641 C CG2  . THR   A 1 71  ? 44.248 2.833   2.270   1.00 18.54 ?  71  THR   A CG2  1 
ATOM   1642 H H    . THR   A 1 71  ? 41.564 5.259   0.774   1.00 16.48 ?  71  THR   A H    1 
ATOM   1643 H HA   . THR   A 1 71  ? 44.166 4.795   0.356   1.00 18.19 ?  71  THR   A HA   1 
ATOM   1644 H HB   . THR   A 1 71  ? 42.344 3.584   2.150   1.00 20.35 ?  71  THR   A HB   1 
ATOM   1645 H HG1  . THR   A 1 71  ? 42.892 5.652   2.677   1.00 22.20 ?  71  THR   A HG1  1 
ATOM   1646 H HG21 . THR   A 1 71  ? 44.374 2.754   3.229   1.00 22.26 ?  71  THR   A HG21 1 
ATOM   1647 H HG22 . THR   A 1 71  ? 43.936 1.983   1.924   1.00 22.26 ?  71  THR   A HG22 1 
ATOM   1648 H HG23 . THR   A 1 71  ? 45.101 3.049   1.860   1.00 22.26 ?  71  THR   A HG23 1 
ATOM   1649 N N    . ASN   A 1 72  ? 41.973 2.651   -0.578  1.00 14.10 ?  72  ASN   A N    1 
ATOM   1650 C CA   . ASN   A 1 72  ? 41.762 1.326   -1.141  1.00 14.19 ?  72  ASN   A CA   1 
ATOM   1651 C C    . ASN   A 1 72  ? 41.138 1.323   -2.522  1.00 14.55 ?  72  ASN   A C    1 
ATOM   1652 O O    . ASN   A 1 72  ? 41.138 0.271   -3.174  1.00 15.93 ?  72  ASN   A O    1 
ATOM   1653 C CB   . ASN   A 1 72  ? 40.873 0.504   -0.200  1.00 15.20 ?  72  ASN   A CB   1 
ATOM   1654 C CG   . ASN   A 1 72  ? 41.487 0.343   1.165   1.00 16.14 ?  72  ASN   A CG   1 
ATOM   1655 O OD1  . ASN   A 1 72  ? 41.040 0.937   2.141   1.00 17.88 ?  72  ASN   A OD1  1 
ATOM   1656 N ND2  . ASN   A 1 72  ? 42.537 -0.445  1.239   1.00 16.91 ?  72  ASN   A ND2  1 
ATOM   1657 H H    . ASN   A 1 72  ? 41.240 3.067   -0.398  1.00 16.92 ?  72  ASN   A H    1 
ATOM   1658 H HA   . ASN   A 1 72  ? 42.615 0.877   -1.211  1.00 17.03 ?  72  ASN   A HA   1 
ATOM   1659 H HB2  . ASN   A 1 72  ? 40.018 0.947   -0.098  1.00 18.25 ?  72  ASN   A HB2  1 
ATOM   1660 H HB3  . ASN   A 1 72  ? 40.746 -0.383  -0.577  1.00 18.25 ?  72  ASN   A HB3  1 
ATOM   1661 H HD21 . ASN   A 1 72  ? 42.932 -0.568  1.997   1.00 20.30 ?  72  ASN   A HD21 1 
ATOM   1662 H HD22 . ASN   A 1 72  ? 42.833 -0.840  0.536   1.00 20.30 ?  72  ASN   A HD22 1 
ATOM   1663 N N    . GLY   A 1 73  ? 40.590 2.442   -2.978  1.00 14.19 ?  73  GLY   A N    1 
ATOM   1664 C CA   . GLY   A 1 73  ? 39.850 2.458   -4.213  1.00 13.91 ?  73  GLY   A CA   1 
ATOM   1665 C C    . GLY   A 1 73  ? 38.462 1.868   -4.043  1.00 13.46 ?  73  GLY   A C    1 
ATOM   1666 O O    . GLY   A 1 73  ? 38.076 1.419   -2.958  1.00 14.12 ?  73  GLY   A O    1 
ATOM   1667 H H    . GLY   A 1 73  ? 40.643 3.214   -2.588  1.00 17.04 ?  73  GLY   A H    1 
ATOM   1668 H HA2  . GLY   A 1 73  ? 39.770 3.376   -4.529  1.00 16.70 ?  73  GLY   A HA2  1 
ATOM   1669 H HA3  . GLY   A 1 73  ? 40.325 1.944   -4.884  1.00 16.70 ?  73  GLY   A HA3  1 
ATOM   1670 N N    . PRO   A 1 74  ? 37.679 1.878   -5.120  1.00 13.92 ?  74  PRO   A N    1 
ATOM   1671 C CA   . PRO   A 1 74  ? 36.280 1.454   -5.029  1.00 13.87 ?  74  PRO   A CA   1 
ATOM   1672 C C    . PRO   A 1 74  ? 36.136 -0.026  -4.712  1.00 13.24 ?  74  PRO   A C    1 
ATOM   1673 O O    . PRO   A 1 74  ? 37.004 -0.859  -4.992  1.00 14.40 ?  74  PRO   A O    1 
ATOM   1674 C CB   . PRO   A 1 74  ? 35.726 1.755   -6.425  1.00 15.36 ?  74  PRO   A CB   1 
ATOM   1675 C CG   . PRO   A 1 74  ? 36.669 2.751   -7.024  1.00 18.36 ?  74  PRO   A CG   1 
ATOM   1676 C CD   . PRO   A 1 74  ? 38.013 2.411   -6.452  1.00 16.00 ?  74  PRO   A CD   1 
ATOM   1677 H HA   . PRO   A 1 74  ? 35.807 1.981   -4.366  1.00 16.66 ?  74  PRO   A HA   1 
ATOM   1678 H HB2  . PRO   A 1 74  ? 35.704 0.941   -6.949  1.00 18.44 ?  74  PRO   A HB2  1 
ATOM   1679 H HB3  . PRO   A 1 74  ? 34.835 2.135   -6.344  1.00 18.44 ?  74  PRO   A HB3  1 
ATOM   1680 H HG2  . PRO   A 1 74  ? 36.676 2.657   -7.989  1.00 22.04 ?  74  PRO   A HG2  1 
ATOM   1681 H HG3  . PRO   A 1 74  ? 36.409 3.648   -6.768  1.00 22.04 ?  74  PRO   A HG3  1 
ATOM   1682 H HD2  . PRO   A 1 74  ? 38.454 1.733   -6.992  1.00 19.20 ?  74  PRO   A HD2  1 
ATOM   1683 H HD3  . PRO   A 1 74  ? 38.560 3.213   -6.384  1.00 19.20 ?  74  PRO   A HD3  1 
ATOM   1684 N N    . LEU   A 1 75  ? 34.992 -0.350  -4.126  1.00 12.67 ?  75  LEU   A N    1 
ATOM   1685 C CA   . LEU   A 1 75  ? 34.595 -1.740  -3.981  1.00 12.32 ?  75  LEU   A CA   1 
ATOM   1686 C C    . LEU   A 1 75  ? 34.202 -2.313  -5.340  1.00 12.81 ?  75  LEU   A C    1 
ATOM   1687 O O    . LEU   A 1 75  ? 34.074 -1.596  -6.334  1.00 14.21 ?  75  LEU   A O    1 
ATOM   1688 C CB   . LEU   A 1 75  ? 33.413 -1.863  -3.021  1.00 12.73 ?  75  LEU   A CB   1 
ATOM   1689 C CG   . LEU   A 1 75  ? 33.634 -1.478  -1.565  1.00 14.26 ?  75  LEU   A CG   1 
ATOM   1690 C CD1  . LEU   A 1 75  ? 32.361 -1.660  -0.759  1.00 16.12 ?  75  LEU   A CD1  1 
ATOM   1691 C CD2  . LEU   A 1 75  ? 34.776 -2.235  -0.936  1.00 17.77 ?  75  LEU   A CD2  1 
ATOM   1692 H H    . LEU   A 1 75  ? 34.434 0.217   -3.800  1.00 15.21 ?  75  LEU   A H    1 
ATOM   1693 H HA   . LEU   A 1 75  ? 35.339 -2.253  -3.635  1.00 14.79 ?  75  LEU   A HA   1 
ATOM   1694 H HB2  . LEU   A 1 75  ? 32.698 -1.307  -3.357  1.00 15.28 ?  75  LEU   A HB2  1 
ATOM   1695 H HB3  . LEU   A 1 75  ? 33.127 -2.792  -3.028  1.00 15.28 ?  75  LEU   A HB3  1 
ATOM   1696 H HG   . LEU   A 1 75  ? 33.872 -0.536  -1.533  1.00 17.12 ?  75  LEU   A HG   1 
ATOM   1697 H HD11 . LEU   A 1 75  ? 32.533 -1.404  0.161   1.00 19.35 ?  75  LEU   A HD11 1 
ATOM   1698 H HD12 . LEU   A 1 75  ? 31.670 -1.096  -1.137  1.00 19.35 ?  75  LEU   A HD12 1 
ATOM   1699 H HD13 . LEU   A 1 75  ? 32.094 -2.590  -0.801  1.00 19.35 ?  75  LEU   A HD13 1 
ATOM   1700 H HD21 . LEU   A 1 75  ? 34.836 -1.999  0.003   1.00 21.34 ?  75  LEU   A HD21 1 
ATOM   1701 H HD22 . LEU   A 1 75  ? 34.614 -3.188  -1.026  1.00 21.34 ?  75  LEU   A HD22 1 
ATOM   1702 H HD23 . LEU   A 1 75  ? 35.607 -2.000  -1.385  1.00 21.34 ?  75  LEU   A HD23 1 
ATOM   1703 N N    . LYS   A 1 76  ? 34.017 -3.630  -5.366  1.00 13.35 ?  76  LYS   A N    1 
ATOM   1704 C CA   . LYS   A 1 76  ? 33.413 -4.341  -6.487  1.00 14.04 ?  76  LYS   A CA   1 
ATOM   1705 C C    . LYS   A 1 76  ? 31.905 -4.426  -6.279  1.00 12.41 ?  76  LYS   A C    1 
ATOM   1706 O O    . LYS   A 1 76  ? 31.435 -4.553  -5.151  1.00 12.55 ?  76  LYS   A O    1 
ATOM   1707 C CB   . LYS   A 1 76  ? 33.960 -5.777  -6.557  1.00 15.99 ?  76  LYS   A CB   1 
ATOM   1708 C CG   . LYS   A 1 76  ? 35.467 -5.879  -6.753  1.00 17.30 ?  76  LYS   A CG   1 
ATOM   1709 C CD   . LYS   A 1 76  ? 35.982 -7.287  -6.553  1.00 18.33 ?  76  LYS   A CD   1 
ATOM   1710 C CE   . LYS   A 1 76  ? 37.484 -7.347  -6.734  1.00 20.98 ?  76  LYS   A CE   1 
ATOM   1711 N NZ   . LYS   A 1 76  ? 38.015 -8.713  -6.574  1.00 22.01 ?  76  LYS   A NZ   1 
ATOM   1712 H H    . LYS   A 1 76  ? 34.242 -4.153  -4.717  1.00 16.03 ?  76  LYS   A H    1 
ATOM   1713 H HA   . LYS   A 1 76  ? 33.601 -3.882  -7.320  1.00 16.86 ?  76  LYS   A HA   1 
ATOM   1714 H HB2  . LYS   A 1 76  ? 33.743 -6.231  -5.729  1.00 19.19 ?  76  LYS   A HB2  1 
ATOM   1715 H HB3  . LYS   A 1 76  ? 33.538 -6.230  -7.301  1.00 19.19 ?  76  LYS   A HB3  1 
ATOM   1716 H HG2  . LYS   A 1 76  ? 35.690 -5.599  -7.656  1.00 20.77 ?  76  LYS   A HG2  1 
ATOM   1717 H HG3  . LYS   A 1 76  ? 35.912 -5.300  -6.110  1.00 20.77 ?  76  LYS   A HG3  1 
ATOM   1718 H HD2  . LYS   A 1 76  ? 35.768 -7.583  -5.654  1.00 22.00 ?  76  LYS   A HD2  1 
ATOM   1719 H HD3  . LYS   A 1 76  ? 35.569 -7.875  -7.207  1.00 22.00 ?  76  LYS   A HD3  1 
ATOM   1720 H HE2  . LYS   A 1 76  ? 37.708 -7.039  -7.625  1.00 25.19 ?  76  LYS   A HE2  1 
ATOM   1721 H HE3  . LYS   A 1 76  ? 37.906 -6.783  -6.069  1.00 25.19 ?  76  LYS   A HE3  1 
ATOM   1722 H HZ1  . LYS   A 1 76  ? 38.898 -8.720  -6.688  1.00 26.42 ?  76  LYS   A HZ1  1 
ATOM   1723 H HZ2  . LYS   A 1 76  ? 37.827 -9.028  -5.762  1.00 26.42 ?  76  LYS   A HZ2  1 
ATOM   1724 H HZ3  . LYS   A 1 76  ? 37.647 -9.261  -7.180  1.00 26.42 ?  76  LYS   A HZ3  1 
ATOM   1725 N N    . VAL   A 1 77  ? 31.146 -4.393  -7.377  1.00 12.85 ?  77  VAL   A N    1 
ATOM   1726 C CA   . VAL   A 1 77  ? 29.741 -4.780  -7.284  1.00 12.63 ?  77  VAL   A CA   1 
ATOM   1727 C C    . VAL   A 1 77  ? 29.680 -6.230  -6.837  1.00 12.28 ?  77  VAL   A C    1 
ATOM   1728 O O    . VAL   A 1 77  ? 30.334 -7.103  -7.420  1.00 12.95 ?  77  VAL   A O    1 
ATOM   1729 C CB   . VAL   A 1 77  ? 29.016 -4.566  -8.619  1.00 14.13 ?  77  VAL   A CB   1 
ATOM   1730 C CG1  . VAL   A 1 77  ? 27.554 -4.990  -8.498  1.00 14.84 ?  77  VAL   A CG1  1 
ATOM   1731 C CG2  . VAL   A 1 77  ? 29.113 -3.115  -9.047  1.00 16.08 ?  77  VAL   A CG2  1 
ATOM   1732 H H    . VAL   A 1 77  ? 31.418 -4.156  -8.157  1.00 15.43 ?  77  VAL   A H    1 
ATOM   1733 H HA   . VAL   A 1 77  ? 29.307 -4.235  -6.611  1.00 15.17 ?  77  VAL   A HA   1 
ATOM   1734 H HB   . VAL   A 1 77  ? 29.438 -5.114  -9.302  1.00 16.97 ?  77  VAL   A HB   1 
ATOM   1735 H HG11 . VAL   A 1 77  ? 27.078 -4.696  -9.289  1.00 17.81 ?  77  VAL   A HG11 1 
ATOM   1736 H HG12 . VAL   A 1 77  ? 27.508 -5.955  -8.423  1.00 17.81 ?  77  VAL   A HG12 1 
ATOM   1737 H HG13 . VAL   A 1 77  ? 27.173 -4.575  -7.709  1.00 17.81 ?  77  VAL   A HG13 1 
ATOM   1738 H HG21 . VAL   A 1 77  ? 28.590 -2.993  -9.855  1.00 19.31 ?  77  VAL   A HG21 1 
ATOM   1739 H HG22 . VAL   A 1 77  ? 28.764 -2.557  -8.337  1.00 19.31 ?  77  VAL   A HG22 1 
ATOM   1740 H HG23 . VAL   A 1 77  ? 30.042 -2.897  -9.217  1.00 19.31 ?  77  VAL   A HG23 1 
ATOM   1741 N N    . GLY   A 1 78  ? 28.905 -6.497  -5.787  1.00 12.14 ?  78  GLY   A N    1 
ATOM   1742 C CA   . GLY   A 1 78  ? 28.886 -7.788  -5.136  1.00 12.50 ?  78  GLY   A CA   1 
ATOM   1743 C C    . GLY   A 1 78  ? 29.810 -7.886  -3.944  1.00 12.07 ?  78  GLY   A C    1 
ATOM   1744 O O    . GLY   A 1 78  ? 29.753 -8.889  -3.212  1.00 12.70 ?  78  GLY   A O    1 
ATOM   1745 H H    . GLY   A 1 78  ? 28.359 -5.924  -5.438  1.00 14.57 ?  78  GLY   A H    1 
ATOM   1746 H HA2  . GLY   A 1 78  ? 27.981 -7.976  -4.839  1.00 15.01 ?  78  GLY   A HA2  1 
ATOM   1747 H HA3  . GLY   A 1 78  ? 29.139 -8.467  -5.780  1.00 15.01 ?  78  GLY   A HA3  1 
ATOM   1748 N N    . GLY   A 1 79  ? 30.661 -6.879  -3.728  1.00 12.00 ?  79  GLY   A N    1 
ATOM   1749 C CA   . GLY   A 1 79  ? 31.629 -6.897  -2.658  1.00 12.17 ?  79  GLY   A CA   1 
ATOM   1750 C C    . GLY   A 1 79  ? 31.174 -6.108  -1.440  1.00 11.51 ?  79  GLY   A C    1 
ATOM   1751 O O    . GLY   A 1 79  ? 30.059 -5.596  -1.358  1.00 12.29 ?  79  GLY   A O    1 
ATOM   1752 H H    . GLY   A 1 79  ? 30.693 -6.163  -4.209  1.00 14.41 ?  79  GLY   A H    1 
ATOM   1753 H HA2  . GLY   A 1 79  ? 31.788 -7.820  -2.391  1.00 14.61 ?  79  GLY   A HA2  1 
ATOM   1754 H HA3  . GLY   A 1 79  ? 32.465 -6.526  -2.976  1.00 14.61 ?  79  GLY   A HA3  1 
ATOM   1755 N N    . SER   A 1 80  ? 32.078 -6.029  -0.467  1.00 12.19 ?  80  SER   A N    1 
ATOM   1756 C CA   . SER   A 1 80  ? 31.762 -5.396  0.801   1.00 12.01 ?  80  SER   A CA   1 
ATOM   1757 C C    . SER   A 1 80  ? 33.032 -4.943  1.497   1.00 11.68 ?  80  SER   A C    1 
ATOM   1758 O O    . SER   A 1 80  ? 34.146 -5.369  1.166   1.00 13.28 ?  80  SER   A O    1 
ATOM   1759 C CB   . SER   A 1 80  ? 30.996 -6.347  1.725   1.00 12.85 ?  80  SER   A CB   1 
ATOM   1760 O OG   . SER   A 1 80  ? 31.826 -7.395  2.197   1.00 14.18 ?  80  SER   A OG   1 
ATOM   1761 H H    . SER   A 1 80  ? 32.882 -6.329  -0.525  1.00 14.63 ?  80  SER   A H    1 
ATOM   1762 H HA   . SER   A 1 80  ? 31.213 -4.618  0.624   1.00 14.42 ?  80  SER   A HA   1 
ATOM   1763 H HB2  . SER   A 1 80  ? 30.663 -5.844  2.483   1.00 15.43 ?  80  SER   A HB2  1 
ATOM   1764 H HB3  . SER   A 1 80  ? 30.252 -6.729  1.230   1.00 15.43 ?  80  SER   A HB3  1 
ATOM   1765 H HG   . SER   A 1 80  ? 32.115 -7.841  1.543   1.00 17.02 ?  80  SER   A HG   1 
ATOM   1766 N N    . CYS   A 1 81  ? 32.840 -4.098  2.504   1.00 11.26 ?  81  CYS   A N    1 
ATOM   1767 C CA   . CYS   A 1 81  ? 33.894 -3.814  3.462   1.00 11.65 ?  81  CYS   A CA   1 
ATOM   1768 C C    . CYS   A 1 81  ? 33.263 -3.578  4.824   1.00 11.47 ?  81  CYS   A C    1 
ATOM   1769 O O    . CYS   A 1 81  ? 32.100 -3.176  4.920   1.00 12.75 ?  81  CYS   A O    1 
ATOM   1770 C CB   . CYS   A 1 81  ? 34.760 -2.625  3.035   1.00 12.85 ?  81  CYS   A CB   1 
ATOM   1771 S SG   . CYS   A 1 81  ? 33.874 -1.047  3.057   1.00 12.87 ?  81  CYS   A SG   1 
ATOM   1772 H H    . CYS   A 1 81  ? 32.100 -3.676  2.657   1.00 13.53 ?  81  CYS   A H    1 
ATOM   1773 H HA   . CYS   A 1 81  ? 34.471 -4.585  3.530   1.00 13.99 ?  81  CYS   A HA   1 
ATOM   1774 H HB2  . CYS   A 1 81  ? 35.516 -2.551  3.641   1.00 15.43 ?  81  CYS   A HB2  1 
ATOM   1775 H HB3  . CYS   A 1 81  ? 35.083 -2.777  2.130   1.00 15.43 ?  81  CYS   A HB3  1 
ATOM   1776 H HG   . CYS   A 1 81  ? 34.625 -0.172  2.707   1.00 15.45 ?  81  CYS   A HG   1 
ATOM   1777 N N    . VAL   A 1 82  ? 34.033 -3.844  5.874   1.00 11.81 ?  82  VAL   A N    1 
ATOM   1778 C CA   . VAL   A 1 82  ? 33.611 -3.602  7.247   1.00 12.62 ?  82  VAL   A CA   1 
ATOM   1779 C C    . VAL   A 1 82  ? 34.219 -2.292  7.716   1.00 12.78 ?  82  VAL   A C    1 
ATOM   1780 O O    . VAL   A 1 82  ? 35.444 -2.122  7.700   1.00 13.66 ?  82  VAL   A O    1 
ATOM   1781 C CB   . VAL   A 1 82  ? 34.034 -4.745  8.178   1.00 14.25 ?  82  VAL   A CB   1 
ATOM   1782 C CG1  . VAL   A 1 82  ? 33.586 -4.448  9.600   1.00 15.79 ?  82  VAL   A CG1  1 
ATOM   1783 C CG2  . VAL   A 1 82  ? 33.476 -6.069  7.698   1.00 15.48 ?  82  VAL   A CG2  1 
ATOM   1784 H H    . VAL   A 1 82  ? 34.824 -4.184  5.813   1.00 14.18 ?  82  VAL   A H    1 
ATOM   1785 H HA   . VAL   A 1 82  ? 32.643 -3.521  7.275   1.00 15.16 ?  82  VAL   A HA   1 
ATOM   1786 H HB   . VAL   A 1 82  ? 35.000 -4.806  8.176   1.00 17.11 ?  82  VAL   A HB   1 
ATOM   1787 H HG11 . VAL   A 1 82  ? 33.667 -5.257  10.129  1.00 18.96 ?  82  VAL   A HG11 1 
ATOM   1788 H HG12 . VAL   A 1 82  ? 34.148 -3.752  9.975   1.00 18.96 ?  82  VAL   A HG12 1 
ATOM   1789 H HG13 . VAL   A 1 82  ? 32.660 -4.155  9.587   1.00 18.96 ?  82  VAL   A HG13 1 
ATOM   1790 H HG21 . VAL   A 1 82  ? 33.719 -6.761  8.332   1.00 18.59 ?  82  VAL   A HG21 1 
ATOM   1791 H HG22 . VAL   A 1 82  ? 32.509 -6.002  7.635   1.00 18.59 ?  82  VAL   A HG22 1 
ATOM   1792 H HG23 . VAL   A 1 82  ? 33.849 -6.273  6.826   1.00 18.59 ?  82  VAL   A HG23 1 
ATOM   1793 N N    . LEU   A 1 83  ? 33.366 -1.369  8.139   1.00 12.30 ?  83  LEU   A N    1 
ATOM   1794 C CA   . LEU   A 1 83  ? 33.792 -0.106  8.715   1.00 12.19 ?  83  LEU   A CA   1 
ATOM   1795 C C    . LEU   A 1 83  ? 33.087 0.068   10.056  1.00 12.50 ?  83  LEU   A C    1 
ATOM   1796 O O    . LEU   A 1 83  ? 32.356 -0.816  10.518  1.00 13.09 ?  83  LEU   A O    1 
ATOM   1797 C CB   . LEU   A 1 83  ? 33.536 1.054   7.740   1.00 12.64 ?  83  LEU   A CB   1 
ATOM   1798 C CG   . LEU   A 1 83  ? 34.430 1.060   6.497   1.00 13.76 ?  83  LEU   A CG   1 
ATOM   1799 C CD1  . LEU   A 1 83  ? 33.984 2.120   5.514   1.00 14.29 ?  83  LEU   A CD1  1 
ATOM   1800 C CD2  . LEU   A 1 83  ? 35.897 1.265   6.873   1.00 14.73 ?  83  LEU   A CD2  1 
ATOM   1801 H H    . LEU   A 1 83  ? 32.511 -1.451  8.090   1.00 14.77 ?  83  LEU   A H    1 
ATOM   1802 H HA   . LEU   A 1 83  ? 34.746 -0.138  8.882   1.00 14.63 ?  83  LEU   A HA   1 
ATOM   1803 H HB2  . LEU   A 1 83  ? 32.616 1.009   7.430   1.00 15.18 ?  83  LEU   A HB2  1 
ATOM   1804 H HB3  . LEU   A 1 83  ? 33.677 1.895   8.203   1.00 15.18 ?  83  LEU   A HB3  1 
ATOM   1805 H HG   . LEU   A 1 83  ? 34.361 0.201   6.058   1.00 16.52 ?  83  LEU   A HG   1 
ATOM   1806 H HD11 . LEU   A 1 83  ? 34.567 2.097   4.736   1.00 17.15 ?  83  LEU   A HD11 1 
ATOM   1807 H HD12 . LEU   A 1 83  ? 33.071 1.934   5.246   1.00 17.15 ?  83  LEU   A HD12 1 
ATOM   1808 H HD13 . LEU   A 1 83  ? 34.035 2.990   5.938   1.00 17.15 ?  83  LEU   A HD13 1 
ATOM   1809 H HD21 . LEU   A 1 83  ? 36.413 1.435   6.065   1.00 17.68 ?  83  LEU   A HD21 1 
ATOM   1810 H HD22 . LEU   A 1 83  ? 35.971 2.028   7.471   1.00 17.68 ?  83  LEU   A HD22 1 
ATOM   1811 H HD23 . LEU   A 1 83  ? 36.231 0.469   7.312   1.00 17.68 ?  83  LEU   A HD23 1 
ATOM   1812 N N    . SER   A 1 84  ? 33.305 1.217   10.687  1.00 12.97 ?  84  SER   A N    1 
ATOM   1813 C CA   . SER   A 1 84  ? 32.663 1.473   11.964  1.00 13.19 ?  84  SER   A CA   1 
ATOM   1814 C C    . SER   A 1 84  ? 31.145 1.558   11.817  1.00 12.63 ?  84  SER   A C    1 
ATOM   1815 O O    . SER   A 1 84  ? 30.621 2.018   10.807  1.00 13.27 ?  84  SER   A O    1 
ATOM   1816 C CB   . SER   A 1 84  ? 33.164 2.788   12.542  1.00 14.55 ?  84  SER   A CB   1 
ATOM   1817 O OG   . SER   A 1 84  ? 32.520 3.056   13.768  1.00 15.61 ?  84  SER   A OG   1 
ATOM   1818 H H    . SER   A 1 84  ? 33.811 1.857   10.392  1.00 15.57 ?  84  SER   A H    1 
ATOM   1819 H HA   . SER   A 1 84  ? 32.880 0.755   12.573  1.00 15.83 ?  84  SER   A HA   1 
ATOM   1820 H HB2  . SER   A 1 84  ? 34.123 2.726   12.678  1.00 17.46 ?  84  SER   A HB2  1 
ATOM   1821 H HB3  . SER   A 1 84  ? 32.963 3.503   11.917  1.00 17.46 ?  84  SER   A HB3  1 
ATOM   1822 H HG   . SER   A 1 84  ? 32.810 3.775   14.090  1.00 18.74 ?  84  SER   A HG   1 
ATOM   1823 N N    . GLY   A 1 85  ? 30.438 1.142   12.862  1.00 13.81 ?  85  GLY   A N    1 
ATOM   1824 C CA   . GLY   A 1 85  ? 29.017 1.380   12.947  1.00 14.59 ?  85  GLY   A CA   1 
ATOM   1825 C C    . GLY   A 1 85  ? 28.650 2.683   13.614  1.00 14.43 ?  85  GLY   A C    1 
ATOM   1826 O O    . GLY   A 1 85  ? 27.459 2.985   13.746  1.00 14.76 ?  85  GLY   A O    1 
ATOM   1827 H H    . GLY   A 1 85  ? 30.771 0.714   13.530  1.00 16.59 ?  85  GLY   A H    1 
ATOM   1828 H HA2  . GLY   A 1 85  ? 28.643 1.376   12.049  1.00 17.52 ?  85  GLY   A HA2  1 
ATOM   1829 H HA3  . GLY   A 1 85  ? 28.608 0.659   13.444  1.00 17.52 ?  85  GLY   A HA3  1 
ATOM   1830 N N    . HIS   A 1 86  ? 29.636 3.453   14.060  1.00 13.84 ?  86  HIS   A N    1 
ATOM   1831 C CA   . HIS   A 1 86  ? 29.402 4.786   14.629  1.00 14.53 ?  86  HIS   A CA   1 
ATOM   1832 C C    . HIS   A 1 86  ? 28.422 4.655   15.789  1.00 15.21 ?  86  HIS   A C    1 
ATOM   1833 O O    . HIS   A 1 86  ? 28.614 3.775   16.642  1.00 16.43 ?  86  HIS   A O    1 
ATOM   1834 C CB   . HIS   A 1 86  ? 29.017 5.764   13.528  1.00 14.58 ?  86  HIS   A CB   1 
ATOM   1835 C CG   . HIS   A 1 86  ? 30.064 5.870   12.478  1.00 14.97 ?  86  HIS   A CG   1 
ATOM   1836 N ND1  . HIS   A 1 86  ? 31.150 6.709   12.604  1.00 16.06 ?  86  HIS   A ND1  1 
ATOM   1837 C CD2  . HIS   A 1 86  ? 30.238 5.194   11.321  1.00 14.93 ?  86  HIS   A CD2  1 
ATOM   1838 C CE1  . HIS   A 1 86  ? 31.933 6.563   11.551  1.00 15.78 ?  86  HIS   A CE1  1 
ATOM   1839 N NE2  . HIS   A 1 86  ? 31.411 5.639   10.766  1.00 15.47 ?  86  HIS   A NE2  1 
ATOM   1840 H H    . HIS   A 1 86  ? 30.462 3.230   14.043  1.00 16.61 ?  86  HIS   A H    1 
ATOM   1841 H HA   . HIS   A 1 86  ? 30.239 5.105   14.994  1.00 17.44 ?  86  HIS   A HA   1 
ATOM   1842 H HB2  . HIS   A 1 86  ? 28.196 5.475   13.100  1.00 17.50 ?  86  HIS   A HB2  1 
ATOM   1843 H HB3  . HIS   A 1 86  ? 28.888 6.654   13.910  1.00 17.50 ?  86  HIS   A HB3  1 
ATOM   1844 H HD2  . HIS   A 1 86  ? 29.680 4.540   10.973  1.00 17.92 ?  86  HIS   A HD2  1 
ATOM   1845 H HE1  . HIS   A 1 86  ? 32.725 7.033   11.380  1.00 18.94 ?  86  HIS   A HE1  1 
ATOM   1846 H HE2  . HIS   A 1 86  ? 31.743 5.376   10.010  1.00 18.57 ?  86  HIS   A HE2  1 
ATOM   1847 N N    . ASN   A 1 87  ? 27.405 5.503   15.870  1.00 16.13 ?  87  ASN   A N    1 
ATOM   1848 C CA   . ASN   A 1 87  ? 26.422 5.476   16.938  1.00 17.00 ?  87  ASN   A CA   1 
ATOM   1849 C C    . ASN   A 1 87  ? 25.305 4.475   16.691  1.00 18.49 ?  87  ASN   A C    1 
ATOM   1850 O O    . ASN   A 1 87  ? 24.383 4.391   17.506  1.00 20.55 ?  87  ASN   A O    1 
ATOM   1851 C CB   . ASN   A 1 87  ? 25.815 6.875   17.110  1.00 17.80 ?  87  ASN   A CB   1 
ATOM   1852 C CG   . ASN   A 1 87  ? 25.306 7.465   15.798  1.00 18.45 ?  87  ASN   A CG   1 
ATOM   1853 O OD1  . ASN   A 1 87  ? 25.957 7.372   14.757  1.00 18.86 ?  87  ASN   A OD1  1 
ATOM   1854 N ND2  . ASN   A 1 87  ? 24.141 8.084   15.850  1.00 19.74 ?  87  ASN   A ND2  1 
ATOM   1855 H H    . ASN   A 1 87  ? 27.265 6.130   15.298  1.00 19.37 ?  87  ASN   A H    1 
ATOM   1856 H HA   . ASN   A 1 87  ? 26.860 5.232   17.772  1.00 20.41 ?  87  ASN   A HA   1 
ATOM   1857 H HB2  . ASN   A 1 87  ? 25.065 6.814   17.732  1.00 21.37 ?  87  ASN   A HB2  1 
ATOM   1858 H HB3  . ASN   A 1 87  ? 26.490 7.468   17.473  1.00 21.37 ?  87  ASN   A HB3  1 
ATOM   1859 H HD21 . ASN   A 1 87  ? 23.814 8.434   15.140  1.00 23.70 ?  87  ASN   A HD21 1 
ATOM   1860 H HD22 . ASN   A 1 87  ? 23.715 8.143   16.597  1.00 23.70 ?  87  ASN   A HD22 1 
ATOM   1861 N N    . LEU   A 1 88  ? 25.371 3.706   15.610  1.00 17.64 ?  88  LEU   A N    1 
ATOM   1862 C CA   . LEU   A 1 88  ? 24.266 2.843   15.214  1.00 17.08 ?  88  LEU   A CA   1 
ATOM   1863 C C    . LEU   A 1 88  ? 24.492 1.369   15.515  1.00 16.85 ?  88  LEU   A C    1 
ATOM   1864 O O    . LEU   A 1 88  ? 23.520 0.631   15.702  1.00 18.22 ?  88  LEU   A O    1 
ATOM   1865 C CB   . LEU   A 1 88  ? 24.008 3.000   13.714  1.00 17.86 ?  88  LEU   A CB   1 
ATOM   1866 C CG   . LEU   A 1 88  ? 23.692 4.417   13.236  1.00 19.53 ?  88  LEU   A CG   1 
ATOM   1867 C CD1  . LEU   A 1 88  ? 23.550 4.435   11.728  1.00 19.84 ?  88  LEU   A CD1  1 
ATOM   1868 C CD2  . LEU   A 1 88  ? 22.430 4.952   13.904  1.00 21.27 ?  88  LEU   A CD2  1 
ATOM   1869 H H    . LEU   A 1 88  ? 26.060 3.661   15.092  1.00 21.18 ?  88  LEU   A H    1 
ATOM   1870 H HA   . LEU   A 1 88  ? 23.469 3.126   15.684  1.00 20.51 ?  88  LEU   A HA   1 
ATOM   1871 H HB2  . LEU   A 1 88  ? 24.795 2.707   13.233  1.00 21.44 ?  88  LEU   A HB2  1 
ATOM   1872 H HB3  . LEU   A 1 88  ? 23.252 2.445   13.476  1.00 21.44 ?  88  LEU   A HB3  1 
ATOM   1873 H HG   . LEU   A 1 88  ? 24.427 5.006   13.472  1.00 23.45 ?  88  LEU   A HG   1 
ATOM   1874 H HD11 . LEU   A 1 88  ? 23.430 5.353   11.432  1.00 23.82 ?  88  LEU   A HD11 1 
ATOM   1875 H HD12 . LEU   A 1 88  ? 24.354 4.065   11.331  1.00 23.82 ?  88  LEU   A HD12 1 
ATOM   1876 H HD13 . LEU   A 1 88  ? 22.780 3.904   11.478  1.00 23.82 ?  88  LEU   A HD13 1 
ATOM   1877 H HD21 . LEU   A 1 88  ? 22.195 5.801   13.498  1.00 25.54 ?  88  LEU   A HD21 1 
ATOM   1878 H HD22 . LEU   A 1 88  ? 21.714 4.312   13.777  1.00 25.54 ?  88  LEU   A HD22 1 
ATOM   1879 H HD23 . LEU   A 1 88  ? 22.604 5.074   14.850  1.00 25.54 ?  88  LEU   A HD23 1 
ATOM   1880 N N    . ALA   A 1 89  ? 25.744 0.929   15.549  1.00 15.80 ?  89  ALA   A N    1 
ATOM   1881 C CA   . ALA   A 1 89  ? 26.089 -0.481  15.642  1.00 15.49 ?  89  ALA   A CA   1 
ATOM   1882 C C    . ALA   A 1 89  ? 27.574 -0.540  15.952  1.00 15.88 ?  89  ALA   A C    1 
ATOM   1883 O O    . ALA   A 1 89  ? 28.284 0.458   15.830  1.00 16.75 ?  89  ALA   A O    1 
ATOM   1884 C CB   . ALA   A 1 89  ? 25.810 -1.191  14.319  1.00 14.64 ?  89  ALA   A CB   1 
ATOM   1885 H H    . ALA   A 1 89  ? 26.430 1.450   15.508  1.00 18.96 ?  89  ALA   A H    1 
ATOM   1886 H HA   . ALA   A 1 89  ? 25.585 -0.901  16.354  1.00 18.60 ?  89  ALA   A HA   1 
ATOM   1887 H HB1  . ALA   A 1 89  ? 26.067 -2.124  14.405  1.00 17.58 ?  89  ALA   A HB1  1 
ATOM   1888 H HB2  . ALA   A 1 89  ? 24.863 -1.129  14.117  1.00 17.58 ?  89  ALA   A HB2  1 
ATOM   1889 H HB3  . ALA   A 1 89  ? 26.328 -0.770  13.617  1.00 17.58 ?  89  ALA   A HB3  1 
ATOM   1890 N N    . LYS   A 1 90  ? 28.057 -1.718  16.337  1.00 16.50 ?  90  LYS   A N    1 
ATOM   1891 C CA   . LYS   A 1 90  ? 29.501 -1.869  16.479  1.00 16.84 ?  90  LYS   A CA   1 
ATOM   1892 C C    . LYS   A 1 90  ? 30.195 -1.676  15.133  1.00 15.47 ?  90  LYS   A C    1 
ATOM   1893 O O    . LYS   A 1 90  ? 31.127 -0.865  15.004  1.00 17.17 ?  90  LYS   A O    1 
ATOM   1894 C CB   . LYS   A 1 90  ? 29.839 -3.229  17.088  1.00 19.97 ?  90  LYS   A CB   1 
ATOM   1895 C CG   . LYS   A 1 90  ? 31.323 -3.393  17.385  1.00 23.91 ?  90  LYS   A CG   1 
ATOM   1896 C CD   . LYS   A 1 90  ? 31.588 -4.615  18.251  1.00 27.84 ?  90  LYS   A CD   1 
ATOM   1897 C CE   . LYS   A 1 90  ? 33.008 -4.616  18.809  1.00 31.15 ?  90  LYS   A CE   1 
ATOM   1898 N NZ   . LYS   A 1 90  ? 34.025 -5.070  17.820  1.00 33.28 ?  90  LYS   A NZ   1 
ATOM   1899 H H    . LYS   A 1 90  ? 27.588 -2.411  16.511  1.00 19.81 ?  90  LYS   A H    1 
ATOM   1900 H HA   . LYS   A 1 90  ? 29.831 -1.182  17.077  1.00 20.22 ?  90  LYS   A HA   1 
ATOM   1901 H HB2  . LYS   A 1 90  ? 29.350 -3.327  17.922  1.00 23.97 ?  90  LYS   A HB2  1 
ATOM   1902 H HB3  . LYS   A 1 90  ? 29.574 -3.927  16.468  1.00 23.97 ?  90  LYS   A HB3  1 
ATOM   1903 H HG2  . LYS   A 1 90  ? 31.805 -3.501  16.551  1.00 28.70 ?  90  LYS   A HG2  1 
ATOM   1904 H HG3  . LYS   A 1 90  ? 31.642 -2.609  17.858  1.00 28.70 ?  90  LYS   A HG3  1 
ATOM   1905 H HD2  . LYS   A 1 90  ? 30.969 -4.619  18.999  1.00 33.42 ?  90  LYS   A HD2  1 
ATOM   1906 H HD3  . LYS   A 1 90  ? 31.472 -5.417  17.718  1.00 33.42 ?  90  LYS   A HD3  1 
ATOM   1907 H HE2  . LYS   A 1 90  ? 33.240 -3.715  19.084  1.00 37.39 ?  90  LYS   A HE2  1 
ATOM   1908 H HE3  . LYS   A 1 90  ? 33.046 -5.213  19.573  1.00 37.39 ?  90  LYS   A HE3  1 
ATOM   1909 H HZ1  . LYS   A 1 90  ? 33.840 -5.899  17.552  1.00 39.95 ?  90  LYS   A HZ1  1 
ATOM   1910 H HZ2  . LYS   A 1 90  ? 34.026 -4.530  17.114  1.00 39.95 ?  90  LYS   A HZ2  1 
ATOM   1911 H HZ3  . LYS   A 1 90  ? 34.835 -5.062  18.192  1.00 39.95 ?  90  LYS   A HZ3  1 
ATOM   1912 N N    . HIS   A 1 91  ? 29.726 -2.391  14.111  1.00 13.76 ?  91  HIS   A N    1 
ATOM   1913 C CA   . HIS   A 1 91  ? 30.286 -2.361  12.776  1.00 13.22 ?  91  HIS   A CA   1 
ATOM   1914 C C    . HIS   A 1 91  ? 29.187 -2.085  11.767  1.00 12.02 ?  91  HIS   A C    1 
ATOM   1915 O O    . HIS   A 1 91  ? 28.024 -2.455  11.968  1.00 13.56 ?  91  HIS   A O    1 
ATOM   1916 C CB   . HIS   A 1 91  ? 30.895 -3.719  12.384  1.00 16.00 ?  91  HIS   A CB   1 
ATOM   1917 C CG   . HIS   A 1 91  ? 31.913 -4.232  13.352  1.00 20.43 ?  91  HIS   A CG   1 
ATOM   1918 N ND1  . HIS   A 1 91  ? 33.186 -3.712  13.440  1.00 22.49 ?  91  HIS   A ND1  1 
ATOM   1919 C CD2  . HIS   A 1 91  ? 31.850 -5.227  14.267  1.00 22.13 ?  91  HIS   A CD2  1 
ATOM   1920 C CE1  . HIS   A 1 91  ? 33.863 -4.363  14.369  1.00 23.36 ?  91  HIS   A CE1  1 
ATOM   1921 N NE2  . HIS   A 1 91  ? 33.074 -5.288  14.887  1.00 23.29 ?  91  HIS   A NE2  1 
ATOM   1922 H H    . HIS   A 1 91  ? 29.054 -2.940  14.181  1.00 16.52 ?  91  HIS   A H    1 
ATOM   1923 H HA   . HIS   A 1 91  ? 30.969 -1.683  12.710  1.00 15.87 ?  91  HIS   A HA   1 
ATOM   1924 H HB2  . HIS   A 1 91  ? 30.189 -4.384  12.329  1.00 19.21 ?  91  HIS   A HB2  1 
ATOM   1925 H HB3  . HIS   A 1 91  ? 31.332 -3.635  11.521  1.00 19.21 ?  91  HIS   A HB3  1 
ATOM   1926 H HD1  . HIS   A 1 91  ? 33.495 -3.068  12.960  1.00 27.00 ?  91  HIS   A HD1  1 
ATOM   1927 H HD2  . HIS   A 1 91  ? 31.121 -5.772  14.448  1.00 26.57 ?  91  HIS   A HD2  1 
ATOM   1928 H HE1  . HIS   A 1 91  ? 34.749 -4.194  14.618  1.00 28.04 ?  91  HIS   A HE1  1 
ATOM   1929 N N    . CYS   A 1 92  ? 29.580 -1.471  10.659  1.00 12.06 ?  92  CYS   A N    1 
ATOM   1930 C CA   . CYS   A 1 92  ? 28.741 -1.399  9.472   1.00 12.00 ?  92  CYS   A CA   1 
ATOM   1931 C C    . CYS   A 1 92  ? 29.382 -2.222  8.368   1.00 11.58 ?  92  CYS   A C    1 
ATOM   1932 O O    . CYS   A 1 92  ? 30.539 -1.976  8.000   1.00 12.41 ?  92  CYS   A O    1 
ATOM   1933 C CB   . CYS   A 1 92  ? 28.542 0.043   9.006   1.00 12.66 ?  92  CYS   A CB   1 
ATOM   1934 S SG   . CYS   A 1 92  ? 27.506 0.155   7.522   1.00 12.10 ?  92  CYS   A SG   1 
ATOM   1935 H H    . CYS   A 1 92  ? 30.338 -1.069  10.572  1.00 14.48 ?  92  CYS   A H    1 
ATOM   1936 H HA   . CYS   A 1 92  ? 27.873 -1.777  9.668   1.00 14.41 ?  92  CYS   A HA   1 
ATOM   1937 H HB2  . CYS   A 1 92  ? 28.108 0.549   9.714   1.00 15.20 ?  92  CYS   A HB2  1 
ATOM   1938 H HB3  . CYS   A 1 92  ? 29.404 0.435   8.800   1.00 15.20 ?  92  CYS   A HB3  1 
ATOM   1939 H HG   . CYS   A 1 92  ? 27.380 1.308   7.228   1.00 14.53 ?  92  CYS   A HG   1 
ATOM   1940 N N    . LEU   A 1 93  ? 28.642 -3.197  7.858   1.00 11.58 ?  93  LEU   A N    1 
ATOM   1941 C CA   . LEU   A 1 93  ? 29.046 -3.953  6.680   1.00 11.13 ?  93  LEU   A CA   1 
ATOM   1942 C C    . LEU   A 1 93  ? 28.448 -3.261  5.463   1.00 10.87 ?  93  LEU   A C    1 
ATOM   1943 O O    . LEU   A 1 93  ? 27.233 -3.316  5.248   1.00 11.24 ?  93  LEU   A O    1 
ATOM   1944 C CB   . LEU   A 1 93  ? 28.568 -5.399  6.790   1.00 11.77 ?  93  LEU   A CB   1 
ATOM   1945 C CG   . LEU   A 1 93  ? 28.943 -6.292  5.614   1.00 11.81 ?  93  LEU   A CG   1 
ATOM   1946 C CD1  . LEU   A 1 93  ? 30.447 -6.556  5.591   1.00 13.05 ?  93  LEU   A CD1  1 
ATOM   1947 C CD2  . LEU   A 1 93  ? 28.182 -7.609  5.660   1.00 12.67 ?  93  LEU   A CD2  1 
ATOM   1948 H H    . LEU   A 1 93  ? 27.883 -3.435  8.183   1.00 13.91 ?  93  LEU   A H    1 
ATOM   1949 H HA   . LEU   A 1 93  ? 30.011 -3.943  6.606   1.00 13.37 ?  93  LEU   A HA   1 
ATOM   1950 H HB2  . LEU   A 1 93  ? 28.952 -5.788  7.592   1.00 14.13 ?  93  LEU   A HB2  1 
ATOM   1951 H HB3  . LEU   A 1 93  ? 27.601 -5.399  6.860   1.00 14.13 ?  93  LEU   A HB3  1 
ATOM   1952 H HG   . LEU   A 1 93  ? 28.714 -5.849  4.789   1.00 14.18 ?  93  LEU   A HG   1 
ATOM   1953 H HD11 . LEU   A 1 93  ? 30.657 -7.167  4.869   1.00 15.66 ?  93  LEU   A HD11 1 
ATOM   1954 H HD12 . LEU   A 1 93  ? 30.918 -5.717  5.463   1.00 15.66 ?  93  LEU   A HD12 1 
ATOM   1955 H HD13 . LEU   A 1 93  ? 30.716 -6.953  6.442   1.00 15.66 ?  93  LEU   A HD13 1 
ATOM   1956 H HD21 . LEU   A 1 93  ? 28.448 -8.158  4.901   1.00 15.22 ?  93  LEU   A HD21 1 
ATOM   1957 H HD22 . LEU   A 1 93  ? 28.393 -8.075  6.486   1.00 15.22 ?  93  LEU   A HD22 1 
ATOM   1958 H HD23 . LEU   A 1 93  ? 27.231 -7.430  5.616   1.00 15.22 ?  93  LEU   A HD23 1 
ATOM   1959 N N    . HIS   A 1 94  ? 29.292 -2.568  4.702   1.00 10.49 ?  94  HIS   A N    1 
ATOM   1960 C CA   . HIS   A 1 94  ? 28.864 -1.894  3.481   1.00 10.63 ?  94  HIS   A CA   1 
ATOM   1961 C C    . HIS   A 1 94  ? 28.869 -2.924  2.370   1.00 10.56 ?  94  HIS   A C    1 
ATOM   1962 O O    . HIS   A 1 94  ? 29.932 -3.437  2.016   1.00 12.05 ?  94  HIS   A O    1 
ATOM   1963 C CB   . HIS   A 1 94  ? 29.813 -0.747  3.142   1.00 10.76 ?  94  HIS   A CB   1 
ATOM   1964 C CG   . HIS   A 1 94  ? 29.811 0.347   4.155   1.00 10.86 ?  94  HIS   A CG   1 
ATOM   1965 N ND1  . HIS   A 1 94  ? 28.930 1.405   4.109   1.00 11.06 ?  94  HIS   A ND1  1 
ATOM   1966 C CD2  . HIS   A 1 94  ? 30.550 0.511   5.274   1.00 11.61 ?  94  HIS   A CD2  1 
ATOM   1967 C CE1  . HIS   A 1 94  ? 29.152 2.187   5.150   1.00 11.34 ?  94  HIS   A CE1  1 
ATOM   1968 N NE2  . HIS   A 1 94  ? 30.127 1.667   5.873   1.00 11.49 ?  94  HIS   A NE2  1 
ATOM   1969 H H    . HIS   A 1 94  ? 30.131 -2.464  4.876   1.00 12.60 ?  94  HIS   A H    1 
ATOM   1970 H HA   . HIS   A 1 94  ? 27.963 -1.545  3.588   1.00 12.76 ?  94  HIS   A HA   1 
ATOM   1971 H HB2  . HIS   A 1 94  ? 30.712 -1.093  3.081   1.00 12.93 ?  94  HIS   A HB2  1 
ATOM   1972 H HB3  . HIS   A 1 94  ? 29.544 -0.361  2.292   1.00 12.93 ?  94  HIS   A HB3  1 
ATOM   1973 H HD2  . HIS   A 1 94  ? 31.227 -0.047  5.576   1.00 13.94 ?  94  HIS   A HD2  1 
ATOM   1974 H HE1  . HIS   A 1 94  ? 28.688 2.972   5.343   1.00 13.62 ?  94  HIS   A HE1  1 
ATOM   1975 H HE2  . HIS   A 1 94  ? 30.446 2.009   6.596   1.00 13.80 ?  94  HIS   A HE2  1 
ATOM   1976 N N    . VAL   A 1 95  ? 27.699 -3.242  1.827   1.00 10.08 ?  95  VAL   A N    1 
ATOM   1977 C CA   . VAL   A 1 95  ? 27.553 -4.275  0.806   1.00 10.58 ?  95  VAL   A CA   1 
ATOM   1978 C C    . VAL   A 1 95  ? 27.010 -3.632  -0.458  1.00 10.12 ?  95  VAL   A C    1 
ATOM   1979 O O    . VAL   A 1 95  ? 26.009 -2.904  -0.409  1.00 11.04 ?  95  VAL   A O    1 
ATOM   1980 C CB   . VAL   A 1 95  ? 26.623 -5.415  1.255   1.00 11.13 ?  95  VAL   A CB   1 
ATOM   1981 C CG1  . VAL   A 1 95  ? 26.516 -6.454  0.148   1.00 12.12 ?  95  VAL   A CG1  1 
ATOM   1982 C CG2  . VAL   A 1 95  ? 27.128 -6.038  2.530   1.00 11.57 ?  95  VAL   A CG2  1 
ATOM   1983 H H    . VAL   A 1 95  ? 26.953 -2.871  2.042   1.00 12.11 ?  95  VAL   A H    1 
ATOM   1984 H HA   . VAL   A 1 95  ? 28.422 -4.655  0.601   1.00 12.71 ?  95  VAL   A HA   1 
ATOM   1985 H HB   . VAL   A 1 95  ? 25.737 -5.059  1.417   1.00 13.36 ?  95  VAL   A HB   1 
ATOM   1986 H HG11 . VAL   A 1 95  ? 26.124 -7.266  0.509   1.00 14.55 ?  95  VAL   A HG11 1 
ATOM   1987 H HG12 . VAL   A 1 95  ? 25.956 -6.111  -0.567  1.00 14.55 ?  95  VAL   A HG12 1 
ATOM   1988 H HG13 . VAL   A 1 95  ? 27.405 -6.649  -0.196  1.00 14.55 ?  95  VAL   A HG13 1 
ATOM   1989 H HG21 . VAL   A 1 95  ? 26.563 -6.799  2.753   1.00 13.90 ?  95  VAL   A HG21 1 
ATOM   1990 H HG22 . VAL   A 1 95  ? 28.041 -6.333  2.400   1.00 13.90 ?  95  VAL   A HG22 1 
ATOM   1991 H HG23 . VAL   A 1 95  ? 27.086 -5.379  3.239   1.00 13.90 ?  95  VAL   A HG23 1 
ATOM   1992 N N    . VAL   A 1 96  ? 27.633 -3.926  -1.593  1.00 10.18 ?  96  VAL   A N    1 
ATOM   1993 C CA   . VAL   A 1 96  ? 27.226 -3.368  -2.871  1.00 10.79 ?  96  VAL   A CA   1 
ATOM   1994 C C    . VAL   A 1 96  ? 26.414 -4.409  -3.629  1.00 11.35 ?  96  VAL   A C    1 
ATOM   1995 O O    . VAL   A 1 96  ? 26.966 -5.352  -4.205  1.00 12.27 ?  96  VAL   A O    1 
ATOM   1996 C CB   . VAL   A 1 96  ? 28.419 -2.893  -3.695  1.00 11.45 ?  96  VAL   A CB   1 
ATOM   1997 C CG1  . VAL   A 1 96  ? 27.917 -2.255  -4.974  1.00 11.56 ?  96  VAL   A CG1  1 
ATOM   1998 C CG2  . VAL   A 1 96  ? 29.281 -1.921  -2.894  1.00 12.38 ?  96  VAL   A CG2  1 
ATOM   1999 H H    . VAL   A 1 96  ? 28.307 -4.462  -1.644  1.00 12.23 ?  96  VAL   A H    1 
ATOM   2000 H HA   . VAL   A 1 96  ? 26.655 -2.602  -2.710  1.00 12.95 ?  96  VAL   A HA   1 
ATOM   2001 H HB   . VAL   A 1 96  ? 28.969 -3.652  -3.933  1.00 13.74 ?  96  VAL   A HB   1 
ATOM   2002 H HG11 . VAL   A 1 96  ? 28.655 -1.776  -5.393  1.00 13.88 ?  96  VAL   A HG11 1 
ATOM   2003 H HG12 . VAL   A 1 96  ? 27.592 -2.941  -5.568  1.00 13.88 ?  96  VAL   A HG12 1 
ATOM   2004 H HG13 . VAL   A 1 96  ? 27.208 -1.629  -4.758  1.00 13.88 ?  96  VAL   A HG13 1 
ATOM   2005 H HG21 . VAL   A 1 96  ? 29.987 -1.576  -3.461  1.00 14.87 ?  96  VAL   A HG21 1 
ATOM   2006 H HG22 . VAL   A 1 96  ? 28.723 -1.186  -2.581  1.00 14.87 ?  96  VAL   A HG22 1 
ATOM   2007 H HG23 . VAL   A 1 96  ? 29.663 -2.386  -2.133  1.00 14.87 ?  96  VAL   A HG23 1 
ATOM   2008 N N    A GLY   A 1 97  ? 25.098 -4.245  -3.646  0.86 11.11 ?  97  GLY   A N    1 
ATOM   2009 N N    B GLY   A 1 97  ? 25.095 -4.234  -3.630  0.14 11.85 ?  97  GLY   A N    1 
ATOM   2010 C CA   A GLY   A 1 97  ? 24.275 -5.006  -4.551  0.86 11.68 ?  97  GLY   A CA   1 
ATOM   2011 C CA   B GLY   A 1 97  ? 24.233 -4.998  -4.494  0.14 12.56 ?  97  GLY   A CA   1 
ATOM   2012 C C    A GLY   A 1 97  ? 24.284 -4.355  -5.920  0.86 11.49 ?  97  GLY   A C    1 
ATOM   2013 C C    B GLY   A 1 97  ? 24.144 -4.351  -5.860  0.14 13.25 ?  97  GLY   A C    1 
ATOM   2014 O O    A GLY   A 1 97  ? 24.585 -3.162  -6.055  0.86 12.84 ?  97  GLY   A O    1 
ATOM   2015 O O    B GLY   A 1 97  ? 24.368 -3.146  -6.014  0.14 13.22 ?  97  GLY   A O    1 
ATOM   2016 H H    A GLY   A 1 97  ? 24.663 -3.701  -3.135  0.86 13.35 ?  97  GLY   A H    1 
ATOM   2017 H H    B GLY   A 1 97  ? 24.677 -3.670  -3.128  0.14 14.23 ?  97  GLY   A H    1 
ATOM   2018 H HA2  A GLY   A 1 97  ? 24.619 -5.909  -4.621  0.86 14.03 ?  97  GLY   A HA2  1 
ATOM   2019 H HA2  B GLY   A 1 97  ? 24.582 -5.897  -4.584  0.14 15.08 ?  97  GLY   A HA2  1 
ATOM   2020 H HA3  A GLY   A 1 97  ? 23.363 -5.040  -4.218  0.86 14.03 ?  97  GLY   A HA3  1 
ATOM   2021 H HA3  B GLY   A 1 97  ? 23.340 -5.042  -4.118  0.14 15.08 ?  97  GLY   A HA3  1 
ATOM   2022 N N    A PRO   A 1 98  ? 23.958 -5.108  -6.966  0.86 11.46 ?  98  PRO   A N    1 
ATOM   2023 N N    B PRO   A 1 98  ? 23.808 -5.135  -6.880  0.14 14.00 ?  98  PRO   A N    1 
ATOM   2024 C CA   A PRO   A 1 98  ? 23.845 -4.500  -8.295  0.86 12.97 ?  98  PRO   A CA   1 
ATOM   2025 C CA   B PRO   A 1 98  ? 23.712 -4.573  -8.232  0.14 14.69 ?  98  PRO   A CA   1 
ATOM   2026 C C    A PRO   A 1 98  ? 22.729 -3.464  -8.340  0.86 12.93 ?  98  PRO   A C    1 
ATOM   2027 C C    B PRO   A 1 98  ? 22.598 -3.543  -8.327  0.14 15.40 ?  98  PRO   A C    1 
ATOM   2028 O O    A PRO   A 1 98  ? 21.656 -3.649  -7.766  0.86 13.04 ?  98  PRO   A O    1 
ATOM   2029 O O    B PRO   A 1 98  ? 21.505 -3.728  -7.789  0.14 15.43 ?  98  PRO   A O    1 
ATOM   2030 C CB   A PRO   A 1 98  ? 23.537 -5.698  -9.203  0.86 13.28 ?  98  PRO   A CB   1 
ATOM   2031 C CB   B PRO   A 1 98  ? 23.414 -5.799  -9.102  0.14 14.62 ?  98  PRO   A CB   1 
ATOM   2032 C CG   A PRO   A 1 98  ? 22.873 -6.693  -8.289  0.86 13.48 ?  98  PRO   A CG   1 
ATOM   2033 C CG   B PRO   A 1 98  ? 22.774 -6.773  -8.169  0.14 14.45 ?  98  PRO   A CG   1 
ATOM   2034 C CD   A PRO   A 1 98  ? 23.625 -6.544  -6.986  0.86 12.10 ?  98  PRO   A CD   1 
ATOM   2035 C CD   B PRO   A 1 98  ? 23.459 -6.564  -6.851  0.14 14.17 ?  98  PRO   A CD   1 
ATOM   2036 H HA   A PRO   A 1 98  ? 24.688 -4.093  -8.559  0.86 15.57 ?  98  PRO   A HA   1 
ATOM   2037 H HA   B PRO   A 1 98  ? 24.555 -4.172  -8.502  0.14 17.63 ?  98  PRO   A HA   1 
ATOM   2038 H HB2  A PRO   A 1 98  ? 22.931 -5.420  -9.908  0.86 15.95 ?  98  PRO   A HB2  1 
ATOM   2039 H HB2  B PRO   A 1 98  ? 22.804 -5.552  -9.816  0.14 17.55 ?  98  PRO   A HB2  1 
ATOM   2040 H HB3  A PRO   A 1 98  ? 24.356 -6.057  -9.566  0.86 15.95 ?  98  PRO   A HB3  1 
ATOM   2041 H HB3  B PRO   A 1 98  ? 24.240 -6.154  -9.461  0.14 17.55 ?  98  PRO   A HB3  1 
ATOM   2042 H HG2  A PRO   A 1 98  ? 21.934 -6.462  -8.174  0.86 16.19 ?  98  PRO   A HG2  1 
ATOM   2043 H HG2  B PRO   A 1 98  ? 21.825 -6.579  -8.096  0.14 17.35 ?  98  PRO   A HG2  1 
ATOM   2044 H HG3  A PRO   A 1 98  ? 22.969 -7.586  -8.646  0.86 16.19 ?  98  PRO   A HG3  1 
ATOM   2045 H HG3  B PRO   A 1 98  ? 22.917 -7.674  -8.491  0.14 17.35 ?  98  PRO   A HG3  1 
ATOM   2046 H HD2  A PRO   A 1 98  ? 23.052 -6.770  -6.233  0.86 14.53 ?  98  PRO   A HD2  1 
ATOM   2047 H HD2  B PRO   A 1 98  ? 22.852 -6.750  -6.117  0.14 17.01 ?  98  PRO   A HD2  1 
ATOM   2048 H HD3  A PRO   A 1 98  ? 24.431 -7.083  -6.993  0.86 14.53 ?  98  PRO   A HD3  1 
ATOM   2049 H HD3  B PRO   A 1 98  ? 24.263 -7.103  -6.795  0.14 17.01 ?  98  PRO   A HD3  1 
ATOM   2050 N N    A ASN   A 1 99  ? 22.996 -2.359  -9.026  0.86 14.22 ?  99  ASN   A N    1 
ATOM   2051 N N    B ASN   A 1 99  ? 22.888 -2.448  -9.022  0.14 16.34 ?  99  ASN   A N    1 
ATOM   2052 C CA   A ASN   A 1 99  ? 22.016 -1.297  -9.236  0.86 15.12 ?  99  ASN   A CA   1 
ATOM   2053 C CA   B ASN   A 1 99  ? 21.904 -1.412  -9.306  0.14 17.45 ?  99  ASN   A CA   1 
ATOM   2054 C C    A ASN   A 1 99  ? 21.445 -1.459  -10.641 0.86 16.61 ?  99  ASN   A C    1 
ATOM   2055 C C    B ASN   A 1 99  ? 21.359 -1.675  -10.705 0.14 18.63 ?  99  ASN   A C    1 
ATOM   2056 O O    A ASN   A 1 99  ? 22.135 -1.212  -11.635 0.86 17.99 ?  99  ASN   A O    1 
ATOM   2057 O O    B ASN   A 1 99  ? 22.080 -1.533  -11.698 0.14 18.67 ?  99  ASN   A O    1 
ATOM   2058 C CB   A ASN   A 1 99  ? 22.659 0.078   -9.043  0.86 16.00 ?  99  ASN   A CB   1 
ATOM   2059 C CB   B ASN   A 1 99  ? 22.539 -0.027  -9.203  0.14 17.59 ?  99  ASN   A CB   1 
ATOM   2060 C CG   A ASN   A 1 99  ? 21.640 1.220   -9.064  0.86 17.04 ?  99  ASN   A CG   1 
ATOM   2061 C CG   B ASN   A 1 99  ? 21.509 1.085   -9.118  0.14 17.79 ?  99  ASN   A CG   1 
ATOM   2062 O OD1  A ASN   A 1 99  ? 20.637 1.163   -9.780  0.86 18.17 ?  99  ASN   A OD1  1 
ATOM   2063 O OD1  B ASN   A 1 99  ? 20.504 1.075   -9.831  0.14 17.82 ?  99  ASN   A OD1  1 
ATOM   2064 N ND2  A ASN   A 1 99  ? 21.906 2.266   -8.279  0.86 17.55 ?  99  ASN   A ND2  1 
ATOM   2065 N ND2  B ASN   A 1 99  ? 21.752 2.050   -8.236  0.14 17.93 ?  99  ASN   A ND2  1 
ATOM   2066 H H    A ASN   A 1 99  ? 23.765 -2.187  -9.369  0.86 17.08 ?  99  ASN   A H    1 
ATOM   2067 H H    B ASN   A 1 99  ? 23.667 -2.278  -9.345  0.14 19.62 ?  99  ASN   A H    1 
ATOM   2068 H HA   A ASN   A 1 99  ? 21.297 -1.387  -8.580  0.86 18.15 ?  99  ASN   A HA   1 
ATOM   2069 H HA   B ASN   A 1 99  ? 21.173 -1.467  -8.671  0.14 20.95 ?  99  ASN   A HA   1 
ATOM   2070 H HB2  A ASN   A 1 99  ? 23.125 0.105   -8.189  0.86 19.21 ?  99  ASN   A HB2  1 
ATOM   2071 H HB2  B ASN   A 1 99  ? 23.087 0.011   -8.403  0.14 21.12 ?  99  ASN   A HB2  1 
ATOM   2072 H HB3  A ASN   A 1 99  ? 23.289 0.234   -9.764  0.86 19.21 ?  99  ASN   A HB3  1 
ATOM   2073 H HB3  B ASN   A 1 99  ? 23.088 0.129   -9.986  0.14 21.12 ?  99  ASN   A HB3  1 
ATOM   2074 H HD21 A ASN   A 1 99  ? 21.369 2.936   -8.249  0.86 21.06 ?  99  ASN   A HD21 1 
ATOM   2075 H HD21 B ASN   A 1 99  ? 21.199 2.703   -8.148  0.14 21.53 ?  99  ASN   A HD21 1 
ATOM   2076 H HD22 A ASN   A 1 99  ? 22.624 2.273   -7.796  0.86 21.06 ?  99  ASN   A HD22 1 
ATOM   2077 H HD22 B ASN   A 1 99  ? 22.463 2.022   -7.752  0.14 21.53 ?  99  ASN   A HD22 1 
ATOM   2078 N N    A VAL   A 1 100 ? 20.181 -1.889  -10.713 0.86 17.37 ?  100 VAL   A N    1 
ATOM   2079 N N    B VAL   A 1 100 ? 20.090 -2.083  -10.778 0.14 19.80 ?  100 VAL   A N    1 
ATOM   2080 C CA   A VAL   A 1 100 ? 19.537 -2.120  -12.001 0.86 19.50 ?  100 VAL   A CA   1 
ATOM   2081 C CA   B VAL   A 1 100 ? 19.479 -2.386  -12.069 0.14 21.20 ?  100 VAL   A CA   1 
ATOM   2082 C C    A VAL   A 1 100 ? 19.418 -0.824  -12.787 0.86 20.14 ?  100 VAL   A C    1 
ATOM   2083 C C    B VAL   A 1 100 ? 19.409 -1.138  -12.934 0.14 22.32 ?  100 VAL   A C    1 
ATOM   2084 O O    A VAL   A 1 100 ? 19.461 -0.833  -14.023 0.86 21.93 ?  100 VAL   A O    1 
ATOM   2085 O O    B VAL   A 1 100 ? 19.540 -1.214  -14.163 0.14 22.70 ?  100 VAL   A O    1 
ATOM   2086 C CB   A VAL   A 1 100 ? 18.176 -2.818  -11.796 0.86 21.13 ?  100 VAL   A CB   1 
ATOM   2087 C CB   B VAL   A 1 100 ? 18.090 -3.022  -11.864 0.14 21.57 ?  100 VAL   A CB   1 
ATOM   2088 C CG1  A VAL   A 1 100 ? 17.421 -2.943  -13.114 0.86 21.90 ?  100 VAL   A CG1  1 
ATOM   2089 C CG1  B VAL   A 1 100 ? 17.474 -3.407  -13.201 0.14 21.74 ?  100 VAL   A CG1  1 
ATOM   2090 C CG2  A VAL   A 1 100 ? 18.388 -4.186  -11.172 0.86 22.07 ?  100 VAL   A CG2  1 
ATOM   2091 C CG2  B VAL   A 1 100 ? 18.197 -4.231  -10.952 0.14 21.79 ?  100 VAL   A CG2  1 
ATOM   2092 H H    A VAL   A 1 100 ? 19.677 -2.050  -10.027 0.86 20.85 ?  100 VAL   A H    1 
ATOM   2093 H H    B VAL   A 1 100 ? 19.572 -2.189  -10.102 0.14 23.76 ?  100 VAL   A H    1 
ATOM   2094 H HA   A VAL   A 1 100 ? 20.095 -2.714  -12.516 0.86 23.41 ?  100 VAL   A HA   1 
ATOM   2095 H HA   B VAL   A 1 100 ? 20.032 -3.034  -12.531 0.14 25.45 ?  100 VAL   A HA   1 
ATOM   2096 H HB   A VAL   A 1 100 ? 17.635 -2.290  -11.189 0.86 25.36 ?  100 VAL   A HB   1 
ATOM   2097 H HB   B VAL   A 1 100 ? 17.505 -2.375  -11.440 0.14 25.90 ?  100 VAL   A HB   1 
ATOM   2098 H HG11 A VAL   A 1 100 ? 16.678 -3.556  -12.993 0.86 26.29 ?  100 VAL   A HG11 1 
ATOM   2099 H HG11 B VAL   A 1 100 ? 16.670 -3.924  -13.039 0.14 26.10 ?  100 VAL   A HG11 1 
ATOM   2100 H HG12 A VAL   A 1 100 ? 17.087 -2.071  -13.376 0.86 26.29 ?  100 VAL   A HG12 1 
ATOM   2101 H HG12 B VAL   A 1 100 ? 17.254 -2.601  -13.694 0.14 26.10 ?  100 VAL   A HG12 1 
ATOM   2102 H HG13 A VAL   A 1 100 ? 18.023 -3.287  -13.793 0.86 26.29 ?  100 VAL   A HG13 1 
ATOM   2103 H HG13 B VAL   A 1 100 ? 18.113 -3.939  -13.701 0.14 26.10 ?  100 VAL   A HG13 1 
ATOM   2104 H HG21 A VAL   A 1 100 ? 17.530 -4.629  -11.089 0.86 26.49 ?  100 VAL   A HG21 1 
ATOM   2105 H HG21 B VAL   A 1 100 ? 17.352 -4.704  -10.956 0.14 26.16 ?  100 VAL   A HG21 1 
ATOM   2106 H HG22 A VAL   A 1 100 ? 18.975 -4.705  -11.744 0.86 26.49 ?  100 VAL   A HG22 1 
ATOM   2107 H HG22 B VAL   A 1 100 ? 18.903 -4.810  -11.281 0.14 26.16 ?  100 VAL   A HG22 1 
ATOM   2108 H HG23 A VAL   A 1 100 ? 18.791 -4.075  -10.297 0.86 26.49 ?  100 VAL   A HG23 1 
ATOM   2109 H HG23 B VAL   A 1 100 ? 18.407 -3.933  -10.054 0.14 26.16 ?  100 VAL   A HG23 1 
ATOM   2110 N N    A ASN   A 1 101 ? 19.264 0.307   -12.101 0.86 21.71 ?  101 ASN   A N    1 
ATOM   2111 N N    B ASN   A 1 101 ? 19.201 0.025   -12.316 0.14 23.16 ?  101 ASN   A N    1 
ATOM   2112 C CA   A ASN   A 1 101 ? 19.213 1.586   -12.800 0.86 23.59 ?  101 ASN   A CA   1 
ATOM   2113 C CA   B ASN   A 1 101 ? 19.153 1.270   -13.074 0.14 23.96 ?  101 ASN   A CA   1 
ATOM   2114 C C    A ASN   A 1 101 ? 20.574 2.013   -13.354 0.86 25.38 ?  101 ASN   A C    1 
ATOM   2115 C C    B ASN   A 1 101 ? 20.506 1.595   -13.694 0.14 24.93 ?  101 ASN   A C    1 
ATOM   2116 O O    A ASN   A 1 101 ? 20.656 3.074   -13.988 0.86 27.49 ?  101 ASN   A O    1 
ATOM   2117 O O    B ASN   A 1 101 ? 20.564 2.210   -14.764 0.14 24.75 ?  101 ASN   A O    1 
ATOM   2118 C CB   A ASN   A 1 101 ? 18.588 2.641   -11.883 0.86 23.53 ?  101 ASN   A CB   1 
ATOM   2119 C CB   B ASN   A 1 101 ? 18.670 2.404   -12.170 0.14 23.77 ?  101 ASN   A CB   1 
ATOM   2120 C CG   A ASN   A 1 101 ? 17.200 2.229   -11.392 0.86 23.12 ?  101 ASN   A CG   1 
ATOM   2121 C CG   B ASN   A 1 101 ? 17.397 2.048   -11.423 0.14 23.48 ?  101 ASN   A CG   1 
ATOM   2122 O OD1  A ASN   A 1 101 ? 16.372 1.744   -12.169 0.86 23.79 ?  101 ASN   A OD1  1 
ATOM   2123 O OD1  B ASN   A 1 101 ? 16.490 1.427   -11.979 0.14 23.31 ?  101 ASN   A OD1  1 
ATOM   2124 N ND2  A ASN   A 1 101 ? 16.949 2.400   -10.099 0.86 22.69 ?  101 ASN   A ND2  1 
ATOM   2125 N ND2  B ASN   A 1 101 ? 17.329 2.427   -10.153 0.14 23.45 ?  101 ASN   A ND2  1 
ATOM   2126 H H    A ASN   A 1 101 ? 19.176 0.361   -11.245 0.86 26.06 ?  101 ASN   A H    1 
ATOM   2127 H H    B ASN   A 1 101 ? 19.087 0.115   -11.470 0.14 27.81 ?  101 ASN   A H    1 
ATOM   2128 H HA   A ASN   A 1 101 ? 18.625 1.492   -13.559 0.86 28.32 ?  101 ASN   A HA   1 
ATOM   2129 H HA   B ASN   A 1 101 ? 18.517 1.176   -13.795 0.14 28.77 ?  101 ASN   A HA   1 
ATOM   2130 H HB2  A ASN   A 1 101 ? 19.154 2.776   -11.109 0.86 28.24 ?  101 ASN   A HB2  1 
ATOM   2131 H HB2  B ASN   A 1 101 ? 19.355 2.606   -11.514 0.14 28.53 ?  101 ASN   A HB2  1 
ATOM   2132 H HB3  A ASN   A 1 101 ? 18.499 3.479   -12.377 0.86 28.24 ?  101 ASN   A HB3  1 
ATOM   2133 H HB3  B ASN   A 1 101 ? 18.487 3.188   -12.713 0.14 28.53 ?  101 ASN   A HB3  1 
ATOM   2134 H HD21 A ASN   A 1 101 ? 16.180 2.188   -9.779  0.86 27.24 ?  101 ASN   A HD21 1 
ATOM   2135 H HD21 B ASN   A 1 101 ? 16.629 2.245   -9.687  0.14 28.15 ?  101 ASN   A HD21 1 
ATOM   2136 H HD22 A ASN   A 1 101 ? 17.550 2.738   -9.585  0.86 27.24 ?  101 ASN   A HD22 1 
ATOM   2137 H HD22 B ASN   A 1 101 ? 17.983 2.857   -9.797  0.14 28.15 ?  101 ASN   A HD22 1 
ATOM   2138 N N    A LYS   A 1 102 ? 21.621 1.202   -13.154 0.86 27.11 ?  102 LYS   A N    1 
ATOM   2139 N N    B LYS   A 1 102 ? 21.597 1.182   -13.048 0.14 26.03 ?  102 LYS   A N    1 
ATOM   2140 C CA   A LYS   A 1 102 ? 22.914 1.374   -13.807 0.86 28.39 ?  102 LYS   A CA   1 
ATOM   2141 C CA   B LYS   A 1 102 ? 22.933 1.328   -13.609 0.14 27.03 ?  102 LYS   A CA   1 
ATOM   2142 C C    A LYS   A 1 102 ? 23.227 0.255   -14.793 0.86 28.83 ?  102 LYS   A C    1 
ATOM   2143 C C    B LYS   A 1 102 ? 23.302 0.186   -14.547 0.14 27.42 ?  102 LYS   A C    1 
ATOM   2144 O O    A LYS   A 1 102 ? 24.316 0.251   -15.375 0.86 29.55 ?  102 LYS   A O    1 
ATOM   2145 O O    B LYS   A 1 102 ? 24.415 0.181   -15.083 0.14 27.62 ?  102 LYS   A O    1 
ATOM   2146 C CB   A LYS   A 1 102 ? 24.043 1.435   -12.768 0.86 30.24 ?  102 LYS   A CB   1 
ATOM   2147 C CB   B LYS   A 1 102 ? 23.974 1.426   -12.488 0.14 27.63 ?  102 LYS   A CB   1 
ATOM   2148 C CG   A LYS   A 1 102 ? 23.924 2.554   -11.753 0.86 31.75 ?  102 LYS   A CG   1 
ATOM   2149 C CG   B LYS   A 1 102 ? 23.847 2.671   -11.622 0.14 28.07 ?  102 LYS   A CG   1 
ATOM   2150 C CD   A LYS   A 1 102 ? 25.106 2.537   -10.789 0.86 33.29 ?  102 LYS   A CD   1 
ATOM   2151 C CD   B LYS   A 1 102 ? 24.819 2.634   -10.451 0.14 28.45 ?  102 LYS   A CD   1 
ATOM   2152 C CE   A LYS   A 1 102 ? 25.002 3.640   -9.746  0.86 34.51 ?  102 LYS   A CE   1 
ATOM   2153 C CE   B LYS   A 1 102 ? 24.734 3.900   -9.615  0.14 28.70 ?  102 LYS   A CE   1 
ATOM   2154 N NZ   A LYS   A 1 102 ? 26.118 3.576   -8.758  0.86 35.19 ?  102 LYS   A NZ   1 
ATOM   2155 N NZ   B LYS   A 1 102 ? 25.580 3.823   -8.391  0.14 28.82 ?  102 LYS   A NZ   1 
ATOM   2156 H H    A LYS   A 1 102 ? 21.599 0.514   -12.635 0.86 32.55 ?  102 LYS   A H    1 
ATOM   2157 H H    B LYS   A 1 102 ? 21.583 0.804   -12.278 0.14 31.24 ?  102 LYS   A H    1 
ATOM   2158 H HA   A LYS   A 1 102 ? 22.911 2.214   -14.289 0.86 34.08 ?  102 LYS   A HA   1 
ATOM   2159 H HA   B LYS   A 1 102 ? 22.970 2.152   -14.115 0.14 32.45 ?  102 LYS   A HA   1 
ATOM   2160 H HB2  A LYS   A 1 102 ? 24.059 0.597   -12.280 0.86 36.30 ?  102 LYS   A HB2  1 
ATOM   2161 H HB2  B LYS   A 1 102 ? 23.888 0.652   -11.911 0.14 33.16 ?  102 LYS   A HB2  1 
ATOM   2162 H HB3  A LYS   A 1 102 ? 24.885 1.554   -13.236 0.86 36.30 ?  102 LYS   A HB3  1 
ATOM   2163 H HB3  B LYS   A 1 102 ? 24.858 1.438   -12.885 0.14 33.16 ?  102 LYS   A HB3  1 
ATOM   2164 H HG2  A LYS   A 1 102 ? 23.913 3.406   -12.214 0.86 38.11 ?  102 LYS   A HG2  1 
ATOM   2165 H HG2  B LYS   A 1 102 ? 24.046 3.456   -12.157 0.14 33.70 ?  102 LYS   A HG2  1 
ATOM   2166 H HG3  A LYS   A 1 102 ? 23.108 2.435   -11.241 0.86 38.11 ?  102 LYS   A HG3  1 
ATOM   2167 H HG3  B LYS   A 1 102 ? 22.946 2.726   -11.266 0.14 33.70 ?  102 LYS   A HG3  1 
ATOM   2168 H HD2  A LYS   A 1 102 ? 25.130 1.684   -10.328 0.86 39.96 ?  102 LYS   A HD2  1 
ATOM   2169 H HD2  B LYS   A 1 102 ? 24.606 1.878   -9.881  0.14 34.14 ?  102 LYS   A HD2  1 
ATOM   2170 H HD3  A LYS   A 1 102 ? 25.927 2.670   -11.290 0.86 39.96 ?  102 LYS   A HD3  1 
ATOM   2171 H HD3  B LYS   A 1 102 ? 25.725 2.553   -10.790 0.14 34.14 ?  102 LYS   A HD3  1 
ATOM   2172 H HE2  A LYS   A 1 102 ? 25.038 4.502   -10.190 0.86 41.41 ?  102 LYS   A HE2  1 
ATOM   2173 H HE2  B LYS   A 1 102 ? 25.039 4.653   -10.146 0.14 34.45 ?  102 LYS   A HE2  1 
ATOM   2174 H HE3  A LYS   A 1 102 ? 24.164 3.546   -9.266  0.86 41.41 ?  102 LYS   A HE3  1 
ATOM   2175 H HE3  B LYS   A 1 102 ? 23.814 4.038   -9.339  0.14 34.45 ?  102 LYS   A HE3  1 
ATOM   2176 H HZ1  A LYS   A 1 102 ? 26.033 4.229   -8.161  0.86 42.23 ?  102 LYS   A HZ1  1 
ATOM   2177 H HZ1  B LYS   A 1 102 ? 25.497 4.571   -7.916  0.14 34.60 ?  102 LYS   A HZ1  1 
ATOM   2178 H HZ2  A LYS   A 1 102 ? 26.104 2.793   -8.334  0.86 42.23 ?  102 LYS   A HZ2  1 
ATOM   2179 H HZ2  B LYS   A 1 102 ? 25.327 3.133   -7.890  0.14 34.60 ?  102 LYS   A HZ2  1 
ATOM   2180 H HZ3  A LYS   A 1 102 ? 26.899 3.664   -9.175  0.86 42.23 ?  102 LYS   A HZ3  1 
ATOM   2181 H HZ3  B LYS   A 1 102 ? 26.434 3.717   -8.618  0.14 34.60 ?  102 LYS   A HZ3  1 
ATOM   2182 N N    A GLY   A 1 103 ? 22.322 -0.703  -14.979 0.86 28.78 ?  103 GLY   A N    1 
ATOM   2183 N N    B GLY   A 1 103 ? 22.405 -0.776  -14.753 0.14 27.55 ?  103 GLY   A N    1 
ATOM   2184 C CA   A GLY   A 1 103 ? 22.545 -1.800  -15.902 0.86 28.53 ?  103 GLY   A CA   1 
ATOM   2185 C CA   B GLY   A 1 103 ? 22.688 -1.886  -15.640 0.14 27.54 ?  103 GLY   A CA   1 
ATOM   2186 C C    A GLY   A 1 103 ? 23.354 -2.957  -15.358 0.86 28.34 ?  103 GLY   A C    1 
ATOM   2187 C C    B GLY   A 1 103 ? 23.615 -2.928  -15.061 0.14 27.55 ?  103 GLY   A C    1 
ATOM   2188 O O    A GLY   A 1 103 ? 23.831 -3.784  -16.141 0.86 29.44 ?  103 GLY   A O    1 
ATOM   2189 O O    B GLY   A 1 103 ? 24.370 -3.560  -15.807 0.14 27.63 ?  103 GLY   A O    1 
ATOM   2190 H H    A GLY   A 1 103 ? 21.569 -0.736  -14.577 0.86 34.54 ?  103 GLY   A H    1 
ATOM   2191 H H    B GLY   A 1 103 ? 21.628 -0.807  -14.387 0.14 33.07 ?  103 GLY   A H    1 
ATOM   2192 H HA2  A GLY   A 1 103 ? 21.684 -2.149  -16.186 0.86 34.25 ?  103 GLY   A HA2  1 
ATOM   2193 H HA2  B GLY   A 1 103 ? 21.853 -2.317  -15.881 0.14 33.05 ?  103 GLY   A HA2  1 
ATOM   2194 H HA3  A GLY   A 1 103 ? 22.999 -1.461  -16.692 0.86 34.25 ?  103 GLY   A HA3  1 
ATOM   2195 H HA3  B GLY   A 1 103 ? 23.097 -1.547  -16.450 0.14 33.05 ?  103 GLY   A HA3  1 
ATOM   2196 N N    A GLU   A 1 104 ? 23.511 -3.057  -14.042 0.86 25.96 ?  104 GLU   A N    1 
ATOM   2197 N N    B GLU   A 1 104 ? 23.582 -3.129  -13.747 0.14 27.34 ?  104 GLU   A N    1 
ATOM   2198 C CA   A GLU   A 1 104 ? 24.395 -4.057  -13.461 0.86 24.37 ?  104 GLU   A CA   1 
ATOM   2199 C CA   B GLU   A 1 104 ? 24.485 -4.059  -13.086 0.14 27.12 ?  104 GLU   A CA   1 
ATOM   2200 C C    A GLU   A 1 104 ? 23.712 -5.420  -13.354 0.86 24.51 ?  104 GLU   A C    1 
ATOM   2201 C C    B GLU   A 1 104 ? 23.835 -5.433  -12.957 0.14 27.35 ?  104 GLU   A C    1 
ATOM   2202 O O    A GLU   A 1 104 ? 22.491 -5.525  -13.204 0.86 24.97 ?  104 GLU   A O    1 
ATOM   2203 O O    B GLU   A 1 104 ? 22.662 -5.551  -12.590 0.14 27.19 ?  104 GLU   A O    1 
ATOM   2204 C CB   A GLU   A 1 104 ? 24.917 -3.570  -12.105 0.86 22.61 ?  104 GLU   A CB   1 
ATOM   2205 C CB   B GLU   A 1 104 ? 24.893 -3.504  -11.719 0.14 26.76 ?  104 GLU   A CB   1 
ATOM   2206 C CG   A GLU   A 1 104 ? 25.855 -2.371  -12.265 0.86 22.03 ?  104 GLU   A CG   1 
ATOM   2207 C CG   B GLU   A 1 104 ? 25.629 -2.169  -11.827 0.14 26.46 ?  104 GLU   A CG   1 
ATOM   2208 C CD   A GLU   A 1 104 ? 26.171 -1.608  -10.985 0.86 21.02 ?  104 GLU   A CD   1 
ATOM   2209 C CD   B GLU   A 1 104 ? 25.888 -1.522  -10.479 0.14 26.29 ?  104 GLU   A CD   1 
ATOM   2210 O OE1  A GLU   A 1 104 ? 25.588 -1.881  -9.919  0.86 19.56 ?  104 GLU   A OE1  1 
ATOM   2211 O OE1  B GLU   A 1 104 ? 25.393 -2.042  -9.458  0.14 26.18 ?  104 GLU   A OE1  1 
ATOM   2212 O OE2  A GLU   A 1 104 ? 27.021 -0.692  -11.075 0.86 21.91 -1 104 GLU   A OE2  1 
ATOM   2213 O OE2  B GLU   A 1 104 ? 26.586 -0.487  -10.443 0.14 26.33 -1 104 GLU   A OE2  1 
ATOM   2214 H H    A GLU   A 1 104 ? 23.118 -2.554  -13.468 0.86 31.17 ?  104 GLU   A H    1 
ATOM   2215 H H    B GLU   A 1 104 ? 23.041 -2.729  -13.210 0.14 32.81 ?  104 GLU   A H    1 
ATOM   2216 H HA   A GLU   A 1 104 ? 25.161 -4.159  -14.045 0.86 29.25 ?  104 GLU   A HA   1 
ATOM   2217 H HA   B GLU   A 1 104 ? 25.290 -4.154  -13.617 0.14 32.55 ?  104 GLU   A HA   1 
ATOM   2218 H HB2  A GLU   A 1 104 ? 24.169 -3.302  -11.552 0.86 27.15 ?  104 GLU   A HB2  1 
ATOM   2219 H HB2  B GLU   A 1 104 ? 24.099 -3.362  -11.180 0.14 32.12 ?  104 GLU   A HB2  1 
ATOM   2220 H HB3  A GLU   A 1 104 ? 25.411 -4.289  -11.680 0.86 27.15 ?  104 GLU   A HB3  1 
ATOM   2221 H HB3  B GLU   A 1 104 ? 25.485 -4.133  -11.278 0.14 32.12 ?  104 GLU   A HB3  1 
ATOM   2222 H HG2  A GLU   A 1 104 ? 26.694 -2.684  -12.637 0.86 26.44 ?  104 GLU   A HG2  1 
ATOM   2223 H HG2  B GLU   A 1 104 ? 26.487 -2.313  -12.259 0.14 31.76 ?  104 GLU   A HG2  1 
ATOM   2224 H HG3  A GLU   A 1 104 ? 25.445 -1.739  -12.876 0.86 26.44 ?  104 GLU   A HG3  1 
ATOM   2225 H HG3  B GLU   A 1 104 ? 25.097 -1.554  -12.359 0.14 31.76 ?  104 GLU   A HG3  1 
ATOM   2226 N N    A ASP   A 1 105 ? 24.533 -6.468  -13.419 0.86 25.13 ?  105 ASP   A N    1 
ATOM   2227 N N    B ASP   A 1 105 ? 24.612 -6.467  -13.274 0.14 27.77 ?  105 ASP   A N    1 
ATOM   2228 C CA   A ASP   A 1 105 ? 24.053 -7.839  -13.560 0.86 26.00 ?  105 ASP   A CA   1 
ATOM   2229 C CA   B ASP   A 1 105 ? 24.118 -7.837  -13.360 0.14 28.14 ?  105 ASP   A CA   1 
ATOM   2230 C C    A ASP   A 1 105 ? 23.364 -8.297  -12.279 0.86 24.08 ?  105 ASP   A C    1 
ATOM   2231 C C    B ASP   A 1 105 ? 23.365 -8.229  -12.096 0.14 27.45 ?  105 ASP   A C    1 
ATOM   2232 O O    A ASP   A 1 105 ? 23.994 -8.373  -11.221 0.86 21.73 ?  105 ASP   A O    1 
ATOM   2233 O O    B ASP   A 1 105 ? 23.919 -8.195  -10.993 0.14 27.37 ?  105 ASP   A O    1 
ATOM   2234 C CB   A ASP   A 1 105 ? 25.246 -8.739  -13.874 0.86 29.11 ?  105 ASP   A CB   1 
ATOM   2235 C CB   B ASP   A 1 105 ? 25.314 -8.768  -13.579 0.14 29.16 ?  105 ASP   A CB   1 
ATOM   2236 C CG   A ASP   A 1 105 ? 24.856 -10.179 -14.096 0.86 31.77 ?  105 ASP   A CG   1 
ATOM   2237 C CG   B ASP   A 1 105 ? 24.902 -10.208 -13.824 0.14 30.03 ?  105 ASP   A CG   1 
ATOM   2238 O OD1  A ASP   A 1 105 ? 23.643 -10.465 -14.156 0.86 32.07 ?  105 ASP   A OD1  1 
ATOM   2239 O OD1  B ASP   A 1 105 ? 23.685 -10.486 -13.868 0.14 30.25 ?  105 ASP   A OD1  1 
ATOM   2240 O OD2  A ASP   A 1 105 ? 25.773 -11.025 -14.211 0.86 33.81 -1 105 ASP   A OD2  1 
ATOM   2241 O OD2  B ASP   A 1 105 ? 25.801 -11.063 -13.972 0.14 30.54 -1 105 ASP   A OD2  1 
ATOM   2242 H H    A ASP   A 1 105 ? 25.391 -6.407  -13.374 0.86 30.16 ?  105 ASP   A H    1 
ATOM   2243 H H    B ASP   A 1 105 ? 25.448 -6.400  -13.447 0.14 33.33 ?  105 ASP   A H    1 
ATOM   2244 H HA   A ASP   A 1 105 ? 23.419 -7.892  -14.289 0.86 31.21 ?  105 ASP   A HA   1 
ATOM   2245 H HA   B ASP   A 1 105 ? 23.518 -7.926  -14.117 0.14 33.78 ?  105 ASP   A HA   1 
ATOM   2246 H HB2  A ASP   A 1 105 ? 25.682 -8.416  -14.679 0.86 34.94 ?  105 ASP   A HB2  1 
ATOM   2247 H HB2  B ASP   A 1 105 ? 25.818 -8.459  -14.352 0.14 35.00 ?  105 ASP   A HB2  1 
ATOM   2248 H HB3  A ASP   A 1 105 ? 25.866 -8.719  -13.130 0.86 34.94 ?  105 ASP   A HB3  1 
ATOM   2249 H HB3  B ASP   A 1 105 ? 25.881 -8.749  -12.792 0.14 35.00 ?  105 ASP   A HB3  1 
ATOM   2250 N N    A ILE   A 1 106 ? 22.076 -8.632  -12.378 0.86 24.18 ?  106 ILE   A N    1 
ATOM   2251 N N    B ILE   A 1 106 ? 22.094 -8.606  -12.263 0.14 26.84 ?  106 ILE   A N    1 
ATOM   2252 C CA   A ILE   A 1 106 ? 21.321 -9.035  -11.198 0.86 23.76 ?  106 ILE   A CA   1 
ATOM   2253 C CA   B ILE   A 1 106 ? 21.284 -9.013  -11.119 0.14 26.22 ?  106 ILE   A CA   1 
ATOM   2254 C C    A ILE   A 1 106 ? 21.870 -10.313 -10.586 0.86 22.86 ?  106 ILE   A C    1 
ATOM   2255 C C    B ILE   A 1 106 ? 21.819 -10.298 -10.502 0.14 25.52 ?  106 ILE   A C    1 
ATOM   2256 O O    A ILE   A 1 106 ? 21.666 -10.556 -9.393  0.86 21.92 ?  106 ILE   A O    1 
ATOM   2257 O O    B ILE   A 1 106 ? 21.616 -10.550 -9.308  0.14 25.38 ?  106 ILE   A O    1 
ATOM   2258 C CB   A ILE   A 1 106 ? 19.811 -9.135  -11.521 0.86 25.43 ?  106 ILE   A CB   1 
ATOM   2259 C CB   B ILE   A 1 106 ? 19.796 -9.125  -11.512 0.14 26.42 ?  106 ILE   A CB   1 
ATOM   2260 C CG1  A ILE   A 1 106 ? 18.980 -9.208  -10.236 0.86 26.12 ?  106 ILE   A CG1  1 
ATOM   2261 C CG1  B ILE   A 1 106 ? 18.914 -9.265  -10.268 0.14 26.48 ?  106 ILE   A CG1  1 
ATOM   2262 C CG2  A ILE   A 1 106 ? 19.524 -10.345 -12.399 0.86 26.21 ?  106 ILE   A CG2  1 
ATOM   2263 C CG2  B ILE   A 1 106 ? 19.569 -10.310 -12.434 0.14 26.55 ?  106 ILE   A CG2  1 
ATOM   2264 C CD1  A ILE   A 1 106 ? 19.087 -7.973  -9.363  0.86 26.66 ?  106 ILE   A CD1  1 
ATOM   2265 C CD1  B ILE   A 1 106 ? 18.981 -8.079  -9.335  0.14 26.49 ?  106 ILE   A CD1  1 
ATOM   2266 H H    A ILE   A 1 106 ? 21.626 -8.628  -13.108 0.86 29.02 ?  106 ILE   A H    1 
ATOM   2267 H H    B ILE   A 1 106 ? 21.683 -8.625  -13.016 0.14 32.22 ?  106 ILE   A H    1 
ATOM   2268 H HA   A ILE   A 1 106 ? 21.428 -8.353  -10.530 0.86 28.52 ?  106 ILE   A HA   1 
ATOM   2269 H HA   B ILE   A 1 106 ? 21.357 -8.326  -10.444 0.14 31.47 ?  106 ILE   A HA   1 
ATOM   2270 H HB   A ILE   A 1 106 ? 19.550 -8.337  -12.007 0.86 30.52 ?  106 ILE   A HB   1 
ATOM   2271 H HB   B ILE   A 1 106 ? 19.538 -8.316  -11.981 0.14 31.71 ?  106 ILE   A HB   1 
ATOM   2272 H HG12 A ILE   A 1 106 ? 18.046 -9.318  -10.473 0.86 31.35 ?  106 ILE   A HG12 1 
ATOM   2273 H HG12 B ILE   A 1 106 ? 17.990 -9.366  -10.548 0.14 31.78 ?  106 ILE   A HG12 1 
ATOM   2274 H HG13 A ILE   A 1 106 ? 19.277 -9.967  -9.711  0.86 31.35 ?  106 ILE   A HG13 1 
ATOM   2275 H HG13 B ILE   A 1 106 ? 19.192 -10.050 -9.770  0.14 31.78 ?  106 ILE   A HG13 1 
ATOM   2276 H HG21 A ILE   A 1 106 ? 18.622 -10.271 -12.749 0.86 31.46 ?  106 ILE   A HG21 1 
ATOM   2277 H HG21 B ILE   A 1 106 ? 18.676 -10.249 -12.810 0.14 31.86 ?  106 ILE   A HG21 1 
ATOM   2278 H HG22 A ILE   A 1 106 ? 20.162 -10.360 -13.128 0.86 31.46 ?  106 ILE   A HG22 1 
ATOM   2279 H HG22 B ILE   A 1 106 ? 20.229 -10.286 -13.143 0.14 31.86 ?  106 ILE   A HG22 1 
ATOM   2280 H HG23 A ILE   A 1 106 ? 19.607 -11.150 -11.866 0.86 31.46 ?  106 ILE   A HG23 1 
ATOM   2281 H HG23 B ILE   A 1 106 ? 19.658 -11.130 -11.924 0.14 31.86 ?  106 ILE   A HG23 1 
ATOM   2282 H HD11 A ILE   A 1 106 ? 18.369 -7.984  -8.713  0.86 32.00 ?  106 ILE   A HD11 1 
ATOM   2283 H HD11 B ILE   A 1 106 ? 18.234 -8.120  -8.720  0.14 31.80 ?  106 ILE   A HD11 1 
ATOM   2284 H HD12 A ILE   A 1 106 ? 19.945 -7.980  -8.907  0.86 32.00 ?  106 ILE   A HD12 1 
ATOM   2285 H HD12 B ILE   A 1 106 ? 19.817 -8.110  -8.843  0.14 31.80 ?  106 ILE   A HD12 1 
ATOM   2286 H HD13 A ILE   A 1 106 ? 19.016 -7.184  -9.922  0.86 32.00 ?  106 ILE   A HD13 1 
ATOM   2287 H HD13 B ILE   A 1 106 ? 18.934 -7.264  -9.859  0.14 31.80 ?  106 ILE   A HD13 1 
ATOM   2288 N N    A GLN   A 1 107 ? 22.570 -11.140 -11.376 0.86 23.77 ?  107 GLN   A N    1 
ATOM   2289 N N    B GLN   A 1 107 ? 22.510 -11.127 -11.288 0.14 25.11 ?  107 GLN   A N    1 
ATOM   2290 C CA   A GLN   A 1 107 ? 23.192 -12.345 -10.834 0.86 26.40 ?  107 GLN   A CA   1 
ATOM   2291 C CA   B GLN   A 1 107 ? 23.107 -12.336 -10.735 0.14 24.82 ?  107 GLN   A CA   1 
ATOM   2292 C C    A GLN   A 1 107 ? 24.163 -12.008 -9.709  0.86 23.40 ?  107 GLN   A C    1 
ATOM   2293 C C    B GLN   A 1 107 ? 24.185 -12.019 -9.709  0.14 22.26 ?  107 GLN   A C    1 
ATOM   2294 O O    A GLN   A 1 107 ? 24.401 -12.833 -8.820  0.86 24.52 ?  107 GLN   A O    1 
ATOM   2295 O O    B GLN   A 1 107 ? 24.542 -12.891 -8.909  0.14 22.58 ?  107 GLN   A O    1 
ATOM   2296 C CB   A GLN   A 1 107 ? 23.910 -13.108 -11.953 0.86 31.75 ?  107 GLN   A CB   1 
ATOM   2297 C CB   B GLN   A 1 107 ? 23.665 -13.217 -11.856 0.14 27.02 ?  107 GLN   A CB   1 
ATOM   2298 C CG   A GLN   A 1 107 ? 23.049 -13.359 -13.189 0.86 37.20 ?  107 GLN   A CG   1 
ATOM   2299 C CG   B GLN   A 1 107 ? 22.602 -13.718 -12.822 0.14 29.04 ?  107 GLN   A CG   1 
ATOM   2300 C CD   A GLN   A 1 107 ? 21.787 -14.135 -12.877 0.86 41.58 ?  107 GLN   A CD   1 
ATOM   2301 C CD   B GLN   A 1 107 ? 21.474 -14.450 -12.120 0.14 30.73 ?  107 GLN   A CD   1 
ATOM   2302 O OE1  A GLN   A 1 107 ? 21.832 -15.192 -12.245 0.86 43.18 ?  107 GLN   A OE1  1 
ATOM   2303 O OE1  B GLN   A 1 107 ? 21.697 -15.454 -11.443 0.14 31.27 ?  107 GLN   A OE1  1 
ATOM   2304 N NE2  A GLN   A 1 107 ? 20.649 -13.610 -13.314 0.86 43.09 ?  107 GLN   A NE2  1 
ATOM   2305 N NE2  B GLN   A 1 107 ? 20.256 -13.942 -12.267 0.14 31.34 ?  107 GLN   A NE2  1 
ATOM   2306 H H    A GLN   A 1 107 ? 22.693 -11.026 -12.219 0.86 28.54 ?  107 GLN   A H    1 
ATOM   2307 H H    B GLN   A 1 107 ? 22.645 -11.011 -12.129 0.14 30.14 ?  107 GLN   A H    1 
ATOM   2308 H HA   A GLN   A 1 107 ? 22.509 -12.929 -10.474 0.86 31.69 ?  107 GLN   A HA   1 
ATOM   2309 H HA   B GLN   A 1 107 ? 22.417 -12.840 -10.280 0.14 29.79 ?  107 GLN   A HA   1 
ATOM   2310 H HB2  A GLN   A 1 107 ? 24.687 -12.601 -12.237 0.86 38.11 ?  107 GLN   A HB2  1 
ATOM   2311 H HB2  B GLN   A 1 107 ? 24.312 -12.706 -12.368 0.14 32.43 ?  107 GLN   A HB2  1 
ATOM   2312 H HB3  A GLN   A 1 107 ? 24.191 -13.976 -11.618 0.86 38.11 ?  107 GLN   A HB3  1 
ATOM   2313 H HB3  B GLN   A 1 107 ? 24.096 -13.993 -11.463 0.14 32.43 ?  107 GLN   A HB3  1 
ATOM   2314 H HG2  A GLN   A 1 107 ? 22.789 -12.509 -13.578 0.86 44.64 ?  107 GLN   A HG2  1 
ATOM   2315 H HG2  B GLN   A 1 107 ? 22.222 -12.961 -13.294 0.14 34.85 ?  107 GLN   A HG2  1 
ATOM   2316 H HG3  A GLN   A 1 107 ? 23.564 -13.869 -13.834 0.86 44.64 ?  107 GLN   A HG3  1 
ATOM   2317 H HG3  B GLN   A 1 107 ? 23.009 -14.332 -13.452 0.14 34.85 ?  107 GLN   A HG3  1 
ATOM   2318 H HE21 A GLN   A 1 107 ? 20.655 -12.869 -13.752 0.86 51.72 ?  107 GLN   A HE21 1 
ATOM   2319 H HE21 B GLN   A 1 107 ? 20.138 -13.236 -12.746 0.14 37.61 ?  107 GLN   A HE21 1 
ATOM   2320 H HE22 A GLN   A 1 107 ? 19.905 -14.012 -13.161 0.86 51.72 ?  107 GLN   A HE22 1 
ATOM   2321 H HE22 B GLN   A 1 107 ? 19.584 -14.318 -11.885 0.14 37.61 ?  107 GLN   A HE22 1 
ATOM   2322 N N    . LEU   A 1 108 ? 24.710 -10.791 -9.708  1.00 19.67 ?  108 LEU   A N    1 
ATOM   2323 C CA   . LEU   A 1 108 ? 25.630 -10.373 -8.662  1.00 16.49 ?  108 LEU   A CA   1 
ATOM   2324 C C    . LEU   A 1 108 ? 24.933 -10.208 -7.321  1.00 14.53 ?  108 LEU   A C    1 
ATOM   2325 O O    . LEU   A 1 108 ? 25.615 -10.048 -6.307  1.00 15.23 ?  108 LEU   A O    1 
ATOM   2326 C CB   . LEU   A 1 108 ? 26.340 -9.075  -9.063  1.00 16.36 ?  108 LEU   A CB   1 
ATOM   2327 C CG   . LEU   A 1 108 ? 27.356 -9.267  -10.193 1.00 18.16 ?  108 LEU   A CG   1 
ATOM   2328 C CD1  . LEU   A 1 108 ? 27.830 -7.932  -10.745 1.00 18.76 ?  108 LEU   A CD1  1 
ATOM   2329 C CD2  . LEU   A 1 108 ? 28.546 -10.088 -9.715  1.00 19.89 ?  108 LEU   A CD2  1 
ATOM   2330 H H    A LEU   A 1 108 ? 24.558 -10.194 -10.301 0.86 23.61 ?  108 LEU   A H    1 
ATOM   2331 H H    B LEU   A 1 108 ? 24.556 -10.199 -10.305 0.14 23.61 ?  108 LEU   A H    1 
ATOM   2332 H HA   . LEU   A 1 108 ? 26.306 -11.059 -8.551  1.00 19.80 ?  108 LEU   A HA   1 
ATOM   2333 H HB2  . LEU   A 1 108 ? 25.679 -8.433  -9.362  1.00 19.64 ?  108 LEU   A HB2  1 
ATOM   2334 H HB3  . LEU   A 1 108 ? 26.814 -8.729  -8.294  1.00 19.64 ?  108 LEU   A HB3  1 
ATOM   2335 H HG   . LEU   A 1 108 ? 26.933 -9.754  -10.918 1.00 21.80 ?  108 LEU   A HG   1 
ATOM   2336 H HD11 . LEU   A 1 108 ? 28.445 -8.093  -11.480 1.00 22.52 ?  108 LEU   A HD11 1 
ATOM   2337 H HD12 . LEU   A 1 108 ? 27.064 -7.429  -11.060 1.00 22.52 ?  108 LEU   A HD12 1 
ATOM   2338 H HD13 . LEU   A 1 108 ? 28.283 -7.441  -10.041 1.00 22.52 ?  108 LEU   A HD13 1 
ATOM   2339 H HD21 . LEU   A 1 108 ? 29.254 -10.029 -10.373 1.00 23.88 ?  108 LEU   A HD21 1 
ATOM   2340 H HD22 . LEU   A 1 108 ? 28.852 -9.730  -8.866  1.00 23.88 ?  108 LEU   A HD22 1 
ATOM   2341 H HD23 . LEU   A 1 108 ? 28.270 -11.010 -9.604  1.00 23.88 ?  108 LEU   A HD23 1 
ATOM   2342 N N    . LEU   A 1 109 ? 23.599 -10.259 -7.285  1.00 14.24 ?  109 LEU   A N    1 
ATOM   2343 C CA   . LEU   A 1 109 ? 22.902 -10.141 -6.012  1.00 13.57 ?  109 LEU   A CA   1 
ATOM   2344 C C    . LEU   A 1 109 ? 23.251 -11.297 -5.078  1.00 12.45 ?  109 LEU   A C    1 
ATOM   2345 O O    . LEU   A 1 109 ? 23.390 -11.104 -3.864  1.00 12.93 ?  109 LEU   A O    1 
ATOM   2346 C CB   . LEU   A 1 109 ? 21.400 -10.055 -6.261  1.00 14.17 ?  109 LEU   A CB   1 
ATOM   2347 C CG   . LEU   A 1 109 ? 20.513 -9.764  -5.056  1.00 14.67 ?  109 LEU   A CG   1 
ATOM   2348 C CD1  . LEU   A 1 109 ? 20.966 -8.497  -4.357  1.00 14.87 ?  109 LEU   A CD1  1 
ATOM   2349 C CD2  . LEU   A 1 109 ? 19.048 -9.649  -5.477  1.00 15.80 ?  109 LEU   A CD2  1 
ATOM   2350 H H    . LEU   A 1 109 ? 23.087 -10.360 -7.969  1.00 17.10 ?  109 LEU   A H    1 
ATOM   2351 H HA   . LEU   A 1 109 ? 23.185 -9.320  -5.584  1.00 16.30 ?  109 LEU   A HA   1 
ATOM   2352 H HB2  . LEU   A 1 109 ? 21.243 -9.347  -6.905  1.00 17.01 ?  109 LEU   A HB2  1 
ATOM   2353 H HB3  . LEU   A 1 109 ? 21.105 -10.898 -6.630  1.00 17.01 ?  109 LEU   A HB3  1 
ATOM   2354 H HG   . LEU   A 1 109 ? 20.581 -10.492 -4.425  1.00 17.61 ?  109 LEU   A HG   1 
ATOM   2355 H HD11 . LEU   A 1 109 ? 20.296 -8.229  -3.711  1.00 17.85 ?  109 LEU   A HD11 1 
ATOM   2356 H HD12 . LEU   A 1 109 ? 21.810 -8.666  -3.909  1.00 17.85 ?  109 LEU   A HD12 1 
ATOM   2357 H HD13 . LEU   A 1 109 ? 21.082 -7.792  -5.020  1.00 17.85 ?  109 LEU   A HD13 1 
ATOM   2358 H HD21 . LEU   A 1 109 ? 18.522 -9.337  -4.721  1.00 18.97 ?  109 LEU   A HD21 1 
ATOM   2359 H HD22 . LEU   A 1 109 ? 18.974 -9.018  -6.210  1.00 18.97 ?  109 LEU   A HD22 1 
ATOM   2360 H HD23 . LEU   A 1 109 ? 18.730 -10.522 -5.761  1.00 18.97 ?  109 LEU   A HD23 1 
ATOM   2361 N N    . LYS   A 1 110 ? 23.395 -12.509 -5.617  1.00 12.67 ?  110 LYS   A N    1 
ATOM   2362 C CA   . LYS   A 1 110 ? 23.778 -13.631 -4.766  1.00 12.60 ?  110 LYS   A CA   1 
ATOM   2363 C C    . LYS   A 1 110 ? 25.159 -13.413 -4.160  1.00 12.24 ?  110 LYS   A C    1 
ATOM   2364 O O    . LYS   A 1 110 ? 25.352 -13.613 -2.957  1.00 12.59 ?  110 LYS   A O    1 
ATOM   2365 C CB   . LYS   A 1 110 ? 23.703 -14.947 -5.539  1.00 13.63 ?  110 LYS   A CB   1 
ATOM   2366 C CG   . LYS   A 1 110 ? 23.888 -16.161 -4.636  1.00 14.10 ?  110 LYS   A CG   1 
ATOM   2367 C CD   . LYS   A 1 110 ? 23.684 -17.475 -5.368  1.00 14.75 ?  110 LYS   A CD   1 
ATOM   2368 C CE   . LYS   A 1 110 ? 23.794 -18.667 -4.434  1.00 15.45 ?  110 LYS   A CE   1 
ATOM   2369 N NZ   . LYS   A 1 110 ? 22.623 -18.814 -3.535  1.00 15.74 ?  110 LYS   A NZ   1 
ATOM   2370 H H    . LYS   A 1 110 ? 23.273 -12.704 -6.445  1.00 15.22 ?  110 LYS   A H    1 
ATOM   2371 H HA   . LYS   A 1 110 ? 23.142 -13.690 -4.032  1.00 15.13 ?  110 LYS   A HA   1 
ATOM   2372 H HB2  . LYS   A 1 110 ? 22.830 -15.015 -5.961  1.00 16.37 ?  110 LYS   A HB2  1 
ATOM   2373 H HB3  . LYS   A 1 110 ? 24.400 -14.958 -6.210  1.00 16.37 ?  110 LYS   A HB3  1 
ATOM   2374 H HG2  . LYS   A 1 110 ? 24.788 -16.152 -4.277  1.00 16.93 ?  110 LYS   A HG2  1 
ATOM   2375 H HG3  . LYS   A 1 110 ? 23.242 -16.116 -3.912  1.00 16.93 ?  110 LYS   A HG3  1 
ATOM   2376 H HD2  . LYS   A 1 110 ? 22.801 -17.483 -5.766  1.00 17.70 ?  110 LYS   A HD2  1 
ATOM   2377 H HD3  . LYS   A 1 110 ? 24.363 -17.562 -6.056  1.00 17.70 ?  110 LYS   A HD3  1 
ATOM   2378 H HE2  . LYS   A 1 110 ? 23.876 -19.474 -4.962  1.00 18.55 ?  110 LYS   A HE2  1 
ATOM   2379 H HE3  . LYS   A 1 110 ? 24.585 -18.556 -3.877  1.00 18.55 ?  110 LYS   A HE3  1 
ATOM   2380 H HZ1  . LYS   A 1 110 ? 22.726 -19.521 -3.008  1.00 18.90 ?  110 LYS   A HZ1  1 
ATOM   2381 H HZ2  . LYS   A 1 110 ? 22.528 -18.086 -3.032  1.00 18.90 ?  110 LYS   A HZ2  1 
ATOM   2382 H HZ3  . LYS   A 1 110 ? 21.881 -18.923 -4.022  1.00 18.90 ?  110 LYS   A HZ3  1 
ATOM   2383 N N    . SER   A 1 111 ? 26.119 -12.961 -4.970  1.00 12.15 ?  111 SER   A N    1 
ATOM   2384 C CA   . SER   A 1 111 ? 27.448 -12.662 -4.448  1.00 12.84 ?  111 SER   A CA   1 
ATOM   2385 C C    . SER   A 1 111 ? 27.385 -11.609 -3.348  1.00 12.32 ?  111 SER   A C    1 
ATOM   2386 O O    . SER   A 1 111 ? 28.078 -11.715 -2.331  1.00 12.83 ?  111 SER   A O    1 
ATOM   2387 C CB   . SER   A 1 111 ? 28.347 -12.168 -5.582  1.00 14.77 ?  111 SER   A CB   1 
ATOM   2388 O OG   . SER   A 1 111 ? 28.454 -13.141 -6.607  1.00 16.72 ?  111 SER   A OG   1 
ATOM   2389 H H    . SER   A 1 111 ? 26.022 -12.817 -5.811  1.00 14.58 ?  111 SER   A H    1 
ATOM   2390 H HA   . SER   A 1 111 ? 27.838 -13.472 -4.079  1.00 15.41 ?  111 SER   A HA   1 
ATOM   2391 H HB2  . SER   A 1 111 ? 27.959 -11.368 -5.966  1.00 17.74 ?  111 SER   A HB2  1 
ATOM   2392 H HB3  . SER   A 1 111 ? 29.227 -11.971 -5.223  1.00 17.74 ?  111 SER   A HB3  1 
ATOM   2393 H HG   . SER   A 1 111 ? 28.976 -12.857 -7.214  1.00 20.07 ?  111 SER   A HG   1 
ATOM   2394 N N    . ALA   A 1 112 ? 26.539 -10.596 -3.527  1.00 11.99 ?  112 ALA   A N    1 
ATOM   2395 C CA   . ALA   A 1 112 ? 26.385 -9.560  -2.509  1.00 11.90 ?  112 ALA   A CA   1 
ATOM   2396 C C    . ALA   A 1 112 ? 25.908 -10.157 -1.187  1.00 11.51 ?  112 ALA   A C    1 
ATOM   2397 O O    . ALA   A 1 112 ? 26.458 -9.859  -0.119  1.00 12.03 ?  112 ALA   A O    1 
ATOM   2398 C CB   . ALA   A 1 112 ? 25.423 -8.480  -3.009  1.00 12.74 ?  112 ALA   A CB   1 
ATOM   2399 H H    . ALA   A 1 112 ? 26.049 -10.484 -4.223  1.00 14.40 ?  112 ALA   A H    1 
ATOM   2400 H HA   . ALA   A 1 112 ? 27.242 -9.135  -2.354  1.00 14.29 ?  112 ALA   A HA   1 
ATOM   2401 H HB1  . ALA   A 1 112 ? 25.342 -7.784  -2.332  1.00 15.29 ?  112 ALA   A HB1  1 
ATOM   2402 H HB2  . ALA   A 1 112 ? 25.765 -8.098  -3.831  1.00 15.29 ?  112 ALA   A HB2  1 
ATOM   2403 H HB3  . ALA   A 1 112 ? 24.549 -8.878  -3.170  1.00 15.29 ?  112 ALA   A HB3  1 
ATOM   2404 N N    . TYR   A 1 113 ? 24.878 -11.008 -1.238  1.00 11.73 ?  113 TYR   A N    1 
ATOM   2405 C CA   . TYR   A 1 113 ? 24.368 -11.619 -0.013  1.00 11.48 ?  113 TYR   A CA   1 
ATOM   2406 C C    . TYR   A 1 113 ? 25.373 -12.570 0.627   1.00 11.41 ?  113 TYR   A C    1 
ATOM   2407 O O    . TYR   A 1 113 ? 25.338 -12.758 1.846   1.00 12.19 ?  113 TYR   A O    1 
ATOM   2408 C CB   . TYR   A 1 113 ? 23.064 -12.356 -0.290  1.00 12.13 ?  113 TYR   A CB   1 
ATOM   2409 C CG   . TYR   A 1 113 ? 21.847 -11.469 -0.196  1.00 12.08 ?  113 TYR   A CG   1 
ATOM   2410 C CD1  . TYR   A 1 113 ? 21.481 -10.883 1.012   1.00 12.10 ?  113 TYR   A CD1  1 
ATOM   2411 C CD2  . TYR   A 1 113 ? 21.042 -11.234 -1.306  1.00 12.31 ?  113 TYR   A CD2  1 
ATOM   2412 C CE1  . TYR   A 1 113 ? 20.351 -10.097 1.115   1.00 12.58 ?  113 TYR   A CE1  1 
ATOM   2413 C CE2  . TYR   A 1 113 ? 19.889 -10.443 -1.212  1.00 12.41 ?  113 TYR   A CE2  1 
ATOM   2414 C CZ   . TYR   A 1 113 ? 19.561 -9.878  -0.001  1.00 12.30 ?  113 TYR   A CZ   1 
ATOM   2415 O OH   . TYR   A 1 113 ? 18.438 -9.093  0.127   1.00 13.20 ?  113 TYR   A OH   1 
ATOM   2416 H H    . TYR   A 1 113 ? 24.469 -11.238 -1.956  1.00 14.08 ?  113 TYR   A H    1 
ATOM   2417 H HA   . TYR   A 1 113 ? 24.185 -10.919 0.628   1.00 13.78 ?  113 TYR   A HA   1 
ATOM   2418 H HB2  . TYR   A 1 113 ? 23.092 -12.720 -1.187  1.00 14.57 ?  113 TYR   A HB2  1 
ATOM   2419 H HB3  . TYR   A 1 113 ? 22.965 -13.070 0.356   1.00 14.57 ?  113 TYR   A HB3  1 
ATOM   2420 H HD1  . TYR   A 1 113 ? 22.005 -11.036 1.768   1.00 14.53 ?  113 TYR   A HD1  1 
ATOM   2421 H HD2  . TYR   A 1 113 ? 21.261 -11.627 -2.116  1.00 14.78 ?  113 TYR   A HD2  1 
ATOM   2422 H HE1  . TYR   A 1 113 ? 20.122 -9.713  1.933   1.00 15.10 ?  113 TYR   A HE1  1 
ATOM   2423 H HE2  . TYR   A 1 113 ? 19.355 -10.291 -1.957  1.00 14.90 ?  113 TYR   A HE2  1 
ATOM   2424 H HH   . TYR   A 1 113 ? 18.048 -9.038  -0.621  1.00 15.84 ?  113 TYR   A HH   1 
ATOM   2425 N N    . GLU   A 1 114 ? 26.277 -13.172 -0.159  1.00 11.76 ?  114 GLU   A N    1 
ATOM   2426 C CA   . GLU   A 1 114 ? 27.269 -14.068 0.431   1.00 12.03 ?  114 GLU   A CA   1 
ATOM   2427 C C    . GLU   A 1 114 ? 28.123 -13.361 1.478   1.00 11.79 ?  114 GLU   A C    1 
ATOM   2428 O O    . GLU   A 1 114 ? 28.599 -14.000 2.425   1.00 12.48 ?  114 GLU   A O    1 
ATOM   2429 C CB   . GLU   A 1 114 ? 28.135 -14.713 -0.663  1.00 12.10 ?  114 GLU   A CB   1 
ATOM   2430 C CG   . GLU   A 1 114 ? 27.375 -15.768 -1.439  1.00 12.52 ?  114 GLU   A CG   1 
ATOM   2431 C CD   . GLU   A 1 114 ? 28.092 -16.293 -2.678  1.00 13.35 ?  114 GLU   A CD   1 
ATOM   2432 O OE1  . GLU   A 1 114 ? 29.057 -15.669 -3.166  1.00 13.65 ?  114 GLU   A OE1  1 
ATOM   2433 O OE2  . GLU   A 1 114 ? 27.648 -17.345 -3.183  1.00 14.58 -1 114 GLU   A OE2  1 
ATOM   2434 H H    . GLU   A 1 114 ? 26.335 -13.075 -1.020  1.00 14.12 ?  114 GLU   A H    1 
ATOM   2435 H HA   . GLU   A 1 114 ? 26.797 -14.785 0.874   1.00 14.44 ?  114 GLU   A HA   1 
ATOM   2436 H HB2  . GLU   A 1 114 ? 28.424 -14.031 -1.293  1.00 14.52 ?  114 GLU   A HB2  1 
ATOM   2437 H HB3  . GLU   A 1 114 ? 28.904 -15.138 -0.256  1.00 14.52 ?  114 GLU   A HB3  1 
ATOM   2438 H HG2  . GLU   A 1 114 ? 27.218 -16.525 -0.857  1.00 15.04 ?  114 GLU   A HG2  1 
ATOM   2439 H HG3  . GLU   A 1 114 ? 26.529 -15.393 -1.727  1.00 15.04 ?  114 GLU   A HG3  1 
ATOM   2440 N N    . ASN   A 1 115 ? 28.305 -12.042 1.350   1.00 11.42 ?  115 ASN   A N    1 
ATOM   2441 C CA   . ASN   A 1 115 ? 29.068 -11.315 2.359   1.00 11.99 ?  115 ASN   A CA   1 
ATOM   2442 C C    . ASN   A 1 115 ? 28.453 -11.449 3.745   1.00 11.69 ?  115 ASN   A C    1 
ATOM   2443 O O    . ASN   A 1 115 ? 29.167 -11.373 4.753   1.00 12.22 ?  115 ASN   A O    1 
ATOM   2444 C CB   . ASN   A 1 115 ? 29.161 -9.840  1.981   1.00 12.03 ?  115 ASN   A CB   1 
ATOM   2445 C CG   . ASN   A 1 115 ? 29.953 -9.617  0.722   1.00 13.10 ?  115 ASN   A CG   1 
ATOM   2446 O OD1  . ASN   A 1 115 ? 31.171 -9.725  0.736   1.00 16.38 ?  115 ASN   A OD1  1 
ATOM   2447 N ND2  . ASN   A 1 115 ? 29.278 -9.318  -0.371  1.00 12.89 ?  115 ASN   A ND2  1 
ATOM   2448 H H    . ASN   A 1 115 ? 28.007 -11.559 0.702   1.00 13.71 ?  115 ASN   A H    1 
ATOM   2449 H HA   . ASN   A 1 115 ? 29.968 -11.674 2.393   1.00 14.40 ?  115 ASN   A HA   1 
ATOM   2450 H HB2  . ASN   A 1 115 ? 28.264 -9.494  1.851   1.00 14.45 ?  115 ASN   A HB2  1 
ATOM   2451 H HB3  . ASN   A 1 115 ? 29.597 -9.362  2.705   1.00 14.45 ?  115 ASN   A HB3  1 
ATOM   2452 H HD21 . ASN   A 1 115 ? 29.691 -9.176  -1.109  1.00 15.48 ?  115 ASN   A HD21 1 
ATOM   2453 H HD22 . ASN   A 1 115 ? 28.415 -9.264  -0.346  1.00 15.48 ?  115 ASN   A HD22 1 
ATOM   2454 N N    . PHE   A 1 116 ? 27.129 -11.631 3.823   1.00 11.81 ?  116 PHE   A N    1 
ATOM   2455 C CA   . PHE   A 1 116 ? 26.479 -11.729 5.125   1.00 11.81 ?  116 PHE   A CA   1 
ATOM   2456 C C    . PHE   A 1 116 ? 26.954 -12.960 5.895   1.00 11.81 ?  116 PHE   A C    1 
ATOM   2457 O O    . PHE   A 1 116 ? 26.888 -12.978 7.125   1.00 12.64 ?  116 PHE   A O    1 
ATOM   2458 C CB   . PHE   A 1 116 ? 24.955 -11.859 4.983   1.00 12.31 ?  116 PHE   A CB   1 
ATOM   2459 C CG   . PHE   A 1 116 ? 24.200 -10.611 4.529   1.00 11.60 ?  116 PHE   A CG   1 
ATOM   2460 C CD1  . PHE   A 1 116 ? 24.770 -9.576  3.798   1.00 11.84 ?  116 PHE   A CD1  1 
ATOM   2461 C CD2  . PHE   A 1 116 ? 22.847 -10.517 4.845   1.00 12.22 ?  116 PHE   A CD2  1 
ATOM   2462 C CE1  . PHE   A 1 116 ? 23.990 -8.498  3.394   1.00 12.10 ?  116 PHE   A CE1  1 
ATOM   2463 C CE2  . PHE   A 1 116 ? 22.076 -9.444  4.451   1.00 12.38 ?  116 PHE   A CE2  1 
ATOM   2464 C CZ   . PHE   A 1 116 ? 22.638 -8.434  3.726   1.00 12.02 ?  116 PHE   A CZ   1 
ATOM   2465 H H    . PHE   A 1 116 ? 26.596 -11.697 3.147   1.00 14.18 ?  116 PHE   A H    1 
ATOM   2466 H HA   . PHE   A 1 116 ? 26.675 -10.936 5.648   1.00 14.18 ?  116 PHE   A HA   1 
ATOM   2467 H HB2  . PHE   A 1 116 ? 24.770 -12.558 4.335   1.00 14.78 ?  116 PHE   A HB2  1 
ATOM   2468 H HB3  . PHE   A 1 116 ? 24.593 -12.119 5.844   1.00 14.78 ?  116 PHE   A HB3  1 
ATOM   2469 H HD1  . PHE   A 1 116 ? 25.667 -9.622  3.564   1.00 14.22 ?  116 PHE   A HD1  1 
ATOM   2470 H HD2  . PHE   A 1 116 ? 22.449 -11.214 5.326   1.00 14.68 ?  116 PHE   A HD2  1 
ATOM   2471 H HE1  . PHE   A 1 116 ? 24.379 -7.808  2.908   1.00 14.53 ?  116 PHE   A HE1  1 
ATOM   2472 H HE2  . PHE   A 1 116 ? 21.173 -9.418  4.678   1.00 14.86 ?  116 PHE   A HE2  1 
ATOM   2473 H HZ   . PHE   A 1 116 ? 22.125 -7.702  3.466   1.00 14.43 ?  116 PHE   A HZ   1 
ATOM   2474 N N    . ASN   A 1 117 ? 27.400 -14.008 5.192   1.00 12.06 ?  117 ASN   A N    1 
ATOM   2475 C CA   . ASN   A 1 117 ? 27.767 -15.253 5.855   1.00 12.42 ?  117 ASN   A CA   1 
ATOM   2476 C C    . ASN   A 1 117 ? 29.031 -15.137 6.680   1.00 12.83 ?  117 ASN   A C    1 
ATOM   2477 O O    . ASN   A 1 117 ? 29.333 -16.062 7.438   1.00 13.80 ?  117 ASN   A O    1 
ATOM   2478 C CB   . ASN   A 1 117 ? 27.882 -16.377 4.834   1.00 12.81 ?  117 ASN   A CB   1 
ATOM   2479 C CG   . ASN   A 1 117 ? 26.537 -16.762 4.299   1.00 12.74 ?  117 ASN   A CG   1 
ATOM   2480 O OD1  . ASN   A 1 117 ? 25.563 -16.799 5.051   1.00 13.78 ?  117 ASN   A OD1  1 
ATOM   2481 N ND2  . ASN   A 1 117 ? 26.453 -17.002 3.008   1.00 12.56 ?  117 ASN   A ND2  1 
ATOM   2482 H H    . ASN   A 1 117 ? 27.480 -14.021 4.333   1.00 14.48 ?  117 ASN   A H    1 
ATOM   2483 H HA   . ASN   A 1 117 ? 27.049 -15.486 6.462   1.00 14.91 ?  117 ASN   A HA   1 
ATOM   2484 H HB2  . ASN   A 1 117 ? 28.435 -16.082 4.093   1.00 15.39 ?  117 ASN   A HB2  1 
ATOM   2485 H HB3  . ASN   A 1 117 ? 28.275 -17.152 5.261   1.00 15.39 ?  117 ASN   A HB3  1 
ATOM   2486 H HD21 . ASN   A 1 117 ? 25.702 -17.217 2.659   1.00 15.08 ?  117 ASN   A HD21 1 
ATOM   2487 H HD22 . ASN   A 1 117 ? 27.160 -16.948 2.516   1.00 15.08 ?  117 ASN   A HD22 1 
ATOM   2488 N N    . GLN   A 1 118 ? 29.767 -14.035 6.560   1.00 12.64 ?  118 GLN   A N    1 
ATOM   2489 C CA   . GLN   A 1 118 ? 30.942 -13.802 7.384   1.00 13.29 ?  118 GLN   A CA   1 
ATOM   2490 C C    . GLN   A 1 118 ? 30.598 -13.236 8.753   1.00 13.55 ?  118 GLN   A C    1 
ATOM   2491 O O    . GLN   A 1 118 ? 31.512 -12.957 9.537   1.00 15.24 ?  118 GLN   A O    1 
ATOM   2492 C CB   . GLN   A 1 118 ? 31.930 -12.890 6.653   1.00 13.75 ?  118 GLN   A CB   1 
ATOM   2493 C CG   . GLN   A 1 118 ? 32.409 -13.458 5.329   1.00 13.84 ?  118 GLN   A CG   1 
ATOM   2494 C CD   . GLN   A 1 118 ? 33.236 -14.715 5.507   1.00 14.08 ?  118 GLN   A CD   1 
ATOM   2495 O OE1  . GLN   A 1 118 ? 34.101 -14.779 6.389   1.00 14.90 ?  118 GLN   A OE1  1 
ATOM   2496 N NE2  . GLN   A 1 118 ? 32.986 -15.719 4.668   1.00 14.22 ?  118 GLN   A NE2  1 
ATOM   2497 H H    . GLN   A 1 118 ? 29.592 -13.391 6.007   1.00 15.18 ?  118 GLN   A H    1 
ATOM   2498 H HA   . GLN   A 1 118 ? 31.375 -14.659 7.526   1.00 15.96 ?  118 GLN   A HA   1 
ATOM   2499 H HB2  . GLN   A 1 118 ? 31.499 -12.041 6.477   1.00 16.51 ?  118 GLN   A HB2  1 
ATOM   2500 H HB3  . GLN   A 1 118 ? 32.705 -12.760 7.221   1.00 16.51 ?  118 GLN   A HB3  1 
ATOM   2501 H HG2  . GLN   A 1 118 ? 31.640 -13.676 4.778   1.00 16.62 ?  118 GLN   A HG2  1 
ATOM   2502 H HG3  . GLN   A 1 118 ? 32.961 -12.798 4.884   1.00 16.62 ?  118 GLN   A HG3  1 
ATOM   2503 H HE21 . GLN   A 1 118 ? 32.369 -15.635 4.069   1.00 17.08 ?  118 GLN   A HE21 1 
ATOM   2504 H HE22 . GLN   A 1 118 ? 33.421 -16.456 4.732   1.00 17.08 ?  118 GLN   A HE22 1 
ATOM   2505 N N    . HIS   A 1 119 ? 29.311 -13.074 9.067   1.00 12.99 ?  119 HIS   A N    1 
ATOM   2506 C CA   . HIS   A 1 119 ? 28.866 -12.473 10.321  1.00 13.11 ?  119 HIS   A CA   1 
ATOM   2507 C C    . HIS   A 1 119 ? 27.730 -13.296 10.896  1.00 13.57 ?  119 HIS   A C    1 
ATOM   2508 O O    . HIS   A 1 119 ? 26.778 -13.622 10.182  1.00 14.43 ?  119 HIS   A O    1 
ATOM   2509 C CB   . HIS   A 1 119 ? 28.402 -11.039 10.075  1.00 13.73 ?  119 HIS   A CB   1 
ATOM   2510 C CG   . HIS   A 1 119 ? 29.478 -10.218 9.468   1.00 15.08 ?  119 HIS   A CG   1 
ATOM   2511 N ND1  . HIS   A 1 119 ? 30.458 -9.621  10.226  1.00 17.14 ?  119 HIS   A ND1  1 
ATOM   2512 C CD2  . HIS   A 1 119 ? 29.814 -10.011 8.176   1.00 15.86 ?  119 HIS   A CD2  1 
ATOM   2513 C CE1  . HIS   A 1 119 ? 31.321 -9.024  9.424   1.00 17.77 ?  119 HIS   A CE1  1 
ATOM   2514 N NE2  . HIS   A 1 119 ? 30.967 -9.263  8.174   1.00 17.12 ?  119 HIS   A NE2  1 
ATOM   2515 H H    . HIS   A 1 119 ? 28.655 -13.313 8.559   1.00 15.59 ?  119 HIS   A H    1 
ATOM   2516 H HA   . HIS   A 1 119 ? 29.604 -12.461 10.959  1.00 15.75 ?  119 HIS   A HA   1 
ATOM   2517 H HB2  . HIS   A 1 119 ? 27.648 -11.054 9.470   1.00 16.49 ?  119 HIS   A HB2  1 
ATOM   2518 H HB3  . HIS   A 1 119 ? 28.153 -10.639 10.922  1.00 16.49 ?  119 HIS   A HB3  1 
ATOM   2519 H HD1  . HIS   A 1 119 ? 30.487 -9.613  11.085  1.00 20.57 ?  119 HIS   A HD1  1 
ATOM   2520 H HD2  . HIS   A 1 119 ? 29.354 -10.314 7.427   1.00 19.03 ?  119 HIS   A HD2  1 
ATOM   2521 H HE1  . HIS   A 1 119 ? 32.056 -8.522  9.696   1.00 21.33 ?  119 HIS   A HE1  1 
ATOM   2522 N N    . GLU   A 1 120 ? 27.826 -13.615 12.186  1.00 14.57 ?  120 GLU   A N    1 
ATOM   2523 C CA   . GLU   A 1 120 ? 26.877 -14.551 12.783  1.00 16.82 ?  120 GLU   A CA   1 
ATOM   2524 C C    . GLU   A 1 120 ? 25.457 -13.992 12.827  1.00 15.23 ?  120 GLU   A C    1 
ATOM   2525 O O    . GLU   A 1 120 ? 24.481 -14.748 12.697  1.00 15.23 ?  120 GLU   A O    1 
ATOM   2526 C CB   . GLU   A 1 120 ? 27.340 -14.936 14.188  1.00 22.69 ?  120 GLU   A CB   1 
ATOM   2527 C CG   . GLU   A 1 120 ? 28.523 -15.889 14.208  1.00 30.81 ?  120 GLU   A CG   1 
ATOM   2528 C CD   . GLU   A 1 120 ? 28.624 -16.651 15.514  1.00 38.50 ?  120 GLU   A CD   1 
ATOM   2529 O OE1  . GLU   A 1 120 ? 28.255 -16.084 16.565  1.00 40.39 ?  120 GLU   A OE1  1 
ATOM   2530 O OE2  . GLU   A 1 120 ? 29.064 -17.821 15.488  1.00 43.88 -1 120 GLU   A OE2  1 
ATOM   2531 H H    . GLU   A 1 120 ? 28.431 -13.318 12.730  1.00 17.49 ?  120 GLU   A H    1 
ATOM   2532 H HA   . GLU   A 1 120 ? 26.864 -15.359 12.253  1.00 20.19 ?  120 GLU   A HA   1 
ATOM   2533 H HB2  . GLU   A 1 120 ? 27.604 -14.137 14.670  1.00 27.23 ?  120 GLU   A HB2  1 
ATOM   2534 H HB3  . GLU   A 1 120 ? 26.607 -15.372 14.655  1.00 27.23 ?  120 GLU   A HB3  1 
ATOM   2535 H HG2  . GLU   A 1 120 ? 28.433 -16.526 13.481  1.00 36.98 ?  120 GLU   A HG2  1 
ATOM   2536 H HG3  . GLU   A 1 120 ? 29.344 -15.384 14.110  1.00 36.98 ?  120 GLU   A HG3  1 
ATOM   2537 N N    . VAL   A 1 121 ? 25.323 -12.684 13.052  1.00 14.61 ?  121 VAL   A N    1 
ATOM   2538 C CA   . VAL   A 1 121 ? 24.031 -12.015 13.174  1.00 14.65 ?  121 VAL   A CA   1 
ATOM   2539 C C    . VAL   A 1 121 ? 24.144 -10.628 12.551  1.00 13.77 ?  121 VAL   A C    1 
ATOM   2540 O O    . VAL   A 1 121 ? 25.118 -9.908  12.795  1.00 14.29 ?  121 VAL   A O    1 
ATOM   2541 C CB   . VAL   A 1 121 ? 23.592 -11.885 14.649  1.00 17.82 ?  121 VAL   A CB   1 
ATOM   2542 C CG1  . VAL   A 1 121 ? 22.209 -11.249 14.744  1.00 18.62 ?  121 VAL   A CG1  1 
ATOM   2543 C CG2  . VAL   A 1 121 ? 23.599 -13.226 15.361  1.00 20.45 ?  121 VAL   A CG2  1 
ATOM   2544 H H    . VAL   A 1 121 ? 25.988 -12.149 13.150  1.00 17.54 ?  121 VAL   A H    1 
ATOM   2545 H HA   . VAL   A 1 121 ? 23.357 -12.526 12.695  1.00 17.59 ?  121 VAL   A HA   1 
ATOM   2546 H HB   . VAL   A 1 121 ? 24.211 -11.304 15.111  1.00 21.39 ?  121 VAL   A HB   1 
ATOM   2547 H HG11 . VAL   A 1 121 ? 21.890 -11.315 15.658  1.00 22.35 ?  121 VAL   A HG11 1 
ATOM   2548 H HG12 . VAL   A 1 121 ? 22.268 -10.315 14.485  1.00 22.35 ?  121 VAL   A HG12 1 
ATOM   2549 H HG13 . VAL   A 1 121 ? 21.601 -11.719 14.150  1.00 22.35 ?  121 VAL   A HG13 1 
ATOM   2550 H HG21 . VAL   A 1 121 ? 23.245 -13.111 16.263  1.00 24.55 ?  121 VAL   A HG21 1 
ATOM   2551 H HG22 . VAL   A 1 121 ? 23.037 -13.852 14.874  1.00 24.55 ?  121 VAL   A HG22 1 
ATOM   2552 H HG23 . VAL   A 1 121 ? 24.505 -13.560 15.407  1.00 24.55 ?  121 VAL   A HG23 1 
ATOM   2553 N N    . LEU   A 1 122 ? 23.132 -10.232 11.774  1.00 13.17 ?  122 LEU   A N    1 
ATOM   2554 C CA   . LEU   A 1 122 ? 23.142 -8.931  11.114  1.00 12.99 ?  122 LEU   A CA   1 
ATOM   2555 C C    . LEU   A 1 122 ? 21.746 -8.343  11.067  1.00 13.10 ?  122 LEU   A C    1 
ATOM   2556 O O    . LEU   A 1 122 ? 20.756 -9.069  10.939  1.00 14.07 ?  122 LEU   A O    1 
ATOM   2557 C CB   . LEU   A 1 122 ? 23.558 -9.016  9.639   1.00 14.53 ?  122 LEU   A CB   1 
ATOM   2558 C CG   . LEU   A 1 122 ? 24.764 -9.860  9.262   1.00 14.65 ?  122 LEU   A CG   1 
ATOM   2559 C CD1  . LEU   A 1 122 ? 24.383 -11.320 9.066   1.00 15.66 ?  122 LEU   A CD1  1 
ATOM   2560 C CD2  . LEU   A 1 122 ? 25.413 -9.298  8.004   1.00 13.64 ?  122 LEU   A CD2  1 
ATOM   2561 H H    . LEU   A 1 122 ? 22.428 -10.702 11.608  1.00 15.81 ?  122 LEU   A H    1 
ATOM   2562 H HA   . LEU   A 1 122 ? 23.741 -8.319  11.579  1.00 15.60 ?  122 LEU   A HA   1 
ATOM   2563 H HB2  . LEU   A 1 122 ? 22.816 -9.372  9.138   1.00 17.45 ?  122 LEU   A HB2  1 
ATOM   2564 H HB3  . LEU   A 1 122 ? 23.749 -8.116  9.329   1.00 17.45 ?  122 LEU   A HB3  1 
ATOM   2565 H HG   . LEU   A 1 122 ? 25.434 -9.814  9.968   1.00 17.59 ?  122 LEU   A HG   1 
ATOM   2566 H HD11 . LEU   A 1 122 ? 25.156 -11.814 8.746   1.00 18.80 ?  122 LEU   A HD11 1 
ATOM   2567 H HD12 . LEU   A 1 122 ? 24.090 -11.682 9.914   1.00 18.80 ?  122 LEU   A HD12 1 
ATOM   2568 H HD13 . LEU   A 1 122 ? 23.668 -11.371 8.414   1.00 18.80 ?  122 LEU   A HD13 1 
ATOM   2569 H HD21 . LEU   A 1 122 ? 26.163 -9.863  7.740   1.00 16.38 ?  122 LEU   A HD21 1 
ATOM   2570 H HD22 . LEU   A 1 122 ? 24.757 -9.275  7.288   1.00 16.38 ?  122 LEU   A HD22 1 
ATOM   2571 H HD23 . LEU   A 1 122 ? 25.736 -8.396  8.179   1.00 16.38 ?  122 LEU   A HD23 1 
ATOM   2572 N N    A LEU   A 1 123 ? 21.681 -7.017  11.175  0.86 12.33 ?  123 LEU   A N    1 
ATOM   2573 N N    B LEU   A 1 123 ? 21.690 -7.013  11.152  0.14 12.70 ?  123 LEU   A N    1 
ATOM   2574 C CA   A LEU   A 1 123 ? 20.508 -6.225  10.825  0.86 12.02 ?  123 LEU   A CA   1 
ATOM   2575 C CA   B LEU   A 1 123 ? 20.490 -6.234  10.871  0.14 12.69 ?  123 LEU   A CA   1 
ATOM   2576 C C    A LEU   A 1 123 ? 20.737 -5.688  9.424   0.86 11.84 ?  123 LEU   A C    1 
ATOM   2577 C C    B LEU   A 1 123 ? 20.696 -5.604  9.500   0.14 12.19 ?  123 LEU   A C    1 
ATOM   2578 O O    A LEU   A 1 123 ? 21.793 -5.110  9.162   0.86 12.07 ?  123 LEU   A O    1 
ATOM   2579 O O    B LEU   A 1 123 ? 21.562 -4.739  9.337   0.14 11.75 ?  123 LEU   A O    1 
ATOM   2580 C CB   A LEU   A 1 123 ? 20.380 -5.053  11.796  0.86 12.54 ?  123 LEU   A CB   1 
ATOM   2581 C CB   B LEU   A 1 123 ? 20.295 -5.159  11.938  0.14 13.26 ?  123 LEU   A CB   1 
ATOM   2582 C CG   A LEU   A 1 123 ? 19.322 -4.001  11.469  0.86 13.52 ?  123 LEU   A CG   1 
ATOM   2583 C CG   B LEU   A 1 123 ? 19.291 -4.054  11.592  0.14 13.65 ?  123 LEU   A CG   1 
ATOM   2584 C CD1  A LEU   A 1 123 ? 17.929 -4.613  11.483  0.86 14.39 ?  123 LEU   A CD1  1 
ATOM   2585 C CD1  B LEU   A 1 123 ? 17.886 -4.623  11.456  0.14 13.83 ?  123 LEU   A CD1  1 
ATOM   2586 C CD2  A LEU   A 1 123 ? 19.416 -2.833  12.449  0.86 14.45 ?  123 LEU   A CD2  1 
ATOM   2587 C CD2  B LEU   A 1 123 ? 19.326 -2.925  12.616  0.14 13.99 ?  123 LEU   A CD2  1 
ATOM   2588 H H    A LEU   A 1 123 ? 22.343 -6.532  11.448  0.86 14.80 ?  123 LEU   A H    1 
ATOM   2589 H H    B LEU   A 1 123 ? 22.367 -6.521  11.366  0.14 15.25 ?  123 LEU   A H    1 
ATOM   2590 H HA   A LEU   A 1 123 ? 19.709 -6.770  10.844  0.86 14.44 ?  123 LEU   A HA   1 
ATOM   2591 H HA   B LEU   A 1 123 ? 19.715 -6.811  10.843  0.14 15.24 ?  123 LEU   A HA   1 
ATOM   2592 H HB2  A LEU   A 1 123 ? 20.162 -5.413  12.670  0.86 15.05 ?  123 LEU   A HB2  1 
ATOM   2593 H HB2  B LEU   A 1 123 ? 19.985 -5.591  12.750  0.14 15.92 ?  123 LEU   A HB2  1 
ATOM   2594 H HB3  A LEU   A 1 123 ? 21.232 -4.599  11.837  0.86 15.05 ?  123 LEU   A HB3  1 
ATOM   2595 H HB3  B LEU   A 1 123 ? 21.151 -4.733  12.106  0.14 15.92 ?  123 LEU   A HB3  1 
ATOM   2596 H HG   A LEU   A 1 123 ? 19.480 -3.645  10.579  0.86 16.24 ?  123 LEU   A HG   1 
ATOM   2597 H HG   B LEU   A 1 123 ? 19.532 -3.666  10.738  0.14 16.39 ?  123 LEU   A HG   1 
ATOM   2598 H HD11 A LEU   A 1 123 ? 17.272 -3.920  11.324  0.86 17.28 ?  123 LEU   A HD11 1 
ATOM   2599 H HD11 B LEU   A 1 123 ? 17.269 -3.897  11.277  0.14 16.61 ?  123 LEU   A HD11 1 
ATOM   2600 H HD12 A LEU   A 1 123 ? 17.874 -5.288  10.787  0.86 17.28 ?  123 LEU   A HD12 1 
ATOM   2601 H HD12 B LEU   A 1 123 ? 17.871 -5.259  10.723  0.14 16.61 ?  123 LEU   A HD12 1 
ATOM   2602 H HD13 A LEU   A 1 123 ? 17.775 -5.023  12.351  0.86 17.28 ?  123 LEU   A HD13 1 
ATOM   2603 H HD13 B LEU   A 1 123 ? 17.644 -5.068  12.284  0.14 16.61 ?  123 LEU   A HD13 1 
ATOM   2604 H HD21 A LEU   A 1 123 ? 18.737 -2.177  12.229  0.86 17.35 ?  123 LEU   A HD21 1 
ATOM   2605 H HD21 B LEU   A 1 123 ? 18.678 -2.249  12.361  0.14 16.79 ?  123 LEU   A HD21 1 
ATOM   2606 H HD22 A LEU   A 1 123 ? 19.267 -3.170  13.350  0.86 17.35 ?  123 LEU   A HD22 1 
ATOM   2607 H HD22 B LEU   A 1 123 ? 19.104 -3.284  13.489  0.14 16.79 ?  123 LEU   A HD22 1 
ATOM   2608 H HD23 A LEU   A 1 123 ? 20.296 -2.438  12.386  0.86 17.35 ?  123 LEU   A HD23 1 
ATOM   2609 H HD23 B LEU   A 1 123 ? 20.217 -2.541  12.632  0.14 16.79 ?  123 LEU   A HD23 1 
ATOM   2610 N N    A ALA   A 1 124 ? 19.762 -5.852  8.529   0.86 11.47 ?  124 ALA   A N    1 
ATOM   2611 N N    B ALA   A 1 124 ? 19.909 -6.028  8.521   0.14 12.15 ?  124 ALA   A N    1 
ATOM   2612 C CA   A ALA   A 1 124 ? 20.026 -5.557  7.128   0.86 11.75 ?  124 ALA   A CA   1 
ATOM   2613 C CA   B ALA   A 1 124 ? 20.156 -5.696  7.128   0.14 12.40 ?  124 ALA   A CA   1 
ATOM   2614 C C    A ALA   A 1 124 ? 18.787 -5.102  6.377   0.86 11.57 ?  124 ALA   A C    1 
ATOM   2615 C C    B ALA   A 1 124 ? 18.904 -5.163  6.455   0.14 12.21 ?  124 ALA   A C    1 
ATOM   2616 O O    A ALA   A 1 124 ? 17.664 -5.477  6.737   0.86 12.69 ?  124 ALA   A O    1 
ATOM   2617 O O    B ALA   A 1 124 ? 17.783 -5.426  6.904   0.14 11.92 ?  124 ALA   A O    1 
ATOM   2618 C CB   A ALA   A 1 124 ? 20.610 -6.780  6.411   0.86 12.24 ?  124 ALA   A CB   1 
ATOM   2619 C CB   B ALA   A 1 124 ? 20.649 -6.930  6.359   0.14 12.64 ?  124 ALA   A CB   1 
ATOM   2620 H H    A ALA   A 1 124 ? 18.964 -6.124  8.704   0.86 13.77 ?  124 ALA   A H    1 
ATOM   2621 H H    B ALA   A 1 124 ? 19.211 -6.518  8.639   0.14 14.59 ?  124 ALA   A H    1 
ATOM   2622 H HA   A ALA   A 1 124 ? 20.687 -4.849  7.088   0.86 14.11 ?  124 ALA   A HA   1 
ATOM   2623 H HA   B ALA   A 1 124 ? 20.842 -5.016  7.086   0.14 14.89 ?  124 ALA   A HA   1 
ATOM   2624 H HB1  A ALA   A 1 124 ? 20.782 -6.557  5.480   0.86 14.70 ?  124 ALA   A HB1  1 
ATOM   2625 H HB1  B ALA   A 1 124 ? 20.808 -6.684  5.434   0.14 15.18 ?  124 ALA   A HB1  1 
ATOM   2626 H HB2  A ALA   A 1 124 ? 21.448 -7.033  6.842   0.86 14.70 ?  124 ALA   A HB2  1 
ATOM   2627 H HB2  B ALA   A 1 124 ? 21.472 -7.245  6.764   0.14 15.18 ?  124 ALA   A HB2  1 
ATOM   2628 H HB3  A ALA   A 1 124 ? 19.982 -7.514  6.464   0.86 14.70 ?  124 ALA   A HB3  1 
ATOM   2629 H HB3  B ALA   A 1 124 ? 19.971 -7.622  6.406   0.14 15.18 ?  124 ALA   A HB3  1 
ATOM   2630 N N    A PRO   A 1 125 ? 18.971 -4.339  5.304   0.86 11.29 ?  125 PRO   A N    1 
ATOM   2631 N N    B PRO   A 1 125 ? 19.066 -4.397  5.370   0.14 12.33 ?  125 PRO   A N    1 
ATOM   2632 C CA   A PRO   A 1 125 ? 17.911 -4.100  4.329   0.86 12.01 ?  125 PRO   A CA   1 
ATOM   2633 C CA   B PRO   A 1 125 ? 17.919 -4.022  4.539   0.14 12.50 ?  125 PRO   A CA   1 
ATOM   2634 C C    A PRO   A 1 125 ? 17.969 -5.171  3.244   0.86 12.01 ?  125 PRO   A C    1 
ATOM   2635 C C    B PRO   A 1 125 ? 17.782 -4.974  3.363   0.14 12.73 ?  125 PRO   A C    1 
ATOM   2636 O O    A PRO   A 1 125 ? 18.939 -5.923  3.128   0.86 12.33 ?  125 PRO   A O    1 
ATOM   2637 O O    B PRO   A 1 125 ? 18.596 -5.891  3.209   0.14 12.92 ?  125 PRO   A O    1 
ATOM   2638 C CB   A PRO   A 1 125 ? 18.343 -2.754  3.734   0.86 12.42 ?  125 PRO   A CB   1 
ATOM   2639 C CB   B PRO   A 1 125 ? 18.303 -2.619  4.062   0.14 12.64 ?  125 PRO   A CB   1 
ATOM   2640 C CG   A PRO   A 1 125 ? 19.846 -2.900  3.660   0.86 12.68 ?  125 PRO   A CG   1 
ATOM   2641 C CG   B PRO   A 1 125 ? 19.797 -2.713  3.896   0.14 12.71 ?  125 PRO   A CG   1 
ATOM   2642 C CD   A PRO   A 1 125 ? 20.233 -3.695  4.895   0.86 12.06 ?  125 PRO   A CD   1 
ATOM   2643 C CD   B PRO   A 1 125 ? 20.294 -3.707  4.934   0.14 12.53 ?  125 PRO   A CD   1 
ATOM   2644 H HA   A PRO   A 1 125 ? 17.029 -4.053  4.736   0.86 14.42 ?  125 PRO   A HA   1 
ATOM   2645 H HA   B PRO   A 1 125 ? 17.096 -3.990  5.054   0.14 15.01 ?  125 PRO   A HA   1 
ATOM   2646 H HB2  A PRO   A 1 125 ? 17.950 -2.640  2.851   0.86 14.91 ?  125 PRO   A HB2  1 
ATOM   2647 H HB2  B PRO   A 1 125 ? 17.870 -2.424  3.215   0.14 15.18 ?  125 PRO   A HB2  1 
ATOM   2648 H HB3  A PRO   A 1 125 ? 18.080 -2.032  4.328   0.86 14.91 ?  125 PRO   A HB3  1 
ATOM   2649 H HB3  B PRO   A 1 125 ? 18.066 -1.959  4.734   0.14 15.18 ?  125 PRO   A HB3  1 
ATOM   2650 H HG2  A PRO   A 1 125 ? 20.092 -3.379  2.853   0.86 15.23 ?  125 PRO   A HG2  1 
ATOM   2651 H HG2  B PRO   A 1 125 ? 20.002 -3.027  3.001   0.14 15.26 ?  125 PRO   A HG2  1 
ATOM   2652 H HG3  A PRO   A 1 125 ? 20.260 -2.021  3.674   0.86 15.23 ?  125 PRO   A HG3  1 
ATOM   2653 H HG3  B PRO   A 1 125 ? 20.194 -1.841  4.047   0.14 15.26 ?  125 PRO   A HG3  1 
ATOM   2654 H HD2  A PRO   A 1 125 ? 20.905 -4.361  4.674   0.86 14.48 ?  125 PRO   A HD2  1 
ATOM   2655 H HD2  B PRO   A 1 125 ? 20.911 -4.339  4.530   0.14 15.04 ?  125 PRO   A HD2  1 
ATOM   2656 H HD3  A PRO   A 1 125 ? 20.546 -3.098  5.597   0.86 14.48 ?  125 PRO   A HD3  1 
ATOM   2657 H HD3  B PRO   A 1 125 ? 20.703 -3.241  5.680   0.14 15.04 ?  125 PRO   A HD3  1 
ATOM   2658 N N    A LEU   A 1 126 ? 16.922 -5.209  2.427   0.86 11.99 ?  126 LEU   A N    1 
ATOM   2659 N N    B LEU   A 1 126 ? 16.775 -4.763  2.519   0.14 12.86 ?  126 LEU   A N    1 
ATOM   2660 C CA   A LEU   A 1 126 ? 16.953 -6.033  1.227   0.86 12.33 ?  126 LEU   A CA   1 
ATOM   2661 C CA   B LEU   A 1 126 ? 16.580 -5.586  1.328   0.14 13.18 ?  126 LEU   A CA   1 
ATOM   2662 C C    A LEU   A 1 126 ? 17.892 -5.417  0.195   0.86 12.52 ?  126 LEU   A C    1 
ATOM   2663 C C    B LEU   A 1 126 ? 17.530 -5.094  0.242   0.14 12.75 ?  126 LEU   A C    1 
ATOM   2664 O O    A LEU   A 1 126 ? 17.696 -4.280  -0.244  0.86 13.54 ?  126 LEU   A O    1 
ATOM   2665 O O    B LEU   A 1 126 ? 17.256 -4.101  -0.435  0.14 12.75 ?  126 LEU   A O    1 
ATOM   2666 C CB   A LEU   A 1 126 ? 15.554 -6.176  0.651   0.86 13.41 ?  126 LEU   A CB   1 
ATOM   2667 C CB   B LEU   A 1 126 ? 15.136 -5.485  0.844   0.14 14.13 ?  126 LEU   A CB   1 
ATOM   2668 C CG   A LEU   A 1 126 ? 14.644 -7.134  1.411   0.86 14.71 ?  126 LEU   A CG   1 
ATOM   2669 C CG   B LEU   A 1 126 ? 14.285 -6.754  0.793   0.14 14.74 ?  126 LEU   A CG   1 
ATOM   2670 C CD1  A LEU   A 1 126 ? 13.229 -6.996  0.895   0.86 15.59 ?  126 LEU   A CD1  1 
ATOM   2671 C CD1  B LEU   A 1 126 ? 13.175 -6.587  -0.234  0.14 14.65 ?  126 LEU   A CD1  1 
ATOM   2672 C CD2  A LEU   A 1 126 ? 15.117 -8.571  1.259   0.86 15.05 ?  126 LEU   A CD2  1 
ATOM   2673 C CD2  B LEU   A 1 126 ? 15.119 -7.980  0.484   0.14 15.09 ?  126 LEU   A CD2  1 
ATOM   2674 H H    A LEU   A 1 126 ? 16.192 -4.771  2.541   0.86 14.39 ?  126 LEU   A H    1 
ATOM   2675 H H    B LEU   A 1 126 ? 16.185 -4.146  2.619   0.14 15.44 ?  126 LEU   A H    1 
ATOM   2676 H HA   A LEU   A 1 126 ? 17.286 -6.913  1.450   0.86 14.81 ?  126 LEU   A HA   1 
ATOM   2677 H HA   B LEU   A 1 126 ? 16.801 -6.506  1.546   0.14 15.82 ?  126 LEU   A HA   1 
ATOM   2678 H HB2  A LEU   A 1 126 ? 15.125 -5.305  0.654   0.86 16.10 ?  126 LEU   A HB2  1 
ATOM   2679 H HB2  B LEU   A 1 126 ? 14.663 -4.860  1.412   0.14 16.96 ?  126 LEU   A HB2  1 
ATOM   2680 H HB3  A LEU   A 1 126 ? 15.624 -6.500  -0.261  0.86 16.10 ?  126 LEU   A HB3  1 
ATOM   2681 H HB3  B LEU   A 1 126 ? 15.153 -5.129  -0.056  0.14 16.96 ?  126 LEU   A HB3  1 
ATOM   2682 H HG   A LEU   A 1 126 ? 14.649 -6.910  2.354   0.86 17.66 ?  126 LEU   A HG   1 
ATOM   2683 H HG   B LEU   A 1 126 ? 13.866 -6.885  1.657   0.14 17.69 ?  126 LEU   A HG   1 
ATOM   2684 H HD11 A LEU   A 1 126 ? 12.654 -7.614  1.376   0.86 18.71 ?  126 LEU   A HD11 1 
ATOM   2685 H HD11 B LEU   A 1 126 ? 12.617 -7.380  -0.227  0.14 17.59 ?  126 LEU   A HD11 1 
ATOM   2686 H HD12 A LEU   A 1 126 ? 12.928 -6.086  1.036   0.86 18.71 ?  126 LEU   A HD12 1 
ATOM   2687 H HD12 B LEU   A 1 126 ? 12.646 -5.807  -0.005  0.14 17.59 ?  126 LEU   A HD12 1 
ATOM   2688 H HD13 A LEU   A 1 126 ? 13.216 -7.207  -0.053  0.86 18.71 ?  126 LEU   A HD13 1 
ATOM   2689 H HD13 B LEU   A 1 126 ? 13.572 -6.471  -1.112  0.14 17.59 ?  126 LEU   A HD13 1 
ATOM   2690 H HD21 A LEU   A 1 126 ? 14.444 -9.169  1.614   0.86 18.07 ?  126 LEU   A HD21 1 
ATOM   2691 H HD21 B LEU   A 1 126 ? 14.547 -8.668  0.122   0.14 18.12 ?  126 LEU   A HD21 1 
ATOM   2692 H HD22 A LEU   A 1 126 ? 15.265 -8.758  0.318   0.86 18.07 ?  126 LEU   A HD22 1 
ATOM   2693 H HD22 B LEU   A 1 126 ? 15.802 -7.738  -0.161  0.14 18.12 ?  126 LEU   A HD22 1 
ATOM   2694 H HD23 A LEU   A 1 126 ? 15.950 -8.684  1.749   0.86 18.07 ?  126 LEU   A HD23 1 
ATOM   2695 H HD23 B LEU   A 1 126 ? 15.536 -8.289  1.305   0.14 18.12 ?  126 LEU   A HD23 1 
ATOM   2696 N N    A LEU   A 1 127 ? 18.912 -6.173  -0.196  0.86 12.32 ?  127 LEU   A N    1 
ATOM   2697 N N    B LEU   A 1 127 ? 18.644 -5.798  0.055   0.14 12.64 ?  127 LEU   A N    1 
ATOM   2698 C CA   A LEU   A 1 127 ? 19.896 -5.664  -1.136  0.86 12.19 ?  127 LEU   A CA   1 
ATOM   2699 C CA   B LEU   A 1 127 ? 19.635 -5.361  -0.921  0.14 12.32 ?  127 LEU   A CA   1 
ATOM   2700 C C    A LEU   A 1 127 ? 19.277 -5.453  -2.509  0.86 11.67 ?  127 LEU   A C    1 
ATOM   2701 C C    B LEU   A 1 127 ? 19.039 -5.306  -2.322  0.14 12.53 ?  127 LEU   A C    1 
ATOM   2702 O O    A LEU   A 1 127 ? 18.443 -6.234  -2.976  0.86 11.92 ?  127 LEU   A O    1 
ATOM   2703 O O    B LEU   A 1 127 ? 18.234 -6.157  -2.712  0.14 12.94 ?  127 LEU   A O    1 
ATOM   2704 C CB   A LEU   A 1 127 ? 21.069 -6.635  -1.246  0.86 12.60 ?  127 LEU   A CB   1 
ATOM   2705 C CB   B LEU   A 1 127 ? 20.842 -6.301  -0.912  0.14 11.76 ?  127 LEU   A CB   1 
ATOM   2706 C CG   A LEU   A 1 127 ? 21.874 -6.879  0.031   0.86 13.28 ?  127 LEU   A CG   1 
ATOM   2707 C CG   B LEU   A 1 127 ? 21.761 -6.217  0.309   0.14 11.05 ?  127 LEU   A CG   1 
ATOM   2708 C CD1  A LEU   A 1 127 ? 22.990 -7.856  -0.234  0.86 13.82 ?  127 LEU   A CD1  1 
ATOM   2709 C CD1  B LEU   A 1 127 ? 22.969 -7.133  0.142   0.14 11.26 ?  127 LEU   A CD1  1 
ATOM   2710 C CD2  A LEU   A 1 127 ? 22.443 -5.586  0.574   0.86 14.23 ?  127 LEU   A CD2  1 
ATOM   2711 C CD2  B LEU   A 1 127 ? 22.200 -4.780  0.559   0.14 10.34 ?  127 LEU   A CD2  1 
ATOM   2712 H H    A LEU   A 1 127 ? 19.058 -6.976  0.077   0.86 14.79 ?  127 LEU   A H    1 
ATOM   2713 H H    B LEU   A 1 127 ? 18.847 -6.517  0.479   0.14 15.18 ?  127 LEU   A H    1 
ATOM   2714 H HA   A LEU   A 1 127 ? 20.235 -4.814  -0.817  0.86 14.64 ?  127 LEU   A HA   1 
ATOM   2715 H HA   B LEU   A 1 127 ? 19.929 -4.468  -0.689  0.14 14.80 ?  127 LEU   A HA   1 
ATOM   2716 H HB2  A LEU   A 1 127 ? 20.728 -7.494  -1.538  0.86 15.13 ?  127 LEU   A HB2  1 
ATOM   2717 H HB2  B LEU   A 1 127 ? 20.513 -7.212  -0.968  0.14 14.12 ?  127 LEU   A HB2  1 
ATOM   2718 H HB3  A LEU   A 1 127 ? 21.687 -6.291  -1.908  0.86 15.13 ?  127 LEU   A HB3  1 
ATOM   2719 H HB3  B LEU   A 1 127 ? 21.378 -6.105  -1.696  0.14 14.12 ?  127 LEU   A HB3  1 
ATOM   2720 H HG   A LEU   A 1 127 ? 21.291 -7.266  0.709   0.86 15.95 ?  127 LEU   A HG   1 
ATOM   2721 H HG   B LEU   A 1 127 ? 21.270 -6.518  1.088   0.14 13.27 ?  127 LEU   A HG   1 
ATOM   2722 H HD11 A LEU   A 1 127 ? 23.477 -8.012  0.594   0.86 16.60 ?  127 LEU   A HD11 1 
ATOM   2723 H HD11 B LEU   A 1 127 ? 23.532 -7.058  0.928   0.14 13.53 ?  127 LEU   A HD11 1 
ATOM   2724 H HD12 A LEU   A 1 127 ? 22.617 -8.688  -0.559  0.86 16.60 ?  127 LEU   A HD12 1 
ATOM   2725 H HD12 B LEU   A 1 127 ? 22.661 -8.048  0.042   0.14 13.53 ?  127 LEU   A HD12 1 
ATOM   2726 H HD13 A LEU   A 1 127 ? 23.587 -7.477  -0.898  0.86 16.60 ?  127 LEU   A HD13 1 
ATOM   2727 H HD13 B LEU   A 1 127 ? 23.464 -6.863  -0.647  0.14 13.53 ?  127 LEU   A HD13 1 
ATOM   2728 H HD21 A LEU   A 1 127 ? 23.057 -5.793  1.296   0.86 17.09 ?  127 LEU   A HD21 1 
ATOM   2729 H HD21 B LEU   A 1 127 ? 22.951 -4.783  1.170   0.14 12.42 ?  127 LEU   A HD21 1 
ATOM   2730 H HD22 A LEU   A 1 127 ? 22.915 -5.132  -0.142  0.86 17.09 ?  127 LEU   A HD22 1 
ATOM   2731 H HD22 B LEU   A 1 127 ? 22.458 -4.379  -0.286  0.14 12.42 ?  127 LEU   A HD22 1 
ATOM   2732 H HD23 A LEU   A 1 127 ? 21.718 -5.035  0.899   0.86 17.09 ?  127 LEU   A HD23 1 
ATOM   2733 H HD23 B LEU   A 1 127 ? 21.458 -4.288  0.945   0.14 12.42 ?  127 LEU   A HD23 1 
ATOM   2734 N N    A SER   A 1 128 ? 19.723 -4.397  -3.164  0.86 11.45 ?  128 SER   A N    1 
ATOM   2735 N N    B SER   A 1 128 ? 19.449 -4.290  -3.080  0.14 12.48 ?  128 SER   A N    1 
ATOM   2736 C CA   A SER   A 1 128 ? 19.315 -4.003  -4.502  0.86 11.67 ?  128 SER   A CA   1 
ATOM   2737 C CA   B SER   A 1 128 ? 19.083 -4.041  -4.472  0.14 12.78 ?  128 SER   A CA   1 
ATOM   2738 C C    A SER   A 1 128 ? 17.864 -3.545  -4.586  0.86 11.91 ?  128 SER   A C    1 
ATOM   2739 C C    B SER   A 1 128 ? 17.615 -3.679  -4.680  0.14 12.98 ?  128 SER   A C    1 
ATOM   2740 O O    A SER   A 1 128 ? 17.402 -3.234  -5.678  0.86 13.30 ?  128 SER   A O    1 
ATOM   2741 O O    B SER   A 1 128 ? 17.201 -3.498  -5.831  0.14 13.54 ?  128 SER   A O    1 
ATOM   2742 C CB   A SER   A 1 128 ? 19.639 -5.047  -5.579  0.86 12.43 ?  128 SER   A CB   1 
ATOM   2743 C CB   B SER   A 1 128 ? 19.487 -5.178  -5.421  0.14 12.85 ?  128 SER   A CB   1 
ATOM   2744 O OG   A SER   A 1 128 ? 21.045 -5.249  -5.655  0.86 12.96 ?  128 SER   A OG   1 
ATOM   2745 O OG   B SER   A 1 128 ? 20.899 -5.263  -5.524  0.14 12.88 ?  128 SER   A OG   1 
ATOM   2746 H H    A SER   A 1 128 ? 20.318 -3.866  -2.832  0.86 13.75 ?  128 SER   A H    1 
ATOM   2747 H H    B SER   A 1 128 ? 19.989 -3.686  -2.783  0.14 14.99 ?  128 SER   A H    1 
ATOM   2748 H HA   A SER   A 1 128 ? 19.850 -3.228  -4.725  0.86 14.01 ?  128 SER   A HA   1 
ATOM   2749 H HA   B SER   A 1 128 ? 19.590 -3.269  -4.755  0.14 15.35 ?  128 SER   A HA   1 
ATOM   2750 H HB2  A SER   A 1 128 ? 19.202 -5.880  -5.360  0.86 14.93 ?  128 SER   A HB2  1 
ATOM   2751 H HB2  B SER   A 1 128 ? 19.139 -6.014  -5.081  0.14 15.43 ?  128 SER   A HB2  1 
ATOM   2752 H HB3  A SER   A 1 128 ? 19.317 -4.717  -6.440  0.86 14.93 ?  128 SER   A HB3  1 
ATOM   2753 H HB3  B SER   A 1 128 ? 19.118 -4.997  -6.302  0.14 15.43 ?  128 SER   A HB3  1 
ATOM   2754 H HG   A SER   A 1 128 ? 21.429 -4.525  -5.843  0.86 15.56 ?  128 SER   A HG   1 
ATOM   2755 H HG   B SER   A 1 128 ? 21.206 -4.533  -5.809  0.14 15.47 ?  128 SER   A HG   1 
ATOM   2756 N N    A ALA   A 1 129 ? 17.157 -3.443  -3.458  0.86 12.94 ?  129 ALA   A N    1 
ATOM   2757 N N    B ALA   A 1 129 ? 16.820 -3.551  -3.622  0.14 13.04 ?  129 ALA   A N    1 
ATOM   2758 C CA   A ALA   A 1 129 ? 15.795 -2.937  -3.444  0.86 13.48 ?  129 ALA   A CA   1 
ATOM   2759 C CA   B ALA   A 1 129 ? 15.445 -3.101  -3.772  0.14 13.51 ?  129 ALA   A CA   1 
ATOM   2760 C C    A ALA   A 1 129 ? 15.805 -1.410  -3.432  0.86 12.92 ?  129 ALA   A C    1 
ATOM   2761 C C    B ALA   A 1 129 ? 15.402 -1.572  -3.802  0.14 13.79 ?  129 ALA   A C    1 
ATOM   2762 O O    A ALA   A 1 129 ? 16.855 -0.766  -3.545  0.86 13.03 ?  129 ALA   A O    1 
ATOM   2763 O O    B ALA   A 1 129 ? 16.434 -0.894  -3.809  0.14 13.82 ?  129 ALA   A O    1 
ATOM   2764 C CB   A ALA   A 1 129 ? 15.020 -3.522  -2.261  0.86 14.90 ?  129 ALA   A CB   1 
ATOM   2765 C CB   B ALA   A 1 129 ? 14.568 -3.697  -2.671  0.14 13.65 ?  129 ALA   A CB   1 
ATOM   2766 H H    A ALA   A 1 129 ? 17.460 -3.652  -2.674  0.86 15.54 ?  129 ALA   A H    1 
ATOM   2767 H H    B ALA   A 1 129 ? 17.052 -3.713  -2.810  0.14 15.65 ?  129 ALA   A H    1 
ATOM   2768 H HA   A ALA   A 1 129 ? 15.360 -3.216  -4.257  0.86 16.18 ?  129 ALA   A HA   1 
ATOM   2769 H HA   B ALA   A 1 129 ? 15.101 -3.426  -4.617  0.14 16.22 ?  129 ALA   A HA   1 
ATOM   2770 H HB1  A ALA   A 1 129 ? 14.111 -3.182  -2.285  0.86 17.89 ?  129 ALA   A HB1  1 
ATOM   2771 H HB1  B ALA   A 1 129 ? 13.709 -3.244  -2.663  0.14 16.38 ?  129 ALA   A HB1  1 
ATOM   2772 H HB2  A ALA   A 1 129 ? 15.013 -4.488  -2.341  0.86 17.89 ?  129 ALA   A HB2  1 
ATOM   2773 H HB2  B ALA   A 1 129 ? 14.437 -4.642  -2.850  0.14 16.38 ?  129 ALA   A HB2  1 
ATOM   2774 H HB3  A ALA   A 1 129 ? 15.451 -3.259  -1.435  0.86 17.89 ?  129 ALA   A HB3  1 
ATOM   2775 H HB3  B ALA   A 1 129 ? 15.008 -3.583  -1.816  0.14 16.38 ?  129 ALA   A HB3  1 
ATOM   2776 N N    A GLY   A 1 130 ? 14.617 -0.821  -3.326  0.86 13.39 ?  130 GLY   A N    1 
ATOM   2777 N N    B GLY   A 1 130 ? 14.193 -1.021  -3.854  0.14 13.99 ?  130 GLY   A N    1 
ATOM   2778 C CA   A GLY   A 1 130 ? 14.512 0.627   -3.296  0.86 14.29 ?  130 GLY   A CA   1 
ATOM   2779 C CA   B GLY   A 1 130 ? 14.040 0.424   -3.800  0.14 14.28 ?  130 GLY   A CA   1 
ATOM   2780 C C    A GLY   A 1 130 ? 15.113 1.235   -4.543  0.86 13.78 ?  130 GLY   A C    1 
ATOM   2781 C C    B GLY   A 1 130 ? 14.673 1.090   -5.005  0.14 14.74 ?  130 GLY   A C    1 
ATOM   2782 O O    A GLY   A 1 130 ? 14.865 0.778   -5.663  0.86 14.14 ?  130 GLY   A O    1 
ATOM   2783 O O    B GLY   A 1 130 ? 14.458 0.690   -6.154  0.14 14.83 ?  130 GLY   A O    1 
ATOM   2784 H H    A GLY   A 1 130 ? 13.866 -1.237  -3.271  0.86 16.07 ?  130 GLY   A H    1 
ATOM   2785 H H    B GLY   A 1 130 ? 13.455 -1.452  -3.932  0.14 16.80 ?  130 GLY   A H    1 
ATOM   2786 H HA2  A GLY   A 1 130 ? 13.576 0.886   -3.236  0.86 17.16 ?  130 GLY   A HA2  1 
ATOM   2787 H HA2  B GLY   A 1 130 ? 13.094 0.652   -3.752  0.14 17.15 ?  130 GLY   A HA2  1 
ATOM   2788 H HA3  A GLY   A 1 130 ? 14.982 0.977   -2.529  0.86 17.16 ?  130 GLY   A HA3  1 
ATOM   2789 H HA3  B GLY   A 1 130 ? 14.477 0.776   -3.009  0.14 17.15 ?  130 GLY   A HA3  1 
ATOM   2790 N N    A ILE   A 1 131 ? 15.918 2.286   -4.351  0.86 13.57 ?  131 ILE   A N    1 
ATOM   2791 N N    B ILE   A 1 131 ? 15.481 2.119   -4.739  0.14 15.07 ?  131 ILE   A N    1 
ATOM   2792 C CA   A ILE   A 1 131 ? 16.481 3.025   -5.477  0.86 13.60 ?  131 ILE   A CA   1 
ATOM   2793 C CA   B ILE   A 1 131 ? 16.085 2.913   -5.804  0.14 15.52 ?  131 ILE   A CA   1 
ATOM   2794 C C    A ILE   A 1 131 ? 17.499 2.229   -6.283  0.86 12.78 ?  131 ILE   A C    1 
ATOM   2795 C C    B ILE   A 1 131 ? 17.165 2.164   -6.567  0.14 15.69 ?  131 ILE   A C    1 
ATOM   2796 O O    A ILE   A 1 131 ? 17.930 2.702   -7.337  0.86 13.89 ?  131 ILE   A O    1 
ATOM   2797 O O    B ILE   A 1 131 ? 17.674 2.684   -7.567  0.14 15.83 ?  131 ILE   A O    1 
ATOM   2798 C CB   A ILE   A 1 131 ? 17.070 4.387   -5.049  0.86 14.78 ?  131 ILE   A CB   1 
ATOM   2799 C CB   B ILE   A 1 131 ? 16.631 4.252   -5.264  0.14 15.82 ?  131 ILE   A CB   1 
ATOM   2800 C CG1  A ILE   A 1 131 ? 18.330 4.214   -4.188  0.86 16.39 ?  131 ILE   A CG1  1 
ATOM   2801 C CG1  B ILE   A 1 131 ? 17.671 4.004   -4.169  0.14 16.21 ?  131 ILE   A CG1  1 
ATOM   2802 C CG2  A ILE   A 1 131 ? 16.015 5.210   -4.323  0.86 15.47 ?  131 ILE   A CG2  1 
ATOM   2803 C CG2  B ILE   A 1 131 ? 15.492 5.125   -4.745  0.14 15.74 ?  131 ILE   A CG2  1 
ATOM   2804 C CD1  A ILE   A 1 131 ? 18.996 5.540   -3.809  0.86 17.96 ?  131 ILE   A CD1  1 
ATOM   2805 C CD1  B ILE   A 1 131 ? 18.154 5.264   -3.495  0.14 16.47 ?  131 ILE   A CD1  1 
ATOM   2806 H H    A ILE   A 1 131 ? 16.131 2.591   -3.580  0.86 16.29 ?  131 ILE   A H    1 
ATOM   2807 H H    B ILE   A 1 131 ? 15.695 2.368   -3.946  0.14 18.09 ?  131 ILE   A H    1 
ATOM   2808 H HA   A ILE   A 1 131 ? 15.756 3.225   -6.083  0.86 16.33 ?  131 ILE   A HA   1 
ATOM   2809 H HA   B ILE   A 1 131 ? 15.393 3.129   -6.443  0.14 18.63 ?  131 ILE   A HA   1 
ATOM   2810 H HB   A ILE   A 1 131 ? 17.320 4.866   -5.853  0.86 17.74 ?  131 ILE   A HB   1 
ATOM   2811 H HB   B ILE   A 1 131 ? 17.063 4.722   -5.994  0.14 18.99 ?  131 ILE   A HB   1 
ATOM   2812 H HG12 A ILE   A 1 131 ? 18.090 3.754   -3.370  0.86 19.68 ?  131 ILE   A HG12 1 
ATOM   2813 H HG12 B ILE   A 1 131 ? 17.287 3.436   -3.485  0.14 19.46 ?  131 ILE   A HG12 1 
ATOM   2814 H HG13 A ILE   A 1 131 ? 18.982 3.690   -4.681  0.86 19.68 ?  131 ILE   A HG13 1 
ATOM   2815 H HG13 B ILE   A 1 131 ? 18.441 3.566   -4.566  0.14 19.46 ?  131 ILE   A HG13 1 
ATOM   2816 H HG21 A ILE   A 1 131 ? 16.340 6.117   -4.217  0.86 18.57 ?  131 ILE   A HG21 1 
ATOM   2817 H HG21 B ILE   A 1 131 ? 15.823 6.024   -4.592  0.14 18.90 ?  131 ILE   A HG21 1 
ATOM   2818 H HG22 A ILE   A 1 131 ? 15.201 5.210   -4.850  0.86 18.57 ?  131 ILE   A HG22 1 
ATOM   2819 H HG22 B ILE   A 1 131 ? 14.783 5.145   -5.406  0.14 18.90 ?  131 ILE   A HG22 1 
ATOM   2820 H HG23 A ILE   A 1 131 ? 15.847 4.811   -3.455  0.86 18.57 ?  131 ILE   A HG23 1 
ATOM   2821 H HG23 B ILE   A 1 131 ? 15.159 4.748   -3.916  0.14 18.90 ?  131 ILE   A HG23 1 
ATOM   2822 H HD11 A ILE   A 1 131 ? 19.843 5.353   -3.371  0.86 21.56 ?  131 ILE   A HD11 1 
ATOM   2823 H HD11 B ILE   A 1 131 ? 18.939 5.057   -2.967  0.14 19.78 ?  131 ILE   A HD11 1 
ATOM   2824 H HD12 A ILE   A 1 131 ? 19.148 6.060   -4.613  0.86 21.56 ?  131 ILE   A HD12 1 
ATOM   2825 H HD12 B ILE   A 1 131 ? 18.373 5.920   -4.175  0.14 19.78 ?  131 ILE   A HD12 1 
ATOM   2826 H HD13 A ILE   A 1 131 ? 18.413 6.026   -3.205  0.86 21.56 ?  131 ILE   A HD13 1 
ATOM   2827 H HD13 B ILE   A 1 131 ? 17.449 5.606   -2.922  0.14 19.78 ?  131 ILE   A HD13 1 
ATOM   2828 N N    A PHE   A 1 132 ? 17.894 1.032   -5.835  0.86 12.30 ?  132 PHE   A N    1 
ATOM   2829 N N    B PHE   A 1 132 ? 17.535 0.959   -6.127  0.14 15.63 ?  132 PHE   A N    1 
ATOM   2830 C CA   A PHE   A 1 132 ? 18.743 0.173   -6.657  0.86 12.84 ?  132 PHE   A CA   1 
ATOM   2831 C CA   B PHE   A 1 132 ? 18.485 0.152   -6.883  0.14 15.60 ?  132 PHE   A CA   1 
ATOM   2832 C C    A PHE   A 1 132 ? 17.953 -0.589  -7.719  0.86 13.49 ?  132 PHE   A C    1 
ATOM   2833 C C    B PHE   A 1 132 ? 17.847 -0.528  -8.089  0.14 15.80 ?  132 PHE   A C    1 
ATOM   2834 O O    A PHE   A 1 132 ? 18.559 -1.237  -8.577  0.86 14.30 ?  132 PHE   A O    1 
ATOM   2835 O O    B PHE   A 1 132 ? 18.558 -0.851  -9.046  0.14 15.86 ?  132 PHE   A O    1 
ATOM   2836 C CB   A PHE   A 1 132 ? 19.554 -0.803  -5.796  0.86 12.25 ?  132 PHE   A CB   1 
ATOM   2837 C CB   B PHE   A 1 132 ? 19.154 -0.881  -5.974  0.14 15.42 ?  132 PHE   A CB   1 
ATOM   2838 C CG   A PHE   A 1 132 ? 20.771 -0.195  -5.133  0.86 12.13 ?  132 PHE   A CG   1 
ATOM   2839 C CG   B PHE   A 1 132 ? 20.289 -0.327  -5.158  0.14 15.23 ?  132 PHE   A CG   1 
ATOM   2840 C CD1  A PHE   A 1 132 ? 20.649 0.837   -4.220  0.86 13.06 ?  132 PHE   A CD1  1 
ATOM   2841 C CD1  B PHE   A 1 132 ? 20.043 0.445   -4.034  0.14 15.14 ?  132 PHE   A CD1  1 
ATOM   2842 C CD2  A PHE   A 1 132 ? 22.034 -0.716  -5.381  0.86 13.00 ?  132 PHE   A CD2  1 
ATOM   2843 C CD2  B PHE   A 1 132 ? 21.603 -0.588  -5.510  0.14 15.11 ?  132 PHE   A CD2  1 
ATOM   2844 C CE1  A PHE   A 1 132 ? 21.771 1.363   -3.595  0.86 13.66 ?  132 PHE   A CE1  1 
ATOM   2845 C CE1  B PHE   A 1 132 ? 21.087 0.951   -3.281  0.14 15.08 ?  132 PHE   A CE1  1 
ATOM   2846 C CE2  A PHE   A 1 132 ? 23.157 -0.191  -4.763  0.86 13.45 ?  132 PHE   A CE2  1 
ATOM   2847 C CE2  B PHE   A 1 132 ? 22.651 -0.086  -4.761  0.14 15.18 ?  132 PHE   A CE2  1 
ATOM   2848 C CZ   A PHE   A 1 132 ? 23.022 0.846   -3.868  0.86 13.55 ?  132 PHE   A CZ   1 
ATOM   2849 C CZ   B PHE   A 1 132 ? 22.392 0.686   -3.647  0.14 14.97 ?  132 PHE   A CZ   1 
ATOM   2850 H H    A PHE   A 1 132 ? 17.693 0.700   -5.059  0.86 14.77 ?  132 PHE   A H    1 
ATOM   2851 H H    B PHE   A 1 132 ? 17.257 0.595   -5.398  0.14 18.76 ?  132 PHE   A H    1 
ATOM   2852 H HA   A PHE   A 1 132 ? 19.381 0.737   -7.117  0.86 15.42 ?  132 PHE   A HA   1 
ATOM   2853 H HA   B PHE   A 1 132 ? 19.179 0.736   -7.217  0.14 18.73 ?  132 PHE   A HA   1 
ATOM   2854 H HB2  A PHE   A 1 132 ? 18.985 -1.145  -5.089  0.86 14.70 ?  132 PHE   A HB2  1 
ATOM   2855 H HB2  B PHE   A 1 132 ? 18.494 -1.227  -5.356  0.14 18.51 ?  132 PHE   A HB2  1 
ATOM   2856 H HB3  A PHE   A 1 132 ? 19.861 -1.537  -6.353  0.86 14.70 ?  132 PHE   A HB3  1 
ATOM   2857 H HB3  B PHE   A 1 132 ? 19.506 -1.600  -6.520  0.14 18.51 ?  132 PHE   A HB3  1 
ATOM   2858 H HD1  A PHE   A 1 132 ? 19.814 1.187   -4.026  0.86 15.69 ?  132 PHE   A HD1  1 
ATOM   2859 H HD1  B PHE   A 1 132 ? 19.166 0.628   -3.785  0.14 18.18 ?  132 PHE   A HD1  1 
ATOM   2860 H HD2  A PHE   A 1 132 ? 22.133 -1.418  -5.987  0.86 15.61 ?  132 PHE   A HD2  1 
ATOM   2861 H HD2  B PHE   A 1 132 ? 21.783 -1.106  -6.261  0.14 18.14 ?  132 PHE   A HD2  1 
ATOM   2862 H HE1  A PHE   A 1 132 ? 21.684 2.065   -2.991  0.86 16.40 ?  132 PHE   A HE1  1 
ATOM   2863 H HE1  B PHE   A 1 132 ? 20.910 1.471   -2.530  0.14 18.11 ?  132 PHE   A HE1  1 
ATOM   2864 H HE2  A PHE   A 1 132 ? 23.998 -0.543  -4.955  0.86 16.15 ?  132 PHE   A HE2  1 
ATOM   2865 H HE2  B PHE   A 1 132 ? 23.529 -0.265  -5.010  0.14 18.23 ?  132 PHE   A HE2  1 
ATOM   2866 H HZ   A PHE   A 1 132 ? 23.777 1.204   -3.455  0.86 16.27 ?  132 PHE   A HZ   1 
ATOM   2867 H HZ   B PHE   A 1 132 ? 23.095 1.026   -3.142  0.14 17.97 ?  132 PHE   A HZ   1 
ATOM   2868 N N    A GLY   A 1 133 ? 16.624 -0.544  -7.680  0.86 13.45 ?  133 GLY   A N    1 
ATOM   2869 N N    B GLY   A 1 133 ? 16.535 -0.758  -8.063  0.14 15.87 ?  133 GLY   A N    1 
ATOM   2870 C CA   A GLY   A 1 133 ? 15.815 -0.905  -8.826  0.86 14.66 ?  133 GLY   A CA   1 
ATOM   2871 C CA   B GLY   A 1 133 ? 15.801 -1.144  -9.250  0.14 15.97 ?  133 GLY   A CA   1 
ATOM   2872 C C    A GLY   A 1 133 ? 15.478 -2.370  -9.014  0.86 14.63 ?  133 GLY   A C    1 
ATOM   2873 C C    B GLY   A 1 133 ? 15.452 -2.611  -9.388  0.14 16.25 ?  133 GLY   A C    1 
ATOM   2874 O O    A GLY   A 1 133 ? 14.777 -2.688  -9.981  0.86 16.33 ?  133 GLY   A O    1 
ATOM   2875 O O    B GLY   A 1 133 ? 14.855 -2.986  -10.404 0.14 16.70 ?  133 GLY   A O    1 
ATOM   2876 H H    A GLY   A 1 133 ? 16.165 -0.305  -6.989  0.86 16.15 ?  133 GLY   A H    1 
ATOM   2877 H H    B GLY   A 1 133 ? 16.046 -0.692  -7.358  0.14 19.05 ?  133 GLY   A H    1 
ATOM   2878 H HA2  A GLY   A 1 133 ? 14.971 -0.429  -8.768  0.86 17.60 ?  133 GLY   A HA2  1 
ATOM   2879 H HA2  B GLY   A 1 133 ? 14.976 -0.636  -9.278  0.14 19.18 ?  133 GLY   A HA2  1 
ATOM   2880 H HA3  A GLY   A 1 133 ? 16.266 -0.606  -9.629  0.86 17.60 ?  133 GLY   A HA3  1 
ATOM   2881 H HA3  B GLY   A 1 133 ? 16.324 -0.905  -10.028 0.14 19.18 ?  133 GLY   A HA3  1 
ATOM   2882 N N    A ALA   A 1 134 ? 15.945 -3.271  -8.151  0.86 14.25 ?  134 ALA   A N    1 
ATOM   2883 N N    B ALA   A 1 134 ? 15.800 -3.452  -8.421  0.14 16.03 ?  134 ALA   A N    1 
ATOM   2884 C CA   A ALA   A 1 134 ? 15.588 -4.672  -8.310  0.86 14.81 ?  134 ALA   A CA   1 
ATOM   2885 C CA   B ALA   A 1 134 ? 15.518 -4.875  -8.541  0.14 16.02 ?  134 ALA   A CA   1 
ATOM   2886 C C    A ALA   A 1 134 ? 14.230 -4.950  -7.672  0.86 15.09 ?  134 ALA   A C    1 
ATOM   2887 C C    B ALA   A 1 134 ? 14.166 -5.222  -7.925  0.14 15.95 ?  134 ALA   A C    1 
ATOM   2888 O O    A ALA   A 1 134 ? 13.707 -4.158  -6.882  0.86 16.17 ?  134 ALA   A O    1 
ATOM   2889 O O    B ALA   A 1 134 ? 13.573 -4.444  -7.174  0.14 16.07 ?  134 ALA   A O    1 
ATOM   2890 C CB   A ALA   A 1 134 ? 16.649 -5.580  -7.689  0.86 15.70 ?  134 ALA   A CB   1 
ATOM   2891 C CB   B ALA   A 1 134 ? 16.616 -5.707  -7.880  0.14 16.11 ?  134 ALA   A CB   1 
ATOM   2892 H H    A ALA   A 1 134 ? 16.466 -3.097  -7.485  0.86 17.11 ?  134 ALA   A H    1 
ATOM   2893 H H    B ALA   A 1 134 ? 16.204 -3.228  -7.694  0.14 19.24 ?  134 ALA   A H    1 
ATOM   2894 H HA   A ALA   A 1 134 ? 15.529 -4.879  -9.257  0.86 17.78 ?  134 ALA   A HA   1 
ATOM   2895 H HA   B ALA   A 1 134 ? 15.488 -5.110  -9.478  0.14 19.23 ?  134 ALA   A HA   1 
ATOM   2896 H HB1  A ALA   A 1 134 ? 16.389 -6.503  -7.823  0.86 18.85 ?  134 ALA   A HB1  1 
ATOM   2897 H HB1  B ALA   A 1 134 ? 16.421 -6.648  -8.018  0.14 19.34 ?  134 ALA   A HB1  1 
ATOM   2898 H HB2  A ALA   A 1 134 ? 17.502 -5.409  -8.121  0.86 18.85 ?  134 ALA   A HB2  1 
ATOM   2899 H HB2  B ALA   A 1 134 ? 17.465 -5.481  -8.289  0.14 19.34 ?  134 ALA   A HB2  1 
ATOM   2900 H HB3  A ALA   A 1 134 ? 16.713 -5.385  -6.742  0.86 18.85 ?  134 ALA   A HB3  1 
ATOM   2901 H HB3  B ALA   A 1 134 ? 16.638 -5.508  -6.933  0.14 19.34 ?  134 ALA   A HB3  1 
ATOM   2902 N N    A ASP   A 1 135 ? 13.661 -6.098  -8.029  0.86 15.83 ?  135 ASP   A N    1 
ATOM   2903 N N    B ASP   A 1 135 ? 13.682 -6.412  -8.262  0.14 15.88 ?  135 ASP   A N    1 
ATOM   2904 C CA   A ASP   A 1 135 ? 12.404 -6.547  -7.444  0.86 17.02 ?  135 ASP   A CA   1 
ATOM   2905 C CA   B ASP   A 1 135 ? 12.436 -6.918  -7.703  0.14 16.00 ?  135 ASP   A CA   1 
ATOM   2906 C C    A ASP   A 1 135 ? 12.654 -7.013  -6.016  0.86 16.45 ?  135 ASP   A C    1 
ATOM   2907 C C    B ASP   A 1 135 ? 12.645 -7.236  -6.229  0.14 15.76 ?  135 ASP   A C    1 
ATOM   2908 O O    A ASP   A 1 135 ? 13.410 -7.971  -5.818  0.86 16.23 ?  135 ASP   A O    1 
ATOM   2909 O O    B ASP   A 1 135 ? 13.507 -8.062  -5.901  0.14 15.74 ?  135 ASP   A O    1 
ATOM   2910 C CB   A ASP   A 1 135 ? 11.874 -7.708  -8.280  0.86 19.70 ?  135 ASP   A CB   1 
ATOM   2911 C CB   B ASP   A 1 135 ? 12.029 -8.185  -8.447  0.14 16.48 ?  135 ASP   A CB   1 
ATOM   2912 C CG   A ASP   A 1 135 ? 10.572 -8.284  -7.743  0.86 22.99 ?  135 ASP   A CG   1 
ATOM   2913 C CG   B ASP   A 1 135 ? 10.842 -8.883  -7.815  0.14 16.60 ?  135 ASP   A CG   1 
ATOM   2914 O OD1  A ASP   A 1 135 ? 10.067 -7.782  -6.715  0.86 23.63 ?  135 ASP   A OD1  1 
ATOM   2915 O OD1  B ASP   A 1 135 ? 10.103 -8.239  -7.042  0.14 16.51 ?  135 ASP   A OD1  1 
ATOM   2916 O OD2  A ASP   A 1 135 ? 10.046 -9.232  -8.369  0.86 25.94 -1 135 ASP   A OD2  1 
ATOM   2917 O OD2  B ASP   A 1 135 ? 10.658 -10.086 -8.087  0.14 17.11 -1 135 ASP   A OD2  1 
ATOM   2918 H H    A ASP   A 1 135 ? 13.984 -6.640  -8.611  0.86 19.00 ?  135 ASP   A H    1 
ATOM   2919 H H    B ASP   A 1 135 ? 14.057 -6.952  -8.815  0.14 19.07 ?  135 ASP   A H    1 
ATOM   2920 H HA   A ASP   A 1 135 ? 11.752 -5.830  -7.457  0.86 20.44 ?  135 ASP   A HA   1 
ATOM   2921 H HA   B ASP   A 1 135 ? 11.734 -6.258  -7.806  0.14 19.21 ?  135 ASP   A HA   1 
ATOM   2922 H HB2  A ASP   A 1 135 ? 11.709 -7.397  -9.182  0.86 23.65 ?  135 ASP   A HB2  1 
ATOM   2923 H HB2  B ASP   A 1 135 ? 11.797 -7.957  -9.359  0.14 19.79 ?  135 ASP   A HB2  1 
ATOM   2924 H HB3  A ASP   A 1 135 ? 12.541 -8.416  -8.291  0.86 23.65 ?  135 ASP   A HB3  1 
ATOM   2925 H HB3  B ASP   A 1 135 ? 12.763 -8.814  -8.434  0.14 19.79 ?  135 ASP   A HB3  1 
ATOM   2926 N N    A PRO   A 1 136 ? 12.067 -6.371  -4.999  0.86 16.44 ?  136 PRO   A N    1 
ATOM   2927 N N    B PRO   A 1 136 ? 11.897 -6.617  -5.312  0.14 15.58 ?  136 PRO   A N    1 
ATOM   2928 C CA   A PRO   A 1 136 ? 12.320 -6.807  -3.614  0.86 16.26 ?  136 PRO   A CA   1 
ATOM   2929 C CA   B PRO   A 1 136 ? 12.077 -6.953  -3.890  0.14 15.41 ?  136 PRO   A CA   1 
ATOM   2930 C C    A PRO   A 1 136 ? 11.881 -8.228  -3.312  0.86 15.48 ?  136 PRO   A C    1 
ATOM   2931 C C    B PRO   A 1 136 ? 11.755 -8.401  -3.571  0.14 15.49 ?  136 PRO   A C    1 
ATOM   2932 O O    A PRO   A 1 136 ? 12.470 -8.861  -2.429  0.86 15.08 ?  136 PRO   A O    1 
ATOM   2933 O O    B PRO   A 1 136 ? 12.449 -9.018  -2.753  0.14 15.66 ?  136 PRO   A O    1 
ATOM   2934 C CB   A PRO   A 1 136 ? 11.547 -5.780  -2.774  0.86 17.32 ?  136 PRO   A CB   1 
ATOM   2935 C CB   B PRO   A 1 136 ? 11.138 -5.970  -3.177  0.14 15.32 ?  136 PRO   A CB   1 
ATOM   2936 C CG   A PRO   A 1 136 ? 10.519 -5.217  -3.706  0.86 18.63 ?  136 PRO   A CG   1 
ATOM   2937 C CG   B PRO   A 1 136 ? 10.122 -5.599  -4.212  0.14 15.44 ?  136 PRO   A CG   1 
ATOM   2938 C CD   A PRO   A 1 136 ? 11.165 -5.209  -5.053  0.86 17.49 ?  136 PRO   A CD   1 
ATOM   2939 C CD   B PRO   A 1 136 ? 10.858 -5.594  -5.513  0.14 15.52 ?  136 PRO   A CD   1 
ATOM   2940 H HA   A PRO   A 1 136 ? 13.268 -6.725  -3.408  0.86 19.52 ?  136 PRO   A HA   1 
ATOM   2941 H HA   B PRO   A 1 136 ? 12.989 -6.771  -3.614  0.14 18.50 ?  136 PRO   A HA   1 
ATOM   2942 H HB2  A PRO   A 1 136 ? 11.124 -6.224  -2.021  0.86 20.79 ?  136 PRO   A HB2  1 
ATOM   2943 H HB2  B PRO   A 1 136 ? 10.717 -6.406  -2.421  0.14 18.40 ?  136 PRO   A HB2  1 
ATOM   2944 H HB3  A PRO   A 1 136 ? 12.152 -5.086  -2.466  0.86 20.79 ?  136 PRO   A HB3  1 
ATOM   2945 H HB3  B PRO   A 1 136 ? 11.638 -5.189  -2.889  0.14 18.40 ?  136 PRO   A HB3  1 
ATOM   2946 H HG2  A PRO   A 1 136 ? 9.735  -5.787  -3.710  0.86 22.37 ?  136 PRO   A HG2  1 
ATOM   2947 H HG2  B PRO   A 1 136 ? 9.413  -6.260  -4.225  0.14 18.53 ?  136 PRO   A HG2  1 
ATOM   2948 H HG3  A PRO   A 1 136 ? 10.289 -4.316  -3.436  0.86 22.37 ?  136 PRO   A HG3  1 
ATOM   2949 H HG3  B PRO   A 1 136 ? 9.767  -4.718  -4.020  0.14 18.53 ?  136 PRO   A HG3  1 
ATOM   2950 H HD2  A PRO   A 1 136 ? 10.495 -5.334  -5.748  0.86 21.00 ?  136 PRO   A HD2  1 
ATOM   2951 H HD2  B PRO   A 1 136 ? 10.267 -5.850  -6.238  0.14 18.63 ?  136 PRO   A HD2  1 
ATOM   2952 H HD3  A PRO   A 1 136 ? 11.670 -4.393  -5.190  0.86 21.00 ?  136 PRO   A HD3  1 
ATOM   2953 H HD3  B PRO   A 1 136 ? 11.270 -4.730  -5.674  0.14 18.63 ?  136 PRO   A HD3  1 
ATOM   2954 N N    A ILE   A 1 137 ? 10.851 -8.739  -3.988  0.86 15.57 ?  137 ILE   A N    1 
ATOM   2955 N N    B ILE   A 1 137 ? 10.716 -8.965  -4.193  0.14 15.54 ?  137 ILE   A N    1 
ATOM   2956 C CA   A ILE   A 1 137 ? 10.462 -10.133 -3.795  0.86 16.31 ?  137 ILE   A CA   1 
ATOM   2957 C CA   B ILE   A 1 137 ? 10.421 -10.382 -4.005  0.14 15.69 ?  137 ILE   A CA   1 
ATOM   2958 C C    A ILE   A 1 137 ? 11.602 -11.057 -4.201  0.86 15.89 ?  137 ILE   A C    1 
ATOM   2959 C C    B ILE   A 1 137 ? 11.633 -11.221 -4.381  0.14 15.42 ?  137 ILE   A C    1 
ATOM   2960 O O    A ILE   A 1 137 ? 11.912 -12.037 -3.509  0.86 16.04 ?  137 ILE   A O    1 
ATOM   2961 O O    B ILE   A 1 137 ? 11.952 -12.215 -3.716  0.14 15.43 ?  137 ILE   A O    1 
ATOM   2962 C CB   A ILE   A 1 137 ? 9.169  -10.441 -4.571  0.86 17.69 ?  137 ILE   A CB   1 
ATOM   2963 C CB   B ILE   A 1 137 ? 9.172  -10.787 -4.811  0.14 16.09 ?  137 ILE   A CB   1 
ATOM   2964 C CG1  A ILE   A 1 137 ? 8.003  -9.601  -4.036  0.86 19.62 ?  137 ILE   A CG1  1 
ATOM   2965 C CG1  B ILE   A 1 137 ? 7.952  -9.989  -4.346  0.14 16.33 ?  137 ILE   A CG1  1 
ATOM   2966 C CG2  A ILE   A 1 137 ? 8.858  -11.933 -4.504  0.86 18.45 ?  137 ILE   A CG2  1 
ATOM   2967 C CG2  B ILE   A 1 137 ? 8.908  -12.284 -4.679  0.14 16.23 ?  137 ILE   A CG2  1 
ATOM   2968 C CD1  A ILE   A 1 137 ? 6.722  -9.755  -4.824  0.86 21.46 ?  137 ILE   A CD1  1 
ATOM   2969 C CD1  B ILE   A 1 137 ? 6.683  -10.311 -5.111  0.14 16.59 ?  137 ILE   A CD1  1 
ATOM   2970 H H    A ILE   A 1 137 ? 10.373 -8.303  -4.553  0.86 18.70 ?  137 ILE   A H    1 
ATOM   2971 H H    B ILE   A 1 137 ? 10.180 -8.556  -4.723  0.14 18.66 ?  137 ILE   A H    1 
ATOM   2972 H HA   A ILE   A 1 137 ? 10.289 -10.280 -2.855  0.86 19.58 ?  137 ILE   A HA   1 
ATOM   2973 H HA   B ILE   A 1 137 ? 10.233 -10.546 -3.069  0.14 18.84 ?  137 ILE   A HA   1 
ATOM   2974 H HB   A ILE   A 1 137 ? 9.310  -10.201 -5.499  0.86 21.24 ?  137 ILE   A HB   1 
ATOM   2975 H HB   B ILE   A 1 137 ? 9.328  -10.587 -5.745  0.14 19.31 ?  137 ILE   A HB   1 
ATOM   2976 H HG12 A ILE   A 1 137 ? 7.824  -9.860  -3.120  0.86 23.56 ?  137 ILE   A HG12 1 
ATOM   2977 H HG12 B ILE   A 1 137 ? 7.790  -10.180 -3.409  0.14 19.61 ?  137 ILE   A HG12 1 
ATOM   2978 H HG13 A ILE   A 1 137 ? 8.255  -8.661  -4.066  0.86 23.56 ?  137 ILE   A HG13 1 
ATOM   2979 H HG13 B ILE   A 1 137 ? 8.134  -9.042  -4.461  0.14 19.61 ?  137 ILE   A HG13 1 
ATOM   2980 H HG21 A ILE   A 1 137 ? 7.943  -12.091 -4.785  0.86 22.15 ?  137 ILE   A HG21 1 
ATOM   2981 H HG21 B ILE   A 1 137 ? 8.157  -12.527 -5.241  0.14 19.48 ?  137 ILE   A HG21 1 
ATOM   2982 H HG22 A ILE   A 1 137 ? 9.464  -12.406 -5.093  0.86 22.15 ?  137 ILE   A HG22 1 
ATOM   2983 H HG22 B ILE   A 1 137 ? 9.690  -12.777 -4.964  0.14 19.48 ?  137 ILE   A HG22 1 
ATOM   2984 H HG23 A ILE   A 1 137 ? 8.975  -12.236 -3.592  0.86 22.15 ?  137 ILE   A HG23 1 
ATOM   2985 H HG23 B ILE   A 1 137 ? 8.707  -12.486 -3.752  0.14 19.48 ?  137 ILE   A HG23 1 
ATOM   2986 H HD11 A ILE   A 1 137 ? 6.012  -10.035 -4.224  0.86 25.76 ?  137 ILE   A HD11 1 
ATOM   2987 H HD11 B ILE   A 1 137 ? 5.967  -9.758  -4.769  0.14 19.91 ?  137 ILE   A HD11 1 
ATOM   2988 H HD12 A ILE   A 1 137 ? 6.505  -8.904  -5.227  0.86 25.76 ?  137 ILE   A HD12 1 
ATOM   2989 H HD12 B ILE   A 1 137 ? 6.828  -10.126 -6.053  0.14 19.91 ?  137 ILE   A HD12 1 
ATOM   2990 H HD13 A ILE   A 1 137 ? 6.847  -10.420 -5.520  0.86 25.76 ?  137 ILE   A HD13 1 
ATOM   2991 H HD13 B ILE   A 1 137 ? 6.458  -11.244 -4.985  0.14 19.91 ?  137 ILE   A HD13 1 
ATOM   2992 N N    A HIS   A 1 138 ? 12.247 -10.754 -5.330  0.86 15.83 ?  138 HIS   A N    1 
ATOM   2993 N N    B HIS   A 1 138 ? 12.326 -10.836 -5.453  0.14 15.20 ?  138 HIS   A N    1 
ATOM   2994 C CA   A HIS   A 1 138 ? 13.404 -11.529 -5.763  0.86 15.49 ?  138 HIS   A CA   1 
ATOM   2995 C CA   B HIS   A 1 138 ? 13.519 -11.569 -5.855  0.14 14.99 ?  138 HIS   A CA   1 
ATOM   2996 C C    A HIS   A 1 138 ? 14.559 -11.395 -4.779  0.86 14.56 ?  138 HIS   A C    1 
ATOM   2997 C C    B HIS   A 1 138 ? 14.643 -11.393 -4.842  0.14 14.44 ?  138 HIS   A C    1 
ATOM   2998 O O    A HIS   A 1 138 ? 15.220 -12.385 -4.443  0.86 15.33 ?  138 HIS   A O    1 
ATOM   2999 O O    B HIS   A 1 138 ? 15.358 -12.353 -4.534  0.14 14.42 ?  138 HIS   A O    1 
ATOM   3000 C CB   A HIS   A 1 138 ? 13.816 -11.091 -7.166  0.86 16.57 ?  138 HIS   A CB   1 
ATOM   3001 C CB   B HIS   A 1 138 ? 13.969 -11.134 -7.248  0.14 15.63 ?  138 HIS   A CB   1 
ATOM   3002 C CG   A HIS   A 1 138 ? 15.091 -11.715 -7.635  0.86 17.55 ?  138 HIS   A CG   1 
ATOM   3003 C CG   B HIS   A 1 138 ? 15.234 -11.792 -7.700  0.14 16.16 ?  138 HIS   A CG   1 
ATOM   3004 N ND1  A HIS   A 1 138 ? 15.213 -13.067 -7.877  0.86 18.80 ?  138 HIS   A ND1  1 
ATOM   3005 N ND1  B HIS   A 1 138 ? 15.309 -13.137 -7.995  0.14 16.58 ?  138 HIS   A ND1  1 
ATOM   3006 C CD2  A HIS   A 1 138 ? 16.306 -11.174 -7.887  0.86 18.04 ?  138 HIS   A CD2  1 
ATOM   3007 C CD2  B HIS   A 1 138 ? 16.478 -11.294 -7.896  0.14 16.40 ?  138 HIS   A CD2  1 
ATOM   3008 C CE1  A HIS   A 1 138 ? 16.448 -13.329 -8.268  0.86 19.01 ?  138 HIS   A CE1  1 
ATOM   3009 C CE1  B HIS   A 1 138 ? 16.543 -13.437 -8.359  0.14 16.70 ?  138 HIS   A CE1  1 
ATOM   3010 N NE2  A HIS   A 1 138 ? 17.131 -12.199 -8.282  0.86 18.63 ?  138 HIS   A NE2  1 
ATOM   3011 N NE2  B HIS   A 1 138 ? 17.272 -12.337 -8.307  0.14 16.60 ?  138 HIS   A NE2  1 
ATOM   3012 H H    A HIS   A 1 138 ? 12.037 -10.102 -5.860  0.86 19.00 ?  138 HIS   A H    1 
ATOM   3013 H H    B HIS   A 1 138 ? 12.128 -10.167 -5.955  0.14 18.24 ?  138 HIS   A H    1 
ATOM   3014 H HA   A HIS   A 1 138 ? 13.152 -12.462 -5.809  0.86 18.60 ?  138 HIS   A HA   1 
ATOM   3015 H HA   B HIS   A 1 138 ? 13.304 -12.513 -5.897  0.14 18.00 ?  138 HIS   A HA   1 
ATOM   3016 H HB2  A HIS   A 1 138 ? 13.113 -11.341 -7.794  0.86 19.90 ?  138 HIS   A HB2  1 
ATOM   3017 H HB2  B HIS   A 1 138 ? 13.272 -11.357 -7.887  0.14 18.77 ?  138 HIS   A HB2  1 
ATOM   3018 H HB3  A HIS   A 1 138 ? 13.933 -10.129 -7.177  0.86 19.90 ?  138 HIS   A HB3  1 
ATOM   3019 H HB3  B HIS   A 1 138 ? 14.119 -10.177 -7.244  0.14 18.77 ?  138 HIS   A HB3  1 
ATOM   3020 H HD1  A HIS   A 1 138 ? 14.583 -13.648 -7.793  0.86 22.57 ?  138 HIS   A HD1  1 
ATOM   3021 H HD2  A HIS   A 1 138 ? 16.533 -10.277 -7.810  0.86 21.66 ?  138 HIS   A HD2  1 
ATOM   3022 H HD2  B HIS   A 1 138 ? 16.743 -10.412 -7.776  0.14 19.69 ?  138 HIS   A HD2  1 
ATOM   3023 H HE1  A HIS   A 1 138 ? 16.779 -14.169 -8.492  0.86 22.83 ?  138 HIS   A HE1  1 
ATOM   3024 H HE1  B HIS   A 1 138 ? 16.847 -14.279 -8.609  0.14 20.05 ?  138 HIS   A HE1  1 
ATOM   3025 H HE2  B HIS   A 1 138 ? 18.108 -12.282 -8.499  0.14 19.93 ?  138 HIS   A HE2  1 
ATOM   3026 N N    . SER   A 1 139 ? 14.819 -10.181 -4.306  1.00 14.27 ?  139 SER   A N    1 
ATOM   3027 C CA   . SER   A 1 139 ? 15.889 -9.986  -3.339  1.00 14.17 ?  139 SER   A CA   1 
ATOM   3028 C C    . SER   A 1 139 ? 15.668 -10.832 -2.092  1.00 13.78 ?  139 SER   A C    1 
ATOM   3029 O O    . SER   A 1 139 ? 16.616 -11.422 -1.560  1.00 13.66 ?  139 SER   A O    1 
ATOM   3030 C CB   . SER   A 1 139 ? 16.016 -8.510  -2.981  1.00 13.97 ?  139 SER   A CB   1 
ATOM   3031 O OG   . SER   A 1 139 ? 17.101 -8.341  -2.087  1.00 14.58 ?  139 SER   A OG   1 
ATOM   3032 H H    A SER   A 1 139 ? 14.393 -9.468  -4.520  0.86 17.13 ?  139 SER   A H    1 
ATOM   3033 H H    B SER   A 1 139 ? 14.347 -9.486  -4.479  0.14 17.13 ?  139 SER   A H    1 
ATOM   3034 H HA   . SER   A 1 139 ? 16.730 -10.262 -3.735  1.00 17.01 ?  139 SER   A HA   1 
ATOM   3035 H HB2  . SER   A 1 139 ? 16.176 -7.992  -3.790  1.00 16.78 ?  139 SER   A HB2  1 
ATOM   3036 H HB3  . SER   A 1 139 ? 15.199 -8.207  -2.550  1.00 16.78 ?  139 SER   A HB3  1 
ATOM   3037 H HG   . SER   A 1 139 ? 17.189 -7.524  -1.889  1.00 17.50 ?  139 SER   A HG   1 
ATOM   3038 N N    . LEU   A 1 140 ? 14.430 -10.898 -1.605  1.00 13.68 ?  140 LEU   A N    1 
ATOM   3039 C CA   . LEU   A 1 140 ? 14.159 -11.709 -0.425  1.00 13.54 ?  140 LEU   A CA   1 
ATOM   3040 C C    . LEU   A 1 140 ? 14.419 -13.182 -0.709  1.00 13.65 ?  140 LEU   A C    1 
ATOM   3041 O O    . LEU   A 1 140 ? 14.978 -13.896 0.133   1.00 14.36 ?  140 LEU   A O    1 
ATOM   3042 C CB   . LEU   A 1 140 ? 12.724 -11.476 0.042   1.00 13.93 ?  140 LEU   A CB   1 
ATOM   3043 C CG   . LEU   A 1 140 ? 12.266 -12.327 1.223   1.00 14.84 ?  140 LEU   A CG   1 
ATOM   3044 C CD1  . LEU   A 1 140 ? 13.177 -12.143 2.430   1.00 15.27 ?  140 LEU   A CD1  1 
ATOM   3045 C CD2  . LEU   A 1 140 ? 10.817 -12.001 1.578   1.00 16.02 ?  140 LEU   A CD2  1 
ATOM   3046 H H    . LEU   A 1 140 ? 13.747 -10.489 -1.929  1.00 16.43 ?  140 LEU   A H    1 
ATOM   3047 H HA   . LEU   A 1 140 ? 14.752 -11.436 0.290   1.00 16.26 ?  140 LEU   A HA   1 
ATOM   3048 H HB2  . LEU   A 1 140 ? 12.631 -10.552 0.305   1.00 16.72 ?  140 LEU   A HB2  1 
ATOM   3049 H HB3  . LEU   A 1 140 ? 12.126 -11.669 -0.696  1.00 16.72 ?  140 LEU   A HB3  1 
ATOM   3050 H HG   . LEU   A 1 140 ? 12.296 -13.267 0.971   1.00 17.81 ?  140 LEU   A HG   1 
ATOM   3051 H HD11 . LEU   A 1 140 ? 12.797 -12.613 3.187   1.00 18.34 ?  140 LEU   A HD11 1 
ATOM   3052 H HD12 . LEU   A 1 140 ? 14.051 -12.513 2.220   1.00 18.34 ?  140 LEU   A HD12 1 
ATOM   3053 H HD13 . LEU   A 1 140 ? 13.251 -11.200 2.625   1.00 18.34 ?  140 LEU   A HD13 1 
ATOM   3054 H HD21 . LEU   A 1 140 ? 10.543 -12.555 2.331   1.00 19.23 ?  140 LEU   A HD21 1 
ATOM   3055 H HD22 . LEU   A 1 140 ? 10.754 -11.066 1.817   1.00 19.23 ?  140 LEU   A HD22 1 
ATOM   3056 H HD23 . LEU   A 1 140 ? 10.254 -12.191 0.812   1.00 19.23 ?  140 LEU   A HD23 1 
ATOM   3057 N N    . ARG   A 1 141 ? 14.020 -13.655 -1.893  1.00 14.08 ?  141 ARG   A N    1 
ATOM   3058 C CA   . ARG   A 1 141 ? 14.270 -15.041 -2.271  1.00 15.31 ?  141 ARG   A CA   1 
ATOM   3059 C C    . ARG   A 1 141 ? 15.765 -15.340 -2.279  1.00 14.47 ?  141 ARG   A C    1 
ATOM   3060 O O    . ARG   A 1 141 ? 16.213 -16.351 -1.724  1.00 14.71 ?  141 ARG   A O    1 
ATOM   3061 C CB   . ARG   A 1 141 ? 13.659 -15.297 -3.650  1.00 17.26 ?  141 ARG   A CB   1 
ATOM   3062 C CG   . ARG   A 1 141 ? 13.662 -16.739 -4.101  1.00 20.36 ?  141 ARG   A CG   1 
ATOM   3063 C CD   . ARG   A 1 141 ? 12.626 -17.523 -3.353  1.00 22.65 ?  141 ARG   A CD   1 
ATOM   3064 N NE   . ARG   A 1 141 ? 13.230 -18.317 -2.296  1.00 23.41 ?  141 ARG   A NE   1 
ATOM   3065 C CZ   . ARG   A 1 141 ? 12.545 -18.882 -1.310  1.00 24.21 ?  141 ARG   A CZ   1 
ATOM   3066 N NH1  . ARG   A 1 141 ? 11.254 -18.645 -1.141  1.00 24.20 ?  141 ARG   A NH1  1 
ATOM   3067 N NH2  . ARG   A 1 141 ? 13.174 -19.691 -0.464  1.00 24.91 ?  141 ARG   A NH2  1 
ATOM   3068 H H    . ARG   A 1 141 ? 13.612 -13.193 -2.495  1.00 16.90 ?  141 ARG   A H    1 
ATOM   3069 H HA   . ARG   A 1 141 ? 13.846 -15.632 -1.634  1.00 18.38 ?  141 ARG   A HA   1 
ATOM   3070 H HB2  . ARG   A 1 141 ? 12.739 -14.990 -3.643  1.00 20.72 ?  141 ARG   A HB2  1 
ATOM   3071 H HB3  . ARG   A 1 141 ? 14.161 -14.788 -4.307  1.00 20.72 ?  141 ARG   A HB3  1 
ATOM   3072 H HG2  . ARG   A 1 141 ? 13.457 -16.783 -5.050  1.00 24.44 ?  141 ARG   A HG2  1 
ATOM   3073 H HG3  . ARG   A 1 141 ? 14.533 -17.134 -3.928  1.00 24.44 ?  141 ARG   A HG3  1 
ATOM   3074 H HD2  . ARG   A 1 141 ? 11.993 -16.914 -2.940  1.00 27.19 ?  141 ARG   A HD2  1 
ATOM   3075 H HD3  . ARG   A 1 141 ? 12.162 -18.115 -3.969  1.00 27.19 ?  141 ARG   A HD3  1 
ATOM   3076 H HE   . ARG   A 1 141 ? 14.055 -18.540 -2.384  1.00 28.10 ?  141 ARG   A HE   1 
ATOM   3077 H HH11 . ARG   A 1 141 ? 10.830 -18.136 -1.689  1.00 29.04 ?  141 ARG   A HH11 1 
ATOM   3078 H HH12 . ARG   A 1 141 ? 10.829 -19.019 -0.491  1.00 29.04 ?  141 ARG   A HH12 1 
ATOM   3079 H HH21 . ARG   A 1 141 ? 14.013 -19.849 -0.562  1.00 29.90 ?  141 ARG   A HH21 1 
ATOM   3080 H HH22 . ARG   A 1 141 ? 12.743 -20.051 0.190   1.00 29.90 ?  141 ARG   A HH22 1 
ATOM   3081 N N    . VAL   A 1 142 ? 16.559 -14.467 -2.906  1.00 13.94 ?  142 VAL   A N    1 
ATOM   3082 C CA   . VAL   A 1 142 ? 18.004 -14.682 -2.934  1.00 13.95 ?  142 VAL   A CA   1 
ATOM   3083 C C    . VAL   A 1 142 ? 18.568 -14.673 -1.521  1.00 13.13 ?  142 VAL   A C    1 
ATOM   3084 O O    . VAL   A 1 142 ? 19.435 -15.483 -1.177  1.00 13.62 ?  142 VAL   A O    1 
ATOM   3085 C CB   . VAL   A 1 142 ? 18.700 -13.653 -3.842  1.00 14.14 ?  142 VAL   A CB   1 
ATOM   3086 C CG1  . VAL   A 1 142 ? 20.204 -13.869 -3.801  1.00 14.13 ?  142 VAL   A CG1  1 
ATOM   3087 C CG2  . VAL   A 1 142 ? 18.212 -13.779 -5.270  1.00 15.71 ?  142 VAL   A CG2  1 
ATOM   3088 H H    . VAL   A 1 142 ? 16.291 -13.750 -3.313  1.00 16.73 ?  142 VAL   A H    1 
ATOM   3089 H HA   . VAL   A 1 142 ? 18.175 -15.553 -3.315  1.00 16.75 ?  142 VAL   A HA   1 
ATOM   3090 H HB   . VAL   A 1 142 ? 18.514 -12.749 -3.530  1.00 16.97 ?  142 VAL   A HB   1 
ATOM   3091 H HG11 . VAL   A 1 142 ? 20.617 -13.382 -4.533  1.00 16.97 ?  142 VAL   A HG11 1 
ATOM   3092 H HG12 . VAL   A 1 142 ? 20.553 -13.540 -2.955  1.00 16.97 ?  142 VAL   A HG12 1 
ATOM   3093 H HG13 . VAL   A 1 142 ? 20.389 -14.816 -3.890  1.00 16.97 ?  142 VAL   A HG13 1 
ATOM   3094 H HG21 . VAL   A 1 142 ? 18.645 -13.098 -5.812  1.00 18.86 ?  142 VAL   A HG21 1 
ATOM   3095 H HG22 . VAL   A 1 142 ? 18.447 -14.660 -5.599  1.00 18.86 ?  142 VAL   A HG22 1 
ATOM   3096 H HG23 . VAL   A 1 142 ? 17.255 -13.659 -5.286  1.00 18.86 ?  142 VAL   A HG23 1 
ATOM   3097 N N    . CYS   A 1 143 ? 18.101 -13.749 -0.686  1.00 12.97 ?  143 CYS   A N    1 
ATOM   3098 C CA   . CYS   A 1 143 ? 18.560 -13.703 0.694   1.00 13.19 ?  143 CYS   A CA   1 
ATOM   3099 C C    . CYS   A 1 143 ? 18.337 -15.041 1.385   1.00 13.05 ?  143 CYS   A C    1 
ATOM   3100 O O    . CYS   A 1 143 ? 19.262 -15.620 1.961   1.00 13.41 ?  143 CYS   A O    1 
ATOM   3101 C CB   . CYS   A 1 143 ? 17.829 -12.589 1.436   1.00 13.57 ?  143 CYS   A CB   1 
ATOM   3102 S SG   . CYS   A 1 143 ? 18.310 -12.422 3.155   1.00 13.98 ?  143 CYS   A SG   1 
ATOM   3103 H H    . CYS   A 1 143 ? 17.521 -13.150 -0.894  1.00 15.57 ?  143 CYS   A H    1 
ATOM   3104 H HA   . CYS   A 1 143 ? 19.508 -13.511 0.706   1.00 15.83 ?  143 CYS   A HA   1 
ATOM   3105 H HB2  . CYS   A 1 143 ? 18.013 -11.745 0.992   1.00 16.29 ?  143 CYS   A HB2  1 
ATOM   3106 H HB3  . CYS   A 1 143 ? 16.880 -12.768 1.410   1.00 16.29 ?  143 CYS   A HB3  1 
ATOM   3107 H HG   . CYS   A 1 143 ? 17.778 -11.458 3.614   1.00 16.79 ?  143 CYS   A HG   1 
ATOM   3108 N N    . VAL   A 1 144 ? 17.110 -15.552 1.328   1.00 13.61 ?  144 VAL   A N    1 
ATOM   3109 C CA   . VAL   A 1 144 ? 16.780 -16.783 2.032   1.00 15.41 ?  144 VAL   A CA   1 
ATOM   3110 C C    . VAL   A 1 144 ? 17.599 -17.946 1.498   1.00 15.12 ?  144 VAL   A C    1 
ATOM   3111 O O    . VAL   A 1 144 ? 17.963 -18.860 2.247   1.00 15.65 ?  144 VAL   A O    1 
ATOM   3112 C CB   . VAL   A 1 144 ? 15.266 -17.036 1.910   1.00 18.23 ?  144 VAL   A CB   1 
ATOM   3113 C CG1  . VAL   A 1 144 ? 14.909 -18.477 2.227   1.00 19.92 ?  144 VAL   A CG1  1 
ATOM   3114 C CG2  . VAL   A 1 144 ? 14.510 -16.044 2.793   1.00 18.20 ?  144 VAL   A CG2  1 
ATOM   3115 H H    . VAL   A 1 144 ? 16.450 -15.197 0.898   1.00 16.35 ?  144 VAL   A H    1 
ATOM   3116 H HA   . VAL   A 1 144 ? 16.983 -16.672 2.972   1.00 18.50 ?  144 VAL   A HA   1 
ATOM   3117 H HB   . VAL   A 1 144 ? 14.993 -16.860 0.993   1.00 21.89 ?  144 VAL   A HB   1 
ATOM   3118 H HG11 . VAL   A 1 144 ? 13.957 -18.532 2.419   1.00 23.92 ?  144 VAL   A HG11 1 
ATOM   3119 H HG12 . VAL   A 1 144 ? 15.120 -19.031 1.461   1.00 23.92 ?  144 VAL   A HG12 1 
ATOM   3120 H HG13 . VAL   A 1 144 ? 15.416 -18.763 3.000   1.00 23.92 ?  144 VAL   A HG13 1 
ATOM   3121 H HG21 . VAL   A 1 144 ? 13.552 -16.175 2.676   1.00 21.84 ?  144 VAL   A HG21 1 
ATOM   3122 H HG22 . VAL   A 1 144 ? 14.749 -16.195 3.720   1.00 21.84 ?  144 VAL   A HG22 1 
ATOM   3123 H HG23 . VAL   A 1 144 ? 14.746 -15.137 2.534   1.00 21.84 ?  144 VAL   A HG23 1 
ATOM   3124 N N    . ASP   A 1 145 ? 17.855 -17.962 0.194   1.00 15.11 ?  145 ASP   A N    1 
ATOM   3125 C CA   . ASP   A 1 145 ? 18.564 -19.059 -0.452  1.00 16.25 ?  145 ASP   A CA   1 
ATOM   3126 C C    . ASP   A 1 145 ? 20.082 -18.917 -0.402  1.00 15.55 ?  145 ASP   A C    1 
ATOM   3127 O O    . ASP   A 1 145 ? 20.788 -19.812 -0.881  1.00 17.76 ?  145 ASP   A O    1 
ATOM   3128 C CB   . ASP   A 1 145 ? 18.120 -19.170 -1.910  1.00 17.92 ?  145 ASP   A CB   1 
ATOM   3129 C CG   . ASP   A 1 145 ? 16.681 -19.629 -2.048  1.00 20.34 ?  145 ASP   A CG   1 
ATOM   3130 O OD1  . ASP   A 1 145 ? 16.124 -20.181 -1.075  1.00 20.81 ?  145 ASP   A OD1  1 
ATOM   3131 O OD2  . ASP   A 1 145 ? 16.108 -19.428 -3.133  1.00 21.81 -1 145 ASP   A OD2  1 
ATOM   3132 H H    . ASP   A 1 145 ? 17.603 -17.339 -0.350  1.00 18.14 ?  145 ASP   A H    1 
ATOM   3133 H HA   . ASP   A 1 145 ? 18.323 -19.883 -0.008  1.00 19.51 ?  145 ASP   A HA   1 
ATOM   3134 H HB2  . ASP   A 1 145 ? 18.211 -18.303 -2.339  1.00 21.51 ?  145 ASP   A HB2  1 
ATOM   3135 H HB3  . ASP   A 1 145 ? 18.676 -19.823 -2.359  1.00 21.51 ?  145 ASP   A HB3  1 
ATOM   3136 N N    . THR   A 1 146 ? 20.605 -17.828 0.152   1.00 13.85 ?  146 THR   A N    1 
ATOM   3137 C CA   . THR   A 1 146 ? 22.043 -17.574 0.168   1.00 13.39 ?  146 THR   A CA   1 
ATOM   3138 C C    . THR   A 1 146 ? 22.605 -17.387 1.564   1.00 13.52 ?  146 THR   A C    1 
ATOM   3139 O O    . THR   A 1 146 ? 23.681 -17.920 1.870   1.00 14.30 ?  146 THR   A O    1 
ATOM   3140 C CB   . THR   A 1 146 ? 22.365 -16.323 -0.667  1.00 13.53 ?  146 THR   A CB   1 
ATOM   3141 O OG1  . THR   A 1 146 ? 21.837 -16.481 -1.984  1.00 14.17 ?  146 THR   A OG1  1 
ATOM   3142 C CG2  . THR   A 1 146 ? 23.864 -16.090 -0.762  1.00 13.80 ?  146 THR   A CG2  1 
ATOM   3143 H H    . THR   A 1 146 ? 20.139 -17.204 0.531   1.00 16.63 ?  146 THR   A H    1 
ATOM   3144 H HA   . THR   A 1 146 ? 22.498 -18.322 -0.238  1.00 16.07 ?  146 THR   A HA   1 
ATOM   3145 H HB   . THR   A 1 146 ? 21.962 -15.542 -0.254  1.00 16.24 ?  146 THR   A HB   1 
ATOM   3146 H HG1  . THR   A 1 146 ? 21.001 -16.562 -1.951  1.00 17.02 ?  146 THR   A HG1  1 
ATOM   3147 H HG21 . THR   A 1 146 ? 24.056 -15.429 -1.443  1.00 16.56 ?  146 THR   A HG21 1 
ATOM   3148 H HG22 . THR   A 1 146 ? 24.208 -15.775 0.089   1.00 16.56 ?  146 THR   A HG22 1 
ATOM   3149 H HG23 . THR   A 1 146 ? 24.313 -16.920 -0.995  1.00 16.56 ?  146 THR   A HG23 1 
ATOM   3150 N N    . VAL   A 1 147 ? 21.926 -16.619 2.405   1.00 13.32 ?  147 VAL   A N    1 
ATOM   3151 C CA   . VAL   A 1 147 ? 22.417 -16.321 3.741   1.00 13.30 ?  147 VAL   A CA   1 
ATOM   3152 C C    . VAL   A 1 147 ? 22.101 -17.491 4.660   1.00 13.10 ?  147 VAL   A C    1 
ATOM   3153 O O    . VAL   A 1 147 ? 20.958 -17.967 4.721   1.00 14.19 ?  147 VAL   A O    1 
ATOM   3154 C CB   . VAL   A 1 147 ? 21.807 -15.013 4.263   1.00 13.33 ?  147 VAL   A CB   1 
ATOM   3155 C CG1  . VAL   A 1 147 ? 22.362 -14.709 5.633   1.00 14.61 ?  147 VAL   A CG1  1 
ATOM   3156 C CG2  . VAL   A 1 147 ? 22.068 -13.876 3.289   1.00 13.94 ?  147 VAL   A CG2  1 
ATOM   3157 H H    . VAL   A 1 147 ? 21.168 -16.252 2.225   1.00 15.99 ?  147 VAL   A H    1 
ATOM   3158 H HA   . VAL   A 1 147 ? 23.382 -16.212 3.707   1.00 15.96 ?  147 VAL   A HA   1 
ATOM   3159 H HB   . VAL   A 1 147 ? 20.849 -15.125 4.348   1.00 16.01 ?  147 VAL   A HB   1 
ATOM   3160 H HG11 . VAL   A 1 147 ? 22.127 -13.802 5.875   1.00 17.55 ?  147 VAL   A HG11 1 
ATOM   3161 H HG12 . VAL   A 1 147 ? 21.975 -15.331 6.277   1.00 17.55 ?  147 VAL   A HG12 1 
ATOM   3162 H HG13 . VAL   A 1 147 ? 23.325 -14.812 5.617   1.00 17.55 ?  147 VAL   A HG13 1 
ATOM   3163 H HG21 . VAL   A 1 147 ? 21.759 -13.047 3.687   1.00 16.74 ?  147 VAL   A HG21 1 
ATOM   3164 H HG22 . VAL   A 1 147 ? 23.019 -13.825 3.112   1.00 16.74 ?  147 VAL   A HG22 1 
ATOM   3165 H HG23 . VAL   A 1 147 ? 21.585 -14.050 2.467   1.00 16.74 ?  147 VAL   A HG23 1 
ATOM   3166 N N    . ARG   A 1 148 ? 23.127 -17.957 5.369   1.00 13.71 ?  148 ARG   A N    1 
ATOM   3167 C CA   . ARG   A 1 148 ? 23.001 -19.037 6.331   1.00 13.67 ?  148 ARG   A CA   1 
ATOM   3168 C C    . ARG   A 1 148 ? 23.132 -18.564 7.766   1.00 13.80 ?  148 ARG   A C    1 
ATOM   3169 O O    . ARG   A 1 148 ? 22.735 -19.289 8.685   1.00 15.64 ?  148 ARG   A O    1 
ATOM   3170 C CB   . ARG   A 1 148 ? 24.050 -20.123 6.053   1.00 14.56 ?  148 ARG   A CB   1 
ATOM   3171 C CG   . ARG   A 1 148 ? 23.904 -20.755 4.686   1.00 16.06 ?  148 ARG   A CG   1 
ATOM   3172 C CD   . ARG   A 1 148 ? 24.988 -21.791 4.410   1.00 17.15 ?  148 ARG   A CD   1 
ATOM   3173 N NE   . ARG   A 1 148 ? 26.321 -21.203 4.437   1.00 17.04 ?  148 ARG   A NE   1 
ATOM   3174 C CZ   . ARG   A 1 148 ? 26.830 -20.467 3.459   1.00 16.21 ?  148 ARG   A CZ   1 
ATOM   3175 N NH1  . ARG   A 1 148 ? 26.156 -20.242 2.343   1.00 16.64 ?  148 ARG   A NH1  1 
ATOM   3176 N NH2  . ARG   A 1 148 ? 28.045 -19.932 3.608   1.00 16.56 ?  148 ARG   A NH2  1 
ATOM   3177 H H    . ARG   A 1 148 ? 23.935 -17.653 5.298   1.00 16.46 ?  148 ARG   A H    1 
ATOM   3178 H HA   . ARG   A 1 148 ? 22.129 -19.440 6.231   1.00 16.41 ?  148 ARG   A HA   1 
ATOM   3179 H HB2  . ARG   A 1 148 ? 24.935 -19.738 6.109   1.00 17.48 ?  148 ARG   A HB2  1 
ATOM   3180 H HB3  . ARG   A 1 148 ? 23.953 -20.830 6.714   1.00 17.48 ?  148 ARG   A HB3  1 
ATOM   3181 H HG2  . ARG   A 1 148 ? 23.039 -21.192 4.631   1.00 19.28 ?  148 ARG   A HG2  1 
ATOM   3182 H HG3  . ARG   A 1 148 ? 23.967 -20.058 4.012   1.00 19.28 ?  148 ARG   A HG3  1 
ATOM   3183 H HD2  . ARG   A 1 148 ? 24.947 -22.481 5.090   1.00 20.59 ?  148 ARG   A HD2  1 
ATOM   3184 H HD3  . ARG   A 1 148 ? 24.841 -22.178 3.533   1.00 20.59 ?  148 ARG   A HD3  1 
ATOM   3185 H HE   . ARG   A 1 148 ? 26.808 -21.343 5.130   1.00 20.46 ?  148 ARG   A HE   1 
ATOM   3186 H HH11 . ARG   A 1 148 ? 25.373 -20.569 2.237   1.00 19.97 ?  148 ARG   A HH11 1 
ATOM   3187 H HH12 . ARG   A 1 148 ? 26.506 -19.751 1.725   1.00 19.97 ?  148 ARG   A HH12 1 
ATOM   3188 H HH21 . ARG   A 1 148 ? 28.488 -20.069 4.333   1.00 19.88 ?  148 ARG   A HH21 1 
ATOM   3189 H HH22 . ARG   A 1 148 ? 28.383 -19.447 2.984   1.00 19.88 ?  148 ARG   A HH22 1 
ATOM   3190 N N    . THR   A 1 149 ? 23.679 -17.372 7.972   1.00 13.81 ?  149 THR   A N    1 
ATOM   3191 C CA   . THR   A 1 149 ? 23.753 -16.772 9.289   1.00 13.97 ?  149 THR   A CA   1 
ATOM   3192 C C    . THR   A 1 149 ? 22.427 -16.078 9.601   1.00 13.71 ?  149 THR   A C    1 
ATOM   3193 O O    . THR   A 1 149 ? 21.490 -16.075 8.794   1.00 14.33 ?  149 THR   A O    1 
ATOM   3194 C CB   . THR   A 1 149 ? 24.951 -15.833 9.347   1.00 14.52 ?  149 THR   A CB   1 
ATOM   3195 O OG1  . THR   A 1 149 ? 24.814 -14.886 8.287   1.00 14.70 ?  149 THR   A OG1  1 
ATOM   3196 C CG2  . THR   A 1 149 ? 26.259 -16.622 9.195   1.00 15.39 ?  149 THR   A CG2  1 
ATOM   3197 H H    . THR   A 1 149 ? 24.029 -16.883 7.349   1.00 16.58 ?  149 THR   A H    1 
ATOM   3198 H HA   . THR   A 1 149 ? 23.886 -17.478 9.944   1.00 16.77 ?  149 THR   A HA   1 
ATOM   3199 H HB   . THR   A 1 149 ? 24.962 -15.381 10.202  1.00 17.43 ?  149 THR   A HB   1 
ATOM   3200 H HG1  . THR   A 1 149 ? 25.466 -14.351 8.297   1.00 17.65 ?  149 THR   A HG1  1 
ATOM   3201 H HG21 . THR   A 1 149 ? 27.018 -16.024 9.263   1.00 18.48 ?  149 THR   A HG21 1 
ATOM   3202 H HG22 . THR   A 1 149 ? 26.328 -17.299 9.888   1.00 18.48 ?  149 THR   A HG22 1 
ATOM   3203 H HG23 . THR   A 1 149 ? 26.285 -17.064 8.328   1.00 18.48 ?  149 THR   A HG23 1 
ATOM   3204 N N    . ASN   A 1 150 ? 22.313 -15.533 10.803  1.00 13.77 ?  150 ASN   A N    1 
ATOM   3205 C CA   . ASN   A 1 150 ? 21.031 -15.030 11.296  1.00 14.39 ?  150 ASN   A CA   1 
ATOM   3206 C C    . ASN   A 1 150 ? 20.842 -13.590 10.839  1.00 13.95 ?  150 ASN   A C    1 
ATOM   3207 O O    . ASN   A 1 150 ? 21.593 -12.697 11.251  1.00 15.51 ?  150 ASN   A O    1 
ATOM   3208 C CB   . ASN   A 1 150 ? 20.988 -15.141 12.813  1.00 17.04 ?  150 ASN   A CB   1 
ATOM   3209 C CG   . ASN   A 1 150 ? 20.864 -16.571 13.276  1.00 21.17 ?  150 ASN   A CG   1 
ATOM   3210 O OD1  . ASN   A 1 150 ? 20.233 -17.387 12.607  1.00 22.65 ?  150 ASN   A OD1  1 
ATOM   3211 N ND2  . ASN   A 1 150 ? 21.481 -16.893 14.411  1.00 23.57 ?  150 ASN   A ND2  1 
ATOM   3212 H H    . ASN   A 1 150 ? 22.969 -15.442 11.355  1.00 16.53 ?  150 ASN   A H    1 
ATOM   3213 H HA   . ASN   A 1 150 ? 20.315 -15.574 10.928  1.00 17.28 ?  150 ASN   A HA   1 
ATOM   3214 H HB2  . ASN   A 1 150 ? 21.806 -14.779 13.184  1.00 20.46 ?  150 ASN   A HB2  1 
ATOM   3215 H HB3  . ASN   A 1 150 ? 20.221 -14.657 13.147  1.00 20.46 ?  150 ASN   A HB3  1 
ATOM   3216 H HD21 . ASN   A 1 150 ? 21.443 -17.701 14.719  1.00 28.30 ?  150 ASN   A HD21 1 
ATOM   3217 H HD22 . ASN   A 1 150 ? 21.916 -16.295 14.851  1.00 28.30 ?  150 ASN   A HD22 1 
ATOM   3218 N N    . VAL   A 1 151 ? 19.857 -13.358 9.979   1.00 13.58 ?  151 VAL   A N    1 
ATOM   3219 C CA   . VAL   A 1 151 ? 19.640 -12.046 9.392   1.00 13.75 ?  151 VAL   A CA   1 
ATOM   3220 C C    . VAL   A 1 151 ? 18.258 -11.533 9.769   1.00 13.61 ?  151 VAL   A C    1 
ATOM   3221 O O    . VAL   A 1 151 ? 17.250 -12.245 9.636   1.00 14.82 ?  151 VAL   A O    1 
ATOM   3222 C CB   . VAL   A 1 151 ? 19.918 -12.033 7.875   1.00 15.12 ?  151 VAL   A CB   1 
ATOM   3223 C CG1  . VAL   A 1 151 ? 19.086 -13.050 7.134   1.00 16.29 ?  151 VAL   A CG1  1 
ATOM   3224 C CG2  . VAL   A 1 151 ? 19.728 -10.629 7.308   1.00 15.70 ?  151 VAL   A CG2  1 
ATOM   3225 H H    . VAL   A 1 151 ? 19.298 -13.963 9.717   1.00 16.31 ?  151 VAL   A H    1 
ATOM   3226 H HA   . VAL   A 1 151 ? 20.284 -11.442 9.788   1.00 16.51 ?  151 VAL   A HA   1 
ATOM   3227 H HB   . VAL   A 1 151 ? 20.849 -12.273 7.733   1.00 18.15 ?  151 VAL   A HB   1 
ATOM   3228 H HG11 . VAL   A 1 151 ? 19.271 -12.986 6.183   1.00 19.55 ?  151 VAL   A HG11 1 
ATOM   3229 H HG12 . VAL   A 1 151 ? 19.317 -13.942 7.450   1.00 19.55 ?  151 VAL   A HG12 1 
ATOM   3230 H HG13 . VAL   A 1 151 ? 18.146 -12.879 7.299   1.00 19.55 ?  151 VAL   A HG13 1 
ATOM   3231 H HG21 . VAL   A 1 151 ? 20.041 -10.614 6.388   1.00 18.85 ?  151 VAL   A HG21 1 
ATOM   3232 H HG22 . VAL   A 1 151 ? 18.789 -10.395 7.341   1.00 18.85 ?  151 VAL   A HG22 1 
ATOM   3233 H HG23 . VAL   A 1 151 ? 20.246 -10.001 7.839   1.00 18.85 ?  151 VAL   A HG23 1 
ATOM   3234 N N    . TYR   A 1 152 ? 18.244 -10.294 10.260  1.00 13.47 ?  152 TYR   A N    1 
ATOM   3235 C CA   . TYR   A 1 152 ? 17.051 -9.562  10.652  1.00 12.87 ?  152 TYR   A CA   1 
ATOM   3236 C C    . TYR   A 1 152 ? 16.859 -8.459  9.627   1.00 12.56 ?  152 TYR   A C    1 
ATOM   3237 O O    . TYR   A 1 152 ? 17.638 -7.501  9.583   1.00 13.21 ?  152 TYR   A O    1 
ATOM   3238 C CB   . TYR   A 1 152 ? 17.238 -9.027  12.068  1.00 13.50 ?  152 TYR   A CB   1 
ATOM   3239 C CG   . TYR   A 1 152 ? 17.210 -10.154 13.060  1.00 14.03 ?  152 TYR   A CG   1 
ATOM   3240 C CD1  . TYR   A 1 152 ? 18.349 -10.894 13.336  1.00 15.82 ?  152 TYR   A CD1  1 
ATOM   3241 C CD2  . TYR   A 1 152 ? 16.031 -10.519 13.683  1.00 14.42 ?  152 TYR   A CD2  1 
ATOM   3242 C CE1  . TYR   A 1 152 ? 18.321 -11.954 14.213  1.00 17.02 ?  152 TYR   A CE1  1 
ATOM   3243 C CE2  . TYR   A 1 152 ? 15.990 -11.585 14.567  1.00 15.58 ?  152 TYR   A CE2  1 
ATOM   3244 C CZ   . TYR   A 1 152 ? 17.138 -12.298 14.827  1.00 16.84 ?  152 TYR   A CZ   1 
ATOM   3245 O OH   . TYR   A 1 152 ? 17.105 -13.367 15.704  1.00 19.53 ?  152 TYR   A OH   1 
ATOM   3246 H H    . TYR   A 1 152 ? 18.965 -9.827  10.359  1.00 16.17 ?  152 TYR   A H    1 
ATOM   3247 H HA   . TYR   A 1 152 ? 16.283 -10.155 10.629  1.00 15.46 ?  152 TYR   A HA   1 
ATOM   3248 H HB2  . TYR   A 1 152 ? 18.096 -8.588  12.130  1.00 16.21 ?  152 TYR   A HB2  1 
ATOM   3249 H HB3  . TYR   A 1 152 ? 16.525 -8.408  12.275  1.00 16.21 ?  152 TYR   A HB3  1 
ATOM   3250 H HD1  . TYR   A 1 152 ? 19.147 -10.668 12.914  1.00 18.99 ?  152 TYR   A HD1  1 
ATOM   3251 H HD2  . TYR   A 1 152 ? 15.247 -10.046 13.502  1.00 17.31 ?  152 TYR   A HD2  1 
ATOM   3252 H HE1  . TYR   A 1 152 ? 19.096 -12.433 14.395  1.00 20.43 ?  152 TYR   A HE1  1 
ATOM   3253 H HE2  . TYR   A 1 152 ? 15.189 -11.813 14.988  1.00 18.70 ?  152 TYR   A HE2  1 
ATOM   3254 H HH   . TYR   A 1 152 ? 16.328 -13.450 16.022  1.00 23.44 ?  152 TYR   A HH   1 
ATOM   3255 N N    A LEU   A 1 153 ? 15.850 -8.621  8.782   0.86 12.56 ?  153 LEU   A N    1 
ATOM   3256 N N    B LEU   A 1 153 ? 15.837 -8.607  8.788   0.14 12.70 ?  153 LEU   A N    1 
ATOM   3257 C CA   A LEU   A 1 153 ? 15.589 -7.711  7.679   0.86 13.16 ?  153 LEU   A CA   1 
ATOM   3258 C CA   B LEU   A 1 153 ? 15.575 -7.667  7.705   0.14 13.02 ?  153 LEU   A CA   1 
ATOM   3259 C C    A LEU   A 1 153 ? 14.592 -6.644  8.095   0.86 13.56 ?  153 LEU   A C    1 
ATOM   3260 C C    B LEU   A 1 153 ? 14.567 -6.625  8.173   0.14 13.30 ?  153 LEU   A C    1 
ATOM   3261 O O    A LEU   A 1 153 ? 13.512 -6.959  8.612   0.86 14.75 ?  153 LEU   A O    1 
ATOM   3262 O O    B LEU   A 1 153 ? 13.434 -6.966  8.530   0.14 13.55 ?  153 LEU   A O    1 
ATOM   3263 C CB   A LEU   A 1 153 ? 15.017 -8.482  6.491   0.86 13.27 ?  153 LEU   A CB   1 
ATOM   3264 C CB   B LEU   A 1 153 ? 15.034 -8.407  6.482   0.14 13.16 ?  153 LEU   A CB   1 
ATOM   3265 C CG   A LEU   A 1 153 ? 15.947 -9.494  5.829   0.86 13.35 ?  153 LEU   A CG   1 
ATOM   3266 C CG   B LEU   A 1 153 ? 15.963 -9.443  5.846   0.14 13.30 ?  153 LEU   A CG   1 
ATOM   3267 C CD1  A LEU   A 1 153 ? 15.142 -10.372 4.890   0.86 14.27 ?  153 LEU   A CD1  1 
ATOM   3268 C CD1  B LEU   A 1 153 ? 15.260 -10.156 4.701   0.14 13.60 ?  153 LEU   A CD1  1 
ATOM   3269 C CD2  A LEU   A 1 153 ? 17.049 -8.764  5.084   0.86 13.90 ?  153 LEU   A CD2  1 
ATOM   3270 C CD2  B LEU   A 1 153 ? 17.247 -8.788  5.363   0.14 13.40 ?  153 LEU   A CD2  1 
ATOM   3271 H H    A LEU   A 1 153 ? 15.281 -9.270  8.832   0.86 15.08 ?  153 LEU   A H    1 
ATOM   3272 H H    B LEU   A 1 153 ? 15.270 -9.255  8.826   0.14 15.25 ?  153 LEU   A H    1 
ATOM   3273 H HA   A LEU   A 1 153 ? 16.416 -7.285  7.413   0.86 15.80 ?  153 LEU   A HA   1 
ATOM   3274 H HA   B LEU   A 1 153 ? 16.396 -7.219  7.458   0.14 15.64 ?  153 LEU   A HA   1 
ATOM   3275 H HB2  A LEU   A 1 153 ? 14.229 -8.957  6.792   0.86 15.93 ?  153 LEU   A HB2  1 
ATOM   3276 H HB2  B LEU   A 1 153 ? 14.222 -8.870  6.740   0.14 15.80 ?  153 LEU   A HB2  1 
ATOM   3277 H HB3  A LEU   A 1 153 ? 14.761 -7.833  5.812   0.86 15.93 ?  153 LEU   A HB3  1 
ATOM   3278 H HB3  B LEU   A 1 153 ? 14.825 -7.751  5.798   0.14 15.80 ?  153 LEU   A HB3  1 
ATOM   3279 H HG   A LEU   A 1 153 ? 16.355 -10.050 6.517   0.86 16.02 ?  153 LEU   A HG   1 
ATOM   3280 H HG   B LEU   A 1 153 ? 16.198 -10.107 6.513   0.14 15.97 ?  153 LEU   A HG   1 
ATOM   3281 H HD11 A LEU   A 1 153 ? 15.734 -11.031 4.500   0.86 17.13 ?  153 LEU   A HD11 1 
ATOM   3282 H HD11 B LEU   A 1 153 ? 15.785 -10.927 4.438   0.14 16.32 ?  153 LEU   A HD11 1 
ATOM   3283 H HD12 A LEU   A 1 153 ? 14.440 -10.805 5.393   0.86 17.13 ?  153 LEU   A HD12 1 
ATOM   3284 H HD12 B LEU   A 1 153 ? 14.383 -10.441 5.000   0.14 16.32 ?  153 LEU   A HD12 1 
ATOM   3285 H HD13 A LEU   A 1 153 ? 14.762 -9.812  4.195   0.86 17.13 ?  153 LEU   A HD13 1 
ATOM   3286 H HD13 B LEU   A 1 153 ? 15.171 -9.543  3.955   0.14 16.32 ?  153 LEU   A HD13 1 
ATOM   3287 H HD21 A LEU   A 1 153 ? 17.606 -9.416  4.636   0.86 16.69 ?  153 LEU   A HD21 1 
ATOM   3288 H HD21 B LEU   A 1 153 ? 17.763 -9.439  4.862   0.14 16.09 ?  153 LEU   A HD21 1 
ATOM   3289 H HD22 A LEU   A 1 153 ? 16.645 -8.168  4.437   0.86 16.69 ?  153 LEU   A HD22 1 
ATOM   3290 H HD22 B LEU   A 1 153 ? 17.022 -8.035  4.794   0.14 16.09 ?  153 LEU   A HD22 1 
ATOM   3291 H HD23 A LEU   A 1 153 ? 17.580 -8.254  5.718   0.86 16.69 ?  153 LEU   A HD23 1 
ATOM   3292 H HD23 B LEU   A 1 153 ? 17.755 -8.483  6.131   0.14 16.09 ?  153 LEU   A HD23 1 
ATOM   3293 N N    A ALA   A 1 154 ? 14.955 -5.390  7.850   0.86 13.61 ?  154 ALA   A N    1 
ATOM   3294 N N    B ALA   A 1 154 ? 14.980 -5.359  8.168   0.14 13.42 ?  154 ALA   A N    1 
ATOM   3295 C CA   A ALA   A 1 154 ? 14.095 -4.242  8.089   0.86 14.64 ?  154 ALA   A CA   1 
ATOM   3296 C CA   B ALA   A 1 154 ? 14.111 -4.243  8.525   0.14 13.92 ?  154 ALA   A CA   1 
ATOM   3297 C C    A ALA   A 1 154 ? 13.607 -3.724  6.746   0.86 14.64 ?  154 ALA   A C    1 
ATOM   3298 C C    B ALA   A 1 154 ? 13.627 -3.589  7.236   0.14 14.15 ?  154 ALA   A C    1 
ATOM   3299 O O    A ALA   A 1 154 ? 14.416 -3.381  5.877   0.86 14.86 ?  154 ALA   A O    1 
ATOM   3300 O O    B ALA   A 1 154 ? 14.407 -2.943  6.528   0.14 13.89 ?  154 ALA   A O    1 
ATOM   3301 C CB   A ALA   A 1 154 ? 14.861 -3.140  8.819   0.86 15.24 ?  154 ALA   A CB   1 
ATOM   3302 C CB   B ALA   A 1 154 ? 14.857 -3.238  9.401   0.14 13.83 ?  154 ALA   A CB   1 
ATOM   3303 H H    A ALA   A 1 154 ? 15.727 -5.174  7.531   0.86 16.35 ?  154 ALA   A H    1 
ATOM   3304 H H    B ALA   A 1 154 ? 15.779 -5.116  7.958   0.14 16.11 ?  154 ALA   A H    1 
ATOM   3305 H HA   A ALA   A 1 154 ? 13.333 -4.501  8.631   0.86 17.57 ?  154 ALA   A HA   1 
ATOM   3306 H HA   B ALA   A 1 154 ? 13.342 -4.567  9.016   0.14 16.72 ?  154 ALA   A HA   1 
ATOM   3307 H HB1  A ALA   A 1 154 ? 14.269 -2.383  8.965   0.86 18.30 ?  154 ALA   A HB1  1 
ATOM   3308 H HB1  B ALA   A 1 154 ? 14.260 -2.506  9.624   0.14 16.61 ?  154 ALA   A HB1  1 
ATOM   3309 H HB2  A ALA   A 1 154 ? 15.181 -3.477  9.670   0.86 18.30 ?  154 ALA   A HB2  1 
ATOM   3310 H HB2  B ALA   A 1 154 ? 15.151 -3.683  10.212  0.14 16.61 ?  154 ALA   A HB2  1 
ATOM   3311 H HB3  A ALA   A 1 154 ? 15.616 -2.861  8.271   0.86 18.30 ?  154 ALA   A HB3  1 
ATOM   3312 H HB3  B ALA   A 1 154 ? 15.625 -2.901  8.913   0.14 16.61 ?  154 ALA   A HB3  1 
ATOM   3313 N N    A VAL   A 1 155 ? 12.291 -3.655  6.593   0.86 15.22 ?  155 VAL   A N    1 
ATOM   3314 N N    B VAL   A 1 155 ? 12.343 -3.758  6.932   0.14 14.77 ?  155 VAL   A N    1 
ATOM   3315 C CA   A VAL   A 1 155 ? 11.643 -3.175  5.381   0.86 16.28 ?  155 VAL   A CA   1 
ATOM   3316 C CA   B VAL   A 1 155 ? 11.739 -3.206  5.725   0.14 15.43 ?  155 VAL   A CA   1 
ATOM   3317 C C    A VAL   A 1 155 ? 10.892 -1.905  5.749   0.86 17.41 ?  155 VAL   A C    1 
ATOM   3318 C C    B VAL   A 1 155 ? 10.966 -1.952  6.109   0.14 16.39 ?  155 VAL   A C    1 
ATOM   3319 O O    A VAL   A 1 155 ? 9.936  -1.952  6.532   0.86 17.82 ?  155 VAL   A O    1 
ATOM   3320 O O    B VAL   A 1 155 ? 10.080 -1.996  6.971   0.14 16.32 ?  155 VAL   A O    1 
ATOM   3321 C CB   A VAL   A 1 155 ? 10.704 -4.231  4.785   0.86 16.74 ?  155 VAL   A CB   1 
ATOM   3322 C CB   B VAL   A 1 155 ? 10.830 -4.232  5.030   0.14 15.45 ?  155 VAL   A CB   1 
ATOM   3323 C CG1  A VAL   A 1 155 ? 9.989  -3.667  3.568   0.86 17.81 ?  155 VAL   A CG1  1 
ATOM   3324 C CG1  B VAL   A 1 155 ? 10.170 -3.609  3.808   0.14 15.54 ?  155 VAL   A CG1  1 
ATOM   3325 C CG2  A VAL   A 1 155 ? 11.497 -5.482  4.422   0.86 17.28 ?  155 VAL   A CG2  1 
ATOM   3326 C CG2  B VAL   A 1 155 ? 11.634 -5.463  4.634   0.14 15.56 ?  155 VAL   A CG2  1 
ATOM   3327 H H    A VAL   A 1 155 ? 11.734 -3.890  7.207   0.86 18.28 ?  155 VAL   A H    1 
ATOM   3328 H H    B VAL   A 1 155 ? 11.790 -4.196  7.423   0.14 17.73 ?  155 VAL   A H    1 
ATOM   3329 H HA   A VAL   A 1 155 ? 12.318 -2.947  4.725   0.86 19.54 ?  155 VAL   A HA   1 
ATOM   3330 H HA   B VAL   A 1 155 ? 12.440 -2.959  5.107   0.14 18.53 ?  155 VAL   A HA   1 
ATOM   3331 H HB   A VAL   A 1 155 ? 10.037 -4.471  5.451   0.86 20.10 ?  155 VAL   A HB   1 
ATOM   3332 H HB   B VAL   A 1 155 ? 10.132 -4.510  5.644   0.14 18.55 ?  155 VAL   A HB   1 
ATOM   3333 H HG11 A VAL   A 1 155 ? 9.555  -4.394  3.096   0.86 21.38 ?  155 VAL   A HG11 1 
ATOM   3334 H HG11 B VAL   A 1 155 ? 9.774  -4.314  3.272   0.14 18.65 ?  155 VAL   A HG11 1 
ATOM   3335 H HG12 A VAL   A 1 155 ? 9.321  -3.021  3.858   0.86 21.38 ?  155 VAL   A HG12 1 
ATOM   3336 H HG12 B VAL   A 1 155 ? 9.482  -2.989  4.098   0.14 18.65 ?  155 VAL   A HG12 1 
ATOM   3337 H HG13 A VAL   A 1 155 ? 10.636 -3.236  2.991   0.86 21.38 ?  155 VAL   A HG13 1 
ATOM   3338 H HG13 B VAL   A 1 155 ? 10.843 -3.141  3.290   0.14 18.65 ?  155 VAL   A HG13 1 
ATOM   3339 H HG21 A VAL   A 1 155 ? 10.901 -6.120  4.008   0.86 20.74 ?  155 VAL   A HG21 1 
ATOM   3340 H HG21 B VAL   A 1 155 ? 11.057 -6.074  4.149   0.14 18.69 ?  155 VAL   A HG21 1 
ATOM   3341 H HG22 A VAL   A 1 155 ? 12.204 -5.235  3.805   0.86 20.74 ?  155 VAL   A HG22 1 
ATOM   3342 H HG22 B VAL   A 1 155 ? 12.374 -5.188  4.070   0.14 18.69 ?  155 VAL   A HG22 1 
ATOM   3343 H HG23 A VAL   A 1 155 ? 11.881 -5.858  5.230   0.86 20.74 ?  155 VAL   A HG23 1 
ATOM   3344 H HG23 B VAL   A 1 155 ? 11.971 -5.892  5.436   0.14 18.69 ?  155 VAL   A HG23 1 
ATOM   3345 N N    A PHE   A 1 156 ? 11.320 -0.773  5.179   0.86 18.98 ?  156 PHE   A N    1 
ATOM   3346 N N    B PHE   A 1 156 ? 11.300 -0.831  5.467   0.14 17.41 ?  156 PHE   A N    1 
ATOM   3347 C CA   A PHE   A 1 156 ? 10.768 0.529   5.557   0.86 20.51 ?  156 PHE   A CA   1 
ATOM   3348 C CA   B PHE   A 1 156 ? 10.685 0.445   5.817   0.14 18.42 ?  156 PHE   A CA   1 
ATOM   3349 C C    A PHE   A 1 156 ? 9.299  0.666   5.173   0.86 21.00 ?  156 PHE   A C    1 
ATOM   3350 C C    B PHE   A 1 156 ? 9.285  0.587   5.227   0.14 18.79 ?  156 PHE   A C    1 
ATOM   3351 O O    A PHE   A 1 156 ? 8.496  1.209   5.942   0.86 22.08 ?  156 PHE   A O    1 
ATOM   3352 O O    B PHE   A 1 156 ? 8.336  0.925   5.943   0.14 19.13 ?  156 PHE   A O    1 
ATOM   3353 C CB   A PHE   A 1 156 ? 11.597 1.625   4.882   0.86 21.63 ?  156 PHE   A CB   1 
ATOM   3354 C CB   B PHE   A 1 156 ? 11.583 1.600   5.368   0.14 19.14 ?  156 PHE   A CB   1 
ATOM   3355 C CG   A PHE   A 1 156 ? 11.137 3.021   5.197   0.86 23.56 ?  156 PHE   A CG   1 
ATOM   3356 C CG   B PHE   A 1 156 ? 11.066 2.951   5.765   0.14 19.99 ?  156 PHE   A CG   1 
ATOM   3357 C CD1  A PHE   A 1 156 ? 11.079 3.456   6.510   0.86 24.75 ?  156 PHE   A CD1  1 
ATOM   3358 C CD1  B PHE   A 1 156 ? 11.270 3.433   7.047   0.14 20.32 ?  156 PHE   A CD1  1 
ATOM   3359 C CD2  A PHE   A 1 156 ? 10.791 3.904   4.184   0.86 24.27 ?  156 PHE   A CD2  1 
ATOM   3360 C CD2  B PHE   A 1 156 ? 10.377 3.737   4.859   0.14 20.35 ?  156 PHE   A CD2  1 
ATOM   3361 C CE1  A PHE   A 1 156 ? 10.668 4.739   6.811   0.86 25.89 ?  156 PHE   A CE1  1 
ATOM   3362 C CE1  B PHE   A 1 156 ? 10.795 4.676   7.417   0.14 20.60 ?  156 PHE   A CE1  1 
ATOM   3363 C CE2  A PHE   A 1 156 ? 10.378 5.193   4.479   0.86 25.40 ?  156 PHE   A CE2  1 
ATOM   3364 C CE2  B PHE   A 1 156 ? 9.896  4.978   5.223   0.14 20.63 ?  156 PHE   A CE2  1 
ATOM   3365 C CZ   A PHE   A 1 156 ? 10.324 5.612   5.795   0.86 25.99 ?  156 PHE   A CZ   1 
ATOM   3366 C CZ   B PHE   A 1 156 ? 10.108 5.449   6.504   0.14 20.68 ?  156 PHE   A CZ   1 
ATOM   3367 H H    A PHE   A 1 156 ? 11.937 -0.732  4.576   0.86 22.78 ?  156 PHE   A H    1 
ATOM   3368 H H    B PHE   A 1 156 ? 11.883 -0.785  4.839   0.14 20.90 ?  156 PHE   A H    1 
ATOM   3369 H HA   A PHE   A 1 156 ? 10.852 0.649   6.514   0.86 24.61 ?  156 PHE   A HA   1 
ATOM   3370 H HA   B PHE   A 1 156 ? 10.604 0.491   6.776   0.14 22.12 ?  156 PHE   A HA   1 
ATOM   3371 H HB2  A PHE   A 1 156 ? 12.523 1.550   5.169   0.86 25.97 ?  156 PHE   A HB2  1 
ATOM   3372 H HB2  B PHE   A 1 156 ? 12.460 1.492   5.768   0.14 22.98 ?  156 PHE   A HB2  1 
ATOM   3373 H HB3  A PHE   A 1 156 ? 11.548 1.513   3.918   0.86 25.97 ?  156 PHE   A HB3  1 
ATOM   3374 H HB3  B PHE   A 1 156 ? 11.662 1.585   4.401   0.14 22.98 ?  156 PHE   A HB3  1 
ATOM   3375 H HD1  A PHE   A 1 156 ? 11.320 2.873   7.195   0.86 29.71 ?  156 PHE   A HD1  1 
ATOM   3376 H HD1  B PHE   A 1 156 ? 11.733 2.914   7.665   0.14 24.39 ?  156 PHE   A HD1  1 
ATOM   3377 H HD2  A PHE   A 1 156 ? 10.830 3.625   3.297   0.86 29.13 ?  156 PHE   A HD2  1 
ATOM   3378 H HD2  B PHE   A 1 156 ? 10.236 3.424   3.994   0.14 24.43 ?  156 PHE   A HD2  1 
ATOM   3379 H HE1  A PHE   A 1 156 ? 10.633 5.019   7.697   0.86 31.08 ?  156 PHE   A HE1  1 
ATOM   3380 H HE1  B PHE   A 1 156 ? 10.938 4.990   8.280   0.14 24.73 ?  156 PHE   A HE1  1 
ATOM   3381 H HE2  A PHE   A 1 156 ? 10.141 5.775   3.793   0.86 30.49 ?  156 PHE   A HE2  1 
ATOM   3382 H HE2  B PHE   A 1 156 ? 9.437  5.500   4.604   0.14 24.76 ?  156 PHE   A HE2  1 
ATOM   3383 H HZ   A PHE   A 1 156 ? 10.041 6.475   5.997   0.86 31.20 ?  156 PHE   A HZ   1 
ATOM   3384 H HZ   B PHE   A 1 156 ? 9.788  6.286   6.751   0.14 24.82 ?  156 PHE   A HZ   1 
ATOM   3385 N N    A ASP   A 1 157 ? 8.944  0.222   3.976   0.86 20.42 ?  157 ASP   A N    1 
ATOM   3386 N N    B ASP   A 1 157 ? 9.138  0.344   3.928   0.14 18.61 ?  157 ASP   A N    1 
ATOM   3387 C CA   A ASP   A 1 157 ? 7.628  0.472   3.404   0.86 21.76 ?  157 ASP   A CA   1 
ATOM   3388 C CA   B ASP   A 1 157 ? 7.858  0.557   3.263   0.14 18.61 ?  157 ASP   A CA   1 
ATOM   3389 C C    A ASP   A 1 157 ? 6.651  -0.587  3.904   0.86 21.71 ?  157 ASP   A C    1 
ATOM   3390 C C    B ASP   A 1 157 ? 6.839  -0.464  3.758   0.14 19.52 ?  157 ASP   A C    1 
ATOM   3391 O O    A ASP   A 1 157 ? 6.840  -1.783  3.642   0.86 21.04 ?  157 ASP   A O    1 
ATOM   3392 O O    B ASP   A 1 157 ? 7.021  -1.673  3.581   0.14 19.49 ?  157 ASP   A O    1 
ATOM   3393 C CB   A ASP   A 1 157 ? 7.736  0.418   1.884   0.86 23.89 ?  157 ASP   A CB   1 
ATOM   3394 C CB   B ASP   A 1 157 ? 8.039  0.458   1.750   0.14 17.74 ?  157 ASP   A CB   1 
ATOM   3395 C CG   A ASP   A 1 157 ? 6.502  0.943   1.199   0.86 26.18 ?  157 ASP   A CG   1 
ATOM   3396 C CG   B ASP   A 1 157 ? 6.820  0.927   0.989   0.14 16.72 ?  157 ASP   A CG   1 
ATOM   3397 O OD1  A ASP   A 1 157 ? 6.314  2.175   1.174   0.86 28.37 ?  157 ASP   A OD1  1 
ATOM   3398 O OD1  B ASP   A 1 157 ? 5.717  0.396   1.241   0.14 16.66 ?  157 ASP   A OD1  1 
ATOM   3399 O OD2  A ASP   A 1 157 ? 5.706  0.121   0.697   0.86 26.38 -1 157 ASP   A OD2  1 
ATOM   3400 O OD2  B ASP   A 1 157 ? 6.959  1.838   0.146   0.14 15.80 -1 157 ASP   A OD2  1 
ATOM   3401 H H    A ASP   A 1 157 ? 9.469  -0.227  3.460   0.86 24.51 ?  157 ASP   A H    1 
ATOM   3402 H H    B ASP   A 1 157 ? 9.759  0.056   3.409   0.14 22.34 ?  157 ASP   A H    1 
ATOM   3403 H HA   A ASP   A 1 157 ? 7.313  1.350   3.671   0.86 26.12 ?  157 ASP   A HA   1 
ATOM   3404 H HA   B ASP   A 1 157 ? 7.527  1.445   3.469   0.14 22.34 ?  157 ASP   A HA   1 
ATOM   3405 H HB2  A ASP   A 1 157 ? 8.511  0.936   1.605   0.86 28.67 ?  157 ASP   A HB2  1 
ATOM   3406 H HB2  B ASP   A 1 157 ? 8.785  1.014   1.483   0.14 21.30 ?  157 ASP   A HB2  1 
ATOM   3407 H HB3  A ASP   A 1 157 ? 7.846  -0.504  1.610   0.86 28.67 ?  157 ASP   A HB3  1 
ATOM   3408 H HB3  B ASP   A 1 157 ? 8.216  -0.461  1.504   0.14 21.30 ?  157 ASP   A HB3  1 
ATOM   3409 N N    A LYS   A 1 158 ? 5.611  -0.149  4.624   0.86 23.22 ?  158 LYS   A N    1 
ATOM   3410 N N    B LYS   A 1 158 ? 5.764  0.029   4.377   0.14 20.46 ?  158 LYS   A N    1 
ATOM   3411 C CA   A LYS   A 1 158 ? 4.645  -1.093  5.179   0.86 24.38 ?  158 LYS   A CA   1 
ATOM   3412 C CA   B LYS   A 1 158 ? 4.754  -0.862  4.942   0.14 21.44 ?  158 LYS   A CA   1 
ATOM   3413 C C    A LYS   A 1 158 ? 3.932  -1.854  4.070   0.86 23.63 ?  158 LYS   A C    1 
ATOM   3414 C C    B LYS   A 1 158 ? 4.071  -1.681  3.853   0.14 21.86 ?  158 LYS   A C    1 
ATOM   3415 O O    A LYS   A 1 158 ? 3.751  -3.076  4.155   0.86 23.92 ?  158 LYS   A O    1 
ATOM   3416 O O    B LYS   A 1 158 ? 3.869  -2.890  4.010   0.14 22.00 ?  158 LYS   A O    1 
ATOM   3417 C CB   A LYS   A 1 158 ? 3.644  -0.349  6.068   0.86 26.08 ?  158 LYS   A CB   1 
ATOM   3418 C CB   B LYS   A 1 158 ? 3.743  -0.047  5.758   0.14 22.01 ?  158 LYS   A CB   1 
ATOM   3419 C CG   A LYS   A 1 158 ? 2.436  -1.175  6.511   0.86 27.92 ?  158 LYS   A CG   1 
ATOM   3420 C CG   B LYS   A 1 158 ? 2.263  -0.352  5.511   0.14 22.52 ?  158 LYS   A CG   1 
ATOM   3421 C CD   A LYS   A 1 158 ? 2.834  -2.421  7.298   0.86 29.42 ?  158 LYS   A CD   1 
ATOM   3422 C CD   B LYS   A 1 158 ? 1.805  -1.622  6.212   0.14 22.99 ?  158 LYS   A CD   1 
ATOM   3423 C CE   A LYS   A 1 158 ? 1.603  -3.130  7.858   0.86 30.44 ?  158 LYS   A CE   1 
ATOM   3424 C CE   B LYS   A 1 158 ? 0.308  -1.833  6.041   0.14 23.35 ?  158 LYS   A CE   1 
ATOM   3425 N NZ   A LYS   A 1 158 ? 1.908  -4.490  8.391   0.86 30.97 ?  158 LYS   A NZ   1 
ATOM   3426 N NZ   B LYS   A 1 158 ? -0.488 -1.065  7.037   0.14 23.49 ?  158 LYS   A NZ   1 
ATOM   3427 H H    A LYS   A 1 158 ? 5.458  0.675   4.807   0.86 27.87 ?  158 LYS   A H    1 
ATOM   3428 H H    B LYS   A 1 158 ? 5.600  0.865   4.476   0.14 24.56 ?  158 LYS   A H    1 
ATOM   3429 H HA   A LYS   A 1 158 ? 5.114  -1.736  5.741   0.86 29.27 ?  158 LYS   A HA   1 
ATOM   3430 H HA   B LYS   A 1 158 ? 5.188  -1.482  5.547   0.14 25.74 ?  158 LYS   A HA   1 
ATOM   3431 H HB2  A LYS   A 1 158 ? 4.101  -0.047  6.873   0.86 31.30 ?  158 LYS   A HB2  1 
ATOM   3432 H HB2  B LYS   A 1 158 ? 3.915  -0.206  6.702   0.14 26.42 ?  158 LYS   A HB2  1 
ATOM   3433 H HB3  A LYS   A 1 158 ? 3.311  0.422   5.581   0.86 31.30 ?  158 LYS   A HB3  1 
ATOM   3434 H HB3  B LYS   A 1 158 ? 3.873  0.893   5.566   0.14 26.42 ?  158 LYS   A HB3  1 
ATOM   3435 H HG2  A LYS   A 1 158 ? 1.875  -0.628  7.084   0.86 33.51 ?  158 LYS   A HG2  1 
ATOM   3436 H HG2  B LYS   A 1 158 ? 1.747  0.377   5.876   0.14 27.04 ?  158 LYS   A HG2  1 
ATOM   3437 H HG3  A LYS   A 1 158 ? 1.931  -1.455  5.731   0.86 33.51 ?  158 LYS   A HG3  1 
ATOM   3438 H HG3  B LYS   A 1 158 ? 2.075  -0.427  4.562   0.14 27.04 ?  158 LYS   A HG3  1 
ATOM   3439 H HD2  A LYS   A 1 158 ? 3.302  -3.035  6.713   0.86 35.32 ?  158 LYS   A HD2  1 
ATOM   3440 H HD2  B LYS   A 1 158 ? 2.265  -2.387  5.839   0.14 27.59 ?  158 LYS   A HD2  1 
ATOM   3441 H HD3  A LYS   A 1 158 ? 3.403  -2.162  8.040   0.86 35.32 ?  158 LYS   A HD3  1 
ATOM   3442 H HD3  B LYS   A 1 158 ? 1.992  -1.546  7.163   0.14 27.59 ?  158 LYS   A HD3  1 
ATOM   3443 H HE2  A LYS   A 1 158 ? 1.230  -2.599  8.580   0.86 36.53 ?  158 LYS   A HE2  1 
ATOM   3444 H HE2  B LYS   A 1 158 ? 0.045  -1.542  5.152   0.14 28.03 ?  158 LYS   A HE2  1 
ATOM   3445 H HE3  A LYS   A 1 158 ? 0.948  -3.226  7.151   0.86 36.53 ?  158 LYS   A HE3  1 
ATOM   3446 H HE3  B LYS   A 1 158 ? 0.105  -2.772  6.159   0.14 28.03 ?  158 LYS   A HE3  1 
ATOM   3447 H HZ1  A LYS   A 1 158 ? 1.167  -4.867  8.707   0.86 37.17 ?  158 LYS   A HZ1  1 
ATOM   3448 H HZ1  B LYS   A 1 158 ? -1.357 -1.210  6.908   0.14 28.20 ?  158 LYS   A HZ1  1 
ATOM   3449 H HZ2  A LYS   A 1 158 ? 2.239  -5.002  7.742   0.86 37.17 ?  158 LYS   A HZ2  1 
ATOM   3450 H HZ2  B LYS   A 1 158 ? -0.271 -1.323  7.861   0.14 28.20 ?  158 LYS   A HZ2  1 
ATOM   3451 H HZ3  A LYS   A 1 158 ? 2.507  -4.433  9.047   0.86 37.17 ?  158 LYS   A HZ3  1 
ATOM   3452 H HZ3  B LYS   A 1 158 ? -0.324 -0.195  6.953   0.14 28.20 ?  158 LYS   A HZ3  1 
ATOM   3453 N N    A ASN   A 1 159 ? 3.534  -1.153  3.011   0.86 24.01 ?  159 ASN   A N    1 
ATOM   3454 N N    B ASN   A 1 159 ? 3.704  -1.039  2.742   0.14 22.26 ?  159 ASN   A N    1 
ATOM   3455 C CA   A ASN   A 1 159 ? 2.883  -1.834  1.900   0.86 24.29 ?  159 ASN   A CA   1 
ATOM   3456 C CA   B ASN   A 1 159 ? 3.062  -1.767  1.655   0.14 22.58 ?  159 ASN   A CA   1 
ATOM   3457 C C    A ASN   A 1 159 ? 3.790  -2.910  1.307   0.86 22.95 ?  159 ASN   A C    1 
ATOM   3458 C C    B ASN   A 1 159 ? 4.010  -2.747  0.982   0.14 21.64 ?  159 ASN   A C    1 
ATOM   3459 O O    A ASN   A 1 159 ? 3.346  -4.034  1.043   0.86 21.94 ?  159 ASN   A O    1 
ATOM   3460 O O    B ASN   A 1 159 ? 3.548  -3.712  0.364   0.14 21.45 ?  159 ASN   A O    1 
ATOM   3461 C CB   A ASN   A 1 159 ? 2.425  -0.812  0.855   0.86 26.72 ?  159 ASN   A CB   1 
ATOM   3462 C CB   B ASN   A 1 159 ? 2.481  -0.793  0.630   0.14 23.89 ?  159 ASN   A CB   1 
ATOM   3463 C CG   A ASN   A 1 159 ? 1.184  -0.050  1.294   0.86 29.56 ?  159 ASN   A CG   1 
ATOM   3464 C CG   B ASN   A 1 159 ? 1.287  -0.032  1.167   0.14 25.09 ?  159 ASN   A CG   1 
ATOM   3465 O OD1  A ASN   A 1 159 ? 0.331  -0.596  1.990   0.86 30.58 ?  159 ASN   A OD1  1 
ATOM   3466 O OD1  B ASN   A 1 159 ? 0.492  -0.567  1.940   0.14 25.48 ?  159 ASN   A OD1  1 
ATOM   3467 N ND2  A ASN   A 1 159 ? 1.078  1.213   0.888   0.86 30.97 ?  159 ASN   A ND2  1 
ATOM   3468 N ND2  B ASN   A 1 159 ? 1.155  1.225   0.765   0.14 25.60 ?  159 ASN   A ND2  1 
ATOM   3469 H H    A ASN   A 1 159 ? 3.634  -0.300  2.922   0.86 28.83 ?  159 ASN   A H    1 
ATOM   3470 H H    B ASN   A 1 159 ? 3.815  -0.199  2.599   0.14 26.72 ?  159 ASN   A H    1 
ATOM   3471 H HA   A ASN   A 1 159 ? 2.093  -2.274  2.243   0.86 29.15 ?  159 ASN   A HA   1 
ATOM   3472 H HA   B ASN   A 1 159 ? 2.327  -2.279  2.022   0.14 27.10 ?  159 ASN   A HA   1 
ATOM   3473 H HB2  A ASN   A 1 159 ? 3.131  -0.165  0.708   0.86 32.08 ?  159 ASN   A HB2  1 
ATOM   3474 H HB2  B ASN   A 1 159 ? 3.162  -0.149  0.383   0.14 28.68 ?  159 ASN   A HB2  1 
ATOM   3475 H HB3  A ASN   A 1 159 ? 2.215  -1.276  0.034   0.86 32.08 ?  159 ASN   A HB3  1 
ATOM   3476 H HB3  B ASN   A 1 159 ? 2.195  -1.293  -0.152  0.14 28.68 ?  159 ASN   A HB3  1 
ATOM   3477 H HD21 A ASN   A 1 159 ? 0.393  1.684   1.112   0.86 37.17 ?  159 ASN   A HD21 1 
ATOM   3478 H HD21 B ASN   A 1 159 ? 0.493  1.696   1.044   0.14 30.73 ?  159 ASN   A HD21 1 
ATOM   3479 H HD22 A ASN   A 1 159 ? 1.697  1.562   0.406   0.86 37.17 ?  159 ASN   A HD22 1 
ATOM   3480 H HD22 B ASN   A 1 159 ? 1.731  1.565   0.226   0.14 30.73 ?  159 ASN   A HD22 1 
ATOM   3481 N N    A LEU   A 1 160 ? 5.073  -2.600  1.129   0.86 21.72 ?  160 LEU   A N    1 
ATOM   3482 N N    B LEU   A 1 160 ? 5.321  -2.525  1.089   0.14 20.79 ?  160 LEU   A N    1 
ATOM   3483 C CA   A LEU   A 1 160 ? 5.993  -3.603  0.606   0.86 20.89 ?  160 LEU   A CA   1 
ATOM   3484 C CA   B LEU   A 1 160 ? 6.278  -3.509  0.597   0.14 19.89 ?  160 LEU   A CA   1 
ATOM   3485 C C    A LEU   A 1 160 ? 6.176  -4.754  1.586   0.86 19.72 ?  160 LEU   A C    1 
ATOM   3486 C C    B LEU   A 1 160 ? 6.340  -4.712  1.529   0.14 19.39 ?  160 LEU   A C    1 
ATOM   3487 O O    A LEU   A 1 160 ? 6.195  -5.922  1.181   0.86 20.31 ?  160 LEU   A O    1 
ATOM   3488 O O    B LEU   A 1 160 ? 6.312  -5.864  1.079   0.14 19.44 ?  160 LEU   A O    1 
ATOM   3489 C CB   A LEU   A 1 160 ? 7.334  -2.965  0.260   0.86 20.37 ?  160 LEU   A CB   1 
ATOM   3490 C CB   B LEU   A 1 160 ? 7.657  -2.866  0.453   0.14 19.57 ?  160 LEU   A CB   1 
ATOM   3491 C CG   A LEU   A 1 160 ? 8.388  -3.971  -0.204  0.86 20.71 ?  160 LEU   A CG   1 
ATOM   3492 C CG   B LEU   A 1 160 ? 8.794  -3.823  0.099   0.14 19.29 ?  160 LEU   A CG   1 
ATOM   3493 C CD1  A LEU   A 1 160 ? 7.896  -4.718  -1.425  0.86 21.41 ?  160 LEU   A CD1  1 
ATOM   3494 C CD1  B LEU   A 1 160 ? 8.470  -4.572  -1.179  0.14 19.15 ?  160 LEU   A CD1  1 
ATOM   3495 C CD2  A LEU   A 1 160 ? 9.710  -3.284  -0.494  0.86 21.04 ?  160 LEU   A CD2  1 
ATOM   3496 C CD2  B LEU   A 1 160 ? 10.111 -3.074  -0.030  0.14 19.14 ?  160 LEU   A CD2  1 
ATOM   3497 H H    A LEU   A 1 160 ? 5.430  -1.830  1.307   0.86 26.07 ?  160 LEU   A H    1 
ATOM   3498 H H    B LEU   A 1 160 ? 5.675  -1.822  1.436   0.14 24.95 ?  160 LEU   A H    1 
ATOM   3499 H HA   A LEU   A 1 160 ? 5.616  -3.959  -0.208  0.86 25.07 ?  160 LEU   A HA   1 
ATOM   3500 H HA   B LEU   A 1 160 ? 5.995  -3.816  -0.276  0.14 23.88 ?  160 LEU   A HA   1 
ATOM   3501 H HB2  A LEU   A 1 160 ? 7.205  -2.309  -0.451  0.86 24.45 ?  160 LEU   A HB2  1 
ATOM   3502 H HB2  B LEU   A 1 160 ? 7.618  -2.178  -0.237  0.14 23.49 ?  160 LEU   A HB2  1 
ATOM   3503 H HB3  A LEU   A 1 160 ? 7.683  -2.524  1.050   0.86 24.45 ?  160 LEU   A HB3  1 
ATOM   3504 H HB3  B LEU   A 1 160 ? 7.886  -2.466  1.303   0.14 23.49 ?  160 LEU   A HB3  1 
ATOM   3505 H HG   A LEU   A 1 160 ? 8.543  -4.615  0.500   0.86 24.86 ?  160 LEU   A HG   1 
ATOM   3506 H HG   B LEU   A 1 160 ? 8.895  -4.473  0.813   0.14 23.15 ?  160 LEU   A HG   1 
ATOM   3507 H HD11 A LEU   A 1 160 ? 8.619  -5.256  -1.774  0.86 25.70 ?  160 LEU   A HD11 1 
ATOM   3508 H HD11 B LEU   A 1 160 ? 9.245  -5.088  -1.442  0.14 22.98 ?  160 LEU   A HD11 1 
ATOM   3509 H HD12 A LEU   A 1 160 ? 7.153  -5.290  -1.169  0.86 25.70 ?  160 LEU   A HD12 1 
ATOM   3510 H HD12 B LEU   A 1 160 ? 7.719  -5.163  -1.018  0.14 22.98 ?  160 LEU   A HD12 1 
ATOM   3511 H HD13 A LEU   A 1 160 ? 7.604  -4.077  -2.093  0.86 25.70 ?  160 LEU   A HD13 1 
ATOM   3512 H HD13 B LEU   A 1 160 ? 8.248  -3.930  -1.872  0.14 22.98 ?  160 LEU   A HD13 1 
ATOM   3513 H HD21 A LEU   A 1 160 ? 10.353 -3.952  -0.783  0.86 25.26 ?  160 LEU   A HD21 1 
ATOM   3514 H HD21 B LEU   A 1 160 ? 10.813 -3.707  -0.250  0.14 22.98 ?  160 LEU   A HD21 1 
ATOM   3515 H HD22 A LEU   A 1 160 ? 9.580  -2.627  -1.196  0.86 25.26 ?  160 LEU   A HD22 1 
ATOM   3516 H HD22 B LEU   A 1 160 ? 10.030 -2.411  -0.733  0.14 22.98 ?  160 LEU   A HD22 1 
ATOM   3517 H HD23 A LEU   A 1 160 ? 10.025 -2.850  0.313   0.86 25.26 ?  160 LEU   A HD23 1 
ATOM   3518 H HD23 B LEU   A 1 160 ? 10.312 -2.639  0.814   0.14 22.98 ?  160 LEU   A HD23 1 
ATOM   3519 N N    A TYR   A 1 161 ? 6.311  -4.445  2.877   0.86 18.70 ?  161 TYR   A N    1 
ATOM   3520 N N    B TYR   A 1 161 ? 6.427  -4.461  2.837   0.14 18.93 ?  161 TYR   A N    1 
ATOM   3521 C CA   A TYR   A 1 161 ? 6.443  -5.494  3.883   0.86 18.44 ?  161 TYR   A CA   1 
ATOM   3522 C CA   B TYR   A 1 161 ? 6.435  -5.546  3.813   0.14 18.71 ?  161 TYR   A CA   1 
ATOM   3523 C C    A TYR   A 1 161 ? 5.296  -6.498  3.786   0.86 18.87 ?  161 TYR   A C    1 
ATOM   3524 C C    B TYR   A 1 161 ? 5.226  -6.454  3.624   0.14 18.97 ?  161 TYR   A C    1 
ATOM   3525 O O    A TYR   A 1 161 ? 5.513  -7.715  3.773   0.86 18.78 ?  161 TYR   A O    1 
ATOM   3526 O O    B TYR   A 1 161 ? 5.355  -7.683  3.583   0.14 18.74 ?  161 TYR   A O    1 
ATOM   3527 C CB   A TYR   A 1 161 ? 6.509  -4.875  5.283   0.86 19.02 ?  161 TYR   A CB   1 
ATOM   3528 C CB   B TYR   A 1 161 ? 6.456  -4.957  5.226   0.14 18.43 ?  161 TYR   A CB   1 
ATOM   3529 C CG   A TYR   A 1 161 ? 6.416  -5.901  6.380   0.86 18.51 ?  161 TYR   A CG   1 
ATOM   3530 C CG   B TYR   A 1 161 ? 6.333  -5.977  6.337   0.14 18.06 ?  161 TYR   A CG   1 
ATOM   3531 C CD1  A TYR   A 1 161 ? 7.539  -6.599  6.796   0.86 18.08 ?  161 TYR   A CD1  1 
ATOM   3532 C CD1  B TYR   A 1 161 ? 5.088  -6.351  6.830   0.14 18.04 ?  161 TYR   A CD1  1 
ATOM   3533 C CD2  A TYR   A 1 161 ? 5.203  -6.183  6.997   0.86 18.77 ?  161 TYR   A CD2  1 
ATOM   3534 C CD2  B TYR   A 1 161 ? 7.462  -6.542  6.917   0.14 17.79 ?  161 TYR   A CD2  1 
ATOM   3535 C CE1  A TYR   A 1 161 ? 7.461  -7.557  7.787   0.86 18.22 ?  161 TYR   A CE1  1 
ATOM   3536 C CE1  B TYR   A 1 161 ? 4.970  -7.273  7.852   0.14 17.92 ?  161 TYR   A CE1  1 
ATOM   3537 C CE2  A TYR   A 1 161 ? 5.114  -7.139  7.992   0.86 18.64 ?  161 TYR   A CE2  1 
ATOM   3538 C CE2  B TYR   A 1 161 ? 7.353  -7.466  7.942   0.14 17.76 ?  161 TYR   A CE2  1 
ATOM   3539 C CZ   A TYR   A 1 161 ? 6.246  -7.824  8.383   0.86 18.89 ?  161 TYR   A CZ   1 
ATOM   3540 C CZ   B TYR   A 1 161 ? 6.105  -7.827  8.404   0.14 17.89 ?  161 TYR   A CZ   1 
ATOM   3541 O OH   A TYR   A 1 161 ? 6.178  -8.778  9.373   0.86 19.83 ?  161 TYR   A OH   1 
ATOM   3542 O OH   B TYR   A 1 161 ? 5.991  -8.746  9.423   0.14 18.17 ?  161 TYR   A OH   1 
ATOM   3543 H H    A TYR   A 1 161 ? 6.316  -3.643  3.193   0.86 22.45 ?  161 TYR   A H    1 
ATOM   3544 H H    B TYR   A 1 161 ? 6.481  -3.676  3.180   0.14 22.72 ?  161 TYR   A H    1 
ATOM   3545 H HA   A TYR   A 1 161 ? 7.269  -5.970  3.732   0.86 22.13 ?  161 TYR   A HA   1 
ATOM   3546 H HA   B TYR   A 1 161 ? 7.237  -6.078  3.695   0.14 22.46 ?  161 TYR   A HA   1 
ATOM   3547 H HB2  A TYR   A 1 161 ? 7.352  -4.407  5.383   0.86 22.84 ?  161 TYR   A HB2  1 
ATOM   3548 H HB2  B TYR   A 1 161 ? 7.295  -4.486  5.352   0.14 22.12 ?  161 TYR   A HB2  1 
ATOM   3549 H HB3  A TYR   A 1 161 ? 5.771  -4.254  5.392   0.86 22.84 ?  161 TYR   A HB3  1 
ATOM   3550 H HB3  B TYR   A 1 161 ? 5.718  -4.335  5.314   0.14 22.12 ?  161 TYR   A HB3  1 
ATOM   3551 H HD1  A TYR   A 1 161 ? 8.359  -6.424  6.393   0.86 21.70 ?  161 TYR   A HD1  1 
ATOM   3552 H HD1  B TYR   A 1 161 ? 4.319  -5.980  6.462   0.14 21.66 ?  161 TYR   A HD1  1 
ATOM   3553 H HD2  A TYR   A 1 161 ? 4.433  -5.731  6.735   0.86 22.54 ?  161 TYR   A HD2  1 
ATOM   3554 H HD2  B TYR   A 1 161 ? 8.305  -6.300  6.609   0.14 21.36 ?  161 TYR   A HD2  1 
ATOM   3555 H HE1  A TYR   A 1 161 ? 8.226  -8.014  8.057   0.86 21.87 ?  161 TYR   A HE1  1 
ATOM   3556 H HE1  B TYR   A 1 161 ? 4.129  -7.518  8.168   0.14 21.52 ?  161 TYR   A HE1  1 
ATOM   3557 H HE2  A TYR   A 1 161 ? 4.293  -7.321  8.399   0.86 22.37 ?  161 TYR   A HE2  1 
ATOM   3558 H HE2  B TYR   A 1 161 ? 8.117  -7.840  8.318   0.14 21.32 ?  161 TYR   A HE2  1 
ATOM   3559 H HH   A TYR   A 1 161 ? 5.380  -8.844  9.656   0.86 23.81 ?  161 TYR   A HH   1 
ATOM   3560 H HH   B TYR   A 1 161 ? 5.181  -8.861  9.618   0.14 21.81 ?  161 TYR   A HH   1 
ATOM   3561 N N    A ASP   A 1 162 ? 4.061  -6.004  3.718   0.86 19.46 ?  162 ASP   A N    1 
ATOM   3562 N N    B ASP   A 1 162 ? 4.037  -5.860  3.505   0.14 19.52 ?  162 ASP   A N    1 
ATOM   3563 C CA   A ASP   A 1 162 ? 2.918  -6.912  3.666   0.86 20.22 ?  162 ASP   A CA   1 
ATOM   3564 C CA   B ASP   A 1 162 ? 2.831  -6.650  3.277   0.14 20.14 ?  162 ASP   A CA   1 
ATOM   3565 C C    A ASP   A 1 162 ? 2.949  -7.763  2.401   0.86 20.09 ?  162 ASP   A C    1 
ATOM   3566 C C    B ASP   A 1 162 ? 2.951  -7.478  2.003   0.14 20.84 ?  162 ASP   A C    1 
ATOM   3567 O O    A ASP   A 1 162 ? 2.597  -8.949  2.430   0.86 20.62 ?  162 ASP   A O    1 
ATOM   3568 O O    B ASP   A 1 162 ? 2.609  -8.666  1.988   0.14 20.69 ?  162 ASP   A O    1 
ATOM   3569 C CB   A ASP   A 1 162 ? 1.605  -6.129  3.746   0.86 21.56 ?  162 ASP   A CB   1 
ATOM   3570 C CB   B ASP   A 1 162 ? 1.610  -5.732  3.205   0.14 20.27 ?  162 ASP   A CB   1 
ATOM   3571 C CG   A ASP   A 1 162 ? 1.335  -5.552  5.117   0.86 23.35 ?  162 ASP   A CG   1 
ATOM   3572 C CG   B ASP   A 1 162 ? 1.250  -5.128  4.546   0.14 20.33 ?  162 ASP   A CG   1 
ATOM   3573 O OD1  A ASP   A 1 162 ? 1.969  -5.983  6.097   0.86 24.41 ?  162 ASP   A OD1  1 
ATOM   3574 O OD1  B ASP   A 1 162 ? 1.919  -5.445  5.551   0.14 20.36 ?  162 ASP   A OD1  1 
ATOM   3575 O OD2  A ASP   A 1 162 ? 0.443  -4.682  5.215   0.86 24.92 -1 162 ASP   A OD2  1 
ATOM   3576 O OD2  B ASP   A 1 162 ? 0.287  -4.334  4.591   0.14 20.43 -1 162 ASP   A OD2  1 
ATOM   3577 H H    A ASP   A 1 162 ? 3.858  -5.171  3.705   0.86 23.37 ?  162 ASP   A H    1 
ATOM   3578 H H    B ASP   A 1 162 ? 3.906  -5.014  3.559   0.14 23.43 ?  162 ASP   A H    1 
ATOM   3579 H HA   A ASP   A 1 162 ? 2.953  -7.514  4.428   0.86 24.27 ?  162 ASP   A HA   1 
ATOM   3580 H HA   B ASP   A 1 162 ? 2.705  -7.261  4.018   0.14 24.18 ?  162 ASP   A HA   1 
ATOM   3581 H HB2  A ASP   A 1 162 ? 1.633  -5.394  3.123   0.86 25.88 ?  162 ASP   A HB2  1 
ATOM   3582 H HB2  B ASP   A 1 162 ? 1.796  -5.004  2.593   0.14 24.33 ?  162 ASP   A HB2  1 
ATOM   3583 H HB3  A ASP   A 1 162 ? 0.867  -6.722  3.541   0.86 25.88 ?  162 ASP   A HB3  1 
ATOM   3584 H HB3  B ASP   A 1 162 ? 0.847  -6.243  2.896   0.14 24.33 ?  162 ASP   A HB3  1 
ATOM   3585 N N    A LYS   A 1 163 ? 3.368  -7.178  1.279   0.86 21.07 ?  163 LYS   A N    1 
ATOM   3586 N N    B LYS   A 1 163 ? 3.430  -6.865  0.917   0.14 21.89 ?  163 LYS   A N    1 
ATOM   3587 C CA   A LYS   A 1 163 ? 3.464  -7.950  0.044   0.86 21.72 ?  163 LYS   A CA   1 
ATOM   3588 C CA   B LYS   A 1 163 ? 3.571  -7.609  -0.331  0.14 22.82 ?  163 LYS   A CA   1 
ATOM   3589 C C    A LYS   A 1 163 ? 4.551  -9.015  0.137   0.86 21.04 ?  163 LYS   A C    1 
ATOM   3590 C C    B LYS   A 1 163 ? 4.589  -8.733  -0.192  0.14 21.65 ?  163 LYS   A C    1 
ATOM   3591 O O    A LYS   A 1 163 ? 4.386  -10.125 -0.379  0.86 21.47 ?  163 LYS   A O    1 
ATOM   3592 O O    B LYS   A 1 163 ? 4.356  -9.852  -0.664  0.14 21.52 ?  163 LYS   A O    1 
ATOM   3593 C CB   A LYS   A 1 163 ? 3.723  -7.019  -1.140  0.86 24.85 ?  163 LYS   A CB   1 
ATOM   3594 C CB   B LYS   A 1 163 ? 3.957  -6.675  -1.479  0.14 24.95 ?  163 LYS   A CB   1 
ATOM   3595 C CG   A LYS   A 1 163 ? 3.792  -7.736  -2.477  0.86 28.34 ?  163 LYS   A CG   1 
ATOM   3596 C CG   B LYS   A 1 163 ? 4.319  -7.424  -2.752  0.14 27.05 ?  163 LYS   A CG   1 
ATOM   3597 C CD   A LYS   A 1 163 ? 4.152  -6.781  -3.601  0.86 32.07 ?  163 LYS   A CD   1 
ATOM   3598 C CD   B LYS   A 1 163 ? 4.307  -6.529  -3.977  0.14 28.87 ?  163 LYS   A CD   1 
ATOM   3599 C CE   A LYS   A 1 163 ? 4.028  -7.458  -4.956  0.86 34.74 ?  163 LYS   A CE   1 
ATOM   3600 C CE   B LYS   A 1 163 ? 4.398  -7.361  -5.246  0.14 30.19 ?  163 LYS   A CE   1 
ATOM   3601 N NZ   A LYS   A 1 163 ? 4.615  -6.639  -6.053  0.86 36.01 ?  163 LYS   A NZ   1 
ATOM   3602 N NZ   B LYS   A 1 163 ? 4.317  -6.535  -6.478  0.14 30.93 ?  163 LYS   A NZ   1 
ATOM   3603 H H    A LYS   A 1 163 ? 3.596  -6.349  1.211   0.86 25.29 ?  163 LYS   A H    1 
ATOM   3604 H H    B LYS   A 1 163 ? 3.672  -6.039  0.878   0.14 26.28 ?  163 LYS   A H    1 
ATOM   3605 H HA   A LYS   A 1 163 ? 2.617  -8.397  -0.107  0.86 26.07 ?  163 LYS   A HA   1 
ATOM   3606 H HA   B LYS   A 1 163 ? 2.716  -8.008  -0.554  0.14 27.40 ?  163 LYS   A HA   1 
ATOM   3607 H HB2  A LYS   A 1 163 ? 3.003  -6.369  -1.190  0.86 29.83 ?  163 LYS   A HB2  1 
ATOM   3608 H HB2  B LYS   A 1 163 ? 3.206  -6.092  -1.680  0.14 29.95 ?  163 LYS   A HB2  1 
ATOM   3609 H HB3  A LYS   A 1 163 ? 4.567  -6.565  -1.001  0.86 29.83 ?  163 LYS   A HB3  1 
ATOM   3610 H HB3  B LYS   A 1 163 ? 4.725  -6.146  -1.214  0.14 29.95 ?  163 LYS   A HB3  1 
ATOM   3611 H HG2  A LYS   A 1 163 ? 4.473  -8.426  -2.440  0.86 34.01 ?  163 LYS   A HG2  1 
ATOM   3612 H HG2  B LYS   A 1 163 ? 5.213  -7.791  -2.662  0.14 32.46 ?  163 LYS   A HG2  1 
ATOM   3613 H HG3  A LYS   A 1 163 ? 2.927  -8.129  -2.675  0.86 34.01 ?  163 LYS   A HG3  1 
ATOM   3614 H HG3  B LYS   A 1 163 ? 3.679  -8.138  -2.895  0.14 32.46 ?  163 LYS   A HG3  1 
ATOM   3615 H HD2  A LYS   A 1 163 ? 3.548  -6.022  -3.583  0.86 38.49 ?  163 LYS   A HD2  1 
ATOM   3616 H HD2  B LYS   A 1 163 ? 3.481  -6.023  -3.999  0.14 34.66 ?  163 LYS   A HD2  1 
ATOM   3617 H HD3  A LYS   A 1 163 ? 5.069  -6.484  -3.488  0.86 38.49 ?  163 LYS   A HD3  1 
ATOM   3618 H HD3  B LYS   A 1 163 ? 5.071  -5.931  -3.947  0.14 34.66 ?  163 LYS   A HD3  1 
ATOM   3619 H HE2  A LYS   A 1 163 ? 4.482  -8.314  -4.931  0.86 41.70 ?  163 LYS   A HE2  1 
ATOM   3620 H HE2  B LYS   A 1 163 ? 5.249  -7.823  -5.256  0.14 36.24 ?  163 LYS   A HE2  1 
ATOM   3621 H HE3  A LYS   A 1 163 ? 3.090  -7.591  -5.155  0.86 41.70 ?  163 LYS   A HE3  1 
ATOM   3622 H HE3  B LYS   A 1 163 ? 3.668  -8.003  -5.259  0.14 36.24 ?  163 LYS   A HE3  1 
ATOM   3623 H HZ1  A LYS   A 1 163 ? 4.527  -7.064  -6.830  0.86 43.23 ?  163 LYS   A HZ1  1 
ATOM   3624 H HZ1  B LYS   A 1 163 ? 4.373  -7.057  -7.197  0.14 37.12 ?  163 LYS   A HZ1  1 
ATOM   3625 H HZ2  A LYS   A 1 163 ? 4.197  -5.855  -6.103  0.86 43.23 ?  163 LYS   A HZ2  1 
ATOM   3626 H HZ2  B LYS   A 1 163 ? 3.545  -6.095  -6.499  0.14 37.12 ?  163 LYS   A HZ2  1 
ATOM   3627 H HZ3  A LYS   A 1 163 ? 5.480  -6.496  -5.898  0.86 43.23 ?  163 LYS   A HZ3  1 
ATOM   3628 H HZ3  B LYS   A 1 163 ? 4.987  -5.949  -6.494  0.14 37.12 ?  163 LYS   A HZ3  1 
ATOM   3629 N N    A LEU   A 1 164 ? 5.676  -8.690  0.777   0.86 19.27 ?  164 LEU   A N    1 
ATOM   3630 N N    B LEU   A 1 164 ? 5.726  -8.458  0.450   0.14 20.61 ?  164 LEU   A N    1 
ATOM   3631 C CA   A LEU   A 1 164 ? 6.765  -9.655  0.917   0.86 18.67 ?  164 LEU   A CA   1 
ATOM   3632 C CA   B LEU   A 1 164 ? 6.744  -9.491  0.615   0.14 19.83 ?  164 LEU   A CA   1 
ATOM   3633 C C    A LEU   A 1 164 ? 6.341  -10.840 1.770   0.86 18.91 ?  164 LEU   A C    1 
ATOM   3634 C C    B LEU   A 1 164 ? 6.228  -10.641 1.467   0.14 19.18 ?  164 LEU   A C    1 
ATOM   3635 O O    A LEU   A 1 164 ? 6.641  -11.993 1.442   0.86 19.32 ?  164 LEU   A O    1 
ATOM   3636 O O    B LEU   A 1 164 ? 6.490  -11.812 1.168   0.14 19.19 ?  164 LEU   A O    1 
ATOM   3637 C CB   A LEU   A 1 164 ? 7.970  -8.966  1.546   0.86 17.70 ?  164 LEU   A CB   1 
ATOM   3638 C CB   B LEU   A 1 164 ? 8.002  -8.895  1.246   0.14 19.71 ?  164 LEU   A CB   1 
ATOM   3639 C CG   A LEU   A 1 164 ? 8.737  -7.995  0.646   0.86 18.00 ?  164 LEU   A CG   1 
ATOM   3640 C CG   B LEU   A 1 164 ? 8.826  -7.932  0.394   0.14 19.59 ?  164 LEU   A CG   1 
ATOM   3641 C CD1  A LEU   A 1 164 ? 9.654  -7.112  1.475   0.86 17.76 ?  164 LEU   A CD1  1 
ATOM   3642 C CD1  B LEU   A 1 164 ? 9.971  -7.367  1.215   0.14 19.53 ?  164 LEU   A CD1  1 
ATOM   3643 C CD2  A LEU   A 1 164 ? 9.541  -8.743  -0.409  0.86 18.26 ?  164 LEU   A CD2  1 
ATOM   3644 C CD2  B LEU   A 1 164 ? 9.349  -8.626  -0.855  0.14 19.56 ?  164 LEU   A CD2  1 
ATOM   3645 H H    A LEU   A 1 164 ? 5.834  -7.922  1.135   0.86 23.13 ?  164 LEU   A H    1 
ATOM   3646 H H    B LEU   A 1 164 ? 5.927  -7.695  0.794   0.14 24.74 ?  164 LEU   A H    1 
ATOM   3647 H HA   A LEU   A 1 164 ? 7.022  -9.981  0.044   0.86 22.41 ?  164 LEU   A HA   1 
ATOM   3648 H HA   B LEU   A 1 164 ? 6.979  -9.845  -0.255  0.14 23.81 ?  164 LEU   A HA   1 
ATOM   3649 H HB2  A LEU   A 1 164 ? 7.672  -8.460  2.316   0.86 21.25 ?  164 LEU   A HB2  1 
ATOM   3650 H HB2  B LEU   A 1 164 ? 7.738  -8.413  2.044   0.14 23.66 ?  164 LEU   A HB2  1 
ATOM   3651 H HB3  A LEU   A 1 164 ? 8.601  -9.644  1.829   0.86 21.25 ?  164 LEU   A HB3  1 
ATOM   3652 H HB3  B LEU   A 1 164 ? 8.588  -9.627  1.494   0.14 23.66 ?  164 LEU   A HB3  1 
ATOM   3653 H HG   A LEU   A 1 164 ? 8.108  -7.416  0.187   0.86 21.61 ?  164 LEU   A HG   1 
ATOM   3654 H HG   B LEU   A 1 164 ? 8.264  -7.193  0.115   0.14 23.52 ?  164 LEU   A HG   1 
ATOM   3655 H HD11 A LEU   A 1 164 ? 10.137 -6.508  0.886   0.86 21.33 ?  164 LEU   A HD11 1 
ATOM   3656 H HD11 B LEU   A 1 164 ? 10.476 -6.746  0.669   0.14 23.45 ?  164 LEU   A HD11 1 
ATOM   3657 H HD12 A LEU   A 1 164 ? 9.120  -6.599  2.103   0.86 21.33 ?  164 LEU   A HD12 1 
ATOM   3658 H HD12 B LEU   A 1 164 ? 9.607  -6.909  1.989   0.14 23.45 ?  164 LEU   A HD12 1 
ATOM   3659 H HD13 A LEU   A 1 164 ? 10.284 -7.671  1.957   0.86 21.33 ?  164 LEU   A HD13 1 
ATOM   3660 H HD13 B LEU   A 1 164 ? 10.543 -8.097  1.502   0.14 23.45 ?  164 LEU   A HD13 1 
ATOM   3661 H HD21 A LEU   A 1 164 ? 10.050 -8.102  -0.934  0.86 21.92 ?  164 LEU   A HD21 1 
ATOM   3662 H HD21 B LEU   A 1 164 ? 10.100 -8.124  -1.206  0.14 23.48 ?  164 LEU   A HD21 1 
ATOM   3663 H HD22 A LEU   A 1 164 ? 10.146 -9.359  0.033   0.86 21.92 ?  164 LEU   A HD22 1 
ATOM   3664 H HD22 B LEU   A 1 164 ? 9.634  -9.523  -0.620  0.14 23.48 ?  164 LEU   A HD22 1 
ATOM   3665 H HD23 A LEU   A 1 164 ? 8.931  -9.229  -0.984  0.86 21.92 ?  164 LEU   A HD23 1 
ATOM   3666 H HD23 B LEU   A 1 164 ? 8.638  -8.668  -1.514  0.14 23.48 ?  164 LEU   A HD23 1 
ATOM   3667 N N    A VAL   A 1 165 ? 5.661  -10.571 2.882   0.86 18.15 ?  165 VAL   A N    1 
ATOM   3668 N N    B VAL   A 1 165 ? 5.493  -10.329 2.534   0.14 18.50 ?  165 VAL   A N    1 
ATOM   3669 C CA   A VAL   A 1 165 ? 5.186  -11.649 3.743   0.86 18.21 ?  165 VAL   A CA   1 
ATOM   3670 C CA   B VAL   A 1 165 ? 5.009  -11.373 3.430   0.14 18.04 ?  165 VAL   A CA   1 
ATOM   3671 C C    A VAL   A 1 165 ? 4.139  -12.483 3.017   0.86 18.42 ?  165 VAL   A C    1 
ATOM   3672 C C    B VAL   A 1 165 ? 4.007  -12.270 2.713   0.14 17.94 ?  165 VAL   A C    1 
ATOM   3673 O O    A VAL   A 1 165 ? 4.220  -13.717 2.974   0.86 18.38 ?  165 VAL   A O    1 
ATOM   3674 O O    B VAL   A 1 165 ? 4.128  -13.499 2.730   0.14 18.01 ?  165 VAL   A O    1 
ATOM   3675 C CB   A VAL   A 1 165 ? 4.634  -11.071 5.059   0.86 18.73 ?  165 VAL   A CB   1 
ATOM   3676 C CB   B VAL   A 1 165 ? 4.427  -10.756 4.716   0.14 17.96 ?  165 VAL   A CB   1 
ATOM   3677 C CG1  A VAL   A 1 165 ? 3.898  -12.147 5.854   0.86 19.50 ?  165 VAL   A CG1  1 
ATOM   3678 C CG1  B VAL   A 1 165 ? 3.661  -11.801 5.512   0.14 17.98 ?  165 VAL   A CG1  1 
ATOM   3679 C CG2  A VAL   A 1 165 ? 5.754  -10.440 5.881   0.86 19.67 ?  165 VAL   A CG2  1 
ATOM   3680 C CG2  B VAL   A 1 165 ? 5.541  -10.154 5.563   0.14 17.94 ?  165 VAL   A CG2  1 
ATOM   3681 H H    A VAL   A 1 165 ? 5.466  -9.783  3.161   0.86 21.78 ?  165 VAL   A H    1 
ATOM   3682 H H    B VAL   A 1 165 ? 5.262  -9.531  2.755   0.14 22.20 ?  165 VAL   A H    1 
ATOM   3683 H HA   A VAL   A 1 165 ? 5.931  -12.231 3.971   0.86 21.86 ?  165 VAL   A HA   1 
ATOM   3684 H HA   B VAL   A 1 165 ? 5.757  -11.928 3.692   0.14 21.66 ?  165 VAL   A HA   1 
ATOM   3685 H HB   A VAL   A 1 165 ? 3.995  -10.371 4.849   0.86 22.49 ?  165 VAL   A HB   1 
ATOM   3686 H HB   B VAL   A 1 165 ? 3.811  -10.043 4.482   0.14 21.57 ?  165 VAL   A HB   1 
ATOM   3687 H HG11 A VAL   A 1 165 ? 3.806  -11.850 6.774   0.86 23.41 ?  165 VAL   A HG11 1 
ATOM   3688 H HG11 B VAL   A 1 165 ? 3.552  -11.485 6.423   0.14 21.58 ?  165 VAL   A HG11 1 
ATOM   3689 H HG12 A VAL   A 1 165 ? 3.015  -12.278 5.466   0.86 23.41 ?  165 VAL   A HG12 1 
ATOM   3690 H HG12 B VAL   A 1 165 ? 2.792  -11.938 5.104   0.14 21.58 ?  165 VAL   A HG12 1 
ATOM   3691 H HG13 A VAL   A 1 165 ? 4.404  -12.969 5.819   0.86 23.41 ?  165 VAL   A HG13 1 
ATOM   3692 H HG13 B VAL   A 1 165 ? 4.166  -12.630 5.510   0.14 21.58 ?  165 VAL   A HG13 1 
ATOM   3693 H HG21 A VAL   A 1 165 ? 5.383  -10.087 6.707   0.86 23.61 ?  165 VAL   A HG21 1 
ATOM   3694 H HG21 B VAL   A 1 165 ? 5.150  -9.701  6.327   0.14 21.54 ?  165 VAL   A HG21 1 
ATOM   3695 H HG22 A VAL   A 1 165 ? 6.420  -11.115 6.080   0.86 23.61 ?  165 VAL   A HG22 1 
ATOM   3696 H HG22 B VAL   A 1 165 ? 6.126  -10.867 5.867   0.14 21.54 ?  165 VAL   A HG22 1 
ATOM   3697 H HG23 A VAL   A 1 165 ? 6.155  -9.720  5.367   0.86 23.61 ?  165 VAL   A HG23 1 
ATOM   3698 H HG23 B VAL   A 1 165 ? 6.043  -9.522  5.025   0.14 21.54 ?  165 VAL   A HG23 1 
ATOM   3699 N N    A SER   A 1 166 ? 3.139  -11.818 2.435   0.86 18.94 ?  166 SER   A N    1 
ATOM   3700 N N    B SER   A 1 166 ? 3.016  -11.671 2.054   0.14 17.88 ?  166 SER   A N    1 
ATOM   3701 C CA   A SER   A 1 166 ? 2.007  -12.540 1.862   0.86 19.74 ?  166 SER   A CA   1 
ATOM   3702 C CA   B SER   A 1 166 ? 1.936  -12.441 1.450   0.14 18.10 ?  166 SER   A CA   1 
ATOM   3703 C C    A SER   A 1 166 ? 2.411  -13.382 0.663   0.86 20.03 ?  166 SER   A C    1 
ATOM   3704 C C    B SER   A 1 166 ? 2.334  -13.134 0.152   0.14 18.73 ?  166 SER   A C    1 
ATOM   3705 O O    A SER   A 1 166 ? 1.745  -14.382 0.360   0.86 21.92 ?  166 SER   A O    1 
ATOM   3706 O O    B SER   A 1 166 ? 1.570  -13.976 -0.334  0.14 18.54 ?  166 SER   A O    1 
ATOM   3707 C CB   A SER   A 1 166 ? 0.907  -11.557 1.457   0.86 21.72 ?  166 SER   A CB   1 
ATOM   3708 C CB   B SER   A 1 166 ? 0.718  -11.546 1.213   0.14 17.75 ?  166 SER   A CB   1 
ATOM   3709 O OG   A SER   A 1 166 ? 0.262  -11.004 2.591   0.86 23.85 ?  166 SER   A OG   1 
ATOM   3710 O OG   B SER   A 1 166 ? 1.090  -10.369 0.524   0.14 17.42 ?  166 SER   A OG   1 
ATOM   3711 H H    A SER   A 1 166 ? 3.089  -10.965 2.376   0.86 22.73 ?  166 SER   A H    1 
ATOM   3712 H H    B SER   A 1 166 ? 2.951  -10.821 1.942   0.14 21.46 ?  166 SER   A H    1 
ATOM   3713 H HA   A SER   A 1 166 ? 1.635  -13.136 2.531   0.86 23.70 ?  166 SER   A HA   1 
ATOM   3714 H HA   B SER   A 1 166 ? 1.671  -13.131 2.069   0.14 21.72 ?  166 SER   A HA   1 
ATOM   3715 H HB2  A SER   A 1 166 ? 1.296  -10.844 0.928   0.86 26.07 ?  166 SER   A HB2  1 
ATOM   3716 H HB2  B SER   A 1 166 ? 0.065  -12.030 0.682   0.14 21.31 ?  166 SER   A HB2  1 
ATOM   3717 H HB3  A SER   A 1 166 ? 0.237  -12.026 0.936   0.86 26.07 ?  166 SER   A HB3  1 
ATOM   3718 H HB3  B SER   A 1 166 ? 0.330  -11.306 2.071   0.14 21.31 ?  166 SER   A HB3  1 
ATOM   3719 H HG   A SER   A 1 166 ? -0.324 -10.449 2.351   0.86 28.63 ?  166 SER   A HG   1 
ATOM   3720 H HG   B SER   A 1 166 ? 1.563  -9.881  1.020   0.14 20.91 ?  166 SER   A HG   1 
ATOM   3721 N N    A SER   A 1 167 ? 3.475  -12.996 -0.039  0.86 19.66 ?  167 SER   A N    1 
ATOM   3722 N N    B SER   A 1 167 ? 3.494  -12.814 -0.418  0.14 19.52 ?  167 SER   A N    1 
ATOM   3723 C CA   A SER   A 1 167 ? 3.915  -13.712 -1.227  0.86 20.34 ?  167 SER   A CA   1 
ATOM   3724 C CA   B SER   A 1 167 ? 3.973  -13.465 -1.631  0.14 20.28 ?  167 SER   A CA   1 
ATOM   3725 C C    A SER   A 1 167 ? 5.062  -14.673 -0.949  0.86 20.19 ?  167 SER   A C    1 
ATOM   3726 C C    B SER   A 1 167 ? 5.086  -14.471 -1.361  0.14 21.22 ?  167 SER   A C    1 
ATOM   3727 O O    A SER   A 1 167 ? 5.555  -15.313 -1.884  0.86 21.42 ?  167 SER   A O    1 
ATOM   3728 O O    B SER   A 1 167 ? 5.575  -15.102 -2.303  0.14 21.11 ?  167 SER   A O    1 
ATOM   3729 C CB   A SER   A 1 167 ? 4.328  -12.719 -2.323  0.86 21.45 ?  167 SER   A CB   1 
ATOM   3730 C CB   B SER   A 1 167 ? 4.458  -12.419 -2.641  0.14 20.15 ?  167 SER   A CB   1 
ATOM   3731 O OG   A SER   A 1 167 ? 5.427  -11.928 -1.903  0.86 21.70 ?  167 SER   A OG   1 
ATOM   3732 O OG   B SER   A 1 167 ? 5.502  -11.630 -2.099  0.14 20.16 ?  167 SER   A OG   1 
ATOM   3733 H H    A SER   A 1 167 ? 3.956  -12.301 0.153   0.86 23.61 ?  167 SER   A H    1 
ATOM   3734 H H    B SER   A 1 167 ? 4.029  -12.213 -0.113  0.14 23.43 ?  167 SER   A H    1 
ATOM   3735 H HA   A SER   A 1 167 ? 3.173  -14.224 -1.569  0.86 24.42 ?  167 SER   A HA   1 
ATOM   3736 H HA   B SER   A 1 167 ? 3.235  -13.941 -2.039  0.14 24.34 ?  167 SER   A HA   1 
ATOM   3737 H HB2  A SER   A 1 167 ? 4.584  -13.214 -3.117  0.86 25.75 ?  167 SER   A HB2  1 
ATOM   3738 H HB2  B SER   A 1 167 ? 4.786  -12.876 -3.432  0.14 24.18 ?  167 SER   A HB2  1 
ATOM   3739 H HB3  A SER   A 1 167 ? 3.571  -12.140 -2.531  0.86 25.75 ?  167 SER   A HB3  1 
ATOM   3740 H HB3  B SER   A 1 167 ? 3.714  -11.842 -2.879  0.14 24.18 ?  167 SER   A HB3  1 
ATOM   3741 H HG   A SER   A 1 167 ? 5.210  -11.466 -1.232  0.86 26.05 ?  167 SER   A HG   1 
ATOM   3742 H HG   B SER   A 1 167 ? 5.228  -11.221 -1.418  0.14 24.20 ?  167 SER   A HG   1 
ATOM   3743 N N    A PHE   A 1 168 ? 5.496  -14.797 0.301   0.86 19.75 ?  168 PHE   A N    1 
ATOM   3744 N N    B PHE   A 1 168 ? 5.490  -14.636 -0.105  0.14 22.33 ?  168 PHE   A N    1 
ATOM   3745 C CA   A PHE   A 1 168 ? 6.686  -15.587 0.588   0.86 20.29 ?  168 PHE   A CA   1 
ATOM   3746 C CA   B PHE   A 1 168 ? 6.590  -15.530 0.227   0.14 23.55 ?  168 PHE   A CA   1 
ATOM   3747 C C    A PHE   A 1 168 ? 6.384  -17.074 0.488   0.86 22.35 ?  168 PHE   A C    1 
ATOM   3748 C C    B PHE   A 1 168 ? 6.182  -16.983 0.014   0.14 25.79 ?  168 PHE   A C    1 
ATOM   3749 O O    A PHE   A 1 168 ? 5.439  -17.573 1.105   0.86 23.39 ?  168 PHE   A O    1 
ATOM   3750 O O    B PHE   A 1 168 ? 5.050  -17.378 0.307   0.14 25.84 ?  168 PHE   A O    1 
ATOM   3751 C CB   A PHE   A 1 168 ? 7.222  -15.278 1.981   0.86 19.46 ?  168 PHE   A CB   1 
ATOM   3752 C CB   B PHE   A 1 168 ? 6.987  -15.321 1.687   0.14 22.61 ?  168 PHE   A CB   1 
ATOM   3753 C CG   A PHE   A 1 168 ? 8.483  -16.025 2.301   0.86 18.58 ?  168 PHE   A CG   1 
ATOM   3754 C CG   B PHE   A 1 168 ? 8.296  -15.955 2.063   0.14 21.78 ?  168 PHE   A CG   1 
ATOM   3755 C CD1  A PHE   A 1 168 ? 9.670  -15.668 1.692   0.86 18.86 ?  168 PHE   A CD1  1 
ATOM   3756 C CD1  B PHE   A 1 168 ? 9.490  -15.283 1.856   0.14 21.44 ?  168 PHE   A CD1  1 
ATOM   3757 C CD2  A PHE   A 1 168 ? 8.486  -17.104 3.173   0.86 18.04 ?  168 PHE   A CD2  1 
ATOM   3758 C CD2  B PHE   A 1 168 ? 8.333  -17.216 2.635   0.14 21.47 ?  168 PHE   A CD2  1 
ATOM   3759 C CE1  A PHE   A 1 168 ? 10.836 -16.353 1.956   0.86 18.54 ?  168 PHE   A CE1  1 
ATOM   3760 C CE1  B PHE   A 1 168 ? 10.697 -15.860 2.206   0.14 21.25 ?  168 PHE   A CE1  1 
ATOM   3761 C CE2  A PHE   A 1 168 ? 9.660  -17.791 3.446   0.86 18.25 ?  168 PHE   A CE2  1 
ATOM   3762 C CE2  B PHE   A 1 168 ? 9.537  -17.798 2.986   0.14 21.26 ?  168 PHE   A CE2  1 
ATOM   3763 C CZ   A PHE   A 1 168 ? 10.834 -17.413 2.835   0.86 18.38 ?  168 PHE   A CZ   1 
ATOM   3764 C CZ   B PHE   A 1 168 ? 10.721 -17.119 2.772   0.14 21.17 ?  168 PHE   A CZ   1 
ATOM   3765 H H    A PHE   A 1 168 ? 5.130  -14.435 0.990   0.86 23.71 ?  168 PHE   A H    1 
ATOM   3766 H H    B PHE   A 1 168 ? 5.146  -14.235 0.572   0.14 26.80 ?  168 PHE   A H    1 
ATOM   3767 H HA   A PHE   A 1 168 ? 7.378  -15.372 -0.059  0.86 24.35 ?  168 PHE   A HA   1 
ATOM   3768 H HA   B PHE   A 1 168 ? 7.353  -15.332 -0.338  0.14 28.27 ?  168 PHE   A HA   1 
ATOM   3769 H HB2  A PHE   A 1 168 ? 7.417  -14.329 2.042   0.86 23.35 ?  168 PHE   A HB2  1 
ATOM   3770 H HB2  B PHE   A 1 168 ? 7.059  -14.369 1.856   0.14 27.14 ?  168 PHE   A HB2  1 
ATOM   3771 H HB3  A PHE   A 1 168 ? 6.558  -15.525 2.639   0.86 23.35 ?  168 PHE   A HB3  1 
ATOM   3772 H HB3  B PHE   A 1 168 ? 6.299  -15.703 2.254   0.14 27.14 ?  168 PHE   A HB3  1 
ATOM   3773 H HD1  A PHE   A 1 168 ? 9.694  -14.952 1.099   0.86 22.64 ?  168 PHE   A HD1  1 
ATOM   3774 H HD1  B PHE   A 1 168 ? 9.479  -14.435 1.475   0.14 25.74 ?  168 PHE   A HD1  1 
ATOM   3775 H HD2  A PHE   A 1 168 ? 7.698  -17.363 3.586   0.86 21.66 ?  168 PHE   A HD2  1 
ATOM   3776 H HD2  B PHE   A 1 168 ? 7.539  -17.678 2.781   0.14 25.77 ?  168 PHE   A HD2  1 
ATOM   3777 H HE1  A PHE   A 1 168 ? 11.640 -16.097 1.548   0.86 22.26 ?  168 PHE   A HE1  1 
ATOM   3778 H HE1  B PHE   A 1 168 ? 11.493 -15.399 2.061   0.14 25.50 ?  168 PHE   A HE1  1 
ATOM   3779 H HE2  A PHE   A 1 168 ? 9.653  -18.513 4.036   0.86 21.91 ?  168 PHE   A HE2  1 
ATOM   3780 H HE2  B PHE   A 1 168 ? 9.550  -18.646 3.368   0.14 25.52 ?  168 PHE   A HE2  1 
ATOM   3781 H HZ   A PHE   A 1 168 ? 11.627 -17.876 3.014   0.86 22.07 ?  168 PHE   A HZ   1 
ATOM   3782 H HZ   B PHE   A 1 168 ? 11.532 -17.508 3.008   0.14 25.41 ?  168 PHE   A HZ   1 
ATOM   3783 N N    A LEU   A 1 169 ? 7.218  -17.789 -0.263  0.86 26.57 ?  169 LEU   A N    1 
ATOM   3784 N N    B LEU   A 1 169 ? 7.115  -17.779 -0.501  0.14 28.00 ?  169 LEU   A N    1 
ATOM   3785 C CA   A LEU   A 1 169 ? 7.040  -19.221 -0.426  0.86 32.49 ?  169 LEU   A CA   1 
ATOM   3786 C CA   B LEU   A 1 169 ? 6.878  -19.205 -0.709  0.14 30.19 ?  169 LEU   A CA   1 
ATOM   3787 C C    A LEU   A 1 169 ? 7.944  -19.968 0.542   0.86 34.81 ?  169 LEU   A C    1 
ATOM   3788 C C    B LEU   A 1 169 ? 7.458  -19.994 0.459   0.14 30.96 ?  169 LEU   A C    1 
ATOM   3789 O O    A LEU   A 1 169 ? 7.502  -20.387 1.613   0.86 35.54 ?  169 LEU   A O    1 
ATOM   3790 O O    B LEU   A 1 169 ? 6.815  -20.893 1.001   0.14 31.21 ?  169 LEU   A O    1 
ATOM   3791 C CB   A LEU   A 1 169 ? 7.334  -19.643 -1.867  0.86 35.29 ?  169 LEU   A CB   1 
ATOM   3792 C CB   B LEU   A 1 169 ? 7.523  -19.663 -2.022  0.14 31.35 ?  169 LEU   A CB   1 
ATOM   3793 C CG   A LEU   A 1 169 ? 7.016  -21.100 -2.214  0.86 37.34 ?  169 LEU   A CG   1 
ATOM   3794 C CG   B LEU   A 1 169 ? 7.001  -20.903 -2.767  0.14 32.26 ?  169 LEU   A CG   1 
ATOM   3795 C CD1  A LEU   A 1 169 ? 5.608  -21.466 -1.768  0.86 38.16 ?  169 LEU   A CD1  1 
ATOM   3796 C CD1  B LEU   A 1 169 ? 6.020  -21.738 -1.950  0.14 32.58 ?  169 LEU   A CD1  1 
ATOM   3797 C CD2  A LEU   A 1 169 ? 7.182  -21.342 -3.707  0.86 37.92 ?  169 LEU   A CD2  1 
ATOM   3798 C CD2  B LEU   A 1 169 ? 6.375  -20.498 -4.097  0.14 32.56 ?  169 LEU   A CD2  1 
ATOM   3799 O OXT  A LEU   A 1 169 ? 9.133  -20.157 0.281   0.86 35.17 -1 169 LEU   A OXT  1 
ATOM   3800 O OXT  B LEU   A 1 169 ? 8.584  -19.746 0.894   0.14 31.24 -1 169 LEU   A OXT  1 
ATOM   3801 H H    A LEU   A 1 169 ? 7.896  -17.467 -0.686  0.86 31.89 ?  169 LEU   A H    1 
ATOM   3802 H H    B LEU   A 1 169 ? 7.896  -17.513 -0.746  0.14 33.61 ?  169 LEU   A H    1 
ATOM   3803 H HA   A LEU   A 1 169 ? 6.120  -19.444 -0.221  0.86 39.00 ?  169 LEU   A HA   1 
ATOM   3804 H HA   B LEU   A 1 169 ? 5.925  -19.370 -0.744  0.14 36.24 ?  169 LEU   A HA   1 
ATOM   3805 H HB2  A LEU   A 1 169 ? 6.811  -19.085 -2.461  0.86 42.36 ?  169 LEU   A HB2  1 
ATOM   3806 H HB2  B LEU   A 1 169 ? 7.461  -18.925 -2.645  0.14 37.63 ?  169 LEU   A HB2  1 
ATOM   3807 H HB3  A LEU   A 1 169 ? 8.278  -19.506 -2.040  0.86 42.36 ?  169 LEU   A HB3  1 
ATOM   3808 H HB3  B LEU   A 1 169 ? 8.458  -19.836 -1.835  0.14 37.63 ?  169 LEU   A HB3  1 
ATOM   3809 H HG   A LEU   A 1 169 ? 7.638  -21.680 -1.748  0.86 44.82 ?  169 LEU   A HG   1 
ATOM   3810 H HG   B LEU   A 1 169 ? 7.758  -21.471 -2.973  0.14 38.72 ?  169 LEU   A HG   1 
ATOM   3811 H HD11 A LEU   A 1 169 ? 5.349  -22.298 -2.192  0.86 45.79 ?  169 LEU   A HD11 1 
ATOM   3812 H HD11 B LEU   A 1 169 ? 5.779  -22.528 -2.462  0.14 39.10 ?  169 LEU   A HD11 1 
ATOM   3813 H HD12 A LEU   A 1 169 ? 5.599  -21.570 -0.803  0.86 45.79 ?  169 LEU   A HD12 1 
ATOM   3814 H HD12 B LEU   A 1 169 ? 6.446  -22.002 -1.121  0.14 39.10 ?  169 LEU   A HD12 1 
ATOM   3815 H HD13 A LEU   A 1 169 ? 5.000  -20.757 -2.031  0.86 45.79 ?  169 LEU   A HD13 1 
ATOM   3816 H HD13 B LEU   A 1 169 ? 5.227  -21.212 -1.767  0.14 39.10 ?  169 LEU   A HD13 1 
ATOM   3817 H HD21 A LEU   A 1 169 ? 6.982  -22.271 -3.901  0.86 45.51 ?  169 LEU   A HD21 1 
ATOM   3818 H HD21 B LEU   A 1 169 ? 6.050  -21.295 -4.547  0.14 39.08 ?  169 LEU   A HD21 1 
ATOM   3819 H HD22 A LEU   A 1 169 ? 6.569  -20.765 -4.190  0.86 45.51 ?  169 LEU   A HD22 1 
ATOM   3820 H HD22 B LEU   A 1 169 ? 5.639  -19.891 -3.927  0.14 39.08 ?  169 LEU   A HD22 1 
ATOM   3821 H HD23 A LEU   A 1 169 ? 8.095  -21.140 -3.961  0.86 45.51 ?  169 LEU   A HD23 1 
ATOM   3822 H HD23 B LEU   A 1 169 ? 7.048  -20.061 -4.642  0.14 39.08 ?  169 LEU   A HD23 1 
ATOM   3823 N N    A SER   B 1 1   ? 50.663 -9.189  -23.792 0.86 30.02 ?  1   SER   B N    1 
ATOM   3824 N N    B SER   B 1 1   ? 50.731 -9.256  -23.899 0.14 28.72 ?  1   SER   B N    1 
ATOM   3825 C CA   A SER   B 1 1   ? 51.165 -10.242 -22.888 0.86 29.59 ?  1   SER   B CA   1 
ATOM   3826 C CA   B SER   B 1 1   ? 51.172 -10.171 -22.823 0.14 28.69 ?  1   SER   B CA   1 
ATOM   3827 C C    A SER   B 1 1   ? 50.090 -11.285 -22.606 0.86 27.87 ?  1   SER   B C    1 
ATOM   3828 C C    B SER   B 1 1   ? 50.117 -11.237 -22.563 0.14 28.60 ?  1   SER   B C    1 
ATOM   3829 O O    A SER   B 1 1   ? 48.893 -11.102 -22.896 0.86 27.23 ?  1   SER   B O    1 
ATOM   3830 O O    B SER   B 1 1   ? 48.961 -11.097 -22.966 0.14 28.48 ?  1   SER   B O    1 
ATOM   3831 C CB   A SER   B 1 1   ? 51.657 -9.641  -21.573 0.86 31.00 ?  1   SER   B CB   1 
ATOM   3832 C CB   B SER   B 1 1   ? 51.466 -9.391  -21.546 0.14 28.74 ?  1   SER   B CB   1 
ATOM   3833 O OG   A SER   B 1 1   ? 50.575 -9.402  -20.694 0.86 33.12 ?  1   SER   B OG   1 
ATOM   3834 O OG   B SER   B 1 1   ? 50.620 -9.810  -20.491 0.14 28.85 ?  1   SER   B OG   1 
ATOM   3835 H H1   A SER   B 1 1   ? 50.529 -9.540  -24.596 0.86 36.03 ?  1   SER   B H1   1 
ATOM   3836 H H1   B SER   B 1 1   ? 51.322 -8.598  -23.976 0.14 34.47 ?  1   SER   B H1   1 
ATOM   3837 H H2   A SER   B 1 1   ? 49.904 -8.870  -23.468 0.86 36.03 ?  1   SER   B H2   1 
ATOM   3838 H H2   B SER   B 1 1   ? 50.681 -9.708  -24.662 0.14 34.47 ?  1   SER   B H2   1 
ATOM   3839 H H3   A SER   B 1 1   ? 51.269 -8.542  -23.842 0.86 36.03 ?  1   SER   B H3   1 
ATOM   3840 H H3   B SER   B 1 1   ? 49.935 -8.925  -23.690 0.14 34.47 ?  1   SER   B H3   1 
ATOM   3841 H HA   A SER   B 1 1   ? 51.914 -10.678 -23.321 0.86 35.52 ?  1   SER   B HA   1 
ATOM   3842 H HA   B SER   B 1 1   ? 51.984 -10.606 -23.114 0.14 34.44 ?  1   SER   B HA   1 
ATOM   3843 H HB2  A SER   B 1 1   ? 52.268 -10.266 -21.156 0.86 37.21 ?  1   SER   B HB2  1 
ATOM   3844 H HB2  B SER   B 1 1   ? 52.389 -9.546  -21.295 0.14 34.50 ?  1   SER   B HB2  1 
ATOM   3845 H HB3  A SER   B 1 1   ? 52.110 -8.803  -21.755 0.86 37.21 ?  1   SER   B HB3  1 
ATOM   3846 H HB3  B SER   B 1 1   ? 51.323 -8.446  -21.714 0.14 34.50 ?  1   SER   B HB3  1 
ATOM   3847 H HG   A SER   B 1 1   ? 50.833 -8.924  -20.052 0.86 39.76 ?  1   SER   B HG   1 
ATOM   3848 H HG   B SER   B 1 1   ? 50.564 -9.200  -19.918 0.14 34.63 ?  1   SER   B HG   1 
ATOM   3849 N N    A MET   B 1 2   ? 50.541 -12.385 -22.022 0.86 27.39 ?  2   MET   B N    1 
ATOM   3850 N N    B MET   B 1 2   ? 50.525 -12.300 -21.876 0.14 28.52 ?  2   MET   B N    1 
ATOM   3851 C CA   A MET   B 1 2   ? 49.734 -13.581 -21.835 0.86 27.19 ?  2   MET   B CA   1 
ATOM   3852 C CA   B MET   B 1 2   ? 49.714 -13.500 -21.710 0.14 28.31 ?  2   MET   B CA   1 
ATOM   3853 C C    A MET   B 1 2   ? 49.511 -13.774 -20.342 0.86 24.64 ?  2   MET   B C    1 
ATOM   3854 C C    B MET   B 1 2   ? 49.460 -13.722 -20.226 0.14 26.27 ?  2   MET   B C    1 
ATOM   3855 O O    A MET   B 1 2   ? 50.455 -14.071 -19.604 0.86 24.89 ?  2   MET   B O    1 
ATOM   3856 O O    B MET   B 1 2   ? 50.363 -14.138 -19.492 0.14 26.42 ?  2   MET   B O    1 
ATOM   3857 C CB   A MET   B 1 2   ? 50.473 -14.771 -22.434 0.86 31.35 ?  2   MET   B CB   1 
ATOM   3858 C CB   B MET   B 1 2   ? 50.442 -14.691 -22.321 0.14 30.14 ?  2   MET   B CB   1 
ATOM   3859 C CG   A MET   B 1 2   ? 49.629 -16.013 -22.658 0.86 35.21 ?  2   MET   B CG   1 
ATOM   3860 C CG   B MET   B 1 2   ? 49.550 -15.855 -22.720 0.14 31.76 ?  2   MET   B CG   1 
ATOM   3861 S SD   A MET   B 1 2   ? 50.500 -17.212 -23.684 0.86 39.03 ?  2   MET   B SD   1 
ATOM   3862 S SD   B MET   B 1 2   ? 50.448 -17.040 -23.731 0.14 33.15 ?  2   MET   B SD   1 
ATOM   3863 C CE   A MET   B 1 2   ? 51.087 -16.140 -24.986 0.86 39.13 ?  2   MET   B CE   1 
ATOM   3864 C CE   B MET   B 1 2   ? 51.359 -15.925 -24.795 0.14 33.47 ?  2   MET   B CE   1 
ATOM   3865 H H    A MET   B 1 2   ? 51.342 -12.474 -21.715 0.86 32.88 ?  2   MET   B H    1 
ATOM   3866 H H    B MET   B 1 2   ? 51.294 -12.352 -21.496 0.14 34.24 ?  2   MET   B H    1 
ATOM   3867 H HA   A MET   B 1 2   ? 48.884 -13.490 -22.290 0.86 32.64 ?  2   MET   B HA   1 
ATOM   3868 H HA   B MET   B 1 2   ? 48.873 -13.397 -22.180 0.14 33.98 ?  2   MET   B HA   1 
ATOM   3869 H HB2  A MET   B 1 2   ? 50.830 -14.474 -23.280 0.86 37.63 ?  2   MET   B HB2  1 
ATOM   3870 H HB2  B MET   B 1 2   ? 50.895 -14.348 -23.102 0.14 36.18 ?  2   MET   B HB2  1 
ATOM   3871 H HB3  A MET   B 1 2   ? 51.200 -15.030 -21.849 0.86 37.63 ?  2   MET   B HB3  1 
ATOM   3872 H HB3  B MET   B 1 2   ? 51.092 -15.038 -21.695 0.14 36.18 ?  2   MET   B HB3  1 
ATOM   3873 H HG2  A MET   B 1 2   ? 49.433 -16.425 -21.798 0.86 42.26 ?  2   MET   B HG2  1 
ATOM   3874 H HG2  B MET   B 1 2   ? 49.240 -16.310 -21.920 0.14 38.12 ?  2   MET   B HG2  1 
ATOM   3875 H HG3  A MET   B 1 2   ? 48.809 -15.778 -23.115 0.86 42.26 ?  2   MET   B HG3  1 
ATOM   3876 H HG3  B MET   B 1 2   ? 48.797 -15.533 -23.234 0.14 38.12 ?  2   MET   B HG3  1 
ATOM   3877 H HE1  A MET   B 1 2   ? 51.260 -16.673 -25.765 0.86 46.96 ?  2   MET   B HE1  1 
ATOM   3878 H HE1  B MET   B 1 2   ? 51.645 -16.409 -25.569 0.14 40.17 ?  2   MET   B HE1  1 
ATOM   3879 H HE2  A MET   B 1 2   ? 50.396 -15.482 -25.173 0.86 46.96 ?  2   MET   B HE2  1 
ATOM   3880 H HE2  B MET   B 1 2   ? 50.778 -15.188 -25.057 0.14 40.17 ?  2   MET   B HE2  1 
ATOM   3881 H HE3  A MET   B 1 2   ? 51.901 -15.689 -24.698 0.86 46.96 ?  2   MET   B HE3  1 
ATOM   3882 H HE3  B MET   B 1 2   ? 52.130 -15.582 -24.308 0.14 40.17 ?  2   MET   B HE3  1 
ATOM   3883 N N    A VAL   B 1 3   ? 48.272 -13.572 -19.898 0.86 22.09 ?  3   VAL   B N    1 
ATOM   3884 N N    B VAL   B 1 3   ? 48.236 -13.440 -19.789 0.14 24.07 ?  3   VAL   B N    1 
ATOM   3885 C CA   A VAL   B 1 3   ? 47.863 -13.836 -18.526 0.86 21.04 ?  3   VAL   B CA   1 
ATOM   3886 C CA   B VAL   B 1 3   ? 47.806 -13.725 -18.427 0.14 22.02 ?  3   VAL   B CA   1 
ATOM   3887 C C    A VAL   B 1 3   ? 46.629 -14.727 -18.559 0.86 19.39 ?  3   VAL   B C    1 
ATOM   3888 C C    B VAL   B 1 3   ? 46.562 -14.600 -18.480 0.14 19.79 ?  3   VAL   B C    1 
ATOM   3889 O O    A VAL   B 1 3   ? 45.897 -14.783 -19.547 0.86 19.86 ?  3   VAL   B O    1 
ATOM   3890 O O    B VAL   B 1 3   ? 45.757 -14.518 -19.412 0.14 19.60 ?  3   VAL   B O    1 
ATOM   3891 C CB   A VAL   B 1 3   ? 47.589 -12.543 -17.723 0.86 22.58 ?  3   VAL   B CB   1 
ATOM   3892 C CB   B VAL   B 1 3   ? 47.539 -12.445 -17.604 0.14 22.30 ?  3   VAL   B CB   1 
ATOM   3893 C CG1  A VAL   B 1 3   ? 48.857 -11.698 -17.620 0.86 23.27 ?  3   VAL   B CG1  1 
ATOM   3894 C CG1  B VAL   B 1 3   ? 48.803 -11.606 -17.495 0.14 22.45 ?  3   VAL   B CG1  1 
ATOM   3895 C CG2  A VAL   B 1 3   ? 46.450 -11.749 -18.350 0.86 23.35 ?  3   VAL   B CG2  1 
ATOM   3896 C CG2  B VAL   B 1 3   ? 46.402 -11.642 -18.215 0.14 22.41 ?  3   VAL   B CG2  1 
ATOM   3897 H H    A VAL   B 1 3   ? 47.633 -13.277 -20.392 0.86 26.52 ?  3   VAL   B H    1 
ATOM   3898 H H    B VAL   B 1 3   ? 47.632 -13.070 -20.277 0.14 28.90 ?  3   VAL   B H    1 
ATOM   3899 H HA   A VAL   B 1 3   ? 48.566 -14.322 -18.070 0.86 25.26 ?  3   VAL   B HA   1 
ATOM   3900 H HA   B VAL   B 1 3   ? 48.504 -14.224 -17.978 0.14 26.43 ?  3   VAL   B HA   1 
ATOM   3901 H HB   A VAL   B 1 3   ? 47.323 -12.783 -16.821 0.86 27.10 ?  3   VAL   B HB   1 
ATOM   3902 H HB   B VAL   B 1 3   ? 47.274 -12.702 -16.707 0.14 26.77 ?  3   VAL   B HB   1 
ATOM   3903 H HG11 A VAL   B 1 3   ? 48.665 -10.901 -17.103 0.86 27.94 ?  3   VAL   B HG11 1 
ATOM   3904 H HG11 B VAL   B 1 3   ? 48.615 -10.822 -16.956 0.14 26.95 ?  3   VAL   B HG11 1 
ATOM   3905 H HG12 A VAL   B 1 3   ? 49.547 -12.220 -17.181 0.86 27.94 ?  3   VAL   B HG12 1 
ATOM   3906 H HG12 B VAL   B 1 3   ? 49.499 -12.137 -17.076 0.14 26.95 ?  3   VAL   B HG12 1 
ATOM   3907 H HG13 A VAL   B 1 3   ? 49.145 -11.453 -18.513 0.86 27.94 ?  3   VAL   B HG13 1 
ATOM   3908 H HG13 B VAL   B 1 3   ? 49.081 -11.338 -18.385 0.14 26.95 ?  3   VAL   B HG13 1 
ATOM   3909 H HG21 A VAL   B 1 3   ? 46.407 -10.876 -17.930 0.86 28.03 ?  3   VAL   B HG21 1 
ATOM   3910 H HG21 B VAL   B 1 3   ? 46.353 -10.781 -17.774 0.14 26.91 ?  3   VAL   B HG21 1 
ATOM   3911 H HG22 A VAL   B 1 3   ? 46.619 -11.652 -19.299 0.86 28.03 ?  3   VAL   B HG22 1 
ATOM   3912 H HG22 B VAL   B 1 3   ? 46.575 -11.520 -19.161 0.14 26.91 ?  3   VAL   B HG22 1 
ATOM   3913 H HG23 A VAL   B 1 3   ? 45.618 -12.226 -18.208 0.86 28.03 ?  3   VAL   B HG23 1 
ATOM   3914 H HG23 B VAL   B 1 3   ? 45.570 -12.125 -18.090 0.14 26.91 ?  3   VAL   B HG23 1 
ATOM   3915 N N    . ASN   B 1 4   ? 46.410 -15.443 -17.460 1.00 17.98 ?  4   ASN   B N    1 
ATOM   3916 C CA   . ASN   B 1 4   ? 45.273 -16.357 -17.357 1.00 16.88 ?  4   ASN   B CA   1 
ATOM   3917 C C    . ASN   B 1 4   ? 45.219 -17.318 -18.543 1.00 17.25 ?  4   ASN   B C    1 
ATOM   3918 O O    . ASN   B 1 4   ? 44.155 -17.589 -19.095 1.00 17.94 ?  4   ASN   B O    1 
ATOM   3919 C CB   . ASN   B 1 4   ? 43.951 -15.600 -17.197 1.00 16.05 ?  4   ASN   B CB   1 
ATOM   3920 C CG   . ASN   B 1 4   ? 43.907 -14.784 -15.924 1.00 15.28 ?  4   ASN   B CG   1 
ATOM   3921 O OD1  . ASN   B 1 4   ? 44.198 -15.286 -14.847 1.00 15.02 ?  4   ASN   B OD1  1 
ATOM   3922 N ND2  . ASN   B 1 4   ? 43.574 -13.505 -16.050 1.00 16.74 ?  4   ASN   B ND2  1 
ATOM   3923 H H    A ASN   B 1 4   ? 46.913 -15.427 -16.765 0.86 21.59 ?  4   ASN   B H    1 
ATOM   3924 H H    B ASN   B 1 4   ? 46.958 -15.497 -16.802 0.14 21.59 ?  4   ASN   B H    1 
ATOM   3925 H HA   . ASN   B 1 4   ? 45.393 -16.893 -16.559 1.00 20.26 ?  4   ASN   B HA   1 
ATOM   3926 H HB2  . ASN   B 1 4   ? 43.835 -14.998 -17.947 1.00 19.27 ?  4   ASN   B HB2  1 
ATOM   3927 H HB3  . ASN   B 1 4   ? 43.222 -16.242 -17.170 1.00 19.27 ?  4   ASN   B HB3  1 
ATOM   3928 H HD21 . ASN   B 1 4   ? 43.540 -12.997 -15.353 1.00 20.10 ?  4   ASN   B HD21 1 
ATOM   3929 H HD22 . ASN   B 1 4   ? 43.385 -13.179 -16.823 1.00 20.10 ?  4   ASN   B HD22 1 
ATOM   3930 N N    . SER   B 1 5   ? 46.382 -17.831 -18.942 1.00 18.64 ?  5   SER   B N    1 
ATOM   3931 C CA   . SER   B 1 5   ? 46.468 -18.754 -20.074 1.00 21.05 ?  5   SER   B CA   1 
ATOM   3932 C C    . SER   B 1 5   ? 46.454 -20.186 -19.551 1.00 22.23 ?  5   SER   B C    1 
ATOM   3933 O O    . SER   B 1 5   ? 47.463 -20.885 -19.520 1.00 24.04 ?  5   SER   B O    1 
ATOM   3934 C CB   . SER   B 1 5   ? 47.715 -18.468 -20.906 1.00 23.01 ?  5   SER   B CB   1 
ATOM   3935 O OG   . SER   B 1 5   ? 48.890 -18.613 -20.127 1.00 25.78 ?  5   SER   B OG   1 
ATOM   3936 H H    . SER   B 1 5   ? 47.142 -17.661 -18.571 1.00 22.37 ?  5   SER   B H    1 
ATOM   3937 H HA   . SER   B 1 5   ? 45.698 -18.634 -20.646 1.00 25.27 ?  5   SER   B HA   1 
ATOM   3938 H HB2  . SER   B 1 5   ? 47.744 -19.088 -21.655 1.00 27.62 ?  5   SER   B HB2  1 
ATOM   3939 H HB3  . SER   B 1 5   ? 47.657 -17.559 -21.238 1.00 27.62 ?  5   SER   B HB3  1 
ATOM   3940 H HG   . SER   B 1 5   ? 48.960 -19.406 -19.861 1.00 30.94 ?  5   SER   B HG   1 
ATOM   3941 N N    . PHE   B 1 6   ? 45.269 -20.605 -19.124 1.00 22.46 ?  6   PHE   B N    1 
ATOM   3942 C CA   . PHE   B 1 6   ? 45.077 -21.950 -18.606 1.00 21.94 ?  6   PHE   B CA   1 
ATOM   3943 C C    . PHE   B 1 6   ? 45.003 -22.934 -19.764 1.00 25.13 ?  6   PHE   B C    1 
ATOM   3944 O O    . PHE   B 1 6   ? 44.340 -22.673 -20.770 1.00 27.08 ?  6   PHE   B O    1 
ATOM   3945 C CB   . PHE   B 1 6   ? 43.786 -22.007 -17.790 1.00 19.92 ?  6   PHE   B CB   1 
ATOM   3946 C CG   . PHE   B 1 6   ? 43.809 -21.152 -16.555 1.00 17.95 ?  6   PHE   B CG   1 
ATOM   3947 C CD1  . PHE   B 1 6   ? 44.315 -21.649 -15.371 1.00 16.70 ?  6   PHE   B CD1  1 
ATOM   3948 C CD2  . PHE   B 1 6   ? 43.331 -19.847 -16.581 1.00 17.24 ?  6   PHE   B CD2  1 
ATOM   3949 C CE1  . PHE   B 1 6   ? 44.336 -20.871 -14.226 1.00 16.13 ?  6   PHE   B CE1  1 
ATOM   3950 C CE2  . PHE   B 1 6   ? 43.355 -19.059 -15.442 1.00 17.64 ?  6   PHE   B CE2  1 
ATOM   3951 C CZ   . PHE   B 1 6   ? 43.866 -19.564 -14.267 1.00 16.34 ?  6   PHE   B CZ   1 
ATOM   3952 H H    . PHE   B 1 6   ? 44.554 -20.128 -19.132 1.00 26.96 ?  6   PHE   B H    1 
ATOM   3953 H HA   . PHE   B 1 6   ? 45.820 -22.193 -18.032 1.00 26.34 ?  6   PHE   B HA   1 
ATOM   3954 H HB2  . PHE   B 1 6   ? 43.051 -21.704 -18.348 1.00 23.91 ?  6   PHE   B HB2  1 
ATOM   3955 H HB3  . PHE   B 1 6   ? 43.630 -22.923 -17.513 1.00 23.91 ?  6   PHE   B HB3  1 
ATOM   3956 H HD1  . PHE   B 1 6   ? 44.642 -22.518 -15.340 1.00 20.05 ?  6   PHE   B HD1  1 
ATOM   3957 H HD2  . PHE   B 1 6   ? 42.986 -19.502 -17.374 1.00 20.70 ?  6   PHE   B HD2  1 
ATOM   3958 H HE1  . PHE   B 1 6   ? 44.688 -21.211 -13.433 1.00 19.36 ?  6   PHE   B HE1  1 
ATOM   3959 H HE2  . PHE   B 1 6   ? 43.028 -18.186 -15.470 1.00 21.18 ?  6   PHE   B HE2  1 
ATOM   3960 H HZ   . PHE   B 1 6   ? 43.880 -19.042 -13.497 1.00 19.61 ?  6   PHE   B HZ   1 
ATOM   3961 N N    . SER   B 1 7   ? 45.705 -24.060 -19.625 1.00 25.83 ?  7   SER   B N    1 
ATOM   3962 C CA   . SER   B 1 7   ? 45.802 -25.047 -20.691 1.00 28.61 ?  7   SER   B CA   1 
ATOM   3963 C C    . SER   B 1 7   ? 45.727 -26.450 -20.108 1.00 27.64 ?  7   SER   B C    1 
ATOM   3964 O O    . SER   B 1 7   ? 46.298 -26.728 -19.050 1.00 28.43 ?  7   SER   B O    1 
ATOM   3965 C CB   . SER   B 1 7   ? 47.112 -24.882 -21.479 1.00 31.79 ?  7   SER   B CB   1 
ATOM   3966 O OG   . SER   B 1 7   ? 47.152 -25.755 -22.593 1.00 33.83 ?  7   SER   B OG   1 
ATOM   3967 H H    . SER   B 1 7   ? 46.147 -24.274 -18.914 1.00 31.00 ?  7   SER   B H    1 
ATOM   3968 H HA   . SER   B 1 7   ? 45.064 -24.934 -21.304 1.00 34.34 ?  7   SER   B HA   1 
ATOM   3969 H HB2  . SER   B 1 7   ? 47.177 -23.965 -21.796 1.00 38.15 ?  7   SER   B HB2  1 
ATOM   3970 H HB3  . SER   B 1 7   ? 47.862 -25.081 -20.896 1.00 38.15 ?  7   SER   B HB3  1 
ATOM   3971 H HG   . SER   B 1 7   ? 47.873 -25.651 -23.015 1.00 40.60 ?  7   SER   B HG   1 
ATOM   3972 N N    . GLY   B 1 8   ? 45.016 -27.331 -20.808 1.00 27.56 ?  8   GLY   B N    1 
ATOM   3973 C CA   . GLY   B 1 8   ? 44.973 -28.726 -20.438 1.00 26.81 ?  8   GLY   B CA   1 
ATOM   3974 C C    . GLY   B 1 8   ? 44.039 -29.060 -19.304 1.00 25.31 ?  8   GLY   B C    1 
ATOM   3975 O O    . GLY   B 1 8   ? 44.186 -30.126 -18.691 1.00 26.85 ?  8   GLY   B O    1 
ATOM   3976 H H    . GLY   B 1 8   ? 44.552 -27.131 -21.499 1.00 33.08 ?  8   GLY   B H    1 
ATOM   3977 H HA2  . GLY   B 1 8   ? 44.696 -29.244 -21.207 1.00 32.18 ?  8   GLY   B HA2  1 
ATOM   3978 H HA3  . GLY   B 1 8   ? 45.859 -29.014 -20.179 1.00 32.18 ?  8   GLY   B HA3  1 
ATOM   3979 N N    . TYR   B 1 9   ? 43.059 -28.207 -19.019 1.00 23.35 ?  9   TYR   B N    1 
ATOM   3980 C CA   . TYR   B 1 9   ? 42.111 -28.493 -17.956 1.00 21.30 ?  9   TYR   B CA   1 
ATOM   3981 C C    . TYR   B 1 9   ? 40.928 -29.289 -18.476 1.00 21.01 ?  9   TYR   B C    1 
ATOM   3982 O O    . TYR   B 1 9   ? 40.510 -29.148 -19.629 1.00 22.83 ?  9   TYR   B O    1 
ATOM   3983 C CB   . TYR   B 1 9   ? 41.608 -27.209 -17.301 1.00 20.55 ?  9   TYR   B CB   1 
ATOM   3984 C CG   . TYR   B 1 9   ? 42.634 -26.587 -16.383 1.00 19.71 ?  9   TYR   B CG   1 
ATOM   3985 C CD1  . TYR   B 1 9   ? 43.735 -25.921 -16.900 1.00 20.11 ?  9   TYR   B CD1  1 
ATOM   3986 C CD2  . TYR   B 1 9   ? 42.520 -26.687 -15.006 1.00 19.10 ?  9   TYR   B CD2  1 
ATOM   3987 C CE1  . TYR   B 1 9   ? 44.688 -25.361 -16.070 1.00 20.53 ?  9   TYR   B CE1  1 
ATOM   3988 C CE2  . TYR   B 1 9   ? 43.469 -26.134 -14.166 1.00 19.48 ?  9   TYR   B CE2  1 
ATOM   3989 C CZ   . TYR   B 1 9   ? 44.553 -25.465 -14.704 1.00 20.46 ?  9   TYR   B CZ   1 
ATOM   3990 O OH   . TYR   B 1 9   ? 45.506 -24.916 -13.879 1.00 20.84 ?  9   TYR   B OH   1 
ATOM   3991 H H    . TYR   B 1 9   ? 42.902 -27.473 -19.442 1.00 28.03 ?  9   TYR   B H    1 
ATOM   3992 H HA   . TYR   B 1 9   ? 42.542 -29.021 -17.273 1.00 25.57 ?  9   TYR   B HA   1 
ATOM   3993 H HB2  . TYR   B 1 9   ? 41.377 -26.558 -17.984 1.00 24.67 ?  9   TYR   B HB2  1 
ATOM   3994 H HB3  . TYR   B 1 9   ? 40.829 -27.421 -16.767 1.00 24.67 ?  9   TYR   B HB3  1 
ATOM   3995 H HD1  . TYR   B 1 9   ? 43.830 -25.846 -17.822 1.00 24.14 ?  9   TYR   B HD1  1 
ATOM   3996 H HD2  . TYR   B 1 9   ? 41.787 -27.136 -14.639 1.00 22.93 ?  9   TYR   B HD2  1 
ATOM   3997 H HE1  . TYR   B 1 9   ? 45.416 -24.918 -16.433 1.00 24.64 ?  9   TYR   B HE1  1 
ATOM   3998 H HE2  . TYR   B 1 9   ? 43.368 -26.211 -13.243 1.00 23.38 ?  9   TYR   B HE2  1 
ATOM   3999 H HH   . TYR   B 1 9   ? 46.098 -24.550 -14.340 1.00 25.02 ?  9   TYR   B HH   1 
ATOM   4000 N N    . LEU   B 1 10  ? 40.402 -30.140 -17.602 1.00 19.51 ?  10  LEU   B N    1 
ATOM   4001 C CA   . LEU   B 1 10  ? 39.195 -30.898 -17.872 1.00 19.26 ?  10  LEU   B CA   1 
ATOM   4002 C C    . LEU   B 1 10  ? 38.005 -30.132 -17.311 1.00 18.83 ?  10  LEU   B C    1 
ATOM   4003 O O    . LEU   B 1 10  ? 38.019 -29.707 -16.153 1.00 18.48 ?  10  LEU   B O    1 
ATOM   4004 C CB   . LEU   B 1 10  ? 39.304 -32.267 -17.203 1.00 20.23 ?  10  LEU   B CB   1 
ATOM   4005 C CG   . LEU   B 1 10  ? 38.143 -33.211 -17.497 1.00 21.93 ?  10  LEU   B CG   1 
ATOM   4006 C CD1  . LEU   B 1 10  ? 38.215 -33.716 -18.932 1.00 23.11 ?  10  LEU   B CD1  1 
ATOM   4007 C CD2  . LEU   B 1 10  ? 38.122 -34.366 -16.511 1.00 22.99 ?  10  LEU   B CD2  1 
ATOM   4008 H H    . LEU   B 1 10  ? 40.735 -30.300 -16.821 1.00 23.42 ?  10  LEU   B H    1 
ATOM   4009 H HA   . LEU   B 1 10  ? 39.077 -31.023 -18.824 1.00 23.12 ?  10  LEU   B HA   1 
ATOM   4010 H HB2  . LEU   B 1 10  ? 40.117 -32.706 -17.510 1.00 24.28 ?  10  LEU   B HB2  1 
ATOM   4011 H HB3  . LEU   B 1 10  ? 39.346 -32.150 -16.240 1.00 24.28 ?  10  LEU   B HB3  1 
ATOM   4012 H HG   . LEU   B 1 10  ? 37.308 -32.729 -17.396 1.00 26.32 ?  10  LEU   B HG   1 
ATOM   4013 H HD11 . LEU   B 1 10  ? 37.503 -34.359 -19.076 1.00 27.74 ?  10  LEU   B HD11 1 
ATOM   4014 H HD12 . LEU   B 1 10  ? 38.107 -32.963 -19.534 1.00 27.74 ?  10  LEU   B HD12 1 
ATOM   4015 H HD13 . LEU   B 1 10  ? 39.076 -34.136 -19.075 1.00 27.74 ?  10  LEU   B HD13 1 
ATOM   4016 H HD21 . LEU   B 1 10  ? 37.376 -34.948 -16.725 1.00 27.59 ?  10  LEU   B HD21 1 
ATOM   4017 H HD22 . LEU   B 1 10  ? 38.955 -34.852 -16.580 1.00 27.59 ?  10  LEU   B HD22 1 
ATOM   4018 H HD23 . LEU   B 1 10  ? 38.016 -34.008 -15.615 1.00 27.59 ?  10  LEU   B HD23 1 
ATOM   4019 N N    . LYS   B 1 11  ? 36.975 -29.969 -18.130 1.00 20.22 ?  11  LYS   B N    1 
ATOM   4020 C CA   . LYS   B 1 11  ? 35.776 -29.258 -17.715 1.00 22.46 ?  11  LYS   B CA   1 
ATOM   4021 C C    . LYS   B 1 11  ? 34.914 -30.184 -16.864 1.00 21.56 ?  11  LYS   B C    1 
ATOM   4022 O O    . LYS   B 1 11  ? 34.560 -31.285 -17.300 1.00 23.37 ?  11  LYS   B O    1 
ATOM   4023 C CB   . LYS   B 1 11  ? 35.018 -28.807 -18.961 1.00 26.30 ?  11  LYS   B CB   1 
ATOM   4024 C CG   . LYS   B 1 11  ? 33.885 -27.831 -18.710 1.00 29.87 ?  11  LYS   B CG   1 
ATOM   4025 C CD   . LYS   B 1 11  ? 33.142 -27.527 -20.005 1.00 32.74 ?  11  LYS   B CD   1 
ATOM   4026 C CE   . LYS   B 1 11  ? 32.131 -26.408 -19.823 1.00 34.87 ?  11  LYS   B CE   1 
ATOM   4027 N NZ   . LYS   B 1 11  ? 32.794 -25.099 -19.580 1.00 36.01 ?  11  LYS   B NZ   1 
ATOM   4028 H H    . LYS   B 1 11  ? 36.943 -30.270 -18.934 1.00 24.28 ?  11  LYS   B H    1 
ATOM   4029 H HA   . LYS   B 1 11  ? 36.018 -28.480 -17.190 1.00 26.96 ?  11  LYS   B HA   1 
ATOM   4030 H HB2  . LYS   B 1 11  ? 35.646 -28.374 -19.563 1.00 31.57 ?  11  LYS   B HB2  1 
ATOM   4031 H HB3  . LYS   B 1 11  ? 34.640 -29.587 -19.394 1.00 31.57 ?  11  LYS   B HB3  1 
ATOM   4032 H HG2  . LYS   B 1 11  ? 33.258 -28.218 -18.082 1.00 35.85 ?  11  LYS   B HG2  1 
ATOM   4033 H HG3  . LYS   B 1 11  ? 34.245 -27.000 -18.363 1.00 35.85 ?  11  LYS   B HG3  1 
ATOM   4034 H HD2  . LYS   B 1 11  ? 33.779 -27.252 -20.684 1.00 39.29 ?  11  LYS   B HD2  1 
ATOM   4035 H HD3  . LYS   B 1 11  ? 32.667 -28.322 -20.296 1.00 39.29 ?  11  LYS   B HD3  1 
ATOM   4036 H HE2  . LYS   B 1 11  ? 31.590 -26.330 -20.625 1.00 41.85 ?  11  LYS   B HE2  1 
ATOM   4037 H HE3  . LYS   B 1 11  ? 31.568 -26.613 -19.060 1.00 41.85 ?  11  LYS   B HE3  1 
ATOM   4038 H HZ1  . LYS   B 1 11  ? 32.182 -24.458 -19.500 1.00 43.22 ?  11  LYS   B HZ1  1 
ATOM   4039 H HZ2  . LYS   B 1 11  ? 33.275 -25.135 -18.833 1.00 43.22 ?  11  LYS   B HZ2  1 
ATOM   4040 H HZ3  . LYS   B 1 11  ? 33.332 -24.901 -20.262 1.00 43.22 ?  11  LYS   B HZ3  1 
ATOM   4041 N N    . LEU   B 1 12  ? 34.582 -29.748 -15.649 1.00 19.37 ?  12  LEU   B N    1 
ATOM   4042 C CA   . LEU   B 1 12  ? 33.628 -30.455 -14.801 1.00 18.75 ?  12  LEU   B CA   1 
ATOM   4043 C C    . LEU   B 1 12  ? 32.239 -29.842 -14.877 1.00 18.79 ?  12  LEU   B C    1 
ATOM   4044 O O    . LEU   B 1 12  ? 31.251 -30.559 -15.030 1.00 19.35 ?  12  LEU   B O    1 
ATOM   4045 C CB   . LEU   B 1 12  ? 34.100 -30.471 -13.343 1.00 18.01 ?  12  LEU   B CB   1 
ATOM   4046 C CG   . LEU   B 1 12  ? 35.441 -31.150 -13.077 1.00 18.06 ?  12  LEU   B CG   1 
ATOM   4047 C CD1  . LEU   B 1 12  ? 35.780 -31.087 -11.600 1.00 18.65 ?  12  LEU   B CD1  1 
ATOM   4048 C CD2  . LEU   B 1 12  ? 35.428 -32.591 -13.561 1.00 18.47 ?  12  LEU   B CD2  1 
ATOM   4049 H H    . LEU   B 1 12  ? 34.900 -29.035 -15.290 1.00 23.26 ?  12  LEU   B H    1 
ATOM   4050 H HA   . LEU   B 1 12  ? 33.558 -31.374 -15.105 1.00 22.51 ?  12  LEU   B HA   1 
ATOM   4051 H HB2  . LEU   B 1 12  ? 34.170 -29.557 -13.037 1.00 21.62 ?  12  LEU   B HB2  1 
ATOM   4052 H HB3  . LEU   B 1 12  ? 33.430 -30.939 -12.815 1.00 21.62 ?  12  LEU   B HB3  1 
ATOM   4053 H HG   . LEU   B 1 12  ? 36.133 -30.677 -13.565 1.00 21.68 ?  12  LEU   B HG   1 
ATOM   4054 H HD11 . LEU   B 1 12  ? 36.637 -31.520 -11.454 1.00 22.39 ?  12  LEU   B HD11 1 
ATOM   4055 H HD12 . LEU   B 1 12  ? 35.828 -30.159 -11.325 1.00 22.39 ?  12  LEU   B HD12 1 
ATOM   4056 H HD13 . LEU   B 1 12  ? 35.090 -31.547 -11.097 1.00 22.39 ?  12  LEU   B HD13 1 
ATOM   4057 H HD21 . LEU   B 1 12  ? 36.234 -33.033 -13.254 1.00 22.18 ?  12  LEU   B HD21 1 
ATOM   4058 H HD22 . LEU   B 1 12  ? 34.647 -33.037 -13.201 1.00 22.18 ?  12  LEU   B HD22 1 
ATOM   4059 H HD23 . LEU   B 1 12  ? 35.395 -32.598 -14.531 1.00 22.18 ?  12  LEU   B HD23 1 
ATOM   4060 N N    . THR   B 1 13  ? 32.153 -28.524 -14.765 1.00 18.83 ?  13  THR   B N    1 
ATOM   4061 C CA   . THR   B 1 13  ? 30.925 -27.775 -14.963 1.00 18.77 ?  13  THR   B CA   1 
ATOM   4062 C C    . THR   B 1 13  ? 31.258 -26.580 -15.847 1.00 21.08 ?  13  THR   B C    1 
ATOM   4063 O O    . THR   B 1 13  ? 32.401 -26.394 -16.276 1.00 21.84 ?  13  THR   B O    1 
ATOM   4064 C CB   . THR   B 1 13  ? 30.339 -27.306 -13.627 1.00 18.34 ?  13  THR   B CB   1 
ATOM   4065 O OG1  . THR   B 1 13  ? 31.182 -26.284 -13.079 1.00 18.05 ?  13  THR   B OG1  1 
ATOM   4066 C CG2  . THR   B 1 13  ? 30.229 -28.464 -12.637 1.00 19.06 ?  13  THR   B CG2  1 
ATOM   4067 H H    . THR   B 1 13  ? 32.824 -28.024 -14.564 1.00 22.61 ?  13  THR   B H    1 
ATOM   4068 H HA   . THR   B 1 13  ? 30.270 -28.333 -15.408 1.00 22.53 ?  13  THR   B HA   1 
ATOM   4069 H HB   . THR   B 1 13  ? 29.447 -26.948 -13.777 1.00 22.02 ?  13  THR   B HB   1 
ATOM   4070 H HG1  . THR   B 1 13  ? 30.887 -25.525 -13.299 1.00 21.66 ?  13  THR   B HG1  1 
ATOM   4071 H HG21 . THR   B 1 13  ? 29.716 -28.188 -11.860 1.00 22.88 ?  13  THR   B HG21 1 
ATOM   4072 H HG22 . THR   B 1 13  ? 29.783 -29.217 -13.055 1.00 22.88 ?  13  THR   B HG22 1 
ATOM   4073 H HG23 . THR   B 1 13  ? 31.113 -28.740 -12.350 1.00 22.88 ?  13  THR   B HG23 1 
ATOM   4074 N N    A ASP   B 1 14  ? 30.245 -25.758 -16.117 0.86 22.65 ?  14  ASP   B N    1 
ATOM   4075 N N    B ASP   B 1 14  ? 30.248 -25.747 -16.107 0.14 21.88 ?  14  ASP   B N    1 
ATOM   4076 C CA   A ASP   B 1 14  ? 30.456 -24.598 -16.975 0.86 24.37 ?  14  ASP   B CA   1 
ATOM   4077 C CA   B ASP   B 1 14  ? 30.447 -24.596 -16.980 0.14 22.57 ?  14  ASP   B CA   1 
ATOM   4078 C C    A ASP   B 1 14  ? 31.557 -23.687 -16.447 0.86 22.20 ?  14  ASP   B C    1 
ATOM   4079 C C    B ASP   B 1 14  ? 31.468 -23.610 -16.428 0.14 20.88 ?  14  ASP   B C    1 
ATOM   4080 O O    A ASP   B 1 14  ? 32.209 -22.989 -17.233 0.86 23.87 ?  14  ASP   B O    1 
ATOM   4081 O O    B ASP   B 1 14  ? 31.964 -22.768 -17.185 0.14 21.04 ?  14  ASP   B O    1 
ATOM   4082 C CB   A ASP   B 1 14  ? 29.152 -23.816 -17.132 0.86 28.07 ?  14  ASP   B CB   1 
ATOM   4083 C CB   B ASP   B 1 14  ? 29.121 -23.872 -17.218 0.14 24.76 ?  14  ASP   B CB   1 
ATOM   4084 C CG   A ASP   B 1 14  ? 28.183 -24.479 -18.088 0.86 31.89 ?  14  ASP   B CG   1 
ATOM   4085 C CG   B ASP   B 1 14  ? 28.212 -24.620 -18.176 0.14 26.61 ?  14  ASP   B CG   1 
ATOM   4086 O OD1  A ASP   B 1 14  ? 28.604 -25.369 -18.859 0.86 33.25 ?  14  ASP   B OD1  1 
ATOM   4087 O OD1  B ASP   B 1 14  ? 28.733 -25.306 -19.080 0.14 27.29 ?  14  ASP   B OD1  1 
ATOM   4088 O OD2  A ASP   B 1 14  ? 26.991 -24.108 -18.069 0.86 33.57 -1 14  ASP   B OD2  1 
ATOM   4089 O OD2  B ASP   B 1 14  ? 26.976 -24.524 -18.024 0.14 27.25 -1 14  ASP   B OD2  1 
ATOM   4090 H H    A ASP   B 1 14  ? 29.445 -25.844 -15.814 0.86 27.18 ?  14  ASP   B H    1 
ATOM   4091 H H    B ASP   B 1 14  ? 29.452 -25.825 -15.792 0.14 26.27 ?  14  ASP   B H    1 
ATOM   4092 H HA   A ASP   B 1 14  ? 30.726 -24.905 -17.854 0.86 29.25 ?  14  ASP   B HA   1 
ATOM   4093 H HA   B ASP   B 1 14  ? 30.771 -24.910 -17.837 0.14 27.09 ?  14  ASP   B HA   1 
ATOM   4094 H HB2  A ASP   B 1 14  ? 28.712 -23.754 -16.270 0.86 33.70 ?  14  ASP   B HB2  1 
ATOM   4095 H HB2  B ASP   B 1 14  ? 28.654 -23.783 -16.373 0.14 29.72 ?  14  ASP   B HB2  1 
ATOM   4096 H HB3  A ASP   B 1 14  ? 29.354 -22.928 -17.467 0.86 33.70 ?  14  ASP   B HB3  1 
ATOM   4097 H HB3  B ASP   B 1 14  ? 29.308 -22.991 -17.586 0.14 29.72 ?  14  ASP   B HB3  1 
ATOM   4098 N N    . ASN   B 1 15  ? 31.783 -23.679 -15.132 1.00 19.15 ?  15  ASN   B N    1 
ATOM   4099 C CA   . ASN   B 1 15  ? 32.741 -22.755 -14.535 1.00 16.71 ?  15  ASN   B CA   1 
ATOM   4100 C C    . ASN   B 1 15  ? 33.832 -23.403 -13.698 1.00 15.41 ?  15  ASN   B C    1 
ATOM   4101 O O    . ASN   B 1 15  ? 34.684 -22.674 -13.187 1.00 15.43 ?  15  ASN   B O    1 
ATOM   4102 C CB   . ASN   B 1 15  ? 32.024 -21.699 -13.680 1.00 16.43 ?  15  ASN   B CB   1 
ATOM   4103 C CG   . ASN   B 1 15  ? 31.407 -22.293 -12.433 1.00 16.44 ?  15  ASN   B CG   1 
ATOM   4104 O OD1  . ASN   B 1 15  ? 30.472 -23.102 -12.510 1.00 18.17 ?  15  ASN   B OD1  1 
ATOM   4105 N ND2  . ASN   B 1 15  ? 31.923 -21.917 -11.279 1.00 15.51 ?  15  ASN   B ND2  1 
ATOM   4106 H H    A ASN   B 1 15  ? 31.384 -24.193 -14.567 0.86 22.99 ?  15  ASN   B H    1 
ATOM   4107 H H    B ASN   B 1 15  ? 31.435 -24.238 -14.577 0.14 22.99 ?  15  ASN   B H    1 
ATOM   4108 H HA   . ASN   B 1 15  ? 33.186 -22.277 -15.244 1.00 20.06 ?  15  ASN   B HA   1 
ATOM   4109 H HB2  . ASN   B 1 15  ? 32.668 -21.019 -13.410 1.00 19.73 ?  15  ASN   B HB2  1 
ATOM   4110 H HB3  . ASN   B 1 15  ? 31.316 -21.287 -14.203 1.00 19.73 ?  15  ASN   B HB3  1 
ATOM   4111 H HD21 . ASN   B 1 15  ? 31.607 -22.224 -10.540 1.00 18.62 ?  15  ASN   B HD21 1 
ATOM   4112 H HD22 . ASN   B 1 15  ? 32.586 -21.359 -11.255 1.00 18.62 ?  15  ASN   B HD22 1 
ATOM   4113 N N    . VAL   B 1 16  ? 33.843 -24.722 -13.535 1.00 15.07 ?  16  VAL   B N    1 
ATOM   4114 C CA   . VAL   B 1 16  ? 34.849 -25.409 -12.729 1.00 14.52 ?  16  VAL   B CA   1 
ATOM   4115 C C    . VAL   B 1 16  ? 35.635 -26.344 -13.633 1.00 14.86 ?  16  VAL   B C    1 
ATOM   4116 O O    . VAL   B 1 16  ? 35.051 -27.222 -14.290 1.00 16.18 ?  16  VAL   B O    1 
ATOM   4117 C CB   . VAL   B 1 16  ? 34.228 -26.179 -11.552 1.00 14.98 ?  16  VAL   B CB   1 
ATOM   4118 C CG1  . VAL   B 1 16  ? 35.318 -26.902 -10.750 1.00 15.26 ?  16  VAL   B CG1  1 
ATOM   4119 C CG2  . VAL   B 1 16  ? 33.416 -25.241 -10.660 1.00 15.65 ?  16  VAL   B CG2  1 
ATOM   4120 H H    . VAL   B 1 16  ? 33.260 -25.254 -13.883 1.00 18.09 ?  16  VAL   B H    1 
ATOM   4121 H HA   . VAL   B 1 16  ? 35.465 -24.756 -12.362 1.00 17.43 ?  16  VAL   B HA   1 
ATOM   4122 H HB   . VAL   B 1 16  ? 33.625 -26.854 -11.899 1.00 17.98 ?  16  VAL   B HB   1 
ATOM   4123 H HG11 . VAL   B 1 16  ? 34.938 -27.213 -9.912  1.00 18.32 ?  16  VAL   B HG11 1 
ATOM   4124 H HG12 . VAL   B 1 16  ? 35.646 -27.655 -11.263 1.00 18.32 ?  16  VAL   B HG12 1 
ATOM   4125 H HG13 . VAL   B 1 16  ? 36.041 -26.280 -10.570 1.00 18.32 ?  16  VAL   B HG13 1 
ATOM   4126 H HG21 . VAL   B 1 16  ? 33.083 -25.739 -9.896  1.00 18.79 ?  16  VAL   B HG21 1 
ATOM   4127 H HG22 . VAL   B 1 16  ? 33.986 -24.518 -10.360 1.00 18.79 ?  16  VAL   B HG22 1 
ATOM   4128 H HG23 . VAL   B 1 16  ? 32.672 -24.887 -11.173 1.00 18.79 ?  16  VAL   B HG23 1 
ATOM   4129 N N    . TYR   B 1 17  ? 36.957 -26.176 -13.629 1.00 15.31 ?  17  TYR   B N    1 
ATOM   4130 C CA   . TYR   B 1 17  ? 37.895 -26.937 -14.437 1.00 15.54 ?  17  TYR   B CA   1 
ATOM   4131 C C    . TYR   B 1 17  ? 38.948 -27.543 -13.519 1.00 14.88 ?  17  TYR   B C    1 
ATOM   4132 O O    . TYR   B 1 17  ? 39.229 -27.011 -12.440 1.00 15.17 ?  17  TYR   B O    1 
ATOM   4133 C CB   . TYR   B 1 17  ? 38.595 -26.022 -15.449 1.00 18.77 ?  17  TYR   B CB   1 
ATOM   4134 C CG   . TYR   B 1 17  ? 37.662 -25.242 -16.345 1.00 22.86 ?  17  TYR   B CG   1 
ATOM   4135 C CD1  . TYR   B 1 17  ? 37.100 -24.041 -15.928 1.00 24.45 ?  17  TYR   B CD1  1 
ATOM   4136 C CD2  . TYR   B 1 17  ? 37.344 -25.706 -17.613 1.00 25.13 ?  17  TYR   B CD2  1 
ATOM   4137 C CE1  . TYR   B 1 17  ? 36.246 -23.326 -16.751 1.00 26.30 ?  17  TYR   B CE1  1 
ATOM   4138 C CE2  . TYR   B 1 17  ? 36.494 -25.001 -18.441 1.00 26.73 ?  17  TYR   B CE2  1 
ATOM   4139 C CZ   . TYR   B 1 17  ? 35.947 -23.814 -18.005 1.00 27.45 ?  17  TYR   B CZ   1 
ATOM   4140 O OH   . TYR   B 1 17  ? 35.102 -23.111 -18.830 1.00 28.72 ?  17  TYR   B OH   1 
ATOM   4141 H H    . TYR   B 1 17  ? 37.356 -25.586 -13.139 1.00 18.38 ?  17  TYR   B H    1 
ATOM   4142 H HA   . TYR   B 1 17  ? 37.427 -27.646 -14.913 1.00 18.65 ?  17  TYR   B HA   1 
ATOM   4143 H HB2  . TYR   B 1 17  ? 39.149 -25.390 -14.969 1.00 22.54 ?  17  TYR   B HB2  1 
ATOM   4144 H HB3  . TYR   B 1 17  ? 39.144 -26.573 -16.023 1.00 22.54 ?  17  TYR   B HB3  1 
ATOM   4145 H HD1  . TYR   B 1 17  ? 37.300 -23.712 -15.083 1.00 29.35 ?  17  TYR   B HD1  1 
ATOM   4146 H HD2  . TYR   B 1 17  ? 37.706 -26.509 -17.913 1.00 30.16 ?  17  TYR   B HD2  1 
ATOM   4147 H HE1  . TYR   B 1 17  ? 35.875 -22.524 -16.459 1.00 31.56 ?  17  TYR   B HE1  1 
ATOM   4148 H HE2  . TYR   B 1 17  ? 36.286 -25.327 -19.289 1.00 32.08 ?  17  TYR   B HE2  1 
ATOM   4149 H HH   . TYR   B 1 17  ? 35.002 -23.515 -19.561 1.00 34.47 ?  17  TYR   B HH   1 
ATOM   4150 N N    . ILE   B 1 18  ? 39.553 -28.650 -13.952 1.00 14.70 ?  18  ILE   B N    1 
ATOM   4151 C CA   . ILE   B 1 18  ? 40.482 -29.370 -13.089 1.00 14.81 ?  18  ILE   B CA   1 
ATOM   4152 C C    . ILE   B 1 18  ? 41.639 -29.922 -13.910 1.00 15.19 ?  18  ILE   B C    1 
ATOM   4153 O O    . ILE   B 1 18  ? 41.477 -30.307 -15.072 1.00 16.45 ?  18  ILE   B O    1 
ATOM   4154 C CB   . ILE   B 1 18  ? 39.733 -30.470 -12.297 1.00 15.42 ?  18  ILE   B CB   1 
ATOM   4155 C CG1  . ILE   B 1 18  ? 40.590 -31.022 -11.156 1.00 15.98 ?  18  ILE   B CG1  1 
ATOM   4156 C CG2  . ILE   B 1 18  ? 39.236 -31.583 -13.228 1.00 15.68 ?  18  ILE   B CG2  1 
ATOM   4157 C CD1  . ILE   B 1 18  ? 39.781 -31.840 -10.156 1.00 17.55 ?  18  ILE   B CD1  1 
ATOM   4158 H H    . ILE   B 1 18  ? 39.441 -29.001 -14.731 1.00 17.64 ?  18  ILE   B H    1 
ATOM   4159 H HA   . ILE   B 1 18  ? 40.844 -28.751 -12.440 1.00 17.78 ?  18  ILE   B HA   1 
ATOM   4160 H HB   . ILE   B 1 18  ? 38.948 -30.067 -11.894 1.00 18.51 ?  18  ILE   B HB   1 
ATOM   4161 H HG12 . ILE   B 1 18  ? 41.279 -31.592 -11.524 1.00 19.19 ?  18  ILE   B HG12 1 
ATOM   4162 H HG13 . ILE   B 1 18  ? 40.990 -30.277 -10.678 1.00 19.19 ?  18  ILE   B HG13 1 
ATOM   4163 H HG21 . ILE   B 1 18  ? 38.638 -32.166 -12.735 1.00 18.82 ?  18  ILE   B HG21 1 
ATOM   4164 H HG22 . ILE   B 1 18  ? 38.764 -31.178 -13.972 1.00 18.82 ?  18  ILE   B HG22 1 
ATOM   4165 H HG23 . ILE   B 1 18  ? 39.998 -32.087 -13.553 1.00 18.82 ?  18  ILE   B HG23 1 
ATOM   4166 H HD11 . ILE   B 1 18  ? 40.362 -32.119 -9.430  1.00 21.06 ?  18  ILE   B HD11 1 
ATOM   4167 H HD12 . ILE   B 1 18  ? 39.057 -31.295 -9.807  1.00 21.06 ?  18  ILE   B HD12 1 
ATOM   4168 H HD13 . ILE   B 1 18  ? 39.417 -32.621 -10.604 1.00 21.06 ?  18  ILE   B HD13 1 
ATOM   4169 N N    . LYS   B 1 19  ? 42.819 -29.957 -13.290 1.00 15.63 ?  19  LYS   B N    1 
ATOM   4170 C CA   . LYS   B 1 19  ? 44.033 -30.430 -13.942 1.00 16.50 ?  19  LYS   B CA   1 
ATOM   4171 C C    . LYS   B 1 19  ? 44.927 -31.112 -12.918 1.00 16.37 ?  19  LYS   B C    1 
ATOM   4172 O O    . LYS   B 1 19  ? 45.011 -30.683 -11.766 1.00 15.89 ?  19  LYS   B O    1 
ATOM   4173 C CB   . LYS   B 1 19  ? 44.811 -29.267 -14.575 1.00 17.87 ?  19  LYS   B CB   1 
ATOM   4174 C CG   . LYS   B 1 19  ? 46.015 -29.683 -15.399 1.00 19.78 ?  19  LYS   B CG   1 
ATOM   4175 C CD   . LYS   B 1 19  ? 46.753 -28.456 -15.917 1.00 21.81 ?  19  LYS   B CD   1 
ATOM   4176 C CE   . LYS   B 1 19  ? 47.889 -28.827 -16.849 1.00 23.99 ?  19  LYS   B CE   1 
ATOM   4177 N NZ   . LYS   B 1 19  ? 48.638 -27.631 -17.316 1.00 25.17 ?  19  LYS   B NZ   1 
ATOM   4178 H H    . LYS   B 1 19  ? 42.932 -29.705 -12.474 1.00 18.77 ?  19  LYS   B H    1 
ATOM   4179 H HA   . LYS   B 1 19  ? 43.794 -31.067 -14.636 1.00 19.81 ?  19  LYS   B HA   1 
ATOM   4180 H HB2  . LYS   B 1 19  ? 44.209 -28.778 -15.159 1.00 21.45 ?  19  LYS   B HB2  1 
ATOM   4181 H HB3  . LYS   B 1 19  ? 45.119 -28.682 -13.863 1.00 21.45 ?  19  LYS   B HB3  1 
ATOM   4182 H HG2  . LYS   B 1 19  ? 46.619 -30.201 -14.846 1.00 23.74 ?  19  LYS   B HG2  1 
ATOM   4183 H HG3  . LYS   B 1 19  ? 45.713 -30.210 -16.158 1.00 23.74 ?  19  LYS   B HG3  1 
ATOM   4184 H HD2  . LYS   B 1 19  ? 46.130 -27.893 -16.404 1.00 26.18 ?  19  LYS   B HD2  1 
ATOM   4185 H HD3  . LYS   B 1 19  ? 47.123 -27.969 -15.164 1.00 26.18 ?  19  LYS   B HD3  1 
ATOM   4186 H HE2  . LYS   B 1 19  ? 48.506 -29.411 -16.381 1.00 28.79 ?  19  LYS   B HE2  1 
ATOM   4187 H HE3  . LYS   B 1 19  ? 47.525 -29.283 -17.627 1.00 28.79 ?  19  LYS   B HE3  1 
ATOM   4188 H HZ1  . LYS   B 1 19  ? 49.251 -27.871 -17.916 1.00 30.21 ?  19  LYS   B HZ1  1 
ATOM   4189 H HZ2  . LYS   B 1 19  ? 48.079 -27.050 -17.693 1.00 30.21 ?  19  LYS   B HZ2  1 
ATOM   4190 H HZ3  . LYS   B 1 19  ? 49.044 -27.239 -16.629 1.00 30.21 ?  19  LYS   B HZ3  1 
ATOM   4191 N N    . ASN   B 1 20  ? 45.601 -32.173 -13.349 1.00 17.52 ?  20  ASN   B N    1 
ATOM   4192 C CA   . ASN   B 1 20  ? 46.630 -32.807 -12.529 1.00 18.73 ?  20  ASN   B CA   1 
ATOM   4193 C C    . ASN   B 1 20  ? 47.909 -31.996 -12.709 1.00 19.09 ?  20  ASN   B C    1 
ATOM   4194 O O    . ASN   B 1 20  ? 48.574 -32.089 -13.746 1.00 21.32 ?  20  ASN   B O    1 
ATOM   4195 C CB   . ASN   B 1 20  ? 46.804 -34.263 -12.957 1.00 20.16 ?  20  ASN   B CB   1 
ATOM   4196 C CG   . ASN   B 1 20  ? 47.969 -34.955 -12.275 1.00 21.93 ?  20  ASN   B CG   1 
ATOM   4197 O OD1  . ASN   B 1 20  ? 48.644 -35.789 -12.885 1.00 24.29 ?  20  ASN   B OD1  1 
ATOM   4198 N ND2  . ASN   B 1 20  ? 48.200 -34.639 -11.009 1.00 21.68 ?  20  ASN   B ND2  1 
ATOM   4199 H H    . ASN   B 1 20  ? 45.476 -32.548 -14.113 1.00 21.04 ?  20  ASN   B H    1 
ATOM   4200 H HA   . ASN   B 1 20  ? 46.351 -32.787 -11.596 1.00 22.48 ?  20  ASN   B HA   1 
ATOM   4201 H HB2  . ASN   B 1 20  ? 45.996 -34.758 -12.737 1.00 24.20 ?  20  ASN   B HB2  1 
ATOM   4202 H HB3  . ASN   B 1 20  ? 46.955 -34.289 -13.913 1.00 24.20 ?  20  ASN   B HB3  1 
ATOM   4203 H HD21 . ASN   B 1 20  ? 48.854 -34.999 -10.586 1.00 26.03 ?  20  ASN   B HD21 1 
ATOM   4204 H HD22 . ASN   B 1 20  ? 47.701 -34.057 -10.608 1.00 26.03 ?  20  ASN   B HD22 1 
ATOM   4205 N N    . ALA   B 1 21  ? 48.251 -31.183 -11.707 1.00 18.53 ?  21  ALA   B N    1 
ATOM   4206 C CA   . ALA   B 1 21  ? 49.373 -30.273 -11.858 1.00 19.34 ?  21  ALA   B CA   1 
ATOM   4207 C C    . ALA   B 1 21  ? 49.823 -29.762 -10.500 1.00 18.43 ?  21  ALA   B C    1 
ATOM   4208 O O    . ALA   B 1 21  ? 49.073 -29.779 -9.519  1.00 18.50 ?  21  ALA   B O    1 
ATOM   4209 C CB   . ALA   B 1 21  ? 49.002 -29.112 -12.777 1.00 20.81 ?  21  ALA   B CB   1 
ATOM   4210 H H    . ALA   B 1 21  ? 47.845 -31.144 -10.941 1.00 22.25 ?  21  ALA   B H    1 
ATOM   4211 H HA   . ALA   B 1 21  ? 50.108 -30.760 -12.257 1.00 23.22 ?  21  ALA   B HA   1 
ATOM   4212 H HB1  . ALA   B 1 21  ? 49.800 -28.593 -12.939 1.00 24.98 ?  21  ALA   B HB1  1 
ATOM   4213 H HB2  . ALA   B 1 21  ? 48.665 -29.475 -13.610 1.00 24.98 ?  21  ALA   B HB2  1 
ATOM   4214 H HB3  . ALA   B 1 21  ? 48.323 -28.576 -12.347 1.00 24.98 ?  21  ALA   B HB3  1 
ATOM   4215 N N    . ASP   B 1 22  ? 51.080 -29.322 -10.476 1.00 17.54 ?  22  ASP   B N    1 
ATOM   4216 C CA   . ASP   B 1 22  ? 51.692 -28.629 -9.348  1.00 17.23 ?  22  ASP   B CA   1 
ATOM   4217 C C    . ASP   B 1 22  ? 51.286 -27.158 -9.434  1.00 15.85 ?  22  ASP   B C    1 
ATOM   4218 O O    . ASP   B 1 22  ? 51.602 -26.483 -10.419 1.00 16.12 ?  22  ASP   B O    1 
ATOM   4219 C CB   . ASP   B 1 22  ? 53.210 -28.810 -9.488  1.00 18.84 ?  22  ASP   B CB   1 
ATOM   4220 C CG   . ASP   B 1 22  ? 54.027 -28.051 -8.452  1.00 20.81 ?  22  ASP   B CG   1 
ATOM   4221 O OD1  . ASP   B 1 22  ? 53.650 -26.942 -8.041  1.00 21.27 ?  22  ASP   B OD1  1 
ATOM   4222 O OD2  . ASP   B 1 22  ? 55.109 -28.559 -8.079  1.00 23.36 -1 22  ASP   B OD2  1 
ATOM   4223 H H    . ASP   B 1 22  ? 51.624 -29.417 -11.141 1.00 21.06 ?  22  ASP   B H    1 
ATOM   4224 H HA   . ASP   B 1 22  ? 51.392 -29.012 -8.507  1.00 20.69 ?  22  ASP   B HA   1 
ATOM   4225 H HB2  . ASP   B 1 22  ? 53.426 -29.748 -9.407  1.00 22.62 ?  22  ASP   B HB2  1 
ATOM   4226 H HB3  . ASP   B 1 22  ? 53.483 -28.478 -10.357 1.00 22.62 ?  22  ASP   B HB3  1 
ATOM   4227 N N    . ILE   B 1 23  ? 50.572 -26.665 -8.415  1.00 15.16 ?  23  ILE   B N    1 
ATOM   4228 C CA   . ILE   B 1 23  ? 49.991 -25.320 -8.479  1.00 14.40 ?  23  ILE   B CA   1 
ATOM   4229 C C    . ILE   B 1 23  ? 51.051 -24.236 -8.623  1.00 14.05 ?  23  ILE   B C    1 
ATOM   4230 O O    . ILE   B 1 23  ? 50.790 -23.195 -9.234  1.00 13.60 ?  23  ILE   B O    1 
ATOM   4231 C CB   . ILE   B 1 23  ? 49.064 -25.066 -7.275  1.00 14.62 ?  23  ILE   B CB   1 
ATOM   4232 C CG1  . ILE   B 1 23  ? 48.237 -23.798 -7.486  1.00 15.27 ?  23  ILE   B CG1  1 
ATOM   4233 C CG2  . ILE   B 1 23  ? 49.850 -25.033 -5.977  1.00 15.86 ?  23  ILE   B CG2  1 
ATOM   4234 C CD1  . ILE   B 1 23  ? 47.103 -23.648 -6.495  1.00 15.80 ?  23  ILE   B CD1  1 
ATOM   4235 H H    . ILE   B 1 23  ? 50.414 -27.089 -7.686  1.00 18.20 ?  23  ILE   B H    1 
ATOM   4236 H HA   . ILE   B 1 23  ? 49.439 -25.278 -9.273  1.00 17.29 ?  23  ILE   B HA   1 
ATOM   4237 H HB   . ILE   B 1 23  ? 48.443 -25.812 -7.226  1.00 17.56 ?  23  ILE   B HB   1 
ATOM   4238 H HG12 . ILE   B 1 23  ? 48.821 -23.027 -7.394  1.00 18.33 ?  23  ILE   B HG12 1 
ATOM   4239 H HG13 . ILE   B 1 23  ? 47.858 -23.815 -8.381  1.00 18.33 ?  23  ILE   B HG13 1 
ATOM   4240 H HG21 . ILE   B 1 23  ? 49.230 -25.017 -5.234  1.00 19.04 ?  23  ILE   B HG21 1 
ATOM   4241 H HG22 . ILE   B 1 23  ? 50.408 -25.826 -5.926  1.00 19.04 ?  23  ILE   B HG22 1 
ATOM   4242 H HG23 . ILE   B 1 23  ? 50.406 -24.239 -5.965  1.00 19.04 ?  23  ILE   B HG23 1 
ATOM   4243 H HD11 . ILE   B 1 23  ? 46.591 -22.859 -6.723  1.00 18.97 ?  23  ILE   B HD11 1 
ATOM   4244 H HD12 . ILE   B 1 23  ? 46.538 -24.437 -6.549  1.00 18.97 ?  23  ILE   B HD12 1 
ATOM   4245 H HD13 . ILE   B 1 23  ? 47.473 -23.565 -5.606  1.00 18.97 ?  23  ILE   B HD13 1 
ATOM   4246 N N    . VAL   B 1 24  ? 52.242 -24.440 -8.056  1.00 14.40 ?  24  VAL   B N    1 
ATOM   4247 C CA   . VAL   B 1 24  ? 53.320 -23.466 -8.228  1.00 14.88 ?  24  VAL   B CA   1 
ATOM   4248 C C    . VAL   B 1 24  ? 53.765 -23.420 -9.683  1.00 14.99 ?  24  VAL   B C    1 
ATOM   4249 O O    . VAL   B 1 24  ? 53.907 -22.342 -10.276 1.00 15.57 ?  24  VAL   B O    1 
ATOM   4250 C CB   . VAL   B 1 24  ? 54.500 -23.792 -7.291  1.00 15.89 ?  24  VAL   B CB   1 
ATOM   4251 C CG1  . VAL   B 1 24  ? 55.710 -22.912 -7.616  1.00 16.83 ?  24  VAL   B CG1  1 
ATOM   4252 C CG2  . VAL   B 1 24  ? 54.090 -23.619 -5.848  1.00 16.81 ?  24  VAL   B CG2  1 
ATOM   4253 H H    . VAL   B 1 24  ? 52.450 -25.121 -7.578  1.00 17.29 ?  24  VAL   B H    1 
ATOM   4254 H HA   . VAL   B 1 24  ? 52.993 -22.587 -7.992  1.00 17.87 ?  24  VAL   B HA   1 
ATOM   4255 H HB   . VAL   B 1 24  ? 54.763 -24.719 -7.417  1.00 19.08 ?  24  VAL   B HB   1 
ATOM   4256 H HG11 . VAL   B 1 24  ? 56.302 -22.897 -6.848  1.00 20.21 ?  24  VAL   B HG11 1 
ATOM   4257 H HG12 . VAL   B 1 24  ? 56.172 -23.286 -8.381  1.00 20.21 ?  24  VAL   B HG12 1 
ATOM   4258 H HG13 . VAL   B 1 24  ? 55.401 -22.015 -7.813  1.00 20.21 ?  24  VAL   B HG13 1 
ATOM   4259 H HG21 . VAL   B 1 24  ? 54.821 -23.898 -5.274  1.00 20.19 ?  24  VAL   B HG21 1 
ATOM   4260 H HG22 . VAL   B 1 24  ? 53.885 -22.684 -5.690  1.00 20.19 ?  24  VAL   B HG22 1 
ATOM   4261 H HG23 . VAL   B 1 24  ? 53.307 -24.165 -5.673  1.00 20.19 ?  24  VAL   B HG23 1 
ATOM   4262 N N    . GLU   B 1 25  ? 54.025 -24.591 -10.271 1.00 16.30 ?  25  GLU   B N    1 
ATOM   4263 C CA   . GLU   B 1 25  ? 54.422 -24.628 -11.673 1.00 18.36 ?  25  GLU   B CA   1 
ATOM   4264 C C    . GLU   B 1 25  ? 53.314 -24.090 -12.562 1.00 16.81 ?  25  GLU   B C    1 
ATOM   4265 O O    . GLU   B 1 25  ? 53.583 -23.389 -13.545 1.00 17.61 ?  25  GLU   B O    1 
ATOM   4266 C CB   . GLU   B 1 25  ? 54.822 -26.050 -12.067 1.00 23.34 ?  25  GLU   B CB   1 
ATOM   4267 C CG   . GLU   B 1 25  ? 56.127 -26.487 -11.416 1.00 29.26 ?  25  GLU   B CG   1 
ATOM   4268 C CD   . GLU   B 1 25  ? 57.233 -25.446 -11.521 1.00 34.56 ?  25  GLU   B CD   1 
ATOM   4269 O OE1  . GLU   B 1 25  ? 57.616 -25.088 -12.655 1.00 36.45 ?  25  GLU   B OE1  1 
ATOM   4270 O OE2  . GLU   B 1 25  ? 57.708 -24.969 -10.465 1.00 36.18 -1 25  GLU   B OE2  1 
ATOM   4271 H H    . GLU   B 1 25  ? 53.969 -25.360 -9.890  1.00 19.57 ?  25  GLU   B H    1 
ATOM   4272 H HA   . GLU   B 1 25  ? 55.176 -24.041 -11.798 1.00 22.04 ?  25  GLU   B HA   1 
ATOM   4273 H HB2  . GLU   B 1 25  ? 54.125 -26.667 -11.784 1.00 28.02 ?  25  GLU   B HB2  1 
ATOM   4274 H HB3  . GLU   B 1 25  ? 54.930 -26.096 -13.030 1.00 28.02 ?  25  GLU   B HB3  1 
ATOM   4275 H HG2  . GLU   B 1 25  ? 55.975 -26.635 -10.475 1.00 35.12 ?  25  GLU   B HG2  1 
ATOM   4276 H HG3  . GLU   B 1 25  ? 56.435 -27.298 -11.845 1.00 35.12 ?  25  GLU   B HG3  1 
ATOM   4277 N N    A GLU   B 1 26  ? 52.061 -24.398 -12.226 0.86 15.62 ?  26  GLU   B N    1 
ATOM   4278 N N    B GLU   B 1 26  ? 52.058 -24.400 -12.229 0.14 16.31 ?  26  GLU   B N    1 
ATOM   4279 C CA   A GLU   B 1 26  ? 50.936 -23.866 -12.986 0.86 16.29 ?  26  GLU   B CA   1 
ATOM   4280 C CA   B GLU   B 1 26  ? 50.934 -23.862 -12.989 0.14 16.17 ?  26  GLU   B CA   1 
ATOM   4281 C C    A GLU   B 1 26  ? 50.893 -22.347 -12.908 0.86 14.97 ?  26  GLU   B C    1 
ATOM   4282 C C    B GLU   B 1 26  ? 50.901 -22.344 -12.911 0.14 15.09 ?  26  GLU   B C    1 
ATOM   4283 O O    A GLU   B 1 26  ? 50.690 -21.671 -13.920 0.86 16.50 ?  26  GLU   B O    1 
ATOM   4284 O O    B GLU   B 1 26  ? 50.735 -21.661 -13.928 0.14 15.38 ?  26  GLU   B O    1 
ATOM   4285 C CB   A GLU   B 1 26  ? 49.623 -24.450 -12.461 0.86 18.39 ?  26  GLU   B CB   1 
ATOM   4286 C CB   B GLU   B 1 26  ? 49.619 -24.444 -12.470 0.14 17.15 ?  26  GLU   B CB   1 
ATOM   4287 C CG   A GLU   B 1 26  ? 49.158 -25.712 -13.163 0.86 21.96 ?  26  GLU   B CG   1 
ATOM   4288 C CG   B GLU   B 1 26  ? 49.232 -25.760 -13.109 0.14 18.32 ?  26  GLU   B CG   1 
ATOM   4289 C CD   A GLU   B 1 26  ? 48.895 -25.508 -14.658 0.86 23.35 ?  26  GLU   B CD   1 
ATOM   4290 C CD   B GLU   B 1 26  ? 49.002 -25.663 -14.605 0.14 19.01 ?  26  GLU   B CD   1 
ATOM   4291 O OE1  A GLU   B 1 26  ? 47.884 -24.880 -15.044 0.86 23.61 ?  26  GLU   B OE1  1 
ATOM   4292 O OE1  B GLU   B 1 26  ? 48.196 -24.813 -15.036 0.14 19.17 ?  26  GLU   B OE1  1 
ATOM   4293 O OE2  A GLU   B 1 26  ? 49.708 -25.997 -15.453 0.86 25.38 -1 26  GLU   B OE2  1 
ATOM   4294 O OE2  B GLU   B 1 26  ? 49.626 -26.448 -15.348 0.14 19.34 -1 26  GLU   B OE2  1 
ATOM   4295 H H    A GLU   B 1 26  ? 51.835 -24.909 -11.568 0.86 18.75 ?  26  GLU   B H    1 
ATOM   4296 H H    B GLU   B 1 26  ? 51.833 -24.912 -11.573 0.14 19.58 ?  26  GLU   B H    1 
ATOM   4297 H HA   A GLU   B 1 26  ? 51.031 -24.120 -13.915 0.86 19.56 ?  26  GLU   B HA   1 
ATOM   4298 H HA   B GLU   B 1 26  ? 51.031 -24.112 -13.919 0.14 19.41 ?  26  GLU   B HA   1 
ATOM   4299 H HB2  A GLU   B 1 26  ? 49.728 -24.663 -11.519 0.86 22.07 ?  26  GLU   B HB2  1 
ATOM   4300 H HB2  B GLU   B 1 26  ? 49.700 -24.598 -11.512 0.14 20.59 ?  26  GLU   B HB2  1 
ATOM   4301 H HB3  A GLU   B 1 26  ? 48.922 -23.786 -12.564 0.86 22.07 ?  26  GLU   B HB3  1 
ATOM   4302 H HB3  B GLU   B 1 26  ? 48.904 -23.810 -12.636 0.14 20.59 ?  26  GLU   B HB3  1 
ATOM   4303 H HG2  A GLU   B 1 26  ? 49.842 -26.390 -13.065 0.86 26.36 ?  26  GLU   B HG2  1 
ATOM   4304 H HG2  B GLU   B 1 26  ? 49.946 -26.390 -12.966 0.14 22.00 ?  26  GLU   B HG2  1 
ATOM   4305 H HG3  A GLU   B 1 26  ? 48.330 -26.015 -12.753 0.86 26.36 ?  26  GLU   B HG3  1 
ATOM   4306 H HG3  B GLU   B 1 26  ? 48.410 -26.072 -12.706 0.14 22.00 ?  26  GLU   B HG3  1 
ATOM   4307 N N    . ALA   B 1 27  ? 51.046 -21.797 -11.703 1.00 14.24 ?  27  ALA   B N    1 
ATOM   4308 C CA   . ALA   B 1 27  ? 51.012 -20.348 -11.552 1.00 14.71 ?  27  ALA   B CA   1 
ATOM   4309 C C    . ALA   B 1 27  ? 52.089 -19.689 -12.402 1.00 15.67 ?  27  ALA   B C    1 
ATOM   4310 O O    . ALA   B 1 27  ? 51.836 -18.679 -13.072 1.00 16.41 ?  27  ALA   B O    1 
ATOM   4311 C CB   . ALA   B 1 27  ? 51.157 -19.973 -10.080 1.00 15.08 ?  27  ALA   B CB   1 
ATOM   4312 H H    A ALA   B 1 27  ? 51.165 -22.235 -10.970 0.86 17.10 ?  27  ALA   B H    1 
ATOM   4313 H H    B ALA   B 1 27  ? 51.165 -22.236 -10.971 0.14 17.10 ?  27  ALA   B H    1 
ATOM   4314 H HA   . ALA   B 1 27  ? 50.157 -20.020 -11.856 1.00 17.65 ?  27  ALA   B HA   1 
ATOM   4315 H HB1  . ALA   B 1 27  ? 51.129 -19.008 -9.994  1.00 18.10 ?  27  ALA   B HB1  1 
ATOM   4316 H HB2  . ALA   B 1 27  ? 50.421 -20.369 -9.580  1.00 18.10 ?  27  ALA   B HB2  1 
ATOM   4317 H HB3  . ALA   B 1 27  ? 52.001 -20.313 -9.744  1.00 18.10 ?  27  ALA   B HB3  1 
ATOM   4318 N N    . LYS   B 1 28  ? 53.298 -20.255 -12.409 1.00 17.27 ?  28  LYS   B N    1 
ATOM   4319 C CA   . LYS   B 1 28  ? 54.371 -19.636 -13.176 1.00 19.65 ?  28  LYS   B CA   1 
ATOM   4320 C C    . LYS   B 1 28  ? 54.110 -19.708 -14.673 1.00 20.82 ?  28  LYS   B C    1 
ATOM   4321 O O    . LYS   B 1 28  ? 54.538 -18.815 -15.415 1.00 21.60 ?  28  LYS   B O    1 
ATOM   4322 C CB   . LYS   B 1 28  ? 55.727 -20.239 -12.801 1.00 22.28 ?  28  LYS   B CB   1 
ATOM   4323 C CG   . LYS   B 1 28  ? 56.138 -19.913 -11.370 1.00 25.33 ?  28  LYS   B CG   1 
ATOM   4324 C CD   . LYS   B 1 28  ? 57.575 -20.304 -11.050 1.00 29.56 ?  28  LYS   B CD   1 
ATOM   4325 C CE   . LYS   B 1 28  ? 57.674 -21.732 -10.565 1.00 32.58 ?  28  LYS   B CE   1 
ATOM   4326 N NZ   . LYS   B 1 28  ? 59.027 -22.036 -10.013 1.00 34.27 ?  28  LYS   B NZ   1 
ATOM   4327 H H    . LYS   B 1 28  ? 53.519 -20.975 -11.993 1.00 20.73 ?  28  LYS   B H    1 
ATOM   4328 H HA   . LYS   B 1 28  ? 54.408 -18.695 -12.951 1.00 23.59 ?  28  LYS   B HA   1 
ATOM   4329 H HB2  . LYS   B 1 28  ? 55.685 -21.202 -12.888 1.00 26.75 ?  28  LYS   B HB2  1 
ATOM   4330 H HB3  . LYS   B 1 28  ? 56.411 -19.883 -13.396 1.00 26.75 ?  28  LYS   B HB3  1 
ATOM   4331 H HG2  . LYS   B 1 28  ? 56.050 -18.955 -11.232 1.00 30.40 ?  28  LYS   B HG2  1 
ATOM   4332 H HG3  . LYS   B 1 28  ? 55.554 -20.389 -10.764 1.00 30.40 ?  28  LYS   B HG3  1 
ATOM   4333 H HD2  . LYS   B 1 28  ? 58.115 -20.213 -11.851 1.00 35.48 ?  28  LYS   B HD2  1 
ATOM   4334 H HD3  . LYS   B 1 28  ? 57.912 -19.719 -10.352 1.00 35.48 ?  28  LYS   B HD3  1 
ATOM   4335 H HE2  . LYS   B 1 28  ? 57.020 -21.877 -9.863  1.00 39.11 ?  28  LYS   B HE2  1 
ATOM   4336 H HE3  . LYS   B 1 28  ? 57.506 -22.335 -11.307 1.00 39.11 ?  28  LYS   B HE3  1 
ATOM   4337 H HZ1  . LYS   B 1 28  ? 59.060 -22.881 -9.734  1.00 41.13 ?  28  LYS   B HZ1  1 
ATOM   4338 H HZ2  . LYS   B 1 28  ? 59.646 -21.914 -10.640 1.00 41.13 ?  28  LYS   B HZ2  1 
ATOM   4339 H HZ3  . LYS   B 1 28  ? 59.202 -21.499 -9.324  1.00 41.13 ?  28  LYS   B HZ3  1 
ATOM   4340 N N    A LYS   B 1 29  ? 53.403 -20.738 -15.134 0.86 21.76 ?  29  LYS   B N    1 
ATOM   4341 N N    B LYS   B 1 29  ? 53.389 -20.733 -15.132 0.14 22.19 ?  29  LYS   B N    1 
ATOM   4342 C CA   A LYS   B 1 29  ? 53.112 -20.870 -16.556 0.86 24.35 ?  29  LYS   B CA   1 
ATOM   4343 C CA   B LYS   B 1 29  ? 53.108 -20.872 -16.557 0.14 23.84 ?  29  LYS   B CA   1 
ATOM   4344 C C    A LYS   B 1 29  ? 51.854 -20.113 -16.970 0.86 23.29 ?  29  LYS   B C    1 
ATOM   4345 C C    B LYS   B 1 29  ? 51.843 -20.133 -16.982 0.14 22.80 ?  29  LYS   B C    1 
ATOM   4346 O O    A LYS   B 1 29  ? 51.836 -19.488 -18.036 0.86 24.53 ?  29  LYS   B O    1 
ATOM   4347 O O    B LYS   B 1 29  ? 51.808 -19.538 -18.064 0.14 23.12 ?  29  LYS   B O    1 
ATOM   4348 C CB   A LYS   B 1 29  ? 52.980 -22.348 -16.930 0.86 28.58 ?  29  LYS   B CB   1 
ATOM   4349 C CB   B LYS   B 1 29  ? 52.997 -22.353 -16.930 0.14 26.62 ?  29  LYS   B CB   1 
ATOM   4350 C CG   A LYS   B 1 29  ? 52.809 -22.603 -18.417 0.86 32.53 ?  29  LYS   B CG   1 
ATOM   4351 C CG   B LYS   B 1 29  ? 52.846 -22.611 -18.422 0.14 29.17 ?  29  LYS   B CG   1 
ATOM   4352 C CD   A LYS   B 1 29  ? 53.050 -24.067 -18.758 0.86 35.62 ?  29  LYS   B CD   1 
ATOM   4353 C CD   B LYS   B 1 29  ? 53.071 -24.080 -18.750 0.14 31.19 ?  29  LYS   B CD   1 
ATOM   4354 C CE   A LYS   B 1 29  ? 51.984 -24.972 -18.162 0.86 37.79 ?  29  LYS   B CE   1 
ATOM   4355 C CE   B LYS   B 1 29  ? 52.051 -24.976 -18.062 0.14 32.59 ?  29  LYS   B CE   1 
ATOM   4356 N NZ   A LYS   B 1 29  ? 52.223 -26.404 -18.504 0.86 38.97 ?  29  LYS   B NZ   1 
ATOM   4357 N NZ   B LYS   B 1 29  ? 52.290 -26.415 -18.361 0.14 33.33 ?  29  LYS   B NZ   1 
ATOM   4358 H H    A LYS   B 1 29  ? 53.074 -21.366 -14.640 0.86 26.12 ?  29  LYS   B H    1 
ATOM   4359 H H    B LYS   B 1 29  ? 53.054 -21.361 -14.638 0.14 26.64 ?  29  LYS   B H    1 
ATOM   4360 H HA   A LYS   B 1 29  ? 53.853 -20.505 -17.056 0.86 29.23 ?  29  LYS   B HA   1 
ATOM   4361 H HA   B LYS   B 1 29  ? 53.849 -20.502 -17.054 0.14 28.62 ?  29  LYS   B HA   1 
ATOM   4362 H HB2  A LYS   B 1 29  ? 53.784 -22.811 -16.646 0.86 34.30 ?  29  LYS   B HB2  1 
ATOM   4363 H HB2  B LYS   B 1 29  ? 53.798 -22.812 -16.633 0.14 31.96 ?  29  LYS   B HB2  1 
ATOM   4364 H HB3  A LYS   B 1 29  ? 52.210 -22.718 -16.478 0.86 34.30 ?  29  LYS   B HB3  1 
ATOM   4365 H HB3  B LYS   B 1 29  ? 52.220 -22.726 -16.487 0.14 31.96 ?  29  LYS   B HB3  1 
ATOM   4366 H HG2  A LYS   B 1 29  ? 51.903 -22.374 -18.678 0.86 39.04 ?  29  LYS   B HG2  1 
ATOM   4367 H HG2  B LYS   B 1 29  ? 51.948 -22.370 -18.702 0.14 35.01 ?  29  LYS   B HG2  1 
ATOM   4368 H HG3  A LYS   B 1 29  ? 53.448 -22.065 -18.912 0.86 39.04 ?  29  LYS   B HG3  1 
ATOM   4369 H HG3  B LYS   B 1 29  ? 53.502 -22.085 -18.908 0.14 35.01 ?  29  LYS   B HG3  1 
ATOM   4370 H HD2  A LYS   B 1 29  ? 53.037 -24.178 -19.721 0.86 42.75 ?  29  LYS   B HD2  1 
ATOM   4371 H HD2  B LYS   B 1 29  ? 52.992 -24.210 -19.708 0.14 37.43 ?  29  LYS   B HD2  1 
ATOM   4372 H HD3  A LYS   B 1 29  ? 53.911 -24.340 -18.401 0.86 42.75 ?  29  LYS   B HD3  1 
ATOM   4373 H HD3  B LYS   B 1 29  ? 53.956 -24.342 -18.449 0.14 37.43 ?  29  LYS   B HD3  1 
ATOM   4374 H HE2  A LYS   B 1 29  ? 51.992 -24.888 -17.195 0.86 45.35 ?  29  LYS   B HE2  1 
ATOM   4375 H HE2  B LYS   B 1 29  ? 52.111 -24.858 -17.101 0.14 39.12 ?  29  LYS   B HE2  1 
ATOM   4376 H HE3  A LYS   B 1 29  ? 51.115 -24.717 -18.512 0.86 45.35 ?  29  LYS   B HE3  1 
ATOM   4377 H HE3  B LYS   B 1 29  ? 51.162 -24.743 -18.373 0.14 39.12 ?  29  LYS   B HE3  1 
ATOM   4378 H HZ1  A LYS   B 1 29  ? 51.587 -26.913 -18.145 0.86 46.77 ?  29  LYS   B HZ1  1 
ATOM   4379 H HZ1  B LYS   B 1 29  ? 51.681 -26.916 -17.948 0.14 40.00 ?  29  LYS   B HZ1  1 
ATOM   4380 H HZ2  A LYS   B 1 29  ? 52.215 -26.510 -19.388 0.86 46.77 ?  29  LYS   B HZ2  1 
ATOM   4381 H HZ2  B LYS   B 1 29  ? 52.235 -26.557 -19.238 0.14 40.00 ?  29  LYS   B HZ2  1 
ATOM   4382 H HZ3  A LYS   B 1 29  ? 53.014 -26.664 -18.189 0.86 46.77 ?  29  LYS   B HZ3  1 
ATOM   4383 H HZ3  B LYS   B 1 29  ? 53.100 -26.653 -18.080 0.14 40.00 ?  29  LYS   B HZ3  1 
ATOM   4384 N N    . VAL   B 1 30  ? 50.801 -20.161 -16.150 1.00 21.55 ?  30  VAL   B N    1 
ATOM   4385 C CA   . VAL   B 1 30  ? 49.523 -19.540 -16.512 1.00 21.06 ?  30  VAL   B CA   1 
ATOM   4386 C C    . VAL   B 1 30  ? 49.546 -18.026 -16.351 1.00 20.03 ?  30  VAL   B C    1 
ATOM   4387 O O    . VAL   B 1 30  ? 48.808 -17.306 -17.042 1.00 21.00 ?  30  VAL   B O    1 
ATOM   4388 C CB   . VAL   B 1 30  ? 48.407 -20.155 -15.644 1.00 21.54 ?  30  VAL   B CB   1 
ATOM   4389 C CG1  . VAL   B 1 30  ? 47.129 -19.337 -15.735 1.00 21.55 ?  30  VAL   B CG1  1 
ATOM   4390 C CG2  . VAL   B 1 30  ? 48.158 -21.601 -16.046 1.00 22.33 ?  30  VAL   B CG2  1 
ATOM   4391 H H    A VAL   B 1 30  ? 50.792 -20.568 -15.387 0.86 25.87 ?  30  VAL   B H    1 
ATOM   4392 H H    B VAL   B 1 30  ? 50.801 -20.544 -15.375 0.14 25.87 ?  30  VAL   B H    1 
ATOM   4393 H HA   . VAL   B 1 30  ? 49.325 -19.754 -17.435 1.00 25.28 ?  30  VAL   B HA   1 
ATOM   4394 H HB   . VAL   B 1 30  ? 48.689 -20.160 -14.715 1.00 25.85 ?  30  VAL   B HB   1 
ATOM   4395 H HG11 . VAL   B 1 30  ? 46.378 -19.913 -15.519 1.00 25.87 ?  30  VAL   B HG11 1 
ATOM   4396 H HG12 . VAL   B 1 30  ? 47.174 -18.607 -15.102 1.00 25.87 ?  30  VAL   B HG12 1 
ATOM   4397 H HG13 . VAL   B 1 30  ? 47.029 -19.005 -16.636 1.00 25.87 ?  30  VAL   B HG13 1 
ATOM   4398 H HG21 . VAL   B 1 30  ? 47.457 -21.975 -15.483 1.00 26.81 ?  30  VAL   B HG21 1 
ATOM   4399 H HG22 . VAL   B 1 30  ? 47.877 -21.629 -16.975 1.00 26.81 ?  30  VAL   B HG22 1 
ATOM   4400 H HG23 . VAL   B 1 30  ? 48.974 -22.110 -15.932 1.00 26.81 ?  30  VAL   B HG23 1 
ATOM   4401 N N    . LYS   B 1 31  ? 50.339 -17.531 -15.411 1.00 19.56 ?  31  LYS   B N    1 
ATOM   4402 C CA   . LYS   B 1 31  ? 50.351 -16.122 -15.042 1.00 20.14 ?  31  LYS   B CA   1 
ATOM   4403 C C    . LYS   B 1 31  ? 48.946 -15.645 -14.664 1.00 17.99 ?  31  LYS   B C    1 
ATOM   4404 O O    . LYS   B 1 31  ? 48.405 -14.727 -15.288 1.00 18.73 ?  31  LYS   B O    1 
ATOM   4405 C CB   . LYS   B 1 31  ? 50.961 -15.272 -16.148 1.00 23.75 ?  31  LYS   B CB   1 
ATOM   4406 C CG   . LYS   B 1 31  ? 52.389 -15.707 -16.490 1.00 27.78 ?  31  LYS   B CG   1 
ATOM   4407 C CD   . LYS   B 1 31  ? 52.948 -14.939 -17.669 1.00 31.39 ?  31  LYS   B CD   1 
ATOM   4408 C CE   . LYS   B 1 31  ? 54.430 -15.204 -17.832 1.00 33.85 ?  31  LYS   B CE   1 
ATOM   4409 N NZ   . LYS   B 1 31  ? 55.189 -14.789 -16.621 1.00 34.97 ?  31  LYS   B NZ   1 
ATOM   4410 H H    . LYS   B 1 31  ? 50.890 -18.010 -14.958 1.00 23.48 ?  31  LYS   B H    1 
ATOM   4411 H HA   . LYS   B 1 31  ? 50.904 -16.024 -14.264 1.00 24.17 ?  31  LYS   B HA   1 
ATOM   4412 H HB2  . LYS   B 1 31  ? 50.423 -15.352 -16.953 1.00 28.51 ?  31  LYS   B HB2  1 
ATOM   4413 H HB3  . LYS   B 1 31  ? 50.990 -14.349 -15.857 1.00 28.51 ?  31  LYS   B HB3  1 
ATOM   4414 H HG2  . LYS   B 1 31  ? 52.956 -15.550 -15.719 1.00 33.34 ?  31  LYS   B HG2  1 
ATOM   4415 H HG3  . LYS   B 1 31  ? 52.390 -16.653 -16.716 1.00 33.34 ?  31  LYS   B HG3  1 
ATOM   4416 H HD2  . LYS   B 1 31  ? 52.491 -15.222 -18.477 1.00 37.68 ?  31  LYS   B HD2  1 
ATOM   4417 H HD3  . LYS   B 1 31  ? 52.817 -13.991 -17.520 1.00 37.68 ?  31  LYS   B HD3  1 
ATOM   4418 H HE2  . LYS   B 1 31  ? 54.573 -16.154 -17.970 1.00 40.62 ?  31  LYS   B HE2  1 
ATOM   4419 H HE3  . LYS   B 1 31  ? 54.763 -14.700 -18.589 1.00 40.62 ?  31  LYS   B HE3  1 
ATOM   4420 H HZ1  . LYS   B 1 31  ? 56.062 -14.813 -16.788 1.00 41.97 ?  31  LYS   B HZ1  1 
ATOM   4421 H HZ2  . LYS   B 1 31  ? 54.960 -13.960 -16.390 1.00 41.97 ?  31  LYS   B HZ2  1 
ATOM   4422 H HZ3  . LYS   B 1 31  ? 55.008 -15.338 -15.944 1.00 41.97 ?  31  LYS   B HZ3  1 
ATOM   4423 N N    . PRO   B 1 32  ? 48.331 -16.255 -13.644 1.00 15.52 ?  32  PRO   B N    1 
ATOM   4424 C CA   . PRO   B 1 32  ? 46.950 -15.903 -13.290 1.00 14.54 ?  32  PRO   B CA   1 
ATOM   4425 C C    . PRO   B 1 32  ? 46.870 -14.556 -12.595 1.00 14.41 ?  32  PRO   B C    1 
ATOM   4426 O O    . PRO   B 1 32  ? 47.801 -14.128 -11.907 1.00 15.71 ?  32  PRO   B O    1 
ATOM   4427 C CB   . PRO   B 1 32  ? 46.555 -17.017 -12.318 1.00 14.97 ?  32  PRO   B CB   1 
ATOM   4428 C CG   . PRO   B 1 32  ? 47.859 -17.349 -11.638 1.00 15.47 ?  32  PRO   B CG   1 
ATOM   4429 C CD   . PRO   B 1 32  ? 48.906 -17.238 -12.706 1.00 15.52 ?  32  PRO   B CD   1 
ATOM   4430 H HA   . PRO   B 1 32  ? 46.371 -15.915 -14.070 1.00 17.46 ?  32  PRO   B HA   1 
ATOM   4431 H HB2  . PRO   B 1 32  ? 45.902 -16.689 -11.678 1.00 17.97 ?  32  PRO   B HB2  1 
ATOM   4432 H HB3  . PRO   B 1 32  ? 46.213 -17.781 -12.806 1.00 17.97 ?  32  PRO   B HB3  1 
ATOM   4433 H HG2  . PRO   B 1 32  ? 48.027 -16.712 -10.922 1.00 18.57 ?  32  PRO   B HG2  1 
ATOM   4434 H HG3  . PRO   B 1 32  ? 47.825 -18.253 -11.285 1.00 18.57 ?  32  PRO   B HG3  1 
ATOM   4435 H HD2  . PRO   B 1 32  ? 49.735 -16.901 -12.328 1.00 18.64 ?  32  PRO   B HD2  1 
ATOM   4436 H HD3  . PRO   B 1 32  ? 49.030 -18.088 -13.145 1.00 18.64 ?  32  PRO   B HD3  1 
ATOM   4437 N N    . THR   B 1 33  ? 45.721 -13.897 -12.758 1.00 14.17 ?  33  THR   B N    1 
ATOM   4438 C CA   . THR   B 1 33  ? 45.430 -12.720 -11.950 1.00 14.42 ?  33  THR   B CA   1 
ATOM   4439 C C    . THR   B 1 33  ? 45.382 -13.074 -10.471 1.00 14.17 ?  33  THR   B C    1 
ATOM   4440 O O    . THR   B 1 33  ? 45.859 -12.300 -9.626  1.00 14.95 ?  33  THR   B O    1 
ATOM   4441 C CB   . THR   B 1 33  ? 44.112 -12.083 -12.399 1.00 15.14 ?  33  THR   B CB   1 
ATOM   4442 O OG1  . THR   B 1 33  ? 44.162 -11.819 -13.800 1.00 15.39 ?  33  THR   B OG1  1 
ATOM   4443 C CG2  . THR   B 1 33  ? 43.862 -10.785 -11.655 1.00 16.38 ?  33  THR   B CG2  1 
ATOM   4444 H H    . THR   B 1 33  ? 45.101 -14.115 -13.315 1.00 17.02 ?  33  THR   B H    1 
ATOM   4445 H HA   . THR   B 1 33  ? 46.132 -12.069 -12.078 1.00 17.31 ?  33  THR   B HA   1 
ATOM   4446 H HB   . THR   B 1 33  ? 43.375 -12.690 -12.211 1.00 18.18 ?  33  THR   B HB   1 
ATOM   4447 H HG1  . THR   B 1 33  ? 43.440 -11.458 -14.057 1.00 18.47 ?  33  THR   B HG1  1 
ATOM   4448 H HG21 . THR   B 1 33  ? 43.112 -10.315 -12.047 1.00 19.67 ?  33  THR   B HG21 1 
ATOM   4449 H HG22 . THR   B 1 33  ? 43.671 -10.965 -10.722 1.00 19.67 ?  33  THR   B HG22 1 
ATOM   4450 H HG23 . THR   B 1 33  ? 44.651 -10.218 -11.711 1.00 19.67 ?  33  THR   B HG23 1 
ATOM   4451 N N    . VAL   B 1 34  ? 44.826 -14.241 -10.138 1.00 13.05 ?  34  VAL   B N    1 
ATOM   4452 C CA   . VAL   B 1 34  ? 44.638 -14.641 -8.749  1.00 12.67 ?  34  VAL   B CA   1 
ATOM   4453 C C    . VAL   B 1 34  ? 45.068 -16.089 -8.591  1.00 11.82 ?  34  VAL   B C    1 
ATOM   4454 O O    . VAL   B 1 34  ? 44.547 -16.975 -9.278  1.00 12.63 ?  34  VAL   B O    1 
ATOM   4455 C CB   . VAL   B 1 34  ? 43.168 -14.504 -8.301  1.00 13.97 ?  34  VAL   B CB   1 
ATOM   4456 C CG1  . VAL   B 1 34  ? 43.006 -14.952 -6.856  1.00 14.59 ?  34  VAL   B CG1  1 
ATOM   4457 C CG2  . VAL   B 1 34  ? 42.667 -13.082 -8.494  1.00 14.84 ?  34  VAL   B CG2  1 
ATOM   4458 H H    . VAL   B 1 34  ? 44.557 -14.832 -10.704 1.00 15.67 ?  34  VAL   B H    1 
ATOM   4459 H HA   . VAL   B 1 34  ? 45.187 -14.091 -8.168  1.00 15.21 ?  34  VAL   B HA   1 
ATOM   4460 H HB   . VAL   B 1 34  ? 42.620 -15.084 -8.850  1.00 16.77 ?  34  VAL   B HB   1 
ATOM   4461 H HG11 . VAL   B 1 34  ? 42.151 -14.634 -6.519  1.00 17.52 ?  34  VAL   B HG11 1 
ATOM   4462 H HG12 . VAL   B 1 34  ? 43.035 -15.920 -6.815  1.00 17.52 ?  34  VAL   B HG12 1 
ATOM   4463 H HG13 . VAL   B 1 34  ? 43.725 -14.574 -6.324  1.00 17.52 ?  34  VAL   B HG13 1 
ATOM   4464 H HG21 . VAL   B 1 34  ? 41.750 -13.023 -8.177  1.00 17.82 ?  34  VAL   B HG21 1 
ATOM   4465 H HG22 . VAL   B 1 34  ? 43.230 -12.475 -7.995  1.00 17.82 ?  34  VAL   B HG22 1 
ATOM   4466 H HG23 . VAL   B 1 34  ? 42.698 -12.863 -9.441  1.00 17.82 ?  34  VAL   B HG23 1 
ATOM   4467 N N    . VAL   B 1 35  ? 45.971 -16.342 -7.653  1.00 11.32 ?  35  VAL   B N    1 
ATOM   4468 C CA   . VAL   B 1 35  ? 46.204 -17.686 -7.142  1.00 11.18 ?  35  VAL   B CA   1 
ATOM   4469 C C    . VAL   B 1 35  ? 45.668 -17.743 -5.722  1.00 10.87 ?  35  VAL   B C    1 
ATOM   4470 O O    . VAL   B 1 35  ? 45.885 -16.818 -4.931  1.00 11.44 ?  35  VAL   B O    1 
ATOM   4471 C CB   . VAL   B 1 35  ? 47.689 -18.109 -7.225  1.00 12.04 ?  35  VAL   B CB   1 
ATOM   4472 C CG1  . VAL   B 1 35  ? 48.584 -17.261 -6.313  1.00 13.21 ?  35  VAL   B CG1  1 
ATOM   4473 C CG2  . VAL   B 1 35  ? 47.846 -19.592 -6.903  1.00 12.35 ?  35  VAL   B CG2  1 
ATOM   4474 H H    . VAL   B 1 35  ? 46.473 -15.742 -7.291  1.00 13.59 ?  35  VAL   B H    1 
ATOM   4475 H HA   . VAL   B 1 35  ? 45.690 -18.315 -7.670  1.00 13.43 ?  35  VAL   B HA   1 
ATOM   4476 H HB   . VAL   B 1 35  ? 47.992 -17.975 -8.139  1.00 14.46 ?  35  VAL   B HB   1 
ATOM   4477 H HG11 . VAL   B 1 35  ? 49.509 -17.481 -6.494  1.00 15.86 ?  35  VAL   B HG11 1 
ATOM   4478 H HG12 . VAL   B 1 35  ? 48.420 -16.325 -6.495  1.00 15.86 ?  35  VAL   B HG12 1 
ATOM   4479 H HG13 . VAL   B 1 35  ? 48.368 -17.464 -5.389  1.00 15.86 ?  35  VAL   B HG13 1 
ATOM   4480 H HG21 . VAL   B 1 35  ? 48.771 -19.848 -7.015  1.00 14.82 ?  35  VAL   B HG21 1 
ATOM   4481 H HG22 . VAL   B 1 35  ? 47.564 -19.750 -5.986  1.00 14.82 ?  35  VAL   B HG22 1 
ATOM   4482 H HG23 . VAL   B 1 35  ? 47.284 -20.110 -7.508  1.00 14.82 ?  35  VAL   B HG23 1 
ATOM   4483 N N    . VAL   B 1 36  ? 44.961 -18.824 -5.403  1.00 10.79 ?  36  VAL   B N    1 
ATOM   4484 C CA   . VAL   B 1 36  ? 44.414 -19.025 -4.073  1.00 10.69 ?  36  VAL   B CA   1 
ATOM   4485 C C    . VAL   B 1 36  ? 45.422 -19.784 -3.223  1.00 10.09 ?  36  VAL   B C    1 
ATOM   4486 O O    . VAL   B 1 36  ? 45.961 -20.818 -3.646  1.00 11.49 ?  36  VAL   B O    1 
ATOM   4487 C CB   . VAL   B 1 36  ? 43.081 -19.784 -4.151  1.00 10.89 ?  36  VAL   B CB   1 
ATOM   4488 C CG1  . VAL   B 1 36  ? 42.574 -20.145 -2.762  1.00 12.06 ?  36  VAL   B CG1  1 
ATOM   4489 C CG2  . VAL   B 1 36  ? 42.057 -18.954 -4.901  1.00 11.56 ?  36  VAL   B CG2  1 
ATOM   4490 H H    . VAL   B 1 36  ? 44.798 -19.469 -5.948  1.00 12.96 ?  36  VAL   B H    1 
ATOM   4491 H HA   . VAL   B 1 36  ? 44.246 -18.162 -3.659  1.00 12.84 ?  36  VAL   B HA   1 
ATOM   4492 H HB   . VAL   B 1 36  ? 43.213 -20.608 -4.646  1.00 13.08 ?  36  VAL   B HB   1 
ATOM   4493 H HG11 . VAL   B 1 36  ? 41.634 -20.379 -2.822  1.00 14.48 ?  36  VAL   B HG11 1 
ATOM   4494 H HG12 . VAL   B 1 36  ? 43.082 -20.895 -2.424  1.00 14.48 ?  36  VAL   B HG12 1 
ATOM   4495 H HG13 . VAL   B 1 36  ? 42.683 -19.375 -2.181  1.00 14.48 ?  36  VAL   B HG13 1 
ATOM   4496 H HG21 . VAL   B 1 36  ? 41.213 -19.435 -4.924  1.00 13.88 ?  36  VAL   B HG21 1 
ATOM   4497 H HG22 . VAL   B 1 36  ? 41.943 -18.106 -4.450  1.00 13.88 ?  36  VAL   B HG22 1 
ATOM   4498 H HG23 . VAL   B 1 36  ? 42.372 -18.807 -5.810  1.00 13.88 ?  36  VAL   B HG23 1 
ATOM   4499 N N    . ASN   B 1 37  ? 45.631 -19.300 -2.007  1.00 10.78 ?  37  ASN   B N    1 
ATOM   4500 C CA   . ASN   B 1 37  ? 46.391 -20.020 -1.002  1.00 11.30 ?  37  ASN   B CA   1 
ATOM   4501 C C    . ASN   B 1 37  ? 45.444 -20.682 -0.011  1.00 11.23 ?  37  ASN   B C    1 
ATOM   4502 O O    . ASN   B 1 37  ? 44.436 -20.097 0.400   1.00 11.53 ?  37  ASN   B O    1 
ATOM   4503 C CB   . ASN   B 1 37  ? 47.321 -19.068 -0.254  1.00 11.25 ?  37  ASN   B CB   1 
ATOM   4504 C CG   . ASN   B 1 37  ? 48.175 -19.781 0.763   1.00 11.77 ?  37  ASN   B CG   1 
ATOM   4505 O OD1  . ASN   B 1 37  ? 48.510 -20.959 0.597   1.00 12.41 ?  37  ASN   B OD1  1 
ATOM   4506 N ND2  . ASN   B 1 37  ? 48.512 -19.089 1.836   1.00 11.88 ?  37  ASN   B ND2  1 
ATOM   4507 H H    . ASN   B 1 37  ? 45.342 -18.536 -1.730  1.00 12.95 ?  37  ASN   B H    1 
ATOM   4508 H HA   . ASN   B 1 37  ? 46.926 -20.712 -1.423  1.00 13.57 ?  37  ASN   B HA   1 
ATOM   4509 H HB2  . ASN   B 1 37  ? 47.915 -18.643 -0.891  1.00 13.50 ?  37  ASN   B HB2  1 
ATOM   4510 H HB3  . ASN   B 1 37  ? 46.796 -18.407 0.214   1.00 13.50 ?  37  ASN   B HB3  1 
ATOM   4511 H HD21 . ASN   B 1 37  ? 49.005 -19.450 2.445   1.00 14.26 ?  37  ASN   B HD21 1 
ATOM   4512 H HD22 . ASN   B 1 37  ? 48.264 -18.277 1.921   1.00 14.26 ?  37  ASN   B HD22 1 
ATOM   4513 N N    . ALA   B 1 38  ? 45.787 -21.910 0.366   1.00 11.40 ?  38  ALA   B N    1 
ATOM   4514 C CA   . ALA   B 1 38  ? 45.134 -22.650 1.446   1.00 12.09 ?  38  ALA   B CA   1 
ATOM   4515 C C    . ALA   B 1 38  ? 45.723 -22.173 2.771   1.00 11.64 ?  38  ALA   B C    1 
ATOM   4516 O O    . ALA   B 1 38  ? 46.625 -22.784 3.355   1.00 12.59 ?  38  ALA   B O    1 
ATOM   4517 C CB   . ALA   B 1 38  ? 45.333 -24.147 1.254   1.00 13.48 ?  38  ALA   B CB   1 
ATOM   4518 H H    . ALA   B 1 38  ? 46.436 -22.352 0.013   1.00 13.69 ?  38  ALA   B H    1 
ATOM   4519 H HA   . ALA   B 1 38  ? 44.181 -22.460 1.447   1.00 14.52 ?  38  ALA   B HA   1 
ATOM   4520 H HB1  . ALA   B 1 38  ? 44.885 -24.622 1.981   1.00 16.18 ?  38  ALA   B HB1  1 
ATOM   4521 H HB2  . ALA   B 1 38  ? 44.941 -24.410 0.407   1.00 16.18 ?  38  ALA   B HB2  1 
ATOM   4522 H HB3  . ALA   B 1 38  ? 46.277 -24.348 1.265   1.00 16.18 ?  38  ALA   B HB3  1 
ATOM   4523 N N    . ALA   B 1 39  ? 45.210 -21.037 3.236   1.00 11.62 ?  39  ALA   B N    1 
ATOM   4524 C CA   . ALA   B 1 39  ? 45.759 -20.299 4.361   1.00 12.11 ?  39  ALA   B CA   1 
ATOM   4525 C C    . ALA   B 1 39  ? 45.141 -20.739 5.686   1.00 11.96 ?  39  ALA   B C    1 
ATOM   4526 O O    . ALA   B 1 39  ? 44.114 -21.422 5.735   1.00 12.85 ?  39  ALA   B O    1 
ATOM   4527 C CB   . ALA   B 1 39  ? 45.508 -18.804 4.163   1.00 12.42 ?  39  ALA   B CB   1 
ATOM   4528 H H    . ALA   B 1 39  ? 44.508 -20.665 2.904   1.00 13.95 ?  39  ALA   B H    1 
ATOM   4529 H HA   . ALA   B 1 39  ? 46.712 -20.443 4.409   1.00 14.54 ?  39  ALA   B HA   1 
ATOM   4530 H HB1  . ALA   B 1 39  ? 45.879 -18.317 4.917   1.00 14.91 ?  39  ALA   B HB1  1 
ATOM   4531 H HB2  . ALA   B 1 39  ? 45.940 -18.518 3.342   1.00 14.91 ?  39  ALA   B HB2  1 
ATOM   4532 H HB3  . ALA   B 1 39  ? 44.552 -18.645 4.106   1.00 14.91 ?  39  ALA   B HB3  1 
ATOM   4533 N N    . ASN   B 1 40  ? 45.780 -20.312 6.776   1.00 12.71 ?  40  ASN   B N    1 
ATOM   4534 C CA   . ASN   B 1 40  ? 45.220 -20.369 8.116   1.00 13.34 ?  40  ASN   B CA   1 
ATOM   4535 C C    . ASN   B 1 40  ? 45.044 -18.943 8.640   1.00 13.37 ?  40  ASN   B C    1 
ATOM   4536 O O    . ASN   B 1 40  ? 45.463 -17.967 8.013   1.00 13.06 ?  40  ASN   B O    1 
ATOM   4537 C CB   . ASN   B 1 40  ? 46.072 -21.240 9.055   1.00 14.24 ?  40  ASN   B CB   1 
ATOM   4538 C CG   . ASN   B 1 40  ? 47.522 -20.839 9.067   1.00 15.42 ?  40  ASN   B CG   1 
ATOM   4539 O OD1  . ASN   B 1 40  ? 47.846 -19.659 9.129   1.00 17.15 ?  40  ASN   B OD1  1 
ATOM   4540 N ND2  . ASN   B 1 40  ? 48.410 -21.818 9.010   1.00 15.52 ?  40  ASN   B ND2  1 
ATOM   4541 H H    . ASN   B 1 40  ? 46.574 -19.982 6.752   1.00 15.26 ?  40  ASN   B H    1 
ATOM   4542 H HA   . ASN   B 1 40  ? 44.339 -20.767 8.069   1.00 16.02 ?  40  ASN   B HA   1 
ATOM   4543 H HB2  . ASN   B 1 40  ? 45.731 -21.154 9.958   1.00 17.10 ?  40  ASN   B HB2  1 
ATOM   4544 H HB3  . ASN   B 1 40  ? 46.018 -22.161 8.763   1.00 17.10 ?  40  ASN   B HB3  1 
ATOM   4545 H HD21 . ASN   B 1 40  ? 49.251 -21.640 9.014   1.00 18.63 ?  40  ASN   B HD21 1 
ATOM   4546 H HD22 . ASN   B 1 40  ? 48.144 -22.636 8.969   1.00 18.63 ?  40  ASN   B HD22 1 
ATOM   4547 N N    . VAL   B 1 41  ? 44.393 -18.812 9.797   1.00 13.64 ?  41  VAL   B N    1 
ATOM   4548 C CA   . VAL   B 1 41  ? 43.937 -17.490 10.237  1.00 14.57 ?  41  VAL   B CA   1 
ATOM   4549 C C    . VAL   B 1 41  ? 45.091 -16.540 10.534  1.00 14.09 ?  41  VAL   B C    1 
ATOM   4550 O O    . VAL   B 1 41  ? 44.912 -15.318 10.464  1.00 14.33 ?  41  VAL   B O    1 
ATOM   4551 C CB   . VAL   B 1 41  ? 42.964 -17.573 11.429  1.00 15.97 ?  41  VAL   B CB   1 
ATOM   4552 C CG1  . VAL   B 1 41  ? 41.670 -18.254 11.022  1.00 16.37 ?  41  VAL   B CG1  1 
ATOM   4553 C CG2  . VAL   B 1 41  ? 43.618 -18.262 12.612  1.00 17.28 ?  41  VAL   B CG2  1 
ATOM   4554 H H    . VAL   B 1 41  ? 44.208 -19.454 10.328  1.00 16.38 ?  41  VAL   B H    1 
ATOM   4555 H HA   . VAL   B 1 41  ? 43.439 -17.094 9.508   1.00 17.49 ?  41  VAL   B HA   1 
ATOM   4556 H HB   . VAL   B 1 41  ? 42.742 -16.673 11.709  1.00 19.17 ?  41  VAL   B HB   1 
ATOM   4557 H HG11 . VAL   B 1 41  ? 41.064 -18.263 11.779  1.00 19.65 ?  41  VAL   B HG11 1 
ATOM   4558 H HG12 . VAL   B 1 41  ? 41.273 -17.760 10.287  1.00 19.65 ?  41  VAL   B HG12 1 
ATOM   4559 H HG13 . VAL   B 1 41  ? 41.864 -19.162 10.742  1.00 19.65 ?  41  VAL   B HG13 1 
ATOM   4560 H HG21 . VAL   B 1 41  ? 42.989 -18.289 13.349  1.00 20.75 ?  41  VAL   B HG21 1 
ATOM   4561 H HG22 . VAL   B 1 41  ? 43.864 -19.167 12.357  1.00 20.75 ?  41  VAL   B HG22 1 
ATOM   4562 H HG23 . VAL   B 1 41  ? 44.410 -17.767 12.872  1.00 20.75 ?  41  VAL   B HG23 1 
ATOM   4563 N N    . TYR   B 1 42  ? 46.261 -17.059 10.908  1.00 14.36 ?  42  TYR   B N    1 
ATOM   4564 C CA   . TYR   B 1 42  ? 47.416 -16.210 11.171  1.00 14.95 ?  42  TYR   B CA   1 
ATOM   4565 C C    . TYR   B 1 42  ? 48.375 -16.139 9.988   1.00 14.07 ?  42  TYR   B C    1 
ATOM   4566 O O    . TYR   B 1 42  ? 49.464 -15.565 10.116  1.00 15.11 ?  42  TYR   B O    1 
ATOM   4567 C CB   . TYR   B 1 42  ? 48.121 -16.613 12.472  1.00 17.18 ?  42  TYR   B CB   1 
ATOM   4568 C CG   . TYR   B 1 42  ? 47.507 -15.949 13.696  1.00 17.71 ?  42  TYR   B CG   1 
ATOM   4569 C CD1  . TYR   B 1 42  ? 47.713 -14.593 13.950  1.00 17.36 ?  42  TYR   B CD1  1 
ATOM   4570 C CD2  . TYR   B 1 42  ? 46.716 -16.663 14.583  1.00 19.80 ?  42  TYR   B CD2  1 
ATOM   4571 C CE1  . TYR   B 1 42  ? 47.151 -13.973 15.050  1.00 18.70 ?  42  TYR   B CE1  1 
ATOM   4572 C CE2  . TYR   B 1 42  ? 46.152 -16.052 15.690  1.00 20.17 ?  42  TYR   B CE2  1 
ATOM   4573 C CZ   . TYR   B 1 42  ? 46.371 -14.705 15.918  1.00 20.40 ?  42  TYR   B CZ   1 
ATOM   4574 O OH   . TYR   B 1 42  ? 45.815 -14.091 17.020  1.00 23.30 ?  42  TYR   B OH   1 
ATOM   4575 H H    . TYR   B 1 42  ? 46.407 -17.905 11.006  1.00 17.25 ?  42  TYR   B H    1 
ATOM   4576 H HA   . TYR   B 1 42  ? 47.086 -15.312 11.305  1.00 17.95 ?  42  TYR   B HA   1 
ATOM   4577 H HB2  . TYR   B 1 42  ? 48.053 -17.572 12.587  1.00 20.62 ?  42  TYR   B HB2  1 
ATOM   4578 H HB3  . TYR   B 1 42  ? 49.050 -16.346 12.419  1.00 20.62 ?  42  TYR   B HB3  1 
ATOM   4579 H HD1  . TYR   B 1 42  ? 48.238 -14.095 13.359  1.00 20.84 ?  42  TYR   B HD1  1 
ATOM   4580 H HD2  . TYR   B 1 42  ? 46.562 -17.568 14.427  1.00 23.76 ?  42  TYR   B HD2  1 
ATOM   4581 H HE1  . TYR   B 1 42  ? 47.304 -13.070 15.203  1.00 22.44 ?  42  TYR   B HE1  1 
ATOM   4582 H HE2  . TYR   B 1 42  ? 45.624 -16.545 16.275  1.00 24.21 ?  42  TYR   B HE2  1 
ATOM   4583 H HH   . TYR   B 1 42  ? 46.035 -13.283 17.035  1.00 27.97 ?  42  TYR   B HH   1 
ATOM   4584 N N    . LEU   B 1 43  ? 47.974 -16.659 8.830   1.00 13.08 ?  43  LEU   B N    1 
ATOM   4585 C CA   . LEU   B 1 43  ? 48.786 -16.597 7.618   1.00 13.07 ?  43  LEU   B CA   1 
ATOM   4586 C C    . LEU   B 1 43  ? 50.198 -17.105 7.873   1.00 13.51 ?  43  LEU   B C    1 
ATOM   4587 O O    . LEU   B 1 43  ? 51.178 -16.515 7.423   1.00 13.84 ?  43  LEU   B O    1 
ATOM   4588 C CB   . LEU   B 1 43  ? 48.800 -15.193 7.009   1.00 13.27 ?  43  LEU   B CB   1 
ATOM   4589 C CG   . LEU   B 1 43  ? 47.439 -14.584 6.636   1.00 13.44 ?  43  LEU   B CG   1 
ATOM   4590 C CD1  . LEU   B 1 43  ? 47.629 -13.180 6.069   1.00 14.53 ?  43  LEU   B CD1  1 
ATOM   4591 C CD2  . LEU   B 1 43  ? 46.682 -15.474 5.656   1.00 13.41 ?  43  LEU   B CD2  1 
ATOM   4592 H H    . LEU   B 1 43  ? 47.224 -17.073 8.720   1.00 15.70 ?  43  LEU   B H    1 
ATOM   4593 H HA   . LEU   B 1 43  ? 48.382 -17.186 6.959   1.00 15.69 ?  43  LEU   B HA   1 
ATOM   4594 H HB2  . LEU   B 1 43  ? 49.218 -14.592 7.639   1.00 15.93 ?  43  LEU   B HB2  1 
ATOM   4595 H HB3  . LEU   B 1 43  ? 49.326 -15.227 6.194   1.00 15.93 ?  43  LEU   B HB3  1 
ATOM   4596 H HG   . LEU   B 1 43  ? 46.901 -14.507 7.435   1.00 16.14 ?  43  LEU   B HG   1 
ATOM   4597 H HD11 . LEU   B 1 43  ? 46.759 -12.810 5.841   1.00 17.44 ?  43  LEU   B HD11 1 
ATOM   4598 H HD12 . LEU   B 1 43  ? 48.054 -12.624 6.743   1.00 17.44 ?  43  LEU   B HD12 1 
ATOM   4599 H HD13 . LEU   B 1 43  ? 48.186 -13.226 5.278   1.00 17.44 ?  43  LEU   B HD13 1 
ATOM   4600 H HD21 . LEU   B 1 43  ? 45.876 -15.015 5.363   1.00 16.10 ?  43  LEU   B HD21 1 
ATOM   4601 H HD22 . LEU   B 1 43  ? 47.248 -15.662 4.890   1.00 16.10 ?  43  LEU   B HD22 1 
ATOM   4602 H HD23 . LEU   B 1 43  ? 46.442 -16.304 6.099   1.00 16.10 ?  43  LEU   B HD23 1 
ATOM   4603 N N    . LYS   B 1 44  ? 50.295 -18.218 8.592   1.00 13.37 ?  44  LYS   B N    1 
ATOM   4604 C CA   . LYS   B 1 44  ? 51.562 -18.898 8.842   1.00 14.18 ?  44  LYS   B CA   1 
ATOM   4605 C C    . LYS   B 1 44  ? 51.675 -20.006 7.806   1.00 13.47 ?  44  LYS   B C    1 
ATOM   4606 O O    . LYS   B 1 44  ? 50.987 -21.027 7.888   1.00 14.73 ?  44  LYS   B O    1 
ATOM   4607 C CB   . LYS   B 1 44  ? 51.606 -19.412 10.277  1.00 15.98 ?  44  LYS   B CB   1 
ATOM   4608 C CG   . LYS   B 1 44  ? 51.776 -18.300 11.302  1.00 18.86 ?  44  LYS   B CG   1 
ATOM   4609 C CD   . LYS   B 1 44  ? 52.990 -17.445 10.939  1.00 21.73 ?  44  LYS   B CD   1 
ATOM   4610 C CE   . LYS   B 1 44  ? 53.429 -16.528 12.051  1.00 24.47 ?  44  LYS   B CE   1 
ATOM   4611 N NZ   . LYS   B 1 44  ? 54.643 -15.755 11.680  1.00 25.96 ?  44  LYS   B NZ   1 
ATOM   4612 H H    . LYS   B 1 44  ? 49.621 -18.610 8.958   1.00 16.05 ?  44  LYS   B H    1 
ATOM   4613 H HA   . LYS   B 1 44  ? 52.292 -18.280 8.684   1.00 17.02 ?  44  LYS   B HA   1 
ATOM   4614 H HB2  . LYS   B 1 44  ? 50.770 -19.870 10.473  1.00 19.19 ?  44  LYS   B HB2  1 
ATOM   4615 H HB3  . LYS   B 1 44  ? 52.348 -20.023 10.371  1.00 19.19 ?  44  LYS   B HB3  1 
ATOM   4616 H HG2  . LYS   B 1 44  ? 50.988 -17.737 11.308  1.00 22.64 ?  44  LYS   B HG2  1 
ATOM   4617 H HG3  . LYS   B 1 44  ? 51.924 -18.691 12.180  1.00 22.64 ?  44  LYS   B HG3  1 
ATOM   4618 H HD2  . LYS   B 1 44  ? 53.731 -18.035 10.706  1.00 26.09 ?  44  LYS   B HD2  1 
ATOM   4619 H HD3  . LYS   B 1 44  ? 52.764 -16.888 10.176  1.00 26.09 ?  44  LYS   B HD3  1 
ATOM   4620 H HE2  . LYS   B 1 44  ? 52.718 -15.899 12.230  1.00 29.37 ?  44  LYS   B HE2  1 
ATOM   4621 H HE3  . LYS   B 1 44  ? 53.627 -17.056 12.839  1.00 29.37 ?  44  LYS   B HE3  1 
ATOM   4622 H HZ1  . LYS   B 1 44  ? 54.877 -15.221 12.351  1.00 31.16 ?  44  LYS   B HZ1  1 
ATOM   4623 H HZ2  . LYS   B 1 44  ? 55.315 -16.308 11.499  1.00 31.16 ?  44  LYS   B HZ2  1 
ATOM   4624 H HZ3  . LYS   B 1 44  ? 54.477 -15.257 10.959  1.00 31.16 ?  44  LYS   B HZ3  1 
ATOM   4625 N N    . HIS   B 1 45  ? 52.524 -19.782 6.807   1.00 13.30 ?  45  HIS   B N    1 
ATOM   4626 C CA   . HIS   B 1 45  ? 52.547 -20.618 5.610   1.00 13.32 ?  45  HIS   B CA   1 
ATOM   4627 C C    . HIS   B 1 45  ? 53.559 -21.745 5.772   1.00 15.25 ?  45  HIS   B C    1 
ATOM   4628 O O    . HIS   B 1 45  ? 54.613 -21.767 5.146   1.00 17.79 ?  45  HIS   B O    1 
ATOM   4629 C CB   . HIS   B 1 45  ? 52.864 -19.771 4.391   1.00 13.13 ?  45  HIS   B CB   1 
ATOM   4630 C CG   . HIS   B 1 45  ? 51.998 -18.567 4.276   1.00 13.12 ?  45  HIS   B CG   1 
ATOM   4631 N ND1  . HIS   B 1 45  ? 50.621 -18.640 4.232   1.00 13.62 ?  45  HIS   B ND1  1 
ATOM   4632 C CD2  . HIS   B 1 45  ? 52.319 -17.255 4.207   1.00 13.88 ?  45  HIS   B CD2  1 
ATOM   4633 C CE1  . HIS   B 1 45  ? 50.139 -17.415 4.122   1.00 13.17 ?  45  HIS   B CE1  1 
ATOM   4634 N NE2  . HIS   B 1 45  ? 51.145 -16.558 4.110   1.00 13.72 ?  45  HIS   B NE2  1 
ATOM   4635 H H    . HIS   B 1 45  ? 53.100 -19.138 6.793   1.00 15.97 ?  45  HIS   B H    1 
ATOM   4636 H HA   . HIS   B 1 45  ? 51.667 -21.008 5.480   1.00 15.99 ?  45  HIS   B HA   1 
ATOM   4637 H HB2  . HIS   B 1 45  ? 53.785 -19.477 4.437   1.00 15.76 ?  45  HIS   B HB2  1 
ATOM   4638 H HB3  . HIS   B 1 45  ? 52.734 -20.313 3.589   1.00 15.76 ?  45  HIS   B HB3  1 
ATOM   4639 H HD2  . HIS   B 1 45  ? 53.179 -16.892 4.219   1.00 16.67 ?  45  HIS   B HD2  1 
ATOM   4640 H HE1  . HIS   B 1 45  ? 49.240 -17.191 4.059   1.00 15.82 ?  45  HIS   B HE1  1 
ATOM   4641 H HE2  . HIS   B 1 45  ? 51.074 -15.702 4.051   1.00 16.47 ?  45  HIS   B HE2  1 
ATOM   4642 N N    . GLY   B 1 46  ? 53.198 -22.704 6.615   1.00 16.70 ?  46  GLY   B N    1 
ATOM   4643 C CA   . GLY   B 1 46  ? 54.115 -23.769 6.971   1.00 18.36 ?  46  GLY   B CA   1 
ATOM   4644 C C    . GLY   B 1 46  ? 54.158 -24.969 6.043   1.00 19.94 ?  46  GLY   B C    1 
ATOM   4645 O O    . GLY   B 1 46  ? 55.232 -25.381 5.594   1.00 23.20 ?  46  GLY   B O    1 
ATOM   4646 H H    . GLY   B 1 46  ? 52.429 -22.743 7.009   1.00 20.05 ?  46  GLY   B H    1 
ATOM   4647 H HA2  . GLY   B 1 46  ? 55.008 -23.398 7.025   1.00 22.04 ?  46  GLY   B HA2  1 
ATOM   4648 H HA3  . GLY   B 1 46  ? 53.875 -24.096 7.852   1.00 22.04 ?  46  GLY   B HA3  1 
ATOM   4649 N N    . GLY   B 1 47  ? 53.005 -25.564 5.758   1.00 19.08 ?  47  GLY   B N    1 
ATOM   4650 C CA   . GLY   B 1 47  ? 52.954 -26.851 5.093   1.00 16.96 ?  47  GLY   B CA   1 
ATOM   4651 C C    . GLY   B 1 47  ? 52.034 -26.829 3.889   1.00 14.79 ?  47  GLY   B C    1 
ATOM   4652 O O    . GLY   B 1 47  ? 51.383 -25.824 3.600   1.00 14.76 ?  47  GLY   B O    1 
ATOM   4653 H H    . GLY   B 1 47  ? 52.229 -25.243 5.962   1.00 22.91 ?  47  GLY   B H    1 
ATOM   4654 H HA2  . GLY   B 1 47  ? 53.843 -27.095 4.793   1.00 20.36 ?  47  GLY   B HA2  1 
ATOM   4655 H HA3  . GLY   B 1 47  ? 52.640 -27.522 5.715   1.00 20.36 ?  47  GLY   B HA3  1 
ATOM   4656 N N    . GLY   B 1 48  ? 51.984 -27.968 3.204   1.00 14.24 ?  48  GLY   B N    1 
ATOM   4657 C CA   . GLY   B 1 48  ? 51.055 -28.121 2.102   1.00 13.87 ?  48  GLY   B CA   1 
ATOM   4658 C C    . GLY   B 1 48  ? 51.199 -27.018 1.079   1.00 13.13 ?  48  GLY   B C    1 
ATOM   4659 O O    . GLY   B 1 48  ? 52.303 -26.556 0.768   1.00 13.89 ?  48  GLY   B O    1 
ATOM   4660 H H    . GLY   B 1 48  ? 52.483 -28.647 3.353   1.00 17.09 ?  48  GLY   B H    1 
ATOM   4661 H HA2  . GLY   B 1 48  ? 51.212 -28.977 1.668   1.00 16.65 ?  48  GLY   B HA2  1 
ATOM   4662 H HA3  . GLY   B 1 48  ? 50.146 -28.112 2.441   1.00 16.65 ?  48  GLY   B HA3  1 
ATOM   4663 N N    . VAL   B 1 49  ? 50.056 -26.586 0.546   1.00 13.02 ?  49  VAL   B N    1 
ATOM   4664 C CA   . VAL   B 1 49  ? 50.042 -25.562 -0.496  1.00 13.34 ?  49  VAL   B CA   1 
ATOM   4665 C C    . VAL   B 1 49  ? 50.705 -24.279 -0.009  1.00 12.60 ?  49  VAL   B C    1 
ATOM   4666 O O    . VAL   B 1 49  ? 51.493 -23.660 -0.733  1.00 13.15 ?  49  VAL   B O    1 
ATOM   4667 C CB   . VAL   B 1 49  ? 48.601 -25.302 -0.977  1.00 14.48 ?  49  VAL   B CB   1 
ATOM   4668 C CG1  . VAL   B 1 49  ? 48.539 -24.047 -1.841  1.00 14.94 ?  49  VAL   B CG1  1 
ATOM   4669 C CG2  . VAL   B 1 49  ? 48.062 -26.498 -1.743  1.00 16.47 ?  49  VAL   B CG2  1 
ATOM   4670 H H    . VAL   B 1 49  ? 49.269 -26.869 0.768   1.00 15.64 ?  49  VAL   B H    1 
ATOM   4671 H HA   . VAL   B 1 49  ? 50.547 -25.884 -1.258  1.00 16.01 ?  49  VAL   B HA   1 
ATOM   4672 H HB   . VAL   B 1 49  ? 48.031 -25.159 -0.207  1.00 17.39 ?  49  VAL   B HB   1 
ATOM   4673 H HG11 . VAL   B 1 49  ? 47.715 -24.059 -2.353  1.00 17.94 ?  49  VAL   B HG11 1 
ATOM   4674 H HG12 . VAL   B 1 49  ? 48.558 -23.265 -1.268  1.00 17.94 ?  49  VAL   B HG12 1 
ATOM   4675 H HG13 . VAL   B 1 49  ? 49.300 -24.040 -2.442  1.00 17.94 ?  49  VAL   B HG13 1 
ATOM   4676 H HG21 . VAL   B 1 49  ? 47.153 -26.309 -2.025  1.00 19.77 ?  49  VAL   B HG21 1 
ATOM   4677 H HG22 . VAL   B 1 49  ? 48.623 -26.651 -2.521  1.00 19.77 ?  49  VAL   B HG22 1 
ATOM   4678 H HG23 . VAL   B 1 49  ? 48.077 -27.274 -1.165  1.00 19.77 ?  49  VAL   B HG23 1 
ATOM   4679 N N    . ALA   B 1 50  ? 50.361 -23.829 1.200   1.00 12.40 ?  50  ALA   B N    1 
ATOM   4680 C CA   . ALA   B 1 50  ? 50.881 -22.552 1.678   1.00 12.23 ?  50  ALA   B CA   1 
ATOM   4681 C C    . ALA   B 1 50  ? 52.399 -22.584 1.777   1.00 12.37 ?  50  ALA   B C    1 
ATOM   4682 O O    . ALA   B 1 50  ? 53.078 -21.616 1.407   1.00 12.45 ?  50  ALA   B O    1 
ATOM   4683 C CB   . ALA   B 1 50  ? 50.261 -22.199 3.028   1.00 12.44 ?  50  ALA   B CB   1 
ATOM   4684 H H    . ALA   B 1 50  ? 49.839 -24.237 1.750   1.00 14.89 ?  50  ALA   B H    1 
ATOM   4685 H HA   . ALA   B 1 50  ? 50.646 -21.858 1.052   1.00 14.68 ?  50  ALA   B HA   1 
ATOM   4686 H HB1  . ALA   B 1 50  ? 50.619 -21.348 3.331   1.00 14.94 ?  50  ALA   B HB1  1 
ATOM   4687 H HB2  . ALA   B 1 50  ? 49.298 -22.133 2.927   1.00 14.94 ?  50  ALA   B HB2  1 
ATOM   4688 H HB3  . ALA   B 1 50  ? 50.477 -22.893 3.673   1.00 14.94 ?  50  ALA   B HB3  1 
ATOM   4689 N N    . GLY   B 1 51  ? 52.950 -23.678 2.291   1.00 12.89 ?  51  GLY   B N    1 
ATOM   4690 C CA   . GLY   B 1 51  ? 54.394 -23.781 2.359   1.00 13.72 ?  51  GLY   B CA   1 
ATOM   4691 C C    . GLY   B 1 51  ? 55.033 -23.729 0.988   1.00 13.51 ?  51  GLY   B C    1 
ATOM   4692 O O    . GLY   B 1 51  ? 56.079 -23.102 0.806   1.00 14.59 ?  51  GLY   B O    1 
ATOM   4693 H H    . GLY   B 1 51  ? 52.525 -24.360 2.598   1.00 15.48 ?  51  GLY   B H    1 
ATOM   4694 H HA2  . GLY   B 1 51  ? 54.752 -23.051 2.889   1.00 16.48 ?  51  GLY   B HA2  1 
ATOM   4695 H HA3  . GLY   B 1 51  ? 54.645 -24.619 2.781   1.00 16.48 ?  51  GLY   B HA3  1 
ATOM   4696 N N    . ALA   B 1 52  ? 54.423 -24.393 0.007   1.00 12.98 ?  52  ALA   B N    1 
ATOM   4697 C CA   . ALA   B 1 52  ? 54.988 -24.406 -1.335  1.00 13.40 ?  52  ALA   B CA   1 
ATOM   4698 C C    . ALA   B 1 52  ? 54.914 -23.033 -1.990  1.00 12.80 ?  52  ALA   B C    1 
ATOM   4699 O O    . ALA   B 1 52  ? 55.884 -22.589 -2.622  1.00 13.69 ?  52  ALA   B O    1 
ATOM   4700 C CB   . ALA   B 1 52  ? 54.280 -25.450 -2.192  1.00 14.09 ?  52  ALA   B CB   1 
ATOM   4701 H H    . ALA   B 1 52  ? 53.683 -24.829 0.089   1.00 15.58 ?  52  ALA   B H    1 
ATOM   4702 H HA   . ALA   B 1 52  ? 55.923 -24.653 -1.277  1.00 16.09 ?  52  ALA   B HA   1 
ATOM   4703 H HB1  . ALA   B 1 52  ? 54.673 -25.445 -3.081  1.00 16.91 ?  52  ALA   B HB1  1 
ATOM   4704 H HB2  . ALA   B 1 52  ? 54.396 -26.321 -1.784  1.00 16.91 ?  52  ALA   B HB2  1 
ATOM   4705 H HB3  . ALA   B 1 52  ? 53.339 -25.229 -2.245  1.00 16.91 ?  52  ALA   B HB3  1 
ATOM   4706 N N    . LEU   B 1 53  ? 53.771 -22.357 -1.878  1.00 12.35 ?  53  LEU   B N    1 
ATOM   4707 C CA   . LEU   B 1 53  ? 53.663 -21.016 -2.442  1.00 12.70 ?  53  LEU   B CA   1 
ATOM   4708 C C    . LEU   B 1 53  ? 54.673 -20.082 -1.792  1.00 12.67 ?  53  LEU   B C    1 
ATOM   4709 O O    . LEU   B 1 53  ? 55.378 -19.332 -2.477  1.00 13.49 ?  53  LEU   B O    1 
ATOM   4710 C CB   . LEU   B 1 53  ? 52.242 -20.470 -2.273  1.00 13.38 ?  53  LEU   B CB   1 
ATOM   4711 C CG   . LEU   B 1 53  ? 51.113 -21.184 -3.019  1.00 13.73 ?  53  LEU   B CG   1 
ATOM   4712 C CD1  . LEU   B 1 53  ? 49.774 -20.573 -2.665  1.00 15.35 ?  53  LEU   B CD1  1 
ATOM   4713 C CD2  . LEU   B 1 53  ? 51.318 -21.167 -4.525  1.00 15.12 ?  53  LEU   B CD2  1 
ATOM   4714 H H    . LEU   B 1 53  ? 53.061 -22.642 -1.483  1.00 14.83 ?  53  LEU   B H    1 
ATOM   4715 H HA   . LEU   B 1 53  ? 53.861 -21.059 -3.394  1.00 15.25 ?  53  LEU   B HA   1 
ATOM   4716 H HB2  . LEU   B 1 53  ? 52.020 -20.500 -1.331  1.00 16.06 ?  53  LEU   B HB2  1 
ATOM   4717 H HB3  . LEU   B 1 53  ? 52.236 -19.550 -2.575  1.00 16.06 ?  53  LEU   B HB3  1 
ATOM   4718 H HG   . LEU   B 1 53  ? 51.087 -22.111 -2.734  1.00 16.48 ?  53  LEU   B HG   1 
ATOM   4719 H HD11 . LEU   B 1 53  ? 49.071 -21.044 -3.146  1.00 18.43 ?  53  LEU   B HD11 1 
ATOM   4720 H HD12 . LEU   B 1 53  ? 49.626 -20.659 -1.707  1.00 18.43 ?  53  LEU   B HD12 1 
ATOM   4721 H HD13 . LEU   B 1 53  ? 49.773 -19.637 -2.915  1.00 18.43 ?  53  LEU   B HD13 1 
ATOM   4722 H HD21 . LEU   B 1 53  ? 50.608 -21.676 -4.948  1.00 18.15 ?  53  LEU   B HD21 1 
ATOM   4723 H HD22 . LEU   B 1 53  ? 51.294 -20.250 -4.837  1.00 18.15 ?  53  LEU   B HD22 1 
ATOM   4724 H HD23 . LEU   B 1 53  ? 52.176 -21.567 -4.732  1.00 18.15 ?  53  LEU   B HD23 1 
ATOM   4725 N N    . ASN   B 1 54  ? 54.765 -20.118 -0.463  1.00 12.26 ?  54  ASN   B N    1 
ATOM   4726 C CA   . ASN   B 1 54  ? 55.680 -19.203 0.207   1.00 12.94 ?  54  ASN   B CA   1 
ATOM   4727 C C    . ASN   B 1 54  ? 57.120 -19.478 -0.194  1.00 13.25 ?  54  ASN   B C    1 
ATOM   4728 O O    . ASN   B 1 54  ? 57.893 -18.540 -0.438  1.00 13.90 ?  54  ASN   B O    1 
ATOM   4729 C CB   . ASN   B 1 54  ? 55.523 -19.278 1.719   1.00 13.68 ?  54  ASN   B CB   1 
ATOM   4730 C CG   . ASN   B 1 54  ? 56.493 -18.352 2.426   1.00 13.85 ?  54  ASN   B CG   1 
ATOM   4731 O OD1  . ASN   B 1 54  ? 56.504 -17.143 2.172   1.00 13.78 ?  54  ASN   B OD1  1 
ATOM   4732 N ND2  . ASN   B 1 54  ? 57.339 -18.911 3.280   1.00 15.60 ?  54  ASN   B ND2  1 
ATOM   4733 H H    . ASN   B 1 54  ? 54.323 -20.648 0.052   1.00 14.72 ?  54  ASN   B H    1 
ATOM   4734 H HA   . ASN   B 1 54  ? 55.460 -18.299 -0.070  1.00 15.53 ?  54  ASN   B HA   1 
ATOM   4735 H HB2  . ASN   B 1 54  ? 54.619 -19.008 1.959   1.00 16.43 ?  54  ASN   B HB2  1 
ATOM   4736 H HB3  . ASN   B 1 54  ? 55.695 -20.179 2.015   1.00 16.43 ?  54  ASN   B HB3  1 
ATOM   4737 H HD21 . ASN   B 1 54  ? 57.914 -18.422 3.696   1.00 18.73 ?  54  ASN   B HD21 1 
ATOM   4738 H HD22 . ASN   B 1 54  ? 57.314 -19.757 3.418   1.00 18.73 ?  54  ASN   B HD22 1 
ATOM   4739 N N    . LYS   B 1 55  ? 57.502 -20.754 -0.258  1.00 13.96 ?  55  LYS   B N    1 
ATOM   4740 C CA   . LYS   B 1 55  ? 58.856 -21.096 -0.676  1.00 14.93 ?  55  LYS   B CA   1 
ATOM   4741 C C    . LYS   B 1 55  ? 59.151 -20.557 -2.071  1.00 14.53 ?  55  LYS   B C    1 
ATOM   4742 O O    . LYS   B 1 55  ? 60.247 -20.047 -2.325  1.00 15.45 ?  55  LYS   B O    1 
ATOM   4743 C CB   . LYS   B 1 55  ? 59.050 -22.609 -0.620  1.00 16.76 ?  55  LYS   B CB   1 
ATOM   4744 C CG   . LYS   B 1 55  ? 60.440 -23.060 -1.017  1.00 21.37 ?  55  LYS   B CG   1 
ATOM   4745 C CD   . LYS   B 1 55  ? 60.617 -24.556 -0.842  1.00 25.09 ?  55  LYS   B CD   1 
ATOM   4746 C CE   . LYS   B 1 55  ? 60.603 -24.962 0.627   1.00 28.14 ?  55  LYS   B CE   1 
ATOM   4747 N NZ   . LYS   B 1 55  ? 60.951 -26.392 0.809   1.00 29.93 ?  55  LYS   B NZ   1 
ATOM   4748 H H    . LYS   B 1 55  ? 56.997 -21.426 -0.074  1.00 16.76 ?  55  LYS   B H    1 
ATOM   4749 H HA   . LYS   B 1 55  ? 59.483 -20.690 -0.061  1.00 17.93 ?  55  LYS   B HA   1 
ATOM   4750 H HB2  . LYS   B 1 55  ? 58.883 -22.905 0.288   1.00 20.12 ?  55  LYS   B HB2  1 
ATOM   4751 H HB3  . LYS   B 1 55  ? 58.419 -23.030 -1.224  1.00 20.12 ?  55  LYS   B HB3  1 
ATOM   4752 H HG2  . LYS   B 1 55  ? 60.595 -22.845 -1.951  1.00 25.65 ?  55  LYS   B HG2  1 
ATOM   4753 H HG3  . LYS   B 1 55  ? 61.095 -22.609 -0.458  1.00 25.65 ?  55  LYS   B HG3  1 
ATOM   4754 H HD2  . LYS   B 1 55  ? 59.892 -25.021 -1.290  1.00 30.12 ?  55  LYS   B HD2  1 
ATOM   4755 H HD3  . LYS   B 1 55  ? 61.470 -24.827 -1.219  1.00 30.12 ?  55  LYS   B HD3  1 
ATOM   4756 H HE2  . LYS   B 1 55  ? 61.250 -24.421 1.110   1.00 33.78 ?  55  LYS   B HE2  1 
ATOM   4757 H HE3  . LYS   B 1 55  ? 59.713 -24.814 0.988   1.00 33.78 ?  55  LYS   B HE3  1 
ATOM   4758 H HZ1  . LYS   B 1 55  ? 60.911 -26.603 1.672   1.00 35.92 ?  55  LYS   B HZ1  1 
ATOM   4759 H HZ2  . LYS   B 1 55  ? 60.375 -26.900 0.359   1.00 35.92 ?  55  LYS   B HZ2  1 
ATOM   4760 H HZ3  . LYS   B 1 55  ? 61.771 -26.543 0.508   1.00 35.92 ?  55  LYS   B HZ3  1 
ATOM   4761 N N    . ALA   B 1 56  ? 58.182 -20.643 -2.986  1.00 13.95 ?  56  ALA   B N    1 
ATOM   4762 C CA   . ALA   B 1 56  ? 58.400 -20.142 -4.339  1.00 15.12 ?  56  ALA   B CA   1 
ATOM   4763 C C    . ALA   B 1 56  ? 58.662 -18.643 -4.344  1.00 14.69 ?  56  ALA   B C    1 
ATOM   4764 O O    . ALA   B 1 56  ? 59.375 -18.141 -5.223  1.00 15.97 ?  56  ALA   B O    1 
ATOM   4765 C CB   . ALA   B 1 56  ? 57.207 -20.485 -5.231  1.00 16.51 ?  56  ALA   B CB   1 
ATOM   4766 H H    . ALA   B 1 56  ? 57.397 -20.971 -2.849  1.00 16.75 ?  56  ALA   B H    1 
ATOM   4767 H HA   . ALA   B 1 56  ? 59.182 -20.572 -4.708  1.00 18.15 ?  56  ALA   B HA   1 
ATOM   4768 H HB1  . ALA   B 1 56  ? 57.379 -20.151 -6.128  1.00 19.82 ?  56  ALA   B HB1  1 
ATOM   4769 H HB2  . ALA   B 1 56  ? 57.102 -21.448 -5.253  1.00 19.82 ?  56  ALA   B HB2  1 
ATOM   4770 H HB3  . ALA   B 1 56  ? 56.410 -20.070 -4.871  1.00 19.82 ?  56  ALA   B HB3  1 
ATOM   4771 N N    . THR   B 1 57  ? 58.100 -17.913 -3.382  1.00 14.53 ?  57  THR   B N    1 
ATOM   4772 C CA   . THR   B 1 57  ? 58.337 -16.478 -3.269  1.00 14.60 ?  57  THR   B CA   1 
ATOM   4773 C C    . THR   B 1 57  ? 59.586 -16.151 -2.458  1.00 15.45 ?  57  THR   B C    1 
ATOM   4774 O O    . THR   B 1 57  ? 59.818 -14.979 -2.143  1.00 16.03 ?  57  THR   B O    1 
ATOM   4775 C CB   . THR   B 1 57  ? 57.139 -15.746 -2.640  1.00 14.11 ?  57  THR   B CB   1 
ATOM   4776 O OG1  . THR   B 1 57  ? 57.112 -15.957 -1.222  1.00 14.83 ?  57  THR   B OG1  1 
ATOM   4777 C CG2  . THR   B 1 57  ? 55.819 -16.168 -3.273  1.00 14.39 ?  57  THR   B CG2  1 
ATOM   4778 H H    . THR   B 1 57  ? 57.559 -18.223 -2.786  1.00 17.45 ?  57  THR   B H    1 
ATOM   4779 H HA   . THR   B 1 57  ? 58.457 -16.115 -4.161  1.00 17.53 ?  57  THR   B HA   1 
ATOM   4780 H HB   . THR   B 1 57  ? 57.243 -14.795 -2.809  1.00 16.94 ?  57  THR   B HB   1 
ATOM   4781 H HG1  . THR   B 1 57  ? 57.047 -16.772 -1.052  1.00 17.81 ?  57  THR   B HG1  1 
ATOM   4782 H HG21 . THR   B 1 57  ? 55.093 -15.626 -2.929  1.00 17.28 ?  57  THR   B HG21 1 
ATOM   4783 H HG22 . THR   B 1 57  ? 55.861 -16.064 -4.237  1.00 17.28 ?  57  THR   B HG22 1 
ATOM   4784 H HG23 . THR   B 1 57  ? 55.635 -17.101 -3.070  1.00 17.28 ?  57  THR   B HG23 1 
ATOM   4785 N N    . ASN   B 1 58  ? 60.382 -17.152 -2.094  1.00 16.15 ?  58  ASN   B N    1 
ATOM   4786 C CA   . ASN   B 1 58  ? 61.581 -16.932 -1.288  1.00 19.11 ?  58  ASN   B CA   1 
ATOM   4787 C C    . ASN   B 1 58  ? 61.245 -16.214 0.019   1.00 16.82 ?  58  ASN   B C    1 
ATOM   4788 O O    . ASN   B 1 58  ? 61.982 -15.336 0.481   1.00 17.88 ?  58  ASN   B O    1 
ATOM   4789 C CB   . ASN   B 1 58  ? 62.668 -16.188 -2.072  1.00 27.08 ?  58  ASN   B CB   1 
ATOM   4790 C CG   . ASN   B 1 58  ? 64.034 -16.301 -1.423  1.00 35.82 ?  58  ASN   B CG   1 
ATOM   4791 O OD1  . ASN   B 1 58  ? 64.343 -17.297 -0.770  1.00 38.48 ?  58  ASN   B OD1  1 
ATOM   4792 N ND2  . ASN   B 1 58  ? 64.860 -15.275 -1.600  1.00 41.96 ?  58  ASN   B ND2  1 
ATOM   4793 H H    . ASN   B 1 58  ? 60.248 -17.977 -2.303  1.00 19.38 ?  58  ASN   B H    1 
ATOM   4794 H HA   . ASN   B 1 58  ? 61.945 -17.802 -1.059  1.00 22.95 ?  58  ASN   B HA   1 
ATOM   4795 H HB2  . ASN   B 1 58  ? 62.729 -16.565 -2.966  1.00 32.51 ?  58  ASN   B HB2  1 
ATOM   4796 H HB3  . ASN   B 1 58  ? 62.440 -15.250 -2.121  1.00 32.51 ?  58  ASN   B HB3  1 
ATOM   4797 H HD21 . ASN   B 1 58  ? 65.648 -15.290 -1.254  1.00 50.36 ?  58  ASN   B HD21 1 
ATOM   4798 H HD22 . ASN   B 1 58  ? 64.607 -14.595 -2.060  1.00 50.36 ?  58  ASN   B HD22 1 
ATOM   4799 N N    . ASN   B 1 59  ? 60.123 -16.603 0.625   1.00 15.61 ?  59  ASN   B N    1 
ATOM   4800 C CA   . ASN   B 1 59  ? 59.652 -16.140 1.932   1.00 15.74 ?  59  ASN   B CA   1 
ATOM   4801 C C    . ASN   B 1 59  ? 59.054 -14.735 1.879   1.00 15.01 ?  59  ASN   B C    1 
ATOM   4802 O O    . ASN   B 1 59  ? 58.629 -14.230 2.923   1.00 15.54 ?  59  ASN   B O    1 
ATOM   4803 C CB   . ASN   B 1 59  ? 60.724 -16.200 3.037   1.00 16.82 ?  59  ASN   B CB   1 
ATOM   4804 C CG   . ASN   B 1 59  ? 60.133 -16.361 4.418   1.00 17.91 ?  59  ASN   B CG   1 
ATOM   4805 O OD1  . ASN   B 1 59  ? 59.302 -17.236 4.646   1.00 18.08 ?  59  ASN   B OD1  1 
ATOM   4806 N ND2  . ASN   B 1 59  ? 60.554 -15.514 5.349   1.00 18.49 ?  59  ASN   B ND2  1 
ATOM   4807 H H    . ASN   B 1 59  ? 59.586 -17.185 0.278   1.00 18.74 ?  59  ASN   B H    1 
ATOM   4808 H HA   . ASN   B 1 59  ? 58.941 -16.740 2.211   1.00 18.90 ?  59  ASN   B HA   1 
ATOM   4809 H HB2  . ASN   B 1 59  ? 61.307 -16.958 2.880   1.00 20.20 ?  59  ASN   B HB2  1 
ATOM   4810 H HB3  . ASN   B 1 59  ? 61.232 -15.379 3.033   1.00 20.20 ?  59  ASN   B HB3  1 
ATOM   4811 H HD21 . ASN   B 1 59  ? 60.242 -15.565 6.152   1.00 22.20 ?  59  ASN   B HD21 1 
ATOM   4812 H HD22 . ASN   B 1 59  ? 61.133 -14.915 5.151   1.00 22.20 ?  59  ASN   B HD22 1 
ATOM   4813 N N    . ALA   B 1 60  ? 58.983 -14.096 0.707   1.00 15.06 ?  60  ALA   B N    1 
ATOM   4814 C CA   . ALA   B 1 60  ? 58.389 -12.763 0.635   1.00 14.92 ?  60  ALA   B CA   1 
ATOM   4815 C C    . ALA   B 1 60  ? 56.921 -12.788 1.037   1.00 14.19 ?  60  ALA   B C    1 
ATOM   4816 O O    . ALA   B 1 60  ? 56.416 -11.835 1.645   1.00 14.59 ?  60  ALA   B O    1 
ATOM   4817 C CB   . ALA   B 1 60  ? 58.549 -12.186 -0.772  1.00 15.72 ?  60  ALA   B CB   1 
ATOM   4818 H H    . ALA   B 1 60  ? 59.273 -14.411 -0.041  1.00 18.08 ?  60  ALA   B H    1 
ATOM   4819 H HA   . ALA   B 1 60  ? 58.856 -12.184 1.253   1.00 17.91 ?  60  ALA   B HA   1 
ATOM   4820 H HB1  . ALA   B 1 60  ? 58.150 -11.306 -0.795  1.00 18.87 ?  60  ALA   B HB1  1 
ATOM   4821 H HB2  . ALA   B 1 60  ? 59.496 -12.129 -0.984  1.00 18.87 ?  60  ALA   B HB2  1 
ATOM   4822 H HB3  . ALA   B 1 60  ? 58.105 -12.772 -1.406  1.00 18.87 ?  60  ALA   B HB3  1 
ATOM   4823 N N    . MET   B 1 61  ? 56.213 -13.865 0.693   1.00 13.60 ?  61  MET   B N    1 
ATOM   4824 C CA   . MET   B 1 61  ? 54.816 -13.981 1.082   1.00 13.17 ?  61  MET   B CA   1 
ATOM   4825 C C    . MET   B 1 61  ? 54.675 -13.985 2.602   1.00 13.40 ?  61  MET   B C    1 
ATOM   4826 O O    . MET   B 1 61  ? 53.779 -13.332 3.150   1.00 13.40 ?  61  MET   B O    1 
ATOM   4827 C CB   . MET   B 1 61  ? 54.235 -15.247 0.453   1.00 13.37 ?  61  MET   B CB   1 
ATOM   4828 C CG   . MET   B 1 61  ? 52.801 -15.544 0.878   1.00 13.42 ?  61  MET   B CG   1 
ATOM   4829 S SD   . MET   B 1 61  ? 52.160 -17.044 0.124   1.00 14.03 ?  61  MET   B SD   1 
ATOM   4830 C CE   . MET   B 1 61  ? 51.919 -16.485 -1.556  1.00 15.36 ?  61  MET   B CE   1 
ATOM   4831 H H    . MET   B 1 61  ? 56.516 -14.538 0.240   1.00 16.32 ?  61  MET   B H    1 
ATOM   4832 H HA   . MET   B 1 61  ? 54.328 -13.226 0.721   1.00 15.81 ?  61  MET   B HA   1 
ATOM   4833 H HB2  . MET   B 1 61  ? 54.240 -15.148 -0.514  1.00 16.06 ?  61  MET   B HB2  1 
ATOM   4834 H HB3  . MET   B 1 61  ? 54.782 -16.005 0.707   1.00 16.06 ?  61  MET   B HB3  1 
ATOM   4835 H HG2  . MET   B 1 61  ? 52.772 -15.660 1.840   1.00 16.11 ?  61  MET   B HG2  1 
ATOM   4836 H HG3  . MET   B 1 61  ? 52.234 -14.804 0.613   1.00 16.11 ?  61  MET   B HG3  1 
ATOM   4837 H HE1  . MET   B 1 61  ? 51.530 -17.208 -2.074  1.00 18.44 ?  61  MET   B HE1  1 
ATOM   4838 H HE2  . MET   B 1 61  ? 51.321 -15.722 -1.554  1.00 18.44 ?  61  MET   B HE2  1 
ATOM   4839 H HE3  . MET   B 1 61  ? 52.777 -16.234 -1.934  1.00 18.44 ?  61  MET   B HE3  1 
ATOM   4840 N N    . GLN   B 1 62  ? 55.556 -14.699 3.306   1.00 12.99 ?  62  GLN   B N    1 
ATOM   4841 C CA   . GLN   B 1 62  ? 55.449 -14.754 4.760   1.00 13.44 ?  62  GLN   B CA   1 
ATOM   4842 C C    . GLN   B 1 62  ? 55.737 -13.400 5.392   1.00 13.84 ?  62  GLN   B C    1 
ATOM   4843 O O    . GLN   B 1 62  ? 55.058 -12.994 6.341   1.00 14.37 ?  62  GLN   B O    1 
ATOM   4844 C CB   . GLN   B 1 62  ? 56.407 -15.801 5.327   1.00 13.96 ?  62  GLN   B CB   1 
ATOM   4845 C CG   . GLN   B 1 62  ? 56.198 -16.064 6.808   1.00 14.61 ?  62  GLN   B CG   1 
ATOM   4846 C CD   . GLN   B 1 62  ? 54.825 -16.654 7.068   1.00 14.18 ?  62  GLN   B CD   1 
ATOM   4847 O OE1  . GLN   B 1 62  ? 54.562 -17.802 6.723   1.00 14.42 ?  62  GLN   B OE1  1 
ATOM   4848 N NE2  . GLN   B 1 62  ? 53.922 -15.854 7.629   1.00 14.60 ?  62  GLN   B NE2  1 
ATOM   4849 H H    . GLN   B 1 62  ? 56.207 -15.154 2.970   1.00 15.60 ?  62  GLN   B H    1 
ATOM   4850 H HA   . GLN   B 1 62  ? 54.544 -15.014 4.998   1.00 16.14 ?  62  GLN   B HA   1 
ATOM   4851 H HB2  . GLN   B 1 62  ? 56.280 -16.638 4.854   1.00 16.76 ?  62  GLN   B HB2  1 
ATOM   4852 H HB3  . GLN   B 1 62  ? 57.319 -15.489 5.207   1.00 16.76 ?  62  GLN   B HB3  1 
ATOM   4853 H HG2  . GLN   B 1 62  ? 56.864 -16.702 7.116   1.00 17.54 ?  62  GLN   B HG2  1 
ATOM   4854 H HG3  . GLN   B 1 62  ? 56.275 -15.235 7.301   1.00 17.54 ?  62  GLN   B HG3  1 
ATOM   4855 H HE21 . GLN   B 1 62  ? 54.136 -15.051 7.848   1.00 17.53 ?  62  GLN   B HE21 1 
ATOM   4856 H HE22 . GLN   B 1 62  ? 53.130 -16.149 7.787   1.00 17.53 ?  62  GLN   B HE22 1 
ATOM   4857 N N    . VAL   B 1 63  ? 56.748 -12.691 4.892   1.00 14.58 ?  63  VAL   B N    1 
ATOM   4858 C CA   . VAL   B 1 63  ? 57.059 -11.375 5.443   1.00 15.56 ?  63  VAL   B CA   1 
ATOM   4859 C C    . VAL   B 1 63  ? 55.872 -10.437 5.260   1.00 14.68 ?  63  VAL   B C    1 
ATOM   4860 O O    . VAL   B 1 63  ? 55.467 -9.726  6.189   1.00 15.62 ?  63  VAL   B O    1 
ATOM   4861 C CB   . VAL   B 1 63  ? 58.349 -10.822 4.817   1.00 17.45 ?  63  VAL   B CB   1 
ATOM   4862 C CG1  . VAL   B 1 63  ? 58.573 -9.378  5.254   1.00 18.15 ?  63  VAL   B CG1  1 
ATOM   4863 C CG2  . VAL   B 1 63  ? 59.524 -11.684 5.226   1.00 18.25 ?  63  VAL   B CG2  1 
ATOM   4864 H H    . VAL   B 1 63  ? 57.255 -12.945 4.246   1.00 17.51 ?  63  VAL   B H    1 
ATOM   4865 H HA   . VAL   B 1 63  ? 57.212 -11.470 6.394   1.00 18.68 ?  63  VAL   B HA   1 
ATOM   4866 H HB   . VAL   B 1 63  ? 58.277 -10.844 3.851   1.00 20.95 ?  63  VAL   B HB   1 
ATOM   4867 H HG11 . VAL   B 1 63  ? 59.491 -9.133  5.072   1.00 21.78 ?  63  VAL   B HG11 1 
ATOM   4868 H HG12 . VAL   B 1 63  ? 57.970 -8.800  4.761   1.00 21.78 ?  63  VAL   B HG12 1 
ATOM   4869 H HG13 . VAL   B 1 63  ? 58.395 -9.307  6.207   1.00 21.78 ?  63  VAL   B HG13 1 
ATOM   4870 H HG21 . VAL   B 1 63  ? 60.335 -11.314 4.843   1.00 21.91 ?  63  VAL   B HG21 1 
ATOM   4871 H HG22 . VAL   B 1 63  ? 59.591 -11.686 6.196   1.00 21.91 ?  63  VAL   B HG22 1 
ATOM   4872 H HG23 . VAL   B 1 63  ? 59.385 -12.586 4.902   1.00 21.91 ?  63  VAL   B HG23 1 
ATOM   4873 N N    . GLU   B 1 64  ? 55.295 -10.427 4.057   1.00 14.54 ?  64  GLU   B N    1 
ATOM   4874 C CA   . GLU   B 1 64  ? 54.133 -9.588  3.787   1.00 13.94 ?  64  GLU   B CA   1 
ATOM   4875 C C    . GLU   B 1 64  ? 52.953 -9.991  4.666   1.00 13.71 ?  64  GLU   B C    1 
ATOM   4876 O O    . GLU   B 1 64  ? 52.213 -9.132  5.174   1.00 14.27 ?  64  GLU   B O    1 
ATOM   4877 C CB   . GLU   B 1 64  ? 53.771 -9.729  2.310   1.00 14.12 ?  64  GLU   B CB   1 
ATOM   4878 C CG   . GLU   B 1 64  ? 52.519 -8.986  1.887   1.00 14.73 ?  64  GLU   B CG   1 
ATOM   4879 C CD   . GLU   B 1 64  ? 51.974 -9.473  0.551   1.00 15.89 ?  64  GLU   B CD   1 
ATOM   4880 O OE1  . GLU   B 1 64  ? 52.152 -10.676 0.220   1.00 16.88 ?  64  GLU   B OE1  1 
ATOM   4881 O OE2  . GLU   B 1 64  ? 51.351 -8.647  -0.160  1.00 16.62 -1 64  GLU   B OE2  1 
ATOM   4882 H H    . GLU   B 1 64  ? 55.564 -10.890 3.380   1.00 17.46 ?  64  GLU   B H    1 
ATOM   4883 H HA   . GLU   B 1 64  ? 54.349 -8.661  3.964   1.00 16.74 ?  64  GLU   B HA   1 
ATOM   4884 H HB2  . GLU   B 1 64  ? 54.505 -9.376  1.774   1.00 16.96 ?  64  GLU   B HB2  1 
ATOM   4885 H HB3  . GLU   B 1 64  ? 53.643 -10.664 2.107   1.00 16.96 ?  64  GLU   B HB3  1 
ATOM   4886 H HG2  . GLU   B 1 64  ? 51.821 -9.114  2.553   1.00 17.68 ?  64  GLU   B HG2  1 
ATOM   4887 H HG3  . GLU   B 1 64  ? 52.720 -8.043  1.800   1.00 17.68 ?  64  GLU   B HG3  1 
ATOM   4888 N N    . SER   B 1 65  ? 52.774 -11.300 4.859   1.00 13.19 ?  65  SER   B N    1 
ATOM   4889 C CA   . SER   B 1 65  ? 51.668 -11.803 5.664   1.00 13.33 ?  65  SER   B CA   1 
ATOM   4890 C C    . SER   B 1 65  ? 51.807 -11.401 7.126   1.00 13.51 ?  65  SER   B C    1 
ATOM   4891 O O    . SER   B 1 65  ? 50.812 -11.027 7.765   1.00 13.85 ?  65  SER   B O    1 
ATOM   4892 C CB   . SER   B 1 65  ? 51.574 -13.323 5.537   1.00 13.54 ?  65  SER   B CB   1 
ATOM   4893 O OG   . SER   B 1 65  ? 51.238 -13.711 4.215   1.00 13.98 ?  65  SER   B OG   1 
ATOM   4894 H H    . SER   B 1 65  ? 53.284 -11.919 4.537   1.00 15.84 ?  65  SER   B H    1 
ATOM   4895 H HA   . SER   B 1 65  ? 50.840 -11.426 5.330   1.00 16.01 ?  65  SER   B HA   1 
ATOM   4896 H HB2  . SER   B 1 65  ? 52.431 -13.715 5.767   1.00 16.26 ?  65  SER   B HB2  1 
ATOM   4897 H HB3  . SER   B 1 65  ? 50.889 -13.648 6.142   1.00 16.26 ?  65  SER   B HB3  1 
ATOM   4898 H HG   . SER   B 1 65  ? 51.822 -13.421 3.676   1.00 16.79 ?  65  SER   B HG   1 
ATOM   4899 N N    . ASP   B 1 66  ? 53.016 -11.503 7.689   1.00 13.78 ?  66  ASP   B N    1 
ATOM   4900 C CA   . ASP   B 1 66  ? 53.202 -11.115 9.084   1.00 14.50 ?  66  ASP   B CA   1 
ATOM   4901 C C    . ASP   B 1 66  ? 52.890 -9.639  9.289   1.00 14.78 ?  66  ASP   B C    1 
ATOM   4902 O O    . ASP   B 1 66  ? 52.317 -9.251  10.314  1.00 15.15 ?  66  ASP   B O    1 
ATOM   4903 C CB   . ASP   B 1 66  ? 54.633 -11.420 9.529   1.00 16.34 ?  66  ASP   B CB   1 
ATOM   4904 C CG   . ASP   B 1 66  ? 54.897 -12.907 9.688   1.00 17.94 ?  66  ASP   B CG   1 
ATOM   4905 O OD1  . ASP   B 1 66  ? 53.939 -13.712 9.633   1.00 18.49 ?  66  ASP   B OD1  1 
ATOM   4906 O OD2  . ASP   B 1 66  ? 56.078 -13.279 9.875   1.00 20.84 -1 66  ASP   B OD2  1 
ATOM   4907 H H    . ASP   B 1 66  ? 53.721 -11.803 7.298   1.00 16.54 ?  66  ASP   B H    1 
ATOM   4908 H HA   . ASP   B 1 66  ? 52.604 -11.626 9.647   1.00 17.41 ?  66  ASP   B HA   1 
ATOM   4909 H HB2  . ASP   B 1 66  ? 55.256 -11.085 8.865   1.00 19.62 ?  66  ASP   B HB2  1 
ATOM   4910 H HB3  . ASP   B 1 66  ? 54.803 -10.991 10.385  1.00 19.62 ?  66  ASP   B HB3  1 
ATOM   4911 N N    . ASP   B 1 67  ? 53.264 -8.795  8.328   1.00 14.50 ?  67  ASP   B N    1 
ATOM   4912 C CA   . ASP   B 1 67  ? 52.921 -7.382  8.422   1.00 15.18 ?  67  ASP   B CA   1 
ATOM   4913 C C    . ASP   B 1 67  ? 51.411 -7.172  8.336   1.00 15.04 ?  67  ASP   B C    1 
ATOM   4914 O O    . ASP   B 1 67  ? 50.843 -6.369  9.086   1.00 15.62 ?  67  ASP   B O    1 
ATOM   4915 C CB   . ASP   B 1 67  ? 53.642 -6.610  7.325   1.00 16.74 ?  67  ASP   B CB   1 
ATOM   4916 C CG   . ASP   B 1 67  ? 53.226 -5.173  7.286   1.00 18.55 ?  67  ASP   B CG   1 
ATOM   4917 O OD1  . ASP   B 1 67  ? 53.722 -4.378  8.119   1.00 19.72 ?  67  ASP   B OD1  1 
ATOM   4918 O OD2  . ASP   B 1 67  ? 52.372 -4.851  6.441   1.00 19.90 -1 67  ASP   B OD2  1 
ATOM   4919 H H    . ASP   B 1 67  ? 53.718 -9.010  7.629   1.00 17.41 ?  67  ASP   B H    1 
ATOM   4920 H HA   . ASP   B 1 67  ? 53.228 -7.035  9.274   1.00 18.23 ?  67  ASP   B HA   1 
ATOM   4921 H HB2  . ASP   B 1 67  ? 54.600 -6.633  7.484   1.00 20.10 ?  67  ASP   B HB2  1 
ATOM   4922 H HB3  . ASP   B 1 67  ? 53.442 -7.012  6.462   1.00 20.10 ?  67  ASP   B HB3  1 
ATOM   4923 N N    . TYR   B 1 68  ? 50.738 -7.898  7.440   1.00 14.62 ?  68  TYR   B N    1 
ATOM   4924 C CA   . TYR   B 1 68  ? 49.281 -7.818  7.365   1.00 15.50 ?  68  TYR   B CA   1 
ATOM   4925 C C    . TYR   B 1 68  ? 48.645 -8.164  8.706   1.00 15.21 ?  68  TYR   B C    1 
ATOM   4926 O O    . TYR   B 1 68  ? 47.717 -7.481  9.158   1.00 15.81 ?  68  TYR   B O    1 
ATOM   4927 C CB   . TYR   B 1 68  ? 48.744 -8.740  6.264   1.00 16.55 ?  68  TYR   B CB   1 
ATOM   4928 C CG   . TYR   B 1 68  ? 47.238 -8.890  6.327   1.00 17.74 ?  68  TYR   B CG   1 
ATOM   4929 C CD1  . TYR   B 1 68  ? 46.646 -9.849  7.145   1.00 18.49 ?  68  TYR   B CD1  1 
ATOM   4930 C CD2  . TYR   B 1 68  ? 46.409 -8.051  5.605   1.00 19.00 ?  68  TYR   B CD2  1 
ATOM   4931 C CE1  . TYR   B 1 68  ? 45.282 -9.971  7.231   1.00 19.72 ?  68  TYR   B CE1  1 
ATOM   4932 C CE2  . TYR   B 1 68  ? 45.033 -8.175  5.680   1.00 19.77 ?  68  TYR   B CE2  1 
ATOM   4933 C CZ   . TYR   B 1 68  ? 44.488 -9.131  6.497   1.00 19.98 ?  68  TYR   B CZ   1 
ATOM   4934 O OH   . TYR   B 1 68  ? 43.121 -9.241  6.584   1.00 21.52 ?  68  TYR   B OH   1 
ATOM   4935 H H    . TYR   B 1 68  ? 51.098 -8.444  6.877   1.00 17.56 ?  68  TYR   B H    1 
ATOM   4936 H HA   . TYR   B 1 68  ? 49.034 -6.910  7.146   1.00 18.61 ?  68  TYR   B HA   1 
ATOM   4937 H HB2  . TYR   B 1 68  ? 48.968 -8.365  5.401   1.00 19.87 ?  68  TYR   B HB2  1 
ATOM   4938 H HB3  . TYR   B 1 68  ? 49.137 -9.619  6.364   1.00 19.87 ?  68  TYR   B HB3  1 
ATOM   4939 H HD1  . TYR   B 1 68  ? 47.184 -10.424 7.644   1.00 22.20 ?  68  TYR   B HD1  1 
ATOM   4940 H HD2  . TYR   B 1 68  ? 46.781 -7.396  5.065   1.00 22.80 ?  68  TYR   B HD2  1 
ATOM   4941 H HE1  . TYR   B 1 68  ? 44.897 -10.631 7.772   1.00 23.67 ?  68  TYR   B HE1  1 
ATOM   4942 H HE2  . TYR   B 1 68  ? 44.480 -7.607  5.194   1.00 23.74 ?  68  TYR   B HE2  1 
ATOM   4943 H HH   . TYR   B 1 68  ? 42.738 -8.685  6.076   1.00 25.83 ?  68  TYR   B HH   1 
ATOM   4944 N N    . ILE   B 1 69  ? 49.125 -9.231  9.351   1.00 14.65 ?  69  ILE   B N    1 
ATOM   4945 C CA   . ILE   B 1 69  ? 48.563 -9.661  10.628  1.00 15.30 ?  69  ILE   B CA   1 
ATOM   4946 C C    . ILE   B 1 69  ? 48.819 -8.619  11.710  1.00 15.24 ?  69  ILE   B C    1 
ATOM   4947 O O    . ILE   B 1 69  ? 47.950 -8.346  12.544  1.00 15.52 ?  69  ILE   B O    1 
ATOM   4948 C CB   . ILE   B 1 69  ? 49.139 -11.036 11.019  1.00 16.23 ?  69  ILE   B CB   1 
ATOM   4949 C CG1  . ILE   B 1 69  ? 48.610 -12.144 10.098  1.00 16.71 ?  69  ILE   B CG1  1 
ATOM   4950 C CG2  . ILE   B 1 69  ? 48.854 -11.345 12.479  1.00 17.29 ?  69  ILE   B CG2  1 
ATOM   4951 C CD1  . ILE   B 1 69  ? 47.142 -12.457 10.273  1.00 16.79 ?  69  ILE   B CD1  1 
ATOM   4952 H H    . ILE   B 1 69  ? 49.771 -9.722  9.069   1.00 17.59 ?  69  ILE   B H    1 
ATOM   4953 H HA   . ILE   B 1 69  ? 47.604 -9.758  10.532  1.00 18.37 ?  69  ILE   B HA   1 
ATOM   4954 H HB   . ILE   B 1 69  ? 50.103 -10.996 10.909  1.00 19.49 ?  69  ILE   B HB   1 
ATOM   4955 H HG12 . ILE   B 1 69  ? 48.748 -11.872 9.176   1.00 20.06 ?  69  ILE   B HG12 1 
ATOM   4956 H HG13 . ILE   B 1 69  ? 49.112 -12.958 10.273  1.00 20.06 ?  69  ILE   B HG13 1 
ATOM   4957 H HG21 . ILE   B 1 69  ? 48.979 -12.297 12.626  1.00 20.75 ?  69  ILE   B HG21 1 
ATOM   4958 H HG22 . ILE   B 1 69  ? 49.471 -10.846 13.037  1.00 20.75 ?  69  ILE   B HG22 1 
ATOM   4959 H HG23 . ILE   B 1 69  ? 47.941 -11.098 12.683  1.00 20.75 ?  69  ILE   B HG23 1 
ATOM   4960 H HD11 . ILE   B 1 69  ? 46.898 -13.160 9.651   1.00 20.15 ?  69  ILE   B HD11 1 
ATOM   4961 H HD12 . ILE   B 1 69  ? 46.988 -12.759 11.183  1.00 20.15 ?  69  ILE   B HD12 1 
ATOM   4962 H HD13 . ILE   B 1 69  ? 46.622 -11.662 10.093  1.00 20.15 ?  69  ILE   B HD13 1 
ATOM   4963 N N    . ALA   B 1 70  ? 50.018 -8.038  11.736  1.00 15.19 ?  70  ALA   B N    1 
ATOM   4964 C CA   . ALA   B 1 70  ? 50.300 -7.007  12.729  1.00 14.82 ?  70  ALA   B CA   1 
ATOM   4965 C C    . ALA   B 1 70  ? 49.313 -5.855  12.612  1.00 15.64 ?  70  ALA   B C    1 
ATOM   4966 O O    . ALA   B 1 70  ? 48.872 -5.303  13.623  1.00 15.73 ?  70  ALA   B O    1 
ATOM   4967 C CB   . ALA   B 1 70  ? 51.740 -6.516  12.574  1.00 15.05 ?  70  ALA   B CB   1 
ATOM   4968 H H    . ALA   B 1 70  ? 50.663 -8.221  11.207  1.00 18.23 ?  70  ALA   B H    1 
ATOM   4969 H HA   . ALA   B 1 70  ? 50.212 -7.391  13.619  1.00 17.79 ?  70  ALA   B HA   1 
ATOM   4970 H HB1  . ALA   B 1 70  ? 51.928 -5.862  13.266  1.00 18.07 ?  70  ALA   B HB1  1 
ATOM   4971 H HB2  . ALA   B 1 70  ? 52.344 -7.272  12.664  1.00 18.07 ?  70  ALA   B HB2  1 
ATOM   4972 H HB3  . ALA   B 1 70  ? 51.844 -6.115  11.698  1.00 18.07 ?  70  ALA   B HB3  1 
ATOM   4973 N N    . THR   B 1 71  ? 48.941 -5.491  11.386  1.00 15.80 ?  71  THR   B N    1 
ATOM   4974 C CA   . THR   B 1 71  ? 48.054 -4.352  11.173  1.00 16.50 ?  71  THR   B CA   1 
ATOM   4975 C C    . THR   B 1 71  ? 46.586 -4.710  11.386  1.00 17.20 ?  71  THR   B C    1 
ATOM   4976 O O    . THR   B 1 71  ? 45.816 -3.889  11.901  1.00 18.82 ?  71  THR   B O    1 
ATOM   4977 C CB   . THR   B 1 71  ? 48.278 -3.793  9.766   1.00 18.33 ?  71  THR   B CB   1 
ATOM   4978 O OG1  . THR   B 1 71  ? 49.614 -3.288  9.661   1.00 20.25 ?  71  THR   B OG1  1 
ATOM   4979 C CG2  . THR   B 1 71  ? 47.284 -2.689  9.446   1.00 19.50 ?  71  THR   B CG2  1 
ATOM   4980 H H    . THR   B 1 71  ? 49.194 -5.885  10.668  1.00 18.96 ?  71  THR   B H    1 
ATOM   4981 H HA   . THR   B 1 71  ? 48.284 -3.655  11.807  1.00 19.81 ?  71  THR   B HA   1 
ATOM   4982 H HB   . THR   B 1 71  ? 48.168 -4.501  9.115   1.00 22.01 ?  71  THR   B HB   1 
ATOM   4983 H HG1  . THR   B 1 71  ? 49.749 -2.963  8.894   1.00 24.31 ?  71  THR   B HG1  1 
ATOM   4984 H HG21 . THR   B 1 71  ? 47.592 -2.179  8.677   1.00 23.41 ?  71  THR   B HG21 1 
ATOM   4985 H HG22 . THR   B 1 71  ? 46.418 -3.068  9.245   1.00 23.41 ?  71  THR   B HG22 1 
ATOM   4986 H HG23 . THR   B 1 71  ? 47.203 -2.086  10.204  1.00 23.41 ?  71  THR   B HG23 1 
ATOM   4987 N N    . ASN   B 1 72  ? 46.183 -5.921  10.999  1.00 16.70 ?  72  ASN   B N    1 
ATOM   4988 C CA   . ASN   B 1 72  ? 44.777 -6.267  10.877  1.00 16.98 ?  72  ASN   B CA   1 
ATOM   4989 C C    . ASN   B 1 72  ? 44.307 -7.361  11.819  1.00 17.61 ?  72  ASN   B C    1 
ATOM   4990 O O    . ASN   B 1 72  ? 43.092 -7.521  11.985  1.00 18.72 ?  72  ASN   B O    1 
ATOM   4991 C CB   . ASN   B 1 72  ? 44.466 -6.692  9.436   1.00 17.88 ?  72  ASN   B CB   1 
ATOM   4992 C CG   . ASN   B 1 72  ? 44.759 -5.595  8.441   1.00 18.98 ?  72  ASN   B CG   1 
ATOM   4993 O OD1  . ASN   B 1 72  ? 45.775 -5.614  7.747   1.00 20.44 ?  72  ASN   B OD1  1 
ATOM   4994 N ND2  . ASN   B 1 72  ? 43.887 -4.608  8.393   1.00 20.62 ?  72  ASN   B ND2  1 
ATOM   4995 H H    . ASN   B 1 72  ? 46.721 -6.570  10.794  1.00 20.05 ?  72  ASN   B H    1 
ATOM   4996 H HA   . ASN   B 1 72  ? 44.255 -5.476  11.065  1.00 20.39 ?  72  ASN   B HA   1 
ATOM   4997 H HB2  . ASN   B 1 72  ? 45.010 -7.465  9.207   1.00 21.47 ?  72  ASN   B HB2  1 
ATOM   4998 H HB3  . ASN   B 1 72  ? 43.525 -6.917  9.370   1.00 21.47 ?  72  ASN   B HB3  1 
ATOM   4999 H HD21 . ASN   B 1 72  ? 44.003 -3.959  7.841   1.00 24.75 ?  72  ASN   B HD21 1 
ATOM   5000 H HD22 . ASN   B 1 72  ? 43.187 -4.626  8.894   1.00 24.75 ?  72  ASN   B HD22 1 
ATOM   5001 N N    . GLY   B 1 73  ? 45.211 -8.110  12.437  1.00 17.11 ?  73  GLY   B N    1 
ATOM   5002 C CA   . GLY   B 1 73  ? 44.819 -9.246  13.232  1.00 16.56 ?  73  GLY   B CA   1 
ATOM   5003 C C    . GLY   B 1 73  ? 44.465 -10.434 12.365  1.00 15.14 ?  73  GLY   B C    1 
ATOM   5004 O O    . GLY   B 1 73  ? 44.455 -10.362 11.135  1.00 15.41 ?  73  GLY   B O    1 
ATOM   5005 H H    . GLY   B 1 73  ? 46.062 -7.968  12.415  1.00 20.55 ?  73  GLY   B H    1 
ATOM   5006 H HA2  . GLY   B 1 73  ? 45.550 -9.492  13.824  1.00 19.88 ?  73  GLY   B HA2  1 
ATOM   5007 H HA3  . GLY   B 1 73  ? 44.050 -9.012  13.777  1.00 19.88 ?  73  GLY   B HA3  1 
ATOM   5008 N N    . PRO   B 1 74  ? 44.149 -11.552 13.007  1.00 15.67 ?  74  PRO   B N    1 
ATOM   5009 C CA   . PRO   B 1 74  ? 43.909 -12.790 12.267  1.00 15.26 ?  74  PRO   B CA   1 
ATOM   5010 C C    . PRO   B 1 74  ? 42.607 -12.741 11.483  1.00 14.45 ?  74  PRO   B C    1 
ATOM   5011 O O    . PRO   B 1 74  ? 41.666 -12.007 11.805  1.00 15.65 ?  74  PRO   B O    1 
ATOM   5012 C CB   . PRO   B 1 74  ? 43.842 -13.847 13.374  1.00 16.85 ?  74  PRO   B CB   1 
ATOM   5013 C CG   . PRO   B 1 74  ? 43.381 -13.094 14.576  1.00 18.32 ?  74  PRO   B CG   1 
ATOM   5014 C CD   . PRO   B 1 74  ? 44.019 -11.739 14.461  1.00 17.50 ?  74  PRO   B CD   1 
ATOM   5015 H HA   . PRO   B 1 74  ? 44.657 -12.981 11.670  1.00 18.33 ?  74  PRO   B HA   1 
ATOM   5016 H HB2  . PRO   B 1 74  ? 43.210 -14.537 13.128  1.00 20.23 ?  74  PRO   B HB2  1 
ATOM   5017 H HB3  . PRO   B 1 74  ? 44.727 -14.226 13.521  1.00 20.23 ?  74  PRO   B HB3  1 
ATOM   5018 H HG2  . PRO   B 1 74  ? 42.414 -13.022 14.559  1.00 21.99 ?  74  PRO   B HG2  1 
ATOM   5019 H HG3  . PRO   B 1 74  ? 43.679 -13.548 15.378  1.00 21.99 ?  74  PRO   B HG3  1 
ATOM   5020 H HD2  . PRO   B 1 74  ? 43.436 -11.059 14.843  1.00 21.01 ?  74  PRO   B HD2  1 
ATOM   5021 H HD3  . PRO   B 1 74  ? 44.890 -11.736 14.887  1.00 21.01 ?  74  PRO   B HD3  1 
ATOM   5022 N N    . LEU   B 1 75  ? 42.575 -13.554 10.432  1.00 13.79 ?  75  LEU   B N    1 
ATOM   5023 C CA   . LEU   B 1 75  ? 41.364 -13.773 9.668   1.00 13.72 ?  75  LEU   B CA   1 
ATOM   5024 C C    . LEU   B 1 75  ? 40.386 -14.626 10.473  1.00 13.94 ?  75  LEU   B C    1 
ATOM   5025 O O    . LEU   B 1 75  ? 40.722 -15.187 11.519  1.00 15.48 ?  75  LEU   B O    1 
ATOM   5026 C CB   . LEU   B 1 75  ? 41.689 -14.489 8.357   1.00 13.85 ?  75  LEU   B CB   1 
ATOM   5027 C CG   . LEU   B 1 75  ? 42.513 -13.732 7.314   1.00 16.18 ?  75  LEU   B CG   1 
ATOM   5028 C CD1  . LEU   B 1 75  ? 42.662 -14.555 6.034   1.00 17.32 ?  75  LEU   B CD1  1 
ATOM   5029 C CD2  . LEU   B 1 75  ? 41.920 -12.386 7.004   1.00 19.62 ?  75  LEU   B CD2  1 
ATOM   5030 H H    . LEU   B 1 75  ? 43.256 -13.996 10.136  1.00 16.56 ?  75  LEU   B H    1 
ATOM   5031 H HA   . LEU   B 1 75  ? 40.941 -12.925 9.465   1.00 16.47 ?  75  LEU   B HA   1 
ATOM   5032 H HB2  . LEU   B 1 75  ? 42.181 -15.299 8.569   1.00 16.63 ?  75  LEU   B HB2  1 
ATOM   5033 H HB3  . LEU   B 1 75  ? 40.853 -14.732 7.928   1.00 16.63 ?  75  LEU   B HB3  1 
ATOM   5034 H HG   . LEU   B 1 75  ? 43.406 -13.588 7.668   1.00 19.42 ?  75  LEU   B HG   1 
ATOM   5035 H HD11 . LEU   B 1 75  ? 43.198 -14.052 5.394   1.00 20.79 ?  75  LEU   B HD11 1 
ATOM   5036 H HD12 . LEU   B 1 75  ? 43.107 -15.392 6.243   1.00 20.79 ?  75  LEU   B HD12 1 
ATOM   5037 H HD13 . LEU   B 1 75  ? 41.785 -14.728 5.663   1.00 20.79 ?  75  LEU   B HD13 1 
ATOM   5038 H HD21 . LEU   B 1 75  ? 42.393 -11.996 6.253   1.00 23.56 ?  75  LEU   B HD21 1 
ATOM   5039 H HD22 . LEU   B 1 75  ? 40.984 -12.501 6.785   1.00 23.56 ?  75  LEU   B HD22 1 
ATOM   5040 H HD23 . LEU   B 1 75  ? 42.011 -11.816 7.784   1.00 23.56 ?  75  LEU   B HD23 1 
ATOM   5041 N N    . LYS   B 1 76  ? 39.157 -14.718 9.967   1.00 15.05 ?  76  LYS   B N    1 
ATOM   5042 C CA   . LYS   B 1 76  ? 38.177 -15.683 10.446  1.00 16.55 ?  76  LYS   B CA   1 
ATOM   5043 C C    . LYS   B 1 76  ? 38.264 -16.952 9.604   1.00 15.27 ?  76  LYS   B C    1 
ATOM   5044 O O    . LYS   B 1 76  ? 38.527 -16.894 8.402   1.00 14.90 ?  76  LYS   B O    1 
ATOM   5045 C CB   . LYS   B 1 76  ? 36.755 -15.123 10.278  1.00 18.72 ?  76  LYS   B CB   1 
ATOM   5046 C CG   . LYS   B 1 76  ? 36.484 -13.725 10.858  1.00 21.17 ?  76  LYS   B CG   1 
ATOM   5047 C CD   . LYS   B 1 76  ? 35.076 -13.215 10.495  1.00 22.89 ?  76  LYS   B CD   1 
ATOM   5048 C CE   . LYS   B 1 76  ? 34.774 -11.877 11.155  1.00 24.98 ?  76  LYS   B CE   1 
ATOM   5049 N NZ   . LYS   B 1 76  ? 33.497 -11.280 10.675  1.00 25.78 ?  76  LYS   B NZ   1 
ATOM   5050 H H    . LYS   B 1 76  ? 38.865 -14.223 9.331   1.00 18.07 ?  76  LYS   B H    1 
ATOM   5051 H HA   . LYS   B 1 76  ? 38.332 -15.902 11.379  1.00 19.87 ?  76  LYS   B HA   1 
ATOM   5052 H HB2  . LYS   B 1 76  ? 36.558 -15.080 9.329   1.00 22.47 ?  76  LYS   B HB2  1 
ATOM   5053 H HB3  . LYS   B 1 76  ? 36.135 -15.733 10.707  1.00 22.47 ?  76  LYS   B HB3  1 
ATOM   5054 H HG2  . LYS   B 1 76  ? 36.556 -13.761 11.825  1.00 25.42 ?  76  LYS   B HG2  1 
ATOM   5055 H HG3  . LYS   B 1 76  ? 37.136 -13.099 10.499  1.00 25.42 ?  76  LYS   B HG3  1 
ATOM   5056 H HD2  . LYS   B 1 76  ? 35.017 -13.101 9.533   1.00 27.47 ?  76  LYS   B HD2  1 
ATOM   5057 H HD3  . LYS   B 1 76  ? 34.417 -13.860 10.796  1.00 27.47 ?  76  LYS   B HD3  1 
ATOM   5058 H HE2  . LYS   B 1 76  ? 34.705 -12.007 12.113  1.00 29.99 ?  76  LYS   B HE2  1 
ATOM   5059 H HE3  . LYS   B 1 76  ? 35.491 -11.256 10.953  1.00 29.99 ?  76  LYS   B HE3  1 
ATOM   5060 H HZ1  . LYS   B 1 76  ? 33.351 -10.500 11.081  1.00 30.94 ?  76  LYS   B HZ1  1 
ATOM   5061 H HZ2  . LYS   B 1 76  ? 33.533 -11.143 9.795   1.00 30.94 ?  76  LYS   B HZ2  1 
ATOM   5062 H HZ3  . LYS   B 1 76  ? 32.816 -11.827 10.853  1.00 30.94 ?  76  LYS   B HZ3  1 
ATOM   5063 N N    . VAL   B 1 77  ? 38.015 -18.107 10.233  1.00 15.48 ?  77  VAL   B N    1 
ATOM   5064 C CA   . VAL   B 1 77  ? 37.803 -19.318 9.448   1.00 15.46 ?  77  VAL   B CA   1 
ATOM   5065 C C    . VAL   B 1 77  ? 36.612 -19.081 8.532   1.00 14.17 ?  77  VAL   B C    1 
ATOM   5066 O O    . VAL   B 1 77  ? 35.545 -18.637 8.978   1.00 14.56 ?  77  VAL   B O    1 
ATOM   5067 C CB   . VAL   B 1 77  ? 37.601 -20.541 10.357  1.00 16.82 ?  77  VAL   B CB   1 
ATOM   5068 C CG1  . VAL   B 1 77  ? 37.334 -21.785 9.510   1.00 17.78 ?  77  VAL   B CG1  1 
ATOM   5069 C CG2  . VAL   B 1 77  ? 38.823 -20.763 11.247  1.00 18.48 ?  77  VAL   B CG2  1 
ATOM   5070 H H    . VAL   B 1 77  ? 37.966 -18.208 11.083  1.00 18.59 ?  77  VAL   B H    1 
ATOM   5071 H HA   . VAL   B 1 77  ? 38.576 -19.480 8.893   1.00 18.56 ?  77  VAL   B HA   1 
ATOM   5072 H HB   . VAL   B 1 77  ? 36.829 -20.394 10.929  1.00 20.20 ?  77  VAL   B HB   1 
ATOM   5073 H HG11 . VAL   B 1 77  ? 37.374 -22.569 10.082  1.00 21.35 ?  77  VAL   B HG11 1 
ATOM   5074 H HG12 . VAL   B 1 77  ? 36.451 -21.717 9.111   1.00 21.35 ?  77  VAL   B HG12 1 
ATOM   5075 H HG13 . VAL   B 1 77  ? 38.008 -21.846 8.818   1.00 21.35 ?  77  VAL   B HG13 1 
ATOM   5076 H HG21 . VAL   B 1 77  ? 38.684 -21.564 11.773  1.00 22.18 ?  77  VAL   B HG21 1 
ATOM   5077 H HG22 . VAL   B 1 77  ? 39.602 -20.862 10.683  1.00 22.18 ?  77  VAL   B HG22 1 
ATOM   5078 H HG23 . VAL   B 1 77  ? 38.926 -19.995 11.830  1.00 22.18 ?  77  VAL   B HG23 1 
ATOM   5079 N N    . GLY   B 1 78  ? 36.795 -19.350 7.245   1.00 13.67 ?  78  GLY   B N    1 
ATOM   5080 C CA   . GLY   B 1 78  ? 35.819 -19.035 6.229   1.00 13.45 ?  78  GLY   B CA   1 
ATOM   5081 C C    . GLY   B 1 78  ? 36.068 -17.723 5.521   1.00 13.19 ?  78  GLY   B C    1 
ATOM   5082 O O    . GLY   B 1 78  ? 35.392 -17.441 4.527   1.00 13.81 ?  78  GLY   B O    1 
ATOM   5083 H H    . GLY   B 1 78  ? 37.502 -19.724 6.932   1.00 16.41 ?  78  GLY   B H    1 
ATOM   5084 H HA2  . GLY   B 1 78  ? 35.809 -19.732 5.565   1.00 16.15 ?  78  GLY   B HA2  1 
ATOM   5085 H HA3  . GLY   B 1 78  ? 34.937 -18.986 6.637   1.00 16.15 ?  78  GLY   B HA3  1 
ATOM   5086 N N    . GLY   B 1 79  ? 37.012 -16.914 6.012   1.00 13.41 ?  79  GLY   B N    1 
ATOM   5087 C CA   . GLY   B 1 79  ? 37.311 -15.621 5.435   1.00 12.99 ?  79  GLY   B CA   1 
ATOM   5088 C C    . GLY   B 1 79  ? 38.536 -15.651 4.534   1.00 12.80 ?  79  GLY   B C    1 
ATOM   5089 O O    . GLY   B 1 79  ? 39.148 -16.689 4.286   1.00 13.24 ?  79  GLY   B O    1 
ATOM   5090 H H    . GLY   B 1 79  ? 37.501 -17.100 6.693   1.00 16.10 ?  79  GLY   B H    1 
ATOM   5091 H HA2  . GLY   B 1 79  ? 36.554 -15.314 4.909   1.00 15.60 ?  79  GLY   B HA2  1 
ATOM   5092 H HA3  . GLY   B 1 79  ? 37.468 -14.976 6.145   1.00 15.60 ?  79  GLY   B HA3  1 
ATOM   5093 N N    . SER   B 1 80  ? 38.902 -14.459 4.056   1.00 12.73 ?  80  SER   B N    1 
ATOM   5094 C CA   . SER   B 1 80  ? 40.007 -14.327 3.119   1.00 12.82 ?  80  SER   B CA   1 
ATOM   5095 C C    . SER   B 1 80  ? 40.587 -12.925 3.180   1.00 12.58 ?  80  SER   B C    1 
ATOM   5096 O O    . SER   B 1 80  ? 39.978 -11.994 3.708   1.00 13.79 ?  80  SER   B O    1 
ATOM   5097 C CB   . SER   B 1 80  ? 39.566 -14.608 1.679   1.00 12.92 ?  80  SER   B CB   1 
ATOM   5098 O OG   . SER   B 1 80  ? 38.712 -13.589 1.188   1.00 14.15 ?  80  SER   B OG   1 
ATOM   5099 H H    . SER   B 1 80  ? 38.531 -13.713 4.264   1.00 15.29 ?  80  SER   B H    1 
ATOM   5100 H HA   . SER   B 1 80  ? 40.699 -14.955 3.360   1.00 15.39 ?  80  SER   B HA   1 
ATOM   5101 H HB2  . SER   B 1 80  ? 40.349 -14.653 1.109   1.00 15.51 ?  80  SER   B HB2  1 
ATOM   5102 H HB3  . SER   B 1 80  ? 39.088 -15.450 1.654   1.00 15.51 ?  80  SER   B HB3  1 
ATOM   5103 H HG   . SER   B 1 80  ? 38.025 -13.531 1.676   1.00 16.99 ?  80  SER   B HG   1 
ATOM   5104 N N    . CYS   B 1 81  ? 41.768 -12.781 2.589   1.00 12.13 ?  81  CYS   B N    1 
ATOM   5105 C CA   . CYS   B 1 81  ? 42.315 -11.470 2.279   1.00 12.49 ?  81  CYS   B CA   1 
ATOM   5106 C C    . CYS   B 1 81  ? 43.082 -11.557 0.968   1.00 11.71 ?  81  CYS   B C    1 
ATOM   5107 O O    . CYS   B 1 81  ? 43.583 -12.621 0.585   1.00 13.09 ?  81  CYS   B O    1 
ATOM   5108 C CB   . CYS   B 1 81  ? 43.207 -10.926 3.404   1.00 13.44 ?  81  CYS   B CB   1 
ATOM   5109 S SG   . CYS   B 1 81  ? 44.724 -11.861 3.665   1.00 13.88 ?  81  CYS   B SG   1 
ATOM   5110 H H    . CYS   B 1 81  ? 42.277 -13.435 2.347   1.00 14.56 ?  81  CYS   B H    1 
ATOM   5111 H HA   . CYS   B 1 81  ? 41.582 -10.845 2.157   1.00 14.99 ?  81  CYS   B HA   1 
ATOM   5112 H HB2  . CYS   B 1 81  ? 43.461 -10.017 3.191   1.00 16.13 ?  81  CYS   B HB2  1 
ATOM   5113 H HB3  . CYS   B 1 81  ? 42.704 -10.940 4.235   1.00 16.13 ?  81  CYS   B HB3  1 
ATOM   5114 H HG   . CYS   B 1 81  ? 45.341 -11.363 4.566   1.00 16.67 ?  81  CYS   B HG   1 
ATOM   5115 N N    . VAL   B 1 82  ? 43.194 -10.412 0.300   1.00 12.09 ?  82  VAL   B N    1 
ATOM   5116 C CA   . VAL   B 1 82  ? 43.956 -10.289 -0.937  1.00 12.55 ?  82  VAL   B CA   1 
ATOM   5117 C C    . VAL   B 1 82  ? 45.292 -9.645  -0.618  1.00 12.63 ?  82  VAL   B C    1 
ATOM   5118 O O    . VAL   B 1 82  ? 45.336 -8.527  -0.085  1.00 13.85 ?  82  VAL   B O    1 
ATOM   5119 C CB   . VAL   B 1 82  ? 43.206 -9.451  -1.985  1.00 13.71 ?  82  VAL   B CB   1 
ATOM   5120 C CG1  . VAL   B 1 82  ? 44.055 -9.316  -3.247  1.00 15.03 ?  82  VAL   B CG1  1 
ATOM   5121 C CG2  . VAL   B 1 82  ? 41.850 -10.047 -2.303  1.00 15.18 ?  82  VAL   B CG2  1 
ATOM   5122 H H    . VAL   B 1 82  ? 42.820 -9.672  0.545   1.00 14.52 ?  82  VAL   B H    1 
ATOM   5123 H HA   . VAL   B 1 82  ? 44.117 -11.168 -1.309  1.00 15.07 ?  82  VAL   B HA   1 
ATOM   5124 H HB   . VAL   B 1 82  ? 43.065 -8.558  -1.634  1.00 16.46 ?  82  VAL   B HB   1 
ATOM   5125 H HG11 . VAL   B 1 82  ? 43.497 -9.004  -3.976  1.00 18.05 ?  82  VAL   B HG11 1 
ATOM   5126 H HG12 . VAL   B 1 82  ? 44.771 -8.677  -3.087  1.00 18.05 ?  82  VAL   B HG12 1 
ATOM   5127 H HG13 . VAL   B 1 82  ? 44.433 -10.182 -3.470  1.00 18.05 ?  82  VAL   B HG13 1 
ATOM   5128 H HG21 . VAL   B 1 82  ? 41.423 -9.513  -2.994  1.00 18.23 ?  82  VAL   B HG21 1 
ATOM   5129 H HG22 . VAL   B 1 82  ? 41.971 -10.957 -2.620  1.00 18.23 ?  82  VAL   B HG22 1 
ATOM   5130 H HG23 . VAL   B 1 82  ? 41.308 -10.044 -1.501  1.00 18.23 ?  82  VAL   B HG23 1 
ATOM   5131 N N    . LEU   B 1 83  ? 46.374 -10.321 -0.992  1.00 12.52 ?  83  LEU   B N    1 
ATOM   5132 C CA   . LEU   B 1 83  ? 47.726 -9.801  -0.872  1.00 12.35 ?  83  LEU   B CA   1 
ATOM   5133 C C    . LEU   B 1 83  ? 48.423 -9.950  -2.220  1.00 12.34 ?  83  LEU   B C    1 
ATOM   5134 O O    . LEU   B 1 83  ? 47.820 -10.377 -3.209  1.00 12.16 ?  83  LEU   B O    1 
ATOM   5135 C CB   . LEU   B 1 83  ? 48.486 -10.472 0.278   1.00 13.03 ?  83  LEU   B CB   1 
ATOM   5136 C CG   . LEU   B 1 83  ? 47.965 -10.132 1.678   1.00 14.38 ?  83  LEU   B CG   1 
ATOM   5137 C CD1  . LEU   B 1 83  ? 48.601 -10.997 2.744   1.00 15.12 ?  83  LEU   B CD1  1 
ATOM   5138 C CD2  . LEU   B 1 83  ? 48.163 -8.650  2.007   1.00 15.98 ?  83  LEU   B CD2  1 
ATOM   5139 H H    . LEU   B 1 83  ? 46.342 -11.114 -1.334  1.00 15.04 ?  83  LEU   B H    1 
ATOM   5140 H HA   . LEU   B 1 83  ? 47.672 -8.855  -0.678  1.00 14.83 ?  83  LEU   B HA   1 
ATOM   5141 H HB2  . LEU   B 1 83  ? 48.433 -11.431 0.168   1.00 15.64 ?  83  LEU   B HB2  1 
ATOM   5142 H HB3  . LEU   B 1 83  ? 49.415 -10.190 0.235   1.00 15.64 ?  83  LEU   B HB3  1 
ATOM   5143 H HG   . LEU   B 1 83  ? 47.014 -10.305 1.695   1.00 17.27 ?  83  LEU   B HG   1 
ATOM   5144 H HD11 . LEU   B 1 83  ? 48.232 -10.755 3.609   1.00 18.16 ?  83  LEU   B HD11 1 
ATOM   5145 H HD12 . LEU   B 1 83  ? 48.398 -11.931 2.553   1.00 18.16 ?  83  LEU   B HD12 1 
ATOM   5146 H HD13 . LEU   B 1 83  ? 49.558 -10.861 2.740   1.00 18.16 ?  83  LEU   B HD13 1 
ATOM   5147 H HD21 . LEU   B 1 83  ? 47.956 -8.504  2.942   1.00 19.19 ?  83  LEU   B HD21 1 
ATOM   5148 H HD22 . LEU   B 1 83  ? 49.087 -8.408  1.831   1.00 19.19 ?  83  LEU   B HD22 1 
ATOM   5149 H HD23 . LEU   B 1 83  ? 47.572 -8.121  1.449   1.00 19.19 ?  83  LEU   B HD23 1 
ATOM   5150 N N    . SER   B 1 84  ? 49.696 -9.568  -2.277  1.00 13.30 ?  84  SER   B N    1 
ATOM   5151 C CA   . SER   B 1 84  ? 50.432 -9.687  -3.524  1.00 13.71 ?  84  SER   B CA   1 
ATOM   5152 C C    . SER   B 1 84  ? 50.594 -11.150 -3.924  1.00 12.59 ?  84  SER   B C    1 
ATOM   5153 O O    . SER   B 1 84  ? 50.705 -12.042 -3.081  1.00 12.65 ?  84  SER   B O    1 
ATOM   5154 C CB   . SER   B 1 84  ? 51.822 -9.074  -3.374  1.00 15.82 ?  84  SER   B CB   1 
ATOM   5155 O OG   . SER   B 1 84  ? 52.583 -9.301  -4.545  1.00 17.59 ?  84  SER   B OG   1 
ATOM   5156 H H    . SER   B 1 84  ? 50.143 -9.236  -1.620  1.00 15.97 ?  84  SER   B H    1 
ATOM   5157 H HA   . SER   B 1 84  ? 49.960 -9.223  -4.231  1.00 16.46 ?  84  SER   B HA   1 
ATOM   5158 H HB2  . SER   B 1 84  ? 51.732 -8.117  -3.227  1.00 18.99 ?  84  SER   B HB2  1 
ATOM   5159 H HB3  . SER   B 1 84  ? 52.273 -9.483  -2.622  1.00 18.99 ?  84  SER   B HB3  1 
ATOM   5160 H HG   . SER   B 1 84  ? 53.349 -8.947  -4.461  1.00 21.11 ?  84  SER   B HG   1 
ATOM   5161 N N    . GLY   B 1 85  ? 50.660 -11.385 -5.226  1.00 13.65 ?  85  GLY   B N    1 
ATOM   5162 C CA   . GLY   B 1 85  ? 51.017 -12.681 -5.749  1.00 14.46 ?  85  GLY   B CA   1 
ATOM   5163 C C    . GLY   B 1 85  ? 52.488 -12.867 -6.058  1.00 13.40 ?  85  GLY   B C    1 
ATOM   5164 O O    . GLY   B 1 85  ? 52.865 -13.946 -6.522  1.00 13.92 ?  85  GLY   B O    1 
ATOM   5165 H H    . GLY   B 1 85  ? 50.510 -10.798 -5.830  1.00 16.39 ?  85  GLY   B H    1 
ATOM   5166 H HA2  . GLY   B 1 85  ? 50.763 -13.363 -5.107  1.00 17.36 ?  85  GLY   B HA2  1 
ATOM   5167 H HA3  . GLY   B 1 85  ? 50.522 -12.839 -6.564  1.00 17.36 ?  85  GLY   B HA3  1 
ATOM   5168 N N    . HIS   B 1 86  ? 53.336 -11.861 -5.844  1.00 13.40 ?  86  HIS   B N    1 
ATOM   5169 C CA   . HIS   B 1 86  ? 54.798 -12.024 -5.938  1.00 13.54 ?  86  HIS   B CA   1 
ATOM   5170 C C    . HIS   B 1 86  ? 55.157 -12.537 -7.331  1.00 13.79 ?  86  HIS   B C    1 
ATOM   5171 O O    . HIS   B 1 86  ? 54.752 -11.927 -8.330  1.00 14.31 ?  86  HIS   B O    1 
ATOM   5172 C CB   . HIS   B 1 86  ? 55.290 -12.864 -4.765  1.00 13.99 ?  86  HIS   B CB   1 
ATOM   5173 C CG   . HIS   B 1 86  ? 54.966 -12.262 -3.437  1.00 14.32 ?  86  HIS   B CG   1 
ATOM   5174 N ND1  . HIS   B 1 86  ? 55.778 -11.335 -2.822  1.00 16.18 ?  86  HIS   B ND1  1 
ATOM   5175 C CD2  . HIS   B 1 86  ? 53.896 -12.429 -2.622  1.00 15.27 ?  86  HIS   B CD2  1 
ATOM   5176 C CE1  . HIS   B 1 86  ? 55.221 -10.954 -1.687  1.00 16.07 ?  86  HIS   B CE1  1 
ATOM   5177 N NE2  . HIS   B 1 86  ? 54.078 -11.601 -1.542  1.00 15.71 ?  86  HIS   B NE2  1 
ATOM   5178 H H    . HIS   B 1 86  ? 53.087 -11.064 -5.650  1.00 16.09 ?  86  HIS   B H    1 
ATOM   5179 H HA   . HIS   B 1 86  ? 55.200 -11.152 -5.849  1.00 16.26 ?  86  HIS   B HA   1 
ATOM   5180 H HB2  . HIS   B 1 86  ? 54.884 -13.742 -4.806  1.00 16.80 ?  86  HIS   B HB2  1 
ATOM   5181 H HB3  . HIS   B 1 86  ? 56.259 -12.946 -4.823  1.00 16.80 ?  86  HIS   B HB3  1 
ATOM   5182 H HD2  . HIS   B 1 86  ? 53.166 -12.989 -2.772  1.00 18.33 ?  86  HIS   B HD2  1 
ATOM   5183 H HE1  . HIS   B 1 86  ? 55.582 -10.348 -1.080  1.00 19.30 ?  86  HIS   B HE1  1 
ATOM   5184 H HE2  . HIS   B 1 86  ? 53.544 -11.532 -0.869  1.00 18.86 ?  86  HIS   B HE2  1 
ATOM   5185 N N    . ASN   B 1 87  ? 55.921 -13.620 -7.450  1.00 14.03 ?  87  ASN   B N    1 
ATOM   5186 C CA   . ASN   B 1 87  ? 56.305 -14.190 -8.732  1.00 14.68 ?  87  ASN   B CA   1 
ATOM   5187 C C    . ASN   B 1 87  ? 55.321 -15.233 -9.226  1.00 14.34 ?  87  ASN   B C    1 
ATOM   5188 O O    . ASN   B 1 87  ? 55.624 -15.937 -10.193 1.00 16.19 ?  87  ASN   B O    1 
ATOM   5189 C CB   . ASN   B 1 87  ? 57.698 -14.823 -8.632  1.00 16.46 ?  87  ASN   B CB   1 
ATOM   5190 C CG   . ASN   B 1 87  ? 57.763 -15.934 -7.588  1.00 17.51 ?  87  ASN   B CG   1 
ATOM   5191 O OD1  . ASN   B 1 87  ? 57.133 -15.854 -6.528  1.00 16.66 ?  87  ASN   B OD1  1 
ATOM   5192 N ND2  . ASN   B 1 87  ? 58.515 -16.992 -7.899  1.00 19.88 ?  87  ASN   B ND2  1 
ATOM   5193 H H    . ASN   B 1 87  ? 56.225 -14.062 -6.780  1.00 16.85 ?  87  ASN   B H    1 
ATOM   5194 H HA   . ASN   B 1 87  ? 56.346 -13.483 -9.392  1.00 17.62 ?  87  ASN   B HA   1 
ATOM   5195 H HB2  . ASN   B 1 87  ? 57.935 -15.203 -9.499  1.00 19.76 ?  87  ASN   B HB2  1 
ATOM   5196 H HB3  . ASN   B 1 87  ? 58.336 -14.142 -8.385  1.00 19.76 ?  87  ASN   B HB3  1 
ATOM   5197 H HD21 . ASN   B 1 87  ? 58.588 -17.646 -7.348  1.00 23.86 ?  87  ASN   B HD21 1 
ATOM   5198 H HD22 . ASN   B 1 87  ? 58.941 -17.017 -8.651  1.00 23.86 ?  87  ASN   B HD22 1 
ATOM   5199 N N    . LEU   B 1 88  ? 54.159 -15.343 -8.590  1.00 13.78 ?  88  LEU   B N    1 
ATOM   5200 C CA   . LEU   B 1 88  ? 53.180 -16.369 -8.917  1.00 13.98 ?  88  LEU   B CA   1 
ATOM   5201 C C    . LEU   B 1 88  ? 51.948 -15.848 -9.635  1.00 13.58 ?  88  LEU   B C    1 
ATOM   5202 O O    . LEU   B 1 88  ? 51.333 -16.597 -10.404 1.00 15.56 ?  88  LEU   B O    1 
ATOM   5203 C CB   . LEU   B 1 88  ? 52.714 -17.058 -7.631  1.00 15.17 ?  88  LEU   B CB   1 
ATOM   5204 C CG   . LEU   B 1 88  ? 53.833 -17.725 -6.842  1.00 17.19 ?  88  LEU   B CG   1 
ATOM   5205 C CD1  . LEU   B 1 88  ? 53.345 -18.114 -5.456  1.00 18.91 ?  88  LEU   B CD1  1 
ATOM   5206 C CD2  . LEU   B 1 88  ? 54.345 -18.937 -7.595  1.00 20.09 ?  88  LEU   B CD2  1 
ATOM   5207 H H    . LEU   B 1 88  ? 53.914 -14.834 -7.940  1.00 16.54 ?  88  LEU   B H    1 
ATOM   5208 H HA   . LEU   B 1 88  ? 53.586 -17.037 -9.480  1.00 16.79 ?  88  LEU   B HA   1 
ATOM   5209 H HB2  . LEU   B 1 88  ? 52.293 -16.403 -7.050  1.00 18.21 ?  88  LEU   B HB2  1 
ATOM   5210 H HB3  . LEU   B 1 88  ? 52.064 -17.748 -7.860  1.00 18.21 ?  88  LEU   B HB3  1 
ATOM   5211 H HG   . LEU   B 1 88  ? 54.565 -17.099 -6.741  1.00 20.64 ?  88  LEU   B HG   1 
ATOM   5212 H HD11 . LEU   B 1 88  ? 53.995 -18.708 -5.050  1.00 22.70 ?  88  LEU   B HD11 1 
ATOM   5213 H HD12 . LEU   B 1 88  ? 53.249 -17.311 -4.920  1.00 22.70 ?  88  LEU   B HD12 1 
ATOM   5214 H HD13 . LEU   B 1 88  ? 52.491 -18.562 -5.540  1.00 22.70 ?  88  LEU   B HD13 1 
ATOM   5215 H HD21 . LEU   B 1 88  ? 54.989 -19.403 -7.039  1.00 24.11 ?  88  LEU   B HD21 1 
ATOM   5216 H HD22 . LEU   B 1 88  ? 53.599 -19.522 -7.797  1.00 24.11 ?  88  LEU   B HD22 1 
ATOM   5217 H HD23 . LEU   B 1 88  ? 54.768 -18.644 -8.417  1.00 24.11 ?  88  LEU   B HD23 1 
ATOM   5218 N N    . ALA   B 1 89  ? 51.548 -14.611 -9.373  1.00 12.95 ?  89  ALA   B N    1 
ATOM   5219 C CA   . ALA   B 1 89  ? 50.252 -14.119 -9.812  1.00 12.31 ?  89  ALA   B CA   1 
ATOM   5220 C C    . ALA   B 1 89  ? 50.226 -12.630 -9.524  1.00 12.63 ?  89  ALA   B C    1 
ATOM   5221 O O    . ALA   B 1 89  ? 51.060 -12.120 -8.775  1.00 13.65 ?  89  ALA   B O    1 
ATOM   5222 C CB   . ALA   B 1 89  ? 49.117 -14.796 -9.051  1.00 12.75 ?  89  ALA   B CB   1 
ATOM   5223 H H    . ALA   B 1 89  ? 52.003 -14.030 -8.929  1.00 15.55 ?  89  ALA   B H    1 
ATOM   5224 H HA   . ALA   B 1 89  ? 50.133 -14.266 -10.765 1.00 14.79 ?  89  ALA   B HA   1 
ATOM   5225 H HB1  . ALA   B 1 89  ? 48.266 -14.462 -9.391  1.00 15.31 ?  89  ALA   B HB1  1 
ATOM   5226 H HB2  . ALA   B 1 89  ? 49.171 -15.753 -9.193  1.00 15.31 ?  89  ALA   B HB2  1 
ATOM   5227 H HB3  . ALA   B 1 89  ? 49.199 -14.590 -8.112  1.00 15.31 ?  89  ALA   B HB3  1 
ATOM   5228 N N    . LYS   B 1 90  ? 49.241 -11.934 -10.092 1.00 13.49 ?  90  LYS   B N    1 
ATOM   5229 C CA   . LYS   B 1 90  ? 49.043 -10.549 -9.686  1.00 13.96 ?  90  LYS   B CA   1 
ATOM   5230 C C    . LYS   B 1 90  ? 48.725 -10.480 -8.199  1.00 13.63 ?  90  LYS   B C    1 
ATOM   5231 O O    . LYS   B 1 90  ? 49.363 -9.730  -7.447  1.00 15.01 ?  90  LYS   B O    1 
ATOM   5232 C CB   . LYS   B 1 90  ? 47.953 -9.895  -10.536 1.00 15.65 ?  90  LYS   B CB   1 
ATOM   5233 C CG   . LYS   B 1 90  ? 47.657 -8.450  -10.165 1.00 16.78 ?  90  LYS   B CG   1 
ATOM   5234 C CD   . LYS   B 1 90  ? 48.866 -7.561  -10.262 1.00 19.41 ?  90  LYS   B CD   1 
ATOM   5235 C CE   . LYS   B 1 90  ? 48.435 -6.135  -10.036 1.00 21.56 ?  90  LYS   B CE   1 
ATOM   5236 N NZ   . LYS   B 1 90  ? 49.586 -5.220  -9.917  1.00 21.66 ?  90  LYS   B NZ   1 
ATOM   5237 H H    . LYS   B 1 90  ? 48.696 -12.233 -10.688 1.00 16.19 ?  90  LYS   B H    1 
ATOM   5238 H HA   . LYS   B 1 90  ? 49.867 -10.064 -9.839  1.00 16.77 ?  90  LYS   B HA   1 
ATOM   5239 H HB2  . LYS   B 1 90  ? 48.231 -9.909  -11.468 1.00 18.79 ?  90  LYS   B HB2  1 
ATOM   5240 H HB3  . LYS   B 1 90  ? 47.131 -10.404 -10.438 1.00 18.79 ?  90  LYS   B HB3  1 
ATOM   5241 H HG2  . LYS   B 1 90  ? 46.977 -8.105  -10.770 1.00 20.14 ?  90  LYS   B HG2  1 
ATOM   5242 H HG3  . LYS   B 1 90  ? 47.323 -8.419  -9.252  1.00 20.14 ?  90  LYS   B HG3  1 
ATOM   5243 H HD2  . LYS   B 1 90  ? 49.508 -7.806  -9.577  1.00 23.30 ?  90  LYS   B HD2  1 
ATOM   5244 H HD3  . LYS   B 1 90  ? 49.259 -7.637  -11.146 1.00 23.30 ?  90  LYS   B HD3  1 
ATOM   5245 H HE2  . LYS   B 1 90  ? 47.895 -5.838  -10.788 1.00 25.88 ?  90  LYS   B HE2  1 
ATOM   5246 H HE3  . LYS   B 1 90  ? 47.923 -6.076  -9.215  1.00 25.88 ?  90  LYS   B HE3  1 
ATOM   5247 H HZ1  . LYS   B 1 90  ? 49.305 -4.381  -9.788  1.00 26.00 ?  90  LYS   B HZ1  1 
ATOM   5248 H HZ2  . LYS   B 1 90  ? 50.101 -5.457  -9.232  1.00 26.00 ?  90  LYS   B HZ2  1 
ATOM   5249 H HZ3  . LYS   B 1 90  ? 50.076 -5.240  -10.664 1.00 26.00 ?  90  LYS   B HZ3  1 
ATOM   5250 N N    . HIS   B 1 91  ? 47.772 -11.302 -7.752  1.00 12.49 ?  91  HIS   B N    1 
ATOM   5251 C CA   . HIS   B 1 91  ? 47.308 -11.321 -6.380  1.00 12.36 ?  91  HIS   B CA   1 
ATOM   5252 C C    . HIS   B 1 91  ? 47.306 -12.744 -5.862  1.00 11.73 ?  91  HIS   B C    1 
ATOM   5253 O O    . HIS   B 1 91  ? 47.070 -13.697 -6.613  1.00 11.91 ?  91  HIS   B O    1 
ATOM   5254 C CB   . HIS   B 1 91  ? 45.859 -10.835 -6.264  1.00 13.84 ?  91  HIS   B CB   1 
ATOM   5255 C CG   . HIS   B 1 91  ? 45.654 -9.427  -6.697  1.00 17.17 ?  91  HIS   B CG   1 
ATOM   5256 N ND1  . HIS   B 1 91  ? 46.280 -8.358  -6.090  1.00 19.59 ?  91  HIS   B ND1  1 
ATOM   5257 C CD2  . HIS   B 1 91  ? 44.866 -8.902  -7.662  1.00 20.02 ?  91  HIS   B CD2  1 
ATOM   5258 C CE1  . HIS   B 1 91  ? 45.898 -7.235  -6.674  1.00 20.48 ?  91  HIS   B CE1  1 
ATOM   5259 N NE2  . HIS   B 1 91  ? 45.034 -7.539  -7.626  1.00 21.20 ?  91  HIS   B NE2  1 
ATOM   5260 H H    . HIS   B 1 91  ? 47.369 -11.874 -8.251  1.00 14.99 ?  91  HIS   B H    1 
ATOM   5261 H HA   . HIS   B 1 91  ? 47.882 -10.767 -5.820  1.00 14.85 ?  91  HIS   B HA   1 
ATOM   5262 H HB2  . HIS   B 1 91  ? 45.295 -11.396 -6.813  1.00 16.61 ?  91  HIS   B HB2  1 
ATOM   5263 H HB3  . HIS   B 1 91  ? 45.582 -10.899 -5.334  1.00 16.61 ?  91  HIS   B HB3  1 
ATOM   5264 H HD1  . HIS   B 1 91  ? 46.837 -8.414  -5.435  1.00 23.52 ?  91  HIS   B HD1  1 
ATOM   5265 H HD2  . HIS   B 1 91  ? 44.316 -9.367  -8.244  1.00 24.03 ?  91  HIS   B HD2  1 
ATOM   5266 H HE1  . HIS   B 1 91  ? 46.188 -6.377  -6.446  1.00 24.58 ?  91  HIS   B HE1  1 
ATOM   5267 N N    . CYS   B 1 92  ? 47.494 -12.872 -4.560  1.00 11.31 ?  92  CYS   B N    1 
ATOM   5268 C CA   . CYS   B 1 92  ? 47.192 -14.110 -3.854  1.00 11.15 ?  92  CYS   B CA   1 
ATOM   5269 C C    . CYS   B 1 92  ? 45.971 -13.877 -2.976  1.00 10.85 ?  92  CYS   B C    1 
ATOM   5270 O O    . CYS   B 1 92  ? 45.969 -12.978 -2.127  1.00 12.22 ?  92  CYS   B O    1 
ATOM   5271 C CB   . CYS   B 1 92  ? 48.373 -14.566 -3.005  1.00 11.73 ?  92  CYS   B CB   1 
ATOM   5272 S SG   . CYS   B 1 92  ? 48.020 -16.105 -2.110  1.00 12.03 ?  92  CYS   B SG   1 
ATOM   5273 H H    . CYS   B 1 92  ? 47.811 -12.250 -4.049  1.00 13.58 ?  92  CYS   B H    1 
ATOM   5274 H HA   . CYS   B 1 92  ? 46.994 -14.805 -4.500  1.00 13.39 ?  92  CYS   B HA   1 
ATOM   5275 H HB2  . CYS   B 1 92  ? 49.139 -14.716 -3.579  1.00 14.09 ?  92  CYS   B HB2  1 
ATOM   5276 H HB3  . CYS   B 1 92  ? 48.574 -13.879 -2.350  1.00 14.09 ?  92  CYS   B HB3  1 
ATOM   5277 H HG   . CYS   B 1 92  ? 48.995 -16.419 -1.485  1.00 14.45 ?  92  CYS   B HG   1 
ATOM   5278 N N    . LEU   B 1 93  ? 44.942 -14.690 -3.186  1.00 10.81 ?  93  LEU   B N    1 
ATOM   5279 C CA   . LEU   B 1 93  ? 43.772 -14.703 -2.320  1.00 10.80 ?  93  LEU   B CA   1 
ATOM   5280 C C    . LEU   B 1 93  ? 44.001 -15.761 -1.253  1.00 10.36 ?  93  LEU   B C    1 
ATOM   5281 O O    . LEU   B 1 93  ? 43.952 -16.963 -1.541  1.00 11.26 ?  93  LEU   B O    1 
ATOM   5282 C CB   . LEU   B 1 93  ? 42.510 -14.992 -3.127  1.00 11.62 ?  93  LEU   B CB   1 
ATOM   5283 C CG   . LEU   B 1 93  ? 41.212 -15.024 -2.321  1.00 12.21 ?  93  LEU   B CG   1 
ATOM   5284 C CD1  . LEU   B 1 93  ? 40.852 -13.637 -1.803  1.00 12.92 ?  93  LEU   B CD1  1 
ATOM   5285 C CD2  . LEU   B 1 93  ? 40.090 -15.602 -3.161  1.00 12.79 ?  93  LEU   B CD2  1 
ATOM   5286 H H    . LEU   B 1 93  ? 44.900 -15.263 -3.837  1.00 12.98 ?  93  LEU   B H    1 
ATOM   5287 H HA   . LEU   B 1 93  ? 43.679 -13.840 -1.893  1.00 12.97 ?  93  LEU   B HA   1 
ATOM   5288 H HB2  . LEU   B 1 93  ? 42.415 -14.299 -3.803  1.00 13.95 ?  93  LEU   B HB2  1 
ATOM   5289 H HB3  . LEU   B 1 93  ? 42.610 -15.852 -3.559  1.00 13.95 ?  93  LEU   B HB3  1 
ATOM   5290 H HG   . LEU   B 1 93  ? 41.334 -15.604 -1.555  1.00 14.66 ?  93  LEU   B HG   1 
ATOM   5291 H HD11 . LEU   B 1 93  ? 40.002 -13.683 -1.343  1.00 15.52 ?  93  LEU   B HD11 1 
ATOM   5292 H HD12 . LEU   B 1 93  ? 41.545 -13.339 -1.190  1.00 15.52 ?  93  LEU   B HD12 1 
ATOM   5293 H HD13 . LEU   B 1 93  ? 40.791 -13.025 -2.554  1.00 15.52 ?  93  LEU   B HD13 1 
ATOM   5294 H HD21 . LEU   B 1 93  ? 39.272 -15.608 -2.637  1.00 15.36 ?  93  LEU   B HD21 1 
ATOM   5295 H HD22 . LEU   B 1 93  ? 39.969 -15.053 -3.953  1.00 15.36 ?  93  LEU   B HD22 1 
ATOM   5296 H HD23 . LEU   B 1 93  ? 40.320 -16.508 -3.422  1.00 15.36 ?  93  LEU   B HD23 1 
ATOM   5297 N N    . HIS   B 1 94  ? 44.270 -15.328 -0.034  1.00 10.51 ?  94  HIS   B N    1 
ATOM   5298 C CA   . HIS   B 1 94  ? 44.488 -16.236 1.085   1.00 10.62 ?  94  HIS   B CA   1 
ATOM   5299 C C    . HIS   B 1 94  ? 43.124 -16.584 1.658   1.00 11.09 ?  94  HIS   B C    1 
ATOM   5300 O O    . HIS   B 1 94  ? 42.451 -15.707 2.201   1.00 12.81 ?  94  HIS   B O    1 
ATOM   5301 C CB   . HIS   B 1 94  ? 45.356 -15.558 2.142   1.00 11.09 ?  94  HIS   B CB   1 
ATOM   5302 C CG   . HIS   B 1 94  ? 46.733 -15.253 1.671   1.00 11.20 ?  94  HIS   B CG   1 
ATOM   5303 N ND1  . HIS   B 1 94  ? 47.760 -16.165 1.761   1.00 11.67 ?  94  HIS   B ND1  1 
ATOM   5304 C CD2  . HIS   B 1 94  ? 47.240 -14.151 1.067   1.00 11.69 ?  94  HIS   B CD2  1 
ATOM   5305 C CE1  . HIS   B 1 94  ? 48.850 -15.622 1.250   1.00 11.74 ?  94  HIS   B CE1  1 
ATOM   5306 N NE2  . HIS   B 1 94  ? 48.564 -14.402 0.824   1.00 11.92 ?  94  HIS   B NE2  1 
ATOM   5307 H H    . HIS   B 1 94  ? 44.336 -14.495 0.175   1.00 12.63 ?  94  HIS   B H    1 
ATOM   5308 H HA   . HIS   B 1 94  ? 44.924 -17.046 0.777   1.00 12.76 ?  94  HIS   B HA   1 
ATOM   5309 H HB2  . HIS   B 1 94  ? 44.939 -14.724 2.398   1.00 13.32 ?  94  HIS   B HB2  1 
ATOM   5310 H HB3  . HIS   B 1 94  ? 45.430 -16.147 2.905   1.00 13.32 ?  94  HIS   B HB3  1 
ATOM   5311 H HD2  . HIS   B 1 94  ? 46.782 -13.368 0.862   1.00 14.04 ?  94  HIS   B HD2  1 
ATOM   5312 H HE1  . HIS   B 1 94  ? 49.684 -16.037 1.192   1.00 14.10 ?  94  HIS   B HE1  1 
ATOM   5313 H HE2  . HIS   B 1 94  ? 49.120 -13.863 0.448   1.00 14.31 ?  94  HIS   B HE2  1 
ATOM   5314 N N    . VAL   B 1 95  ? 42.695 -17.836 1.509   1.00 11.00 ?  95  VAL   B N    1 
ATOM   5315 C CA   . VAL   B 1 95  ? 41.373 -18.276 1.948   1.00 11.19 ?  95  VAL   B CA   1 
ATOM   5316 C C    . VAL   B 1 95  ? 41.540 -19.312 3.046   1.00 11.63 ?  95  VAL   B C    1 
ATOM   5317 O O    . VAL   B 1 95  ? 42.305 -20.269 2.889   1.00 12.30 ?  95  VAL   B O    1 
ATOM   5318 C CB   . VAL   B 1 95  ? 40.554 -18.880 0.794   1.00 11.59 ?  95  VAL   B CB   1 
ATOM   5319 C CG1  . VAL   B 1 95  ? 39.189 -19.325 1.283   1.00 13.04 ?  95  VAL   B CG1  1 
ATOM   5320 C CG2  . VAL   B 1 95  ? 40.421 -17.895 -0.337  1.00 11.88 ?  95  VAL   B CG2  1 
ATOM   5321 H H    . VAL   B 1 95  ? 43.162 -18.464 1.148   1.00 13.20 ?  95  VAL   B H    1 
ATOM   5322 H HA   . VAL   B 1 95  ? 40.883 -17.522 2.311   1.00 13.44 ?  95  VAL   B HA   1 
ATOM   5323 H HB   . VAL   B 1 95  ? 41.015 -19.659 0.453   1.00 13.91 ?  95  VAL   B HB   1 
ATOM   5324 H HG11 . VAL   B 1 95  ? 38.621 -19.500 0.516   1.00 15.66 ?  95  VAL   B HG11 1 
ATOM   5325 H HG12 . VAL   B 1 95  ? 39.289 -20.133 1.810   1.00 15.66 ?  95  VAL   B HG12 1 
ATOM   5326 H HG13 . VAL   B 1 95  ? 38.802 -18.620 1.825   1.00 15.66 ?  95  VAL   B HG13 1 
ATOM   5327 H HG21 . VAL   B 1 95  ? 39.837 -18.271 -1.013  1.00 14.26 ?  95  VAL   B HG21 1 
ATOM   5328 H HG22 . VAL   B 1 95  ? 40.040 -17.071 0.009   1.00 14.26 ?  95  VAL   B HG22 1 
ATOM   5329 H HG23 . VAL   B 1 95  ? 41.298 -17.726 -0.708  1.00 14.26 ?  95  VAL   B HG23 1 
ATOM   5330 N N    . VAL   B 1 96  ? 40.814 -19.142 4.143   1.00 11.89 ?  96  VAL   B N    1 
ATOM   5331 C CA   . VAL   B 1 96  ? 40.896 -20.053 5.282   1.00 12.17 ?  96  VAL   B CA   1 
ATOM   5332 C C    . VAL   B 1 96  ? 39.708 -21.013 5.232   1.00 12.64 ?  96  VAL   B C    1 
ATOM   5333 O O    . VAL   B 1 96  ? 38.587 -20.662 5.615   1.00 13.35 ?  96  VAL   B O    1 
ATOM   5334 C CB   . VAL   B 1 96  ? 40.943 -19.302 6.615   1.00 12.94 ?  96  VAL   B CB   1 
ATOM   5335 C CG1  . VAL   B 1 96  ? 41.111 -20.293 7.761   1.00 13.68 ?  96  VAL   B CG1  1 
ATOM   5336 C CG2  . VAL   B 1 96  ? 42.059 -18.269 6.627   1.00 14.07 ?  96  VAL   B CG2  1 
ATOM   5337 H H    . VAL   B 1 96  ? 40.257 -18.499 4.258   1.00 14.28 ?  96  VAL   B H    1 
ATOM   5338 H HA   . VAL   B 1 96  ? 41.709 -20.581 5.211   1.00 14.61 ?  96  VAL   B HA   1 
ATOM   5339 H HB   . VAL   B 1 96  ? 40.099 -18.840 6.744   1.00 15.54 ?  96  VAL   B HB   1 
ATOM   5340 H HG11 . VAL   B 1 96  ? 41.294 -19.800 8.578   1.00 16.42 ?  96  VAL   B HG11 1 
ATOM   5341 H HG12 . VAL   B 1 96  ? 40.293 -20.805 7.867   1.00 16.42 ?  96  VAL   B HG12 1 
ATOM   5342 H HG13 . VAL   B 1 96  ? 41.851 -20.886 7.563   1.00 16.42 ?  96  VAL   B HG13 1 
ATOM   5343 H HG21 . VAL   B 1 96  ? 42.101 -17.857 7.506   1.00 16.89 ?  96  VAL   B HG21 1 
ATOM   5344 H HG22 . VAL   B 1 96  ? 42.899 -18.704 6.424   1.00 16.89 ?  96  VAL   B HG22 1 
ATOM   5345 H HG23 . VAL   B 1 96  ? 41.867 -17.589 5.958   1.00 16.89 ?  96  VAL   B HG23 1 
ATOM   5346 N N    . GLY   B 1 97  ? 39.945 -22.244 4.788   1.00 12.88 ?  97  GLY   B N    1 
ATOM   5347 C CA   . GLY   B 1 97  ? 38.969 -23.294 4.949   1.00 13.54 ?  97  GLY   B CA   1 
ATOM   5348 C C    . GLY   B 1 97  ? 39.097 -23.896 6.330   1.00 14.58 ?  97  GLY   B C    1 
ATOM   5349 O O    . GLY   B 1 97  ? 40.141 -23.768 6.984   1.00 15.05 ?  97  GLY   B O    1 
ATOM   5350 H H    . GLY   B 1 97  ? 40.673 -22.482 4.385   1.00 15.46 ?  97  GLY   B H    1 
ATOM   5351 H HA2  . GLY   B 1 97  ? 38.077 -22.921 4.832   1.00 16.26 ?  97  GLY   B HA2  1 
ATOM   5352 H HA3  . GLY   B 1 97  ? 39.110 -23.977 4.273   1.00 16.26 ?  97  GLY   B HA3  1 
ATOM   5353 N N    . PRO   B 1 98  ? 38.050 -24.577 6.797   1.00 14.94 ?  98  PRO   B N    1 
ATOM   5354 C CA   . PRO   B 1 98  ? 38.141 -25.268 8.085   1.00 16.09 ?  98  PRO   B CA   1 
ATOM   5355 C C    . PRO   B 1 98  ? 39.166 -26.389 8.044   1.00 15.52 ?  98  PRO   B C    1 
ATOM   5356 O O    . PRO   B 1 98  ? 39.271 -27.126 7.064   1.00 16.04 ?  98  PRO   B O    1 
ATOM   5357 C CB   . PRO   B 1 98  ? 36.724 -25.816 8.290   1.00 16.11 ?  98  PRO   B CB   1 
ATOM   5358 C CG   . PRO   B 1 98  ? 36.172 -25.948 6.922   1.00 15.78 ?  98  PRO   B CG   1 
ATOM   5359 C CD   . PRO   B 1 98  ? 36.739 -24.778 6.157   1.00 15.04 ?  98  PRO   B CD   1 
ATOM   5360 H HA   . PRO   B 1 98  ? 38.367 -24.645 8.786   1.00 19.31 ?  98  PRO   B HA   1 
ATOM   5361 H HB2  . PRO   B 1 98  ? 36.772 -26.681 8.726   1.00 19.34 ?  98  PRO   B HB2  1 
ATOM   5362 H HB3  . PRO   B 1 98  ? 36.208 -25.188 8.811   1.00 19.34 ?  98  PRO   B HB3  1 
ATOM   5363 H HG2  . PRO   B 1 98  ? 36.464 -26.788 6.529   1.00 18.94 ?  98  PRO   B HG2  1 
ATOM   5364 H HG3  . PRO   B 1 98  ? 35.206 -25.902 6.954   1.00 18.94 ?  98  PRO   B HG3  1 
ATOM   5365 H HD2  . PRO   B 1 98  ? 36.838 -25.004 5.214   1.00 18.06 ?  98  PRO   B HD2  1 
ATOM   5366 H HD3  . PRO   B 1 98  ? 36.185 -23.991 6.275   1.00 18.06 ?  98  PRO   B HD3  1 
ATOM   5367 N N    . ASN   B 1 99  ? 39.920 -26.509 9.126   1.00 16.60 ?  99  ASN   B N    1 
ATOM   5368 C CA   . ASN   B 1 99  ? 40.892 -27.585 9.298   1.00 17.54 ?  99  ASN   B CA   1 
ATOM   5369 C C    . ASN   B 1 99  ? 40.253 -28.663 10.172  1.00 20.46 ?  99  ASN   B C    1 
ATOM   5370 O O    . ASN   B 1 99  ? 40.175 -28.522 11.395  1.00 21.28 ?  99  ASN   B O    1 
ATOM   5371 C CB   . ASN   B 1 99  ? 42.166 -27.038 9.930   1.00 18.14 ?  99  ASN   B CB   1 
ATOM   5372 C CG   . ASN   B 1 99  ? 43.296 -28.045 9.932   1.00 19.06 ?  99  ASN   B CG   1 
ATOM   5373 O OD1  . ASN   B 1 99  ? 43.070 -29.238 10.089  1.00 19.70 ?  99  ASN   B OD1  1 
ATOM   5374 N ND2  . ASN   B 1 99  ? 44.519 -27.567 9.749   1.00 19.33 ?  99  ASN   B ND2  1 
ATOM   5375 H H    . ASN   B 1 99  ? 39.889 -25.970 9.788   1.00 19.93 ?  99  ASN   B H    1 
ATOM   5376 H HA   . ASN   B 1 99  ? 41.113 -27.978 8.438   1.00 21.05 ?  99  ASN   B HA   1 
ATOM   5377 H HB2  . ASN   B 1 99  ? 42.454 -26.262 9.434   1.00 21.78 ?  99  ASN   B HB2  1 
ATOM   5378 H HB3  . ASN   B 1 99  ? 41.978 -26.799 10.853  1.00 21.78 ?  99  ASN   B HB3  1 
ATOM   5379 H HD21 . ASN   B 1 99  ? 45.193 -28.097 9.739   1.00 23.21 ?  99  ASN   B HD21 1 
ATOM   5380 H HD22 . ASN   B 1 99  ? 44.631 -26.720 9.645   1.00 23.21 ?  99  ASN   B HD22 1 
ATOM   5381 N N    A VAL   B 1 100 ? 39.777 -29.737 9.534   0.86 21.98 ?  100 VAL   B N    1 
ATOM   5382 N N    B VAL   B 1 100 ? 39.793 -29.744 9.533   0.14 22.60 ?  100 VAL   B N    1 
ATOM   5383 C CA   A VAL   B 1 100 ? 39.157 -30.838 10.271  0.86 24.92 ?  100 VAL   B CA   1 
ATOM   5384 C CA   B VAL   B 1 100 ? 39.165 -30.840 10.266  0.14 24.79 ?  100 VAL   B CA   1 
ATOM   5385 C C    A VAL   B 1 100 ? 40.154 -31.502 11.213  0.86 25.59 ?  100 VAL   B C    1 
ATOM   5386 C C    B VAL   B 1 100 ? 40.156 -31.499 11.214  0.14 25.55 ?  100 VAL   B C    1 
ATOM   5387 O O    A VAL   B 1 100 ? 39.772 -31.999 12.279  0.86 26.55 ?  100 VAL   B O    1 
ATOM   5388 O O    B VAL   B 1 100 ? 39.774 -31.973 12.292  0.14 25.83 ?  100 VAL   B O    1 
ATOM   5389 C CB   A VAL   B 1 100 ? 38.518 -31.847 9.294   0.86 27.55 ?  100 VAL   B CB   1 
ATOM   5390 C CB   B VAL   B 1 100 ? 38.539 -31.850 9.281   0.14 26.11 ?  100 VAL   B CB   1 
ATOM   5391 C CG1  A VAL   B 1 100 ? 38.072 -33.104 10.026  0.86 28.76 ?  100 VAL   B CG1  1 
ATOM   5392 C CG1  B VAL   B 1 100 ? 38.018 -33.075 10.018  0.14 26.65 ?  100 VAL   B CG1  1 
ATOM   5393 C CG2  A VAL   B 1 100 ? 37.339 -31.205 8.575   0.86 28.27 ?  100 VAL   B CG2  1 
ATOM   5394 C CG2  B VAL   B 1 100 ? 37.422 -31.188 8.490   0.14 26.50 ?  100 VAL   B CG2  1 
ATOM   5395 H H    A VAL   B 1 100 ? 39.785 -29.841 8.678   0.86 26.39 ?  100 VAL   B H    1 
ATOM   5396 H H    B VAL   B 1 100 ? 39.832 -29.862 8.683   0.14 27.13 ?  100 VAL   B H    1 
ATOM   5397 H HA   A VAL   B 1 100 ? 38.438 -30.476 10.813  0.86 29.91 ?  100 VAL   B HA   1 
ATOM   5398 H HA   B VAL   B 1 100 ? 38.445 -30.479 10.803  0.14 29.76 ?  100 VAL   B HA   1 
ATOM   5399 H HB   A VAL   B 1 100 ? 39.173 -32.106 8.628   0.86 33.06 ?  100 VAL   B HB   1 
ATOM   5400 H HB   B VAL   B 1 100 ? 39.217 -32.145 8.653   0.14 31.34 ?  100 VAL   B HB   1 
ATOM   5401 H HG11 A VAL   B 1 100 ? 37.473 -33.608 9.450   0.86 34.52 ?  100 VAL   B HG11 1 
ATOM   5402 H HG11 B VAL   B 1 100 ? 37.443 -33.580 9.420   0.14 31.99 ?  100 VAL   B HG11 1 
ATOM   5403 H HG12 A VAL   B 1 100 ? 38.850 -33.643 10.241  0.86 34.52 ?  100 VAL   B HG12 1 
ATOM   5404 H HG12 B VAL   B 1 100 ? 38.769 -33.625 10.292  0.14 31.99 ?  100 VAL   B HG12 1 
ATOM   5405 H HG13 A VAL   B 1 100 ? 37.608 -32.850 10.839  0.86 34.52 ?  100 VAL   B HG13 1 
ATOM   5406 H HG13 B VAL   B 1 100 ? 37.514 -32.787 10.794  0.14 31.99 ?  100 VAL   B HG13 1 
ATOM   5407 H HG21 A VAL   B 1 100 ? 36.963 -31.847 7.952   0.86 33.93 ?  100 VAL   B HG21 1 
ATOM   5408 H HG21 B VAL   B 1 100 ? 37.030 -31.841 7.890   0.14 31.81 ?  100 VAL   B HG21 1 
ATOM   5409 H HG22 A VAL   B 1 100 ? 36.670 -30.952 9.231   0.86 33.93 ?  100 VAL   B HG22 1 
ATOM   5410 H HG22 B VAL   B 1 100 ? 36.750 -30.861 9.109   0.14 31.81 ?  100 VAL   B HG22 1 
ATOM   5411 H HG23 A VAL   B 1 100 ? 37.649 -30.423 8.098   0.86 33.93 ?  100 VAL   B HG23 1 
ATOM   5412 H HG23 B VAL   B 1 100 ? 37.791 -30.450 7.982   0.14 31.81 ?  100 VAL   B HG23 1 
ATOM   5413 N N    . ASN   B 1 101 ? 41.435 -31.546 10.838  1.00 25.92 ?  101 ASN   B N    1 
ATOM   5414 C CA   . ASN   B 1 101 ? 42.462 -32.090 11.726  1.00 28.08 ?  101 ASN   B CA   1 
ATOM   5415 C C    . ASN   B 1 101 ? 42.662 -31.246 12.979  1.00 30.32 ?  101 ASN   B C    1 
ATOM   5416 O O    . ASN   B 1 101 ? 43.327 -31.706 13.916  1.00 31.38 ?  101 ASN   B O    1 
ATOM   5417 C CB   . ASN   B 1 101 ? 43.788 -32.243 10.978  1.00 28.01 ?  101 ASN   B CB   1 
ATOM   5418 C CG   . ASN   B 1 101 ? 43.760 -33.376 9.973   1.00 27.60 ?  101 ASN   B CG   1 
ATOM   5419 O OD1  . ASN   B 1 101 ? 43.069 -34.371 10.169  1.00 28.49 ?  101 ASN   B OD1  1 
ATOM   5420 N ND2  . ASN   B 1 101 ? 44.503 -33.227 8.885   1.00 27.05 ?  101 ASN   B ND2  1 
ATOM   5421 H H    A ASN   B 1 101 ? 41.728 -31.285 10.073  0.86 31.12 ?  101 ASN   B H    1 
ATOM   5422 H H    B ASN   B 1 101 ? 41.728 -31.280 10.075  0.14 31.12 ?  101 ASN   B H    1 
ATOM   5423 H HA   . ASN   B 1 101 ? 42.185 -32.971 12.014  1.00 33.71 ?  101 ASN   B HA   1 
ATOM   5424 H HB2  . ASN   B 1 101 ? 43.987 -31.426 10.499  1.00 33.62 ?  101 ASN   B HB2  1 
ATOM   5425 H HB3  . ASN   B 1 101 ? 44.494 -32.430 11.620  1.00 33.62 ?  101 ASN   B HB3  1 
ATOM   5426 H HD21 . ASN   B 1 101 ? 44.519 -33.846 8.287   1.00 32.47 ?  101 ASN   B HD21 1 
ATOM   5427 H HD22 . ASN   B 1 101 ? 44.968 -32.513 8.777   1.00 32.47 ?  101 ASN   B HD22 1 
ATOM   5428 N N    . LYS   B 1 102 ? 42.115 -30.030 13.011  1.00 32.64 ?  102 LYS   B N    1 
ATOM   5429 C CA   . LYS   B 1 102 ? 42.098 -29.191 14.202  1.00 35.42 ?  102 LYS   B CA   1 
ATOM   5430 C C    . LYS   B 1 102 ? 40.719 -29.134 14.847  1.00 34.52 ?  102 LYS   B C    1 
ATOM   5431 O O    . LYS   B 1 102 ? 40.510 -28.341 15.771  1.00 34.99 ?  102 LYS   B O    1 
ATOM   5432 C CB   . LYS   B 1 102 ? 42.559 -27.771 13.864  1.00 39.48 ?  102 LYS   B CB   1 
ATOM   5433 C CG   . LYS   B 1 102 ? 44.027 -27.643 13.503  1.00 43.45 ?  102 LYS   B CG   1 
ATOM   5434 C CD   . LYS   B 1 102 ? 44.329 -26.231 13.023  1.00 47.10 ?  102 LYS   B CD   1 
ATOM   5435 C CE   . LYS   B 1 102 ? 45.821 -25.958 12.943  1.00 49.87 ?  102 LYS   B CE   1 
ATOM   5436 N NZ   . LYS   B 1 102 ? 46.088 -24.559 12.499  1.00 51.38 ?  102 LYS   B NZ   1 
ATOM   5437 H H    . LYS   B 1 102 ? 41.734 -29.661 12.334  1.00 39.17 ?  102 LYS   B H    1 
ATOM   5438 H HA   . LYS   B 1 102 ? 42.719 -29.555 14.849  1.00 42.51 ?  102 LYS   B HA   1 
ATOM   5439 H HB2  . LYS   B 1 102 ? 42.042 -27.449 13.110  1.00 47.39 ?  102 LYS   B HB2  1 
ATOM   5440 H HB3  . LYS   B 1 102 ? 42.397 -27.203 14.635  1.00 47.39 ?  102 LYS   B HB3  1 
ATOM   5441 H HG2  . LYS   B 1 102 ? 44.572 -27.825 14.285  1.00 52.14 ?  102 LYS   B HG2  1 
ATOM   5442 H HG3  . LYS   B 1 102 ? 44.241 -28.264 12.789  1.00 52.14 ?  102 LYS   B HG3  1 
ATOM   5443 H HD2  . LYS   B 1 102 ? 43.953 -26.109 12.136  1.00 56.52 ?  102 LYS   B HD2  1 
ATOM   5444 H HD3  . LYS   B 1 102 ? 43.938 -25.593 13.641  1.00 56.52 ?  102 LYS   B HD3  1 
ATOM   5445 H HE2  . LYS   B 1 102 ? 46.218 -26.081 13.820  1.00 59.85 ?  102 LYS   B HE2  1 
ATOM   5446 H HE3  . LYS   B 1 102 ? 46.226 -26.564 12.302  1.00 59.85 ?  102 LYS   B HE3  1 
ATOM   5447 H HZ1  . LYS   B 1 102 ? 46.964 -24.414 12.457  1.00 61.67 ?  102 LYS   B HZ1  1 
ATOM   5448 H HZ2  . LYS   B 1 102 ? 45.733 -24.423 11.694  1.00 61.67 ?  102 LYS   B HZ2  1 
ATOM   5449 H HZ3  . LYS   B 1 102 ? 45.726 -23.984 13.074  1.00 61.67 ?  102 LYS   B HZ3  1 
ATOM   5450 N N    A GLY   B 1 103 ? 39.772 -29.944 14.378  0.86 33.49 ?  103 GLY   B N    1 
ATOM   5451 N N    B GLY   B 1 103 ? 39.771 -29.939 14.374  0.14 34.22 ?  103 GLY   B N    1 
ATOM   5452 C CA   A GLY   B 1 103 ? 38.439 -29.979 14.942  0.86 33.06 ?  103 GLY   B CA   1 
ATOM   5453 C CA   B GLY   B 1 103 ? 38.452 -29.973 14.970  0.14 33.86 ?  103 GLY   B CA   1 
ATOM   5454 C C    A GLY   B 1 103 ? 37.503 -28.899 14.449  0.86 31.95 ?  103 GLY   B C    1 
ATOM   5455 C C    B GLY   B 1 103 ? 37.521 -28.873 14.520  0.14 33.20 ?  103 GLY   B C    1 
ATOM   5456 O O    A GLY   B 1 103 ? 36.369 -28.815 14.941  0.86 32.37 ?  103 GLY   B O    1 
ATOM   5457 O O    B GLY   B 1 103 ? 36.496 -28.642 15.170  0.14 33.34 ?  103 GLY   B O    1 
ATOM   5458 H H    A GLY   B 1 103 ? 39.883 -30.487 13.721  0.86 40.20 ?  103 GLY   B H    1 
ATOM   5459 H H    B GLY   B 1 103 ? 39.869 -30.468 13.704  0.14 41.07 ?  103 GLY   B H    1 
ATOM   5460 H HA2  A GLY   B 1 103 ? 38.033 -30.835 14.735  0.86 39.68 ?  103 GLY   B HA2  1 
ATOM   5461 H HA2  B GLY   B 1 103 ? 38.037 -30.824 14.764  0.14 40.64 ?  103 GLY   B HA2  1 
ATOM   5462 H HA3  A GLY   B 1 103 ? 38.506 -29.906 15.908  0.86 39.68 ?  103 GLY   B HA3  1 
ATOM   5463 H HA3  B GLY   B 1 103 ? 38.540 -29.907 15.934  0.14 40.64 ?  103 GLY   B HA3  1 
ATOM   5464 N N    A GLU   B 1 104 ? 37.929 -28.074 13.497  0.86 30.41 ?  104 GLU   B N    1 
ATOM   5465 N N    B GLU   B 1 104 ? 37.840 -28.186 13.428  0.14 32.26 ?  104 GLU   B N    1 
ATOM   5466 C CA   A GLU   B 1 104 ? 37.089 -26.991 13.015  0.86 28.86 ?  104 GLU   B CA   1 
ATOM   5467 C CA   B GLU   B 1 104 ? 37.012 -27.085 12.963  0.14 31.27 ?  104 GLU   B CA   1 
ATOM   5468 C C    A GLU   B 1 104 ? 35.925 -27.539 12.189  0.86 29.25 ?  104 GLU   B C    1 
ATOM   5469 C C    B GLU   B 1 104 ? 35.854 -27.601 12.116  0.14 31.12 ?  104 GLU   B C    1 
ATOM   5470 O O    A GLU   B 1 104 ? 35.986 -28.633 11.619  0.86 29.99 ?  104 GLU   B O    1 
ATOM   5471 O O    B GLU   B 1 104 ? 35.946 -28.643 11.461  0.14 31.13 ?  104 GLU   B O    1 
ATOM   5472 C CB   A GLU   B 1 104 ? 37.927 -25.997 12.212  0.86 27.53 ?  104 GLU   B CB   1 
ATOM   5473 C CB   B GLU   B 1 104 ? 37.859 -26.085 12.176  0.14 30.49 ?  104 GLU   B CB   1 
ATOM   5474 C CG   A GLU   B 1 104 ? 39.045 -25.388 13.044  0.86 26.44 ?  104 GLU   B CG   1 
ATOM   5475 C CG   B GLU   B 1 104 ? 38.953 -25.444 13.019  0.14 29.85 ?  104 GLU   B CG   1 
ATOM   5476 C CD   A GLU   B 1 104 ? 39.986 -24.506 12.254  0.86 25.39 ?  104 GLU   B CD   1 
ATOM   5477 C CD   B GLU   B 1 104 ? 39.865 -24.540 12.214  0.14 29.32 ?  104 GLU   B CD   1 
ATOM   5478 O OE1  A GLU   B 1 104 ? 39.967 -24.538 11.007  0.86 23.54 ?  104 GLU   B OE1  1 
ATOM   5479 O OE1  B GLU   B 1 104 ? 39.762 -24.539 10.970  0.14 29.03 ?  104 GLU   B OE1  1 
ATOM   5480 O OE2  A GLU   B 1 104 ? 40.760 -23.777 12.902  0.86 26.16 -1 104 GLU   B OE2  1 
ATOM   5481 O OE2  B GLU   B 1 104 ? 40.687 -23.830 12.830  0.14 29.22 -1 104 GLU   B OE2  1 
ATOM   5482 H H    A GLU   B 1 104 ? 38.702 -28.117 13.126  0.86 36.50 ?  104 GLU   B H    1 
ATOM   5483 H H    B GLU   B 1 104 ? 38.535 -28.336 12.943  0.14 38.72 ?  104 GLU   B H    1 
ATOM   5484 H HA   A GLU   B 1 104 ? 36.721 -26.516 13.778  0.86 34.64 ?  104 GLU   B HA   1 
ATOM   5485 H HA   B GLU   B 1 104 ? 36.641 -26.624 13.729  0.14 37.54 ?  104 GLU   B HA   1 
ATOM   5486 H HB2  A GLU   B 1 104 ? 38.328 -26.454 11.458  0.86 33.04 ?  104 GLU   B HB2  1 
ATOM   5487 H HB2  B GLU   B 1 104 ? 38.283 -26.542 11.433  0.14 36.60 ?  104 GLU   B HB2  1 
ATOM   5488 H HB3  A GLU   B 1 104 ? 37.356 -25.276 11.902  0.86 33.04 ?  104 GLU   B HB3  1 
ATOM   5489 H HB3  B GLU   B 1 104 ? 37.284 -25.377 11.844  0.14 36.60 ?  104 GLU   B HB3  1 
ATOM   5490 H HG2  A GLU   B 1 104 ? 38.658 -24.841 13.747  0.86 31.74 ?  104 GLU   B HG2  1 
ATOM   5491 H HG2  B GLU   B 1 104 ? 38.542 -24.910 13.718  0.14 35.83 ?  104 GLU   B HG2  1 
ATOM   5492 H HG3  A GLU   B 1 104 ? 39.577 -26.097 13.436  0.86 31.74 ?  104 GLU   B HG3  1 
ATOM   5493 H HG3  B GLU   B 1 104 ? 39.495 -26.144 13.418  0.14 35.83 ?  104 GLU   B HG3  1 
ATOM   5494 N N    A ASP   B 1 105 ? 34.851 -26.755 12.134  0.86 29.13 ?  105 ASP   B N    1 
ATOM   5495 N N    B ASP   B 1 105 ? 34.754 -26.851 12.136  0.14 31.02 ?  105 ASP   B N    1 
ATOM   5496 C CA   A ASP   B 1 105 ? 33.578 -27.223 11.601  0.86 29.84 ?  105 ASP   B CA   1 
ATOM   5497 C CA   B ASP   B 1 105 ? 33.504 -27.312 11.544  0.14 30.98 ?  105 ASP   B CA   1 
ATOM   5498 C C    A ASP   B 1 105 ? 33.630 -27.276 10.078  0.86 27.76 ?  105 ASP   B C    1 
ATOM   5499 C C    B ASP   B 1 105 ? 33.613 -27.331 10.024  0.14 30.08 ?  105 ASP   B C    1 
ATOM   5500 O O    A ASP   B 1 105 ? 33.773 -26.241 9.417   0.86 26.99 ?  105 ASP   B O    1 
ATOM   5501 O O    B ASP   B 1 105 ? 33.860 -26.297 9.395   0.14 29.91 ?  105 ASP   B O    1 
ATOM   5502 C CB   A ASP   B 1 105 ? 32.454 -26.299 12.066  0.86 32.90 ?  105 ASP   B CB   1 
ATOM   5503 C CB   B ASP   B 1 105 ? 32.360 -26.402 11.987  0.14 31.80 ?  105 ASP   B CB   1 
ATOM   5504 C CG   A ASP   B 1 105 ? 31.083 -26.791 11.644  0.86 35.53 ?  105 ASP   B CG   1 
ATOM   5505 C CG   B ASP   B 1 105 ? 30.996 -26.981 11.659  0.14 32.52 ?  105 ASP   B CG   1 
ATOM   5506 O OD1  A ASP   B 1 105 ? 30.998 -27.879 11.037  0.86 35.80 ?  105 ASP   B OD1  1 
ATOM   5507 O OD1  B ASP   B 1 105 ? 30.941 -28.032 10.988  0.14 32.72 ?  105 ASP   B OD1  1 
ATOM   5508 O OD2  A ASP   B 1 105 ? 30.086 -26.087 11.921  0.86 37.36 -1 105 ASP   B OD2  1 
ATOM   5509 O OD2  B ASP   B 1 105 ? 29.979 -26.387 12.077  0.14 32.83 -1 105 ASP   B OD2  1 
ATOM   5510 H H    A ASP   B 1 105 ? 34.838 -25.936 12.398  0.86 34.96 ?  105 ASP   B H    1 
ATOM   5511 H H    B ASP   B 1 105 ? 34.707 -26.068 12.484  0.14 37.23 ?  105 ASP   B H    1 
ATOM   5512 H HA   A ASP   B 1 105 ? 33.395 -28.116 11.935  0.86 35.82 ?  105 ASP   B HA   1 
ATOM   5513 H HA   B ASP   B 1 105 ? 33.313 -28.212 11.849  0.14 37.19 ?  105 ASP   B HA   1 
ATOM   5514 H HB2  A ASP   B 1 105 ? 32.478 -26.233 13.037  0.86 39.49 ?  105 ASP   B HB2  1 
ATOM   5515 H HB2  B ASP   B 1 105 ? 32.411 -26.273 12.949  0.14 38.17 ?  105 ASP   B HB2  1 
ATOM   5516 H HB3  A ASP   B 1 105 ? 32.583 -25.421 11.674  0.86 39.49 ?  105 ASP   B HB3  1 
ATOM   5517 H HB3  B ASP   B 1 105 ? 32.438 -25.547 11.535  0.14 38.17 ?  105 ASP   B HB3  1 
ATOM   5518 N N    A ILE   B 1 106 ? 33.490 -28.483 9.523   0.86 27.26 ?  106 ILE   B N    1 
ATOM   5519 N N    B ILE   B 1 106 ? 33.421 -28.515 9.435   0.14 29.38 ?  106 ILE   B N    1 
ATOM   5520 C CA   A ILE   B 1 106 ? 33.479 -28.666 8.077   0.86 26.48 ?  106 ILE   B CA   1 
ATOM   5521 C CA   B ILE   B 1 106 ? 33.448 -28.661 7.985   0.14 28.75 ?  106 ILE   B CA   1 
ATOM   5522 C C    A ILE   B 1 106 ? 32.386 -27.836 7.407   0.86 24.83 ?  106 ILE   B C    1 
ATOM   5523 C C    B ILE   B 1 106 ? 32.353 -27.841 7.315   0.14 28.03 ?  106 ILE   B C    1 
ATOM   5524 O O    A ILE   B 1 106 ? 32.494 -27.511 6.220   0.86 23.95 ?  106 ILE   B O    1 
ATOM   5525 O O    B ILE   B 1 106 ? 32.444 -27.547 6.118   0.14 27.94 ?  106 ILE   B O    1 
ATOM   5526 C CB   A ILE   B 1 106 ? 33.370 -30.174 7.746   0.86 27.43 ?  106 ILE   B CB   1 
ATOM   5527 C CB   B ILE   B 1 106 ? 33.360 -30.159 7.611   0.14 28.88 ?  106 ILE   B CB   1 
ATOM   5528 C CG1  A ILE   B 1 106 ? 33.627 -30.429 6.261   0.86 28.26 ?  106 ILE   B CG1  1 
ATOM   5529 C CG1  B ILE   B 1 106 ? 33.641 -30.371 6.120   0.14 28.95 ?  106 ILE   B CG1  1 
ATOM   5530 C CG2  A ILE   B 1 106 ? 32.007 -30.721 8.156   0.86 28.24 ?  106 ILE   B CG2  1 
ATOM   5531 C CG2  B ILE   B 1 106 ? 31.996 -30.725 7.979   0.14 29.01 ?  106 ILE   B CG2  1 
ATOM   5532 C CD1  A ILE   B 1 106 ? 34.973 -29.939 5.793   0.86 28.50 ?  106 ILE   B CD1  1 
ATOM   5533 C CD1  B ILE   B 1 106 ? 34.994 -29.864 5.677   0.14 28.97 ?  106 ILE   B CD1  1 
ATOM   5534 H H    A ILE   B 1 106 ? 33.401 -29.212 9.972   0.86 32.72 ?  106 ILE   B H    1 
ATOM   5535 H H    B ILE   B 1 106 ? 33.285 -29.248 9.859   0.14 35.26 ?  106 ILE   B H    1 
ATOM   5536 H HA   A ILE   B 1 106 ? 34.325 -28.352 7.736   0.86 31.78 ?  106 ILE   B HA   1 
ATOM   5537 H HA   B ILE   B 1 106 ? 34.297 -28.325 7.665   0.14 34.51 ?  106 ILE   B HA   1 
ATOM   5538 H HB   A ILE   B 1 106 ? 34.046 -30.648 8.258   0.86 32.93 ?  106 ILE   B HB   1 
ATOM   5539 H HB   B ILE   B 1 106 ? 34.033 -30.638 8.117   0.14 34.67 ?  106 ILE   B HB   1 
ATOM   5540 H HG12 A ILE   B 1 106 ? 33.587 -31.387 6.098   0.86 33.92 ?  106 ILE   B HG12 1 
ATOM   5541 H HG12 B ILE   B 1 106 ? 33.608 -31.323 5.929   0.14 34.74 ?  106 ILE   B HG12 1 
ATOM   5542 H HG13 A ILE   B 1 106 ? 32.946 -29.979 5.742   0.86 33.92 ?  106 ILE   B HG13 1 
ATOM   5543 H HG13 B ILE   B 1 106 ? 32.965 -29.910 5.601   0.14 34.74 ?  106 ILE   B HG13 1 
ATOM   5544 H HG21 A ILE   B 1 106 ? 32.015 -31.688 8.071   0.86 33.90 ?  106 ILE   B HG21 1 
ATOM   5545 H HG21 B ILE   B 1 106 ? 32.017 -31.690 7.874   0.14 34.83 ?  106 ILE   B HG21 1 
ATOM   5546 H HG22 A ILE   B 1 106 ? 31.830 -30.474 9.078   0.86 33.90 ?  106 ILE   B HG22 1 
ATOM   5547 H HG22 B ILE   B 1 106 ? 31.799 -30.499 8.901   0.14 34.83 ?  106 ILE   B HG22 1 
ATOM   5548 H HG23 A ILE   B 1 106 ? 31.326 -30.345 7.577   0.86 33.90 ?  106 ILE   B HG23 1 
ATOM   5549 H HG23 B ILE   B 1 106 ? 31.324 -30.344 7.393   0.14 34.83 ?  106 ILE   B HG23 1 
ATOM   5550 H HD11 A ILE   B 1 106 ? 35.187 -30.363 4.949   0.86 34.21 ?  106 ILE   B HD11 1 
ATOM   5551 H HD11 B ILE   B 1 106 ? 35.209 -30.252 4.817   0.14 34.77 ?  106 ILE   B HD11 1 
ATOM   5552 H HD12 A ILE   B 1 106 ? 34.937 -28.976 5.678   0.86 34.21 ?  106 ILE   B HD12 1 
ATOM   5553 H HD12 B ILE   B 1 106 ? 34.960 -28.897 5.605   0.14 34.77 ?  106 ILE   B HD12 1 
ATOM   5554 H HD13 A ILE   B 1 106 ? 35.643 -30.169 6.457   0.86 34.21 ?  106 ILE   B HD13 1 
ATOM   5555 H HD13 B ILE   B 1 106 ? 35.658 -30.125 6.334   0.14 34.77 ?  106 ILE   B HD13 1 
ATOM   5556 N N    A GLN   B 1 107 ? 31.336 -27.469 8.144   0.86 25.42 ?  107 GLN   B N    1 
ATOM   5557 N N    B GLN   B 1 107 ? 31.314 -27.460 8.062   0.14 27.53 ?  107 GLN   B N    1 
ATOM   5558 C CA   A GLN   B 1 107 ? 30.259 -26.669 7.567   0.86 25.62 ?  107 GLN   B CA   1 
ATOM   5559 C CA   B GLN   B 1 107 ? 30.241 -26.649 7.498   0.14 27.01 ?  107 GLN   B CA   1 
ATOM   5560 C C    A GLN   B 1 107 ? 30.743 -25.316 7.055   0.86 23.65 ?  107 GLN   B C    1 
ATOM   5561 C C    B GLN   B 1 107 ? 30.730 -25.278 7.047   0.14 24.36 ?  107 GLN   B C    1 
ATOM   5562 O O    A GLN   B 1 107 ? 30.111 -24.743 6.164   0.86 24.20 ?  107 GLN   B O    1 
ATOM   5563 O O    B GLN   B 1 107 ? 30.076 -24.645 6.211   0.14 24.46 ?  107 GLN   B O    1 
ATOM   5564 C CB   A GLN   B 1 107 ? 29.144 -26.483 8.601   0.86 29.49 ?  107 GLN   B CB   1 
ATOM   5565 C CB   B GLN   B 1 107 ? 29.113 -26.502 8.524   0.14 29.24 ?  107 GLN   B CB   1 
ATOM   5566 C CG   A GLN   B 1 107 ? 27.811 -26.023 8.021   0.86 33.73 ?  107 GLN   B CG   1 
ATOM   5567 C CG   B GLN   B 1 107 ? 27.785 -26.026 7.948   0.14 31.34 ?  107 GLN   B CG   1 
ATOM   5568 C CD   A GLN   B 1 107 ? 27.693 -24.511 7.925   0.86 36.91 ?  107 GLN   B CD   1 
ATOM   5569 C CD   B GLN   B 1 107 ? 27.644 -24.515 7.953   0.14 33.00 ?  107 GLN   B CD   1 
ATOM   5570 O OE1  A GLN   B 1 107 ? 28.537 -23.775 8.440   0.86 38.20 ?  107 GLN   B OE1  1 
ATOM   5571 O OE1  B GLN   B 1 107 ? 28.484 -23.801 8.502   0.14 33.61 ?  107 GLN   B OE1  1 
ATOM   5572 N NE2  A GLN   B 1 107 ? 26.636 -24.040 7.267   0.86 38.05 ?  107 GLN   B NE2  1 
ATOM   5573 N NE2  B GLN   B 1 107 ? 26.573 -24.021 7.342   0.14 33.56 ?  107 GLN   B NE2  1 
ATOM   5574 H H    A GLN   B 1 107 ? 31.225 -27.671 8.969   0.86 30.51 ?  107 GLN   B H    1 
ATOM   5575 H H    B GLN   B 1 107 ? 31.205 -27.664 8.888   0.14 33.04 ?  107 GLN   B H    1 
ATOM   5576 H HA   A GLN   B 1 107 ? 29.882 -27.155 6.814   0.86 30.75 ?  107 GLN   B HA   1 
ATOM   5577 H HA   B GLN   B 1 107 ? 29.876 -27.105 6.724   0.14 32.42 ?  107 GLN   B HA   1 
ATOM   5578 H HB2  A GLN   B 1 107 ? 28.991 -27.329 9.046   0.86 35.40 ?  107 GLN   B HB2  1 
ATOM   5579 H HB2  B GLN   B 1 107 ? 28.957 -27.365 8.934   0.14 35.10 ?  107 GLN   B HB2  1 
ATOM   5580 H HB3  A GLN   B 1 107 ? 29.430 -25.821 9.250   0.86 35.40 ?  107 GLN   B HB3  1 
ATOM   5581 H HB3  B GLN   B 1 107 ? 29.388 -25.865 9.201   0.14 35.10 ?  107 GLN   B HB3  1 
ATOM   5582 H HG2  A GLN   B 1 107 ? 27.710 -26.384 7.127   0.86 40.49 ?  107 GLN   B HG2  1 
ATOM   5583 H HG2  B GLN   B 1 107 ? 27.710 -26.329 7.030   0.14 37.62 ?  107 GLN   B HG2  1 
ATOM   5584 H HG3  A GLN   B 1 107 ? 27.091 -26.346 8.590   0.86 40.49 ?  107 GLN   B HG3  1 
ATOM   5585 H HG3  B GLN   B 1 107 ? 27.060 -26.398 8.479   0.14 37.62 ?  107 GLN   B HG3  1 
ATOM   5586 H HE21 A GLN   B 1 107 ? 26.066 -24.585 6.919   0.86 45.66 ?  107 GLN   B HE21 1 
ATOM   5587 H HE21 B GLN   B 1 107 ? 26.007 -24.550 6.968   0.14 40.28 ?  107 GLN   B HE21 1 
ATOM   5588 H HE22 A GLN   B 1 107 ? 26.519 -23.191 7.188   0.86 45.66 ?  107 GLN   B HE22 1 
ATOM   5589 H HE22 B GLN   B 1 107 ? 26.446 -23.171 7.320   0.14 40.28 ?  107 GLN   B HE22 1 
ATOM   5590 N N    . LEU   B 1 108 ? 31.862 -24.805 7.574   1.00 21.72 ?  108 LEU   B N    1 
ATOM   5591 C CA   . LEU   B 1 108 ? 32.410 -23.512 7.160   1.00 19.20 ?  108 LEU   B CA   1 
ATOM   5592 C C    . LEU   B 1 108 ? 33.061 -23.545 5.786   1.00 17.01 ?  108 LEU   B C    1 
ATOM   5593 O O    . LEU   B 1 108 ? 33.493 -22.494 5.290   1.00 16.66 ?  108 LEU   B O    1 
ATOM   5594 C CB   . LEU   B 1 108 ? 33.413 -23.021 8.201   1.00 20.02 ?  108 LEU   B CB   1 
ATOM   5595 C CG   . LEU   B 1 108 ? 32.783 -22.516 9.500   1.00 21.59 ?  108 LEU   B CG   1 
ATOM   5596 C CD1  . LEU   B 1 108 ? 33.803 -22.477 10.622  1.00 22.05 ?  108 LEU   B CD1  1 
ATOM   5597 C CD2  . LEU   B 1 108 ? 32.187 -21.134 9.281   1.00 22.67 ?  108 LEU   B CD2  1 
ATOM   5598 H H    A LEU   B 1 108 ? 32.318 -25.193 8.186   0.86 26.07 ?  108 LEU   B H    1 
ATOM   5599 H H    B LEU   B 1 108 ? 32.318 -25.209 8.176   0.14 26.07 ?  108 LEU   B H    1 
ATOM   5600 H HA   . LEU   B 1 108 ? 31.687 -22.871 7.125   1.00 23.04 ?  108 LEU   B HA   1 
ATOM   5601 H HB2  . LEU   B 1 108 ? 34.004 -23.752 8.434   1.00 24.03 ?  108 LEU   B HB2  1 
ATOM   5602 H HB3  . LEU   B 1 108 ? 33.921 -22.291 7.822   1.00 24.03 ?  108 LEU   B HB3  1 
ATOM   5603 H HG   . LEU   B 1 108 ? 32.063 -23.113 9.766   1.00 25.92 ?  108 LEU   B HG   1 
ATOM   5604 H HD11 . LEU   B 1 108 ? 33.369 -22.172 11.437  1.00 26.47 ?  108 LEU   B HD11 1 
ATOM   5605 H HD12 . LEU   B 1 108 ? 34.162 -23.368 10.754  1.00 26.47 ?  108 LEU   B HD12 1 
ATOM   5606 H HD13 . LEU   B 1 108 ? 34.515 -21.864 10.380  1.00 26.47 ?  108 LEU   B HD13 1 
ATOM   5607 H HD21 . LEU   B 1 108 ? 31.840 -20.802 10.122  1.00 27.21 ?  108 LEU   B HD21 1 
ATOM   5608 H HD22 . LEU   B 1 108 ? 32.883 -20.543 8.952   1.00 27.21 ?  108 LEU   B HD22 1 
ATOM   5609 H HD23 . LEU   B 1 108 ? 31.472 -21.198 8.629   1.00 27.21 ?  108 LEU   B HD23 1 
ATOM   5610 N N    . LEU   B 1 109 ? 33.127 -24.716 5.158   1.00 15.89 ?  109 LEU   B N    1 
ATOM   5611 C CA   . LEU   B 1 109 ? 33.760 -24.822 3.853   1.00 14.91 ?  109 LEU   B CA   1 
ATOM   5612 C C    . LEU   B 1 109 ? 32.995 -24.040 2.790   1.00 14.27 ?  109 LEU   B C    1 
ATOM   5613 O O    . LEU   B 1 109 ? 33.613 -23.448 1.897   1.00 14.16 ?  109 LEU   B O    1 
ATOM   5614 C CB   . LEU   B 1 109 ? 33.888 -26.297 3.480   1.00 15.28 ?  109 LEU   B CB   1 
ATOM   5615 C CG   . LEU   B 1 109 ? 34.664 -26.634 2.209   1.00 15.15 ?  109 LEU   B CG   1 
ATOM   5616 C CD1  . LEU   B 1 109 ? 36.037 -25.989 2.228   1.00 14.92 ?  109 LEU   B CD1  1 
ATOM   5617 C CD2  . LEU   B 1 109 ? 34.771 -28.142 2.061   1.00 15.66 ?  109 LEU   B CD2  1 
ATOM   5618 H H    . LEU   B 1 109 ? 32.816 -25.456 5.459   1.00 19.07 ?  109 LEU   B H    1 
ATOM   5619 H HA   . LEU   B 1 109 ? 34.653 -24.451 3.905   1.00 17.90 ?  109 LEU   B HA   1 
ATOM   5620 H HB2  . LEU   B 1 109 ? 34.335 -26.757 4.209   1.00 18.35 ?  109 LEU   B HB2  1 
ATOM   5621 H HB3  . LEU   B 1 109 ? 32.997 -26.664 3.372   1.00 18.35 ?  109 LEU   B HB3  1 
ATOM   5622 H HG   . LEU   B 1 109 ? 34.178 -26.302 1.438   1.00 18.19 ?  109 LEU   B HG   1 
ATOM   5623 H HD11 . LEU   B 1 109 ? 36.568 -26.358 1.505   1.00 17.92 ?  109 LEU   B HD11 1 
ATOM   5624 H HD12 . LEU   B 1 109 ? 35.933 -25.036 2.115   1.00 17.92 ?  109 LEU   B HD12 1 
ATOM   5625 H HD13 . LEU   B 1 109 ? 36.460 -26.185 3.080   1.00 17.92 ?  109 LEU   B HD13 1 
ATOM   5626 H HD21 . LEU   B 1 109 ? 35.342 -28.350 1.303   1.00 18.80 ?  109 LEU   B HD21 1 
ATOM   5627 H HD22 . LEU   B 1 109 ? 35.150 -28.516 2.871   1.00 18.80 ?  109 LEU   B HD22 1 
ATOM   5628 H HD23 . LEU   B 1 109 ? 33.883 -28.514 1.912   1.00 18.80 ?  109 LEU   B HD23 1 
ATOM   5629 N N    . LYS   B 1 110 ? 31.660 -24.021 2.861   1.00 13.99 ?  110 LYS   B N    1 
ATOM   5630 C CA   . LYS   B 1 110 ? 30.907 -23.259 1.873   1.00 13.99 ?  110 LYS   B CA   1 
ATOM   5631 C C    . LYS   B 1 110 ? 31.244 -21.773 1.965   1.00 13.63 ?  110 LYS   B C    1 
ATOM   5632 O O    . LYS   B 1 110 ? 31.487 -21.119 0.948   1.00 13.47 ?  110 LYS   B O    1 
ATOM   5633 C CB   . LYS   B 1 110 ? 29.405 -23.502 2.026   1.00 14.61 ?  110 LYS   B CB   1 
ATOM   5634 C CG   . LYS   B 1 110 ? 28.597 -22.879 0.897   1.00 15.05 ?  110 LYS   B CG   1 
ATOM   5635 C CD   . LYS   B 1 110 ? 27.146 -23.334 0.919   1.00 15.65 ?  110 LYS   B CD   1 
ATOM   5636 C CE   . LYS   B 1 110 ? 26.362 -22.801 -0.279  1.00 16.46 ?  110 LYS   B CE   1 
ATOM   5637 N NZ   . LYS   B 1 110 ? 26.695 -23.506 -1.545  1.00 16.82 ?  110 LYS   B NZ   1 
ATOM   5638 H H    . LYS   B 1 110 ? 31.186 -24.441 3.444   1.00 16.80 ?  110 LYS   B H    1 
ATOM   5639 H HA   . LYS   B 1 110 ? 31.161 -23.562 0.986   1.00 16.80 ?  110 LYS   B HA   1 
ATOM   5640 H HB2  . LYS   B 1 110 ? 29.234 -24.461 2.018   1.00 17.54 ?  110 LYS   B HB2  1 
ATOM   5641 H HB3  . LYS   B 1 110 ? 29.101 -23.120 2.861   1.00 17.54 ?  110 LYS   B HB3  1 
ATOM   5642 H HG2  . LYS   B 1 110 ? 28.606 -21.912 0.991   1.00 18.06 ?  110 LYS   B HG2  1 
ATOM   5643 H HG3  . LYS   B 1 110 ? 28.978 -23.135 0.043   1.00 18.06 ?  110 LYS   B HG3  1 
ATOM   5644 H HD2  . LYS   B 1 110 ? 27.115 -24.307 0.896   1.00 18.79 ?  110 LYS   B HD2  1 
ATOM   5645 H HD3  . LYS   B 1 110 ? 26.718 -23.011 1.730   1.00 18.79 ?  110 LYS   B HD3  1 
ATOM   5646 H HE2  . LYS   B 1 110 ? 25.414 -22.916 -0.115  1.00 19.76 ?  110 LYS   B HE2  1 
ATOM   5647 H HE3  . LYS   B 1 110 ? 26.570 -21.863 -0.397  1.00 19.76 ?  110 LYS   B HE3  1 
ATOM   5648 H HZ1  . LYS   B 1 110 ? 26.224 -23.169 -2.216  1.00 20.20 ?  110 LYS   B HZ1  1 
ATOM   5649 H HZ2  . LYS   B 1 110 ? 27.565 -23.415 -1.724  1.00 20.20 ?  110 LYS   B HZ2  1 
ATOM   5650 H HZ3  . LYS   B 1 110 ? 26.510 -24.376 -1.467  1.00 20.20 ?  110 LYS   B HZ3  1 
ATOM   5651 N N    . SER   B 1 111 ? 31.274 -21.226 3.185   1.00 13.94 ?  111 SER   B N    1 
ATOM   5652 C CA   . SER   B 1 111 ? 31.656 -19.826 3.362   1.00 14.10 ?  111 SER   B CA   1 
ATOM   5653 C C    . SER   B 1 111 ? 33.032 -19.559 2.769   1.00 13.49 ?  111 SER   B C    1 
ATOM   5654 O O    . SER   B 1 111 ? 33.252 -18.530 2.116   1.00 13.70 ?  111 SER   B O    1 
ATOM   5655 C CB   . SER   B 1 111 ? 31.650 -19.477 4.847   1.00 15.40 ?  111 SER   B CB   1 
ATOM   5656 O OG   . SER   B 1 111 ? 30.343 -19.472 5.367   1.00 17.12 ?  111 SER   B OG   1 
ATOM   5657 H H    . SER   B 1 111 ? 31.090 -21.647 3.914   1.00 16.74 ?  111 SER   B H    1 
ATOM   5658 H HA   . SER   B 1 111 ? 31.014 -19.263 2.910   1.00 16.93 ?  111 SER   B HA   1 
ATOM   5659 H HB2  . SER   B 1 111 ? 32.173 -20.137 5.330   1.00 18.49 ?  111 SER   B HB2  1 
ATOM   5660 H HB3  . SER   B 1 111 ? 32.033 -18.598 4.965   1.00 18.49 ?  111 SER   B HB3  1 
ATOM   5661 H HG   . SER   B 1 111 ? 30.356 -19.280 6.190   1.00 20.55 ?  111 SER   B HG   1 
ATOM   5662 N N    . ALA   B 1 112 ? 33.972 -20.477 2.987   1.00 13.30 ?  112 ALA   B N    1 
ATOM   5663 C CA   . ALA   B 1 112 ? 35.313 -20.301 2.445   1.00 12.73 ?  112 ALA   B CA   1 
ATOM   5664 C C    . ALA   B 1 112 ? 35.279 -20.207 0.923   1.00 12.19 ?  112 ALA   B C    1 
ATOM   5665 O O    . ALA   B 1 112 ? 35.908 -19.319 0.327   1.00 12.81 ?  112 ALA   B O    1 
ATOM   5666 C CB   . ALA   B 1 112 ? 36.216 -21.442 2.916   1.00 13.54 ?  112 ALA   B CB   1 
ATOM   5667 H H    . ALA   B 1 112 ? 33.857 -21.203 3.446   1.00 15.97 ?  112 ALA   B H    1 
ATOM   5668 H HA   . ALA   B 1 112 ? 35.676 -19.471 2.791   1.00 15.28 ?  112 ALA   B HA   1 
ATOM   5669 H HB1  . ALA   B 1 112 ? 37.108 -21.301 2.556   1.00 16.26 ?  112 ALA   B HB1  1 
ATOM   5670 H HB2  . ALA   B 1 112 ? 36.254 -21.434 3.889   1.00 16.26 ?  112 ALA   B HB2  1 
ATOM   5671 H HB3  . ALA   B 1 112 ? 35.858 -22.281 2.605   1.00 16.26 ?  112 ALA   B HB3  1 
ATOM   5672 N N    . TYR   B 1 113 ? 34.544 -21.114 0.270   1.00 12.36 ?  113 TYR   B N    1 
ATOM   5673 C CA   . TYR   B 1 113 ? 34.473 -21.068 -1.184  1.00 11.86 ?  113 TYR   B CA   1 
ATOM   5674 C C    . TYR   B 1 113 ? 33.767 -19.818 -1.700  1.00 11.87 ?  113 TYR   B C    1 
ATOM   5675 O O    . TYR   B 1 113 ? 34.034 -19.389 -2.828  1.00 12.16 ?  113 TYR   B O    1 
ATOM   5676 C CB   . TYR   B 1 113 ? 33.804 -22.323 -1.735  1.00 12.52 ?  113 TYR   B CB   1 
ATOM   5677 C CG   . TYR   B 1 113 ? 34.762 -23.469 -1.990  1.00 12.88 ?  113 TYR   B CG   1 
ATOM   5678 C CD1  . TYR   B 1 113 ? 35.752 -23.370 -2.959  1.00 13.56 ?  113 TYR   B CD1  1 
ATOM   5679 C CD2  . TYR   B 1 113 ? 34.658 -24.659 -1.288  1.00 13.27 ?  113 TYR   B CD2  1 
ATOM   5680 C CE1  . TYR   B 1 113 ? 36.636 -24.404 -3.200  1.00 13.35 ?  113 TYR   B CE1  1 
ATOM   5681 C CE2  . TYR   B 1 113 ? 35.526 -25.713 -1.531  1.00 13.46 ?  113 TYR   B CE2  1 
ATOM   5682 C CZ   . TYR   B 1 113 ? 36.511 -25.583 -2.491  1.00 13.41 ?  113 TYR   B CZ   1 
ATOM   5683 O OH   . TYR   B 1 113 ? 37.393 -26.605 -2.761  1.00 14.29 ?  113 TYR   B OH   1 
ATOM   5684 H H    . TYR   B 1 113 ? 34.086 -21.745 0.644   1.00 14.84 ?  113 TYR   B H    1 
ATOM   5685 H HA   . TYR   B 1 113 ? 35.372 -21.048 -1.521  1.00 14.25 ?  113 TYR   B HA   1 
ATOM   5686 H HB2  . TYR   B 1 113 ? 33.138 -22.637 -1.098  1.00 15.03 ?  113 TYR   B HB2  1 
ATOM   5687 H HB3  . TYR   B 1 113 ? 33.372 -22.105 -2.575  1.00 15.03 ?  113 TYR   B HB3  1 
ATOM   5688 H HD1  . TYR   B 1 113 ? 35.840 -22.575 -3.441  1.00 16.28 ?  113 TYR   B HD1  1 
ATOM   5689 H HD2  . TYR   B 1 113 ? 33.992 -24.752 -0.650  1.00 15.93 ?  113 TYR   B HD2  1 
ATOM   5690 H HE1  . TYR   B 1 113 ? 37.292 -24.315 -3.860  1.00 16.03 ?  113 TYR   B HE1  1 
ATOM   5691 H HE2  . TYR   B 1 113 ? 35.443 -26.508 -1.061  1.00 16.16 ?  113 TYR   B HE2  1 
ATOM   5692 H HH   . TYR   B 1 113 ? 37.208 -27.273 -2.284  1.00 17.16 ?  113 TYR   B HH   1 
ATOM   5693 N N    . GLU   B 1 114 ? 32.840 -19.243 -0.925  1.00 12.04 ?  114 GLU   B N    1 
ATOM   5694 C CA   . GLU   B 1 114 ? 32.151 -18.038 -1.383  1.00 12.42 ?  114 GLU   B CA   1 
ATOM   5695 C C    . GLU   B 1 114 ? 33.129 -16.916 -1.681  1.00 11.99 ?  114 GLU   B C    1 
ATOM   5696 O O    . GLU   B 1 114 ? 32.846 -16.060 -2.524  1.00 12.83 ?  114 GLU   B O    1 
ATOM   5697 C CB   . GLU   B 1 114 ? 31.091 -17.612 -0.366  1.00 13.14 ?  114 GLU   B CB   1 
ATOM   5698 C CG   . GLU   B 1 114 ? 29.875 -18.525 -0.438  1.00 13.22 ?  114 GLU   B CG   1 
ATOM   5699 C CD   . GLU   B 1 114 ? 28.861 -18.345 0.682   1.00 13.46 ?  114 GLU   B CD   1 
ATOM   5700 O OE1  . GLU   B 1 114 ? 29.152 -17.729 1.728   1.00 14.03 ?  114 GLU   B OE1  1 
ATOM   5701 O OE2  . GLU   B 1 114 ? 27.738 -18.879 0.522   1.00 14.48 -1 114 GLU   B OE2  1 
ATOM   5702 H H    . GLU   B 1 114 ? 32.583 -19.533 -0.150  1.00 14.45 ?  114 GLU   B H    1 
ATOM   5703 H HA   . GLU   B 1 114 ? 31.689 -18.243 -2.205  1.00 14.91 ?  114 GLU   B HA   1 
ATOM   5704 H HB2  . GLU   B 1 114 ? 31.460 -17.660 0.531   1.00 15.78 ?  114 GLU   B HB2  1 
ATOM   5705 H HB3  . GLU   B 1 114 ? 30.802 -16.705 -0.562  1.00 15.78 ?  114 GLU   B HB3  1 
ATOM   5706 H HG2  . GLU   B 1 114 ? 29.423 -18.364 -1.276  1.00 15.87 ?  114 GLU   B HG2  1 
ATOM   5707 H HG3  . GLU   B 1 114 ? 30.189 -19.444 -0.405  1.00 15.87 ?  114 GLU   B HG3  1 
ATOM   5708 N N    . ASN   B 1 115 ? 34.294 -16.907 -1.028  1.00 11.74 ?  115 ASN   B N    1 
ATOM   5709 C CA   . ASN   B 1 115 ? 35.283 -15.875 -1.322  1.00 11.75 ?  115 ASN   B CA   1 
ATOM   5710 C C    . ASN   B 1 115 ? 35.695 -15.892 -2.785  1.00 11.74 ?  115 ASN   B C    1 
ATOM   5711 O O    . ASN   B 1 115 ? 36.086 -14.855 -3.335  1.00 12.48 ?  115 ASN   B O    1 
ATOM   5712 C CB   . ASN   B 1 115 ? 36.520 -16.059 -0.440  1.00 12.64 ?  115 ASN   B CB   1 
ATOM   5713 C CG   . ASN   B 1 115 ? 36.254 -15.788 1.019   1.00 13.38 ?  115 ASN   B CG   1 
ATOM   5714 O OD1  . ASN   B 1 115 ? 36.245 -14.639 1.454   1.00 15.54 ?  115 ASN   B OD1  1 
ATOM   5715 N ND2  . ASN   B 1 115 ? 36.094 -16.856 1.801   1.00 13.65 ?  115 ASN   B ND2  1 
ATOM   5716 H H    . ASN   B 1 115 ? 34.531 -17.469 -0.414  1.00 14.09 ?  115 ASN   B H    1 
ATOM   5717 H HA   . ASN   B 1 115 ? 34.905 -15.004 -1.124  1.00 14.11 ?  115 ASN   B HA   1 
ATOM   5718 H HB2  . ASN   B 1 115 ? 36.837 -16.972 -0.525  1.00 15.18 ?  115 ASN   B HB2  1 
ATOM   5719 H HB3  . ASN   B 1 115 ? 37.211 -15.442 -0.730  1.00 15.18 ?  115 ASN   B HB3  1 
ATOM   5720 H HD21 . ASN   B 1 115 ? 35.948 -16.764 2.645   1.00 16.39 ?  115 ASN   B HD21 1 
ATOM   5721 H HD22 . ASN   B 1 115 ? 36.119 -17.652 1.461   1.00 16.39 ?  115 ASN   B HD22 1 
ATOM   5722 N N    . PHE   B 1 116 ? 35.668 -17.066 -3.422  1.00 11.30 ?  116 PHE   B N    1 
ATOM   5723 C CA   . PHE   B 1 116 ? 36.095 -17.161 -4.811  1.00 12.05 ?  116 PHE   B CA   1 
ATOM   5724 C C    . PHE   B 1 116 ? 35.196 -16.335 -5.722  1.00 11.60 ?  116 PHE   B C    1 
ATOM   5725 O O    . PHE   B 1 116 ? 35.628 -15.919 -6.797  1.00 12.33 ?  116 PHE   B O    1 
ATOM   5726 C CB   . PHE   B 1 116 ? 36.058 -18.610 -5.330  1.00 11.51 ?  116 PHE   B CB   1 
ATOM   5727 C CG   . PHE   B 1 116 ? 37.128 -19.562 -4.782  1.00 11.64 ?  116 PHE   B CG   1 
ATOM   5728 C CD1  . PHE   B 1 116 ? 37.782 -19.378 -3.575  1.00 12.34 ?  116 PHE   B CD1  1 
ATOM   5729 C CD2  . PHE   B 1 116 ? 37.438 -20.689 -5.519  1.00 11.99 ?  116 PHE   B CD2  1 
ATOM   5730 C CE1  . PHE   B 1 116 ? 38.716 -20.310 -3.122  1.00 12.59 ?  116 PHE   B CE1  1 
ATOM   5731 C CE2  . PHE   B 1 116 ? 38.368 -21.627 -5.072  1.00 12.09 ?  116 PHE   B CE2  1 
ATOM   5732 C CZ   . PHE   B 1 116 ? 39.003 -21.441 -3.877  1.00 12.22 ?  116 PHE   B CZ   1 
ATOM   5733 H H    . PHE   B 1 116 ? 35.403 -17.815 -3.077  1.00 13.57 ?  116 PHE   B H    1 
ATOM   5734 H HA   . PHE   B 1 116 ? 37.002 -16.837 -4.895  1.00 14.47 ?  116 PHE   B HA   1 
ATOM   5735 H HB2  . PHE   B 1 116 ? 35.189 -18.990 -5.110  1.00 13.83 ?  116 PHE   B HB2  1 
ATOM   5736 H HB3  . PHE   B 1 116 ? 36.157 -18.591 -6.296  1.00 13.83 ?  116 PHE   B HB3  1 
ATOM   5737 H HD1  . PHE   B 1 116 ? 37.579 -18.633 -3.053  1.00 14.81 ?  116 PHE   B HD1  1 
ATOM   5738 H HD2  . PHE   B 1 116 ? 36.996 -20.838 -6.328  1.00 14.40 ?  116 PHE   B HD2  1 
ATOM   5739 H HE1  . PHE   B 1 116 ? 39.151 -20.175 -2.309  1.00 15.11 ?  116 PHE   B HE1  1 
ATOM   5740 H HE2  . PHE   B 1 116 ? 38.561 -22.373 -5.588  1.00 14.52 ?  116 PHE   B HE2  1 
ATOM   5741 H HZ   . PHE   B 1 116 ? 39.640 -22.047 -3.581  1.00 14.67 ?  116 PHE   B HZ   1 
ATOM   5742 N N    . ASN   B 1 117 ? 33.925 -16.142 -5.347  1.00 12.15 ?  117 ASN   B N    1 
ATOM   5743 C CA   . ASN   B 1 117 ? 32.985 -15.438 -6.214  1.00 12.82 ?  117 ASN   B CA   1 
ATOM   5744 C C    . ASN   B 1 117 ? 33.300 -13.961 -6.363  1.00 12.80 ?  117 ASN   B C    1 
ATOM   5745 O O    . ASN   B 1 117 ? 32.701 -13.301 -7.216  1.00 13.91 ?  117 ASN   B O    1 
ATOM   5746 C CB   . ASN   B 1 117 ? 31.566 -15.655 -5.710  1.00 12.83 ?  117 ASN   B CB   1 
ATOM   5747 C CG   . ASN   B 1 117 ? 31.111 -17.064 -5.952  1.00 12.99 ?  117 ASN   B CG   1 
ATOM   5748 O OD1  . ASN   B 1 117 ? 31.452 -17.653 -6.977  1.00 14.00 ?  117 ASN   B OD1  1 
ATOM   5749 N ND2  . ASN   B 1 117 ? 30.376 -17.630 -5.009  1.00 12.78 ?  117 ASN   B ND2  1 
ATOM   5750 H H    . ASN   B 1 117 ? 33.597 -16.406 -4.597  1.00 14.58 ?  117 ASN   B H    1 
ATOM   5751 H HA   . ASN   B 1 117 ? 33.041 -15.838 -7.094  1.00 15.40 ?  117 ASN   B HA   1 
ATOM   5752 H HB2  . ASN   B 1 117 ? 31.531 -15.488 -4.754  1.00 15.40 ?  117 ASN   B HB2  1 
ATOM   5753 H HB3  . ASN   B 1 117 ? 30.965 -15.051 -6.177  1.00 15.40 ?  117 ASN   B HB3  1 
ATOM   5754 H HD21 . ASN   B 1 117 ? 30.093 -18.437 -5.105  1.00 15.35 ?  117 ASN   B HD21 1 
ATOM   5755 H HD22 . ASN   B 1 117 ? 30.164 -17.185 -4.302  1.00 15.35 ?  117 ASN   B HD22 1 
ATOM   5756 N N    . GLN   B 1 118 ? 34.234 -13.435 -5.582  1.00 12.37 ?  118 GLN   B N    1 
ATOM   5757 C CA   . GLN   B 1 118 ? 34.659 -12.048 -5.718  1.00 13.06 ?  118 GLN   B CA   1 
ATOM   5758 C C    . GLN   B 1 118 ? 35.725 -11.857 -6.790  1.00 13.21 ?  118 GLN   B C    1 
ATOM   5759 O O    . GLN   B 1 118 ? 36.199 -10.734 -6.968  1.00 14.75 ?  118 GLN   B O    1 
ATOM   5760 C CB   . GLN   B 1 118 ? 35.133 -11.515 -4.362  1.00 13.74 ?  118 GLN   B CB   1 
ATOM   5761 C CG   . GLN   B 1 118 ? 34.048 -11.544 -3.293  1.00 13.94 ?  118 GLN   B CG   1 
ATOM   5762 C CD   . GLN   B 1 118 ? 32.879 -10.642 -3.632  1.00 13.82 ?  118 GLN   B CD   1 
ATOM   5763 O OE1  . GLN   B 1 118 ? 33.063 -9.505  -4.081  1.00 14.70 ?  118 GLN   B OE1  1 
ATOM   5764 N NE2  . GLN   B 1 118 ? 31.668 -11.139 -3.426  1.00 14.41 ?  118 GLN   B NE2  1 
ATOM   5765 H H    . GLN   B 1 118 ? 34.655 -13.865 -4.964  1.00 14.85 ?  118 GLN   B H    1 
ATOM   5766 H HA   . GLN   B 1 118 ? 33.890 -11.523 -5.987  1.00 15.68 ?  118 GLN   B HA   1 
ATOM   5767 H HB2  . GLN   B 1 118 ? 35.874 -12.051 -4.051  1.00 16.50 ?  118 GLN   B HB2  1 
ATOM   5768 H HB3  . GLN   B 1 118 ? 35.413 -10.589 -4.468  1.00 16.50 ?  118 GLN   B HB3  1 
ATOM   5769 H HG2  . GLN   B 1 118 ? 33.718 -12.453 -3.204  1.00 16.74 ?  118 GLN   B HG2  1 
ATOM   5770 H HG3  . GLN   B 1 118 ? 34.428 -11.247 -2.450  1.00 16.74 ?  118 GLN   B HG3  1 
ATOM   5771 H HE21 . GLN   B 1 118 ? 31.580 -11.938 -3.113  1.00 17.30 ?  118 GLN   B HE21 1 
ATOM   5772 H HE22 . GLN   B 1 118 ? 30.979 -10.666 -3.601  1.00 17.30 ?  118 GLN   B HE22 1 
ATOM   5773 N N    . HIS   B 1 119 ? 36.074 -12.911 -7.526  1.00 12.32 ?  119 HIS   B N    1 
ATOM   5774 C CA   . HIS   B 1 119 ? 37.120 -12.859 -8.538  1.00 12.80 ?  119 HIS   B CA   1 
ATOM   5775 C C    . HIS   B 1 119 ? 36.645 -13.588 -9.782  1.00 12.88 ?  119 HIS   B C    1 
ATOM   5776 O O    . HIS   B 1 119 ? 36.134 -14.703 -9.685  1.00 13.75 ?  119 HIS   B O    1 
ATOM   5777 C CB   . HIS   B 1 119 ? 38.397 -13.492 -7.986  1.00 13.18 ?  119 HIS   B CB   1 
ATOM   5778 C CG   . HIS   B 1 119 ? 38.876 -12.800 -6.757  1.00 14.29 ?  119 HIS   B CG   1 
ATOM   5779 N ND1  . HIS   B 1 119 ? 39.678 -11.680 -6.806  1.00 15.83 ?  119 HIS   B ND1  1 
ATOM   5780 C CD2  . HIS   B 1 119 ? 38.587 -13.002 -5.452  1.00 15.31 ?  119 HIS   B CD2  1 
ATOM   5781 C CE1  . HIS   B 1 119 ? 39.895 -11.250 -5.577  1.00 16.97 ?  119 HIS   B CE1  1 
ATOM   5782 N NE2  . HIS   B 1 119 ? 39.234 -12.026 -4.738  1.00 16.86 ?  119 HIS   B NE2  1 
ATOM   5783 H H    . HIS   B 1 119 ? 35.701 -13.685 -7.459  1.00 14.80 ?  119 HIS   B H    1 
ATOM   5784 H HA   . HIS   B 1 119 ? 37.301 -11.931 -8.770  1.00 15.37 ?  119 HIS   B HA   1 
ATOM   5785 H HB2  . HIS   B 1 119 ? 38.217 -14.416 -7.769  1.00 15.83 ?  119 HIS   B HB2  1 
ATOM   5786 H HB3  . HIS   B 1 119 ? 39.090 -13.432 -8.663  1.00 15.83 ?  119 HIS   B HB3  1 
ATOM   5787 H HD2  . HIS   B 1 119 ? 38.050 -13.677 -5.104  1.00 18.38 ?  119 HIS   B HD2  1 
ATOM   5788 H HE1  . HIS   B 1 119 ? 40.435 -10.528 -5.339  1.00 20.37 ?  119 HIS   B HE1  1 
ATOM   5789 H HE2  . HIS   B 1 119 ? 39.244 -11.955 -3.879  1.00 20.24 ?  119 HIS   B HE2  1 
ATOM   5790 N N    . GLU   B 1 120 ? 36.807 -12.971 -10.949 1.00 13.40 ?  120 GLU   B N    1 
ATOM   5791 C CA   . GLU   B 1 120 ? 36.222 -13.549 -12.152 1.00 15.33 ?  120 GLU   B CA   1 
ATOM   5792 C C    . GLU   B 1 120 ? 36.890 -14.854 -12.557 1.00 14.03 ?  120 GLU   B C    1 
ATOM   5793 O O    . GLU   B 1 120 ? 36.222 -15.728 -13.122 1.00 14.47 ?  120 GLU   B O    1 
ATOM   5794 C CB   . GLU   B 1 120 ? 36.261 -12.542 -13.297 1.00 20.33 ?  120 GLU   B CB   1 
ATOM   5795 C CG   . GLU   B 1 120 ? 35.311 -11.374 -13.090 1.00 26.68 ?  120 GLU   B CG   1 
ATOM   5796 C CD   . GLU   B 1 120 ? 35.151 -10.515 -14.327 1.00 32.74 ?  120 GLU   B CD   1 
ATOM   5797 O OE1  . GLU   B 1 120 ? 36.141 -10.354 -15.072 1.00 35.16 ?  120 GLU   B OE1  1 
ATOM   5798 O OE2  . GLU   B 1 120 ? 34.035 -10.002 -14.552 1.00 35.48 -1 120 GLU   B OE2  1 
ATOM   5799 H H    . GLU   B 1 120 ? 37.242 -12.232 -11.071 1.00 16.09 ?  120 GLU   B H    1 
ATOM   5800 H HA   . GLU   B 1 120 ? 35.296 -13.747 -11.972 1.00 18.40 ?  120 GLU   B HA   1 
ATOM   5801 H HB2  . GLU   B 1 120 ? 37.155 -12.181 -13.381 1.00 24.41 ?  120 GLU   B HB2  1 
ATOM   5802 H HB3  . GLU   B 1 120 ? 36.004 -12.987 -14.121 1.00 24.41 ?  120 GLU   B HB3  1 
ATOM   5803 H HG2  . GLU   B 1 120 ? 34.433 -11.713 -12.847 1.00 32.03 ?  120 GLU   B HG2  1 
ATOM   5804 H HG3  . GLU   B 1 120 ? 35.652 -10.805 -12.383 1.00 32.03 ?  120 GLU   B HG3  1 
ATOM   5805 N N    . VAL   B 1 121 ? 38.190 -15.000 -12.294 1.00 13.62 ?  121 VAL   B N    1 
ATOM   5806 C CA   . VAL   B 1 121 ? 38.931 -16.210 -12.642 1.00 13.24 ?  121 VAL   B CA   1 
ATOM   5807 C C    . VAL   B 1 121 ? 40.039 -16.420 -11.618 1.00 12.54 ?  121 VAL   B C    1 
ATOM   5808 O O    . VAL   B 1 121 ? 40.717 -15.467 -11.223 1.00 13.41 ?  121 VAL   B O    1 
ATOM   5809 C CB   . VAL   B 1 121 ? 39.451 -16.154 -14.096 1.00 15.10 ?  121 VAL   B CB   1 
ATOM   5810 C CG1  . VAL   B 1 121 ? 40.334 -14.934 -14.329 1.00 16.69 ?  121 VAL   B CG1  1 
ATOM   5811 C CG2  . VAL   B 1 121 ? 40.191 -17.431 -14.447 1.00 16.45 ?  121 VAL   B CG2  1 
ATOM   5812 H H    . VAL   B 1 121 ? 38.679 -14.399 -11.915 1.00 16.35 ?  121 VAL   B H    1 
ATOM   5813 H HA   . VAL   B 1 121 ? 38.322 -16.961 -12.585 1.00 15.89 ?  121 VAL   B HA   1 
ATOM   5814 H HB   . VAL   B 1 121 ? 38.691 -16.085 -14.699 1.00 18.13 ?  121 VAL   B HB   1 
ATOM   5815 H HG11 . VAL   B 1 121 ? 40.644 -14.937 -15.249 1.00 20.04 ?  121 VAL   B HG11 1 
ATOM   5816 H HG12 . VAL   B 1 121 ? 39.815 -14.131 -14.160 1.00 20.04 ?  121 VAL   B HG12 1 
ATOM   5817 H HG13 . VAL   B 1 121 ? 41.092 -14.972 -13.726 1.00 20.04 ?  121 VAL   B HG13 1 
ATOM   5818 H HG21 . VAL   B 1 121 ? 40.389 -17.431 -15.399 1.00 19.74 ?  121 VAL   B HG21 1 
ATOM   5819 H HG22 . VAL   B 1 121 ? 41.019 -17.467 -13.942 1.00 19.74 ?  121 VAL   B HG22 1 
ATOM   5820 H HG23 . VAL   B 1 121 ? 39.633 -18.192 -14.228 1.00 19.74 ?  121 VAL   B HG23 1 
ATOM   5821 N N    . LEU   B 1 122 ? 40.218 -17.671 -11.183 1.00 12.09 ?  122 LEU   B N    1 
ATOM   5822 C CA   . LEU   B 1 122 ? 41.198 -18.026 -10.159 1.00 12.00 ?  122 LEU   B CA   1 
ATOM   5823 C C    . LEU   B 1 122 ? 41.856 -19.355 -10.490 1.00 11.64 ?  122 LEU   B C    1 
ATOM   5824 O O    . LEU   B 1 122 ? 41.199 -20.273 -10.996 1.00 12.98 ?  122 LEU   B O    1 
ATOM   5825 C CB   . LEU   B 1 122 ? 40.543 -18.256 -8.785  1.00 13.84 ?  122 LEU   B CB   1 
ATOM   5826 C CG   . LEU   B 1 122 ? 39.515 -17.232 -8.299  1.00 13.91 ?  122 LEU   B CG   1 
ATOM   5827 C CD1  . LEU   B 1 122 ? 38.112 -17.575 -8.772  1.00 15.18 ?  122 LEU   B CD1  1 
ATOM   5828 C CD2  . LEU   B 1 122 ? 39.560 -17.124 -6.791  1.00 13.48 ?  122 LEU   B CD2  1 
ATOM   5829 H H    . LEU   B 1 122 ? 39.769 -18.350 -11.472 1.00 14.52 ?  122 LEU   B H    1 
ATOM   5830 H HA   . LEU   B 1 122 ? 41.870 -17.333 -10.077 1.00 14.41 ?  122 LEU   B HA   1 
ATOM   5831 H HB2  . LEU   B 1 122 ? 40.083 -19.111 -8.809  1.00 16.61 ?  122 LEU   B HB2  1 
ATOM   5832 H HB3  . LEU   B 1 122 ? 41.241 -18.290 -8.117  1.00 16.61 ?  122 LEU   B HB3  1 
ATOM   5833 H HG   . LEU   B 1 122 ? 39.748 -16.359 -8.659  1.00 16.70 ?  122 LEU   B HG   1 
ATOM   5834 H HD11 . LEU   B 1 122 ? 37.492 -16.922 -8.410  1.00 18.22 ?  122 LEU   B HD11 1 
ATOM   5835 H HD12 . LEU   B 1 122 ? 38.094 -17.545 -9.740  1.00 18.22 ?  122 LEU   B HD12 1 
ATOM   5836 H HD13 . LEU   B 1 122 ? 37.884 -18.460 -8.458  1.00 18.22 ?  122 LEU   B HD13 1 
ATOM   5837 H HD21 . LEU   B 1 122 ? 38.885 -16.496 -6.494  1.00 16.19 ?  122 LEU   B HD21 1 
ATOM   5838 H HD22 . LEU   B 1 122 ? 39.394 -17.998 -6.406  1.00 16.19 ?  122 LEU   B HD22 1 
ATOM   5839 H HD23 . LEU   B 1 122 ? 40.442 -16.810 -6.521  1.00 16.19 ?  122 LEU   B HD23 1 
ATOM   5840 N N    . LEU   B 1 123 ? 43.140 -19.466 -10.130 1.00 11.36 ?  123 LEU   B N    1 
ATOM   5841 C CA   . LEU   B 1 123 ? 43.851 -20.736 -10.015 1.00 11.75 ?  123 LEU   B CA   1 
ATOM   5842 C C    . LEU   B 1 123 ? 43.826 -21.131 -8.547  1.00 11.36 ?  123 LEU   B C    1 
ATOM   5843 O O    . LEU   B 1 123 ? 44.183 -20.309 -7.694  1.00 12.22 ?  123 LEU   B O    1 
ATOM   5844 C CB   . LEU   B 1 123 ? 45.297 -20.553 -10.475 1.00 12.39 ?  123 LEU   B CB   1 
ATOM   5845 C CG   . LEU   B 1 123 ? 46.235 -21.739 -10.245 1.00 12.69 ?  123 LEU   B CG   1 
ATOM   5846 C CD1  . LEU   B 1 123 ? 45.805 -22.975 -11.037 1.00 12.93 ?  123 LEU   B CD1  1 
ATOM   5847 C CD2  . LEU   B 1 123 ? 47.645 -21.336 -10.616 1.00 13.49 ?  123 LEU   B CD2  1 
ATOM   5848 H H    . LEU   B 1 123 ? 43.635 -18.785 -9.938  1.00 13.64 ?  123 LEU   B H    1 
ATOM   5849 H HA   . LEU   B 1 123 ? 43.411 -21.421 -10.547 1.00 14.10 ?  123 LEU   B HA   1 
ATOM   5850 H HB2  . LEU   B 1 123 ? 45.289 -20.375 -11.427 1.00 14.87 ?  123 LEU   B HB2  1 
ATOM   5851 H HB3  . LEU   B 1 123 ? 45.670 -19.797 -10.004 1.00 14.87 ?  123 LEU   B HB3  1 
ATOM   5852 H HG   . LEU   B 1 123 ? 46.236 -21.978 -9.304  1.00 15.24 ?  123 LEU   B HG   1 
ATOM   5853 H HD11 . LEU   B 1 123 ? 46.439 -23.692 -10.877 1.00 15.53 ?  123 LEU   B HD11 1 
ATOM   5854 H HD12 . LEU   B 1 123 ? 44.920 -23.245 -10.744 1.00 15.53 ?  123 LEU   B HD12 1 
ATOM   5855 H HD13 . LEU   B 1 123 ? 45.788 -22.754 -11.981 1.00 15.53 ?  123 LEU   B HD13 1 
ATOM   5856 H HD21 . LEU   B 1 123 ? 48.239 -22.088 -10.474 1.00 16.20 ?  123 LEU   B HD21 1 
ATOM   5857 H HD22 . LEU   B 1 123 ? 47.660 -21.072 -11.549 1.00 16.20 ?  123 LEU   B HD22 1 
ATOM   5858 H HD23 . LEU   B 1 123 ? 47.914 -20.590 -10.057 1.00 16.20 ?  123 LEU   B HD23 1 
ATOM   5859 N N    . ALA   B 1 124 ? 43.381 -22.357 -8.243  1.00 11.43 ?  124 ALA   B N    1 
ATOM   5860 C CA   . ALA   B 1 124 ? 43.131 -22.681 -6.847  1.00 11.70 ?  124 ALA   B CA   1 
ATOM   5861 C C    . ALA   B 1 124 ? 43.402 -24.140 -6.515  1.00 11.42 ?  124 ALA   B C    1 
ATOM   5862 O O    . ALA   B 1 124 ? 43.267 -25.014 -7.381  1.00 11.90 ?  124 ALA   B O    1 
ATOM   5863 C CB   . ALA   B 1 124 ? 41.678 -22.370 -6.478  1.00 12.22 ?  124 ALA   B CB   1 
ATOM   5864 H H    . ALA   B 1 124 ? 43.218 -22.993 -8.803  1.00 13.72 ?  124 ALA   B H    1 
ATOM   5865 H HA   . ALA   B 1 124 ? 43.704 -22.127 -6.298  1.00 14.04 ?  124 ALA   B HA   1 
ATOM   5866 H HB1  . ALA   B 1 124 ? 41.528 -22.590 -5.544  1.00 14.67 ?  124 ALA   B HB1  1 
ATOM   5867 H HB2  . ALA   B 1 124 ? 41.510 -21.423 -6.622  1.00 14.67 ?  124 ALA   B HB2  1 
ATOM   5868 H HB3  . ALA   B 1 124 ? 41.086 -22.897 -7.039  1.00 14.67 ?  124 ALA   B HB3  1 
ATOM   5869 N N    . PRO   B 1 125 ? 43.704 -24.429 -5.254  1.00 11.67 ?  125 PRO   B N    1 
ATOM   5870 C CA   . PRO   B 1 125 ? 43.647 -25.795 -4.734  1.00 12.35 ?  125 PRO   B CA   1 
ATOM   5871 C C    . PRO   B 1 125 ? 42.246 -26.069 -4.187  1.00 12.39 ?  125 PRO   B C    1 
ATOM   5872 O O    . PRO   B 1 125 ? 41.447 -25.155 -3.980  1.00 13.16 ?  125 PRO   B O    1 
ATOM   5873 C CB   . PRO   B 1 125 ? 44.636 -25.714 -3.567  1.00 13.44 ?  125 PRO   B CB   1 
ATOM   5874 C CG   . PRO   B 1 125 ? 44.390 -24.327 -2.996  1.00 13.64 ?  125 PRO   B CG   1 
ATOM   5875 C CD   . PRO   B 1 125 ? 44.015 -23.457 -4.187  1.00 12.43 ?  125 PRO   B CD   1 
ATOM   5876 H HA   . PRO   B 1 125 ? 43.917 -26.458 -5.384  1.00 14.83 ?  125 PRO   B HA   1 
ATOM   5877 H HB2  . PRO   B 1 125 ? 44.436 -26.398 -2.908  1.00 16.14 ?  125 PRO   B HB2  1 
ATOM   5878 H HB3  . PRO   B 1 125 ? 45.545 -25.798 -3.893  1.00 16.14 ?  125 PRO   B HB3  1 
ATOM   5879 H HG2  . PRO   B 1 125 ? 43.663 -24.356 -2.354  1.00 16.38 ?  125 PRO   B HG2  1 
ATOM   5880 H HG3  . PRO   B 1 125 ? 45.202 -23.996 -2.571  1.00 16.38 ?  125 PRO   B HG3  1 
ATOM   5881 H HD2  . PRO   B 1 125 ? 43.240 -22.912 -3.980  1.00 14.92 ?  125 PRO   B HD2  1 
ATOM   5882 H HD3  . PRO   B 1 125 ? 44.774 -22.900 -4.447  1.00 14.92 ?  125 PRO   B HD3  1 
ATOM   5883 N N    . LEU   B 1 126 ? 41.979 -27.343 -3.906  1.00 12.93 ?  126 LEU   B N    1 
ATOM   5884 C CA   . LEU   B 1 126 ? 40.762 -27.708 -3.191  1.00 13.37 ?  126 LEU   B CA   1 
ATOM   5885 C C    . LEU   B 1 126 ? 40.882 -27.306 -1.727  1.00 13.44 ?  126 LEU   B C    1 
ATOM   5886 O O    . LEU   B 1 126 ? 41.781 -27.762 -1.016  1.00 15.50 ?  126 LEU   B O    1 
ATOM   5887 C CB   . LEU   B 1 126 ? 40.508 -29.205 -3.302  1.00 15.00 ?  126 LEU   B CB   1 
ATOM   5888 C CG   . LEU   B 1 126 ? 39.998 -29.689 -4.657  1.00 15.90 ?  126 LEU   B CG   1 
ATOM   5889 C CD1  . LEU   B 1 126 ? 40.014 -31.198 -4.724  1.00 17.76 ?  126 LEU   B CD1  1 
ATOM   5890 C CD2  . LEU   B 1 126 ? 38.592 -29.169 -4.920  1.00 16.63 ?  126 LEU   B CD2  1 
ATOM   5891 H H    . LEU   B 1 126 ? 42.487 -28.010 -4.106  1.00 15.52 ?  126 LEU   B H    1 
ATOM   5892 H HA   . LEU   B 1 126 ? 40.010 -27.233 -3.577  1.00 16.05 ?  126 LEU   B HA   1 
ATOM   5893 H HB2  . LEU   B 1 126 ? 41.336 -29.670 -3.119  1.00 18.01 ?  126 LEU   B HB2  1 
ATOM   5894 H HB3  . LEU   B 1 126 ? 39.843 -29.452 -2.638  1.00 18.01 ?  126 LEU   B HB3  1 
ATOM   5895 H HG   . LEU   B 1 126 ? 40.582 -29.347 -5.355  1.00 19.09 ?  126 LEU   B HG   1 
ATOM   5896 H HD11 . LEU   B 1 126 ? 39.689 -31.479 -5.593  1.00 21.32 ?  126 LEU   B HD11 1 
ATOM   5897 H HD12 . LEU   B 1 126 ? 40.920 -31.512 -4.590  1.00 21.32 ?  126 LEU   B HD12 1 
ATOM   5898 H HD13 . LEU   B 1 126 ? 39.435 -31.548 -4.027  1.00 21.32 ?  126 LEU   B HD13 1 
ATOM   5899 H HD21 . LEU   B 1 126 ? 38.243 -29.600 -5.715  1.00 19.96 ?  126 LEU   B HD21 1 
ATOM   5900 H HD22 . LEU   B 1 126 ? 38.034 -29.375 -4.157  1.00 19.96 ?  126 LEU   B HD22 1 
ATOM   5901 H HD23 . LEU   B 1 126 ? 38.629 -28.208 -5.055  1.00 19.96 ?  126 LEU   B HD23 1 
ATOM   5902 N N    . LEU   B 1 127 ? 39.959 -26.474 -1.265  1.00 13.11 ?  127 LEU   B N    1 
ATOM   5903 C CA   . LEU   B 1 127 ? 40.021 -25.993 0.102   1.00 13.54 ?  127 LEU   B CA   1 
ATOM   5904 C C    . LEU   B 1 127 ? 39.739 -27.112 1.094   1.00 13.50 ?  127 LEU   B C    1 
ATOM   5905 O O    . LEU   B 1 127 ? 38.912 -28.001 0.864   1.00 13.85 ?  127 LEU   B O    1 
ATOM   5906 C CB   . LEU   B 1 127 ? 39.016 -24.862 0.322   1.00 14.34 ?  127 LEU   B CB   1 
ATOM   5907 C CG   . LEU   B 1 127 ? 39.189 -23.598 -0.516  1.00 15.39 ?  127 LEU   B CG   1 
ATOM   5908 C CD1  . LEU   B 1 127 ? 38.068 -22.631 -0.194  1.00 15.88 ?  127 LEU   B CD1  1 
ATOM   5909 C CD2  . LEU   B 1 127 ? 40.543 -22.946 -0.270  1.00 16.23 ?  127 LEU   B CD2  1 
ATOM   5910 H H    . LEU   B 1 127 ? 39.289 -26.168 -1.720  1.00 15.74 ?  127 LEU   B H    1 
ATOM   5911 H HA   . LEU   B 1 127 ? 40.910 -25.641 0.276   1.00 16.26 ?  127 LEU   B HA   1 
ATOM   5912 H HB2  . LEU   B 1 127 ? 38.129 -25.210 0.137   1.00 17.22 ?  127 LEU   B HB2  1 
ATOM   5913 H HB3  . LEU   B 1 127 ? 39.063 -24.595 1.254   1.00 17.22 ?  127 LEU   B HB3  1 
ATOM   5914 H HG   . LEU   B 1 127 ? 39.119 -23.822 -1.455  1.00 18.48 ?  127 LEU   B HG   1 
ATOM   5915 H HD11 . LEU   B 1 127 ? 38.178 -21.822 -0.724  1.00 19.06 ?  127 LEU   B HD11 1 
ATOM   5916 H HD12 . LEU   B 1 127 ? 37.213 -23.042 -0.402  1.00 19.06 ?  127 LEU   B HD12 1 
ATOM   5917 H HD13 . LEU   B 1 127 ? 38.100 -22.405 0.752   1.00 19.06 ?  127 LEU   B HD13 1 
ATOM   5918 H HD21 . LEU   B 1 127 ? 40.580 -22.101 -0.744  1.00 19.48 ?  127 LEU   B HD21 1 
ATOM   5919 H HD22 . LEU   B 1 127 ? 40.652 -22.793 0.684   1.00 19.48 ?  127 LEU   B HD22 1 
ATOM   5920 H HD23 . LEU   B 1 127 ? 41.238 -23.539 -0.591  1.00 19.48 ?  127 LEU   B HD23 1 
ATOM   5921 N N    . SER   B 1 128 ? 40.414 -27.024 2.231   1.00 13.44 ?  128 SER   B N    1 
ATOM   5922 C CA   . SER   B 1 128 ? 40.302 -27.932 3.360   1.00 14.23 ?  128 SER   B CA   1 
ATOM   5923 C C    . SER   B 1 128 ? 40.785 -29.342 3.041   1.00 15.30 ?  128 SER   B C    1 
ATOM   5924 O O    . SER   B 1 128 ? 40.691 -30.214 3.899   1.00 16.76 ?  128 SER   B O    1 
ATOM   5925 C CB   . SER   B 1 128 ? 38.906 -27.939 3.996   1.00 14.56 ?  128 SER   B CB   1 
ATOM   5926 O OG   . SER   B 1 128 ? 38.594 -26.656 4.528   1.00 15.09 ?  128 SER   B OG   1 
ATOM   5927 H H    . SER   B 1 128 ? 40.978 -26.391 2.382   1.00 16.13 ?  128 SER   B H    1 
ATOM   5928 H HA   . SER   B 1 128 ? 40.898 -27.597 4.042   1.00 17.08 ?  128 SER   B HA   1 
ATOM   5929 H HB2  . SER   B 1 128 ? 38.247 -28.185 3.330   1.00 17.48 ?  128 SER   B HB2  1 
ATOM   5930 H HB3  . SER   B 1 128 ? 38.895 -28.598 4.723   1.00 17.48 ?  128 SER   B HB3  1 
ATOM   5931 H HG   . SER   B 1 128 ? 39.163 -26.447 5.107   1.00 18.12 ?  128 SER   B HG   1 
ATOM   5932 N N    . ALA   B 1 129 ? 41.352 -29.573 1.854   1.00 16.25 ?  129 ALA   B N    1 
ATOM   5933 C CA   . ALA   B 1 129 ? 41.896 -30.873 1.506   1.00 17.50 ?  129 ALA   B CA   1 
ATOM   5934 C C    . ALA   B 1 129 ? 43.288 -31.038 2.099   1.00 16.41 ?  129 ALA   B C    1 
ATOM   5935 O O    . ALA   B 1 129 ? 43.848 -30.130 2.731   1.00 16.35 ?  129 ALA   B O    1 
ATOM   5936 C CB   . ALA   B 1 129 ? 41.941 -31.046 -0.010  1.00 19.58 ?  129 ALA   B CB   1 
ATOM   5937 H H    . ALA   B 1 129 ? 41.434 -28.986 1.228   1.00 19.51 ?  129 ALA   B H    1 
ATOM   5938 H HA   . ALA   B 1 129 ? 41.329 -31.565 1.873   1.00 21.01 ?  129 ALA   B HA   1 
ATOM   5939 H HB1  . ALA   B 1 129 ? 42.296 -31.927 -0.218  1.00 23.51 ?  129 ALA   B HB1  1 
ATOM   5940 H HB2  . ALA   B 1 129 ? 41.042 -30.963 -0.363  1.00 23.51 ?  129 ALA   B HB2  1 
ATOM   5941 H HB3  . ALA   B 1 129 ? 42.513 -30.362 -0.392  1.00 23.51 ?  129 ALA   B HB3  1 
ATOM   5942 N N    . GLY   B 1 130 ? 43.850 -32.225 1.877   1.00 16.06 ?  130 GLY   B N    1 
ATOM   5943 C CA   . GLY   B 1 130 ? 45.237 -32.469 2.225   1.00 16.77 ?  130 GLY   B CA   1 
ATOM   5944 C C    . GLY   B 1 130 ? 45.446 -32.362 3.716   1.00 16.85 ?  130 GLY   B C    1 
ATOM   5945 O O    . GLY   B 1 130 ? 44.743 -32.996 4.515   1.00 17.65 ?  130 GLY   B O    1 
ATOM   5946 H H    . GLY   B 1 130 ? 43.451 -32.902 1.522   1.00 19.28 ?  130 GLY   B H    1 
ATOM   5947 H HA2  . GLY   B 1 130 ? 45.498 -33.360 1.936   1.00 20.13 ?  130 GLY   B HA2  1 
ATOM   5948 H HA3  . GLY   B 1 130 ? 45.807 -31.822 1.780   1.00 20.13 ?  130 GLY   B HA3  1 
ATOM   5949 N N    . ILE   B 1 131 ? 46.424 -31.536 4.103   1.00 17.14 ?  131 ILE   B N    1 
ATOM   5950 C CA   . ILE   B 1 131 ? 46.776 -31.408 5.510   1.00 17.73 ?  131 ILE   B CA   1 
ATOM   5951 C C    . ILE   B 1 131 ? 45.662 -30.800 6.344   1.00 17.38 ?  131 ILE   B C    1 
ATOM   5952 O O    . ILE   B 1 131 ? 45.742 -30.849 7.573   1.00 19.01 ?  131 ILE   B O    1 
ATOM   5953 C CB   . ILE   B 1 131 ? 48.100 -30.639 5.712   1.00 19.70 ?  131 ILE   B CB   1 
ATOM   5954 C CG1  . ILE   B 1 131 ? 47.949 -29.166 5.312   1.00 20.54 ?  131 ILE   B CG1  1 
ATOM   5955 C CG2  . ILE   B 1 131 ? 49.228 -31.312 4.928   1.00 20.71 ?  131 ILE   B CG2  1 
ATOM   5956 C CD1  . ILE   B 1 131 ? 49.161 -28.317 5.630   1.00 21.44 ?  131 ILE   B CD1  1 
ATOM   5957 H H    . ILE   B 1 131 ? 46.889 -31.043 3.573   1.00 20.57 ?  131 ILE   B H    1 
ATOM   5958 H HA   . ILE   B 1 131 ? 46.915 -32.301 5.856   1.00 21.28 ?  131 ILE   B HA   1 
ATOM   5959 H HB   . ILE   B 1 131 ? 48.323 -30.674 6.656   1.00 23.64 ?  131 ILE   B HB   1 
ATOM   5960 H HG12 . ILE   B 1 131 ? 47.790 -29.119 4.357   1.00 24.66 ?  131 ILE   B HG12 1 
ATOM   5961 H HG13 . ILE   B 1 131 ? 47.191 -28.782 5.786   1.00 24.66 ?  131 ILE   B HG13 1 
ATOM   5962 H HG21 . ILE   B 1 131 ? 50.070 -30.911 5.188   1.00 24.86 ?  131 ILE   B HG21 1 
ATOM   5963 H HG22 . ILE   B 1 131 ? 49.229 -32.257 5.133   1.00 24.86 ?  131 ILE   B HG22 1 
ATOM   5964 H HG23 . ILE   B 1 131 ? 49.071 -31.176 3.980   1.00 24.86 ?  131 ILE   B HG23 1 
ATOM   5965 H HD11 . ILE   B 1 131 ? 48.953 -27.389 5.435   1.00 25.74 ?  131 ILE   B HD11 1 
ATOM   5966 H HD12 . ILE   B 1 131 ? 49.377 -28.417 6.570   1.00 25.74 ?  131 ILE   B HD12 1 
ATOM   5967 H HD13 . ILE   B 1 131 ? 49.904 -28.612 5.084   1.00 25.74 ?  131 ILE   B HD13 1 
ATOM   5968 N N    . PHE   B 1 132 ? 44.630 -30.224 5.714   1.00 16.23 ?  132 PHE   B N    1 
ATOM   5969 C CA   . PHE   B 1 132 ? 43.473 -29.716 6.442   1.00 16.51 ?  132 PHE   B CA   1 
ATOM   5970 C C    . PHE   B 1 132 ? 42.448 -30.804 6.764   1.00 17.93 ?  132 PHE   B C    1 
ATOM   5971 O O    . PHE   B 1 132 ? 41.539 -30.557 7.561   1.00 19.62 ?  132 PHE   B O    1 
ATOM   5972 C CB   . PHE   B 1 132 ? 42.805 -28.585 5.651   1.00 15.80 ?  132 PHE   B CB   1 
ATOM   5973 C CG   . PHE   B 1 132 ? 43.508 -27.244 5.763   1.00 15.76 ?  132 PHE   B CG   1 
ATOM   5974 C CD1  . PHE   B 1 132 ? 44.802 -27.060 5.298   1.00 17.03 ?  132 PHE   B CD1  1 
ATOM   5975 C CD2  . PHE   B 1 132 ? 42.838 -26.146 6.285   1.00 15.52 ?  132 PHE   B CD2  1 
ATOM   5976 C CE1  . PHE   B 1 132 ? 45.426 -25.818 5.393   1.00 17.41 ?  132 PHE   B CE1  1 
ATOM   5977 C CE2  . PHE   B 1 132 ? 43.448 -24.900 6.371   1.00 15.99 ?  132 PHE   B CE2  1 
ATOM   5978 C CZ   . PHE   B 1 132 ? 44.743 -24.741 5.929   1.00 17.10 ?  132 PHE   B CZ   1 
ATOM   5979 H H    . PHE   B 1 132 ? 44.581 -30.120 4.859   1.00 19.49 ?  132 PHE   B H    1 
ATOM   5980 H HA   . PHE   B 1 132 ? 43.782 -29.340 7.279   1.00 19.82 ?  132 PHE   B HA   1 
ATOM   5981 H HB2  . PHE   B 1 132 ? 42.796 -28.827 4.713   1.00 18.96 ?  132 PHE   B HB2  1 
ATOM   5982 H HB3  . PHE   B 1 132 ? 41.900 -28.469 5.974   1.00 18.96 ?  132 PHE   B HB3  1 
ATOM   5983 H HD1  . PHE   B 1 132 ? 45.268 -27.784 4.943   1.00 20.45 ?  132 PHE   B HD1  1 
ATOM   5984 H HD2  . PHE   B 1 132 ? 41.964 -26.250 6.586   1.00 18.63 ?  132 PHE   B HD2  1 
ATOM   5985 H HE1  . PHE   B 1 132 ? 46.300 -25.713 5.093   1.00 20.90 ?  132 PHE   B HE1  1 
ATOM   5986 H HE2  . PHE   B 1 132 ? 42.985 -24.180 6.739   1.00 19.20 ?  132 PHE   B HE2  1 
ATOM   5987 H HZ   . PHE   B 1 132 ? 45.155 -23.909 5.994   1.00 20.53 ?  132 PHE   B HZ   1 
ATOM   5988 N N    . GLY   B 1 133 ? 42.555 -31.992 6.157   1.00 17.33 ?  133 GLY   B N    1 
ATOM   5989 C CA   . GLY   B 1 133 ? 41.848 -33.163 6.641   1.00 18.25 ?  133 GLY   B CA   1 
ATOM   5990 C C    . GLY   B 1 133 ? 40.450 -33.415 6.111   1.00 18.40 ?  133 GLY   B C    1 
ATOM   5991 O O    . GLY   B 1 133 ? 39.853 -34.425 6.491   1.00 20.69 ?  133 GLY   B O    1 
ATOM   5992 H H    . GLY   B 1 133 ? 43.037 -32.131 5.456   1.00 20.81 ?  133 GLY   B H    1 
ATOM   5993 H HA2  . GLY   B 1 133 ? 42.382 -33.942 6.430   1.00 21.91 ?  133 GLY   B HA2  1 
ATOM   5994 H HA3  . GLY   B 1 133 ? 41.786 -33.098 7.605   1.00 21.91 ?  133 GLY   B HA3  1 
ATOM   5995 N N    . ALA   B 1 134 ? 39.895 -32.545 5.274   1.00 17.68 ?  134 ALA   B N    1 
ATOM   5996 C CA   . ALA   B 1 134 ? 38.574 -32.823 4.730   1.00 18.13 ?  134 ALA   B CA   1 
ATOM   5997 C C    . ALA   B 1 134 ? 38.670 -33.813 3.575   1.00 17.96 ?  134 ALA   B C    1 
ATOM   5998 O O    . ALA   B 1 134 ? 39.726 -33.995 2.964   1.00 19.06 ?  134 ALA   B O    1 
ATOM   5999 C CB   . ALA   B 1 134 ? 37.901 -31.535 4.258   1.00 18.60 ?  134 ALA   B CB   1 
ATOM   6000 H H    . ALA   B 1 134 ? 40.250 -31.796 5.018   1.00 21.22 ?  134 ALA   B H    1 
ATOM   6001 H HA   . ALA   B 1 134 ? 38.023 -33.212 5.423   1.00 21.77 ?  134 ALA   B HA   1 
ATOM   6002 H HB1  . ALA   B 1 134 ? 37.016 -31.748 3.922   1.00 22.33 ?  134 ALA   B HB1  1 
ATOM   6003 H HB2  . ALA   B 1 134 ? 37.830 -30.920 5.006   1.00 22.33 ?  134 ALA   B HB2  1 
ATOM   6004 H HB3  . ALA   B 1 134 ? 38.435 -31.135 3.553   1.00 22.33 ?  134 ALA   B HB3  1 
ATOM   6005 N N    . ASP   B 1 135 ? 37.544 -34.452 3.282   1.00 18.17 ?  135 ASP   B N    1 
ATOM   6006 C CA   . ASP   B 1 135 ? 37.453 -35.348 2.139   1.00 18.68 ?  135 ASP   B CA   1 
ATOM   6007 C C    . ASP   B 1 135 ? 37.547 -34.510 0.871   1.00 17.54 ?  135 ASP   B C    1 
ATOM   6008 O O    . ASP   B 1 135 ? 36.698 -33.634 0.657   1.00 17.87 ?  135 ASP   B O    1 
ATOM   6009 C CB   . ASP   B 1 135 ? 36.112 -36.081 2.192   1.00 20.49 ?  135 ASP   B CB   1 
ATOM   6010 C CG   . ASP   B 1 135 ? 35.927 -37.074 1.057   1.00 22.38 ?  135 ASP   B CG   1 
ATOM   6011 O OD1  . ASP   B 1 135 ? 36.782 -37.112 0.148   1.00 22.51 ?  135 ASP   B OD1  1 
ATOM   6012 O OD2  . ASP   B 1 135 ? 34.932 -37.840 1.088   1.00 25.42 -1 135 ASP   B OD2  1 
ATOM   6013 H H    . ASP   B 1 135 ? 36.818 -34.382 3.734   1.00 21.81 ?  135 ASP   B H    1 
ATOM   6014 H HA   . ASP   B 1 135 ? 38.173 -35.995 2.168   1.00 22.43 ?  135 ASP   B HA   1 
ATOM   6015 H HB2  . ASP   B 1 135 ? 36.060 -36.570 3.025   1.00 24.60 ?  135 ASP   B HB2  1 
ATOM   6016 H HB3  . ASP   B 1 135 ? 35.399 -35.428 2.139   1.00 24.60 ?  135 ASP   B HB3  1 
ATOM   6017 N N    . PRO   B 1 136 ? 38.548 -34.722 0.016   1.00 17.68 ?  136 PRO   B N    1 
ATOM   6018 C CA   . PRO   B 1 136 ? 38.645 -33.899 -1.200  1.00 16.96 ?  136 PRO   B CA   1 
ATOM   6019 C C    . PRO   B 1 136 ? 37.456 -34.055 -2.124  1.00 16.18 ?  136 PRO   B C    1 
ATOM   6020 O O    . PRO   B 1 136 ? 37.130 -33.105 -2.841  1.00 15.57 ?  136 PRO   B O    1 
ATOM   6021 C CB   . PRO   B 1 136 ? 39.954 -34.374 -1.848  1.00 17.81 ?  136 PRO   B CB   1 
ATOM   6022 C CG   . PRO   B 1 136 ? 40.142 -35.765 -1.321  1.00 19.17 ?  136 PRO   B CG   1 
ATOM   6023 C CD   . PRO   B 1 136 ? 39.605 -35.741 0.079   1.00 18.79 ?  136 PRO   B CD   1 
ATOM   6024 H HA   . PRO   B 1 136 ? 38.735 -32.962 -0.970  1.00 20.36 ?  136 PRO   B HA   1 
ATOM   6025 H HB2  . PRO   B 1 136 ? 39.864 -34.383 -2.816  1.00 21.38 ?  136 PRO   B HB2  1 
ATOM   6026 H HB3  . PRO   B 1 136 ? 40.685 -33.799 -1.576  1.00 21.38 ?  136 PRO   B HB3  1 
ATOM   6027 H HG2  . PRO   B 1 136 ? 39.641 -36.396 -1.864  1.00 23.02 ?  136 PRO   B HG2  1 
ATOM   6028 H HG3  . PRO   B 1 136 ? 41.085 -35.993 -1.316  1.00 23.02 ?  136 PRO   B HG3  1 
ATOM   6029 H HD2  . PRO   B 1 136 ? 39.224 -36.601 0.317   1.00 22.55 ?  136 PRO   B HD2  1 
ATOM   6030 H HD3  . PRO   B 1 136 ? 40.292 -35.470 0.710   1.00 22.55 ?  136 PRO   B HD3  1 
ATOM   6031 N N    . ILE   B 1 137 ? 36.794 -35.216 -2.133  1.00 16.69 ?  137 ILE   B N    1 
ATOM   6032 C CA   . ILE   B 1 137 ? 35.578 -35.377 -2.925  1.00 17.27 ?  137 ILE   B CA   1 
ATOM   6033 C C    . ILE   B 1 137 ? 34.507 -34.410 -2.440  1.00 17.04 ?  137 ILE   B C    1 
ATOM   6034 O O    . ILE   B 1 137 ? 33.796 -33.786 -3.238  1.00 16.44 ?  137 ILE   B O    1 
ATOM   6035 C CB   . ILE   B 1 137 ? 35.103 -36.843 -2.874  1.00 19.03 ?  137 ILE   B CB   1 
ATOM   6036 C CG1  . ILE   B 1 137 ? 36.103 -37.746 -3.600  1.00 21.12 ?  137 ILE   B CG1  1 
ATOM   6037 C CG2  . ILE   B 1 137 ? 33.710 -36.983 -3.478  1.00 19.79 ?  137 ILE   B CG2  1 
ATOM   6038 C CD1  . ILE   B 1 137 ? 35.810 -39.229 -3.468  1.00 23.56 ?  137 ILE   B CD1  1 
ATOM   6039 H H    . ILE   B 1 137 ? 37.031 -35.918 -1.701  1.00 20.03 ?  137 ILE   B H    1 
ATOM   6040 H HA   . ILE   B 1 137 ? 35.773 -35.163 -3.855  1.00 20.73 ?  137 ILE   B HA   1 
ATOM   6041 H HB   . ILE   B 1 137 ? 35.061 -37.116 -1.950  1.00 22.85 ?  137 ILE   B HB   1 
ATOM   6042 H HG12 . ILE   B 1 137 ? 36.096 -37.529 -4.545  1.00 25.35 ?  137 ILE   B HG12 1 
ATOM   6043 H HG13 . ILE   B 1 137 ? 36.987 -37.589 -3.234  1.00 25.35 ?  137 ILE   B HG13 1 
ATOM   6044 H HG21 . ILE   B 1 137 ? 33.457 -37.920 -3.494  1.00 23.75 ?  137 ILE   B HG21 1 
ATOM   6045 H HG22 . ILE   B 1 137 ? 33.075 -36.494 -2.937  1.00 23.75 ?  137 ILE   B HG22 1 
ATOM   6046 H HG23 . ILE   B 1 137 ? 33.720 -36.632 -4.382  1.00 23.75 ?  137 ILE   B HG23 1 
ATOM   6047 H HD11 . ILE   B 1 137 ? 36.412 -39.708 -4.054  1.00 28.28 ?  137 ILE   B HD11 1 
ATOM   6048 H HD12 . ILE   B 1 137 ? 35.953 -39.502 -2.547  1.00 28.28 ?  137 ILE   B HD12 1 
ATOM   6049 H HD13 . ILE   B 1 137 ? 34.895 -39.412 -3.730  1.00 28.28 ?  137 ILE   B HD13 1 
ATOM   6050 N N    . HIS   B 1 138 ? 34.386 -34.261 -1.124  1.00 16.78 ?  138 HIS   B N    1 
ATOM   6051 C CA   . HIS   B 1 138 ? 33.440 -33.296 -0.581  1.00 17.29 ?  138 HIS   B CA   1 
ATOM   6052 C C    . HIS   B 1 138 ? 33.860 -31.868 -0.898  1.00 16.43 ?  138 HIS   B C    1 
ATOM   6053 O O    . HIS   B 1 138 ? 33.015 -31.020 -1.202  1.00 16.77 ?  138 HIS   B O    1 
ATOM   6054 C CB   . HIS   B 1 138 ? 33.320 -33.476 0.923   1.00 18.63 ?  138 HIS   B CB   1 
ATOM   6055 C CG   . HIS   B 1 138 ? 32.390 -32.496 1.560   1.00 19.86 ?  138 HIS   B CG   1 
ATOM   6056 N ND1  . HIS   B 1 138 ? 31.049 -32.434 1.245   1.00 21.13 ?  138 HIS   B ND1  1 
ATOM   6057 C CD2  . HIS   B 1 138 ? 32.611 -31.514 2.465   1.00 20.24 ?  138 HIS   B CD2  1 
ATOM   6058 C CE1  . HIS   B 1 138 ? 30.480 -31.469 1.944   1.00 21.07 ?  138 HIS   B CE1  1 
ATOM   6059 N NE2  . HIS   B 1 138 ? 31.406 -30.895 2.693   1.00 20.65 ?  138 HIS   B NE2  1 
ATOM   6060 H H    . HIS   B 1 138 ? 34.839 -34.698 -0.539  1.00 20.14 ?  138 HIS   B H    1 
ATOM   6061 H HA   . HIS   B 1 138 ? 32.569 -33.456 -0.980  1.00 20.76 ?  138 HIS   B HA   1 
ATOM   6062 H HB2  . HIS   B 1 138 ? 32.980 -34.369 1.106   1.00 22.37 ?  138 HIS   B HB2  1 
ATOM   6063 H HB3  . HIS   B 1 138 ? 34.192 -33.365 1.324   1.00 22.37 ?  138 HIS   B HB3  1 
ATOM   6064 H HD1  . HIS   B 1 138 ? 30.645 -32.951 0.683   1.00 25.36 ?  138 HIS   B HD1  1 
ATOM   6065 H HD2  . HIS   B 1 138 ? 33.416 -31.309 2.872   1.00 24.30 ?  138 HIS   B HD2  1 
ATOM   6066 H HE1  . HIS   B 1 138 ? 29.575 -31.240 1.913   1.00 25.30 ?  138 HIS   B HE1  1 
ATOM   6067 N N    . SER   B 1 139 ? 35.152 -31.570 -0.815  1.00 15.61 ?  139 SER   B N    1 
ATOM   6068 C CA   . SER   B 1 139 ? 35.588 -30.221 -1.134  1.00 14.87 ?  139 SER   B CA   1 
ATOM   6069 C C    . SER   B 1 139 ? 35.253 -29.871 -2.575  1.00 14.17 ?  139 SER   B C    1 
ATOM   6070 O O    . SER   B 1 139 ? 34.806 -28.756 -2.857  1.00 14.37 ?  139 SER   B O    1 
ATOM   6071 C CB   . SER   B 1 139 ? 37.082 -30.085 -0.872  1.00 15.42 ?  139 SER   B CB   1 
ATOM   6072 O OG   . SER   B 1 139 ? 37.490 -28.757 -1.129  1.00 15.98 ?  139 SER   B OG   1 
ATOM   6073 H H    . SER   B 1 139 ? 35.774 -32.115 -0.589  1.00 18.75 ?  139 SER   B H    1 
ATOM   6074 H HA   . SER   B 1 139 ? 35.121 -29.596 -0.562  1.00 17.85 ?  139 SER   B HA   1 
ATOM   6075 H HB2  . SER   B 1 139 ? 37.263 -30.307 0.055   1.00 18.52 ?  139 SER   B HB2  1 
ATOM   6076 H HB3  . SER   B 1 139 ? 37.567 -30.690 -1.460  1.00 18.52 ?  139 SER   B HB3  1 
ATOM   6077 H HG   . SER   B 1 139 ? 38.320 -28.681 -0.982  1.00 19.19 ?  139 SER   B HG   1 
ATOM   6078 N N    . LEU   B 1 140 ? 35.433 -30.819 -3.497  1.00 13.93 ?  140 LEU   B N    1 
ATOM   6079 C CA   . LEU   B 1 140 ? 35.072 -30.567 -4.885  1.00 14.32 ?  140 LEU   B CA   1 
ATOM   6080 C C    . LEU   B 1 140 ? 33.570 -30.336 -5.017  1.00 14.61 ?  140 LEU   B C    1 
ATOM   6081 O O    . LEU   B 1 140 ? 33.135 -29.444 -5.750  1.00 14.84 ?  140 LEU   B O    1 
ATOM   6082 C CB   . LEU   B 1 140 ? 35.537 -31.730 -5.761  1.00 14.52 ?  140 LEU   B CB   1 
ATOM   6083 C CG   . LEU   B 1 140 ? 35.177 -31.622 -7.234  1.00 14.81 ?  140 LEU   B CG   1 
ATOM   6084 C CD1  . LEU   B 1 140 ? 35.726 -30.344 -7.837  1.00 15.94 ?  140 LEU   B CD1  1 
ATOM   6085 C CD2  . LEU   B 1 140 ? 35.676 -32.845 -7.973  1.00 15.48 ?  140 LEU   B CD2  1 
ATOM   6086 H H    . LEU   B 1 140 ? 35.754 -31.600 -3.349  1.00 16.72 ?  140 LEU   B H    1 
ATOM   6087 H HA   . LEU   B 1 140 ? 35.529 -29.763 -5.189  1.00 17.19 ?  140 LEU   B HA   1 
ATOM   6088 H HB2  . LEU   B 1 140 ? 36.505 -31.794 -5.702  1.00 17.43 ?  140 LEU   B HB2  1 
ATOM   6089 H HB3  . LEU   B 1 140 ? 35.138 -32.547 -5.426  1.00 17.43 ?  140 LEU   B HB3  1 
ATOM   6090 H HG   . LEU   B 1 140 ? 34.214 -31.594 -7.319  1.00 17.78 ?  140 LEU   B HG   1 
ATOM   6091 H HD11 . LEU   B 1 140 ? 35.604 -30.375 -8.798  1.00 19.13 ?  140 LEU   B HD11 1 
ATOM   6092 H HD12 . LEU   B 1 140 ? 35.241 -29.586 -7.468  1.00 19.13 ?  140 LEU   B HD12 1 
ATOM   6093 H HD13 . LEU   B 1 140 ? 36.668 -30.271 -7.623  1.00 19.13 ?  140 LEU   B HD13 1 
ATOM   6094 H HD21 . LEU   B 1 140 ? 35.437 -32.764 -8.911  1.00 18.59 ?  140 LEU   B HD21 1 
ATOM   6095 H HD22 . LEU   B 1 140 ? 36.635 -32.906 -7.877  1.00 18.59 ?  140 LEU   B HD22 1 
ATOM   6096 H HD23 . LEU   B 1 140 ? 35.251 -33.632 -7.593  1.00 18.59 ?  140 LEU   B HD23 1 
ATOM   6097 N N    . ARG   B 1 141 ? 32.769 -31.124 -4.299  1.00 14.48 ?  141 ARG   B N    1 
ATOM   6098 C CA   . ARG   B 1 141 ? 31.321 -30.949 -4.282  1.00 15.67 ?  141 ARG   B CA   1 
ATOM   6099 C C    . ARG   B 1 141 ? 30.945 -29.539 -3.851  1.00 15.20 ?  141 ARG   B C    1 
ATOM   6100 O O    . ARG   B 1 141 ? 30.137 -28.863 -4.504  1.00 15.39 ?  141 ARG   B O    1 
ATOM   6101 C CB   . ARG   B 1 141 ? 30.734 -31.977 -3.308  1.00 17.03 ?  141 ARG   B CB   1 
ATOM   6102 C CG   . ARG   B 1 141 ? 29.265 -31.869 -3.007  1.00 19.14 ?  141 ARG   B CG   1 
ATOM   6103 C CD   . ARG   B 1 141 ? 28.484 -32.519 -4.086  1.00 20.85 ?  141 ARG   B CD   1 
ATOM   6104 N NE   . ARG   B 1 141 ? 28.205 -31.599 -5.178  1.00 21.18 ?  141 ARG   B NE   1 
ATOM   6105 C CZ   . ARG   B 1 141 ? 28.168 -31.939 -6.460  1.00 21.10 ?  141 ARG   B CZ   1 
ATOM   6106 N NH1  . ARG   B 1 141 ? 28.575 -33.128 -6.874  1.00 21.30 ?  141 ARG   B NH1  1 
ATOM   6107 N NH2  . ARG   B 1 141 ? 27.718 -31.059 -7.349  1.00 22.21 ?  141 ARG   B NH2  1 
ATOM   6108 H H    . ARG   B 1 141 ? 33.052 -31.766 -3.805  1.00 17.39 ?  141 ARG   B H    1 
ATOM   6109 H HA   . ARG   B 1 141 ? 30.962 -31.107 -5.165  1.00 18.82 ?  141 ARG   B HA   1 
ATOM   6110 H HB2  . ARG   B 1 141 ? 30.903 -32.860 -3.668  1.00 20.44 ?  141 ARG   B HB2  1 
ATOM   6111 H HB3  . ARG   B 1 141 ? 31.203 -31.888 -2.464  1.00 20.44 ?  141 ARG   B HB3  1 
ATOM   6112 H HG2  . ARG   B 1 141 ? 29.076 -32.317 -2.170  1.00 22.98 ?  141 ARG   B HG2  1 
ATOM   6113 H HG3  . ARG   B 1 141 ? 28.997 -30.933 -2.952  1.00 22.98 ?  141 ARG   B HG3  1 
ATOM   6114 H HD2  . ARG   B 1 141 ? 28.987 -33.276 -4.435  1.00 25.03 ?  141 ARG   B HD2  1 
ATOM   6115 H HD3  . ARG   B 1 141 ? 27.641 -32.833 -3.724  1.00 25.03 ?  141 ARG   B HD3  1 
ATOM   6116 H HE   . ARG   B 1 141 ? 28.017 -30.787 -4.974  1.00 25.42 ?  141 ARG   B HE   1 
ATOM   6117 H HH11 . ARG   B 1 141 ? 28.849 -33.717 -6.311  1.00 25.57 ?  141 ARG   B HH11 1 
ATOM   6118 H HH12 . ARG   B 1 141 ? 28.547 -33.321 -7.710  1.00 25.57 ?  141 ARG   B HH12 1 
ATOM   6119 H HH21 . ARG   B 1 141 ? 27.465 -30.277 -7.092  1.00 26.66 ?  141 ARG   B HH21 1 
ATOM   6120 H HH22 . ARG   B 1 141 ? 27.714 -31.256 -8.187  1.00 26.66 ?  141 ARG   B HH22 1 
ATOM   6121 N N    . VAL   B 1 142 ? 31.497 -29.092 -2.726  1.00 14.83 ?  142 VAL   B N    1 
ATOM   6122 C CA   . VAL   B 1 142 ? 31.161 -27.763 -2.239  1.00 14.72 ?  142 VAL   B CA   1 
ATOM   6123 C C    . VAL   B 1 142 ? 31.633 -26.706 -3.228  1.00 14.44 ?  142 VAL   B C    1 
ATOM   6124 O O    . VAL   B 1 142 ? 30.930 -25.723 -3.487  1.00 14.92 ?  142 VAL   B O    1 
ATOM   6125 C CB   . VAL   B 1 142 ? 31.710 -27.540 -0.818  1.00 15.18 ?  142 VAL   B CB   1 
ATOM   6126 C CG1  . VAL   B 1 142 ? 31.402 -26.117 -0.343  1.00 14.82 ?  142 VAL   B CG1  1 
ATOM   6127 C CG2  . VAL   B 1 142 ? 31.123 -28.558 0.142   1.00 15.94 ?  142 VAL   B CG2  1 
ATOM   6128 H H    . VAL   B 1 142 ? 32.056 -29.528 -2.235  1.00 17.80 ?  142 VAL   B H    1 
ATOM   6129 H HA   . VAL   B 1 142 ? 30.199 -27.692 -2.183  1.00 17.68 ?  142 VAL   B HA   1 
ATOM   6130 H HB   . VAL   B 1 142 ? 32.673 -27.653 -0.823  1.00 18.23 ?  142 VAL   B HB   1 
ATOM   6131 H HG11 . VAL   B 1 142 ? 31.591 -26.053 0.605   1.00 17.79 ?  142 VAL   B HG11 1 
ATOM   6132 H HG12 . VAL   B 1 142 ? 31.960 -25.492 -0.833  1.00 17.79 ?  142 VAL   B HG12 1 
ATOM   6133 H HG13 . VAL   B 1 142 ? 30.466 -25.926 -0.508  1.00 17.79 ?  142 VAL   B HG13 1 
ATOM   6134 H HG21 . VAL   B 1 142 ? 31.444 -28.371 1.038   1.00 19.14 ?  142 VAL   B HG21 1 
ATOM   6135 H HG22 . VAL   B 1 142 ? 30.155 -28.492 0.117   1.00 19.14 ?  142 VAL   B HG22 1 
ATOM   6136 H HG23 . VAL   B 1 142 ? 31.400 -29.446 -0.131  1.00 19.14 ?  142 VAL   B HG23 1 
ATOM   6137 N N    . CYS   B 1 143 ? 32.812 -26.906 -3.820  1.00 13.98 ?  143 CYS   B N    1 
ATOM   6138 C CA   . CYS   B 1 143 ? 33.307 -25.965 -4.821  1.00 14.06 ?  143 CYS   B CA   1 
ATOM   6139 C C    . CYS   B 1 143 ? 32.305 -25.818 -5.962  1.00 13.80 ?  143 CYS   B C    1 
ATOM   6140 O O    . CYS   B 1 143 ? 31.898 -24.706 -6.317  1.00 14.33 ?  143 CYS   B O    1 
ATOM   6141 C CB   . CYS   B 1 143 ? 34.659 -26.446 -5.351  1.00 14.27 ?  143 CYS   B CB   1 
ATOM   6142 S SG   . CYS   B 1 143 ? 35.405 -25.349 -6.575  1.00 14.80 ?  143 CYS   B SG   1 
ATOM   6143 H H    . CYS   B 1 143 ? 33.339 -27.568 -3.661  1.00 16.78 ?  143 CYS   B H    1 
ATOM   6144 H HA   . CYS   B 1 143 ? 33.433 -25.095 -4.413  1.00 16.88 ?  143 CYS   B HA   1 
ATOM   6145 H HB2  . CYS   B 1 143 ? 35.279 -26.531 -4.610  1.00 17.13 ?  143 CYS   B HB2  1 
ATOM   6146 H HB3  . CYS   B 1 143 ? 34.539 -27.313 -5.768  1.00 17.13 ?  143 CYS   B HB3  1 
ATOM   6147 H HG   . CYS   B 1 143 ? 36.477 -25.784 -6.903  1.00 17.76 ?  143 CYS   B HG   1 
ATOM   6148 N N    . VAL   B 1 144 ? 31.899 -26.939 -6.553  1.00 14.44 ?  144 VAL   B N    1 
ATOM   6149 C CA   . VAL   B 1 144 ? 30.992 -26.876 -7.693  1.00 15.71 ?  144 VAL   B CA   1 
ATOM   6150 C C    . VAL   B 1 144 ? 29.655 -26.264 -7.313  1.00 15.63 ?  144 VAL   B C    1 
ATOM   6151 O O    . VAL   B 1 144 ? 29.039 -25.552 -8.118  1.00 16.96 ?  144 VAL   B O    1 
ATOM   6152 C CB   . VAL   B 1 144 ? 30.825 -28.286 -8.274  1.00 17.75 ?  144 VAL   B CB   1 
ATOM   6153 C CG1  . VAL   B 1 144 ? 29.556 -28.397 -9.121  1.00 20.43 ?  144 VAL   B CG1  1 
ATOM   6154 C CG2  . VAL   B 1 144 ? 32.071 -28.686 -9.057  1.00 18.21 ?  144 VAL   B CG2  1 
ATOM   6155 H H    . VAL   B 1 144 ? 32.133 -27.733 -6.322  1.00 17.33 ?  144 VAL   B H    1 
ATOM   6156 H HA   . VAL   B 1 144 ? 31.380 -26.321 -8.381  1.00 18.86 ?  144 VAL   B HA   1 
ATOM   6157 H HB   . VAL   B 1 144 ? 30.734 -28.918 -7.539  1.00 21.31 ?  144 VAL   B HB   1 
ATOM   6158 H HG11 . VAL   B 1 144 ? 29.633 -29.179 -9.696  1.00 24.52 ?  144 VAL   B HG11 1 
ATOM   6159 H HG12 . VAL   B 1 144 ? 28.792 -28.499 -8.534  1.00 24.52 ?  144 VAL   B HG12 1 
ATOM   6160 H HG13 . VAL   B 1 144 ? 29.467 -27.601 -9.662  1.00 24.52 ?  144 VAL   B HG13 1 
ATOM   6161 H HG21 . VAL   B 1 144 ? 31.949 -29.582 -9.411  1.00 21.86 ?  144 VAL   B HG21 1 
ATOM   6162 H HG22 . VAL   B 1 144 ? 32.194 -28.058 -9.788  1.00 21.86 ?  144 VAL   B HG22 1 
ATOM   6163 H HG23 . VAL   B 1 144 ? 32.835 -28.662 -8.466  1.00 21.86 ?  144 VAL   B HG23 1 
ATOM   6164 N N    . ASP   B 1 145 ? 29.196 -26.504 -6.091  1.00 15.73 ?  145 ASP   B N    1 
ATOM   6165 C CA   . ASP   B 1 145 ? 27.886 -26.036 -5.667  1.00 16.56 ?  145 ASP   B CA   1 
ATOM   6166 C C    . ASP   B 1 145 ? 27.912 -24.617 -5.123  1.00 16.33 ?  145 ASP   B C    1 
ATOM   6167 O O    . ASP   B 1 145 ? 26.852 -24.077 -4.786  1.00 18.11 ?  145 ASP   B O    1 
ATOM   6168 C CB   . ASP   B 1 145 ? 27.301 -26.953 -4.587  1.00 18.44 ?  145 ASP   B CB   1 
ATOM   6169 C CG   . ASP   B 1 145 ? 26.945 -28.331 -5.100  1.00 20.51 ?  145 ASP   B CG   1 
ATOM   6170 O OD1  . ASP   B 1 145 ? 26.824 -28.520 -6.327  1.00 20.97 ?  145 ASP   B OD1  1 
ATOM   6171 O OD2  . ASP   B 1 145 ? 26.773 -29.229 -4.253  1.00 22.74 -1 145 ASP   B OD2  1 
ATOM   6172 H H    . ASP   B 1 145 ? 29.634 -26.930 -5.481  1.00 18.89 ?  145 ASP   B H    1 
ATOM   6173 H HA   . ASP   B 1 145 ? 27.294 -26.038 -6.430  1.00 19.89 ?  145 ASP   B HA   1 
ATOM   6174 H HB2  . ASP   B 1 145 ? 27.945 -27.063 -3.881  1.00 22.13 ?  145 ASP   B HB2  1 
ATOM   6175 H HB3  . ASP   B 1 145 ? 26.489 -26.540 -4.242  1.00 22.13 ?  145 ASP   B HB3  1 
ATOM   6176 N N    . THR   B 1 146 ? 29.085 -24.006 -5.015  1.00 14.39 ?  146 THR   B N    1 
ATOM   6177 C CA   . THR   B 1 146 ? 29.218 -22.686 -4.412  1.00 14.23 ?  146 THR   B CA   1 
ATOM   6178 C C    . THR   B 1 146 ? 29.845 -21.661 -5.338  1.00 13.99 ?  146 THR   B C    1 
ATOM   6179 O O    . THR   B 1 146 ? 29.387 -20.506 -5.385  1.00 14.22 ?  146 THR   B O    1 
ATOM   6180 C CB   . THR   B 1 146 ? 30.054 -22.789 -3.131  1.00 14.21 ?  146 THR   B CB   1 
ATOM   6181 O OG1  . THR   B 1 146 ? 29.482 -23.779 -2.266  1.00 14.69 ?  146 THR   B OG1  1 
ATOM   6182 C CG2  . THR   B 1 146 ? 30.121 -21.451 -2.418  1.00 14.68 ?  146 THR   B CG2  1 
ATOM   6183 H H    . THR   B 1 146 ? 29.840 -24.339 -5.281  1.00 17.28 ?  146 THR   B H    1 
ATOM   6184 H HA   . THR   B 1 146 ? 28.345 -22.361 -4.166  1.00 17.08 ?  146 THR   B HA   1 
ATOM   6185 H HB   . THR   B 1 146 ? 30.961 -23.049 -3.358  1.00 17.06 ?  146 THR   B HB   1 
ATOM   6186 H HG1  . THR   B 1 146 ? 29.513 -24.536 -2.640  1.00 17.64 ?  146 THR   B HG1  1 
ATOM   6187 H HG21 . THR   B 1 146 ? 30.463 -21.567 -1.521  1.00 17.63 ?  146 THR   B HG21 1 
ATOM   6188 H HG22 . THR   B 1 146 ? 30.708 -20.844 -2.902  1.00 17.63 ?  146 THR   B HG22 1 
ATOM   6189 H HG23 . THR   B 1 146 ? 29.235 -21.057 -2.371  1.00 17.63 ?  146 THR   B HG23 1 
ATOM   6190 N N    . VAL   B 1 147 ? 30.898 -22.036 -6.050  1.00 13.58 ?  147 VAL   B N    1 
ATOM   6191 C CA   . VAL   B 1 147 ? 31.625 -21.091 -6.880  1.00 13.26 ?  147 VAL   B CA   1 
ATOM   6192 C C    . VAL   B 1 147 ? 30.899 -20.952 -8.204  1.00 13.71 ?  147 VAL   B C    1 
ATOM   6193 O O    . VAL   B 1 147 ? 30.527 -21.950 -8.836  1.00 14.48 ?  147 VAL   B O    1 
ATOM   6194 C CB   . VAL   B 1 147 ? 33.080 -21.543 -7.078  1.00 13.41 ?  147 VAL   B CB   1 
ATOM   6195 C CG1  . VAL   B 1 147 ? 33.841 -20.502 -7.881  1.00 13.83 ?  147 VAL   B CG1  1 
ATOM   6196 C CG2  . VAL   B 1 147 ? 33.747 -21.755 -5.730  1.00 13.71 ?  147 VAL   B CG2  1 
ATOM   6197 H H    . VAL   B 1 147 ? 31.215 -22.841 -6.074  1.00 16.30 ?  147 VAL   B H    1 
ATOM   6198 H HA   . VAL   B 1 147 ? 31.639 -20.226 -6.445  1.00 15.91 ?  147 VAL   B HA   1 
ATOM   6199 H HB   . VAL   B 1 147 ? 33.103 -22.383 -7.565  1.00 16.10 ?  147 VAL   B HB   1 
ATOM   6200 H HG11 . VAL   B 1 147 ? 34.789 -20.712 -7.864  1.00 16.60 ?  147 VAL   B HG11 1 
ATOM   6201 H HG12 . VAL   B 1 147 ? 33.520 -20.504 -8.795  1.00 16.60 ?  147 VAL   B HG12 1 
ATOM   6202 H HG13 . VAL   B 1 147 ? 33.696 -19.626 -7.482  1.00 16.60 ?  147 VAL   B HG13 1 
ATOM   6203 H HG21 . VAL   B 1 147 ? 34.691 -21.939 -5.865  1.00 16.47 ?  147 VAL   B HG21 1 
ATOM   6204 H HG22 . VAL   B 1 147 ? 33.639 -20.956 -5.193  1.00 16.47 ?  147 VAL   B HG22 1 
ATOM   6205 H HG23 . VAL   B 1 147 ? 33.328 -22.511 -5.284  1.00 16.47 ?  147 VAL   B HG23 1 
ATOM   6206 N N    . ARG   B 1 148 ? 30.688 -19.705 -8.614  1.00 13.79 ?  148 ARG   B N    1 
ATOM   6207 C CA   . ARG   B 1 148 ? 30.062 -19.387 -9.886  1.00 13.94 ?  148 ARG   B CA   1 
ATOM   6208 C C    . ARG   B 1 148 ? 31.013 -18.709 -10.858 1.00 13.89 ?  148 ARG   B C    1 
ATOM   6209 O O    . ARG   B 1 148 ? 30.724 -18.676 -12.056 1.00 15.29 ?  148 ARG   B O    1 
ATOM   6210 C CB   . ARG   B 1 148 ? 28.825 -18.503 -9.666  1.00 14.73 ?  148 ARG   B CB   1 
ATOM   6211 C CG   . ARG   B 1 148 ? 27.760 -19.207 -8.841  1.00 15.39 ?  148 ARG   B CG   1 
ATOM   6212 C CD   . ARG   B 1 148 ? 26.550 -18.328 -8.537  1.00 16.23 ?  148 ARG   B CD   1 
ATOM   6213 N NE   . ARG   B 1 148 ? 26.923 -17.125 -7.805  1.00 16.02 ?  148 ARG   B NE   1 
ATOM   6214 C CZ   . ARG   B 1 148 ? 27.226 -17.092 -6.515  1.00 15.12 ?  148 ARG   B CZ   1 
ATOM   6215 N NH1  . ARG   B 1 148 ? 27.156 -18.176 -5.758  1.00 15.05 ?  148 ARG   B NH1  1 
ATOM   6216 N NH2  . ARG   B 1 148 ? 27.630 -15.946 -5.974  1.00 15.38 ?  148 ARG   B NH2  1 
ATOM   6217 H H    . ARG   B 1 148 ? 30.910 -19.010 -8.154  1.00 16.55 ?  148 ARG   B H    1 
ATOM   6218 H HA   . ARG   B 1 148 ? 29.766 -20.211 -10.296 1.00 16.74 ?  148 ARG   B HA   1 
ATOM   6219 H HB2  . ARG   B 1 148 ? 29.090 -17.699 -9.193  1.00 17.69 ?  148 ARG   B HB2  1 
ATOM   6220 H HB3  . ARG   B 1 148 ? 28.443 -18.276 -10.526 1.00 17.69 ?  148 ARG   B HB3  1 
ATOM   6221 H HG2  . ARG   B 1 148 ? 27.447 -19.988 -9.331  1.00 18.47 ?  148 ARG   B HG2  1 
ATOM   6222 H HG3  . ARG   B 1 148 ? 28.145 -19.488 -7.996  1.00 18.47 ?  148 ARG   B HG3  1 
ATOM   6223 H HD2  . ARG   B 1 148 ? 26.135 -18.060 -9.371  1.00 19.49 ?  148 ARG   B HD2  1 
ATOM   6224 H HD3  . ARG   B 1 148 ? 25.918 -18.830 -7.996  1.00 19.49 ?  148 ARG   B HD3  1 
ATOM   6225 H HE   . ARG   B 1 148 ? 26.963 -16.390 -8.245  1.00 19.24 ?  148 ARG   B HE   1 
ATOM   6226 H HH11 . ARG   B 1 148 ? 26.894 -18.925 -6.092  1.00 18.07 ?  148 ARG   B HH11 1 
ATOM   6227 H HH12 . ARG   B 1 148 ? 27.351 -18.130 -4.920  1.00 18.07 ?  148 ARG   B HH12 1 
ATOM   6228 H HH21 . ARG   B 1 148 ? 27.689 -15.239 -6.460  1.00 18.47 ?  148 ARG   B HH21 1 
ATOM   6229 H HH22 . ARG   B 1 148 ? 27.831 -15.910 -5.139  1.00 18.47 ?  148 ARG   B HH22 1 
ATOM   6230 N N    . THR   B 1 149 ? 32.125 -18.163 -10.374 1.00 13.82 ?  149 THR   B N    1 
ATOM   6231 C CA   . THR   B 1 149 ? 33.159 -17.603 -11.228 1.00 13.79 ?  149 THR   B CA   1 
ATOM   6232 C C    . THR   B 1 149 ? 34.044 -18.743 -11.735 1.00 13.48 ?  149 THR   B C    1 
ATOM   6233 O O    . THR   B 1 149 ? 33.846 -19.914 -11.397 1.00 13.95 ?  149 THR   B O    1 
ATOM   6234 C CB   . THR   B 1 149 ? 33.935 -16.553 -10.448 1.00 14.10 ?  149 THR   B CB   1 
ATOM   6235 O OG1  . THR   B 1 149 ? 34.406 -17.160 -9.243  1.00 14.15 ?  149 THR   B OG1  1 
ATOM   6236 C CG2  . THR   B 1 149 ? 33.046 -15.348 -10.133 1.00 14.65 ?  149 THR   B CG2  1 
ATOM   6237 H H    . THR   B 1 149 ? 32.298 -18.096 -9.535  1.00 16.59 ?  149 THR   B H    1 
ATOM   6238 H HA   . THR   B 1 149 ? 32.744 -17.173 -11.993 1.00 16.56 ?  149 THR   B HA   1 
ATOM   6239 H HB   . THR   B 1 149 ? 34.687 -16.253 -10.975 1.00 16.92 ?  149 THR   B HB   1 
ATOM   6240 H HG1  . THR   B 1 149 ? 34.829 -16.585 -8.786  1.00 16.99 ?  149 THR   B HG1  1 
ATOM   6241 H HG21 . THR   B 1 149 ? 33.558 -14.678 -9.650  1.00 17.59 ?  149 THR   B HG21 1 
ATOM   6242 H HG22 . THR   B 1 149 ? 32.714 -14.954 -10.956 1.00 17.59 ?  149 THR   B HG22 1 
ATOM   6243 H HG23 . THR   B 1 149 ? 32.292 -15.620 -9.588  1.00 17.59 ?  149 THR   B HG23 1 
ATOM   6244 N N    . ASN   B 1 150 ? 35.008 -18.424 -12.589 1.00 13.40 ?  150 ASN   B N    1 
ATOM   6245 C CA   . ASN   B 1 150 ? 35.769 -19.450 -13.291 1.00 13.99 ?  150 ASN   B CA   1 
ATOM   6246 C C    . ASN   B 1 150 ? 36.935 -19.897 -12.423 1.00 13.32 ?  150 ASN   B C    1 
ATOM   6247 O O    . ASN   B 1 150 ? 37.862 -19.126 -12.171 1.00 14.57 ?  150 ASN   B O    1 
ATOM   6248 C CB   . ASN   B 1 150 ? 36.238 -18.915 -14.638 1.00 15.86 ?  150 ASN   B CB   1 
ATOM   6249 C CG   . ASN   B 1 150 ? 35.093 -18.692 -15.580 1.00 18.39 ?  150 ASN   B CG   1 
ATOM   6250 O OD1  . ASN   B 1 150 ? 34.197 -19.524 -15.669 1.00 19.62 ?  150 ASN   B OD1  1 
ATOM   6251 N ND2  . ASN   B 1 150 ? 35.087 -17.556 -16.263 1.00 20.43 ?  150 ASN   B ND2  1 
ATOM   6252 H H    . ASN   B 1 150 ? 35.246 -17.614 -12.780 1.00 16.09 ?  150 ASN   B H    1 
ATOM   6253 H HA   . ASN   B 1 150 ? 35.192 -20.215 -13.454 1.00 16.79 ?  150 ASN   B HA   1 
ATOM   6254 H HB2  . ASN   B 1 150 ? 36.688 -18.066 -14.507 1.00 19.04 ?  150 ASN   B HB2  1 
ATOM   6255 H HB3  . ASN   B 1 150 ? 36.841 -19.556 -15.044 1.00 19.04 ?  150 ASN   B HB3  1 
ATOM   6256 H HD21 . ASN   B 1 150 ? 34.449 -17.384 -16.818 1.00 24.53 ?  150 ASN   B HD21 1 
ATOM   6257 H HD22 . ASN   B 1 150 ? 35.728 -16.990 -16.163 1.00 24.53 ?  150 ASN   B HD22 1 
ATOM   6258 N N    . VAL   B 1 151 ? 36.899 -21.140 -11.967 1.00 13.20 ?  151 VAL   B N    1 
ATOM   6259 C CA   . VAL   B 1 151 ? 37.918 -21.666 -11.074 1.00 13.45 ?  151 VAL   B CA   1 
ATOM   6260 C C    . VAL   B 1 151 ? 38.619 -22.841 -11.744 1.00 13.36 ?  151 VAL   B C    1 
ATOM   6261 O O    . VAL   B 1 151 ? 37.976 -23.771 -12.253 1.00 14.43 ?  151 VAL   B O    1 
ATOM   6262 C CB   . VAL   B 1 151 ? 37.356 -21.999 -9.677  1.00 14.60 ?  151 VAL   B CB   1 
ATOM   6263 C CG1  . VAL   B 1 151 ? 36.210 -23.013 -9.750  1.00 16.04 ?  151 VAL   B CG1  1 
ATOM   6264 C CG2  . VAL   B 1 151 ? 38.468 -22.470 -8.756  1.00 15.02 ?  151 VAL   B CG2  1 
ATOM   6265 H H    . VAL   B 1 151 ? 36.278 -21.706 -12.163 1.00 15.85 ?  151 VAL   B H    1 
ATOM   6266 H HA   . VAL   B 1 151 ? 38.587 -20.973 -10.946 1.00 16.15 ?  151 VAL   B HA   1 
ATOM   6267 H HB   . VAL   B 1 151 ? 36.996 -21.180 -9.293  1.00 17.53 ?  151 VAL   B HB   1 
ATOM   6268 H HG11 . VAL   B 1 151 ? 35.884 -23.186 -8.853  1.00 19.26 ?  151 VAL   B HG11 1 
ATOM   6269 H HG12 . VAL   B 1 151 ? 35.496 -22.644 -10.294 1.00 19.26 ?  151 VAL   B HG12 1 
ATOM   6270 H HG13 . VAL   B 1 151 ? 36.539 -23.833 -10.147 1.00 19.26 ?  151 VAL   B HG13 1 
ATOM   6271 H HG21 . VAL   B 1 151 ? 38.116 -22.546 -7.853  1.00 18.04 ?  151 VAL   B HG21 1 
ATOM   6272 H HG22 . VAL   B 1 151 ? 38.787 -23.333 -9.058  1.00 18.04 ?  151 VAL   B HG22 1 
ATOM   6273 H HG23 . VAL   B 1 151 ? 39.191 -21.823 -8.770  1.00 18.04 ?  151 VAL   B HG23 1 
ATOM   6274 N N    . TYR   B 1 152 ? 39.945 -22.757 -11.764 1.00 12.79 ?  152 TYR   B N    1 
ATOM   6275 C CA   . TYR   B 1 152 ? 40.846 -23.739 -12.347 1.00 13.04 ?  152 TYR   B CA   1 
ATOM   6276 C C    . TYR   B 1 152 ? 41.562 -24.412 -11.183 1.00 12.31 ?  152 TYR   B C    1 
ATOM   6277 O O    . TYR   B 1 152 ? 42.397 -23.790 -10.519 1.00 12.86 ?  152 TYR   B O    1 
ATOM   6278 C CB   . TYR   B 1 152 ? 41.816 -23.029 -13.291 1.00 13.90 ?  152 TYR   B CB   1 
ATOM   6279 C CG   . TYR   B 1 152 ? 41.139 -22.564 -14.559 1.00 14.48 ?  152 TYR   B CG   1 
ATOM   6280 C CD1  . TYR   B 1 152 ? 40.478 -21.340 -14.619 1.00 14.95 ?  152 TYR   B CD1  1 
ATOM   6281 C CD2  . TYR   B 1 152 ? 41.144 -23.361 -15.690 1.00 15.95 ?  152 TYR   B CD2  1 
ATOM   6282 C CE1  . TYR   B 1 152 ? 39.840 -20.934 -15.772 1.00 16.36 ?  152 TYR   B CE1  1 
ATOM   6283 C CE2  . TYR   B 1 152 ? 40.508 -22.965 -16.849 1.00 16.77 ?  152 TYR   B CE2  1 
ATOM   6284 C CZ   . TYR   B 1 152 ? 39.862 -21.747 -16.888 1.00 17.13 ?  152 TYR   B CZ   1 
ATOM   6285 O OH   . TYR   B 1 152 ? 39.238 -21.352 -18.046 1.00 19.60 ?  152 TYR   B OH   1 
ATOM   6286 H H    . TYR   B 1 152 ? 40.377 -22.093 -11.417 1.00 15.35 ?  152 TYR   B H    1 
ATOM   6287 H HA   . TYR   B 1 152 ? 40.340 -24.406 -12.843 1.00 15.65 ?  152 TYR   B HA   1 
ATOM   6288 H HB2  . TYR   B 1 152 ? 42.178 -22.251 -12.835 1.00 16.69 ?  152 TYR   B HB2  1 
ATOM   6289 H HB3  . TYR   B 1 152 ? 42.530 -23.636 -13.530 1.00 16.69 ?  152 TYR   B HB3  1 
ATOM   6290 H HD1  . TYR   B 1 152 ? 40.455 -20.791 -13.866 1.00 17.95 ?  152 TYR   B HD1  1 
ATOM   6291 H HD2  . TYR   B 1 152 ? 41.577 -24.187 -15.664 1.00 19.15 ?  152 TYR   B HD2  1 
ATOM   6292 H HE1  . TYR   B 1 152 ? 39.406 -20.113 -15.807 1.00 19.64 ?  152 TYR   B HE1  1 
ATOM   6293 H HE2  . TYR   B 1 152 ? 40.530 -23.511 -17.603 1.00 20.13 ?  152 TYR   B HE2  1 
ATOM   6294 H HH   . TYR   B 1 152 ? 39.341 -21.940 -18.641 1.00 23.52 ?  152 TYR   B HH   1 
ATOM   6295 N N    . LEU   B 1 153 ? 41.197 -25.666 -10.916 1.00 12.48 ?  153 LEU   B N    1 
ATOM   6296 C CA   . LEU   B 1 153 ? 41.707 -26.419 -9.781  1.00 12.33 ?  153 LEU   B CA   1 
ATOM   6297 C C    . LEU   B 1 153 ? 42.935 -27.222 -10.184 1.00 12.80 ?  153 LEU   B C    1 
ATOM   6298 O O    . LEU   B 1 153 ? 42.918 -27.941 -11.186 1.00 14.21 ?  153 LEU   B O    1 
ATOM   6299 C CB   . LEU   B 1 153 ? 40.630 -27.369 -9.264  1.00 12.78 ?  153 LEU   B CB   1 
ATOM   6300 C CG   . LEU   B 1 153 ? 39.376 -26.712 -8.698  1.00 13.61 ?  153 LEU   B CG   1 
ATOM   6301 C CD1  . LEU   B 1 153 ? 38.295 -27.762 -8.535  1.00 14.39 ?  153 LEU   B CD1  1 
ATOM   6302 C CD2  . LEU   B 1 153 ? 39.682 -26.051 -7.364  1.00 14.34 ?  153 LEU   B CD2  1 
ATOM   6303 H H    . LEU   B 1 153 ? 40.625 -26.112 -11.390 1.00 14.98 ?  153 LEU   B H    1 
ATOM   6304 H HA   . LEU   B 1 153 ? 41.943 -25.808 -9.071  1.00 14.81 ?  153 LEU   B HA   1 
ATOM   6305 H HB2  . LEU   B 1 153 ? 40.345 -27.946 -9.991  1.00 15.34 ?  153 LEU   B HB2  1 
ATOM   6306 H HB3  . LEU   B 1 153 ? 41.010 -27.915 -8.554  1.00 15.34 ?  153 LEU   B HB3  1 
ATOM   6307 H HG   . LEU   B 1 153 ? 39.059 -26.029 -9.311  1.00 16.34 ?  153 LEU   B HG   1 
ATOM   6308 H HD11 . LEU   B 1 153 ? 37.495 -27.334 -8.192  1.00 17.28 ?  153 LEU   B HD11 1 
ATOM   6309 H HD12 . LEU   B 1 153 ? 38.117 -28.157 -9.399  1.00 17.28 ?  153 LEU   B HD12 1 
ATOM   6310 H HD13 . LEU   B 1 153 ? 38.607 -28.434 -7.914  1.00 17.28 ?  153 LEU   B HD13 1 
ATOM   6311 H HD21 . LEU   B 1 153 ? 38.870 -25.678 -6.995  1.00 17.22 ?  153 LEU   B HD21 1 
ATOM   6312 H HD22 . LEU   B 1 153 ? 40.047 -26.718 -6.757  1.00 17.22 ?  153 LEU   B HD22 1 
ATOM   6313 H HD23 . LEU   B 1 153 ? 40.338 -25.345 -7.502  1.00 17.22 ?  153 LEU   B HD23 1 
ATOM   6314 N N    . ALA   B 1 154 ? 43.987 -27.114 -9.384  1.00 12.61 ?  154 ALA   B N    1 
ATOM   6315 C CA   . ALA   B 1 154 ? 45.213 -27.876 -9.571  1.00 13.91 ?  154 ALA   B CA   1 
ATOM   6316 C C    . ALA   B 1 154 ? 45.284 -28.945 -8.492  1.00 14.76 ?  154 ALA   B C    1 
ATOM   6317 O O    . ALA   B 1 154 ? 45.225 -28.641 -7.293  1.00 16.53 ?  154 ALA   B O    1 
ATOM   6318 C CB   . ALA   B 1 154 ? 46.439 -26.968 -9.521  1.00 15.15 ?  154 ALA   B CB   1 
ATOM   6319 H H    . ALA   B 1 154 ? 44.014 -26.580 -8.705  1.00 15.14 ?  154 ALA   B H    1 
ATOM   6320 H HA   . ALA   B 1 154 ? 45.192 -28.311 -10.434 1.00 16.70 ?  154 ALA   B HA   1 
ATOM   6321 H HB1  . ALA   B 1 154 ? 47.237 -27.506 -9.646  1.00 18.18 ?  154 ALA   B HB1  1 
ATOM   6322 H HB2  . ALA   B 1 154 ? 46.374 -26.305 -10.227 1.00 18.18 ?  154 ALA   B HB2  1 
ATOM   6323 H HB3  . ALA   B 1 154 ? 46.473 -26.525 -8.657  1.00 18.18 ?  154 ALA   B HB3  1 
ATOM   6324 N N    . VAL   B 1 155 ? 45.403 -30.192 -8.921  1.00 13.82 ?  155 VAL   B N    1 
ATOM   6325 C CA   . VAL   B 1 155 ? 45.503 -31.336 -8.025  1.00 14.24 ?  155 VAL   B CA   1 
ATOM   6326 C C    . VAL   B 1 155 ? 46.838 -32.012 -8.305  1.00 14.38 ?  155 VAL   B C    1 
ATOM   6327 O O    . VAL   B 1 155 ? 47.073 -32.499 -9.418  1.00 15.89 ?  155 VAL   B O    1 
ATOM   6328 C CB   . VAL   B 1 155 ? 44.340 -32.322 -8.223  1.00 15.57 ?  155 VAL   B CB   1 
ATOM   6329 C CG1  . VAL   B 1 155 ? 44.509 -33.525 -7.319  1.00 15.98 ?  155 VAL   B CG1  1 
ATOM   6330 C CG2  . VAL   B 1 155 ? 43.006 -31.626 -7.951  1.00 16.77 ?  155 VAL   B CG2  1 
ATOM   6331 H H    . VAL   B 1 155 ? 45.436 -30.410 -9.752  1.00 16.60 ?  155 VAL   B H    1 
ATOM   6332 H HA   . VAL   B 1 155 ? 45.493 -31.040 -7.105  1.00 17.10 ?  155 VAL   B HA   1 
ATOM   6333 H HB   . VAL   B 1 155 ? 44.331 -32.634 -9.144  1.00 18.69 ?  155 VAL   B HB   1 
ATOM   6334 H HG11 . VAL   B 1 155 ? 43.677 -34.026 -7.292  1.00 19.19 ?  155 VAL   B HG11 1 
ATOM   6335 H HG12 . VAL   B 1 155 ? 45.218 -34.092 -7.668  1.00 19.19 ?  155 VAL   B HG12 1 
ATOM   6336 H HG13 . VAL   B 1 155 ? 44.738 -33.222 -6.427  1.00 19.19 ?  155 VAL   B HG13 1 
ATOM   6337 H HG21 . VAL   B 1 155 ? 42.287 -32.271 -8.042  1.00 20.13 ?  155 VAL   B HG21 1 
ATOM   6338 H HG22 . VAL   B 1 155 ? 43.018 -31.272 -7.047  1.00 20.13 ?  155 VAL   B HG22 1 
ATOM   6339 H HG23 . VAL   B 1 155 ? 42.889 -30.906 -8.587  1.00 20.13 ?  155 VAL   B HG23 1 
ATOM   6340 N N    . PHE   B 1 156 ? 47.703 -32.053 -7.293  1.00 14.77 ?  156 PHE   B N    1 
ATOM   6341 C CA   . PHE   B 1 156 ? 49.079 -32.514 -7.491  1.00 16.23 ?  156 PHE   B CA   1 
ATOM   6342 C C    . PHE   B 1 156 ? 49.171 -34.013 -7.767  1.00 17.24 ?  156 PHE   B C    1 
ATOM   6343 O O    . PHE   B 1 156 ? 49.891 -34.444 -8.677  1.00 19.22 ?  156 PHE   B O    1 
ATOM   6344 C CB   . PHE   B 1 156 ? 49.903 -32.147 -6.260  1.00 16.50 ?  156 PHE   B CB   1 
ATOM   6345 C CG   . PHE   B 1 156 ? 51.323 -32.614 -6.317  1.00 16.71 ?  156 PHE   B CG   1 
ATOM   6346 C CD1  . PHE   B 1 156 ? 52.204 -32.080 -7.239  1.00 18.49 ?  156 PHE   B CD1  1 
ATOM   6347 C CD2  . PHE   B 1 156 ? 51.786 -33.570 -5.434  1.00 17.20 ?  156 PHE   B CD2  1 
ATOM   6348 C CE1  . PHE   B 1 156 ? 53.517 -32.496 -7.290  1.00 19.24 ?  156 PHE   B CE1  1 
ATOM   6349 C CE2  . PHE   B 1 156 ? 53.097 -33.989 -5.477  1.00 18.53 ?  156 PHE   B CE2  1 
ATOM   6350 C CZ   . PHE   B 1 156 ? 53.959 -33.454 -6.409  1.00 18.96 ?  156 PHE   B CZ   1 
ATOM   6351 H H    . PHE   B 1 156 ? 47.517 -31.826 -6.485  1.00 17.73 ?  156 PHE   B H    1 
ATOM   6352 H HA   . PHE   B 1 156 ? 49.455 -32.051 -8.250  1.00 19.48 ?  156 PHE   B HA   1 
ATOM   6353 H HB2  . PHE   B 1 156 ? 49.914 -31.183 -6.171  1.00 19.81 ?  156 PHE   B HB2  1 
ATOM   6354 H HB3  . PHE   B 1 156 ? 49.495 -32.547 -5.476  1.00 19.81 ?  156 PHE   B HB3  1 
ATOM   6355 H HD1  . PHE   B 1 156 ? 51.910 -31.431 -7.838  1.00 22.19 ?  156 PHE   B HD1  1 
ATOM   6356 H HD2  . PHE   B 1 156 ? 51.201 -33.937 -4.808  1.00 20.65 ?  156 PHE   B HD2  1 
ATOM   6357 H HE1  . PHE   B 1 156 ? 54.103 -32.135 -7.916  1.00 23.10 ?  156 PHE   B HE1  1 
ATOM   6358 H HE2  . PHE   B 1 156 ? 53.395 -34.643 -4.884  1.00 22.24 ?  156 PHE   B HE2  1 
ATOM   6359 H HZ   . PHE   B 1 156 ? 54.845 -33.742 -6.438  1.00 22.76 ?  156 PHE   B HZ   1 
ATOM   6360 N N    . ASP   B 1 157 ? 48.501 -34.827 -6.963  1.00 17.03 ?  157 ASP   B N    1 
ATOM   6361 C CA   . ASP   B 1 157 ? 48.646 -36.274 -7.051  1.00 18.18 ?  157 ASP   B CA   1 
ATOM   6362 C C    . ASP   B 1 157 ? 47.734 -36.821 -8.144  1.00 18.15 ?  157 ASP   B C    1 
ATOM   6363 O O    . ASP   B 1 157 ? 46.507 -36.701 -8.048  1.00 17.65 ?  157 ASP   B O    1 
ATOM   6364 C CB   . ASP   B 1 157 ? 48.280 -36.883 -5.703  1.00 19.85 ?  157 ASP   B CB   1 
ATOM   6365 C CG   . ASP   B 1 157 ? 48.428 -38.388 -5.680  1.00 22.32 ?  157 ASP   B CG   1 
ATOM   6366 O OD1  . ASP   B 1 157 ? 48.760 -38.992 -6.727  1.00 23.01 ?  157 ASP   B OD1  1 
ATOM   6367 O OD2  . ASP   B 1 157 ? 48.226 -38.970 -4.596  1.00 25.04 -1 157 ASP   B OD2  1 
ATOM   6368 H H    . ASP   B 1 157 ? 47.954 -34.570 -6.357  1.00 20.44 ?  157 ASP   B H    1 
ATOM   6369 H HA   . ASP   B 1 157 ? 49.566 -36.508 -7.263  1.00 21.82 ?  157 ASP   B HA   1 
ATOM   6370 H HB2  . ASP   B 1 157 ? 48.855 -36.501 -5.024  1.00 23.83 ?  157 ASP   B HB2  1 
ATOM   6371 H HB3  . ASP   B 1 157 ? 47.351 -36.669 -5.506  1.00 23.83 ?  157 ASP   B HB3  1 
ATOM   6372 N N    . LYS   B 1 158 ? 48.332 -37.447 -9.166  1.00 19.42 ?  158 LYS   B N    1 
ATOM   6373 C CA   . LYS   B 1 158 ? 47.559 -38.063 -10.249 1.00 20.75 ?  158 LYS   B CA   1 
ATOM   6374 C C    . LYS   B 1 158 ? 46.497 -39.023 -9.720  1.00 20.15 ?  158 LYS   B C    1 
ATOM   6375 O O    . LYS   B 1 158 ? 45.391 -39.109 -10.269 1.00 20.72 ?  158 LYS   B O    1 
ATOM   6376 C CB   . LYS   B 1 158 ? 48.507 -38.793 -11.211 1.00 23.12 ?  158 LYS   B CB   1 
ATOM   6377 C CG   . LYS   B 1 158 ? 47.826 -39.687 -12.244 1.00 26.16 ?  158 LYS   B CG   1 
ATOM   6378 C CD   . LYS   B 1 158 ? 46.987 -38.891 -13.223 1.00 28.72 ?  158 LYS   B CD   1 
ATOM   6379 C CE   . LYS   B 1 158 ? 46.377 -39.797 -14.281 1.00 30.80 ?  158 LYS   B CE   1 
ATOM   6380 N NZ   . LYS   B 1 158 ? 45.354 -39.087 -15.100 1.00 31.90 ?  158 LYS   B NZ   1 
ATOM   6381 H H    . LYS   B 1 158 ? 49.187 -37.535 -9.257  1.00 23.31 ?  158 LYS   B H    1 
ATOM   6382 H HA   . LYS   B 1 158 ? 47.114 -37.366 -10.757 1.00 24.90 ?  158 LYS   B HA   1 
ATOM   6383 H HB2  . LYS   B 1 158 ? 49.026 -38.133 -11.704 1.00 27.75 ?  158 LYS   B HB2  1 
ATOM   6384 H HB3  . LYS   B 1 158 ? 49.108 -39.353 -10.695 1.00 27.75 ?  158 LYS   B HB3  1 
ATOM   6385 H HG2  . LYS   B 1 158 ? 48.510 -40.155 -12.752 1.00 31.41 ?  158 LYS   B HG2  1 
ATOM   6386 H HG3  . LYS   B 1 158 ? 47.254 -40.335 -11.801 1.00 31.41 ?  158 LYS   B HG3  1 
ATOM   6387 H HD2  . LYS   B 1 158 ? 46.267 -38.449 -12.747 1.00 34.48 ?  158 LYS   B HD2  1 
ATOM   6388 H HD3  . LYS   B 1 158 ? 47.548 -38.237 -13.670 1.00 34.48 ?  158 LYS   B HD3  1 
ATOM   6389 H HE2  . LYS   B 1 158 ? 47.075 -40.110 -14.876 1.00 36.97 ?  158 LYS   B HE2  1 
ATOM   6390 H HE3  . LYS   B 1 158 ? 45.946 -40.551 -13.847 1.00 36.97 ?  158 LYS   B HE3  1 
ATOM   6391 H HZ1  . LYS   B 1 158 ? 45.013 -39.639 -15.709 1.00 38.29 ?  158 LYS   B HZ1  1 
ATOM   6392 H HZ2  . LYS   B 1 158 ? 44.697 -38.791 -14.577 1.00 38.29 ?  158 LYS   B HZ2  1 
ATOM   6393 H HZ3  . LYS   B 1 158 ? 45.727 -38.393 -15.515 1.00 38.29 ?  158 LYS   B HZ3  1 
ATOM   6394 N N    . ASN   B 1 159 ? 46.819 -39.781 -8.671  1.00 20.40 ?  159 ASN   B N    1 
ATOM   6395 C CA   . ASN   B 1 159 ? 45.864 -40.760 -8.165  1.00 21.03 ?  159 ASN   B CA   1 
ATOM   6396 C C    . ASN   B 1 159 ? 44.670 -40.084 -7.492  1.00 20.03 ?  159 ASN   B C    1 
ATOM   6397 O O    . ASN   B 1 159 ? 43.536 -40.566 -7.602  1.00 20.47 ?  159 ASN   B O    1 
ATOM   6398 C CB   . ASN   B 1 159 ? 46.565 -41.740 -7.231  1.00 22.89 ?  159 ASN   B CB   1 
ATOM   6399 C CG   . ASN   B 1 159 ? 47.594 -42.577 -7.951  1.00 25.07 ?  159 ASN   B CG   1 
ATOM   6400 O OD1  . ASN   B 1 159 ? 47.340 -43.072 -9.053  1.00 25.67 ?  159 ASN   B OD1  1 
ATOM   6401 N ND2  . ASN   B 1 159 ? 48.766 -42.735 -7.342  1.00 25.88 ?  159 ASN   B ND2  1 
ATOM   6402 H H    . ASN   B 1 159 ? 47.560 -39.735 -8.248  1.00 24.49 ?  159 ASN   B H    1 
ATOM   6403 H HA   . ASN   B 1 159 ? 45.523 -41.267 -8.920  1.00 25.25 ?  159 ASN   B HA   1 
ATOM   6404 H HB2  . ASN   B 1 159 ? 47.014 -41.248 -6.530  1.00 27.48 ?  159 ASN   B HB2  1 
ATOM   6405 H HB3  . ASN   B 1 159 ? 45.906 -42.341 -6.852  1.00 27.48 ?  159 ASN   B HB3  1 
ATOM   6406 H HD21 . ASN   B 1 159 ? 49.386 -43.210 -7.710  1.00 31.07 ?  159 ASN   B HD21 1 
ATOM   6407 H HD22 . ASN   B 1 159 ? 48.901 -42.388 -6.567  1.00 31.07 ?  159 ASN   B HD22 1 
ATOM   6408 N N    . LEU   B 1 160 ? 44.888 -38.953 -6.813  1.00 19.29 ?  160 LEU   B N    1 
ATOM   6409 C CA   . LEU   B 1 160 ? 43.755 -38.211 -6.274  1.00 18.18 ?  160 LEU   B CA   1 
ATOM   6410 C C    . LEU   B 1 160 ? 42.967 -37.547 -7.391  1.00 17.54 ?  160 LEU   B C    1 
ATOM   6411 O O    . LEU   B 1 160 ? 41.730 -37.554 -7.376  1.00 16.95 ?  160 LEU   B O    1 
ATOM   6412 C CB   . LEU   B 1 160 ? 44.217 -37.184 -5.243  1.00 17.71 ?  160 LEU   B CB   1 
ATOM   6413 C CG   . LEU   B 1 160 ? 43.092 -36.283 -4.720  1.00 17.20 ?  160 LEU   B CG   1 
ATOM   6414 C CD1  . LEU   B 1 160 ? 41.968 -37.110 -4.109  1.00 18.01 ?  160 LEU   B CD1  1 
ATOM   6415 C CD2  . LEU   B 1 160 ? 43.638 -35.285 -3.713  1.00 17.49 ?  160 LEU   B CD2  1 
ATOM   6416 H H    . LEU   B 1 160 ? 45.663 -38.610 -6.655  1.00 23.16 ?  160 LEU   B H    1 
ATOM   6417 H HA   . LEU   B 1 160 ? 43.164 -38.834 -5.832  1.00 21.83 ?  160 LEU   B HA   1 
ATOM   6418 H HB2  . LEU   B 1 160 ? 44.599 -37.658 -4.485  1.00 21.26 ?  160 LEU   B HB2  1 
ATOM   6419 H HB3  . LEU   B 1 160 ? 44.894 -36.616 -5.646  1.00 21.26 ?  160 LEU   B HB3  1 
ATOM   6420 H HG   . LEU   B 1 160 ? 42.723 -35.780 -5.461  1.00 20.64 ?  160 LEU   B HG   1 
ATOM   6421 H HD11 . LEU   B 1 160 ? 41.340 -36.513 -3.678  1.00 21.63 ?  160 LEU   B HD11 1 
ATOM   6422 H HD12 . LEU   B 1 160 ? 41.522 -37.610 -4.811  1.00 21.63 ?  160 LEU   B HD12 1 
ATOM   6423 H HD13 . LEU   B 1 160 ? 42.345 -37.722 -3.455  1.00 21.63 ?  160 LEU   B HD13 1 
ATOM   6424 H HD21 . LEU   B 1 160 ? 42.915 -34.711 -3.417  1.00 21.00 ?  160 LEU   B HD21 1 
ATOM   6425 H HD22 . LEU   B 1 160 ? 44.010 -35.767 -2.958  1.00 21.00 ?  160 LEU   B HD22 1 
ATOM   6426 H HD23 . LEU   B 1 160 ? 44.330 -34.752 -4.138  1.00 21.00 ?  160 LEU   B HD23 1 
ATOM   6427 N N    . TYR   B 1 161 ? 43.665 -36.984 -8.377  1.00 17.59 ?  161 TYR   B N    1 
ATOM   6428 C CA   . TYR   B 1 161 ? 42.991 -36.415 -9.537  1.00 17.45 ?  161 TYR   B CA   1 
ATOM   6429 C C    . TYR   B 1 161 ? 42.046 -37.433 -10.159 1.00 17.15 ?  161 TYR   B C    1 
ATOM   6430 O O    . TYR   B 1 161 ? 40.878 -37.132 -10.427 1.00 16.88 ?  161 TYR   B O    1 
ATOM   6431 C CB   . TYR   B 1 161 ? 44.035 -35.941 -10.555 1.00 18.05 ?  161 TYR   B CB   1 
ATOM   6432 C CG   . TYR   B 1 161 ? 43.462 -35.471 -11.868 1.00 18.70 ?  161 TYR   B CG   1 
ATOM   6433 C CD1  . TYR   B 1 161 ? 43.063 -34.152 -12.034 1.00 18.45 ?  161 TYR   B CD1  1 
ATOM   6434 C CD2  . TYR   B 1 161 ? 43.310 -36.343 -12.941 1.00 19.61 ?  161 TYR   B CD2  1 
ATOM   6435 C CE1  . TYR   B 1 161 ? 42.536 -33.716 -13.221 1.00 19.65 ?  161 TYR   B CE1  1 
ATOM   6436 C CE2  . TYR   B 1 161 ? 42.774 -35.915 -14.133 1.00 20.62 ?  161 TYR   B CE2  1 
ATOM   6437 C CZ   . TYR   B 1 161 ? 42.390 -34.601 -14.269 1.00 20.51 ?  161 TYR   B CZ   1 
ATOM   6438 O OH   . TYR   B 1 161 ? 41.859 -34.167 -15.456 1.00 22.73 ?  161 TYR   B OH   1 
ATOM   6439 H H    . TYR   B 1 161 ? 44.524 -36.930 -8.407  1.00 21.12 ?  161 TYR   B H    1 
ATOM   6440 H HA   . TYR   B 1 161 ? 42.469 -35.647 -9.264  1.00 20.95 ?  161 TYR   B HA   1 
ATOM   6441 H HB2  . TYR   B 1 161 ? 44.532 -35.198 -10.172 1.00 21.67 ?  161 TYR   B HB2  1 
ATOM   6442 H HB3  . TYR   B 1 161 ? 44.643 -36.672 -10.749 1.00 21.67 ?  161 TYR   B HB3  1 
ATOM   6443 H HD1  . TYR   B 1 161 ? 43.161 -33.549 -11.333 1.00 22.15 ?  161 TYR   B HD1  1 
ATOM   6444 H HD2  . TYR   B 1 161 ? 43.563 -37.232 -12.854 1.00 23.54 ?  161 TYR   B HD2  1 
ATOM   6445 H HE1  . TYR   B 1 161 ? 42.276 -32.824 -13.317 1.00 23.59 ?  161 TYR   B HE1  1 
ATOM   6446 H HE2  . TYR   B 1 161 ? 42.674 -36.504 -14.847 1.00 24.76 ?  161 TYR   B HE2  1 
ATOM   6447 H HH   . TYR   B 1 161 ? 41.829 -34.797 -16.011 1.00 27.29 ?  161 TYR   B HH   1 
ATOM   6448 N N    . ASP   B 1 162 ? 42.537 -38.656 -10.373 1.00 17.66 ?  162 ASP   B N    1 
ATOM   6449 C CA   . ASP   B 1 162 ? 41.715 -39.689 -10.993 1.00 18.43 ?  162 ASP   B CA   1 
ATOM   6450 C C    . ASP   B 1 162 ? 40.506 -40.026 -10.130 1.00 17.65 ?  162 ASP   B C    1 
ATOM   6451 O O    . ASP   B 1 162 ? 39.402 -40.229 -10.650 1.00 18.16 ?  162 ASP   B O    1 
ATOM   6452 C CB   . ASP   B 1 162 ? 42.546 -40.950 -11.247 1.00 19.99 ?  162 ASP   B CB   1 
ATOM   6453 C CG   . ASP   B 1 162 ? 43.550 -40.784 -12.374 1.00 21.33 ?  162 ASP   B CG   1 
ATOM   6454 O OD1  . ASP   B 1 162 ? 43.413 -39.849 -13.184 1.00 21.88 ?  162 ASP   B OD1  1 
ATOM   6455 O OD2  . ASP   B 1 162 ? 44.463 -41.630 -12.472 1.00 23.54 -1 162 ASP   B OD2  1 
ATOM   6456 H H    . ASP   B 1 162 ? 43.337 -38.907 -10.175 1.00 21.20 ?  162 ASP   B H    1 
ATOM   6457 H HA   . ASP   B 1 162 ? 41.392 -39.368 -11.847 1.00 22.12 ?  162 ASP   B HA   1 
ATOM   6458 H HB2  . ASP   B 1 162 ? 43.033 -41.178 -10.442 1.00 24.00 ?  162 ASP   B HB2  1 
ATOM   6459 H HB3  . ASP   B 1 162 ? 41.949 -41.677 -11.492 1.00 24.00 ?  162 ASP   B HB3  1 
ATOM   6460 N N    A LYS   B 1 163 ? 40.692 -40.099 -8.811  0.86 16.77 ?  163 LYS   B N    1 
ATOM   6461 N N    B LYS   B 1 163 ? 40.688 -40.085 -8.809  0.14 18.32 ?  163 LYS   B N    1 
ATOM   6462 C CA   A LYS   B 1 163 ? 39.569 -40.372 -7.922  0.86 17.46 ?  163 LYS   B CA   1 
ATOM   6463 C CA   B LYS   B 1 163 ? 39.560 -40.378 -7.928  0.14 19.34 ?  163 LYS   B CA   1 
ATOM   6464 C C    A LYS   B 1 163 ? 38.530 -39.258 -7.984  0.86 16.42 ?  163 LYS   B C    1 
ATOM   6465 C C    B LYS   B 1 163 ? 38.528 -39.255 -7.958  0.14 17.26 ?  163 LYS   B C    1 
ATOM   6466 O O    A LYS   B 1 163 ? 37.320 -39.523 -7.984  0.86 17.52 ?  163 LYS   B O    1 
ATOM   6467 O O    B LYS   B 1 163 ? 37.320 -39.513 -7.906  0.14 17.21 ?  163 LYS   B O    1 
ATOM   6468 C CB   A LYS   B 1 163 ? 40.060 -40.558 -6.489  0.86 20.59 ?  163 LYS   B CB   1 
ATOM   6469 C CB   B LYS   B 1 163 ? 40.052 -40.616 -6.500  0.14 22.71 ?  163 LYS   B CB   1 
ATOM   6470 C CG   A LYS   B 1 163 ? 38.967 -41.029 -5.556  0.86 26.19 ?  163 LYS   B CG   1 
ATOM   6471 C CG   B LYS   B 1 163 ? 38.959 -41.092 -5.561  0.14 26.15 ?  163 LYS   B CG   1 
ATOM   6472 C CD   A LYS   B 1 163 ? 39.438 -41.179 -4.123  0.86 31.20 ?  163 LYS   B CD   1 
ATOM   6473 C CD   B LYS   B 1 163 ? 39.453 -41.248 -4.136  0.14 29.62 ?  163 LYS   B CD   1 
ATOM   6474 C CE   A LYS   B 1 163 ? 38.356 -41.843 -3.282  0.86 34.62 ?  163 LYS   B CE   1 
ATOM   6475 C CE   B LYS   B 1 163 ? 38.379 -41.886 -3.270  0.14 32.05 ?  163 LYS   B CE   1 
ATOM   6476 N NZ   A LYS   B 1 163 ? 38.514 -41.592 -1.823  0.86 37.13 ?  163 LYS   B NZ   1 
ATOM   6477 N NZ   B LYS   B 1 163 ? 38.649 -41.724 -1.816  0.14 32.76 ?  163 LYS   B NZ   1 
ATOM   6478 H H    A LYS   B 1 163 ? 41.450 -39.988 -8.414  0.86 20.13 ?  163 LYS   B H    1 
ATOM   6479 H H    B LYS   B 1 163 ? 41.440 -39.965 -8.407  0.14 22.00 ?  163 LYS   B H    1 
ATOM   6480 H HA   A LYS   B 1 163 ? 39.144 -41.195 -8.203  0.86 20.96 ?  163 LYS   B HA   1 
ATOM   6481 H HA   B LYS   B 1 163 ? 39.128 -41.190 -8.232  0.14 23.22 ?  163 LYS   B HA   1 
ATOM   6482 H HB2  A LYS   B 1 163 ? 40.769 -41.224 -6.482  0.86 24.72 ?  163 LYS   B HB2  1 
ATOM   6483 H HB2  B LYS   B 1 163 ? 40.747 -41.294 -6.514  0.14 27.26 ?  163 LYS   B HB2  1 
ATOM   6484 H HB3  A LYS   B 1 163 ? 40.397 -39.713 -6.156  0.86 24.72 ?  163 LYS   B HB3  1 
ATOM   6485 H HB3  B LYS   B 1 163 ? 40.409 -39.787 -6.146  0.14 27.26 ?  163 LYS   B HB3  1 
ATOM   6486 H HG2  A LYS   B 1 163 ? 38.240 -40.389 -5.565  0.86 31.43 ?  163 LYS   B HG2  1 
ATOM   6487 H HG2  B LYS   B 1 163 ? 38.236 -40.445 -5.557  0.14 31.38 ?  163 LYS   B HG2  1 
ATOM   6488 H HG3  A LYS   B 1 163 ? 38.646 -41.897 -5.858  0.86 31.43 ?  163 LYS   B HG3  1 
ATOM   6489 H HG3  B LYS   B 1 163 ? 38.634 -41.954 -5.863  0.14 31.38 ?  163 LYS   B HG3  1 
ATOM   6490 H HD2  A LYS   B 1 163 ? 40.232 -41.737 -4.099  0.86 37.45 ?  163 LYS   B HD2  1 
ATOM   6491 H HD2  B LYS   B 1 163 ? 40.237 -41.820 -4.126  0.14 35.55 ?  163 LYS   B HD2  1 
ATOM   6492 H HD3  A LYS   B 1 163 ? 39.625 -40.304 -3.751  0.86 37.45 ?  163 LYS   B HD3  1 
ATOM   6493 H HD3  B LYS   B 1 163 ? 39.666 -40.375 -3.769  0.14 35.55 ?  163 LYS   B HD3  1 
ATOM   6494 H HE2  A LYS   B 1 163 ? 37.489 -41.506 -3.556  0.86 41.55 ?  163 LYS   B HE2  1 
ATOM   6495 H HE2  B LYS   B 1 163 ? 37.524 -41.475 -3.469  0.14 38.47 ?  163 LYS   B HE2  1 
ATOM   6496 H HE3  A LYS   B 1 163 ? 38.394 -42.802 -3.425  0.86 41.55 ?  163 LYS   B HE3  1 
ATOM   6497 H HE3  B LYS   B 1 163 ? 38.342 -42.836 -3.465  0.14 38.47 ?  163 LYS   B HE3  1 
ATOM   6498 H HZ1  A LYS   B 1 163 ? 37.861 -41.997 -1.374  0.86 44.57 ?  163 LYS   B HZ1  1 
ATOM   6499 H HZ1  B LYS   B 1 163 ? 38.000 -42.109 -1.343  0.14 39.32 ?  163 LYS   B HZ1  1 
ATOM   6500 H HZ2  A LYS   B 1 163 ? 39.297 -41.908 -1.544  0.86 44.57 ?  163 LYS   B HZ2  1 
ATOM   6501 H HZ2  B LYS   B 1 163 ? 39.425 -42.105 -1.607  0.14 39.32 ?  163 LYS   B HZ2  1 
ATOM   6502 H HZ3  A LYS   B 1 163 ? 38.478 -40.718 -1.660  0.86 44.57 ?  163 LYS   B HZ3  1 
ATOM   6503 H HZ3  B LYS   B 1 163 ? 38.684 -40.859 -1.609  0.14 39.32 ?  163 LYS   B HZ3  1 
ATOM   6504 N N    . LEU   B 1 164 ? 38.986 -38.005 -8.043  1.00 15.51 ?  164 LEU   B N    1 
ATOM   6505 C CA   . LEU   B 1 164 ? 38.073 -36.869 -8.089  1.00 15.33 ?  164 LEU   B CA   1 
ATOM   6506 C C    . LEU   B 1 164 ? 37.291 -36.845 -9.398  1.00 15.87 ?  164 LEU   B C    1 
ATOM   6507 O O    . LEU   B 1 164 ? 36.069 -36.639 -9.402  1.00 16.77 ?  164 LEU   B O    1 
ATOM   6508 C CB   . LEU   B 1 164 ? 38.878 -35.581 -7.919  1.00 14.91 ?  164 LEU   B CB   1 
ATOM   6509 C CG   . LEU   B 1 164 ? 39.418 -35.306 -6.519  1.00 15.66 ?  164 LEU   B CG   1 
ATOM   6510 C CD1  . LEU   B 1 164 ? 40.499 -34.234 -6.572  1.00 15.60 ?  164 LEU   B CD1  1 
ATOM   6511 C CD2  . LEU   B 1 164 ? 38.302 -34.897 -5.578  1.00 17.27 ?  164 LEU   B CD2  1 
ATOM   6512 H H    A LEU   B 1 164 ? 39.822 -37.790 -8.056  0.86 18.62 ?  164 LEU   B H    1 
ATOM   6513 H H    B LEU   B 1 164 ? 39.822 -37.792 -8.078  0.14 18.62 ?  164 LEU   B H    1 
ATOM   6514 H HA   . LEU   B 1 164 ? 37.446 -36.935 -7.358  1.00 18.40 ?  164 LEU   B HA   1 
ATOM   6515 H HB2  . LEU   B 1 164 ? 39.644 -35.614 -8.519  1.00 17.90 ?  164 LEU   B HB2  1 
ATOM   6516 H HB3  . LEU   B 1 164 ? 38.316 -34.832 -8.161  1.00 17.90 ?  164 LEU   B HB3  1 
ATOM   6517 H HG   . LEU   B 1 164 ? 39.826 -36.114 -6.171  1.00 18.80 ?  164 LEU   B HG   1 
ATOM   6518 H HD11 . LEU   B 1 164 ? 40.828 -34.067 -5.673  1.00 18.73 ?  164 LEU   B HD11 1 
ATOM   6519 H HD12 . LEU   B 1 164 ? 41.233 -34.549 -7.131  1.00 18.73 ?  164 LEU   B HD12 1 
ATOM   6520 H HD13 . LEU   B 1 164 ? 40.129 -33.422 -6.945  1.00 18.73 ?  164 LEU   B HD13 1 
ATOM   6521 H HD21 . LEU   B 1 164 ? 38.679 -34.668 -4.715  1.00 20.73 ?  164 LEU   B HD21 1 
ATOM   6522 H HD22 . LEU   B 1 164 ? 37.838 -34.131 -5.951  1.00 20.73 ?  164 LEU   B HD22 1 
ATOM   6523 H HD23 . LEU   B 1 164 ? 37.686 -35.642 -5.482  1.00 20.73 ?  164 LEU   B HD23 1 
ATOM   6524 N N    . VAL   B 1 165 ? 37.984 -37.028 -10.523 1.00 17.34 ?  165 VAL   B N    1 
ATOM   6525 C CA   . VAL   B 1 165 ? 37.334 -36.956 -11.828 1.00 18.46 ?  165 VAL   B CA   1 
ATOM   6526 C C    . VAL   B 1 165 ? 36.412 -38.152 -12.026 1.00 20.01 ?  165 VAL   B C    1 
ATOM   6527 O O    . VAL   B 1 165 ? 35.258 -38.013 -12.449 1.00 21.04 ?  165 VAL   B O    1 
ATOM   6528 C CB   . VAL   B 1 165 ? 38.389 -36.869 -12.946 1.00 19.19 ?  165 VAL   B CB   1 
ATOM   6529 C CG1  . VAL   B 1 165 ? 37.739 -36.984 -14.304 1.00 20.39 ?  165 VAL   B CG1  1 
ATOM   6530 C CG2  . VAL   B 1 165 ? 39.167 -35.574 -12.838 1.00 19.34 ?  165 VAL   B CG2  1 
ATOM   6531 H H    . VAL   B 1 165 ? 38.830 -37.189 -10.556 1.00 20.82 ?  165 VAL   B H    1 
ATOM   6532 H HA   . VAL   B 1 165 ? 36.797 -36.152 -11.868 1.00 22.16 ?  165 VAL   B HA   1 
ATOM   6533 H HB   . VAL   B 1 165 ? 39.023 -37.597 -12.846 1.00 23.03 ?  165 VAL   B HB   1 
ATOM   6534 H HG11 . VAL   B 1 165 ? 38.364 -36.684 -14.980 1.00 24.48 ?  165 VAL   B HG11 1 
ATOM   6535 H HG12 . VAL   B 1 165 ? 37.509 -37.915 -14.461 1.00 24.48 ?  165 VAL   B HG12 1 
ATOM   6536 H HG13 . VAL   B 1 165 ? 36.942 -36.437 -14.318 1.00 24.48 ?  165 VAL   B HG13 1 
ATOM   6537 H HG21 . VAL   B 1 165 ? 39.811 -35.525 -13.565 1.00 23.22 ?  165 VAL   B HG21 1 
ATOM   6538 H HG22 . VAL   B 1 165 ? 38.550 -34.825 -12.898 1.00 23.22 ?  165 VAL   B HG22 1 
ATOM   6539 H HG23 . VAL   B 1 165 ? 39.633 -35.546 -11.986 1.00 23.22 ?  165 VAL   B HG23 1 
ATOM   6540 N N    . SER   B 1 166 ? 36.918 -39.351 -11.726 1.00 20.83 ?  166 SER   B N    1 
ATOM   6541 C CA   . SER   B 1 166 ? 36.160 -40.559 -12.012 1.00 22.28 ?  166 SER   B CA   1 
ATOM   6542 C C    . SER   B 1 166 ? 34.906 -40.652 -11.158 1.00 22.59 ?  166 SER   B C    1 
ATOM   6543 O O    . SER   B 1 166 ? 33.932 -41.268 -11.584 1.00 24.29 ?  166 SER   B O    1 
ATOM   6544 C CB   . SER   B 1 166 ? 37.027 -41.814 -11.845 1.00 23.13 ?  166 SER   B CB   1 
ATOM   6545 O OG   . SER   B 1 166 ? 37.406 -42.025 -10.494 1.00 23.29 ?  166 SER   B OG   1 
ATOM   6546 H H    . SER   B 1 166 ? 37.692 -39.488 -11.374 1.00 25.00 ?  166 SER   B H    1 
ATOM   6547 H HA   . SER   B 1 166 ? 35.878 -40.535 -12.939 1.00 26.75 ?  166 SER   B HA   1 
ATOM   6548 H HB2  . SER   B 1 166 ? 36.524 -42.586 -12.147 1.00 27.77 ?  166 SER   B HB2  1 
ATOM   6549 H HB3  . SER   B 1 166 ? 37.827 -41.715 -12.388 1.00 27.77 ?  166 SER   B HB3  1 
ATOM   6550 H HG   . SER   B 1 166 ? 37.866 -41.372 -10.221 1.00 27.96 ?  166 SER   B HG   1 
ATOM   6551 N N    . SER   B 1 167 ? 34.892 -40.048 -9.973  1.00 20.93 ?  167 SER   B N    1 
ATOM   6552 C CA   . SER   B 1 167 ? 33.741 -40.108 -9.080  1.00 20.73 ?  167 SER   B CA   1 
ATOM   6553 C C    . SER   B 1 167 ? 32.819 -38.891 -9.178  1.00 20.08 ?  167 SER   B C    1 
ATOM   6554 O O    . SER   B 1 167 ? 31.744 -38.896 -8.566  1.00 20.26 ?  167 SER   B O    1 
ATOM   6555 C CB   . SER   B 1 167 ? 34.198 -40.284 -7.626  1.00 20.93 ?  167 SER   B CB   1 
ATOM   6556 O OG   . SER   B 1 167 ? 34.880 -39.127 -7.169  1.00 20.67 ?  167 SER   B OG   1 
ATOM   6557 H H    . SER   B 1 167 ? 35.548 -39.595 -9.666  1.00 25.12 ?  167 SER   B H    1 
ATOM   6558 H HA   . SER   B 1 167 ? 33.216 -40.890 -9.313  1.00 24.88 ?  167 SER   B HA   1 
ATOM   6559 H HB2  . SER   B 1 167 ? 33.419 -40.435 -7.068  1.00 25.12 ?  167 SER   B HB2  1 
ATOM   6560 H HB3  . SER   B 1 167 ? 34.791 -41.057 -7.575  1.00 25.12 ?  167 SER   B HB3  1 
ATOM   6561 H HG   . SER   B 1 167 ? 35.570 -39.004 -7.639  1.00 24.81 ?  167 SER   B HG   1 
ATOM   6562 N N    . PHE   B 1 168 ? 33.196 -37.857 -9.930  1.00 19.69 ?  168 PHE   B N    1 
ATOM   6563 C CA   . PHE   B 1 168 ? 32.368 -36.654 -9.988  1.00 19.42 ?  168 PHE   B CA   1 
ATOM   6564 C C    . PHE   B 1 168 ? 31.059 -36.907 -10.726 1.00 17.31 ?  168 PHE   B C    1 
ATOM   6565 O O    . PHE   B 1 168 ? 30.020 -36.315 -10.383 1.00 17.84 ?  168 PHE   B O    1 
ATOM   6566 C CB   . PHE   B 1 168 ? 33.133 -35.513 -10.651 1.00 19.93 ?  168 PHE   B CB   1 
ATOM   6567 C CG   . PHE   B 1 168 ? 32.331 -34.257 -10.772 1.00 20.10 ?  168 PHE   B CG   1 
ATOM   6568 C CD1  . PHE   B 1 168 ? 31.993 -33.531 -9.641  1.00 21.19 ?  168 PHE   B CD1  1 
ATOM   6569 C CD2  . PHE   B 1 168 ? 31.880 -33.822 -12.002 1.00 19.61 ?  168 PHE   B CD2  1 
ATOM   6570 C CE1  . PHE   B 1 168 ? 31.233 -32.380 -9.734  1.00 21.21 ?  168 PHE   B CE1  1 
ATOM   6571 C CE2  . PHE   B 1 168 ? 31.129 -32.660 -12.110 1.00 20.64 ?  168 PHE   B CE2  1 
ATOM   6572 C CZ   . PHE   B 1 168 ? 30.801 -31.938 -10.972 1.00 20.63 ?  168 PHE   B CZ   1 
ATOM   6573 H H    . PHE   B 1 168 ? 33.921 -37.821 -10.394 1.00 23.63 ?  168 PHE   B H    1 
ATOM   6574 H HA   . PHE   B 1 168 ? 32.147 -36.382 -9.087  1.00 23.31 ?  168 PHE   B HA   1 
ATOM   6575 H HB2  . PHE   B 1 168 ? 33.918 -35.310 -10.118 1.00 23.92 ?  168 PHE   B HB2  1 
ATOM   6576 H HB3  . PHE   B 1 168 ? 33.398 -35.782 -11.542 1.00 23.92 ?  168 PHE   B HB3  1 
ATOM   6577 H HD1  . PHE   B 1 168 ? 32.279 -33.828 -8.807  1.00 25.44 ?  168 PHE   B HD1  1 
ATOM   6578 H HD2  . PHE   B 1 168 ? 32.098 -34.294 -12.769 1.00 23.54 ?  168 PHE   B HD2  1 
ATOM   6579 H HE1  . PHE   B 1 168 ? 31.015 -31.902 -8.967  1.00 25.46 ?  168 PHE   B HE1  1 
ATOM   6580 H HE2  . PHE   B 1 168 ? 30.835 -32.369 -12.944 1.00 24.77 ?  168 PHE   B HE2  1 
ATOM   6581 H HZ   . PHE   B 1 168 ? 30.288 -31.164 -11.042 1.00 24.76 ?  168 PHE   B HZ   1 
ATOM   6582 N N    . LEU   B 1 169 ? 31.092 -37.776 -11.735 1.00 18.42 ?  169 LEU   B N    1 
ATOM   6583 C CA   . LEU   B 1 169 ? 29.916 -38.093 -12.532 1.00 20.77 ?  169 LEU   B CA   1 
ATOM   6584 C C    . LEU   B 1 169 ? 29.910 -39.542 -13.001 1.00 23.51 ?  169 LEU   B C    1 
ATOM   6585 O O    . LEU   B 1 169 ? 29.006 -39.969 -13.722 1.00 26.17 ?  169 LEU   B O    1 
ATOM   6586 C CB   . LEU   B 1 169 ? 29.843 -37.169 -13.747 1.00 22.56 ?  169 LEU   B CB   1 
ATOM   6587 C CG   . LEU   B 1 169 ? 28.575 -36.320 -13.833 1.00 25.36 ?  169 LEU   B CG   1 
ATOM   6588 C CD1  . LEU   B 1 169 ? 28.496 -35.659 -15.191 1.00 26.34 ?  169 LEU   B CD1  1 
ATOM   6589 C CD2  . LEU   B 1 169 ? 27.329 -37.147 -13.566 1.00 25.60 ?  169 LEU   B CD2  1 
ATOM   6590 O OXT  . LEU   B 1 169 ? 30.811 -40.309 -12.673 1.00 24.19 -1 169 LEU   B OXT  1 
ATOM   6591 H H    . LEU   B 1 169 ? 31.801 -38.197 -11.991 1.00 22.12 ?  169 LEU   B H    1 
ATOM   6592 H HA   . LEU   B 1 169 ? 29.132 -37.949 -11.988 1.00 24.93 ?  169 LEU   B HA   1 
ATOM   6593 H HB2  . LEU   B 1 169 ? 30.598 -36.559 -13.727 1.00 27.08 ?  169 LEU   B HB2  1 
ATOM   6594 H HB3  . LEU   B 1 169 ? 29.881 -37.704 -14.557 1.00 27.08 ?  169 LEU   B HB3  1 
ATOM   6595 H HG   . LEU   B 1 169 ? 28.618 -35.616 -13.163 1.00 30.45 ?  169 LEU   B HG   1 
ATOM   6596 H HD11 . LEU   B 1 169 ? 27.705 -35.098 -15.223 1.00 31.62 ?  169 LEU   B HD11 1 
ATOM   6597 H HD12 . LEU   B 1 169 ? 29.291 -35.120 -15.324 1.00 31.62 ?  169 LEU   B HD12 1 
ATOM   6598 H HD13 . LEU   B 1 169 ? 28.443 -36.348 -15.870 1.00 31.62 ?  169 LEU   B HD13 1 
ATOM   6599 H HD21 . LEU   B 1 169 ? 26.574 -36.739 -14.011 1.00 30.73 ?  169 LEU   B HD21 1 
ATOM   6600 H HD22 . LEU   B 1 169 ? 27.471 -38.046 -13.907 1.00 30.73 ?  169 LEU   B HD22 1 
ATOM   6601 H HD23 . LEU   B 1 169 ? 27.174 -37.179 -12.610 1.00 30.73 ?  169 LEU   B HD23 1 
HETATM 6602 N N2   B A1A5Y C 2 .   ? 13.004 5.794   5.056   0.14 19.52 ?  201 A1A5Y A N2   1 
HETATM 6603 C C3   B A1A5Y C 2 .   ? 15.524 4.528   5.694   0.14 19.01 ?  201 A1A5Y A C3   1 
HETATM 6604 C C6   B A1A5Y C 2 .   ? 14.795 3.298   2.114   0.14 19.01 ?  201 A1A5Y A C6   1 
HETATM 6605 C C9   B A1A5Y C 2 .   ? 13.095 -0.072  1.539   0.14 16.89 ?  201 A1A5Y A C9   1 
HETATM 6606 C C12  B A1A5Y C 2 .   ? 14.570 -0.772  -0.396  0.14 17.28 ?  201 A1A5Y A C12  1 
HETATM 6607 C C14  B A1A5Y C 2 .   ? 16.613 -1.041  1.193   0.14 16.93 ?  201 A1A5Y A C14  1 
HETATM 6608 C C17  B A1A5Y C 2 .   ? 16.741 0.235   -0.847  0.14 17.21 ?  201 A1A5Y A C17  1 
HETATM 6609 C C19  B A1A5Y C 2 .   ? 12.974 4.767   2.844   0.14 19.39 ?  201 A1A5Y A C19  1 
HETATM 6610 C C1   B A1A5Y C 2 .   ? 13.590 6.200   6.193   0.14 19.61 ?  201 A1A5Y A C1   1 
HETATM 6611 C C10  B A1A5Y C 2 .   ? 12.125 -0.654  2.555   0.14 16.83 ?  201 A1A5Y A C10  1 
HETATM 6612 C C11  B A1A5Y C 2 .   ? 13.455 -1.196  0.559   0.14 17.02 ?  201 A1A5Y A C11  1 
HETATM 6613 C C13  B A1A5Y C 2 .   ? 15.768 -0.080  0.310   0.14 17.20 ?  201 A1A5Y A C13  1 
HETATM 6614 C C15  B A1A5Y C 2 .   ? 17.981 -1.280  0.560   0.14 16.93 ?  201 A1A5Y A C15  1 
HETATM 6615 C C16  B A1A5Y C 2 .   ? 17.821 -0.853  -0.892  0.14 17.12 ?  201 A1A5Y A C16  1 
HETATM 6616 C C18  B A1A5Y C 2 .   ? 13.558 3.940   1.861   0.14 19.45 ?  201 A1A5Y A C18  1 
HETATM 6617 C C2   B A1A5Y C 2 .   ? 15.031 5.758   6.486   0.14 19.34 ?  201 A1A5Y A C2   1 
HETATM 6618 C C20  B A1A5Y C 2 .   ? 13.611 4.961   4.084   0.14 19.42 ?  201 A1A5Y A C20  1 
HETATM 6619 C C4   B A1A5Y C 2 .   ? 14.839 4.322   4.350   0.14 19.28 ?  201 A1A5Y A C4   1 
HETATM 6620 C C5   B A1A5Y C 2 .   ? 15.423 3.492   3.369   0.14 19.28 ?  201 A1A5Y A C5   1 
HETATM 6621 C C7   B A1A5Y C 2 .   ? 15.451 2.392   1.097   0.14 18.10 ?  201 A1A5Y A C7   1 
HETATM 6622 C C8   B A1A5Y C 2 .   ? 14.358 0.473   2.231   0.14 17.18 ?  201 A1A5Y A C8   1 
HETATM 6623 F F1   B A1A5Y C 2 .   ? 12.919 3.771   0.678   0.14 19.98 ?  201 A1A5Y A F1   1 
HETATM 6624 N N1   B A1A5Y C 2 .   ? 15.238 1.034   1.179   0.14 17.31 ?  201 A1A5Y A N1   1 
HETATM 6625 O O1   B A1A5Y C 2 .   ? 13.002 6.924   6.994   0.14 20.03 ?  201 A1A5Y A O1   1 
HETATM 6626 O O2   B A1A5Y C 2 .   ? 16.160 2.946   0.256   0.14 18.09 ?  201 A1A5Y A O2   1 
HETATM 6627 O O3   B A1A5Y C 2 .   ? 10.918 -0.351  2.457   0.14 16.93 ?  201 A1A5Y A O3   1 
HETATM 6628 O O4   B A1A5Y C 2 .   ? 12.629 -1.405  3.417   0.14 16.67 ?  201 A1A5Y A O4   1 
HETATM 6629 H H22  B A1A5Y C 2 .   ? 12.058 6.095   4.881   0.14 23.43 ?  201 A1A5Y A H22  1 
HETATM 6630 H H5   B A1A5Y C 2 .   ? 16.597 4.622   5.517   0.14 22.82 ?  201 A1A5Y A H5   1 
HETATM 6631 H H4   B A1A5Y C 2 .   ? 15.404 3.634   6.309   0.14 22.82 ?  201 A1A5Y A H4   1 
HETATM 6632 H H1   B A1A5Y C 2 .   ? 12.599 0.744   1.010   0.14 20.28 ?  201 A1A5Y A H1   1 
HETATM 6633 H H12  B A1A5Y C 2 .   ? 14.935 -1.655  -0.926  0.14 20.74 ?  201 A1A5Y A H12  1 
HETATM 6634 H H11  B A1A5Y C 2 .   ? 14.132 -0.130  -1.158  0.14 20.74 ?  201 A1A5Y A H11  1 
HETATM 6635 H H13  B A1A5Y C 2 .   ? 16.083 -1.991  1.285   0.14 20.33 ?  201 A1A5Y A H13  1 
HETATM 6636 H H14  B A1A5Y C 2 .   ? 16.762 -0.670  2.206   0.14 20.33 ?  201 A1A5Y A H14  1 
HETATM 6637 H H20  B A1A5Y C 2 .   ? 16.216 0.183   -1.795  0.14 20.66 ?  201 A1A5Y A H20  1 
HETATM 6638 H H19  B A1A5Y C 2 .   ? 17.135 1.233   -0.788  0.14 20.66 ?  201 A1A5Y A H19  1 
HETATM 6639 H H21  B A1A5Y C 2 .   ? 12.034 5.253   2.644   0.14 23.27 ?  201 A1A5Y A H21  1 
HETATM 6640 H H9   B A1A5Y C 2 .   ? 13.758 -2.088  1.105   0.14 20.43 ?  201 A1A5Y A H9   1 
HETATM 6641 H H10  B A1A5Y C 2 .   ? 12.569 -1.482  -0.005  0.14 20.43 ?  201 A1A5Y A H10  1 
HETATM 6642 H H15  B A1A5Y C 2 .   ? 18.750 -0.700  1.076   0.14 20.32 ?  201 A1A5Y A H15  1 
HETATM 6643 H H16  B A1A5Y C 2 .   ? 18.265 -2.328  0.645   0.14 20.32 ?  201 A1A5Y A H16  1 
HETATM 6644 H H17  B A1A5Y C 2 .   ? 18.757 -0.492  -1.317  0.14 20.56 ?  201 A1A5Y A H17  1 
HETATM 6645 H H18  B A1A5Y C 2 .   ? 17.488 -1.702  -1.495  0.14 20.56 ?  201 A1A5Y A H18  1 
HETATM 6646 H H3   B A1A5Y C 2 .   ? 15.707 6.597   6.336   0.14 23.21 ?  201 A1A5Y A H3   1 
HETATM 6647 H H2   B A1A5Y C 2 .   ? 15.080 5.530   7.553   0.14 23.21 ?  201 A1A5Y A H2   1 
HETATM 6648 H H6   B A1A5Y C 2 .   ? 16.365 3.007   3.587   0.14 23.14 ?  201 A1A5Y A H6   1 
HETATM 6649 H H8   B A1A5Y C 2 .   ? 14.048 1.153   3.011   0.14 20.63 ?  201 A1A5Y A H8   1 
HETATM 6650 H H7   B A1A5Y C 2 .   ? 14.858 -0.302  2.804   0.14 20.63 ?  201 A1A5Y A H7   1 
HETATM 6651 O O    . HOH   D 3 .   ? 4.776  3.854   0.727   1.00 25.57 ?  301 HOH   A O    1 
HETATM 6652 O O    . HOH   D 3 .   ? 14.757 -4.766  20.582  1.00 42.70 ?  302 HOH   A O    1 
HETATM 6653 O O    . HOH   D 3 .   ? 11.552 -10.917 -10.143 1.00 43.06 ?  303 HOH   A O    1 
HETATM 6654 O O    . HOH   D 3 .   ? 26.839 11.419  1.628   1.00 18.49 ?  304 HOH   A O    1 
HETATM 6655 O O    . HOH   D 3 .   ? 15.232 -21.579 14.240  1.00 18.74 ?  305 HOH   A O    1 
HETATM 6656 O O    . HOH   D 3 .   ? 15.191 -12.233 18.734  1.00 38.57 ?  306 HOH   A O    1 
HETATM 6657 O O    . HOH   D 3 .   ? 16.203 16.717  8.642   1.00 33.68 ?  307 HOH   A O    1 
HETATM 6658 O O    . HOH   D 3 .   ? 34.459 -1.822  12.501  1.00 41.65 ?  308 HOH   A O    1 
HETATM 6659 O O    . HOH   D 3 .   ? 12.181 0.272   14.922  1.00 34.53 ?  309 HOH   A O    1 
HETATM 6660 O O    . HOH   D 3 .   ? 13.259 -1.433  -6.574  1.00 18.52 ?  310 HOH   A O    1 
HETATM 6661 O O    . HOH   D 3 .   ? 3.644  -9.360  10.004  1.00 35.57 ?  311 HOH   A O    1 
HETATM 6662 O O    . HOH   D 3 .   ? 25.639 -0.758  -7.332  1.00 16.20 ?  312 HOH   A O    1 
HETATM 6663 O O    . HOH   D 3 .   ? 6.970  -8.163  11.904  1.00 22.39 ?  313 HOH   A O    1 
HETATM 6664 O O    . HOH   D 3 .   ? 14.631 -3.544  3.188   1.00 19.65 ?  314 HOH   A O    1 
HETATM 6665 O O    . HOH   D 3 .   ? 24.503 1.974   -6.953  1.00 19.80 ?  315 HOH   A O    1 
HETATM 6666 O O    . HOH   D 3 .   ? 42.366 10.528  5.224   1.00 21.21 ?  316 HOH   A O    1 
HETATM 6667 O O    . HOH   D 3 .   ? 30.210 -13.263 -8.498  1.00 28.11 ?  317 HOH   A O    1 
HETATM 6668 O O    . HOH   D 3 .   ? 9.879  -21.325 5.693   1.00 20.67 ?  318 HOH   A O    1 
HETATM 6669 O O    . HOH   D 3 .   ? 7.960  -12.553 -0.832  1.00 21.39 ?  319 HOH   A O    1 
HETATM 6670 O O    . HOH   D 3 .   ? 28.268 -6.387  19.607  1.00 42.73 ?  320 HOH   A O    1 
HETATM 6671 O O    . HOH   D 3 .   ? 15.138 -8.092  -9.619  1.00 22.97 ?  321 HOH   A O    1 
HETATM 6672 O O    . HOH   D 3 .   ? 19.016 -21.941 6.926   1.00 34.68 ?  322 HOH   A O    1 
HETATM 6673 O O    . HOH   D 3 .   ? 28.894 0.520   -9.692  1.00 22.63 ?  323 HOH   A O    1 
HETATM 6674 O O    . HOH   D 3 .   ? 33.966 -1.005  -8.892  1.00 29.69 ?  324 HOH   A O    1 
HETATM 6675 O O    . HOH   D 3 .   ? 14.759 -14.010 16.727  1.00 26.31 ?  325 HOH   A O    1 
HETATM 6676 O O    . HOH   D 3 .   ? 28.203 -0.049  -13.356 1.00 38.52 ?  326 HOH   A O    1 
HETATM 6677 O O    A HOH   D 3 .   ? 14.023 -4.564  -11.692 0.86 27.06 ?  327 HOH   A O    1 
HETATM 6678 O O    . HOH   D 3 .   ? 36.166 -5.096  -0.529  1.00 29.30 ?  328 HOH   A O    1 
HETATM 6679 O O    . HOH   D 3 .   ? 19.860 -12.501 -8.922  1.00 27.35 ?  329 HOH   A O    1 
HETATM 6680 O O    . HOH   D 3 .   ? 26.483 -19.299 -1.802  1.00 15.73 ?  330 HOH   A O    1 
HETATM 6681 O O    . HOH   D 3 .   ? 22.272 -19.252 11.309  1.00 35.34 ?  331 HOH   A O    1 
HETATM 6682 O O    . HOH   D 3 .   ? -0.577 -8.489  2.299   1.00 42.48 ?  332 HOH   A O    1 
HETATM 6683 O O    . HOH   D 3 .   ? 31.007 -18.123 7.739   1.00 19.84 ?  333 HOH   A O    1 
HETATM 6684 O O    . HOH   D 3 .   ? 18.736 -19.401 13.526  1.00 40.64 ?  334 HOH   A O    1 
HETATM 6685 O O    . HOH   D 3 .   ? 9.073  -10.188 19.358  1.00 43.75 ?  335 HOH   A O    1 
HETATM 6686 O O    . HOH   D 3 .   ? 37.549 2.804   10.165  1.00 30.09 ?  336 HOH   A O    1 
HETATM 6687 O O    . HOH   D 3 .   ? 20.608 -19.749 -5.040  1.00 33.06 ?  337 HOH   A O    1 
HETATM 6688 O O    . HOH   D 3 .   ? 38.231 10.108  7.151   1.00 43.16 ?  338 HOH   A O    1 
HETATM 6689 O O    A HOH   D 3 .   ? 17.467 -1.703  0.481   0.86 18.76 ?  339 HOH   A O    1 
HETATM 6690 O O    . HOH   D 3 .   ? 8.015  -21.500 4.009   1.00 47.37 ?  340 HOH   A O    1 
HETATM 6691 O O    A HOH   D 3 .   ? 17.114 -18.106 15.083  0.86 24.70 ?  341 HOH   A O    1 
HETATM 6692 O O    . HOH   D 3 .   ? 15.790 -0.942  5.370   1.00 28.65 ?  342 HOH   A O    1 
HETATM 6693 O O    . HOH   D 3 .   ? 18.551 -2.400  -16.371 1.00 45.18 ?  343 HOH   A O    1 
HETATM 6694 O O    . HOH   D 3 .   ? 22.439 5.328   19.133  1.00 42.50 ?  344 HOH   A O    1 
HETATM 6695 O O    . HOH   D 3 .   ? 17.033 -19.283 4.925   1.00 16.40 ?  345 HOH   A O    1 
HETATM 6696 O O    . HOH   D 3 .   ? 39.702 -1.012  -5.237  1.00 21.05 ?  346 HOH   A O    1 
HETATM 6697 O O    . HOH   D 3 .   ? 0.760  -4.411  0.311   1.00 30.92 ?  347 HOH   A O    1 
HETATM 6698 O O    . HOH   D 3 .   ? 17.130 -17.789 -5.042  1.00 27.74 ?  348 HOH   A O    1 
HETATM 6699 O O    . HOH   D 3 .   ? 31.655 8.185   14.830  1.00 28.49 ?  349 HOH   A O    1 
HETATM 6700 O O    . HOH   D 3 .   ? 6.476  -5.577  11.206  1.00 21.45 ?  350 HOH   A O    1 
HETATM 6701 O O    . HOH   D 3 .   ? 38.501 4.952   6.976   1.00 17.72 ?  351 HOH   A O    1 
HETATM 6702 O O    . HOH   D 3 .   ? 21.220 -2.372  -2.133  1.00 16.78 ?  352 HOH   A O    1 
HETATM 6703 O O    . HOH   D 3 .   ? 23.991 -2.094  -2.052  1.00 11.57 ?  353 HOH   A O    1 
HETATM 6704 O O    . HOH   D 3 .   ? 31.666 -9.373  -6.694  1.00 23.17 ?  354 HOH   A O    1 
HETATM 6705 O O    . HOH   D 3 .   ? 27.869 0.839   -7.164  1.00 15.03 ?  355 HOH   A O    1 
HETATM 6706 O O    . HOH   D 3 .   ? 27.327 13.774  2.835   1.00 28.37 ?  356 HOH   A O    1 
HETATM 6707 O O    . HOH   D 3 .   ? 42.567 4.302   5.379   1.00 33.76 ?  357 HOH   A O    1 
HETATM 6708 O O    . HOH   D 3 .   ? 44.264 7.106   6.465   1.00 26.89 ?  358 HOH   A O    1 
HETATM 6709 O O    . HOH   D 3 .   ? 37.244 11.933  4.961   1.00 34.26 ?  359 HOH   A O    1 
HETATM 6710 O O    . HOH   D 3 .   ? 21.841 -21.861 8.376   1.00 29.63 ?  360 HOH   A O    1 
HETATM 6711 O O    . HOH   D 3 .   ? 35.762 -12.644 6.842   1.00 16.86 ?  361 HOH   A O    1 
HETATM 6712 O O    . HOH   D 3 .   ? 43.296 7.801   2.714   1.00 29.55 ?  362 HOH   A O    1 
HETATM 6713 O O    . HOH   D 3 .   ? 37.191 -2.800  9.707   1.00 42.70 ?  363 HOH   A O    1 
HETATM 6714 O O    . HOH   D 3 .   ? 31.068 -13.922 -2.490  1.00 15.59 ?  364 HOH   A O    1 
HETATM 6715 O O    . HOH   D 3 .   ? 15.121 3.835   17.920  1.00 40.93 ?  365 HOH   A O    1 
HETATM 6716 O O    . HOH   D 3 .   ? 15.530 11.934  7.983   1.00 38.94 ?  366 HOH   A O    1 
HETATM 6717 O O    . HOH   D 3 .   ? 14.336 -21.144 -4.355  1.00 32.28 ?  367 HOH   A O    1 
HETATM 6718 O O    . HOH   D 3 .   ? 28.507 -10.560 -14.096 1.00 42.84 ?  368 HOH   A O    1 
HETATM 6719 O O    . HOH   D 3 .   ? 13.561 -15.233 -7.455  1.00 27.86 ?  369 HOH   A O    1 
HETATM 6720 O O    . HOH   D 3 .   ? 30.776 3.091   8.272   1.00 13.53 ?  370 HOH   A O    1 
HETATM 6721 O O    A HOH   D 3 .   ? -0.502 -3.093  3.167   0.86 36.96 ?  371 HOH   A O    1 
HETATM 6722 O O    B HOH   D 3 .   ? 20.946 2.621   0.374   0.14 13.67 ?  372 HOH   A O    1 
HETATM 6723 O O    . HOH   D 3 .   ? 24.315 3.610   -1.776  1.00 17.06 ?  373 HOH   A O    1 
HETATM 6724 O O    . HOH   D 3 .   ? 20.012 4.507   -7.601  1.00 19.96 ?  374 HOH   A O    1 
HETATM 6725 O O    . HOH   D 3 .   ? 31.667 -7.190  -9.851  1.00 22.70 ?  375 HOH   A O    1 
HETATM 6726 O O    . HOH   D 3 .   ? 33.633 -7.139  4.286   1.00 18.19 ?  376 HOH   A O    1 
HETATM 6727 O O    . HOH   D 3 .   ? 27.496 -10.604 14.043  1.00 17.69 ?  377 HOH   A O    1 
HETATM 6728 O O    . HOH   D 3 .   ? 18.542 9.442   9.043   1.00 22.63 ?  378 HOH   A O    1 
HETATM 6729 O O    . HOH   D 3 .   ? 43.912 8.484   -3.090  1.00 26.22 ?  379 HOH   A O    1 
HETATM 6730 O O    . HOH   D 3 .   ? 22.714 12.516  1.633   1.00 16.56 ?  380 HOH   A O    1 
HETATM 6731 O O    . HOH   D 3 .   ? 13.974 -5.009  17.552  1.00 25.49 ?  381 HOH   A O    1 
HETATM 6732 O O    A HOH   D 3 .   ? 9.012  -12.136 17.229  0.86 39.60 ?  382 HOH   A O    1 
HETATM 6733 O O    . HOH   D 3 .   ? 16.484 -22.060 0.960   1.00 31.44 ?  383 HOH   A O    1 
HETATM 6734 O O    . HOH   D 3 .   ? 24.703 -17.536 12.669  1.00 24.86 ?  384 HOH   A O    1 
HETATM 6735 O O    . HOH   D 3 .   ? 27.248 -5.832  -13.963 1.00 38.39 ?  385 HOH   A O    1 
HETATM 6736 O O    . HOH   D 3 .   ? 14.249 0.489   6.811   1.00 22.43 ?  386 HOH   A O    1 
HETATM 6737 O O    . HOH   D 3 .   ? 24.275 -7.789  14.444  1.00 17.91 ?  387 HOH   A O    1 
HETATM 6738 O O    . HOH   D 3 .   ? 30.057 -10.097 12.976  1.00 21.72 ?  388 HOH   A O    1 
HETATM 6739 O O    . HOH   D 3 .   ? 14.468 -0.536  -12.118 1.00 28.17 ?  389 HOH   A O    1 
HETATM 6740 O O    . HOH   D 3 .   ? 32.772 -9.223  6.002   1.00 20.60 ?  390 HOH   A O    1 
HETATM 6741 O O    . HOH   D 3 .   ? 15.991 6.968   3.040   1.00 16.70 ?  391 HOH   A O    1 
HETATM 6742 O O    . HOH   D 3 .   ? 30.686 1.839   16.682  1.00 22.86 ?  392 HOH   A O    1 
HETATM 6743 O O    . HOH   D 3 .   ? 14.087 -23.037 7.422   1.00 19.81 ?  393 HOH   A O    1 
HETATM 6744 O O    . HOH   D 3 .   ? 37.565 -2.000  5.813   1.00 28.12 ?  394 HOH   A O    1 
HETATM 6745 O O    . HOH   D 3 .   ? 7.638  -6.309  -6.564  1.00 41.29 ?  395 HOH   A O    1 
HETATM 6746 O O    . HOH   D 3 .   ? 23.431 11.376  4.124   1.00 13.75 ?  396 HOH   A O    1 
HETATM 6747 O O    A HOH   D 3 .   ? 18.925 -0.655  -1.588  0.86 13.91 ?  397 HOH   A O    1 
HETATM 6748 O O    . HOH   D 3 .   ? 22.733 -12.022 21.818  1.00 42.57 ?  398 HOH   A O    1 
HETATM 6749 O O    . HOH   D 3 .   ? 23.952 -15.673 -9.160  1.00 35.31 ?  399 HOH   A O    1 
HETATM 6750 O O    . HOH   D 3 .   ? 21.191 10.324  15.084  1.00 35.29 ?  400 HOH   A O    1 
HETATM 6751 O O    . HOH   D 3 .   ? 10.448 -22.192 -1.238  1.00 47.50 ?  401 HOH   A O    1 
HETATM 6752 O O    . HOH   D 3 .   ? 20.553 -20.010 2.757   1.00 20.26 ?  402 HOH   A O    1 
HETATM 6753 O O    . HOH   D 3 .   ? 11.011 1.607   12.827  1.00 25.73 ?  403 HOH   A O    1 
HETATM 6754 O O    A HOH   D 3 .   ? 21.315 3.169   -0.311  0.86 13.82 ?  404 HOH   A O    1 
HETATM 6755 O O    . HOH   D 3 .   ? 40.835 -8.172  -6.825  1.00 36.44 ?  405 HOH   A O    1 
HETATM 6756 O O    . HOH   D 3 .   ? 26.890 4.168   -0.652  1.00 14.07 ?  406 HOH   A O    1 
HETATM 6757 O O    . HOH   D 3 .   ? 14.433 -24.678 11.584  1.00 38.62 ?  407 HOH   A O    1 
HETATM 6758 O O    . HOH   D 3 .   ? 5.253  2.737   5.268   1.00 31.91 ?  408 HOH   A O    1 
HETATM 6759 O O    . HOH   D 3 .   ? 44.906 -0.628  2.901   1.00 40.57 ?  409 HOH   A O    1 
HETATM 6760 O O    . HOH   D 3 .   ? 30.886 6.216   -12.358 1.00 34.15 ?  410 HOH   A O    1 
HETATM 6761 O O    . HOH   D 3 .   ? 41.592 1.496   4.939   1.00 38.96 ?  411 HOH   A O    1 
HETATM 6762 O O    . HOH   D 3 .   ? 21.744 -13.790 -8.128  1.00 38.14 ?  412 HOH   A O    1 
HETATM 6763 O O    . HOH   D 3 .   ? 6.735  -3.409  13.031  1.00 32.57 ?  413 HOH   A O    1 
HETATM 6764 O O    . HOH   D 3 .   ? 36.685 -4.957  5.368   1.00 25.62 ?  414 HOH   A O    1 
HETATM 6765 O O    . HOH   D 3 .   ? 16.261 -14.161 20.273  1.00 49.47 ?  415 HOH   A O    1 
HETATM 6766 O O    . HOH   D 3 .   ? 30.345 -12.937 13.507  1.00 20.99 ?  416 HOH   A O    1 
HETATM 6767 O O    . HOH   D 3 .   ? 38.081 -1.367  -1.987  1.00 20.43 ?  417 HOH   A O    1 
HETATM 6768 O O    . HOH   D 3 .   ? 23.946 -20.271 -1.363  1.00 19.22 ?  418 HOH   A O    1 
HETATM 6769 O O    . HOH   D 3 .   ? 32.588 -4.205  -9.926  1.00 28.22 ?  419 HOH   A O    1 
HETATM 6770 O O    . HOH   D 3 .   ? 35.060 -5.186  -3.106  1.00 18.88 ?  420 HOH   A O    1 
HETATM 6771 O O    . HOH   D 3 .   ? 22.674 8.108   18.400  1.00 44.47 ?  421 HOH   A O    1 
HETATM 6772 O O    . HOH   D 3 .   ? 27.275 2.258   18.790  1.00 31.99 ?  422 HOH   A O    1 
HETATM 6773 O O    A HOH   D 3 .   ? 11.039 -0.374  1.985   0.86 21.83 ?  423 HOH   A O    1 
HETATM 6774 O O    . HOH   D 3 .   ? 23.962 3.921   -4.802  1.00 22.27 ?  424 HOH   A O    1 
HETATM 6775 O O    . HOH   D 3 .   ? 10.383 -13.725 -1.630  1.00 18.39 ?  425 HOH   A O    1 
HETATM 6776 O O    . HOH   D 3 .   ? 27.153 -3.263  19.318  1.00 35.57 ?  426 HOH   A O    1 
HETATM 6777 O O    . HOH   D 3 .   ? 32.429 -10.603 3.294   1.00 33.75 ?  427 HOH   A O    1 
HETATM 6778 O O    . HOH   D 3 .   ? 21.286 -9.199  21.353  1.00 52.40 ?  428 HOH   A O    1 
HETATM 6779 O O    . HOH   D 3 .   ? 11.700 -10.858 16.983  1.00 25.94 ?  429 HOH   A O    1 
HETATM 6780 O O    . HOH   D 3 .   ? 19.537 -11.123 24.123  1.00 69.56 ?  430 HOH   A O    1 
HETATM 6781 O O    . HOH   D 3 .   ? 18.903 2.067   -0.710  1.00 15.32 ?  431 HOH   A O    1 
HETATM 6782 O O    . HOH   D 3 .   ? 23.610 -8.039  17.040  1.00 23.76 ?  432 HOH   A O    1 
HETATM 6783 O O    . HOH   D 3 .   ? 18.420 -16.017 16.305  1.00 37.61 ?  433 HOH   A O    1 
HETATM 6784 O O    . HOH   D 3 .   ? 20.580 -17.754 24.820  1.00 49.44 ?  434 HOH   A O    1 
HETATM 6785 O O    A HOH   D 3 .   ? 16.223 2.960   -1.394  0.86 16.81 ?  435 HOH   A O    1 
HETATM 6786 O O    . HOH   D 3 .   ? 23.379 -20.932 1.267   1.00 20.68 ?  436 HOH   A O    1 
HETATM 6787 O O    . HOH   D 3 .   ? 9.497  -16.275 -1.995  1.00 39.86 ?  437 HOH   A O    1 
HETATM 6788 O O    . HOH   D 3 .   ? 34.407 -8.029  -0.602  1.00 29.75 ?  438 HOH   A O    1 
HETATM 6789 O O    . HOH   D 3 .   ? 23.221 7.557   -3.168  1.00 34.80 ?  439 HOH   A O    1 
HETATM 6790 O O    . HOH   D 3 .   ? 37.685 -8.781  -3.502  1.00 25.28 ?  440 HOH   A O    1 
HETATM 6791 O O    . HOH   D 3 .   ? 15.923 2.223   24.754  1.00 52.25 ?  441 HOH   A O    1 
HETATM 6792 O O    . HOH   D 3 .   ? 30.510 14.743  2.787   1.00 20.36 ?  442 HOH   A O    1 
HETATM 6793 O O    . HOH   D 3 .   ? 18.193 4.523   -15.257 1.00 54.57 ?  443 HOH   A O    1 
HETATM 6794 O O    . HOH   D 3 .   ? 21.584 -14.766 18.031  1.00 51.99 ?  444 HOH   A O    1 
HETATM 6795 O O    . HOH   D 3 .   ? 31.322 -12.767 0.002   1.00 21.94 ?  445 HOH   A O    1 
HETATM 6796 O O    A HOH   D 3 .   ? 14.002 -0.333  3.508   0.86 17.63 ?  446 HOH   A O    1 
HETATM 6797 O O    . HOH   D 3 .   ? -1.450 -4.995  7.768   1.00 39.93 ?  447 HOH   A O    1 
HETATM 6798 O O    . HOH   D 3 .   ? 14.879 8.651   5.023   1.00 40.02 ?  448 HOH   A O    1 
HETATM 6799 O O    . HOH   D 3 .   ? 25.409 8.227   -4.790  1.00 35.78 ?  449 HOH   A O    1 
HETATM 6800 O O    . HOH   D 3 .   ? 27.769 7.133   -6.429  1.00 36.01 ?  450 HOH   A O    1 
HETATM 6801 O O    . HOH   D 3 .   ? 29.888 -16.112 10.751  1.00 33.74 ?  451 HOH   A O    1 
HETATM 6802 O O    . HOH   D 3 .   ? 32.475 -15.934 10.792  1.00 36.23 ?  452 HOH   A O    1 
HETATM 6803 O O    . HOH   D 3 .   ? 29.736 -1.913  -12.697 1.00 45.09 ?  453 HOH   A O    1 
HETATM 6804 O O    . HOH   D 3 .   ? 23.155 -22.226 -3.350  1.00 39.76 ?  454 HOH   A O    1 
HETATM 6805 O O    . HOH   D 3 .   ? 19.869 -17.312 -5.098  1.00 26.12 ?  455 HOH   A O    1 
HETATM 6806 O O    . HOH   D 3 .   ? 16.880 -20.558 16.049  1.00 32.24 ?  456 HOH   A O    1 
HETATM 6807 O O    . HOH   D 3 .   ? 24.887 5.661   20.765  1.00 51.28 ?  457 HOH   A O    1 
HETATM 6808 O O    . HOH   D 3 .   ? 24.559 14.545  7.855   1.00 37.74 ?  458 HOH   A O    1 
HETATM 6809 O O    . HOH   D 3 .   ? 27.529 -11.274 16.498  1.00 38.54 ?  459 HOH   A O    1 
HETATM 6810 O O    . HOH   D 3 .   ? 26.909 11.669  -1.374  1.00 31.62 ?  460 HOH   A O    1 
HETATM 6811 O O    . HOH   D 3 .   ? 23.449 13.706  5.546   1.00 21.22 ?  461 HOH   A O    1 
HETATM 6812 O O    . HOH   D 3 .   ? 10.954 -14.993 -6.029  1.00 36.26 ?  462 HOH   A O    1 
HETATM 6813 O O    . HOH   D 3 .   ? 15.763 -21.541 3.692   1.00 25.95 ?  463 HOH   A O    1 
HETATM 6814 O O    . HOH   D 3 .   ? 21.941 5.280   -5.984  1.00 32.25 ?  464 HOH   A O    1 
HETATM 6815 O O    . HOH   D 3 .   ? 18.699 10.791  11.376  1.00 37.38 ?  465 HOH   A O    1 
HETATM 6816 O O    . HOH   D 3 .   ? 39.614 -7.023  -3.532  1.00 47.24 ?  466 HOH   A O    1 
HETATM 6817 O O    . HOH   D 3 .   ? 12.269 1.626   17.358  1.00 42.45 ?  467 HOH   A O    1 
HETATM 6818 O O    . HOH   D 3 .   ? 12.068 -13.357 16.395  1.00 43.36 ?  468 HOH   A O    1 
HETATM 6819 O O    . HOH   D 3 .   ? 25.756 10.759  -3.718  1.00 28.69 ?  469 HOH   A O    1 
HETATM 6820 O O    . HOH   D 3 .   ? 18.142 -16.165 -8.834  1.00 42.54 ?  470 HOH   A O    1 
HETATM 6821 O O    . HOH   D 3 .   ? 28.810 8.940   17.489  1.00 35.08 ?  471 HOH   A O    1 
HETATM 6822 O O    . HOH   D 3 .   ? 35.126 7.425   12.202  1.00 45.51 ?  472 HOH   A O    1 
HETATM 6823 O O    . HOH   D 3 .   ? 15.763 -17.117 -6.964  1.00 33.02 ?  473 HOH   A O    1 
HETATM 6824 O O    . HOH   D 3 .   ? 15.919 -6.759  -11.777 1.00 43.91 ?  474 HOH   A O    1 
HETATM 6825 O O    . HOH   D 3 .   ? 23.111 11.823  -4.050  1.00 20.92 ?  475 HOH   A O    1 
HETATM 6826 O O    . HOH   D 3 .   ? 17.390 -18.723 19.788  1.00 55.14 ?  476 HOH   A O    1 
HETATM 6827 O O    . HOH   D 3 .   ? 40.919 -3.955  -0.426  1.00 39.38 ?  477 HOH   A O    1 
HETATM 6828 O O    . HOH   D 3 .   ? 30.896 0.701   19.186  1.00 41.10 ?  478 HOH   A O    1 
HETATM 6829 O O    . HOH   D 3 .   ? 13.978 -10.303 -10.904 1.00 33.67 ?  479 HOH   A O    1 
HETATM 6830 O O    . HOH   D 3 .   ? 20.513 -16.082 -7.383  1.00 32.05 ?  480 HOH   A O    1 
HETATM 6831 O O    . HOH   D 3 .   ? 41.669 9.262   -4.111  1.00 31.07 ?  481 HOH   A O    1 
HETATM 6832 O O    . HOH   D 3 .   ? 44.491 10.462  -1.567  1.00 36.06 ?  482 HOH   A O    1 
HETATM 6833 O O    . HOH   D 3 .   ? 18.419 -23.156 1.985   1.00 52.10 ?  483 HOH   A O    1 
HETATM 6834 O O    . HOH   D 3 .   ? 23.304 -12.915 19.352  1.00 52.14 ?  484 HOH   A O    1 
HETATM 6835 O O    . HOH   D 3 .   ? 39.147 2.367   7.495   1.00 32.77 ?  485 HOH   A O    1 
HETATM 6836 O O    . HOH   D 3 .   ? 28.551 -4.637  -12.297 1.00 38.28 ?  486 HOH   A O    1 
HETATM 6837 O O    . HOH   D 3 .   ? 28.645 -7.855  -15.315 1.00 45.18 ?  487 HOH   A O    1 
HETATM 6838 O O    . HOH   D 3 .   ? 31.413 -0.578  -10.572 1.00 29.16 ?  488 HOH   A O    1 
HETATM 6839 O O    . HOH   D 3 .   ? 20.049 -22.316 4.226   1.00 31.18 ?  489 HOH   A O    1 
HETATM 6840 O O    . HOH   D 3 .   ? 40.517 -0.259  -7.842  1.00 33.99 ?  490 HOH   A O    1 
HETATM 6841 O O    . HOH   D 3 .   ? 14.089 -25.303 8.911   1.00 33.13 ?  491 HOH   A O    1 
HETATM 6842 O O    . HOH   D 3 .   ? 16.176 -23.367 5.756   1.00 30.20 ?  492 HOH   A O    1 
HETATM 6843 O O    . HOH   D 3 .   ? 30.708 -5.718  -11.793 1.00 50.56 ?  493 HOH   A O    1 
HETATM 6844 O O    . HOH   D 3 .   ? 37.382 -6.608  7.557   1.00 27.50 ?  494 HOH   A O    1 
HETATM 6845 O O    . HOH   D 3 .   ? 30.688 5.814   -14.706 1.00 36.02 ?  495 HOH   A O    1 
HETATM 6846 O O    . HOH   D 3 .   ? 23.078 -23.733 1.604   1.00 33.41 ?  496 HOH   A O    1 
HETATM 6847 O O    . HOH   D 3 .   ? 39.520 -0.016  6.599   1.00 31.77 ?  497 HOH   A O    1 
HETATM 6848 O O    . HOH   D 3 .   ? 37.977 13.888  6.815   1.00 47.22 ?  498 HOH   A O    1 
HETATM 6849 O O    . HOH   D 3 .   ? 28.947 14.439  0.872   1.00 50.78 ?  499 HOH   A O    1 
HETATM 6850 O O    . HOH   D 3 .   ? 8.146  -3.028  -5.712  1.00 45.45 ?  500 HOH   A O    1 
HETATM 6851 O O    . HOH   D 3 .   ? 22.038 -24.024 4.463   1.00 28.88 ?  501 HOH   A O    1 
HETATM 6852 O O    . HOH   D 3 .   ? 36.473 -6.538  10.165  1.00 51.37 ?  502 HOH   A O    1 
HETATM 6853 O O    . HOH   D 3 .   ? 17.379 -6.632  -14.199 1.00 39.90 ?  503 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 24.027 9.025   -7.233  1.00 39.28 ?  504 HOH   A O    1 
HETATM 6855 O O    . HOH   D 3 .   ? 16.347 -21.461 18.882  1.00 40.36 ?  505 HOH   A O    1 
HETATM 6856 O O    . HOH   D 3 .   ? 15.887 -12.406 27.549  1.00 46.23 ?  506 HOH   A O    1 
HETATM 6857 O O    . HOH   D 3 .   ? 14.654 -22.782 19.898  1.00 38.63 ?  507 HOH   A O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 29.834 -22.391 5.472   1.00 21.44 ?  201 HOH   B O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 41.654 -35.971 -17.220 1.00 35.70 ?  202 HOH   B O    1 
HETATM 6860 O O    . HOH   E 3 .   ? 27.712 -29.125 -1.890  1.00 38.35 ?  203 HOH   B O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 27.787 -41.662 -15.232 1.00 38.26 ?  204 HOH   B O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 48.070 -6.836  15.540  1.00 27.02 ?  205 HOH   B O    1 
HETATM 6863 O O    . HOH   E 3 .   ? 41.360 -7.724  5.450   1.00 41.36 ?  206 HOH   B O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 59.099 -18.690 6.795   1.00 36.96 ?  207 HOH   B O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 58.140 -12.932 8.311   1.00 34.48 ?  208 HOH   B O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 50.216 -3.339  7.118   1.00 37.84 ?  209 HOH   B O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 49.368 -22.662 -19.768 1.00 47.73 ?  210 HOH   B O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 54.469 -9.360  -8.785  1.00 21.32 ?  211 HOH   B O    1 
HETATM 6869 O O    . HOH   E 3 .   ? 37.943 -39.453 -0.169  1.00 42.75 ?  212 HOH   B O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 56.313 -19.720 7.156   1.00 32.85 ?  213 HOH   B O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 47.406 -7.352  -3.933  1.00 41.43 ?  214 HOH   B O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 30.187 -40.984 -8.139  1.00 17.51 ?  215 HOH   B O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 30.921 -28.706 4.299   1.00 29.41 ?  216 HOH   B O    1 
HETATM 6874 O O    . HOH   E 3 .   ? 29.913 -26.271 4.017   1.00 29.77 ?  217 HOH   B O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 55.407 -16.522 -14.366 1.00 35.22 ?  218 HOH   B O    1 
HETATM 6876 O O    . HOH   E 3 .   ? 52.939 -13.458 -20.387 1.00 37.67 ?  219 HOH   B O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 57.378 -16.238 -12.218 1.00 19.21 ?  220 HOH   B O    1 
HETATM 6878 O O    . HOH   E 3 .   ? 44.390 -7.141  2.028   1.00 36.63 ?  221 HOH   B O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 29.829 -34.167 -0.428  1.00 34.27 ?  222 HOH   B O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 39.335 -10.881 6.084   1.00 28.25 ?  223 HOH   B O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 34.500 -36.326 -7.221  1.00 19.46 ?  224 HOH   B O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 50.628 -6.070  0.241   1.00 32.14 ?  225 HOH   B O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 44.473 -27.748 -0.718  1.00 25.36 ?  226 HOH   B O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 56.620 -30.783 -7.742  1.00 31.40 ?  227 HOH   B O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 45.189 -34.884 6.849   1.00 41.30 ?  228 HOH   B O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 40.564 -16.101 14.072  1.00 26.71 ?  229 HOH   B O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 48.476 -36.541 -15.490 1.00 45.19 ?  230 HOH   B O    1 
HETATM 6888 O O    . HOH   E 3 .   ? 25.454 -25.916 -1.357  1.00 34.56 ?  231 HOH   B O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 46.352 -1.591  13.250  1.00 29.08 ?  232 HOH   B O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 41.351 -9.623  13.081  1.00 23.50 ?  233 HOH   B O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 57.718 -24.427 5.005   1.00 42.37 ?  234 HOH   B O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 41.449 -39.156 -14.945 1.00 23.29 ?  235 HOH   B O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 57.134 -26.772 -7.697  1.00 43.44 ?  236 HOH   B O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 32.795 -43.741 -11.387 1.00 21.73 ?  237 HOH   B O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 50.722 -12.948 -0.505  1.00 13.64 ?  238 HOH   B O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 35.079 -7.978  -3.044  1.00 19.37 ?  239 HOH   B O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 37.035 -19.728 -18.134 1.00 41.57 ?  240 HOH   B O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 39.480 -11.111 0.290   1.00 18.15 ?  241 HOH   B O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 44.893 -43.506 -10.514 1.00 29.00 ?  242 HOH   B O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 43.044 -43.212 -8.159  1.00 29.91 ?  243 HOH   B O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 42.552 -25.348 2.652   1.00 16.80 ?  244 HOH   B O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 42.613 -22.836 3.831   1.00 12.70 ?  245 HOH   B O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 28.384 -19.649 -13.137 1.00 25.17 ?  246 HOH   B O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 34.274 -18.421 11.418  1.00 25.28 ?  247 HOH   B O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 51.511 -13.823 10.941  1.00 29.80 ?  248 HOH   B O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 35.951 -43.267 -8.503  1.00 36.31 ?  249 HOH   B O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 41.841 -23.470 9.281   1.00 18.58 ?  250 HOH   B O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 57.605 -24.370 -3.851  1.00 23.08 ?  251 HOH   B O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 51.601 -6.488  4.348   1.00 22.13 ?  252 HOH   B O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 29.709 -25.166 -10.830 1.00 18.17 ?  253 HOH   B O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 34.866 -33.219 -19.260 1.00 32.93 ?  254 HOH   B O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 34.909 -24.544 13.805  1.00 32.88 ?  255 HOH   B O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 58.149 -10.611 -4.069  1.00 22.04 ?  256 HOH   B O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 40.316 -12.738 -11.536 1.00 16.46 ?  257 HOH   B O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 27.119 -31.762 -9.974  1.00 21.25 ?  258 HOH   B O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 43.163 -32.323 -17.085 1.00 25.46 ?  259 HOH   B O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 47.995 -24.412 -17.792 1.00 32.58 ?  260 HOH   B O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 30.840 -15.701 2.634   1.00 15.36 ?  261 HOH   B O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 46.829 -29.526 9.783   1.00 32.61 ?  262 HOH   B O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 38.395 -11.057 -2.253  1.00 19.67 ?  263 HOH   B O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 31.785 -17.887 -14.522 1.00 33.23 ?  264 HOH   B O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 33.501 -16.996 7.992   1.00 20.57 ?  265 HOH   B O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 47.991 -22.693 5.805   1.00 18.87 ?  266 HOH   B O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 28.226 -34.309 -9.400  1.00 21.41 ?  267 HOH   B O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 38.899 -11.985 12.310  1.00 36.92 ?  268 HOH   B O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 57.473 -9.232  1.362   1.00 21.11 ?  269 HOH   B O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 49.287 -28.697 -6.917  1.00 16.88 ?  270 HOH   B O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 34.474 -12.772 2.624   1.00 27.34 ?  271 HOH   B O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 43.358 -15.767 -12.190 1.00 15.15 ?  272 HOH   B O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 50.928 -39.931 -8.281  1.00 32.57 ?  273 HOH   B O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 28.451 -30.788 -14.694 1.00 30.48 ?  274 HOH   B O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 56.917 -8.635  8.362   1.00 21.50 ?  275 HOH   B O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 42.375 -34.650 3.726   1.00 26.96 ?  276 HOH   B O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 49.771 -0.526  10.278  1.00 36.87 ?  277 HOH   B O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 56.135 -23.481 -14.786 1.00 29.83 ?  278 HOH   B O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 46.602 -31.214 -4.812  1.00 22.58 ?  279 HOH   B O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 42.320 -9.857  9.327   1.00 22.55 ?  280 HOH   B O    1 
HETATM 6938 O O    . HOH   E 3 .   ? 27.958 -22.859 -8.017  1.00 18.63 ?  281 HOH   B O    1 
HETATM 6939 O O    . HOH   E 3 .   ? 57.101 -12.118 12.272  1.00 42.37 ?  282 HOH   B O    1 
HETATM 6940 O O    . HOH   E 3 .   ? 33.526 -15.266 -13.941 1.00 22.68 ?  283 HOH   B O    1 
HETATM 6941 O O    . HOH   E 3 .   ? 48.378 -25.032 3.095   1.00 14.37 ?  284 HOH   B O    1 
HETATM 6942 O O    . HOH   E 3 .   ? 47.038 -33.958 -4.661  1.00 19.12 ?  285 HOH   B O    1 
HETATM 6943 O O    . HOH   E 3 .   ? 30.530 -42.279 -10.615 1.00 31.13 ?  286 HOH   B O    1 
HETATM 6944 O O    . HOH   E 3 .   ? 42.812 -20.252 -20.764 1.00 35.16 ?  287 HOH   B O    1 
HETATM 6945 O O    . HOH   E 3 .   ? 37.359 -35.619 7.240   1.00 35.91 ?  288 HOH   B O    1 
HETATM 6946 O O    . HOH   E 3 .   ? 43.600 -15.455 18.236  1.00 33.12 ?  289 HOH   B O    1 
HETATM 6947 O O    . HOH   E 3 .   ? 45.357 -33.339 -15.963 1.00 25.49 ?  290 HOH   B O    1 
HETATM 6948 O O    . HOH   E 3 .   ? 41.157 -5.460  11.460  1.00 47.66 ?  291 HOH   B O    1 
HETATM 6949 O O    . HOH   E 3 .   ? 48.692 -19.980 5.894   1.00 14.86 ?  292 HOH   B O    1 
HETATM 6950 O O    . HOH   E 3 .   ? 52.533 -10.393 12.951  1.00 24.87 ?  293 HOH   B O    1 
HETATM 6951 O O    . HOH   E 3 .   ? 35.091 -33.549 4.504   1.00 29.73 ?  294 HOH   B O    1 
HETATM 6952 O O    . HOH   E 3 .   ? 42.610 -12.324 -18.500 1.00 31.24 ?  295 HOH   B O    1 
HETATM 6953 O O    . HOH   E 3 .   ? 36.775 -12.758 -1.470  1.00 29.62 ?  296 HOH   B O    1 
HETATM 6954 O O    . HOH   E 3 .   ? 51.184 -37.570 -9.636  1.00 26.29 ?  297 HOH   B O    1 
HETATM 6955 O O    . HOH   E 3 .   ? 42.308 -9.920  -14.965 1.00 39.48 ?  298 HOH   B O    1 
HETATM 6956 O O    . HOH   E 3 .   ? 27.533 -26.630 -15.582 1.00 35.55 ?  299 HOH   B O    1 
HETATM 6957 O O    . HOH   E 3 .   ? 44.602 -27.435 1.958   1.00 16.79 ?  300 HOH   B O    1 
HETATM 6958 O O    . HOH   E 3 .   ? 40.212 -10.810 -9.531  1.00 18.52 ?  301 HOH   B O    1 
HETATM 6959 O O    . HOH   E 3 .   ? 52.545 -35.637 -8.642  1.00 29.65 ?  302 HOH   B O    1 
HETATM 6960 O O    . HOH   E 3 .   ? 59.750 -15.259 8.144   1.00 35.12 ?  303 HOH   B O    1 
HETATM 6961 O O    . HOH   E 3 .   ? 49.867 -24.680 5.825   1.00 35.69 ?  304 HOH   B O    1 
HETATM 6962 O O    . HOH   E 3 .   ? 44.042 -29.321 -4.698  1.00 23.78 ?  305 HOH   B O    1 
HETATM 6963 O O    . HOH   E 3 .   ? 53.148 -16.078 -12.736 1.00 28.81 ?  306 HOH   B O    1 
HETATM 6964 O O    . HOH   E 3 .   ? 52.487 -29.203 -13.048 1.00 26.47 ?  307 HOH   B O    1 
HETATM 6965 O O    . HOH   E 3 .   ? 37.513 -18.055 13.127  1.00 30.97 ?  308 HOH   B O    1 
HETATM 6966 O O    . HOH   E 3 .   ? 45.848 -40.362 -3.571  1.00 33.60 ?  309 HOH   B O    1 
HETATM 6967 O O    . HOH   E 3 .   ? 53.403 -30.174 4.552   1.00 20.00 ?  310 HOH   B O    1 
HETATM 6968 O O    . HOH   E 3 .   ? 62.668 -13.591 4.597   1.00 27.60 ?  311 HOH   B O    1 
HETATM 6969 O O    . HOH   E 3 .   ? 51.648 -5.997  -7.948  1.00 49.22 ?  312 HOH   B O    1 
HETATM 6970 O O    . HOH   E 3 .   ? 25.941 -21.440 -3.528  1.00 18.43 ?  313 HOH   B O    1 
HETATM 6971 O O    . HOH   E 3 .   ? 41.722 -8.069  1.356   1.00 26.42 ?  314 HOH   B O    1 
HETATM 6972 O O    . HOH   E 3 .   ? 37.853 -10.206 -10.750 1.00 18.68 ?  315 HOH   B O    1 
HETATM 6973 O O    . HOH   E 3 .   ? 43.119 -34.470 0.084   1.00 23.40 ?  316 HOH   B O    1 
HETATM 6974 O O    . HOH   E 3 .   ? 32.795 -34.553 -5.923  1.00 17.89 ?  317 HOH   B O    1 
HETATM 6975 O O    . HOH   E 3 .   ? 43.182 -21.384 10.661  1.00 17.47 ?  318 HOH   B O    1 
HETATM 6976 O O    . HOH   E 3 .   ? 62.816 -20.146 -0.825  1.00 42.85 ?  319 HOH   B O    1 
HETATM 6977 O O    . HOH   E 3 .   ? 38.337 -12.742 7.892   1.00 19.22 ?  320 HOH   B O    1 
HETATM 6978 O O    . HOH   E 3 .   ? 37.079 -30.614 -21.041 1.00 32.87 ?  321 HOH   B O    1 
HETATM 6979 O O    . HOH   E 3 .   ? 48.100 -32.608 -16.648 1.00 45.64 ?  322 HOH   B O    1 
HETATM 6980 O O    . HOH   E 3 .   ? 44.574 -24.583 9.609   1.00 21.83 ?  323 HOH   B O    1 
HETATM 6981 O O    . HOH   E 3 .   ? 41.275 -24.489 15.766  1.00 44.27 ?  324 HOH   B O    1 
HETATM 6982 O O    . HOH   E 3 .   ? 26.326 -21.011 -6.266  1.00 18.16 ?  325 HOH   B O    1 
HETATM 6983 O O    . HOH   E 3 .   ? 44.208 -1.751  7.543   1.00 45.36 ?  326 HOH   B O    1 
HETATM 6984 O O    . HOH   E 3 .   ? 59.878 -17.249 -10.557 1.00 35.42 ?  327 HOH   B O    1 
HETATM 6985 O O    . HOH   E 3 .   ? 57.522 -21.927 3.340   1.00 32.47 ?  328 HOH   B O    1 
HETATM 6986 O O    . HOH   E 3 .   ? 36.721 -12.358 4.284   1.00 20.19 ?  329 HOH   B O    1 
HETATM 6987 O O    . HOH   E 3 .   ? 33.681 -31.122 11.030  1.00 37.20 ?  330 HOH   B O    1 
HETATM 6988 O O    . HOH   E 3 .   ? 27.794 -14.731 -9.480  1.00 36.39 ?  331 HOH   B O    1 
HETATM 6989 O O    . HOH   E 3 .   ? 47.131 -24.454 8.163   1.00 27.85 ?  332 HOH   B O    1 
HETATM 6990 O O    . HOH   E 3 .   ? 38.394 -9.310  -13.283 1.00 32.20 ?  333 HOH   B O    1 
HETATM 6991 O O    . HOH   E 3 .   ? 51.390 -32.968 -10.907 1.00 43.54 ?  334 HOH   B O    1 
HETATM 6992 O O    . HOH   E 3 .   ? 47.478 -27.410 1.989   1.00 16.50 ?  335 HOH   B O    1 
HETATM 6993 O O    . HOH   E 3 .   ? 45.707 -36.223 -16.156 1.00 37.29 ?  336 HOH   B O    1 
HETATM 6994 O O    . HOH   E 3 .   ? 46.835 -19.775 12.238  1.00 32.87 ?  337 HOH   B O    1 
HETATM 6995 O O    . HOH   E 3 .   ? 53.608 -12.518 -22.323 1.00 36.47 ?  338 HOH   B O    1 
HETATM 6996 O O    . HOH   E 3 .   ? 48.587 -11.917 -13.914 1.00 27.32 ?  339 HOH   B O    1 
HETATM 6997 O O    . HOH   E 3 .   ? 28.850 -42.812 -12.430 1.00 42.61 ?  340 HOH   B O    1 
HETATM 6998 O O    . HOH   E 3 .   ? 36.992 -15.087 -16.530 1.00 39.93 ?  341 HOH   B O    1 
HETATM 6999 O O    . HOH   E 3 .   ? 38.357 -12.207 -16.286 1.00 41.80 ?  342 HOH   B O    1 
HETATM 7000 O O    . HOH   E 3 .   ? 42.772 -43.490 -14.388 1.00 44.30 ?  343 HOH   B O    1 
HETATM 7001 O O    . HOH   E 3 .   ? 37.081 -45.114 -9.796  1.00 37.51 ?  344 HOH   B O    1 
HETATM 7002 O O    . HOH   E 3 .   ? 39.546 -23.612 -20.334 1.00 40.10 ?  345 HOH   B O    1 
HETATM 7003 O O    . HOH   E 3 .   ? 32.970 -14.651 1.009   1.00 22.38 ?  346 HOH   B O    1 
HETATM 7004 O O    . HOH   E 3 .   ? 33.630 -9.630  -8.758  1.00 31.82 ?  347 HOH   B O    1 
HETATM 7005 O O    . HOH   E 3 .   ? 34.556 -10.345 7.665   1.00 25.15 ?  348 HOH   B O    1 
HETATM 7006 O O    . HOH   E 3 .   ? 27.774 -26.574 -0.585  1.00 33.72 ?  349 HOH   B O    1 
HETATM 7007 O O    . HOH   E 3 .   ? 40.323 -43.452 -9.163  1.00 27.58 ?  350 HOH   B O    1 
HETATM 7008 O O    . HOH   E 3 .   ? 39.854 -44.266 -11.238 1.00 39.74 ?  351 HOH   B O    1 
HETATM 7009 O O    . HOH   E 3 .   ? 44.151 -37.375 -17.797 1.00 36.55 ?  352 HOH   B O    1 
HETATM 7010 O O    . HOH   E 3 .   ? 23.232 -23.647 6.718   1.00 37.26 ?  353 HOH   B O    1 
HETATM 7011 O O    . HOH   E 3 .   ? 62.525 -20.129 -4.890  1.00 50.10 ?  354 HOH   B O    1 
HETATM 7012 O O    . HOH   E 3 .   ? 38.552 -22.212 15.060  1.00 44.64 ?  355 HOH   B O    1 
HETATM 7013 O O    . HOH   E 3 .   ? 55.635 -8.257  10.823  1.00 27.23 ?  356 HOH   B O    1 
HETATM 7014 O O    . HOH   E 3 .   ? 56.535 -7.272  2.991   1.00 30.40 ?  357 HOH   B O    1 
HETATM 7015 O O    . HOH   E 3 .   ? 36.126 -8.477  -9.737  1.00 38.29 ?  358 HOH   B O    1 
HETATM 7016 O O    . HOH   E 3 .   ? 43.163 -12.710 -21.194 1.00 43.87 ?  359 HOH   B O    1 
HETATM 7017 O O    . HOH   E 3 .   ? 33.997 -7.751  11.553  1.00 43.84 ?  360 HOH   B O    1 
HETATM 7018 O O    . HOH   E 3 .   ? 61.496 -19.903 1.677   1.00 37.43 ?  361 HOH   B O    1 
HETATM 7019 O O    . HOH   E 3 .   ? 56.866 -21.513 -16.519 1.00 41.93 ?  362 HOH   B O    1 
HETATM 7020 O O    . HOH   E 3 .   ? 27.166 -25.948 -11.364 1.00 33.97 ?  363 HOH   B O    1 
HETATM 7021 O O    . HOH   E 3 .   ? 40.233 -8.807  9.880   1.00 38.57 ?  364 HOH   B O    1 
HETATM 7022 O O    . HOH   E 3 .   ? 58.887 -10.509 9.183   1.00 40.64 ?  365 HOH   B O    1 
HETATM 7023 O O    . HOH   E 3 .   ? 54.131 -5.714  2.944   1.00 39.02 ?  366 HOH   B O    1 
HETATM 7024 O O    . HOH   E 3 .   ? 40.185 -11.304 -13.924 1.00 35.45 ?  367 HOH   B O    1 
HETATM 7025 O O    . HOH   E 3 .   ? 32.443 -23.581 14.047  1.00 43.22 ?  368 HOH   B O    1 
HETATM 7026 O O    . HOH   E 3 .   ? 36.202 -8.731  8.971   1.00 37.20 ?  369 HOH   B O    1 
HETATM 7027 O O    . HOH   E 3 .   ? 48.338 -26.441 8.728   1.00 41.59 ?  370 HOH   B O    1 
HETATM 7028 O O    . HOH   E 3 .   ? 39.808 -7.100  7.789   1.00 44.69 ?  371 HOH   B O    1 
HETATM 7029 O O    . HOH   E 3 .   ? 55.963 -7.777  -0.666  1.00 42.04 ?  372 HOH   B O    1 
HETATM 7030 O O    . HOH   E 3 .   ? 52.035 -12.898 13.275  1.00 34.82 ?  373 HOH   B O    1 
HETATM 7031 O O    . HOH   E 3 .   ? 41.785 -9.945  -17.429 1.00 55.50 ?  374 HOH   B O    1 
HETATM 7032 O O    . HOH   E 3 .   ? 63.060 -12.360 6.875   1.00 38.37 ?  375 HOH   B O    1 
HETATM 7033 O O    . HOH   E 3 .   ? 38.034 -10.540 10.012  1.00 31.30 ?  376 HOH   B O    1 
HETATM 7034 O O    . HOH   E 3 .   ? 36.525 -22.728 13.309  1.00 28.81 ?  377 HOH   B O    1 
HETATM 7035 O O    . HOH   E 3 .   ? 41.817 -6.709  -4.800  1.00 47.39 ?  378 HOH   B O    1 
HETATM 7036 O O    . HOH   E 3 .   ? 44.089 -5.560  -3.534  1.00 44.64 ?  379 HOH   B O    1 
HETATM 7037 O O    . HOH   E 3 .   ? 42.594 -17.057 -23.195 1.00 46.02 ?  380 HOH   B O    1 
HETATM 7038 O O    . HOH   E 3 .   ? 40.105 -7.607  3.128   1.00 37.42 ?  381 HOH   B O    1 
HETATM 7039 O O    . HOH   E 3 .   ? 39.758 -14.073 15.748  1.00 57.97 ?  382 HOH   B O    1 
HETATM 7040 O O    . HOH   E 3 .   ? 52.827 -29.863 7.175   1.00 24.14 ?  383 HOH   B O    1 
HETATM 7041 O O    . HOH   E 3 .   ? 60.437 -22.274 2.784   1.00 57.94 ?  384 HOH   B O    1 
HETATM 7042 O O    . HOH   E 3 .   ? 46.722 -5.321  2.842   1.00 42.51 ?  385 HOH   B O    1 
HETATM 7043 O O    . HOH   E 3 .   ? 40.998 -9.788  15.810  1.00 48.05 ?  386 HOH   B O    1 
HETATM 7044 O O    . HOH   E 3 .   ? 25.803 -18.839 -11.908 1.00 41.20 ?  387 HOH   B O    1 
HETATM 7045 O O    . HOH   E 3 .   ? 35.386 -33.637 7.287   1.00 41.64 ?  388 HOH   B O    1 
HETATM 7046 O O    . HOH   E 3 .   ? 23.907 -20.863 -7.688  1.00 30.00 ?  389 HOH   B O    1 
HETATM 7047 O O    . HOH   E 3 .   ? 35.272 -20.326 13.319  1.00 33.29 ?  390 HOH   B O    1 
HETATM 7048 O O    . HOH   E 3 .   ? 40.679 -6.589  -0.851  1.00 29.63 ?  391 HOH   B O    1 
HETATM 7049 O O    . HOH   E 3 .   ? 44.094 -31.798 -3.844  1.00 36.97 ?  392 HOH   B O    1 
HETATM 7050 O O    . HOH   E 3 .   ? 26.632 -27.887 -13.438 1.00 39.42 ?  393 HOH   B O    1 
HETATM 7051 O O    . HOH   E 3 .   ? 27.955 -27.091 2.239   1.00 32.78 ?  394 HOH   B O    1 
HETATM 7052 O O    . HOH   E 3 .   ? 24.603 -20.611 -10.475 1.00 38.88 ?  395 HOH   B O    1 
HETATM 7053 O O    . HOH   E 3 .   ? 50.605 -30.826 8.678   1.00 30.98 ?  396 HOH   B O    1 
HETATM 7054 O O    . HOH   E 3 .   ? 26.837 -30.624 -12.652 1.00 29.52 ?  397 HOH   B O    1 
HETATM 7055 O O    . HOH   E 3 .   ? 34.414 -33.432 9.608   1.00 36.04 ?  398 HOH   B O    1 
HETATM 7056 O O    . HOH   E 3 .   ? 45.631 -20.209 15.237  1.00 54.25 ?  399 HOH   B O    1 
HETATM 7057 O O    . HOH   E 3 .   ? 57.469 -6.392  -2.340  1.00 34.29 ?  400 HOH   B O    1 
HETATM 7058 O O    . HOH   E 3 .   ? 40.858 -11.804 -22.329 1.00 48.23 ?  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   ? 0.7123 0.6978 0.7482 0.0155  -0.0250 0.0832  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7030 0.6945 0.7078 0.0082  -0.0152 0.0454  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7091 0.6951 0.7378 0.0144  -0.0246 0.0817  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7003 0.6921 0.7028 0.0078  -0.0157 0.0474  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6926 0.6819 0.7044 0.0094  -0.0251 0.0799  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6883 0.6807 0.6843 0.0055  -0.0198 0.0603  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6951 0.6839 0.7165 0.0112  -0.0259 0.0834  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6917 0.6832 0.6945 0.0059  -0.0203 0.0599  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7196 0.7031 0.7503 0.0170  -0.0222 0.0822  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7072 0.6988 0.7096 0.0092  -0.0121 0.0385  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7234 0.7061 0.7539 0.0182  -0.0214 0.0821  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7097 0.7012 0.7118 0.0097  -0.0109 0.0353  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7229 0.7056 0.7534 0.0177  -0.0207 0.0829  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7094 0.7009 0.7117 0.0096  -0.0108 0.0355  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6702 0.6644 0.6500 0.0024  -0.0235 0.0743  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.6278 0.6272 0.5523 -0.0086 -0.0238 0.0811  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5724 0.5836 0.5009 -0.0226 -0.0101 0.0587  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5750 0.5860 0.4862 -0.0237 -0.0125 0.0622  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.6378 0.6308 0.5056 -0.0070 -0.0365 0.1080  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.6457 0.6322 0.4603 -0.0065 -0.0481 0.1327  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.6494 0.6334 0.4431 -0.0058 -0.0559 0.1392  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.6479 0.6316 0.4451 -0.0059 -0.0499 0.1455  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.5106 0.5330 0.4581 -0.0366 0.0045  0.0337  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4475 0.4858 0.4168 -0.0476 0.0202  0.0089  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3799 0.4212 0.3392 -0.0529 0.0362  -0.0058 5   SER   A C   
49   O O   . SER   A 5   ? 0.3856 0.4324 0.3301 -0.0417 0.0404  -0.0199 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4540 0.4997 0.4518 -0.0513 0.0201  -0.0004 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4583 0.5033 0.4715 -0.0519 0.0222  -0.0053 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.3273 0.3762 0.2912 -0.0757 0.0560  0.0006  6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3530 0.3885 0.3214 -0.0449 0.0333  -0.0094 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2833 0.3350 0.2469 -0.0881 0.0687  0.0152  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.3257 0.3552 0.3016 -0.0370 0.0293  -0.0106 6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2754 0.3391 0.2649 -0.0977 0.0809  0.0121  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.3087 0.3351 0.3049 -0.0342 0.0298  -0.0114 6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2778 0.3523 0.2861 -0.1042 0.0754  0.0223  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.3099 0.3372 0.3122 -0.0343 0.0298  -0.0119 6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2595 0.3018 0.2200 -0.0762 0.0543  0.0228  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.3154 0.3417 0.2798 -0.0320 0.0255  -0.0109 6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2379 0.2734 0.2017 -0.0661 0.0384  0.0302  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.3059 0.3286 0.2601 -0.0282 0.0224  -0.0107 6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2249 0.2603 0.2001 -0.0577 0.0314  0.0332  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.3017 0.3235 0.2511 -0.0256 0.0209  -0.0101 6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2426 0.2669 0.2167 -0.0469 0.0290  0.0205  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.3022 0.3227 0.2520 -0.0260 0.0230  -0.0114 6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2264 0.2539 0.2096 -0.0487 0.0262  0.0349  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2993 0.3201 0.2457 -0.0244 0.0217  -0.0090 6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2397 0.2618 0.2234 -0.0369 0.0219  0.0174  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2995 0.3191 0.2466 -0.0249 0.0227  -0.0101 6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2351 0.2581 0.2143 -0.0408 0.0219  0.0241  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2988 0.3186 0.2439 -0.0241 0.0220  -0.0090 6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2635 0.3273 0.2642 -0.0972 0.0869  0.0062  7   SER   A N   
98   N N   B SER   A 7   ? 0.2903 0.3131 0.3004 -0.0315 0.0290  -0.0108 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2666 0.3279 0.2810 -0.0839 0.0821  -0.0155 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2728 0.2922 0.2929 -0.0288 0.0277  -0.0130 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2506 0.2861 0.2724 -0.0795 0.0848  -0.0170 7   SER   A C   
102  C C   B SER   A 7   ? 0.2566 0.2702 0.2771 -0.0253 0.0250  -0.0089 7   SER   A C   
103  O O   A SER   A 7   ? 0.2565 0.2704 0.2844 -0.0834 0.0870  -0.0092 7   SER   A O   
104  O O   B SER   A 7   ? 0.2566 0.2680 0.2797 -0.0233 0.0256  -0.0096 7   SER   A O   
105  C CB  A SER   A 7   ? 0.2892 0.3609 0.3082 -0.0681 0.0727  -0.0214 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2721 0.2928 0.2990 -0.0285 0.0276  -0.0175 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.3103 0.3752 0.3411 -0.0522 0.0712  -0.0216 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2720 0.2947 0.3052 -0.0287 0.0278  -0.0196 7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2321 0.2677 0.2713 -0.0732 0.0885  -0.0262 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2422 0.2516 0.2600 -0.0235 0.0205  -0.0085 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.2215 0.2454 0.2812 -0.0601 0.0790  -0.0157 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2307 0.2347 0.2443 -0.0177 0.0210  -0.0061 8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1992 0.2287 0.2719 -0.0466 0.0688  -0.0093 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2192 0.2188 0.2299 -0.0132 0.0209  -0.0054 8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1994 0.2302 0.2937 -0.0327 0.0627  -0.0225 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.2187 0.2178 0.2266 -0.0117 0.0249  -0.0077 8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1758 0.2135 0.2528 -0.0365 0.0573  0.0099  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.2081 0.2043 0.2159 -0.0094 0.0190  -0.0063 9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1717 0.1970 0.2265 -0.0292 0.0385  0.0210  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1989 0.1927 0.1995 -0.0074 0.0151  -0.0057 9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1763 0.1818 0.2207 -0.0197 0.0486  0.0385  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1951 0.1810 0.1900 -0.0098 0.0161  0.0014  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.2050 0.1994 0.2397 -0.0272 0.0368  0.0354  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1990 0.1778 0.1850 -0.0111 0.0173  -0.0011 9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1607 0.2064 0.2236 -0.0191 0.0300  0.0198  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1926 0.1921 0.1928 -0.0049 0.0123  -0.0104 9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1598 0.2125 0.2178 -0.0061 0.0310  0.0112  9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1892 0.1924 0.1848 -0.0018 0.0101  -0.0127 9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1608 0.2140 0.2310 -0.0190 0.0397  0.0068  9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1877 0.1917 0.1844 -0.0017 0.0085  -0.0153 9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1537 0.2052 0.2165 -0.0014 0.0248  0.0255  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1879 0.1914 0.1870 -0.0015 0.0121  -0.0097 9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1636 0.2146 0.2404 -0.0203 0.0413  0.0025  9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1885 0.1939 0.1867 -0.0027 0.0077  -0.0156 9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1594 0.2097 0.2261 -0.0038 0.0350  0.0191  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1890 0.1941 0.1899 -0.0028 0.0124  -0.0110 9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1637 0.2111 0.2570 -0.0225 0.0467  0.0134  9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1916 0.1961 0.1939 -0.0049 0.0121  -0.0121 9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1719 0.2212 0.2914 -0.0329 0.0480  0.0107  9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1981 0.1984 0.1997 -0.0070 0.0156  -0.0117 9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1574 0.1669 0.2214 -0.0166 0.0279  0.0376  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1859 0.1723 0.1870 -0.0124 0.0162  0.0085  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1527 0.1712 0.2287 -0.0167 0.0172  0.0362  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1767 0.1662 0.1822 -0.0168 0.0191  0.0174  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1520 0.1596 0.2212 -0.0185 0.0090  0.0350  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1741 0.1598 0.1819 -0.0130 0.0178  0.0095  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1511 0.1479 0.2372 -0.0210 0.0298  0.0362  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1734 0.1538 0.1838 -0.0102 0.0204  0.0053  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1548 0.1857 0.2659 -0.0184 0.0020  0.0506  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1717 0.1673 0.1777 -0.0242 0.0237  0.0287  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1676 0.2067 0.3070 -0.0080 -0.0299 0.0626  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1681 0.1668 0.1656 -0.0304 0.0283  0.0415  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1964 0.2198 0.3463 -0.0180 -0.0203 0.0600  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1693 0.1670 0.1670 -0.0346 0.0259  0.0411  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1973 0.2359 0.3308 -0.0030 -0.0081 0.0474  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1700 0.1697 0.1733 -0.0298 0.0288  0.0432  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1538 0.1592 0.2075 -0.0288 0.0101  0.0492  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1740 0.1642 0.1804 -0.0109 0.0187  0.0046  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1560 0.1590 0.2200 -0.0323 0.0093  0.0510  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1771 0.1720 0.1835 -0.0098 0.0189  0.0022  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1488 0.1667 0.2118 -0.0312 0.0074  0.0476  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1769 0.1771 0.1794 -0.0079 0.0226  0.0014  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1527 0.2144 0.2349 -0.0623 0.0237  0.0211  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1771 0.1834 0.1892 -0.0160 0.0268  -0.0030 11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1594 0.1520 0.2032 -0.0341 0.0027  0.0374  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1816 0.1777 0.1872 -0.0075 0.0164  0.0018  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1758 0.1613 0.2049 -0.0326 0.0074  0.0434  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1873 0.1852 0.1945 -0.0043 0.0126  0.0004  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1832 0.1633 0.2108 -0.0313 0.0086  0.0384  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1923 0.1901 0.2046 -0.0035 0.0130  0.0020  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1949 0.1625 0.2027 -0.0221 0.0060  0.0410  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1960 0.1932 0.2109 -0.0022 0.0126  0.0013  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1992 0.1640 0.2301 -0.0044 -0.0028 0.0442  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1958 0.1941 0.2186 -0.0011 0.0113  0.0015  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1320 0.1602 0.2107 -0.0261 0.0029  0.0332  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1781 0.1755 0.1752 -0.0051 0.0197  0.0038  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1294 0.1789 0.2055 -0.0264 0.0059  0.0470  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1805 0.1760 0.1731 -0.0018 0.0136  0.0103  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1374 0.1715 0.2049 -0.0362 0.0136  0.0498  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1859 0.1751 0.1758 -0.0006 0.0076  0.0080  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1468 0.1769 0.2193 -0.0235 0.0118  0.0431  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1858 0.1756 0.1832 -0.0001 0.0062  0.0074  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1412 0.1801 0.2214 -0.0221 0.0081  0.0540  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1816 0.1755 0.1748 0.0004  0.0112  0.0147  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1483 0.1871 0.2411 -0.0143 0.0198  0.0596  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1819 0.1745 0.1816 0.0031  0.0060  0.0143  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1679 0.1941 0.2639 -0.0096 0.0268  0.0685  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1833 0.1733 0.1824 0.0059  -0.0026 0.0149  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1471 0.1975 0.2498 -0.0075 0.0207  0.0477  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1815 0.1748 0.1845 0.0036  0.0122  0.0147  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1335 0.1634 0.2052 -0.0299 0.0066  0.0343  13  THR   A N   
296  N N   B THR   A 13  ? 0.1907 0.1763 0.1739 -0.0018 0.0038  0.0080  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1419 0.1591 0.2167 -0.0235 0.0068  0.0357  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1925 0.1773 0.1701 -0.0014 0.0028  0.0083  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1468 0.1564 0.2244 -0.0297 0.0077  0.0345  13  THR   A C   
300  C C   B THR   A 13  ? 0.1971 0.1792 0.1770 -0.0041 0.0042  0.0117  13  THR   A C   
301  O O   A THR   A 13  ? 0.1457 0.1571 0.2334 -0.0182 0.0127  0.0325  13  THR   A O   
302  O O   B THR   A 13  ? 0.1987 0.1804 0.1800 -0.0043 0.0069  0.0133  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1448 0.1689 0.2320 -0.0187 0.0111  0.0439  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1915 0.1784 0.1658 0.0019  -0.0001 0.0091  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1456 0.1737 0.2613 -0.0247 0.0166  0.0432  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1931 0.1752 0.1606 0.0069  -0.0082 0.0129  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1557 0.1821 0.2464 -0.0109 0.0174  0.0301  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1904 0.1790 0.1691 0.0003  0.0029  0.0069  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1545 0.1552 0.2291 -0.0278 0.0036  0.0396  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1999 0.1793 0.1867 -0.0048 0.0018  0.0159  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1583 0.1618 0.2432 -0.0220 0.0020  0.0393  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.2006 0.1799 0.2036 -0.0047 0.0005  0.0209  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1597 0.1554 0.2271 -0.0197 -0.0029 0.0399  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1941 0.1774 0.1855 -0.0057 -0.0022 0.0271  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1787 0.1666 0.2379 -0.0378 -0.0087 0.0470  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1991 0.1753 0.1839 -0.0068 -0.0029 0.0277  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1860 0.1839 0.2908 -0.0219 0.0011  0.0539  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.2095 0.1809 0.2395 -0.0074 0.0007  0.0215  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.2104 0.2334 0.3701 -0.0267 0.0014  0.0512  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.2173 0.1841 0.2707 -0.0092 0.0088  0.0199  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.2254 0.2463 0.3931 -0.0050 -0.0119 0.0594  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.2215 0.1852 0.2877 -0.0084 0.0100  0.0190  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2292 0.2723 0.4187 -0.0208 -0.0004 0.0374  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.2196 0.1839 0.2832 -0.0145 0.0134  0.0194  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1431 0.1464 0.2284 -0.0224 0.0037  0.0451  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1822 0.1752 0.1750 -0.0043 0.0006  0.0309  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1369 0.1508 0.2490 -0.0238 -0.0059 0.0328  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1726 0.1723 0.1685 -0.0031 0.0035  0.0287  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1341 0.1553 0.2717 -0.0261 0.0062  0.0368  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1697 0.1677 0.1699 0.0017  0.0130  0.0254  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1362 0.1611 0.3030 -0.0249 -0.0109 0.0396  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1679 0.1647 0.1799 0.0082  0.0232  0.0286  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1402 0.1498 0.2379 -0.0194 -0.0101 0.0308  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1688 0.1761 0.1666 -0.0049 -0.0001 0.0305  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1460 0.1589 0.2388 -0.0100 -0.0046 0.0271  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1647 0.1797 0.1618 -0.0071 -0.0015 0.0318  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1532 0.1720 0.2581 -0.0216 -0.0077 0.0290  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1608 0.1841 0.1624 -0.0120 -0.0018 0.0354  15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1519 0.1749 0.2228 -0.0168 0.0030  0.0245  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1653 0.1816 0.1574 -0.0089 0.0030  0.0304  15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1363 0.1500 0.2671 -0.0211 -0.0042 0.0479  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1685 0.1662 0.1668 0.0001  0.0060  0.0206  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1358 0.1526 0.2557 -0.0195 0.0029  0.0514  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1669 0.1665 0.1699 -0.0007 0.0031  0.0126  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1315 0.1508 0.2461 -0.0214 0.0001  0.0503  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1688 0.1677 0.1694 -0.0028 0.0032  0.0125  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1248 0.1402 0.2588 -0.0202 0.0077  0.0374  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1682 0.1630 0.1711 -0.0021 0.0076  0.0114  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1504 0.1625 0.2554 -0.0026 0.0209  0.0577  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1654 0.1669 0.1773 0.0019  0.0019  0.0062  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1601 0.1720 0.2591 0.0027  0.0291  0.0538  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1657 0.1689 0.1829 0.0027  -0.0021 0.0020  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1631 0.1791 0.2711 0.0038  0.0423  0.0625  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1632 0.1664 0.1837 -0.0001 0.0044  -0.0005 16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1298 0.1478 0.2367 -0.0137 0.0157  0.0478  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1704 0.1715 0.1652 -0.0026 0.0007  0.0123  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1356 0.1534 0.2252 -0.0199 0.0148  0.0499  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1714 0.1770 0.1653 -0.0058 -0.0038 0.0122  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1354 0.1480 0.2442 -0.0178 0.0103  0.0458  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1724 0.1770 0.1615 -0.0099 -0.0090 0.0084  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1288 0.1523 0.2504 -0.0125 0.0201  0.0546  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1738 0.1780 0.1615 -0.0114 -0.0125 0.0132  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1583 0.1578 0.2318 -0.0226 0.0013  0.0471  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1743 0.1838 0.1771 -0.0028 -0.0046 0.0136  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1724 0.1644 0.2296 -0.0286 -0.0132 0.0337  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1776 0.1912 0.1905 -0.0011 -0.0040 0.0133  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1823 0.1725 0.2426 -0.0179 -0.0185 0.0354  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1805 0.1945 0.1988 0.0006  -0.0061 0.0126  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1903 0.1716 0.2205 -0.0333 -0.0069 0.0371  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1800 0.1961 0.1981 0.0008  -0.0008 0.0147  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1892 0.1714 0.2391 -0.0262 -0.0274 0.0379  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.1845 0.2001 0.2046 0.0004  -0.0036 0.0136  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.2011 0.1715 0.2203 -0.0357 -0.0148 0.0255  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.1814 0.1998 0.2044 0.0022  0.0002  0.0146  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.2012 0.1692 0.2284 -0.0304 -0.0289 0.0392  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.1846 0.2031 0.2087 0.0016  -0.0040 0.0141  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.2126 0.1697 0.2373 -0.0328 -0.0244 0.0382  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.1889 0.2077 0.2184 0.0033  -0.0087 0.0173  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1340 0.1539 0.2434 -0.0155 0.0202  0.0597  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1696 0.1789 0.1602 -0.0121 -0.0065 0.0029  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1413 0.1570 0.2560 -0.0130 0.0220  0.0493  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1664 0.1812 0.1603 -0.0119 -0.0043 -0.0050 18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1416 0.1669 0.2632 -0.0154 0.0143  0.0483  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1709 0.1884 0.1573 -0.0084 -0.0113 -0.0117 18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1397 0.1808 0.2737 -0.0225 0.0306  0.0619  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1733 0.1892 0.1526 -0.0087 -0.0071 -0.0140 18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1593 0.1632 0.2489 -0.0024 0.0135  0.0672  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1579 0.1785 0.1584 -0.0150 0.0055  -0.0004 18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1712 0.1756 0.2464 -0.0009 -0.0012 0.0693  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1524 0.1815 0.1559 -0.0221 0.0174  0.0055  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1640 0.1664 0.2642 -0.0145 0.0156  0.0591  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1561 0.1779 0.1632 -0.0149 0.0022  0.0000  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1922 0.1904 0.2641 0.0016  -0.0062 0.0691  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1494 0.1839 0.1538 -0.0229 0.0279  0.0046  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1472 0.1589 0.2781 -0.0082 0.0385  0.0507  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1762 0.1954 0.1702 -0.0039 -0.0101 -0.0149 19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1614 0.1723 0.2985 -0.0045 0.0437  0.0541  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1843 0.2050 0.1928 -0.0018 -0.0060 -0.0164 19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1513 0.1659 0.3228 0.0013  0.0401  0.0571  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1845 0.2084 0.1994 0.0024  -0.0030 -0.0155 19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1477 0.1645 0.3366 0.0103  0.0325  0.0602  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1849 0.2097 0.1984 0.0012  -0.0029 -0.0141 19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1795 0.1965 0.2983 -0.0069 0.0615  0.0402  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1911 0.2118 0.2086 -0.0035 -0.0006 -0.0175 19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.2218 0.2162 0.3006 -0.0033 0.0606  0.0228  19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.2025 0.2178 0.2251 -0.0030 0.0060  -0.0154 19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.2543 0.2323 0.2987 -0.0008 0.0654  0.0221  19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.2121 0.2232 0.2373 -0.0025 0.0114  -0.0111 19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.2753 0.2356 0.2993 -0.0059 0.0642  0.0154  19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.2175 0.2255 0.2441 -0.0024 0.0135  -0.0090 19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.2863 0.2395 0.2970 -0.0171 0.0755  -0.0000 19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.2191 0.2257 0.2478 -0.0014 0.0142  -0.0107 19  LYS   A NZ  
531  N N   A ASN   A 20  ? 0.1575 0.1659 0.3388 -0.0004 0.0423  0.0577  20  ASN   A N   
532  N N   B ASN   A 20  ? 0.1858 0.2107 0.2091 0.0088  0.0031  -0.0165 20  ASN   A N   
533  C CA  A ASN   A 20  ? 0.1804 0.1862 0.3496 0.0206  0.0548  0.0436  20  ASN   A CA  
534  C CA  B ASN   A 20  ? 0.1874 0.2140 0.2218 0.0172  0.0116  -0.0150 20  ASN   A CA  
535  C C   A ASN   A 20  ? 0.1996 0.1828 0.3466 0.0187  0.0689  0.0382  20  ASN   A C   
536  C C   B ASN   A 20  ? 0.1928 0.2152 0.2245 0.0195  0.0192  -0.0066 20  ASN   A C   
537  O O   A ASN   A 20  ? 0.2175 0.1976 0.3597 0.0107  0.0652  0.0239  20  ASN   A O   
538  O O   B ASN   A 20  ? 0.1915 0.2165 0.2260 0.0245  0.0254  -0.0006 20  ASN   A O   
539  C CB  A ASN   A 20  ? 0.1868 0.1962 0.3632 0.0286  0.0582  0.0542  20  ASN   A CB  
540  C CB  B ASN   A 20  ? 0.1839 0.2139 0.2320 0.0213  0.0120  -0.0193 20  ASN   A CB  
541  C CG  A ASN   A 20  ? 0.2027 0.2078 0.3945 0.0395  0.0664  0.0547  20  ASN   A CG  
542  C CG  B ASN   A 20  ? 0.1822 0.2131 0.2426 0.0251  0.0143  -0.0277 20  ASN   A CG  
543  O OD1 A ASN   A 20  ? 0.2325 0.2178 0.4347 0.0528  0.0857  0.0491  20  ASN   A OD1 
544  O OD1 B ASN   A 20  ? 0.1807 0.2100 0.2452 0.0283  0.0219  -0.0395 20  ASN   A OD1 
545  N ND2 A ASN   A 20  ? 0.2086 0.2014 0.3963 0.0350  0.0498  0.0634  20  ASN   A ND2 
546  N ND2 B ASN   A 20  ? 0.1867 0.2151 0.2511 0.0230  0.0108  -0.0252 20  ASN   A ND2 
559  N N   A ALA   A 21  ? 0.1995 0.1810 0.3436 0.0218  0.0624  0.0255  21  ALA   A N   
560  N N   B ALA   A 21  ? 0.1972 0.2154 0.2287 0.0174  0.0156  -0.0074 21  ALA   A N   
561  C CA  A ALA   A 21  ? 0.1999 0.1844 0.3331 0.0092  0.0658  0.0297  21  ALA   A CA  
562  C CA  B ALA   A 21  ? 0.2017 0.2157 0.2317 0.0137  0.0185  -0.0078 21  ALA   A CA  
563  C C   A ALA   A 21  ? 0.1904 0.1854 0.3216 0.0092  0.0641  0.0183  21  ALA   A C   
564  C C   B ALA   A 21  ? 0.2027 0.2139 0.2258 0.0123  0.0176  -0.0076 21  ALA   A C   
565  O O   A ALA   A 21  ? 0.1919 0.1860 0.3196 0.0069  0.0559  0.0234  21  ALA   A O   
566  O O   B ALA   A 21  ? 0.2012 0.2107 0.2161 0.0103  0.0235  -0.0085 21  ALA   A O   
567  C CB  A ALA   A 21  ? 0.2189 0.1928 0.3385 -0.0006 0.0522  0.0399  21  ALA   A CB  
568  C CB  B ALA   A 21  ? 0.2012 0.2164 0.2374 0.0154  0.0220  -0.0090 21  ALA   A CB  
579  N N   A ASP   A 22  ? 0.1918 0.1823 0.3179 -0.0029 0.0656  0.0296  22  ASP   A N   
580  N N   B ASP   A 22  ? 0.2070 0.2155 0.2284 0.0110  0.0150  -0.0024 22  ASP   A N   
581  C CA  A ASP   A 22  ? 0.1985 0.1858 0.3097 0.0034  0.0540  0.0235  22  ASP   A CA  
582  C CA  B ASP   A 22  ? 0.2117 0.2191 0.2299 0.0112  0.0117  -0.0005 22  ASP   A CA  
583  C C   A ASP   A 22  ? 0.1842 0.1940 0.2602 -0.0046 0.0600  0.0233  22  ASP   A C   
584  C C   B ASP   A 22  ? 0.2098 0.2186 0.2143 0.0045  0.0108  0.0005  22  ASP   A C   
585  O O   A ASP   A 22  ? 0.1871 0.2063 0.2618 -0.0142 0.0599  0.0273  22  ASP   A O   
586  O O   B ASP   A 22  ? 0.2094 0.2157 0.2168 0.0031  0.0125  0.0030  22  ASP   A O   
587  C CB  A ASP   A 22  ? 0.2286 0.1911 0.3648 0.0008  0.0525  0.0204  22  ASP   A CB  
588  C CB  B ASP   A 22  ? 0.2160 0.2206 0.2437 0.0204  0.0125  0.0046  22  ASP   A CB  
589  C CG  A ASP   A 22  ? 0.2530 0.1987 0.4158 -0.0010 0.0399  0.0281  22  ASP   A CG  
590  C CG  B ASP   A 22  ? 0.2207 0.2221 0.2619 0.0274  0.0123  0.0101  22  ASP   A CG  
591  O OD1 A ASP   A 22  ? 0.2544 0.1937 0.4282 -0.0150 0.0385  0.0493  22  ASP   A OD1 
592  O OD1 B ASP   A 22  ? 0.2213 0.2183 0.2657 0.0318  0.0097  0.0130  22  ASP   A OD1 
593  O OD2 A ASP   A 22  ? 0.2820 0.2153 0.4517 0.0101  0.0356  0.0130  22  ASP   A OD2 
594  O OD2 B ASP   A 22  ? 0.2234 0.2285 0.2766 0.0293  0.0132  0.0120  22  ASP   A OD2 
603  N N   A ILE   A 23  ? 0.1850 0.1961 0.2476 0.0004  0.0510  0.0228  23  ILE   A N   
604  N N   B ILE   A 23  ? 0.2093 0.2210 0.2010 0.0025  0.0093  -0.0001 23  ILE   A N   
605  C CA  A ILE   A 23  ? 0.1810 0.1837 0.2355 -0.0057 0.0474  0.0284  23  ILE   A CA  
606  C CA  B ILE   A 23  ? 0.2080 0.2251 0.1960 0.0003  0.0065  0.0011  23  ILE   A CA  
607  C C   A ILE   A 23  ? 0.1772 0.1959 0.2335 -0.0079 0.0614  0.0218  23  ILE   A C   
608  C C   B ILE   A 23  ? 0.2111 0.2315 0.1957 -0.0028 0.0120  -0.0011 23  ILE   A C   
609  O O   A ILE   A 23  ? 0.1846 0.1985 0.2426 -0.0037 0.0590  0.0138  23  ILE   A O   
610  O O   B ILE   A 23  ? 0.2093 0.2281 0.1866 -0.0020 0.0159  -0.0018 23  ILE   A O   
611  C CB  A ILE   A 23  ? 0.1921 0.1867 0.2123 -0.0030 0.0378  0.0233  23  ILE   A CB  
612  C CB  B ILE   A 23  ? 0.2051 0.2207 0.1895 0.0021  0.0013  0.0026  23  ILE   A CB  
613  C CG1 A ILE   A 23  ? 0.1972 0.1873 0.2161 0.0020  0.0264  0.0143  23  ILE   A CG1 
614  C CG1 B ILE   A 23  ? 0.2043 0.2199 0.1866 0.0014  -0.0050 0.0017  23  ILE   A CG1 
615  C CG2 A ILE   A 23  ? 0.2001 0.1913 0.2090 -0.0057 0.0428  0.0345  23  ILE   A CG2 
616  C CG2 B ILE   A 23  ? 0.2043 0.2185 0.1893 0.0047  0.0010  0.0029  23  ILE   A CG2 
617  C CD1 A ILE   A 23  ? 0.2013 0.1804 0.2138 0.0061  0.0048  0.0058  23  ILE   A CD1 
618  C CD1 B ILE   A 23  ? 0.2034 0.2187 0.1858 0.0009  -0.0087 0.0006  23  ILE   A CD1 
641  N N   A VAL   A 24  ? 0.1890 0.2027 0.2486 -0.0166 0.0537  0.0126  24  VAL   A N   
642  N N   B VAL   A 24  ? 0.2185 0.2412 0.2125 -0.0063 0.0112  -0.0018 24  VAL   A N   
643  C CA  A VAL   A 24  ? 0.2075 0.2082 0.2714 -0.0252 0.0551  0.0068  24  VAL   A CA  
644  C CA  B VAL   A 24  ? 0.2280 0.2503 0.2308 -0.0065 0.0089  0.0011  24  VAL   A CA  
645  C C   A VAL   A 24  ? 0.2175 0.2236 0.2775 -0.0338 0.0612  -0.0006 24  VAL   A C   
646  C C   B VAL   A 24  ? 0.2374 0.2613 0.2429 -0.0078 0.0127  -0.0017 24  VAL   A C   
647  O O   A VAL   A 24  ? 0.2271 0.2214 0.2827 -0.0170 0.0600  -0.0130 24  VAL   A O   
648  O O   B VAL   A 24  ? 0.2363 0.2619 0.2447 -0.0058 0.0145  -0.0024 24  VAL   A O   
649  C CB  A VAL   A 24  ? 0.2180 0.2160 0.2940 -0.0254 0.0559  0.0190  24  VAL   A CB  
650  C CB  B VAL   A 24  ? 0.2285 0.2500 0.2369 -0.0047 0.0037  0.0073  24  VAL   A CB  
651  C CG1 A VAL   A 24  ? 0.2349 0.2251 0.3043 -0.0225 0.0530  0.0125  24  VAL   A CG1 
652  C CG1 B VAL   A 24  ? 0.2293 0.2494 0.2414 -0.0034 -0.0016 0.0088  24  VAL   A CG1 
653  C CG2 A VAL   A 24  ? 0.2330 0.2304 0.3140 -0.0151 0.0673  0.0329  24  VAL   A CG2 
654  C CG2 B VAL   A 24  ? 0.2295 0.2505 0.2395 -0.0021 0.0065  0.0112  24  VAL   A CG2 
673  N N   A GLU   A 25  ? 0.2239 0.2543 0.2802 -0.0410 0.0798  -0.0076 25  GLU   A N   
674  N N   B GLU   A 25  ? 0.2474 0.2709 0.2559 -0.0095 0.0184  -0.0041 25  GLU   A N   
675  C CA  A GLU   A 25  ? 0.2472 0.2920 0.2864 -0.0345 0.0931  -0.0184 25  GLU   A CA  
676  C CA  B GLU   A 25  ? 0.2591 0.2811 0.2720 -0.0131 0.0219  -0.0049 25  GLU   A CA  
677  C C   A GLU   A 25  ? 0.2358 0.2921 0.2446 -0.0471 0.0966  -0.0155 25  GLU   A C   
678  C C   B GLU   A 25  ? 0.2587 0.2824 0.2557 -0.0173 0.0235  -0.0073 25  GLU   A C   
679  O O   A GLU   A 25  ? 0.2439 0.3032 0.2518 -0.0497 0.0957  -0.0112 25  GLU   A O   
680  O O   B GLU   A 25  ? 0.2603 0.2826 0.2529 -0.0181 0.0236  -0.0077 25  GLU   A O   
681  C CB  A GLU   A 25  ? 0.2782 0.3235 0.3350 -0.0257 0.1048  -0.0165 25  GLU   A CB  
682  C CB  B GLU   A 25  ? 0.2700 0.2885 0.3035 -0.0127 0.0246  -0.0025 25  GLU   A CB  
683  C CG  A GLU   A 25  ? 0.3134 0.3530 0.4067 -0.0221 0.0919  -0.0163 25  GLU   A CG  
684  C CG  B GLU   A 25  ? 0.2811 0.2962 0.3359 -0.0117 0.0239  0.0001  25  GLU   A CG  
685  C CD  A GLU   A 25  ? 0.3431 0.3807 0.4742 -0.0174 0.0770  -0.0151 25  GLU   A CD  
686  C CD  B GLU   A 25  ? 0.2905 0.3025 0.3632 -0.0110 0.0227  0.0017  25  GLU   A CD  
687  O OE1 A GLU   A 25  ? 0.3545 0.3923 0.4931 -0.0110 0.0622  -0.0208 25  GLU   A OE1 
688  O OE1 B GLU   A 25  ? 0.2930 0.3036 0.3713 -0.0093 0.0201  0.0037  25  GLU   A OE1 
689  O OE2 A GLU   A 25  ? 0.3531 0.3911 0.5081 -0.0190 0.0741  -0.0221 25  GLU   A OE2 
690  O OE2 B GLU   A 25  ? 0.2947 0.3043 0.3744 -0.0131 0.0243  0.0007  25  GLU   A OE2 
703  N N   A GLU   A 26  ? 0.2196 0.2792 0.2444 -0.0634 0.0988  -0.0182 26  GLU   A N   
704  N N   B GLU   A 26  ? 0.2578 0.2830 0.2469 -0.0212 0.0257  -0.0113 26  GLU   A N   
705  C CA  A GLU   A 26  ? 0.2333 0.2721 0.2349 -0.0764 0.0909  -0.0065 26  GLU   A CA  
706  C CA  B GLU   A 26  ? 0.2589 0.2841 0.2394 -0.0240 0.0265  -0.0148 26  GLU   A CA  
707  C C   A GLU   A 26  ? 0.2289 0.2577 0.2091 -0.0725 0.0777  -0.0097 26  GLU   A C   
708  C C   B GLU   A 26  ? 0.2623 0.2820 0.2254 -0.0235 0.0316  -0.0189 26  GLU   A C   
709  O O   A GLU   A 26  ? 0.2373 0.2557 0.2107 -0.0808 0.0716  -0.0035 26  GLU   A O   
710  O O   B GLU   A 26  ? 0.2625 0.2808 0.2245 -0.0203 0.0335  -0.0206 26  GLU   A O   
711  C CB  A GLU   A 26  ? 0.2648 0.2745 0.2711 -0.0856 0.0737  -0.0000 26  GLU   A CB  
712  C CB  B GLU   A 26  ? 0.2583 0.2879 0.2459 -0.0278 0.0186  -0.0161 26  GLU   A CB  
713  C CG  A GLU   A 26  ? 0.2924 0.2842 0.3283 -0.0919 0.0770  -0.0060 26  GLU   A CG  
714  C CG  B GLU   A 26  ? 0.2595 0.2894 0.2531 -0.0316 0.0128  -0.0154 26  GLU   A CG  
715  C CD  A GLU   A 26  ? 0.3029 0.2831 0.3555 -0.1054 0.1053  -0.0088 26  GLU   A CD  
716  C CD  B GLU   A 26  ? 0.2590 0.2890 0.2548 -0.0371 0.0098  -0.0154 26  GLU   A CD  
717  O OE1 A GLU   A 26  ? 0.2933 0.3065 0.3562 -0.0913 0.1358  -0.0608 26  GLU   A OE1 
718  O OE1 B GLU   A 26  ? 0.2600 0.2920 0.2556 -0.0383 0.0078  -0.0193 26  GLU   A OE1 
719  O OE2 A GLU   A 26  ? 0.3248 0.2930 0.3769 -0.0964 0.1065  0.0067  26  GLU   A OE2 
720  O OE2 B GLU   A 26  ? 0.2577 0.2883 0.2527 -0.0403 0.0061  -0.0168 26  GLU   A OE2 
733  N N   A ALA   A 27  ? 0.2079 0.2392 0.2002 -0.0690 0.0689  -0.0099 27  ALA   A N   
734  N N   B ALA   A 27  ? 0.2653 0.2813 0.2175 -0.0285 0.0344  -0.0216 27  ALA   A N   
735  C CA  A ALA   A 27  ? 0.2196 0.2463 0.1874 -0.0580 0.0656  -0.0104 27  ALA   A CA  
736  C CA  B ALA   A 27  ? 0.2709 0.2832 0.2104 -0.0342 0.0385  -0.0271 27  ALA   A CA  
737  C C   A ALA   A 27  ? 0.2449 0.2622 0.1988 -0.0613 0.0711  -0.0276 27  ALA   A C   
738  C C   B ALA   A 27  ? 0.2779 0.2863 0.2110 -0.0427 0.0463  -0.0368 27  ALA   A C   
739  O O   A ALA   A 27  ? 0.2546 0.2588 0.2042 -0.0676 0.0507  -0.0274 27  ALA   A O   
740  O O   B ALA   A 27  ? 0.2803 0.2861 0.2083 -0.0431 0.0435  -0.0351 27  ALA   A O   
741  C CB  A ALA   A 27  ? 0.2121 0.2369 0.1971 -0.0537 0.0560  -0.0018 27  ALA   A CB  
742  C CB  B ALA   A 27  ? 0.2699 0.2821 0.2093 -0.0329 0.0371  -0.0246 27  ALA   A CB  
753  N N   . LYS   A 28  ? 0.2848 0.2894 0.2176 -0.0517 0.0543  -0.0487 28  LYS   A N   
754  C CA  . LYS   A 28  ? 0.3328 0.3294 0.2599 -0.0473 0.0599  -0.0714 28  LYS   A CA  
755  C C   . LYS   A 28  ? 0.3576 0.3639 0.2541 -0.0549 0.0758  -0.0564 28  LYS   A C   
756  O O   . LYS   A 28  ? 0.3630 0.3746 0.3003 -0.0560 0.0555  -0.0477 28  LYS   A O   
757  C CB  . LYS   A 28  ? 0.3570 0.3453 0.3177 -0.0339 0.0544  -0.0895 28  LYS   A CB  
758  C CG  . LYS   A 28  ? 0.3752 0.3611 0.3766 -0.0254 0.0492  -0.0959 28  LYS   A CG  
759  C CD  . LYS   A 28  ? 0.3907 0.3824 0.4430 -0.0143 0.0426  -0.1006 28  LYS   A CD  
760  C CE  . LYS   A 28  ? 0.4027 0.3944 0.4920 -0.0099 0.0369  -0.1064 28  LYS   A CE  
761  N NZ  . LYS   A 28  ? 0.4114 0.3997 0.5226 -0.0045 0.0366  -0.1116 28  LYS   A NZ  
776  N N   . LYS   A 29  ? 0.3723 0.3882 0.2377 -0.0649 0.1078  -0.0379 29  LYS   A N   
777  C CA  . LYS   A 29  ? 0.3945 0.4190 0.2626 -0.0712 0.1190  -0.0214 29  LYS   A CA  
778  C C   . LYS   A 29  ? 0.3895 0.4091 0.2273 -0.0833 0.1078  -0.0214 29  LYS   A C   
779  O O   . LYS   A 29  ? 0.3995 0.4181 0.2377 -0.0751 0.0987  -0.0271 29  LYS   A O   
780  C CB  . LYS   A 29  ? 0.4173 0.4556 0.3398 -0.0607 0.1344  -0.0076 29  LYS   A CB  
781  C CG  . LYS   A 29  ? 0.4431 0.4859 0.4313 -0.0491 0.1348  0.0007  29  LYS   A CG  
782  C CD  . LYS   A 29  ? 0.4647 0.5142 0.5194 -0.0390 0.1302  0.0028  29  LYS   A CD  
783  C CE  . LYS   A 29  ? 0.4805 0.5347 0.5783 -0.0330 0.1279  0.0045  29  LYS   A CE  
784  N NZ  . LYS   A 29  ? 0.4882 0.5431 0.6121 -0.0298 0.1272  0.0037  29  LYS   A NZ  
798  N N   . VAL   A 30  ? 0.3696 0.3860 0.2107 -0.1001 0.0995  -0.0174 30  VAL   A N   
799  C CA  . VAL   A 30  ? 0.3625 0.3690 0.2103 -0.1149 0.0706  0.0071  30  VAL   A CA  
800  C C   . VAL   A 30  ? 0.3623 0.3570 0.1573 -0.1155 0.0677  0.0142  30  VAL   A C   
801  O O   . VAL   A 30  ? 0.3674 0.3564 0.1731 -0.1199 0.0571  0.0136  30  VAL   A O   
802  C CB  . VAL   A 30  ? 0.3552 0.3621 0.2416 -0.1291 0.0424  0.0147  30  VAL   A CB  
803  C CG1 . VAL   A 30  ? 0.3586 0.3601 0.2555 -0.1305 0.0214  0.0178  30  VAL   A CG1 
804  C CG2 . VAL   A 30  ? 0.3515 0.3630 0.2675 -0.1344 0.0431  0.0170  30  VAL   A CG2 
814  N N   . LYS   A 31  ? 0.3491 0.3399 0.1406 -0.1126 0.0561  0.0145  31  LYS   A N   
815  C CA  . LYS   A 31  ? 0.3672 0.3441 0.1664 -0.1004 0.0269  0.0079  31  LYS   A CA  
816  C C   . LYS   A 31  ? 0.3268 0.3085 0.1074 -0.0694 0.0142  0.0381  31  LYS   A C   
817  O O   . LYS   A 31  ? 0.3375 0.3203 0.1282 -0.0684 -0.0130 0.0470  31  LYS   A O   
818  C CB  . LYS   A 31  ? 0.4155 0.3854 0.2866 -0.0883 0.0106  -0.0119 31  LYS   A CB  
819  C CG  . LYS   A 31  ? 0.4694 0.4355 0.4324 -0.0782 -0.0069 -0.0236 31  LYS   A CG  
820  C CD  . LYS   A 31  ? 0.5099 0.4713 0.5459 -0.0676 -0.0231 -0.0340 31  LYS   A CD  
821  C CE  . LYS   A 31  ? 0.5406 0.4974 0.6169 -0.0602 -0.0362 -0.0438 31  LYS   A CE  
822  N NZ  . LYS   A 31  ? 0.5578 0.5151 0.6526 -0.0587 -0.0438 -0.0504 31  LYS   A NZ  
836  N N   . PRO   A 32  ? 0.2839 0.2740 0.0927 -0.0617 0.0179  0.0259  32  PRO   A N   
837  C CA  . PRO   A 32  ? 0.2791 0.2558 0.1495 -0.0593 0.0065  0.0353  32  PRO   A CA  
838  C C   . PRO   A 32  ? 0.2719 0.2465 0.1619 -0.0531 -0.0021 0.0439  32  PRO   A C   
839  O O   . PRO   A 32  ? 0.2680 0.2385 0.1707 -0.0547 -0.0111 0.0476  32  PRO   A O   
840  C CB  . PRO   A 32  ? 0.2673 0.2599 0.1542 -0.0569 0.0006  0.0316  32  PRO   A CB  
841  C CG  . PRO   A 32  ? 0.2658 0.2678 0.0857 -0.0606 -0.0127 0.0236  32  PRO   A CG  
842  C CD  . PRO   A 32  ? 0.2712 0.2706 0.0877 -0.0654 0.0046  0.0220  32  PRO   A CD  
850  N N   . THR   A 33  ? 0.2760 0.2415 0.1592 -0.0537 -0.0069 0.0503  33  THR   A N   
851  C CA  . THR   A 33  ? 0.2742 0.2470 0.1694 -0.0366 -0.0253 0.0436  33  THR   A CA  
852  C C   . THR   A 33  ? 0.2384 0.2303 0.1603 -0.0413 -0.0213 0.0319  33  THR   A C   
853  O O   . THR   A 33  ? 0.2259 0.2307 0.1664 -0.0423 -0.0349 0.0393  33  THR   A O   
854  C CB  . THR   A 33  ? 0.3030 0.2648 0.1841 -0.0261 -0.0399 0.0645  33  THR   A CB  
855  O OG1 . THR   A 33  ? 0.3265 0.2731 0.2255 -0.0174 -0.0298 0.0844  33  THR   A OG1 
856  C CG2 . THR   A 33  ? 0.3073 0.2749 0.2047 -0.0152 -0.0513 0.0561  33  THR   A CG2 
864  N N   . VAL   A 34  ? 0.2076 0.2085 0.1421 -0.0408 -0.0148 0.0390  34  VAL   A N   
865  C CA  . VAL   A 34  ? 0.1925 0.1890 0.1400 -0.0340 -0.0086 0.0366  34  VAL   A CA  
866  C C   . VAL   A 34  ? 0.1815 0.1790 0.1345 -0.0298 -0.0013 0.0199  34  VAL   A C   
867  O O   . VAL   A 34  ? 0.1821 0.1787 0.1667 -0.0352 -0.0007 0.0278  34  VAL   A O   
868  C CB  . VAL   A 34  ? 0.1914 0.1871 0.1642 -0.0301 -0.0022 0.0175  34  VAL   A CB  
869  C CG1 . VAL   A 34  ? 0.1986 0.1946 0.1741 -0.0191 0.0095  0.0029  34  VAL   A CG1 
870  C CG2 . VAL   A 34  ? 0.1970 0.2010 0.1906 -0.0174 -0.0167 0.0168  34  VAL   A CG2 
880  N N   . VAL   A 35  ? 0.1689 0.1629 0.1363 -0.0286 -0.0062 0.0129  35  VAL   A N   
881  C CA  . VAL   A 35  ? 0.1578 0.1652 0.1430 -0.0312 0.0001  0.0147  35  VAL   A CA  
882  C C   . VAL   A 35  ? 0.1486 0.1513 0.1432 -0.0192 0.0075  0.0234  35  VAL   A C   
883  O O   . VAL   A 35  ? 0.1434 0.1633 0.1615 -0.0230 0.0096  0.0140  35  VAL   A O   
884  C CB  . VAL   A 35  ? 0.1662 0.1725 0.1575 -0.0193 0.0132  0.0019  35  VAL   A CB  
885  C CG1 . VAL   A 35  ? 0.1821 0.1742 0.1655 -0.0077 0.0079  0.0000  35  VAL   A CG1 
886  C CG2 . VAL   A 35  ? 0.1645 0.1755 0.1836 -0.0194 0.0187  0.0064  35  VAL   A CG2 
896  N N   . VAL   A 36  ? 0.1317 0.1505 0.1405 -0.0211 0.0101  0.0186  36  VAL   A N   
897  C CA  . VAL   A 36  ? 0.1253 0.1394 0.1504 -0.0095 0.0129  0.0103  36  VAL   A CA  
898  C C   . VAL   A 36  ? 0.1262 0.1402 0.1577 -0.0142 0.0127  0.0073  36  VAL   A C   
899  O O   . VAL   A 36  ? 0.1353 0.1371 0.1760 -0.0045 0.0175  0.0129  36  VAL   A O   
900  C CB  . VAL   A 36  ? 0.1349 0.1261 0.1516 -0.0145 -0.0006 0.0111  36  VAL   A CB  
901  C CG1 . VAL   A 36  ? 0.1458 0.1303 0.1588 -0.0173 -0.0019 0.0025  36  VAL   A CG1 
902  C CG2 . VAL   A 36  ? 0.1472 0.1323 0.1749 -0.0123 -0.0057 0.0230  36  VAL   A CG2 
912  N N   . ASN   A 37  ? 0.1227 0.1312 0.1434 -0.0058 0.0066  0.0141  37  ASN   A N   
913  C CA  . ASN   A 37  ? 0.1259 0.1300 0.1356 0.0017  0.0077  0.0149  37  ASN   A CA  
914  C C   . ASN   A 37  ? 0.1240 0.1241 0.1362 -0.0027 0.0153  0.0210  37  ASN   A C   
915  O O   . ASN   A 37  ? 0.1374 0.1340 0.1487 0.0086  0.0116  0.0091  37  ASN   A O   
916  C CB  . ASN   A 37  ? 0.1304 0.1208 0.1492 -0.0012 0.0031  0.0155  37  ASN   A CB  
917  C CG  . ASN   A 37  ? 0.1304 0.1269 0.1685 -0.0031 0.0056  0.0086  37  ASN   A CG  
918  O OD1 . ASN   A 37  ? 0.1303 0.1303 0.1867 0.0010  0.0101  0.0152  37  ASN   A OD1 
919  N ND2 . ASN   A 37  ? 0.1328 0.1282 0.1745 -0.0062 -0.0063 0.0214  37  ASN   A ND2 
926  N N   A ALA   A 38  ? 0.1225 0.1435 0.1476 0.0029  0.0164  0.0075  38  ALA   A N   
927  N N   B ALA   A 38  ? 0.1284 0.1372 0.1360 -0.0018 0.0059  0.0150  38  ALA   A N   
928  C CA  A ALA   A 38  ? 0.1317 0.1469 0.1555 -0.0040 0.0006  -0.0043 38  ALA   A CA  
929  C CA  B ALA   A 38  ? 0.1343 0.1463 0.1417 -0.0039 -0.0055 0.0082  38  ALA   A CA  
930  C C   A ALA   A 38  ? 0.1282 0.1427 0.1504 0.0020  -0.0037 -0.0017 38  ALA   A C   
931  C C   B ALA   A 38  ? 0.1363 0.1446 0.1365 -0.0028 -0.0135 0.0105  38  ALA   A C   
932  O O   A ALA   A 38  ? 0.1337 0.1341 0.1706 0.0097  -0.0044 0.0078  38  ALA   A O   
933  O O   B ALA   A 38  ? 0.1335 0.1444 0.1375 -0.0051 -0.0218 0.0113  38  ALA   A O   
934  C CB  A ALA   A 38  ? 0.1419 0.1752 0.1778 -0.0161 -0.0093 0.0011  38  ALA   A CB  
935  C CB  B ALA   A 38  ? 0.1373 0.1558 0.1528 -0.0035 -0.0095 0.0004  38  ALA   A CB  
946  N N   A ALA   A 39  ? 0.1227 0.1299 0.1567 0.0008  0.0021  0.0143  39  ALA   A N   
947  N N   B ALA   A 39  ? 0.1409 0.1398 0.1365 -0.0006 -0.0109 0.0169  39  ALA   A N   
948  C CA  A ALA   A 39  ? 0.1245 0.1255 0.1517 0.0036  0.0043  0.0072  39  ALA   A CA  
949  C CA  B ALA   A 39  ? 0.1466 0.1392 0.1420 -0.0023 -0.0154 0.0117  39  ALA   A CA  
950  C C   A ALA   A 39  ? 0.1323 0.1224 0.1453 -0.0033 0.0086  0.0019  39  ALA   A C   
951  C C   B ALA   A 39  ? 0.1485 0.1376 0.1474 -0.0008 -0.0104 0.0074  39  ALA   A C   
952  O O   A ALA   A 39  ? 0.1514 0.1278 0.1495 -0.0064 0.0057  0.0051  39  ALA   A O   
953  O O   B ALA   A 39  ? 0.1502 0.1387 0.1507 -0.0026 -0.0079 0.0075  39  ALA   A O   
954  C CB  A ALA   A 39  ? 0.1268 0.1382 0.1713 0.0025  -0.0008 0.0027  39  ALA   A CB  
955  C CB  B ALA   A 39  ? 0.1514 0.1406 0.1415 -0.0023 -0.0198 0.0109  39  ALA   A CB  
966  N N   A ASN   A 40  ? 0.1495 0.1318 0.1400 -0.0091 0.0213  0.0023  40  ASN   A N   
967  N N   B ASN   A 40  ? 0.1533 0.1367 0.1492 0.0022  -0.0085 0.0071  40  ASN   A N   
968  C CA  A ASN   A 40  ? 0.1517 0.1307 0.1411 -0.0040 0.0050  0.0004  40  ASN   A CA  
969  C CA  B ASN   A 40  ? 0.1543 0.1356 0.1531 0.0068  -0.0125 0.0106  40  ASN   A CA  
970  C C   A ASN   A 40  ? 0.1492 0.1192 0.1296 -0.0066 0.0187  0.0108  40  ASN   A C   
971  C C   B ASN   A 40  ? 0.1547 0.1367 0.1539 0.0034  -0.0071 0.0146  40  ASN   A C   
972  O O   A ASN   A 40  ? 0.1436 0.1263 0.1449 -0.0085 0.0190  0.0127  40  ASN   A O   
973  O O   B ASN   A 40  ? 0.1520 0.1374 0.1553 0.0012  -0.0120 0.0195  40  ASN   A O   
974  C CB  A ASN   A 40  ? 0.1657 0.1379 0.1585 -0.0015 -0.0066 0.0058  40  ASN   A CB  
975  C CB  B ASN   A 40  ? 0.1567 0.1337 0.1556 0.0127  -0.0154 0.0105  40  ASN   A CB  
976  C CG  A ASN   A 40  ? 0.1750 0.1430 0.2008 -0.0012 -0.0088 0.0099  40  ASN   A CG  
977  C CG  B ASN   A 40  ? 0.1589 0.1324 0.1585 0.0178  -0.0211 0.0112  40  ASN   A CG  
978  O OD1 A ASN   A 40  ? 0.1764 0.1465 0.2343 -0.0037 -0.0103 0.0041  40  ASN   A OD1 
979  O OD1 B ASN   A 40  ? 0.1605 0.1318 0.1730 0.0193  -0.0252 0.0090  40  ASN   A OD1 
980  N ND2 A ASN   A 40  ? 0.1770 0.1571 0.2174 0.0009  0.0018  0.0008  40  ASN   A ND2 
981  N ND2 B ASN   A 40  ? 0.1597 0.1347 0.1567 0.0205  -0.0179 0.0084  40  ASN   A ND2 
994  N N   A VAL   A 41  ? 0.1596 0.1250 0.1325 -0.0038 0.0219  0.0158  41  VAL   A N   
995  N N   B VAL   A 41  ? 0.1615 0.1413 0.1537 0.0009  -0.0021 0.0186  41  VAL   A N   
996  C CA  A VAL   A 41  ? 0.1673 0.1344 0.1555 -0.0059 0.0275  0.0077  41  VAL   A CA  
997  C CA  B VAL   A 41  ? 0.1663 0.1448 0.1487 -0.0020 0.0061  0.0207  41  VAL   A CA  
998  C C   A VAL   A 41  ? 0.1587 0.1309 0.1659 -0.0055 0.0178  0.0106  41  VAL   A C   
999  C C   B VAL   A 41  ? 0.1654 0.1468 0.1467 -0.0050 0.0100  0.0216  41  VAL   A C   
1000 O O   A VAL   A 41  ? 0.1606 0.1258 0.1893 -0.0009 0.0210  -0.0009 41  VAL   A O   
1001 O O   B VAL   A 41  ? 0.1627 0.1427 0.1461 -0.0069 0.0103  0.0205  41  VAL   A O   
1002 C CB  A VAL   A 41  ? 0.1802 0.1450 0.1603 -0.0149 0.0416  0.0025  41  VAL   A CB  
1003 C CB  B VAL   A 41  ? 0.1728 0.1476 0.1515 -0.0041 0.0131  0.0196  41  VAL   A CB  
1004 C CG1 A VAL   A 41  ? 0.1869 0.1573 0.1764 -0.0081 0.0399  -0.0060 41  VAL   A CG1 
1005 C CG1 B VAL   A 41  ? 0.1786 0.1510 0.1578 -0.0032 0.0197  0.0128  41  VAL   A CG1 
1006 C CG2 A VAL   A 41  ? 0.2085 0.1617 0.1640 -0.0265 0.0411  0.0028  41  VAL   A CG2 
1007 C CG2 B VAL   A 41  ? 0.1771 0.1480 0.1516 -0.0085 0.0150  0.0204  41  VAL   A CG2 
1026 N N   A TYR   A 42  ? 0.1392 0.1236 0.1838 0.0015  0.0267  0.0218  42  TYR   A N   
1027 N N   B TYR   A 42  ? 0.1652 0.1515 0.1547 -0.0038 0.0138  0.0238  42  TYR   A N   
1028 C CA  A TYR   A 42  ? 0.1488 0.1184 0.1855 -0.0081 0.0245  0.0236  42  TYR   A CA  
1029 C CA  B TYR   A 42  ? 0.1671 0.1556 0.1560 -0.0034 0.0139  0.0197  42  TYR   A CA  
1030 C C   A TYR   A 42  ? 0.1383 0.1213 0.1835 -0.0034 0.0212  0.0165  42  TYR   A C   
1031 C C   B TYR   A 42  ? 0.1677 0.1582 0.1442 -0.0028 0.0167  0.0246  42  TYR   A C   
1032 O O   A TYR   A 42  ? 0.1376 0.1230 0.2068 -0.0145 0.0144  -0.0004 42  TYR   A O   
1033 O O   B TYR   A 42  ? 0.1683 0.1588 0.1440 -0.0037 0.0204  0.0285  42  TYR   A O   
1034 C CB  A TYR   A 42  ? 0.1785 0.1377 0.1883 -0.0046 0.0334  0.0312  42  TYR   A CB  
1035 C CB  B TYR   A 42  ? 0.1697 0.1600 0.1686 -0.0024 0.0167  0.0109  42  TYR   A CB  
1036 C CG  A TYR   A 42  ? 0.1994 0.1544 0.1899 0.0005  0.0254  0.0389  42  TYR   A CG  
1037 C CG  B TYR   A 42  ? 0.1724 0.1652 0.1772 -0.0011 0.0174  0.0044  42  TYR   A CG  
1038 C CD1 A TYR   A 42  ? 0.2054 0.1614 0.2016 -0.0141 0.0324  0.0438  42  TYR   A CD1 
1039 C CD1 B TYR   A 42  ? 0.1764 0.1688 0.1858 -0.0015 0.0177  -0.0039 42  TYR   A CD1 
1040 C CD2 A TYR   A 42  ? 0.2162 0.1840 0.1897 0.0002  0.0295  0.0282  42  TYR   A CD2 
1041 C CD2 B TYR   A 42  ? 0.1720 0.1692 0.1801 0.0003  0.0178  0.0020  42  TYR   A CD2 
1042 C CE1 A TYR   A 42  ? 0.2175 0.1800 0.1937 -0.0169 0.0357  0.0344  42  TYR   A CE1 
1043 C CE1 B TYR   A 42  ? 0.1787 0.1723 0.1902 -0.0017 0.0176  -0.0082 42  TYR   A CE1 
1044 C CE2 A TYR   A 42  ? 0.2281 0.2012 0.1996 -0.0131 0.0301  0.0230  42  TYR   A CE2 
1045 C CE2 B TYR   A 42  ? 0.1721 0.1710 0.1865 -0.0010 0.0187  -0.0019 42  TYR   A CE2 
1046 C CZ  A TYR   A 42  ? 0.2329 0.2012 0.1881 -0.0197 0.0447  0.0288  42  TYR   A CZ  
1047 C CZ  B TYR   A 42  ? 0.1774 0.1746 0.1871 -0.0015 0.0194  -0.0073 42  TYR   A CZ  
1048 O OH  A TYR   A 42  ? 0.2467 0.2252 0.2174 -0.0292 0.0374  0.0148  42  TYR   A OH  
1049 O OH  B TYR   A 42  ? 0.1825 0.1798 0.1918 -0.0004 0.0189  -0.0106 42  TYR   A OH  
1068 N N   A LEU   A 43  ? 0.1378 0.1205 0.1638 -0.0122 0.0083  0.0072  43  LEU   A N   
1069 N N   B LEU   A 43  ? 0.1692 0.1609 0.1457 -0.0041 0.0155  0.0214  43  LEU   A N   
1070 C CA  A LEU   A 43  ? 0.1292 0.1200 0.1721 -0.0082 0.0096  -0.0004 43  LEU   A CA  
1071 C CA  B LEU   A 43  ? 0.1715 0.1642 0.1497 -0.0049 0.0110  0.0154  43  LEU   A CA  
1072 C C   A LEU   A 43  ? 0.1250 0.1194 0.1753 -0.0060 0.0016  0.0019  43  LEU   A C   
1073 C C   B LEU   A 43  ? 0.1769 0.1715 0.1577 -0.0054 0.0072  0.0087  43  LEU   A C   
1074 O O   A LEU   A 43  ? 0.1455 0.1246 0.1939 0.0041  -0.0065 -0.0013 43  LEU   A O   
1075 O O   B LEU   A 43  ? 0.1794 0.1731 0.1561 -0.0031 0.0069  0.0059  43  LEU   A O   
1076 C CB  A LEU   A 43  ? 0.1369 0.1214 0.1762 -0.0134 0.0143  0.0012  43  LEU   A CB  
1077 C CB  B LEU   A 43  ? 0.1728 0.1601 0.1527 -0.0065 0.0064  0.0174  43  LEU   A CB  
1078 C CG  A LEU   A 43  ? 0.1391 0.1198 0.1839 -0.0034 0.0099  -0.0023 43  LEU   A CG  
1079 C CG  B LEU   A 43  ? 0.1724 0.1560 0.1536 -0.0076 0.0047  0.0171  43  LEU   A CG  
1080 C CD1 A LEU   A 43  ? 0.1556 0.1343 0.2039 -0.0018 -0.0031 0.0111  43  LEU   A CD1 
1081 C CD1 B LEU   A 43  ? 0.1734 0.1566 0.1579 -0.0091 0.0026  0.0160  43  LEU   A CD1 
1082 C CD2 A LEU   A 43  ? 0.1522 0.1263 0.1870 0.0019  0.0062  0.0216  43  LEU   A CD2 
1083 C CD2 B LEU   A 43  ? 0.1746 0.1536 0.1521 -0.0091 0.0030  0.0228  43  LEU   A CD2 
1106 N N   A LYS   A 44  ? 0.1296 0.1229 0.1741 -0.0040 0.0122  0.0051  44  LYS   A N   
1107 N N   B LYS   A 44  ? 0.1822 0.1782 0.1696 -0.0070 0.0040  0.0051  44  LYS   A N   
1108 C CA  A LYS   A 44  ? 0.1466 0.1237 0.1825 -0.0018 0.0159  0.0158  44  LYS   A CA  
1109 C CA  B LYS   A 44  ? 0.1891 0.1840 0.1855 -0.0085 0.0002  0.0038  44  LYS   A CA  
1110 C C   A LYS   A 44  ? 0.1317 0.1253 0.1582 0.0013  0.0062  0.0102  44  LYS   A C   
1111 C C   B LYS   A 44  ? 0.1794 0.1773 0.1666 -0.0062 -0.0024 0.0032  44  LYS   A C   
1112 O O   A LYS   A 44  ? 0.1450 0.1428 0.1809 -0.0015 0.0066  -0.0005 44  LYS   A O   
1113 O O   B LYS   A 44  ? 0.1818 0.1784 0.1659 -0.0064 -0.0035 0.0019  44  LYS   A O   
1114 C CB  A LYS   A 44  ? 0.1729 0.1407 0.2282 -0.0009 0.0275  0.0272  44  LYS   A CB  
1115 C CB  B LYS   A 44  ? 0.2049 0.1970 0.2246 -0.0116 0.0001  0.0028  44  LYS   A CB  
1116 C CG  A LYS   A 44  ? 0.2069 0.1804 0.2992 -0.0136 0.0511  0.0318  44  LYS   A CG  
1117 C CG  B LYS   A 44  ? 0.2201 0.2079 0.2663 -0.0145 0.0029  0.0030  44  LYS   A CG  
1118 C CD  A LYS   A 44  ? 0.2443 0.2466 0.3982 -0.0166 0.0365  0.0280  44  LYS   A CD  
1119 C CD  B LYS   A 44  ? 0.2337 0.2194 0.3084 -0.0159 0.0010  0.0043  44  LYS   A CD  
1120 C CE  A LYS   A 44  ? 0.2601 0.2813 0.4652 -0.0153 0.0215  0.0280  44  LYS   A CE  
1121 C CE  B LYS   A 44  ? 0.2404 0.2255 0.3384 -0.0164 -0.0019 0.0071  44  LYS   A CE  
1122 N NZ  A LYS   A 44  ? 0.2669 0.3049 0.4966 -0.0121 0.0145  0.0264  44  LYS   A NZ  
1123 N NZ  B LYS   A 44  ? 0.2443 0.2284 0.3556 -0.0158 -0.0028 0.0112  44  LYS   A NZ  
1150 N N   A HIS   A 45  ? 0.1255 0.1262 0.1544 0.0019  0.0031  0.0177  45  HIS   A N   
1151 N N   B HIS   A 45  ? 0.1687 0.1702 0.1557 -0.0044 -0.0039 0.0036  45  HIS   A N   
1152 C CA  A HIS   A 45  ? 0.1258 0.1290 0.1590 0.0034  -0.0034 0.0111  45  HIS   A CA  
1153 C CA  B HIS   A 45  ? 0.1586 0.1630 0.1474 -0.0025 -0.0048 0.0041  45  HIS   A CA  
1154 C C   A HIS   A 45  ? 0.1361 0.1429 0.1672 0.0074  0.0036  0.0191  45  HIS   A C   
1155 C C   B HIS   A 45  ? 0.1569 0.1596 0.1481 -0.0026 0.0032  0.0051  45  HIS   A C   
1156 O O   A HIS   A 45  ? 0.1486 0.1510 0.1856 0.0148  0.0073  0.0028  45  HIS   A O   
1157 O O   B HIS   A 45  ? 0.1595 0.1555 0.1535 0.0019  0.0112  0.0045  45  HIS   A O   
1158 C CB  A HIS   A 45  ? 0.1267 0.1290 0.1639 -0.0039 0.0038  -0.0012 45  HIS   A CB  
1159 C CB  B HIS   A 45  ? 0.1491 0.1599 0.1370 -0.0003 -0.0102 0.0035  45  HIS   A CB  
1160 C CG  A HIS   A 45  ? 0.1267 0.1229 0.1619 -0.0084 0.0021  0.0115  45  HIS   A CG  
1161 C CG  B HIS   A 45  ? 0.1389 0.1558 0.1252 0.0003  -0.0054 0.0001  45  HIS   A CG  
1162 N ND1 A HIS   A 45  ? 0.1278 0.1280 0.1751 -0.0015 0.0089  0.0159  45  HIS   A ND1 
1163 N ND1 B HIS   A 45  ? 0.1342 0.1533 0.1276 0.0035  -0.0070 0.0018  45  HIS   A ND1 
1164 C CD2 A HIS   A 45  ? 0.1274 0.1333 0.1671 -0.0119 -0.0052 0.0218  45  HIS   A CD2 
1165 C CD2 B HIS   A 45  ? 0.1315 0.1503 0.1203 0.0024  -0.0001 -0.0058 45  HIS   A CD2 
1166 C CE1 A HIS   A 45  ? 0.1282 0.1299 0.1631 -0.0052 0.0078  0.0200  45  HIS   A CE1 
1167 C CE1 B HIS   A 45  ? 0.1310 0.1459 0.1212 0.0019  -0.0061 -0.0045 45  HIS   A CE1 
1168 N NE2 A HIS   A 45  ? 0.1262 0.1382 0.1662 -0.0081 0.0020  0.0311  45  HIS   A NE2 
1169 N NE2 B HIS   A 45  ? 0.1304 0.1462 0.1193 0.0006  -0.0042 -0.0089 45  HIS   A NE2 
1184 N N   A GLY   A 46  ? 0.1485 0.1662 0.1950 0.0213  -0.0113 0.0185  46  GLY   A N   
1185 N N   B GLY   A 46  ? 0.1538 0.1590 0.1490 -0.0067 0.0055  0.0055  46  GLY   A N   
1186 C CA  A GLY   A 46  ? 0.1562 0.1676 0.2091 0.0209  -0.0098 0.0330  46  GLY   A CA  
1187 C CA  B GLY   A 46  ? 0.1472 0.1576 0.1429 -0.0095 0.0119  0.0064  46  GLY   A CA  
1188 C C   A GLY   A 46  ? 0.1605 0.1549 0.2121 0.0314  -0.0176 0.0437  46  GLY   A C   
1189 C C   B GLY   A 46  ? 0.1466 0.1551 0.1372 -0.0070 0.0168  0.0087  46  GLY   A C   
1190 O O   A GLY   A 46  ? 0.1690 0.1604 0.2504 0.0233  -0.0292 0.0317  46  GLY   A O   
1191 O O   B GLY   A 46  ? 0.1514 0.1583 0.1386 -0.0097 0.0164  0.0006  46  GLY   A O   
1198 N N   A GLY   A 47  ? 0.1618 0.1555 0.2171 0.0330  -0.0114 0.0282  47  GLY   A N   
1199 N N   B GLY   A 47  ? 0.1470 0.1508 0.1362 -0.0007 0.0122  0.0023  47  GLY   A N   
1200 C CA  A GLY   A 47  ? 0.1657 0.1625 0.2176 0.0310  -0.0195 0.0115  47  GLY   A CA  
1201 C CA  B GLY   A 47  ? 0.1431 0.1452 0.1353 0.0034  0.0082  -0.0001 47  GLY   A CA  
1202 C C   A GLY   A 47  ? 0.1665 0.1493 0.1840 0.0304  -0.0326 0.0010  47  GLY   A C   
1203 C C   B GLY   A 47  ? 0.1382 0.1349 0.1176 0.0082  0.0093  -0.0025 47  GLY   A C   
1204 O O   A GLY   A 47  ? 0.1656 0.1476 0.2062 0.0313  -0.0301 0.0113  47  GLY   A O   
1205 O O   B GLY   A 47  ? 0.1331 0.1334 0.1228 0.0099  0.0132  0.0022  47  GLY   A O   
1212 N N   A GLY   A 48  ? 0.1658 0.1562 0.1823 0.0257  -0.0365 -0.0007 48  GLY   A N   
1213 N N   B GLY   A 48  ? 0.1360 0.1315 0.0991 0.0084  0.0122  -0.0021 48  GLY   A N   
1214 C CA  A GLY   A 48  ? 0.1563 0.1594 0.1838 0.0150  -0.0245 -0.0129 48  GLY   A CA  
1215 C CA  B GLY   A 48  ? 0.1307 0.1276 0.0776 0.0091  0.0146  -0.0089 48  GLY   A CA  
1216 C C   A GLY   A 48  ? 0.1411 0.1498 0.1681 0.0123  -0.0068 -0.0102 48  GLY   A C   
1217 C C   B GLY   A 48  ? 0.1265 0.1202 0.0781 0.0118  0.0076  -0.0060 48  GLY   A C   
1218 O O   A GLY   A 48  ? 0.1520 0.1463 0.1774 0.0152  -0.0105 -0.0138 48  GLY   A O   
1219 O O   B GLY   A 48  ? 0.1267 0.1218 0.0708 0.0138  0.0198  -0.0069 48  GLY   A O   
1226 N N   A VAL   A 49  ? 0.1356 0.1386 0.1753 -0.0035 -0.0050 -0.0074 49  VAL   A N   
1227 N N   B VAL   A 49  ? 0.1239 0.1124 0.0824 0.0088  -0.0041 -0.0143 49  VAL   A N   
1228 C CA  A VAL   A 49  ? 0.1504 0.1371 0.1753 -0.0153 -0.0042 -0.0004 49  VAL   A CA  
1229 C CA  B VAL   A 49  ? 0.1242 0.1138 0.1035 0.0099  -0.0144 -0.0164 49  VAL   A CA  
1230 C C   A VAL   A 49  ? 0.1366 0.1238 0.1604 -0.0075 -0.0032 0.0055  49  VAL   A C   
1231 C C   B VAL   A 49  ? 0.1247 0.1113 0.1216 0.0093  -0.0119 -0.0279 49  VAL   A C   
1232 O O   A VAL   A 49  ? 0.1397 0.1315 0.1610 -0.0138 0.0045  0.0040  49  VAL   A O   
1233 O O   B VAL   A 49  ? 0.1241 0.1157 0.1335 0.0107  -0.0154 -0.0235 49  VAL   A O   
1234 C CB  A VAL   A 49  ? 0.1785 0.1405 0.1846 -0.0200 -0.0083 0.0022  49  VAL   A CB  
1235 C CB  B VAL   A 49  ? 0.1233 0.1154 0.1136 0.0142  -0.0273 -0.0092 49  VAL   A CB  
1236 C CG1 A VAL   A 49  ? 0.2034 0.1380 0.2032 -0.0120 -0.0095 0.0081  49  VAL   A CG1 
1237 C CG1 B VAL   A 49  ? 0.1187 0.1112 0.1215 0.0180  -0.0365 0.0066  49  VAL   A CG1 
1238 C CG2 A VAL   A 49  ? 0.1945 0.1674 0.2174 -0.0418 -0.0119 0.0016  49  VAL   A CG2 
1239 C CG2 B VAL   A 49  ? 0.1290 0.1210 0.1120 0.0071  -0.0385 -0.0147 49  VAL   A CG2 
1258 N N   A ALA   A 50  ? 0.1332 0.1253 0.1564 -0.0022 -0.0089 0.0104  50  ALA   A N   
1259 N N   B ALA   A 50  ? 0.1266 0.1109 0.1198 0.0087  -0.0080 -0.0330 50  ALA   A N   
1260 C CA  A ALA   A 50  ? 0.1243 0.1235 0.1611 -0.0069 -0.0030 0.0127  50  ALA   A CA  
1261 C CA  B ALA   A 50  ? 0.1249 0.1122 0.1255 0.0070  -0.0018 -0.0338 50  ALA   A CA  
1262 C C   A ALA   A 50  ? 0.1242 0.1273 0.1515 -0.0139 0.0012  0.0064  50  ALA   A C   
1263 C C   B ALA   A 50  ? 0.1262 0.1129 0.1291 0.0061  -0.0059 -0.0293 50  ALA   A C   
1264 O O   A ALA   A 50  ? 0.1293 0.1318 0.1753 -0.0084 -0.0028 -0.0036 50  ALA   A O   
1265 O O   B ALA   A 50  ? 0.1246 0.1145 0.1267 0.0098  -0.0052 -0.0280 50  ALA   A O   
1266 C CB  A ALA   A 50  ? 0.1286 0.1195 0.1670 0.0036  -0.0051 0.0078  50  ALA   A CB  
1267 C CB  B ALA   A 50  ? 0.1253 0.1118 0.1233 0.0031  0.0031  -0.0425 50  ALA   A CB  
1278 N N   A GLY   A 51  ? 0.1253 0.1213 0.1614 0.0045  -0.0080 0.0095  51  GLY   A N   
1279 N N   B GLY   A 51  ? 0.1310 0.1114 0.1362 0.0044  -0.0056 -0.0305 51  GLY   A N   
1280 C CA  A GLY   A 51  ? 0.1410 0.1229 0.1737 0.0072  -0.0127 -0.0002 51  GLY   A CA  
1281 C CA  B GLY   A 51  ? 0.1385 0.1132 0.1333 0.0018  -0.0035 -0.0370 51  GLY   A CA  
1282 C C   A GLY   A 51  ? 0.1297 0.1315 0.1744 0.0070  0.0027  -0.0096 51  GLY   A C   
1283 C C   B GLY   A 51  ? 0.1394 0.1197 0.1430 0.0012  -0.0009 -0.0369 51  GLY   A C   
1284 O O   A GLY   A 51  ? 0.1388 0.1433 0.1802 -0.0016 0.0006  -0.0078 51  GLY   A O   
1285 O O   B GLY   A 51  ? 0.1429 0.1217 0.1549 0.0062  0.0030  -0.0408 51  GLY   A O   
1292 N N   A ALA   A 52  ? 0.1263 0.1433 0.1828 0.0057  0.0050  -0.0108 52  ALA   A N   
1293 N N   B ALA   A 52  ? 0.1407 0.1251 0.1410 -0.0042 0.0034  -0.0410 52  ALA   A N   
1294 C CA  A ALA   A 52  ? 0.1235 0.1559 0.1950 0.0049  0.0077  -0.0083 52  ALA   A CA  
1295 C CA  B ALA   A 52  ? 0.1384 0.1344 0.1443 -0.0047 -0.0007 -0.0380 52  ALA   A CA  
1296 C C   A ALA   A 52  ? 0.1237 0.1508 0.1703 -0.0084 0.0127  -0.0066 52  ALA   A C   
1297 C C   B ALA   A 52  ? 0.1329 0.1347 0.1419 -0.0089 -0.0036 -0.0373 52  ALA   A C   
1298 O O   A ALA   A 52  ? 0.1381 0.1567 0.1738 -0.0004 0.0114  0.0005  52  ALA   A O   
1299 O O   B ALA   A 52  ? 0.1355 0.1326 0.1527 -0.0124 -0.0047 -0.0367 52  ALA   A O   
1300 C CB  A ALA   A 52  ? 0.1310 0.1839 0.2086 0.0016  -0.0016 0.0055  52  ALA   A CB  
1301 C CB  B ALA   A 52  ? 0.1411 0.1448 0.1552 -0.0030 -0.0074 -0.0321 52  ALA   A CB  
1312 N N   A LEU   A 53  ? 0.1256 0.1409 0.1727 -0.0047 0.0028  0.0040  53  LEU   A N   
1313 N N   B LEU   A 53  ? 0.1279 0.1353 0.1337 -0.0067 -0.0124 -0.0364 53  LEU   A N   
1314 C CA  A LEU   A 53  ? 0.1396 0.1529 0.1592 -0.0085 0.0006  0.0023  53  LEU   A CA  
1315 C CA  B LEU   A 53  ? 0.1306 0.1407 0.1308 -0.0047 -0.0150 -0.0293 53  LEU   A CA  
1316 C C   A LEU   A 53  ? 0.1330 0.1495 0.1297 0.0027  0.0069  0.0028  53  LEU   A C   
1317 C C   B LEU   A 53  ? 0.1373 0.1485 0.1348 -0.0060 -0.0112 -0.0253 53  LEU   A C   
1318 O O   A LEU   A 53  ? 0.1566 0.1610 0.1493 -0.0133 0.0011  0.0002  53  LEU   A O   
1319 O O   B LEU   A 53  ? 0.1418 0.1516 0.1468 -0.0064 -0.0108 -0.0223 53  LEU   A O   
1320 C CB  A LEU   A 53  ? 0.1445 0.1535 0.1660 -0.0104 0.0089  0.0022  53  LEU   A CB  
1321 C CB  B LEU   A 53  ? 0.1271 0.1379 0.1197 -0.0026 -0.0210 -0.0278 53  LEU   A CB  
1322 C CG  A LEU   A 53  ? 0.1595 0.1529 0.1782 -0.0198 0.0094  0.0039  53  LEU   A CG  
1323 C CG  B LEU   A 53  ? 0.1258 0.1348 0.1253 -0.0011 -0.0268 -0.0231 53  LEU   A CG  
1324 C CD1 A LEU   A 53  ? 0.1622 0.1567 0.1781 -0.0046 -0.0001 0.0071  53  LEU   A CD1 
1325 C CD1 B LEU   A 53  ? 0.1238 0.1363 0.1243 0.0029  -0.0324 -0.0286 53  LEU   A CD1 
1326 C CD2 A LEU   A 53  ? 0.1892 0.1706 0.1992 -0.0227 0.0136  0.0060  53  LEU   A CD2 
1327 C CD2 B LEU   A 53  ? 0.1291 0.1323 0.1279 -0.0051 -0.0231 -0.0238 53  LEU   A CD2 
1350 N N   A ASN   A 54  ? 0.1255 0.1437 0.1433 -0.0055 0.0051  0.0027  54  ASN   A N   
1351 N N   B ASN   A 54  ? 0.1411 0.1554 0.1393 -0.0083 -0.0085 -0.0191 54  ASN   A N   
1352 C CA  A ASN   A 54  ? 0.1151 0.1330 0.1643 -0.0026 0.0029  0.0013  54  ASN   A CA  
1353 C CA  B ASN   A 54  ? 0.1444 0.1612 0.1436 -0.0090 -0.0047 -0.0150 54  ASN   A CA  
1354 C C   A ASN   A 54  ? 0.1212 0.1372 0.1748 -0.0161 0.0094  -0.0014 54  ASN   A C   
1355 C C   B ASN   A 54  ? 0.1492 0.1664 0.1421 -0.0111 -0.0008 -0.0148 54  ASN   A C   
1356 O O   A ASN   A 54  ? 0.1308 0.1491 0.1905 -0.0095 -0.0000 -0.0079 54  ASN   A O   
1357 O O   B ASN   A 54  ? 0.1516 0.1686 0.1351 -0.0118 -0.0000 -0.0146 54  ASN   A O   
1358 C CB  A ASN   A 54  ? 0.1189 0.1305 0.1787 -0.0064 -0.0038 -0.0077 54  ASN   A CB  
1359 C CB  B ASN   A 54  ? 0.1453 0.1633 0.1455 -0.0078 0.0007  -0.0103 54  ASN   A CB  
1360 C CG  A ASN   A 54  ? 0.1189 0.1361 0.1770 -0.0033 -0.0033 -0.0059 54  ASN   A CG  
1361 C CG  B ASN   A 54  ? 0.1458 0.1657 0.1405 -0.0068 0.0070  -0.0045 54  ASN   A CG  
1362 O OD1 A ASN   A 54  ? 0.1206 0.1321 0.1786 -0.0050 -0.0082 0.0019  54  ASN   A OD1 
1363 O OD1 B ASN   A 54  ? 0.1459 0.1696 0.1439 -0.0104 0.0120  -0.0008 54  ASN   A OD1 
1364 N ND2 A ASN   A 54  ? 0.1234 0.1442 0.1876 -0.0054 -0.0166 0.0092  54  ASN   A ND2 
1365 N ND2 B ASN   A 54  ? 0.1476 0.1643 0.1354 -0.0054 0.0082  -0.0009 54  ASN   A ND2 
1378 N N   A LYS   A 55  ? 0.1268 0.1380 0.1778 -0.0070 -0.0046 -0.0157 55  LYS   A N   
1379 N N   B LYS   A 55  ? 0.1520 0.1697 0.1508 -0.0081 0.0027  -0.0182 55  LYS   A N   
1380 C CA  A LYS   A 55  ? 0.1380 0.1464 0.1845 0.0018  -0.0060 -0.0261 55  LYS   A CA  
1381 C CA  B LYS   A 55  ? 0.1547 0.1768 0.1691 -0.0053 0.0095  -0.0160 55  LYS   A CA  
1382 C C   A LYS   A 55  ? 0.1359 0.1582 0.1725 -0.0034 0.0006  -0.0253 55  LYS   A C   
1383 C C   B LYS   A 55  ? 0.1490 0.1751 0.1709 -0.0072 0.0100  -0.0197 55  LYS   A C   
1384 O O   A LYS   A 55  ? 0.1458 0.1707 0.1879 -0.0019 0.0018  -0.0293 55  LYS   A O   
1385 O O   B LYS   A 55  ? 0.1515 0.1755 0.1664 -0.0029 0.0124  -0.0185 55  LYS   A O   
1386 C CB  A LYS   A 55  ? 0.1438 0.1514 0.1973 0.0129  -0.0034 -0.0219 55  LYS   A CB  
1387 C CB  B LYS   A 55  ? 0.1592 0.1850 0.1868 -0.0042 0.0165  -0.0085 55  LYS   A CB  
1388 C CG  A LYS   A 55  ? 0.1631 0.1760 0.2056 0.0182  -0.0147 -0.0212 55  LYS   A CG  
1389 C CG  B LYS   A 55  ? 0.1639 0.1940 0.2053 -0.0047 0.0183  -0.0084 55  LYS   A CG  
1390 C CD  A LYS   A 55  ? 0.1722 0.2009 0.2136 0.0236  -0.0109 -0.0249 55  LYS   A CD  
1391 C CD  B LYS   A 55  ? 0.1707 0.2008 0.2263 -0.0044 0.0197  -0.0093 55  LYS   A CD  
1392 C CE  A LYS   A 55  ? 0.1846 0.2273 0.2261 0.0306  -0.0147 -0.0202 55  LYS   A CE  
1393 C CE  B LYS   A 55  ? 0.1782 0.2061 0.2440 -0.0065 0.0198  -0.0101 55  LYS   A CE  
1394 N NZ  A LYS   A 55  ? 0.1913 0.2397 0.2424 0.0376  -0.0186 -0.0159 55  LYS   A NZ  
1395 N NZ  B LYS   A 55  ? 0.1810 0.2073 0.2541 -0.0082 0.0188  -0.0097 55  LYS   A NZ  
1422 N N   . ALA   A 56  ? 0.1417 0.1737 0.1785 -0.0137 0.0148  -0.0272 56  ALA   A N   
1423 C CA  . ALA   A 56  ? 0.1598 0.1910 0.1763 -0.0198 0.0154  -0.0248 56  ALA   A CA  
1424 C C   . ALA   A 56  ? 0.1673 0.1970 0.1544 -0.0139 0.0224  -0.0293 56  ALA   A C   
1425 O O   . ALA   A 56  ? 0.1732 0.2298 0.1665 0.0012  0.0330  -0.0176 56  ALA   A O   
1426 C CB  . ALA   A 56  ? 0.1677 0.2135 0.1938 -0.0231 0.0175  -0.0116 56  ALA   A CB  
1433 N N   . THR   A 57  ? 0.1488 0.1779 0.1532 -0.0098 0.0161  -0.0266 57  THR   A N   
1434 C CA  . THR   A 57  ? 0.1539 0.1699 0.1664 -0.0147 0.0017  -0.0158 57  THR   A CA  
1435 C C   . THR   A 57  ? 0.1519 0.1748 0.1690 -0.0085 -0.0004 -0.0179 57  THR   A C   
1436 O O   . THR   A 57  ? 0.1505 0.1810 0.1932 -0.0111 -0.0029 -0.0314 57  THR   A O   
1437 C CB  . THR   A 57  ? 0.1540 0.1638 0.1649 -0.0105 0.0075  -0.0102 57  THR   A CB  
1438 O OG1 . THR   A 57  ? 0.1424 0.1614 0.1725 -0.0089 0.0016  -0.0125 57  THR   A OG1 
1439 C CG2 . THR   A 57  ? 0.1580 0.1683 0.1393 -0.0076 0.0032  -0.0025 57  THR   A CG2 
1447 N N   . ASN   A 58  ? 0.1543 0.1711 0.1853 -0.0081 0.0056  -0.0343 58  ASN   A N   
1448 C CA  . ASN   A 58  ? 0.1760 0.1644 0.2124 -0.0099 0.0183  -0.0503 58  ASN   A CA  
1449 C C   . ASN   A 58  ? 0.1524 0.1524 0.1968 -0.0039 0.0029  -0.0318 58  ASN   A C   
1450 O O   . ASN   A 58  ? 0.1536 0.1646 0.2146 -0.0165 0.0001  -0.0391 58  ASN   A O   
1451 C CB  . ASN   A 58  ? 0.2283 0.1802 0.2465 -0.0192 0.0483  -0.0609 58  ASN   A CB  
1452 C CG  . ASN   A 58  ? 0.2769 0.2060 0.3163 -0.0224 0.0511  -0.0454 58  ASN   A CG  
1453 O OD1 . ASN   A 58  ? 0.3027 0.1948 0.3583 0.0127  0.0843  -0.0351 58  ASN   A OD1 
1454 N ND2 . ASN   A 58  ? 0.2937 0.2179 0.3433 -0.0263 0.0363  -0.0451 58  ASN   A ND2 
1461 N N   . ASN   A 59  ? 0.1365 0.1440 0.1880 -0.0062 -0.0078 -0.0265 59  ASN   A N   
1462 C CA  . ASN   A 59  ? 0.1339 0.1359 0.1855 -0.0004 -0.0089 -0.0145 59  ASN   A CA  
1463 C C   . ASN   A 59  ? 0.1391 0.1364 0.1695 -0.0067 -0.0034 -0.0082 59  ASN   A C   
1464 O O   . ASN   A 59  ? 0.1409 0.1434 0.1719 -0.0073 0.0025  -0.0022 59  ASN   A O   
1465 C CB  . ASN   A 59  ? 0.1451 0.1294 0.1830 0.0011  -0.0152 -0.0190 59  ASN   A CB  
1466 C CG  . ASN   A 59  ? 0.1506 0.1384 0.1879 -0.0037 -0.0212 -0.0014 59  ASN   A CG  
1467 O OD1 . ASN   A 59  ? 0.1576 0.1484 0.1785 -0.0099 -0.0250 0.0035  59  ASN   A OD1 
1468 N ND2 . ASN   A 59  ? 0.1595 0.1446 0.1958 -0.0091 -0.0208 0.0094  59  ASN   A ND2 
1475 N N   . ALA   A 60  ? 0.1315 0.1446 0.1607 -0.0035 0.0013  -0.0079 60  ALA   A N   
1476 C CA  . ALA   A 60  ? 0.1381 0.1451 0.1701 -0.0041 -0.0005 -0.0044 60  ALA   A CA  
1477 C C   . ALA   A 60  ? 0.1347 0.1404 0.1766 -0.0058 -0.0052 -0.0031 60  ALA   A C   
1478 O O   . ALA   A 60  ? 0.1293 0.1485 0.1990 -0.0063 -0.0124 -0.0083 60  ALA   A O   
1479 C CB  . ALA   A 60  ? 0.1463 0.1584 0.1704 0.0026  -0.0081 -0.0201 60  ALA   A CB  
1485 N N   . MET   A 61  ? 0.1323 0.1313 0.1729 -0.0012 0.0016  -0.0062 61  MET   A N   
1486 C CA  . MET   A 61  ? 0.1325 0.1257 0.1759 -0.0059 0.0064  0.0039  61  MET   A CA  
1487 C C   . MET   A 61  ? 0.1233 0.1225 0.1804 -0.0111 0.0054  -0.0091 61  MET   A C   
1488 O O   . MET   A 61  ? 0.1326 0.1291 0.1825 -0.0037 0.0099  -0.0038 61  MET   A O   
1489 C CB  . MET   A 61  ? 0.1390 0.1277 0.1753 -0.0072 -0.0003 -0.0015 61  MET   A CB  
1490 C CG  . MET   A 61  ? 0.1456 0.1439 0.1839 0.0018  0.0032  -0.0031 61  MET   A CG  
1491 S SD  . MET   A 61  ? 0.1458 0.1491 0.2178 -0.0124 0.0005  -0.0220 61  MET   A SD  
1492 C CE  . MET   A 61  ? 0.1699 0.1660 0.2471 -0.0179 0.0215  -0.0152 61  MET   A CE  
1502 N N   . GLN   A 62  ? 0.1342 0.1270 0.1678 -0.0052 -0.0002 -0.0070 62  GLN   A N   
1503 C CA  . GLN   A 62  ? 0.1334 0.1261 0.1780 -0.0022 0.0060  -0.0001 62  GLN   A CA  
1504 C C   . GLN   A 62  ? 0.1337 0.1164 0.1828 0.0010  0.0062  0.0002  62  GLN   A C   
1505 O O   . GLN   A 62  ? 0.1313 0.1343 0.1942 -0.0029 0.0036  0.0026  62  GLN   A O   
1506 C CB  . GLN   A 62  ? 0.1337 0.1201 0.1786 0.0013  0.0011  -0.0034 62  GLN   A CB  
1507 C CG  . GLN   A 62  ? 0.1329 0.1263 0.1846 -0.0065 -0.0015 0.0102  62  GLN   A CG  
1508 C CD  . GLN   A 62  ? 0.1427 0.1287 0.1814 -0.0059 0.0089  0.0080  62  GLN   A CD  
1509 O OE1 . GLN   A 62  ? 0.1425 0.1409 0.1950 -0.0027 -0.0034 0.0007  62  GLN   A OE1 
1510 N NE2 . GLN   A 62  ? 0.1511 0.1385 0.1929 -0.0029 -0.0063 -0.0063 62  GLN   A NE2 
1519 N N   . VAL   A 63  ? 0.1311 0.1290 0.1864 -0.0057 0.0076  -0.0175 63  VAL   A N   
1520 C CA  . VAL   A 63  ? 0.1324 0.1377 0.2187 -0.0160 0.0005  -0.0172 63  VAL   A CA  
1521 C C   . VAL   A 63  ? 0.1191 0.1416 0.1963 -0.0147 -0.0116 -0.0144 63  VAL   A C   
1522 O O   . VAL   A 63  ? 0.1221 0.1456 0.2079 -0.0174 -0.0010 -0.0182 63  VAL   A O   
1523 C CB  . VAL   A 63  ? 0.1508 0.1583 0.2497 -0.0183 -0.0039 -0.0397 63  VAL   A CB  
1524 C CG1 . VAL   A 63  ? 0.1665 0.1823 0.2734 -0.0160 -0.0086 -0.0598 63  VAL   A CG1 
1525 C CG2 . VAL   A 63  ? 0.1561 0.1513 0.2647 -0.0170 0.0140  -0.0430 63  VAL   A CG2 
1535 N N   . GLU   A 64  ? 0.1288 0.1507 0.1845 -0.0033 -0.0050 -0.0114 64  GLU   A N   
1536 C CA  . GLU   A 64  ? 0.1280 0.1471 0.1977 -0.0090 -0.0087 0.0034  64  GLU   A CA  
1537 C C   . GLU   A 64  ? 0.1194 0.1367 0.2006 -0.0096 0.0010  -0.0051 64  GLU   A C   
1538 O O   . GLU   A 64  ? 0.1300 0.1506 0.1997 0.0002  -0.0002 -0.0023 64  GLU   A O   
1539 C CB  . GLU   A 64  ? 0.1400 0.1553 0.2132 -0.0064 -0.0012 -0.0040 64  GLU   A CB  
1540 C CG  . GLU   A 64  ? 0.1505 0.1659 0.2301 -0.0122 0.0005  -0.0030 64  GLU   A CG  
1541 C CD  . GLU   A 64  ? 0.1692 0.1770 0.2261 -0.0173 0.0058  -0.0004 64  GLU   A CD  
1542 O OE1 . GLU   A 64  ? 0.1720 0.1833 0.2643 -0.0224 0.0195  -0.0025 64  GLU   A OE1 
1543 O OE2 . GLU   A 64  ? 0.1928 0.1829 0.2129 -0.0255 0.0004  0.0094  64  GLU   A OE2 
1550 N N   . SER   A 65  ? 0.1156 0.1361 0.1843 -0.0009 0.0011  -0.0096 65  SER   A N   
1551 C CA  . SER   A 65  ? 0.1292 0.1309 0.1776 -0.0018 -0.0009 -0.0121 65  SER   A CA  
1552 C C   . SER   A 65  ? 0.1293 0.1375 0.1836 -0.0037 -0.0099 -0.0031 65  SER   A C   
1553 O O   . SER   A 65  ? 0.1388 0.1394 0.1974 0.0015  0.0086  -0.0077 65  SER   A O   
1554 C CB  . SER   A 65  ? 0.1284 0.1318 0.1818 -0.0125 0.0054  0.0014  65  SER   A CB  
1555 O OG  . SER   A 65  ? 0.1316 0.1411 0.1989 -0.0072 0.0010  0.0103  65  SER   A OG  
1561 N N   . ASP   A 66  ? 0.1310 0.1325 0.1882 -0.0004 0.0077  0.0080  66  ASP   A N   
1562 C CA  . ASP   A 66  ? 0.1459 0.1429 0.2015 -0.0025 0.0102  0.0140  66  ASP   A CA  
1563 C C   . ASP   A 66  ? 0.1373 0.1412 0.1983 -0.0076 0.0105  0.0128  66  ASP   A C   
1564 O O   . ASP   A 66  ? 0.1471 0.1525 0.2190 -0.0034 0.0262  0.0235  66  ASP   A O   
1565 C CB  . ASP   A 66  ? 0.1559 0.1520 0.2396 0.0089  0.0131  0.0349  66  ASP   A CB  
1566 C CG  . ASP   A 66  ? 0.1795 0.1685 0.2687 0.0008  0.0039  0.0459  66  ASP   A CG  
1567 O OD1 . ASP   A 66  ? 0.1832 0.1994 0.2506 -0.0059 -0.0018 0.0541  66  ASP   A OD1 
1568 O OD2 . ASP   A 66  ? 0.1992 0.1845 0.3518 0.0229  -0.0159 0.0212  66  ASP   A OD2 
1573 N N   . ASP   A 67  ? 0.1287 0.1484 0.2111 -0.0045 0.0086  0.0126  67  ASP   A N   
1574 C CA  . ASP   A 67  ? 0.1303 0.1676 0.2200 -0.0004 0.0045  0.0244  67  ASP   A CA  
1575 C C   . ASP   A 67  ? 0.1269 0.1700 0.2161 0.0012  0.0107  0.0265  67  ASP   A C   
1576 O O   . ASP   A 67  ? 0.1284 0.1770 0.2400 -0.0032 0.0214  0.0340  67  ASP   A O   
1577 C CB  . ASP   A 67  ? 0.1435 0.1830 0.2638 -0.0012 -0.0165 0.0343  67  ASP   A CB  
1578 C CG  . ASP   A 67  ? 0.1433 0.1977 0.3021 -0.0091 -0.0342 0.0361  67  ASP   A CG  
1579 O OD1 . ASP   A 67  ? 0.1468 0.2154 0.3776 -0.0125 -0.0496 0.0455  67  ASP   A OD1 
1580 O OD2 . ASP   A 67  ? 0.1475 0.2043 0.2919 0.0112  -0.0182 0.0333  67  ASP   A OD2 
1585 N N   . TYR   A 68  ? 0.1339 0.1534 0.2105 0.0100  0.0136  0.0281  68  TYR   A N   
1586 C CA  . TYR   A 68  ? 0.1498 0.1442 0.2053 0.0070  0.0233  0.0258  68  TYR   A CA  
1587 C C   . TYR   A 68  ? 0.1399 0.1414 0.2002 0.0015  0.0250  0.0213  68  TYR   A C   
1588 O O   . TYR   A 68  ? 0.1495 0.1466 0.2076 0.0091  0.0304  0.0222  68  TYR   A O   
1589 C CB  . TYR   A 68  ? 0.1456 0.1452 0.2264 0.0137  0.0404  0.0356  68  TYR   A CB  
1590 C CG  . TYR   A 68  ? 0.1528 0.1619 0.2594 0.0090  0.0625  0.0344  68  TYR   A CG  
1591 C CD1 . TYR   A 68  ? 0.1704 0.1718 0.3011 -0.0239 0.0473  -0.0067 68  TYR   A CD1 
1592 C CD2 . TYR   A 68  ? 0.1814 0.1693 0.3142 0.0106  0.0625  0.0310  68  TYR   A CD2 
1593 C CE1 . TYR   A 68  ? 0.1783 0.1811 0.3404 -0.0193 0.0564  -0.0159 68  TYR   A CE1 
1594 C CE2 . TYR   A 68  ? 0.1784 0.1688 0.3319 -0.0039 0.0781  0.0102  68  TYR   A CE2 
1595 C CZ  . TYR   A 68  ? 0.1815 0.1715 0.3592 -0.0222 0.0590  -0.0241 68  TYR   A CZ  
1596 O OH  . TYR   A 68  ? 0.2115 0.1802 0.3936 -0.0211 0.0374  -0.0582 68  TYR   A OH  
1606 N N   . ILE   A 69  ? 0.1290 0.1363 0.2120 0.0027  0.0198  0.0098  69  ILE   A N   
1607 C CA  . ILE   A 69  ? 0.1388 0.1447 0.2066 0.0063  0.0086  -0.0002 69  ILE   A CA  
1608 C C   . ILE   A 69  ? 0.1459 0.1461 0.1935 0.0036  0.0130  0.0105  69  ILE   A C   
1609 O O   . ILE   A 69  ? 0.1533 0.1531 0.1887 0.0012  0.0182  0.0202  69  ILE   A O   
1610 C CB  . ILE   A 69  ? 0.1454 0.1672 0.2100 0.0098  0.0118  -0.0143 69  ILE   A CB  
1611 C CG1 . ILE   A 69  ? 0.1477 0.1790 0.2216 0.0047  0.0209  -0.0169 69  ILE   A CG1 
1612 C CG2 . ILE   A 69  ? 0.1729 0.1860 0.2322 0.0212  -0.0062 -0.0183 69  ILE   A CG2 
1613 C CD1 . ILE   A 69  ? 0.1531 0.1830 0.2475 -0.0067 0.0154  -0.0229 69  ILE   A CD1 
1625 N N   . ALA   A 70  ? 0.1496 0.1475 0.1941 -0.0074 0.0157  0.0210  70  ALA   A N   
1626 C CA  . ALA   A 70  ? 0.1534 0.1622 0.2183 -0.0191 0.0256  0.0200  70  ALA   A CA  
1627 C C   . ALA   A 70  ? 0.1486 0.1782 0.2150 -0.0197 0.0214  0.0177  70  ALA   A C   
1628 O O   . ALA   A 70  ? 0.1697 0.2088 0.2357 -0.0015 0.0345  0.0383  70  ALA   A O   
1629 C CB  . ALA   A 70  ? 0.1527 0.1610 0.2379 -0.0162 0.0240  0.0116  70  ALA   A CB  
1635 N N   . THR   A 71  ? 0.1379 0.1740 0.2097 -0.0110 0.0142  0.0240  71  THR   A N   
1636 C CA  . THR   A 71  ? 0.1494 0.1887 0.2374 0.0051  0.0139  0.0232  71  THR   A CA  
1637 C C   . THR   A 71  ? 0.1383 0.1830 0.2572 0.0186  0.0261  0.0177  71  THR   A C   
1638 O O   . THR   A 71  ? 0.1444 0.2153 0.3029 0.0097  0.0403  -0.0101 71  THR   A O   
1639 C CB  . THR   A 71  ? 0.1768 0.2131 0.2543 0.0150  -0.0159 0.0301  71  THR   A CB  
1640 O OG1 . THR   A 71  ? 0.2053 0.2335 0.2639 0.0067  -0.0341 0.0219  71  THR   A OG1 
1641 C CG2 . THR   A 71  ? 0.1918 0.2318 0.2808 0.0199  -0.0209 0.0446  71  THR   A CG2 
1649 N N   . ASN   A 72  ? 0.1407 0.1659 0.2290 0.0174  0.0195  0.0225  72  ASN   A N   
1650 C CA  . ASN   A 72  ? 0.1519 0.1646 0.2225 0.0187  0.0377  0.0229  72  ASN   A CA  
1651 C C   . ASN   A 72  ? 0.1626 0.1615 0.2287 0.0101  0.0455  0.0197  72  ASN   A C   
1652 O O   . ASN   A 72  ? 0.1859 0.1635 0.2558 0.0164  0.0442  0.0038  72  ASN   A O   
1653 C CB  . ASN   A 72  ? 0.1799 0.1743 0.2234 0.0172  0.0366  0.0213  72  ASN   A CB  
1654 C CG  . ASN   A 72  ? 0.1994 0.1869 0.2267 0.0224  0.0327  0.0190  72  ASN   A CG  
1655 O OD1 . ASN   A 72  ? 0.2154 0.2195 0.2446 0.0214  0.0359  0.0237  72  ASN   A OD1 
1656 N ND2 . ASN   A 72  ? 0.2180 0.1904 0.2340 0.0487  0.0155  0.0193  72  ASN   A ND2 
1663 N N   . GLY   A 73  ? 0.1659 0.1607 0.2127 0.0034  0.0436  0.0069  73  GLY   A N   
1664 C CA  . GLY   A 73  ? 0.1659 0.1580 0.2045 -0.0106 0.0359  0.0048  73  GLY   A CA  
1665 C C   . GLY   A 73  ? 0.1703 0.1459 0.1954 0.0039  0.0450  0.0301  73  GLY   A C   
1666 O O   . GLY   A 73  ? 0.1736 0.1549 0.2080 0.0141  0.0397  0.0308  73  GLY   A O   
1670 N N   . PRO   A 74  ? 0.1794 0.1526 0.1968 -0.0091 0.0468  0.0174  74  PRO   A N   
1671 C CA  . PRO   A 74  ? 0.1776 0.1475 0.2020 -0.0039 0.0461  0.0141  74  PRO   A CA  
1672 C C   . PRO   A 74  ? 0.1735 0.1335 0.1962 -0.0004 0.0265  0.0072  74  PRO   A C   
1673 O O   . PRO   A 74  ? 0.1805 0.1403 0.2263 -0.0010 0.0318  -0.0055 74  PRO   A O   
1674 C CB  . PRO   A 74  ? 0.1944 0.1695 0.2196 0.0023  0.0461  0.0231  74  PRO   A CB  
1675 C CG  . PRO   A 74  ? 0.2213 0.2072 0.2692 -0.0117 0.0283  0.0123  74  PRO   A CG  
1676 C CD  . PRO   A 74  ? 0.2009 0.1820 0.2248 -0.0166 0.0373  0.0126  74  PRO   A CD  
1684 N N   . LEU   A 75  ? 0.1622 0.1248 0.1943 -0.0008 0.0240  0.0058  75  LEU   A N   
1685 C CA  . LEU   A 75  ? 0.1669 0.1322 0.1688 0.0002  0.0077  0.0124  75  LEU   A CA  
1686 C C   . LEU   A 75  ? 0.1766 0.1427 0.1674 0.0079  0.0069  0.0139  75  LEU   A C   
1687 O O   . LEU   A 75  ? 0.2113 0.1530 0.1757 0.0155  0.0035  0.0094  75  LEU   A O   
1688 C CB  . LEU   A 75  ? 0.1778 0.1379 0.1678 -0.0145 0.0131  0.0193  75  LEU   A CB  
1689 C CG  . LEU   A 75  ? 0.1936 0.1751 0.1732 -0.0429 0.0112  0.0193  75  LEU   A CG  
1690 C CD1 . LEU   A 75  ? 0.2064 0.2261 0.1801 -0.0406 0.0071  -0.0016 75  LEU   A CD1 
1691 C CD2 . LEU   A 75  ? 0.2219 0.2232 0.2301 -0.0182 0.0115  0.0229  75  LEU   A CD2 
1703 N N   . LYS   A 76  ? 0.1830 0.1428 0.1815 -0.0043 0.0119  -0.0008 76  LYS   A N   
1704 C CA  . LYS   A 76  ? 0.1828 0.1630 0.1876 -0.0114 0.0138  -0.0133 76  LYS   A CA  
1705 C C   . LYS   A 76  ? 0.1753 0.1438 0.1525 -0.0002 0.0051  0.0021  76  LYS   A C   
1706 O O   . LYS   A 76  ? 0.1742 0.1366 0.1662 -0.0001 0.0157  0.0081  76  LYS   A O   
1707 C CB  . LYS   A 76  ? 0.1818 0.1890 0.2367 0.0035  0.0112  -0.0400 76  LYS   A CB  
1708 C CG  . LYS   A 76  ? 0.1896 0.1817 0.2860 0.0068  0.0015  -0.0352 76  LYS   A CG  
1709 C CD  . LYS   A 76  ? 0.1951 0.1754 0.3257 0.0120  -0.0095 -0.0356 76  LYS   A CD  
1710 C CE  . LYS   A 76  ? 0.2124 0.2009 0.3840 0.0018  -0.0041 -0.0411 76  LYS   A CE  
1711 N NZ  . LYS   A 76  ? 0.2143 0.2003 0.4216 -0.0077 -0.0057 -0.0525 76  LYS   A NZ  
1725 N N   . VAL   A 77  ? 0.1826 0.1505 0.1554 0.0034  0.0203  0.0096  77  VAL   A N   
1726 C CA  . VAL   A 77  ? 0.1773 0.1455 0.1572 0.0068  0.0171  0.0081  77  VAL   A CA  
1727 C C   . VAL   A 77  ? 0.1690 0.1421 0.1556 0.0089  0.0096  0.0068  77  VAL   A C   
1728 O O   . VAL   A 77  ? 0.1801 0.1478 0.1640 0.0134  0.0260  -0.0054 77  VAL   A O   
1729 C CB  . VAL   A 77  ? 0.2010 0.1687 0.1673 -0.0000 0.0119  0.0135  77  VAL   A CB  
1730 C CG1 . VAL   A 77  ? 0.1955 0.1807 0.1874 0.0088  -0.0013 0.0014  77  VAL   A CG1 
1731 C CG2 . VAL   A 77  ? 0.2304 0.1821 0.1986 -0.0035 -0.0006 0.0127  77  VAL   A CG2 
1741 N N   . GLY   A 78  ? 0.1661 0.1411 0.1540 0.0054  0.0242  0.0032  78  GLY   A N   
1742 C CA  . GLY   A 78  ? 0.1664 0.1354 0.1733 0.0087  0.0241  0.0023  78  GLY   A CA  
1743 C C   . GLY   A 78  ? 0.1532 0.1315 0.1740 0.0063  0.0172  0.0097  78  GLY   A C   
1744 O O   . GLY   A 78  ? 0.1488 0.1378 0.1958 0.0050  0.0209  0.0257  78  GLY   A O   
1748 N N   . GLY   A 79  ? 0.1508 0.1280 0.1773 -0.0011 0.0131  0.0127  79  GLY   A N   
1749 C CA  . GLY   A 79  ? 0.1515 0.1332 0.1778 0.0054  0.0139  0.0117  79  GLY   A CA  
1750 C C   . GLY   A 79  ? 0.1347 0.1348 0.1680 0.0030  0.0123  0.0106  79  GLY   A C   
1751 O O   . GLY   A 79  ? 0.1419 0.1431 0.1819 0.0182  0.0091  0.0067  79  GLY   A O   
1755 N N   . SER   A 80  ? 0.1306 0.1462 0.1863 0.0014  0.0109  -0.0053 80  SER   A N   
1756 C CA  . SER   A 80  ? 0.1364 0.1378 0.1822 0.0022  0.0032  -0.0043 80  SER   A CA  
1757 C C   . SER   A 80  ? 0.1336 0.1387 0.1717 0.0002  0.0049  0.0055  80  SER   A C   
1758 O O   . SER   A 80  ? 0.1343 0.1656 0.2047 0.0055  0.0136  -0.0049 80  SER   A O   
1759 C CB  . SER   A 80  ? 0.1496 0.1376 0.2009 -0.0036 0.0122  0.0017  80  SER   A CB  
1760 O OG  . SER   A 80  ? 0.1763 0.1385 0.2239 0.0032  -0.0019 0.0120  80  SER   A OG  
1766 N N   . CYS   A 81  ? 0.1247 0.1335 0.1698 -0.0012 -0.0035 0.0074  81  CYS   A N   
1767 C CA  . CYS   A 81  ? 0.1267 0.1488 0.1670 -0.0046 -0.0043 0.0221  81  CYS   A CA  
1768 C C   . CYS   A 81  ? 0.1281 0.1380 0.1697 -0.0130 -0.0029 0.0274  81  CYS   A C   
1769 O O   . CYS   A 81  ? 0.1267 0.1695 0.1882 -0.0042 -0.0005 0.0337  81  CYS   A O   
1770 C CB  . CYS   A 81  ? 0.1392 0.1552 0.1939 -0.0094 -0.0024 0.0212  81  CYS   A CB  
1771 S SG  . CYS   A 81  ? 0.1524 0.1413 0.1951 -0.0153 0.0026  0.0129  81  CYS   A SG  
1777 N N   . VAL   A 82  ? 0.1321 0.1513 0.1654 0.0038  -0.0122 0.0201  82  VAL   A N   
1778 C CA  . VAL   A 82  ? 0.1428 0.1567 0.1802 0.0026  -0.0089 0.0211  82  VAL   A CA  
1779 C C   . VAL   A 82  ? 0.1444 0.1607 0.1805 -0.0039 -0.0090 0.0303  82  VAL   A C   
1780 O O   . VAL   A 82  ? 0.1341 0.1728 0.2122 -0.0019 -0.0030 -0.0029 82  VAL   A O   
1781 C CB  . VAL   A 82  ? 0.1783 0.1705 0.1926 -0.0022 -0.0003 0.0285  82  VAL   A CB  
1782 C CG1 . VAL   A 82  ? 0.1986 0.1872 0.2142 0.0084  0.0037  0.0240  82  VAL   A CG1 
1783 C CG2 . VAL   A 82  ? 0.1897 0.1772 0.2215 -0.0074 -0.0015 0.0314  82  VAL   A CG2 
1793 N N   . LEU   A 83  ? 0.1400 0.1549 0.1724 -0.0104 -0.0104 0.0124  83  LEU   A N   
1794 C CA  . LEU   A 83  ? 0.1415 0.1605 0.1609 -0.0065 -0.0115 0.0072  83  LEU   A CA  
1795 C C   . LEU   A 83  ? 0.1475 0.1631 0.1643 -0.0113 -0.0134 0.0044  83  LEU   A C   
1796 O O   . LEU   A 83  ? 0.1579 0.1631 0.1764 -0.0140 -0.0028 0.0118  83  LEU   A O   
1797 C CB  . LEU   A 83  ? 0.1496 0.1646 0.1662 -0.0133 -0.0082 0.0116  83  LEU   A CB  
1798 C CG  . LEU   A 83  ? 0.1648 0.1792 0.1789 -0.0116 0.0065  0.0043  83  LEU   A CG  
1799 C CD1 . LEU   A 83  ? 0.1779 0.1794 0.1854 -0.0246 -0.0018 0.0215  83  LEU   A CD1 
1800 C CD2 . LEU   A 83  ? 0.1642 0.1944 0.2010 -0.0137 0.0249  0.0159  83  LEU   A CD2 
1812 N N   . SER   A 84  ? 0.1639 0.1672 0.1615 -0.0149 -0.0008 0.0135  84  SER   A N   
1813 C CA  . SER   A 84  ? 0.1768 0.1731 0.1511 -0.0163 -0.0040 0.0051  84  SER   A CA  
1814 C C   . SER   A 84  ? 0.1771 0.1652 0.1375 -0.0218 0.0026  0.0104  84  SER   A C   
1815 O O   . SER   A 84  ? 0.1748 0.1826 0.1468 -0.0154 -0.0109 0.0108  84  SER   A O   
1816 C CB  . SER   A 84  ? 0.1880 0.2018 0.1629 -0.0147 -0.0036 -0.0002 84  SER   A CB  
1817 O OG  . SER   A 84  ? 0.1914 0.2238 0.1780 -0.0110 -0.0136 -0.0201 84  SER   A OG  
1823 N N   . GLY   A 85  ? 0.1930 0.1799 0.1521 -0.0248 0.0080  0.0099  85  GLY   A N   
1824 C CA  . GLY   A 85  ? 0.1974 0.1881 0.1690 -0.0295 0.0101  -0.0041 85  GLY   A CA  
1825 C C   . GLY   A 85  ? 0.1900 0.1981 0.1604 -0.0235 0.0081  -0.0029 85  GLY   A C   
1826 O O   . GLY   A 85  ? 0.1839 0.2113 0.1657 -0.0277 0.0234  -0.0142 85  GLY   A O   
1830 N N   . HIS   A 86  ? 0.1888 0.1837 0.1532 -0.0216 0.0032  0.0011  86  HIS   A N   
1831 C CA  . HIS   A 86  ? 0.2062 0.1940 0.1519 -0.0232 0.0009  0.0011  86  HIS   A CA  
1832 C C   . HIS   A 86  ? 0.2283 0.2103 0.1392 -0.0221 -0.0048 0.0008  86  HIS   A C   
1833 O O   . HIS   A 86  ? 0.2358 0.2275 0.1607 -0.0189 0.0108  -0.0014 86  HIS   A O   
1834 C CB  . HIS   A 86  ? 0.2017 0.1863 0.1659 -0.0188 0.0071  -0.0006 86  HIS   A CB  
1835 C CG  . HIS   A 86  ? 0.1979 0.1913 0.1795 -0.0124 0.0128  0.0114  86  HIS   A CG  
1836 N ND1 . HIS   A 86  ? 0.2008 0.1933 0.2163 -0.0224 0.0088  0.0149  86  HIS   A ND1 
1837 C CD2 . HIS   A 86  ? 0.2017 0.1865 0.1788 0.0017  0.0138  0.0188  86  HIS   A CD2 
1838 C CE1 . HIS   A 86  ? 0.1994 0.1900 0.2100 -0.0167 0.0259  0.0160  86  HIS   A CE1 
1839 N NE2 . HIS   A 86  ? 0.2029 0.1879 0.1970 0.0002  0.0215  0.0300  86  HIS   A NE2 
1847 N N   . ASN   A 87  ? 0.2435 0.2173 0.1521 -0.0176 0.0138  -0.0091 87  ASN   A N   
1848 C CA  . ASN   A 87  ? 0.2570 0.2285 0.1603 -0.0153 0.0405  -0.0127 87  ASN   A CA  
1849 C C   . ASN   A 87  ? 0.2570 0.2441 0.2015 -0.0223 0.0615  -0.0001 87  ASN   A C   
1850 O O   . ASN   A 87  ? 0.2764 0.2619 0.2426 -0.0343 0.0864  -0.0087 87  ASN   A O   
1851 C CB  . ASN   A 87  ? 0.2747 0.2359 0.1658 -0.0012 0.0379  -0.0134 87  ASN   A CB  
1852 C CG  . ASN   A 87  ? 0.2826 0.2437 0.1747 0.0114  0.0533  -0.0075 87  ASN   A CG  
1853 O OD1 . ASN   A 87  ? 0.2945 0.2390 0.1832 0.0328  0.0505  0.0051  87  ASN   A OD1 
1854 N ND2 . ASN   A 87  ? 0.2880 0.2662 0.1960 0.0091  0.0570  -0.0059 87  ASN   A ND2 
1861 N N   . LEU   A 88  ? 0.2337 0.2384 0.1983 -0.0334 0.0424  0.0102  88  LEU   A N   
1862 C CA  . LEU   A 88  ? 0.2148 0.2337 0.2006 -0.0382 0.0454  0.0246  88  LEU   A CA  
1863 C C   . LEU   A 88  ? 0.2079 0.2380 0.1944 -0.0396 0.0365  0.0264  88  LEU   A C   
1864 O O   . LEU   A 88  ? 0.2129 0.2480 0.2315 -0.0420 0.0372  0.0391  88  LEU   A O   
1865 C CB  . LEU   A 88  ? 0.2143 0.2409 0.2235 -0.0441 0.0080  0.0295  88  LEU   A CB  
1866 C CG  . LEU   A 88  ? 0.2333 0.2530 0.2558 -0.0407 -0.0116 0.0296  88  LEU   A CG  
1867 C CD1 . LEU   A 88  ? 0.2446 0.2606 0.2487 -0.0364 -0.0191 0.0114  88  LEU   A CD1 
1868 C CD2 . LEU   A 88  ? 0.2448 0.2647 0.2988 -0.0333 -0.0140 0.0238  88  LEU   A CD2 
1880 N N   . ALA   A 89  ? 0.2077 0.2215 0.1710 -0.0382 0.0246  0.0057  89  ALA   A N   
1881 C CA  . ALA   A 89  ? 0.2118 0.2175 0.1594 -0.0347 0.0090  0.0174  89  ALA   A CA  
1882 C C   . ALA   A 89  ? 0.2178 0.2249 0.1608 -0.0196 -0.0014 0.0134  89  ALA   A C   
1883 O O   . ALA   A 89  ? 0.2107 0.2224 0.2034 -0.0296 -0.0074 -0.0117 89  ALA   A O   
1884 C CB  . ALA   A 89  ? 0.1975 0.2134 0.1453 -0.0273 0.0057  0.0222  89  ALA   A CB  
1890 N N   . LYS   A 90  ? 0.2317 0.2401 0.1550 -0.0298 -0.0202 0.0219  90  LYS   A N   
1891 C CA  . LYS   A 90  ? 0.2399 0.2534 0.1466 -0.0273 -0.0281 0.0151  90  LYS   A CA  
1892 C C   . LYS   A 90  ? 0.2136 0.2334 0.1407 -0.0300 -0.0253 0.0099  90  LYS   A C   
1893 O O   . LYS   A 90  ? 0.2138 0.2500 0.1884 -0.0369 -0.0290 0.0026  90  LYS   A O   
1894 C CB  . LYS   A 90  ? 0.2666 0.2881 0.2041 -0.0224 -0.0298 0.0364  90  LYS   A CB  
1895 C CG  . LYS   A 90  ? 0.2980 0.3169 0.2936 -0.0200 -0.0262 0.0438  90  LYS   A CG  
1896 C CD  . LYS   A 90  ? 0.3301 0.3424 0.3853 -0.0207 -0.0174 0.0494  90  LYS   A CD  
1897 C CE  . LYS   A 90  ? 0.3561 0.3681 0.4594 -0.0212 -0.0105 0.0471  90  LYS   A CE  
1898 N NZ  . LYS   A 90  ? 0.3691 0.3859 0.5095 -0.0232 -0.0061 0.0410  90  LYS   A NZ  
1912 N N   . HIS   A 91  ? 0.2026 0.2029 0.1172 -0.0263 -0.0292 0.0115  91  HIS   A N   
1913 C CA  . HIS   A 91  ? 0.1941 0.1829 0.1252 -0.0208 -0.0217 0.0169  91  HIS   A CA  
1914 C C   . HIS   A 91  ? 0.1703 0.1670 0.1195 -0.0168 -0.0084 0.0242  91  HIS   A C   
1915 O O   . HIS   A 91  ? 0.1664 0.1885 0.1602 -0.0184 0.0027  0.0226  91  HIS   A O   
1916 C CB  . HIS   A 91  ? 0.2068 0.2132 0.1879 0.0023  -0.0414 0.0171  91  HIS   A CB  
1917 C CG  . HIS   A 91  ? 0.2470 0.2657 0.2636 0.0101  -0.0603 0.0044  91  HIS   A CG  
1918 N ND1 . HIS   A 91  ? 0.2598 0.2935 0.3012 0.0124  -0.0669 -0.0180 91  HIS   A ND1 
1919 C CD2 . HIS   A 91  ? 0.2686 0.2857 0.2867 0.0209  -0.0707 0.0076  91  HIS   A CD2 
1920 C CE1 . HIS   A 91  ? 0.2690 0.3020 0.3166 0.0198  -0.0684 -0.0092 91  HIS   A CE1 
1921 N NE2 . HIS   A 91  ? 0.2771 0.2996 0.3083 0.0282  -0.0754 -0.0005 91  HIS   A NE2 
1929 N N   . CYS   A 92  ? 0.1579 0.1629 0.1375 -0.0205 -0.0110 0.0245  92  CYS   A N   
1930 C CA  . CYS   A 92  ? 0.1451 0.1588 0.1523 -0.0115 0.0026  0.0136  92  CYS   A CA  
1931 C C   . CYS   A 92  ? 0.1339 0.1511 0.1549 -0.0147 0.0035  0.0197  92  CYS   A C   
1932 O O   . CYS   A 92  ? 0.1453 0.1591 0.1671 -0.0186 -0.0035 0.0080  92  CYS   A O   
1933 C CB  . CYS   A 92  ? 0.1579 0.1607 0.1623 -0.0042 -0.0022 0.0092  92  CYS   A CB  
1934 S SG  . CYS   A 92  ? 0.1515 0.1484 0.1598 -0.0113 -0.0009 0.0102  92  CYS   A SG  
1940 N N   . LEU   A 93  ? 0.1332 0.1394 0.1675 -0.0119 0.0133  0.0149  93  LEU   A N   
1941 C CA  . LEU   A 93  ? 0.1274 0.1316 0.1641 -0.0067 0.0082  0.0152  93  LEU   A CA  
1942 C C   . LEU   A 93  ? 0.1310 0.1247 0.1572 -0.0037 0.0057  0.0099  93  LEU   A C   
1943 O O   . LEU   A 93  ? 0.1240 0.1421 0.1610 -0.0053 0.0028  0.0141  93  LEU   A O   
1944 C CB  . LEU   A 93  ? 0.1374 0.1370 0.1729 -0.0054 0.0009  0.0259  93  LEU   A CB  
1945 C CG  . LEU   A 93  ? 0.1431 0.1384 0.1674 -0.0057 0.0017  0.0176  93  LEU   A CG  
1946 C CD1 . LEU   A 93  ? 0.1491 0.1418 0.2047 -0.0024 0.0143  0.0078  93  LEU   A CD1 
1947 C CD2 . LEU   A 93  ? 0.1578 0.1343 0.1894 -0.0067 0.0008  0.0168  93  LEU   A CD2 
1959 N N   . HIS   A 94  ? 0.1249 0.1219 0.1519 -0.0021 0.0064  0.0133  94  HIS   A N   
1960 C CA  . HIS   A 94  ? 0.1262 0.1220 0.1555 -0.0050 0.0010  0.0084  94  HIS   A CA  
1961 C C   . HIS   A 94  ? 0.1218 0.1200 0.1593 -0.0056 0.0040  0.0121  94  HIS   A C   
1962 O O   . HIS   A 94  ? 0.1206 0.1416 0.1955 0.0020  0.0031  -0.0114 94  HIS   A O   
1963 C CB  . HIS   A 94  ? 0.1228 0.1246 0.1616 -0.0057 0.0025  0.0136  94  HIS   A CB  
1964 C CG  . HIS   A 94  ? 0.1265 0.1241 0.1622 -0.0077 -0.0050 0.0150  94  HIS   A CG  
1965 N ND1 . HIS   A 94  ? 0.1296 0.1214 0.1692 -0.0031 -0.0037 0.0141  94  HIS   A ND1 
1966 C CD2 . HIS   A 94  ? 0.1377 0.1340 0.1693 -0.0020 -0.0174 0.0080  94  HIS   A CD2 
1967 C CE1 . HIS   A 94  ? 0.1343 0.1235 0.1732 -0.0065 -0.0155 0.0050  94  HIS   A CE1 
1968 N NE2 . HIS   A 94  ? 0.1434 0.1304 0.1629 -0.0090 -0.0130 0.0040  94  HIS   A NE2 
1976 N N   . VAL   A 95  ? 0.1178 0.1164 0.1489 0.0002  0.0118  0.0037  95  VAL   A N   
1977 C CA  . VAL   A 95  ? 0.1316 0.1232 0.1472 -0.0037 0.0093  0.0151  95  VAL   A CA  
1978 C C   . VAL   A 95  ? 0.1295 0.1216 0.1333 -0.0164 0.0026  0.0146  95  VAL   A C   
1979 O O   . VAL   A 95  ? 0.1327 0.1357 0.1509 0.0124  0.0062  0.0091  95  VAL   A O   
1980 C CB  . VAL   A 95  ? 0.1333 0.1239 0.1656 -0.0105 0.0067  0.0099  95  VAL   A CB  
1981 C CG1 . VAL   A 95  ? 0.1475 0.1356 0.1774 -0.0147 0.0066  0.0036  95  VAL   A CG1 
1982 C CG2 . VAL   A 95  ? 0.1400 0.1321 0.1676 -0.0093 0.0067  0.0169  95  VAL   A CG2 
1992 N N   . VAL   A 96  ? 0.1338 0.1280 0.1250 -0.0063 0.0079  0.0155  96  VAL   A N   
1993 C CA  . VAL   A 96  ? 0.1437 0.1278 0.1383 -0.0006 0.0114  0.0153  96  VAL   A CA  
1994 C C   . VAL   A 96  ? 0.1469 0.1353 0.1490 -0.0034 0.0093  0.0141  96  VAL   A C   
1995 O O   . VAL   A 96  ? 0.1590 0.1386 0.1686 -0.0054 0.0200  -0.0079 96  VAL   A O   
1996 C CB  . VAL   A 96  ? 0.1476 0.1348 0.1525 -0.0023 0.0152  0.0169  96  VAL   A CB  
1997 C CG1 . VAL   A 96  ? 0.1557 0.1389 0.1444 -0.0051 0.0195  0.0095  96  VAL   A CG1 
1998 C CG2 . VAL   A 96  ? 0.1454 0.1481 0.1769 -0.0139 0.0115  0.0105  96  VAL   A CG2 
2008 N N   A GLY   A 97  ? 0.1351 0.1338 0.1534 -0.0048 0.0124  0.0097  97  GLY   A N   
2009 N N   B GLY   A 97  ? 0.1570 0.1434 0.1499 0.0003  0.0047  0.0103  97  GLY   A N   
2010 C CA  A GLY   A 97  ? 0.1459 0.1519 0.1461 -0.0040 -0.0069 0.0104  97  GLY   A CA  
2011 C CA  B GLY   A 97  ? 0.1693 0.1523 0.1556 0.0038  -0.0017 0.0101  97  GLY   A CA  
2012 C C   A GLY   A 97  ? 0.1407 0.1631 0.1328 -0.0081 0.0042  0.0071  97  GLY   A C   
2013 C C   B GLY   A 97  ? 0.1797 0.1609 0.1629 0.0070  -0.0043 0.0087  97  GLY   A C   
2014 O O   A GLY   A 97  ? 0.1605 0.1662 0.1614 -0.0119 0.0072  0.0081  97  GLY   A O   
2015 O O   B GLY   A 97  ? 0.1808 0.1578 0.1639 0.0131  -0.0072 0.0066  97  GLY   A O   
2022 N N   A PRO   A 98  ? 0.1548 0.1666 0.1139 -0.0059 -0.0067 0.0185  98  PRO   A N   
2023 N N   B PRO   A 98  ? 0.1918 0.1709 0.1693 0.0049  -0.0056 0.0093  98  PRO   A N   
2024 C CA  A PRO   A 98  ? 0.1695 0.1887 0.1345 -0.0102 -0.0018 0.0051  98  PRO   A CA  
2025 C CA  B PRO   A 98  ? 0.2007 0.1816 0.1757 0.0035  -0.0041 0.0066  98  PRO   A CA  
2026 C C   A PRO   A 98  ? 0.1713 0.1925 0.1275 -0.0130 -0.0006 0.0217  98  PRO   A C   
2027 C C   B PRO   A 98  ? 0.2088 0.1932 0.1832 0.0041  -0.0051 0.0080  98  PRO   A C   
2028 O O   A PRO   A 98  ? 0.1673 0.1711 0.1570 -0.0109 -0.0012 0.0163  98  PRO   A O   
2029 O O   B PRO   A 98  ? 0.2095 0.1908 0.1861 0.0065  -0.0081 0.0047  98  PRO   A O   
2030 C CB  A PRO   A 98  ? 0.1869 0.1935 0.1242 0.0050  -0.0043 -0.0134 98  PRO   A CB  
2031 C CB  B PRO   A 98  ? 0.2015 0.1793 0.1747 0.0036  -0.0045 0.0057  98  PRO   A CB  
2032 C CG  A PRO   A 98  ? 0.1875 0.1817 0.1431 -0.0009 -0.0045 -0.0139 98  PRO   A CG  
2033 C CG  B PRO   A 98  ? 0.1989 0.1755 0.1747 0.0018  -0.0046 0.0059  98  PRO   A CG  
2034 C CD  A PRO   A 98  ? 0.1675 0.1641 0.1283 0.0014  -0.0055 0.0056  98  PRO   A CD  
2035 C CD  B PRO   A 98  ? 0.1955 0.1717 0.1712 0.0038  -0.0042 0.0090  98  PRO   A CD  
2050 N N   A ASN   A 99  ? 0.1800 0.2196 0.1409 -0.0154 0.0023  0.0432  99  ASN   A N   
2051 N N   B ASN   A 99  ? 0.2168 0.2090 0.1950 0.0029  -0.0052 0.0122  99  ASN   A N   
2052 C CA  A ASN   A 99  ? 0.2007 0.2379 0.1359 -0.0215 0.0015  0.0611  99  ASN   A CA  
2053 C CA  B ASN   A 99  ? 0.2281 0.2254 0.2094 0.0028  -0.0066 0.0124  99  ASN   A CA  
2054 C C   A ASN   A 99  ? 0.2238 0.2845 0.1229 -0.0338 0.0099  0.0726  99  ASN   A C   
2055 C C   B ASN   A 99  ? 0.2429 0.2435 0.2214 -0.0019 -0.0064 0.0157  99  ASN   A C   
2056 O O   A ASN   A 99  ? 0.2304 0.3180 0.1351 -0.0280 -0.0102 0.0603  99  ASN   A O   
2057 O O   B ASN   A 99  ? 0.2438 0.2455 0.2200 -0.0028 -0.0089 0.0166  99  ASN   A O   
2058 C CB  A ASN   A 99  ? 0.2010 0.2234 0.1835 -0.0182 -0.0209 0.0608  99  ASN   A CB  
2059 C CB  B ASN   A 99  ? 0.2251 0.2267 0.2166 0.0062  -0.0084 0.0116  99  ASN   A CB  
2060 C CG  A ASN   A 99  ? 0.2026 0.2204 0.2245 -0.0172 -0.0320 0.0520  99  ASN   A CG  
2061 C CG  B ASN   A 99  ? 0.2225 0.2290 0.2244 0.0088  -0.0078 0.0095  99  ASN   A CG  
2062 O OD1 A ASN   A 99  ? 0.2221 0.2323 0.2359 -0.0093 -0.0422 0.0521  99  ASN   A OD1 
2063 O OD1 B ASN   A 99  ? 0.2234 0.2301 0.2235 0.0111  -0.0071 0.0074  99  ASN   A OD1 
2064 N ND2 A ASN   A 99  ? 0.2061 0.2051 0.2555 -0.0143 -0.0320 0.0521  99  ASN   A ND2 
2065 N ND2 B ASN   A 99  ? 0.2223 0.2284 0.2307 0.0087  -0.0079 0.0111  99  ASN   A ND2 
2078 N N   A VAL   A 100 ? 0.2394 0.2940 0.1266 -0.0532 -0.0193 0.0653  100 VAL   A N   
2079 N N   B VAL   A 100 ? 0.2565 0.2604 0.2352 -0.0064 -0.0073 0.0166  100 VAL   A N   
2080 C CA  A VAL   A 100 ? 0.2660 0.3221 0.1529 -0.0609 -0.0238 0.0551  100 VAL   A CA  
2081 C CA  B VAL   A 100 ? 0.2702 0.2800 0.2553 -0.0105 -0.0070 0.0187  100 VAL   A CA  
2082 C C   A VAL   A 100 ? 0.2773 0.3434 0.1447 -0.0657 -0.0346 0.0784  100 VAL   A C   
2083 C C   B VAL   A 100 ? 0.2817 0.2977 0.2685 -0.0113 -0.0092 0.0260  100 VAL   A C   
2084 O O   A VAL   A 100 ? 0.2884 0.3580 0.1869 -0.0644 -0.0098 0.0731  100 VAL   A O   
2085 O O   B VAL   A 100 ? 0.2833 0.3028 0.2765 -0.0113 -0.0059 0.0258  100 VAL   A O   
2086 C CB  A VAL   A 100 ? 0.2883 0.3265 0.1879 -0.0654 -0.0290 0.0371  100 VAL   A CB  
2087 C CB  B VAL   A 100 ? 0.2733 0.2814 0.2650 -0.0129 -0.0061 0.0153  100 VAL   A CB  
2088 C CG1 A VAL   A 100 ? 0.2917 0.3343 0.2061 -0.0651 -0.0254 0.0319  100 VAL   A CG1 
2089 C CG1 B VAL   A 100 ? 0.2733 0.2820 0.2708 -0.0143 -0.0066 0.0148  100 VAL   A CG1 
2090 C CG2 A VAL   A 100 ? 0.3051 0.3310 0.2024 -0.0695 -0.0268 0.0247  100 VAL   A CG2 
2091 C CG2 B VAL   A 100 ? 0.2761 0.2826 0.2694 -0.0149 -0.0042 0.0131  100 VAL   A CG2 
2110 N N   A ASN   A 101 ? 0.2850 0.3525 0.1875 -0.0652 -0.0500 0.1130  101 ASN   A N   
2111 N N   B ASN   A 101 ? 0.2913 0.3087 0.2802 -0.0114 -0.0141 0.0335  101 ASN   A N   
2112 C CA  A ASN   A 101 ? 0.3117 0.3662 0.2185 -0.0671 -0.0512 0.1336  101 ASN   A CA  
2113 C CA  B ASN   A 101 ? 0.3021 0.3184 0.2900 -0.0112 -0.0181 0.0386  101 ASN   A CA  
2114 C C   A ASN   A 101 ? 0.3374 0.3930 0.2339 -0.0702 -0.0172 0.1623  101 ASN   A C   
2115 C C   B ASN   A 101 ? 0.3117 0.3317 0.3038 -0.0125 -0.0153 0.0410  101 ASN   A C   
2116 O O   A ASN   A 101 ? 0.3590 0.4010 0.2844 -0.0644 -0.0231 0.1556  101 ASN   A O   
2117 O O   B ASN   A 101 ? 0.3123 0.3302 0.2979 -0.0129 -0.0167 0.0468  101 ASN   A O   
2118 C CB  A ASN   A 101 ? 0.3150 0.3515 0.2275 -0.0568 -0.0799 0.1101  101 ASN   A CB  
2119 C CB  B ASN   A 101 ? 0.3034 0.3134 0.2864 -0.0094 -0.0226 0.0398  101 ASN   A CB  
2120 C CG  A ASN   A 101 ? 0.3173 0.3367 0.2244 -0.0561 -0.0881 0.0768  101 ASN   A CG  
2121 C CG  B ASN   A 101 ? 0.3043 0.3080 0.2798 -0.0085 -0.0241 0.0386  101 ASN   A CG  
2122 O OD1 A ASN   A 101 ? 0.3138 0.3447 0.2452 -0.0445 -0.0856 0.0401  101 ASN   A OD1 
2123 O OD1 B ASN   A 101 ? 0.3040 0.3063 0.2754 -0.0089 -0.0223 0.0382  101 ASN   A OD1 
2124 N ND2 A ASN   A 101 ? 0.3193 0.3195 0.2235 -0.0645 -0.0839 0.0797  101 ASN   A ND2 
2125 N ND2 B ASN   A 101 ? 0.3056 0.3058 0.2796 -0.0080 -0.0263 0.0379  101 ASN   A ND2 
2138 N N   A LYS   A 102 ? 0.3406 0.4274 0.2621 -0.0899 0.0052  0.1642  102 LYS   A N   
2139 N N   B LYS   A 102 ? 0.3201 0.3452 0.3236 -0.0144 -0.0103 0.0337  102 LYS   A N   
2140 C CA  A LYS   A 102 ? 0.3552 0.4573 0.2662 -0.0911 0.0092  0.1519  102 LYS   A CA  
2141 C CA  B LYS   A 102 ? 0.3295 0.3570 0.3407 -0.0153 -0.0057 0.0251  102 LYS   A CA  
2142 C C   A LYS   A 102 ? 0.3683 0.4782 0.2489 -0.0761 0.0017  0.1396  102 LYS   A C   
2143 C C   B LYS   A 102 ? 0.3352 0.3631 0.3433 -0.0126 -0.0023 0.0223  102 LYS   A C   
2144 O O   A LYS   A 102 ? 0.3768 0.4937 0.2522 -0.0685 0.0070  0.1312  102 LYS   A O   
2145 O O   B LYS   A 102 ? 0.3372 0.3657 0.3465 -0.0122 -0.0018 0.0226  102 LYS   A O   
2146 C CB  A LYS   A 102 ? 0.3639 0.4652 0.3199 -0.1017 0.0065  0.1314  102 LYS   A CB  
2147 C CB  B LYS   A 102 ? 0.3338 0.3620 0.3538 -0.0182 -0.0042 0.0193  102 LYS   A CB  
2148 C CG  A LYS   A 102 ? 0.3728 0.4689 0.3646 -0.1094 -0.0015 0.1036  102 LYS   A CG  
2149 C CG  B LYS   A 102 ? 0.3379 0.3653 0.3635 -0.0208 -0.0032 0.0139  102 LYS   A CG  
2150 C CD  A LYS   A 102 ? 0.3838 0.4745 0.4066 -0.1133 -0.0126 0.0750  102 LYS   A CD  
2151 C CD  B LYS   A 102 ? 0.3416 0.3683 0.3709 -0.0225 -0.0015 0.0089  102 LYS   A CD  
2152 C CE  A LYS   A 102 ? 0.3933 0.4790 0.4387 -0.1152 -0.0219 0.0551  102 LYS   A CE  
2153 C CE  B LYS   A 102 ? 0.3444 0.3704 0.3759 -0.0233 0.0004  0.0052  102 LYS   A CE  
2154 N NZ  A LYS   A 102 ? 0.3990 0.4809 0.4570 -0.1206 -0.0217 0.0423  102 LYS   A NZ  
2155 N NZ  B LYS   A 102 ? 0.3460 0.3713 0.3779 -0.0239 0.0027  0.0027  102 LYS   A NZ  
2182 N N   A GLY   A 103 ? 0.3687 0.4862 0.2385 -0.0633 -0.0147 0.1137  103 GLY   A N   
2183 N N   B GLY   A 103 ? 0.3382 0.3661 0.3424 -0.0089 -0.0011 0.0182  103 GLY   A N   
2184 C CA  A GLY   A 103 ? 0.3700 0.4869 0.2273 -0.0535 -0.0175 0.0870  103 GLY   A CA  
2185 C CA  B GLY   A 103 ? 0.3415 0.3677 0.3371 -0.0059 0.0003  0.0157  103 GLY   A CA  
2186 C C   A GLY   A 103 ? 0.3654 0.4867 0.2247 -0.0486 -0.0112 0.0533  103 GLY   A C   
2187 C C   B GLY   A 103 ? 0.3436 0.3692 0.3341 -0.0033 0.0021  0.0126  103 GLY   A C   
2188 O O   A GLY   A 103 ? 0.3762 0.4959 0.2464 -0.0447 -0.0104 0.0333  103 GLY   A O   
2189 O O   B GLY   A 103 ? 0.3443 0.3701 0.3353 -0.0031 0.0019  0.0110  103 GLY   A O   
2196 N N   A GLU   A 104 ? 0.3429 0.4708 0.1729 -0.0525 -0.0073 0.0423  104 GLU   A N   
2197 N N   B GLU   A 104 ? 0.3439 0.3683 0.3266 -0.0009 0.0034  0.0107  104 GLU   A N   
2198 C CA  A GLU   A 104 ? 0.3158 0.4506 0.1595 -0.0637 -0.0027 0.0321  104 GLU   A CA  
2199 C CA  B GLU   A 104 ? 0.3435 0.3666 0.3203 0.0010  0.0048  0.0080  104 GLU   A CA  
2200 C C   A GLU   A 104 ? 0.3097 0.4562 0.1652 -0.0676 0.0091  0.0122  104 GLU   A C   
2201 C C   B GLU   A 104 ? 0.3464 0.3686 0.3243 -0.0013 0.0052  0.0058  104 GLU   A C   
2202 O O   A GLU   A 104 ? 0.3030 0.4556 0.1903 -0.0697 -0.0009 0.0088  104 GLU   A O   
2203 O O   B GLU   A 104 ? 0.3460 0.3678 0.3192 -0.0009 0.0071  0.0082  104 GLU   A O   
2204 C CB  A GLU   A 104 ? 0.2910 0.4253 0.1430 -0.0704 0.0070  0.0477  104 GLU   A CB  
2205 C CB  B GLU   A 104 ? 0.3399 0.3636 0.3132 0.0049  0.0058  0.0056  104 GLU   A CB  
2206 C CG  A GLU   A 104 ? 0.2754 0.4048 0.1568 -0.0668 -0.0020 0.0615  104 GLU   A CG  
2207 C CG  B GLU   A 104 ? 0.3366 0.3605 0.3081 0.0092  0.0064  0.0026  104 GLU   A CG  
2208 C CD  A GLU   A 104 ? 0.2588 0.3858 0.1540 -0.0637 -0.0014 0.0671  104 GLU   A CD  
2209 C CD  B GLU   A 104 ? 0.3339 0.3582 0.3068 0.0124  0.0068  0.0003  104 GLU   A CD  
2210 O OE1 A GLU   A 104 ? 0.2405 0.3720 0.1309 -0.0605 -0.0036 0.0641  104 GLU   A OE1 
2211 O OE1 B GLU   A 104 ? 0.3324 0.3573 0.3050 0.0148  0.0077  -0.0015 104 GLU   A OE1 
2212 O OE2 A GLU   A 104 ? 0.2716 0.3785 0.1825 -0.0671 0.0008  0.0784  104 GLU   A OE2 
2213 O OE2 B GLU   A 104 ? 0.3339 0.3577 0.3088 0.0131  0.0092  -0.0023 104 GLU   A OE2 
2226 N N   A ASP   A 105 ? 0.3122 0.4604 0.1822 -0.0679 0.0224  -0.0157 105 ASP   A N   
2227 N N   B ASP   A 105 ? 0.3495 0.3714 0.3343 -0.0040 0.0045  -0.0005 105 ASP   A N   
2228 C CA  A ASP   A 105 ? 0.3148 0.4615 0.2116 -0.0578 0.0299  -0.0521 105 ASP   A CA  
2229 C CA  B ASP   A 105 ? 0.3521 0.3734 0.3437 -0.0061 0.0027  -0.0080 105 ASP   A CA  
2230 C C   A ASP   A 105 ? 0.2836 0.4394 0.1918 -0.0637 0.0246  -0.0620 105 ASP   A C   
2231 C C   B ASP   A 105 ? 0.3466 0.3675 0.3291 -0.0106 0.0018  -0.0090 105 ASP   A C   
2232 O O   A ASP   A 105 ? 0.2593 0.4218 0.1446 -0.0581 0.0303  -0.0894 105 ASP   A O   
2233 O O   B ASP   A 105 ? 0.3461 0.3678 0.3260 -0.0098 0.0006  -0.0084 105 ASP   A O   
2234 C CB  A ASP   A 105 ? 0.3447 0.4859 0.2753 -0.0445 0.0374  -0.0713 105 ASP   A CB  
2235 C CB  B ASP   A 105 ? 0.3595 0.3800 0.3683 -0.0041 0.0021  -0.0151 105 ASP   A CB  
2236 C CG  A ASP   A 105 ? 0.3713 0.5025 0.3333 -0.0332 0.0378  -0.0882 105 ASP   A CG  
2237 C CG  B ASP   A 105 ? 0.3657 0.3853 0.3902 -0.0028 0.0009  -0.0213 105 ASP   A CG  
2238 O OD1 A ASP   A 105 ? 0.3793 0.5087 0.3305 -0.0345 0.0380  -0.1040 105 ASP   A OD1 
2239 O OD1 B ASP   A 105 ? 0.3677 0.3869 0.3948 -0.0032 -0.0004 -0.0238 105 ASP   A OD1 
2240 O OD2 A ASP   A 105 ? 0.3888 0.5095 0.3862 -0.0284 0.0387  -0.0845 105 ASP   A OD2 
2241 O OD2 B ASP   A 105 ? 0.3692 0.3878 0.4032 -0.0027 0.0003  -0.0228 105 ASP   A OD2 
2250 N N   A ILE   A 106 ? 0.2725 0.4267 0.2195 -0.0677 0.0023  -0.0577 106 ILE   A N   
2251 N N   B ILE   A 106 ? 0.3407 0.3601 0.3191 -0.0155 0.0007  -0.0109 106 ILE   A N   
2252 C CA  A ILE   A 106 ? 0.2511 0.4113 0.2404 -0.0750 -0.0187 -0.0695 106 ILE   A CA  
2253 C CA  B ILE   A 106 ? 0.3332 0.3513 0.3116 -0.0204 0.0001  -0.0142 106 ILE   A CA  
2254 C C   A ILE   A 106 ? 0.2391 0.3838 0.2456 -0.0881 -0.0164 -0.0881 106 ILE   A C   
2255 C C   B ILE   A 106 ? 0.3245 0.3385 0.3068 -0.0265 0.0057  -0.0198 106 ILE   A C   
2256 O O   A ILE   A 106 ? 0.2177 0.3692 0.2459 -0.0936 0.0016  -0.0936 106 ILE   A O   
2257 O O   B ILE   A 106 ? 0.3248 0.3374 0.3022 -0.0261 0.0065  -0.0212 106 ILE   A O   
2258 C CB  A ILE   A 106 ? 0.2542 0.4239 0.2879 -0.0622 -0.0391 -0.0429 106 ILE   A CB  
2259 C CB  B ILE   A 106 ? 0.3344 0.3545 0.3148 -0.0186 -0.0053 -0.0104 106 ILE   A CB  
2260 C CG1 A ILE   A 106 ? 0.2480 0.4263 0.3181 -0.0463 -0.0442 -0.0238 106 ILE   A CG1 
2261 C CG1 B ILE   A 106 ? 0.3334 0.3548 0.3178 -0.0167 -0.0080 -0.0077 106 ILE   A CG1 
2262 C CG2 A ILE   A 106 ? 0.2638 0.4295 0.3025 -0.0586 -0.0466 -0.0385 106 ILE   A CG2 
2263 C CG2 B ILE   A 106 ? 0.3361 0.3561 0.3164 -0.0181 -0.0071 -0.0095 106 ILE   A CG2 
2264 C CD1 A ILE   A 106 ? 0.2473 0.4239 0.3418 -0.0350 -0.0365 -0.0152 106 ILE   A CD1 
2265 C CD1 B ILE   A 106 ? 0.3327 0.3541 0.3196 -0.0155 -0.0084 -0.0061 106 ILE   A CD1 
2288 N N   A GLN   A 107 ? 0.2615 0.3675 0.2743 -0.0849 -0.0014 -0.1004 107 GLN   A N   
2289 N N   B GLN   A 107 ? 0.3152 0.3257 0.3131 -0.0326 0.0124  -0.0244 107 GLN   A N   
2290 C CA  A GLN   A 107 ? 0.2898 0.3520 0.3612 -0.0712 0.0136  -0.0968 107 GLN   A CA  
2291 C CA  B GLN   A 107 ? 0.3049 0.3124 0.3257 -0.0373 0.0195  -0.0310 107 GLN   A CA  
2292 C C   A GLN   A 107 ? 0.2592 0.2956 0.3342 -0.0588 0.0345  -0.0752 107 GLN   A C   
2293 C C   B GLN   A 107 ? 0.2702 0.2823 0.2934 -0.0440 0.0297  -0.0428 107 GLN   A C   
2294 O O   A GLN   A 107 ? 0.2610 0.2851 0.3857 -0.0472 0.0502  -0.0776 107 GLN   A O   
2295 O O   B GLN   A 107 ? 0.2725 0.2834 0.3022 -0.0436 0.0318  -0.0394 107 GLN   A O   
2296 C CB  A GLN   A 107 ? 0.3423 0.3893 0.4749 -0.0766 -0.0046 -0.1015 107 GLN   A CB  
2297 C CB  B GLN   A 107 ? 0.3273 0.3276 0.3718 -0.0361 0.0144  -0.0230 107 GLN   A CB  
2298 C CG  A GLN   A 107 ? 0.3946 0.4263 0.5924 -0.0780 -0.0177 -0.0970 107 GLN   A CG  
2299 C CG  B GLN   A 107 ? 0.3463 0.3402 0.4169 -0.0354 0.0101  -0.0158 107 GLN   A CG  
2300 C CD  A GLN   A 107 ? 0.4338 0.4536 0.6924 -0.0780 -0.0233 -0.0864 107 GLN   A CD  
2301 C CD  B GLN   A 107 ? 0.3621 0.3510 0.4545 -0.0333 0.0067  -0.0085 107 GLN   A CD  
2302 O OE1 A GLN   A 107 ? 0.4453 0.4632 0.7320 -0.0794 -0.0240 -0.0821 107 GLN   A OE1 
2303 O OE1 B GLN   A 107 ? 0.3672 0.3549 0.4661 -0.0328 0.0068  -0.0044 107 GLN   A OE1 
2304 N NE2 A GLN   A 107 ? 0.4495 0.4633 0.7245 -0.0788 -0.0271 -0.0860 107 GLN   A NE2 
2305 N NE2 B GLN   A 107 ? 0.3679 0.3549 0.4679 -0.0328 0.0045  -0.0068 107 GLN   A NE2 
2322 N N   . LEU   A 108 ? 0.2323 0.2500 0.2650 -0.0500 0.0374  -0.0590 108 LEU   A N   
2323 C CA  . LEU   A 108 ? 0.1997 0.1939 0.2331 -0.0223 0.0300  -0.0218 108 LEU   A CA  
2324 C C   . LEU   A 108 ? 0.1731 0.1578 0.2211 -0.0063 0.0190  -0.0059 108 LEU   A C   
2325 O O   . LEU   A 108 ? 0.1747 0.1570 0.2471 0.0010  0.0287  0.0003  108 LEU   A O   
2326 C CB  . LEU   A 108 ? 0.2033 0.2029 0.2155 -0.0237 0.0358  -0.0196 108 LEU   A CB  
2327 C CG  . LEU   A 108 ? 0.2165 0.2288 0.2446 -0.0212 0.0393  -0.0265 108 LEU   A CG  
2328 C CD1 . LEU   A 108 ? 0.2335 0.2357 0.2436 -0.0257 0.0514  -0.0282 108 LEU   A CD1 
2329 C CD2 . LEU   A 108 ? 0.2185 0.2562 0.2809 -0.0100 0.0363  -0.0105 108 LEU   A CD2 
2342 N N   . LEU   A 109 ? 0.1547 0.1613 0.2252 -0.0007 0.0109  0.0128  109 LEU   A N   
2343 C CA  . LEU   A 109 ? 0.1528 0.1527 0.2103 0.0062  -0.0036 0.0130  109 LEU   A CA  
2344 C C   . LEU   A 109 ? 0.1390 0.1439 0.1899 -0.0058 0.0014  0.0081  109 LEU   A C   
2345 O O   . LEU   A 109 ? 0.1537 0.1322 0.2053 -0.0019 0.0002  0.0042  109 LEU   A O   
2346 C CB  . LEU   A 109 ? 0.1531 0.1553 0.2300 0.0104  -0.0137 0.0315  109 LEU   A CB  
2347 C CG  . LEU   A 109 ? 0.1543 0.1647 0.2385 0.0080  0.0062  0.0341  109 LEU   A CG  
2348 C CD1 . LEU   A 109 ? 0.1578 0.1539 0.2533 0.0024  0.0177  0.0125  109 LEU   A CD1 
2349 C CD2 . LEU   A 109 ? 0.1532 0.1880 0.2590 0.0047  0.0044  0.0385  109 LEU   A CD2 
2361 N N   . LYS   A 110 ? 0.1405 0.1388 0.2022 -0.0067 -0.0012 0.0033  110 LYS   A N   
2362 C CA  . LYS   A 110 ? 0.1434 0.1325 0.2030 -0.0054 -0.0080 0.0102  110 LYS   A CA  
2363 C C   . LYS   A 110 ? 0.1427 0.1265 0.1957 -0.0057 -0.0016 -0.0027 110 LYS   A C   
2364 O O   . LYS   A 110 ? 0.1404 0.1302 0.2076 -0.0053 0.0024  -0.0098 110 LYS   A O   
2365 C CB  . LYS   A 110 ? 0.1542 0.1444 0.2195 -0.0045 -0.0161 -0.0072 110 LYS   A CB  
2366 C CG  . LYS   A 110 ? 0.1560 0.1446 0.2351 -0.0022 -0.0197 -0.0117 110 LYS   A CG  
2367 C CD  . LYS   A 110 ? 0.1575 0.1518 0.2510 -0.0102 -0.0146 -0.0127 110 LYS   A CD  
2368 C CE  . LYS   A 110 ? 0.1700 0.1532 0.2640 -0.0119 0.0050  -0.0118 110 LYS   A CE  
2369 N NZ  . LYS   A 110 ? 0.1699 0.1545 0.2737 -0.0155 0.0128  -0.0114 110 LYS   A NZ  
2383 N N   . SER   A 111 ? 0.1410 0.1325 0.1879 0.0017  -0.0003 0.0052  111 SER   A N   
2384 C CA  . SER   A 111 ? 0.1346 0.1405 0.2126 0.0010  0.0040  0.0054  111 SER   A CA  
2385 C C   . SER   A 111 ? 0.1321 0.1284 0.2077 -0.0068 0.0037  0.0111  111 SER   A C   
2386 O O   . SER   A 111 ? 0.1480 0.1235 0.2160 -0.0077 0.0050  0.0091  111 SER   A O   
2387 C CB  . SER   A 111 ? 0.1610 0.1671 0.2332 -0.0023 0.0189  -0.0135 111 SER   A CB  
2388 O OG  . SER   A 111 ? 0.2118 0.1869 0.2366 0.0037  0.0254  -0.0199 111 SER   A OG  
2394 N N   . ALA   A 112 ? 0.1374 0.1186 0.1995 -0.0061 0.0102  0.0051  112 ALA   A N   
2395 C CA  . ALA   A 112 ? 0.1399 0.1189 0.1933 -0.0031 0.0114  0.0024  112 ALA   A CA  
2396 C C   . ALA   A 112 ? 0.1325 0.1174 0.1872 0.0032  0.0063  0.0047  112 ALA   A C   
2397 O O   . ALA   A 112 ? 0.1419 0.1195 0.1957 -0.0111 0.0059  0.0068  112 ALA   A O   
2398 C CB  . ALA   A 112 ? 0.1536 0.1253 0.2050 -0.0071 0.0100  0.0153  112 ALA   A CB  
2404 N N   . TYR   A 113 ? 0.1257 0.1247 0.1951 -0.0015 0.0038  0.0133  113 TYR   A N   
2405 C CA  . TYR   A 113 ? 0.1244 0.1223 0.1893 -0.0024 0.0077  0.0084  113 TYR   A CA  
2406 C C   . TYR   A 113 ? 0.1217 0.1227 0.1892 -0.0088 0.0102  0.0066  113 TYR   A C   
2407 O O   . TYR   A 113 ? 0.1331 0.1264 0.2036 -0.0045 0.0103  0.0025  113 TYR   A O   
2408 C CB  . TYR   A 113 ? 0.1211 0.1344 0.2055 -0.0042 -0.0027 0.0167  113 TYR   A CB  
2409 C CG  . TYR   A 113 ? 0.1282 0.1398 0.1909 -0.0135 0.0097  0.0231  113 TYR   A CG  
2410 C CD1 . TYR   A 113 ? 0.1254 0.1441 0.1905 -0.0005 0.0040  0.0208  113 TYR   A CD1 
2411 C CD2 . TYR   A 113 ? 0.1357 0.1437 0.1883 -0.0112 0.0021  0.0213  113 TYR   A CD2 
2412 C CE1 . TYR   A 113 ? 0.1350 0.1490 0.1938 0.0004  0.0015  0.0231  113 TYR   A CE1 
2413 C CE2 . TYR   A 113 ? 0.1317 0.1511 0.1886 -0.0092 -0.0036 0.0177  113 TYR   A CE2 
2414 C CZ  . TYR   A 113 ? 0.1306 0.1525 0.1841 0.0001  0.0101  0.0242  113 TYR   A CZ  
2415 O OH  . TYR   A 113 ? 0.1320 0.1581 0.2113 0.0110  0.0116  0.0348  113 TYR   A OH  
2425 N N   . GLU   A 114 ? 0.1268 0.1220 0.1979 0.0006  0.0161  0.0163  114 GLU   A N   
2426 C CA  . GLU   A 114 ? 0.1309 0.1193 0.2069 0.0063  0.0052  0.0187  114 GLU   A CA  
2427 C C   . GLU   A 114 ? 0.1214 0.1249 0.2015 0.0041  0.0128  0.0144  114 GLU   A C   
2428 O O   . GLU   A 114 ? 0.1432 0.1287 0.2024 0.0062  0.0023  0.0113  114 GLU   A O   
2429 C CB  . GLU   A 114 ? 0.1312 0.1252 0.2032 -0.0038 -0.0004 0.0110  114 GLU   A CB  
2430 C CG  . GLU   A 114 ? 0.1374 0.1283 0.2101 0.0042  0.0035  -0.0005 114 GLU   A CG  
2431 C CD  . GLU   A 114 ? 0.1508 0.1328 0.2236 -0.0027 0.0019  0.0055  114 GLU   A CD  
2432 O OE1 . GLU   A 114 ? 0.1519 0.1313 0.2354 -0.0072 0.0139  -0.0123 114 GLU   A OE1 
2433 O OE2 . GLU   A 114 ? 0.1693 0.1377 0.2472 -0.0102 0.0120  -0.0122 114 GLU   A OE2 
2440 N N   . ASN   A 115 ? 0.1233 0.1241 0.1864 -0.0035 0.0116  0.0090  115 ASN   A N   
2441 C CA  . ASN   A 115 ? 0.1267 0.1334 0.1955 -0.0055 0.0104  0.0115  115 ASN   A CA  
2442 C C   . ASN   A 115 ? 0.1306 0.1269 0.1865 -0.0077 0.0070  0.0095  115 ASN   A C   
2443 O O   . ASN   A 115 ? 0.1318 0.1445 0.1880 -0.0128 0.0111  0.0170  115 ASN   A O   
2444 C CB  . ASN   A 115 ? 0.1362 0.1357 0.1852 -0.0070 0.0099  0.0085  115 ASN   A CB  
2445 C CG  . ASN   A 115 ? 0.1401 0.1541 0.2036 -0.0166 0.0146  0.0053  115 ASN   A CG  
2446 O OD1 . ASN   A 115 ? 0.1430 0.2523 0.2270 -0.0170 0.0178  0.0241  115 ASN   A OD1 
2447 N ND2 . ASN   A 115 ? 0.1453 0.1428 0.2017 -0.0138 0.0258  0.0158  115 ASN   A ND2 
2454 N N   . PHE   A 116 ? 0.1210 0.1307 0.1971 -0.0031 0.0097  0.0166  116 PHE   A N   
2455 C CA  . PHE   A 116 ? 0.1307 0.1362 0.1817 0.0011  0.0141  0.0163  116 PHE   A CA  
2456 C C   . PHE   A 116 ? 0.1251 0.1349 0.1888 -0.0046 0.0115  0.0192  116 PHE   A C   
2457 O O   . PHE   A 116 ? 0.1337 0.1485 0.1980 0.0025  0.0100  0.0261  116 PHE   A O   
2458 C CB  . PHE   A 116 ? 0.1290 0.1297 0.2088 -0.0044 0.0196  0.0155  116 PHE   A CB  
2459 C CG  . PHE   A 116 ? 0.1313 0.1222 0.1874 -0.0053 0.0111  0.0030  116 PHE   A CG  
2460 C CD1 . PHE   A 116 ? 0.1330 0.1235 0.1933 -0.0078 0.0108  0.0133  116 PHE   A CD1 
2461 C CD2 . PHE   A 116 ? 0.1342 0.1295 0.2008 -0.0040 0.0118  0.0082  116 PHE   A CD2 
2462 C CE1 . PHE   A 116 ? 0.1394 0.1230 0.1973 -0.0122 0.0102  0.0107  116 PHE   A CE1 
2463 C CE2 . PHE   A 116 ? 0.1365 0.1254 0.2084 -0.0026 0.0163  0.0053  116 PHE   A CE2 
2464 C CZ  . PHE   A 116 ? 0.1394 0.1203 0.1969 -0.0012 0.0053  0.0101  116 PHE   A CZ  
2474 N N   . ASN   A 117 ? 0.1289 0.1263 0.2030 -0.0034 0.0092  0.0208  117 ASN   A N   
2475 C CA  . ASN   A 117 ? 0.1323 0.1303 0.2092 -0.0049 0.0102  0.0283  117 ASN   A CA  
2476 C C   . ASN   A 117 ? 0.1305 0.1343 0.2226 0.0034  0.0189  0.0177  117 ASN   A C   
2477 O O   . ASN   A 117 ? 0.1400 0.1424 0.2419 -0.0025 -0.0059 0.0344  117 ASN   A O   
2478 C CB  . ASN   A 117 ? 0.1341 0.1389 0.2140 -0.0023 0.0064  0.0328  117 ASN   A CB  
2479 C CG  . ASN   A 117 ? 0.1289 0.1389 0.2162 -0.0030 0.0118  0.0241  117 ASN   A CG  
2480 O OD1 . ASN   A 117 ? 0.1326 0.1637 0.2274 -0.0097 0.0134  0.0178  117 ASN   A OD1 
2481 N ND2 . ASN   A 117 ? 0.1251 0.1314 0.2207 0.0010  0.0055  0.0223  117 ASN   A ND2 
2488 N N   . GLN   A 118 ? 0.1263 0.1388 0.2152 -0.0039 0.0052  0.0265  118 GLN   A N   
2489 C CA  . GLN   A 118 ? 0.1330 0.1497 0.2222 -0.0040 0.0014  0.0179  118 GLN   A CA  
2490 C C   . GLN   A 118 ? 0.1349 0.1637 0.2161 -0.0069 -0.0040 0.0203  118 GLN   A C   
2491 O O   . GLN   A 118 ? 0.1390 0.1978 0.2423 -0.0007 -0.0053 0.0062  118 GLN   A O   
2492 C CB  . GLN   A 118 ? 0.1385 0.1569 0.2272 0.0006  0.0091  0.0153  118 GLN   A CB  
2493 C CG  . GLN   A 118 ? 0.1331 0.1583 0.2344 -0.0053 0.0052  0.0209  118 GLN   A CG  
2494 C CD  . GLN   A 118 ? 0.1277 0.1595 0.2476 0.0010  0.0033  0.0204  118 GLN   A CD  
2495 O OE1 . GLN   A 118 ? 0.1343 0.1730 0.2589 0.0101  -0.0006 0.0085  118 GLN   A OE1 
2496 N NE2 . GLN   A 118 ? 0.1386 0.1562 0.2456 0.0107  -0.0023 0.0243  118 GLN   A NE2 
2505 N N   . HIS   A 119 ? 0.1423 0.1565 0.1947 0.0015  0.0071  0.0212  119 HIS   A N   
2506 C CA  . HIS   A 119 ? 0.1461 0.1609 0.1913 -0.0056 0.0087  0.0331  119 HIS   A CA  
2507 C C   . HIS   A 119 ? 0.1563 0.1652 0.1942 -0.0107 0.0035  0.0318  119 HIS   A C   
2508 O O   . HIS   A 119 ? 0.1619 0.1758 0.2107 -0.0280 -0.0019 0.0333  119 HIS   A O   
2509 C CB  . HIS   A 119 ? 0.1485 0.1579 0.2154 -0.0040 0.0198  0.0275  119 HIS   A CB  
2510 C CG  . HIS   A 119 ? 0.1519 0.1695 0.2516 0.0001  0.0115  0.0333  119 HIS   A CG  
2511 N ND1 . HIS   A 119 ? 0.1665 0.1913 0.2933 -0.0108 0.0143  0.0281  119 HIS   A ND1 
2512 C CD2 . HIS   A 119 ? 0.1664 0.1740 0.2621 0.0066  0.0294  0.0486  119 HIS   A CD2 
2513 C CE1 . HIS   A 119 ? 0.1653 0.1962 0.3137 -0.0177 0.0312  0.0404  119 HIS   A CE1 
2514 N NE2 . HIS   A 119 ? 0.1732 0.1762 0.3009 0.0028  0.0443  0.0572  119 HIS   A NE2 
2522 N N   . GLU   A 120 ? 0.1670 0.1928 0.1938 -0.0037 -0.0064 0.0505  120 GLU   A N   
2523 C CA  . GLU   A 120 ? 0.1941 0.2277 0.2172 0.0054  -0.0050 0.0884  120 GLU   A CA  
2524 C C   . GLU   A 120 ? 0.1679 0.2091 0.2018 -0.0091 -0.0023 0.0773  120 GLU   A C   
2525 O O   . GLU   A 120 ? 0.1666 0.2011 0.2111 -0.0130 -0.0009 0.0708  120 GLU   A O   
2526 C CB  . GLU   A 120 ? 0.2751 0.3057 0.2811 0.0305  -0.0024 0.1419  120 GLU   A CB  
2527 C CG  . GLU   A 120 ? 0.3745 0.3954 0.4009 0.0415  -0.0057 0.1460  120 GLU   A CG  
2528 C CD  . GLU   A 120 ? 0.4711 0.4689 0.5226 0.0504  -0.0006 0.1395  120 GLU   A CD  
2529 O OE1 . GLU   A 120 ? 0.4956 0.4908 0.5482 0.0532  0.0019  0.1371  120 GLU   A OE1 
2530 O OE2 . GLU   A 120 ? 0.5428 0.5428 0.5817 0.0531  0.0026  0.1367  120 GLU   A OE2 
2537 N N   . VAL   A 121 ? 0.1629 0.2069 0.1852 -0.0105 0.0124  0.0609  121 VAL   A N   
2538 C CA  . VAL   A 121 ? 0.1713 0.2177 0.1678 -0.0103 0.0219  0.0613  121 VAL   A CA  
2539 C C   . VAL   A 121 ? 0.1582 0.1997 0.1653 -0.0183 0.0171  0.0419  121 VAL   A C   
2540 O O   . VAL   A 121 ? 0.1631 0.2045 0.1752 -0.0287 -0.0088 0.0415  121 VAL   A O   
2541 C CB  . VAL   A 121 ? 0.2137 0.2609 0.2026 0.0082  0.0327  0.0677  121 VAL   A CB  
2542 C CG1 . VAL   A 121 ? 0.2200 0.2766 0.2108 0.0165  0.0358  0.0662  121 VAL   A CG1 
2543 C CG2 . VAL   A 121 ? 0.2434 0.2858 0.2478 -0.0014 0.0333  0.0446  121 VAL   A CG2 
2553 N N   . LEU   A 122 ? 0.1491 0.1778 0.1734 -0.0125 0.0119  0.0410  122 LEU   A N   
2554 C CA  . LEU   A 122 ? 0.1554 0.1601 0.1781 -0.0192 0.0252  0.0422  122 LEU   A CA  
2555 C C   . LEU   A 122 ? 0.1558 0.1608 0.1809 -0.0205 0.0109  0.0309  122 LEU   A C   
2556 O O   . LEU   A 122 ? 0.1535 0.1666 0.2145 -0.0245 0.0132  0.0302  122 LEU   A O   
2557 C CB  . LEU   A 122 ? 0.1806 0.1618 0.2097 -0.0083 0.0134  0.0555  122 LEU   A CB  
2558 C CG  . LEU   A 122 ? 0.1840 0.1692 0.2036 -0.0053 0.0180  0.0334  122 LEU   A CG  
2559 C CD1 . LEU   A 122 ? 0.2055 0.1761 0.2134 -0.0095 0.0246  0.0321  122 LEU   A CD1 
2560 C CD2 . LEU   A 122 ? 0.1725 0.1575 0.1883 -0.0057 0.0308  0.0213  122 LEU   A CD2 
2572 N N   A LEU   A 123 ? 0.1442 0.1554 0.1689 -0.0216 0.0018  0.0284  123 LEU   A N   
2573 N N   B LEU   A 123 ? 0.1576 0.1601 0.1650 -0.0155 0.0062  0.0209  123 LEU   A N   
2574 C CA  A LEU   A 123 ? 0.1439 0.1555 0.1575 -0.0203 0.0137  0.0304  123 LEU   A CA  
2575 C CA  B LEU   A 123 ? 0.1607 0.1621 0.1595 -0.0114 0.0039  0.0115  123 LEU   A CA  
2576 C C   A LEU   A 123 ? 0.1359 0.1450 0.1688 -0.0079 0.0116  0.0294  123 LEU   A C   
2577 C C   B LEU   A 123 ? 0.1603 0.1568 0.1462 -0.0084 0.0037  0.0043  123 LEU   A C   
2578 O O   A LEU   A 123 ? 0.1332 0.1531 0.1724 -0.0196 0.0072  0.0272  123 LEU   A O   
2579 O O   B LEU   A 123 ? 0.1575 0.1529 0.1361 -0.0075 0.0080  0.0002  123 LEU   A O   
2580 C CB  A LEU   A 123 ? 0.1583 0.1662 0.1519 -0.0222 0.0252  0.0346  123 LEU   A CB  
2581 C CB  B LEU   A 123 ? 0.1647 0.1688 0.1704 -0.0098 0.0018  0.0096  123 LEU   A CB  
2582 C CG  A LEU   A 123 ? 0.1654 0.1785 0.1700 -0.0202 0.0268  0.0119  123 LEU   A CG  
2583 C CG  B LEU   A 123 ? 0.1670 0.1742 0.1773 -0.0080 0.0028  0.0089  123 LEU   A CG  
2584 C CD1 A LEU   A 123 ? 0.1691 0.1868 0.1908 -0.0034 0.0258  0.0015  123 LEU   A CD1 
2585 C CD1 B LEU   A 123 ? 0.1677 0.1760 0.1819 -0.0042 0.0038  0.0084  123 LEU   A CD1 
2586 C CD2 A LEU   A 123 ? 0.1804 0.1855 0.1831 -0.0210 0.0213  0.0065  123 LEU   A CD2 
2587 C CD2 B LEU   A 123 ? 0.1704 0.1779 0.1832 -0.0065 0.0012  0.0078  123 LEU   A CD2 
2610 N N   A ALA   A 124 ? 0.1359 0.1404 0.1595 -0.0107 0.0097  0.0267  124 ALA   A N   
2611 N N   B ALA   A 124 ? 0.1632 0.1545 0.1438 -0.0077 -0.0023 -0.0014 124 ALA   A N   
2612 C CA  A ALA   A 124 ? 0.1271 0.1412 0.1780 -0.0121 0.0042  0.0249  124 ALA   A CA  
2613 C CA  B ALA   A 124 ? 0.1675 0.1593 0.1443 -0.0096 -0.0063 0.0004  124 ALA   A CA  
2614 C C   A ALA   A 124 ? 0.1237 0.1389 0.1769 -0.0097 0.0061  0.0261  124 ALA   A C   
2615 C C   B ALA   A 124 ? 0.1678 0.1601 0.1362 -0.0081 -0.0102 0.0020  124 ALA   A C   
2616 O O   A ALA   A 124 ? 0.1242 0.1451 0.2129 -0.0111 0.0158  0.0401  124 ALA   A O   
2617 O O   B ALA   A 124 ? 0.1655 0.1614 0.1260 -0.0072 -0.0147 0.0034  124 ALA   A O   
2618 C CB  A ALA   A 124 ? 0.1357 0.1309 0.1986 -0.0125 0.0069  0.0266  124 ALA   A CB  
2619 C CB  B ALA   A 124 ? 0.1705 0.1602 0.1495 -0.0114 -0.0052 -0.0003 124 ALA   A CB  
2630 N N   A PRO   A 125 ? 0.1256 0.1379 0.1655 -0.0077 0.0102  0.0367  125 PRO   A N   
2631 N N   B PRO   A 125 ? 0.1690 0.1601 0.1392 -0.0067 -0.0092 0.0043  125 PRO   A N   
2632 C CA  A PRO   A 125 ? 0.1388 0.1435 0.1741 -0.0019 0.0071  0.0310  125 PRO   A CA  
2633 C CA  B PRO   A 125 ? 0.1696 0.1612 0.1440 -0.0065 -0.0143 0.0031  125 PRO   A CA  
2634 C C   A PRO   A 125 ? 0.1246 0.1462 0.1857 -0.0048 0.0173  0.0256  125 PRO   A C   
2635 C C   B PRO   A 125 ? 0.1667 0.1624 0.1545 -0.0058 -0.0198 0.0012  125 PRO   A C   
2636 O O   A PRO   A 125 ? 0.1282 0.1449 0.1951 -0.0001 0.0000  0.0244  125 PRO   A O   
2637 O O   B PRO   A 125 ? 0.1668 0.1624 0.1617 -0.0050 -0.0192 0.0044  125 PRO   A O   
2638 C CB  A PRO   A 125 ? 0.1551 0.1420 0.1748 -0.0112 0.0163  0.0264  125 PRO   A CB  
2639 C CB  B PRO   A 125 ? 0.1725 0.1616 0.1462 -0.0078 -0.0060 0.0045  125 PRO   A CB  
2640 C CG  A PRO   A 125 ? 0.1516 0.1386 0.1916 -0.0178 0.0116  0.0347  125 PRO   A CG  
2641 C CG  B PRO   A 125 ? 0.1737 0.1616 0.1476 -0.0086 -0.0048 0.0044  125 PRO   A CG  
2642 C CD  A PRO   A 125 ? 0.1380 0.1435 0.1765 -0.0193 0.0123  0.0304  125 PRO   A CD  
2643 C CD  B PRO   A 125 ? 0.1713 0.1615 0.1431 -0.0076 -0.0047 0.0040  125 PRO   A CD  
2658 N N   A LEU   A 126 ? 0.1245 0.1542 0.1767 0.0003  0.0117  0.0289  126 LEU   A N   
2659 N N   B LEU   A 126 ? 0.1684 0.1648 0.1554 -0.0055 -0.0273 0.0009  126 LEU   A N   
2660 C CA  A LEU   A 126 ? 0.1269 0.1522 0.1895 -0.0033 0.0012  0.0309  126 LEU   A CA  
2661 C CA  B LEU   A 126 ? 0.1691 0.1660 0.1657 -0.0006 -0.0259 0.0010  126 LEU   A CA  
2662 C C   A LEU   A 126 ? 0.1385 0.1459 0.1912 0.0013  -0.0056 0.0287  126 LEU   A C   
2663 C C   B LEU   A 126 ? 0.1644 0.1627 0.1573 0.0028  -0.0321 0.0043  126 LEU   A C   
2664 O O   A LEU   A 126 ? 0.1537 0.1415 0.2191 0.0089  0.0174  0.0383  126 LEU   A O   
2665 O O   B LEU   A 126 ? 0.1645 0.1629 0.1571 0.0025  -0.0446 0.0087  126 LEU   A O   
2666 C CB  A LEU   A 126 ? 0.1434 0.1684 0.1979 -0.0080 -0.0049 0.0260  126 LEU   A CB  
2667 C CB  B LEU   A 126 ? 0.1734 0.1722 0.1910 0.0037  -0.0219 -0.0008 126 LEU   A CB  
2668 C CG  A LEU   A 126 ? 0.1391 0.1969 0.2229 -0.0149 0.0037  0.0251  126 LEU   A CG  
2669 C CG  B LEU   A 126 ? 0.1766 0.1770 0.2063 0.0069  -0.0171 0.0013  126 LEU   A CG  
2670 C CD1 A LEU   A 126 ? 0.1376 0.2156 0.2390 -0.0148 0.0037  0.0181  126 LEU   A CD1 
2671 C CD1 B LEU   A 126 ? 0.1760 0.1780 0.2027 0.0063  -0.0155 0.0026  126 LEU   A CD1 
2672 C CD2 A LEU   A 126 ? 0.1522 0.1880 0.2318 -0.0341 0.0108  0.0376  126 LEU   A CD2 
2673 C CD2 B LEU   A 126 ? 0.1780 0.1803 0.2152 0.0102  -0.0128 -0.0024 126 LEU   A CD2 
2696 N N   A LEU   A 127 ? 0.1335 0.1463 0.1881 0.0086  0.0057  0.0270  127 LEU   A N   
2697 N N   B LEU   A 127 ? 0.1618 0.1616 0.1570 0.0069  -0.0281 0.0104  127 LEU   A N   
2698 C CA  A LEU   A 127 ? 0.1328 0.1505 0.1800 0.0007  -0.0049 0.0145  127 LEU   A CA  
2699 C CA  B LEU   A 127 ? 0.1561 0.1621 0.1501 0.0108  -0.0282 0.0130  127 LEU   A CA  
2700 C C   A LEU   A 127 ? 0.1346 0.1354 0.1733 -0.0005 -0.0082 0.0142  127 LEU   A C   
2701 C C   B LEU   A 127 ? 0.1606 0.1615 0.1540 0.0113  -0.0206 0.0072  127 LEU   A C   
2702 O O   A LEU   A 127 ? 0.1468 0.1345 0.1716 -0.0084 -0.0041 0.0218  127 LEU   A O   
2703 O O   B LEU   A 127 ? 0.1649 0.1627 0.1642 0.0149  -0.0183 0.0028  127 LEU   A O   
2704 C CB  A LEU   A 127 ? 0.1437 0.1595 0.1756 0.0117  0.0031  0.0183  127 LEU   A CB  
2705 C CB  B LEU   A 127 ? 0.1477 0.1624 0.1368 0.0110  -0.0343 0.0185  127 LEU   A CB  
2706 C CG  A LEU   A 127 ? 0.1557 0.1671 0.1820 0.0133  -0.0013 0.0266  127 LEU   A CG  
2707 C CG  B LEU   A 127 ? 0.1382 0.1614 0.1201 0.0087  -0.0405 0.0252  127 LEU   A CG  
2708 C CD1 A LEU   A 127 ? 0.1639 0.1613 0.2000 0.0106  0.0063  0.0326  127 LEU   A CD1 
2709 C CD1 B LEU   A 127 ? 0.1376 0.1629 0.1274 0.0129  -0.0357 0.0278  127 LEU   A CD1 
2710 C CD2 A LEU   A 127 ? 0.1761 0.1776 0.1871 0.0171  -0.0180 0.0273  127 LEU   A CD2 
2711 C CD2 B LEU   A 127 ? 0.1348 0.1600 0.0981 0.0087  -0.0499 0.0226  127 LEU   A CD2 
2734 N N   A SER   A 128 ? 0.1384 0.1324 0.1643 -0.0112 -0.0072 0.0222  128 SER   A N   
2735 N N   B SER   A 128 ? 0.1623 0.1609 0.1511 0.0101  -0.0096 0.0081  128 SER   A N   
2736 C CA  A SER   A 128 ? 0.1509 0.1366 0.1558 -0.0124 -0.0121 0.0266  128 SER   A CA  
2737 C CA  B SER   A 128 ? 0.1702 0.1607 0.1548 0.0086  -0.0026 0.0087  128 SER   A CA  
2738 C C   A SER   A 128 ? 0.1593 0.1341 0.1592 -0.0001 -0.0167 0.0302  128 SER   A C   
2739 C C   B SER   A 128 ? 0.1773 0.1606 0.1554 0.0118  -0.0077 0.0073  128 SER   A C   
2740 O O   A SER   A 128 ? 0.1750 0.1494 0.1808 -0.0008 -0.0287 0.0116  128 SER   A O   
2741 O O   B SER   A 128 ? 0.1828 0.1624 0.1693 0.0191  -0.0008 0.0058  128 SER   A O   
2742 C CB  A SER   A 128 ? 0.1504 0.1516 0.1704 -0.0136 -0.0058 0.0232  128 SER   A CB  
2743 C CB  B SER   A 128 ? 0.1688 0.1613 0.1582 0.0079  0.0073  0.0086  128 SER   A CB  
2744 O OG  A SER   A 128 ? 0.1497 0.1676 0.1750 -0.0091 -0.0030 0.0157  128 SER   A OG  
2745 O OG  B SER   A 128 ? 0.1694 0.1607 0.1595 0.0068  0.0140  0.0107  128 SER   A OG  
2756 N N   A ALA   A 129 ? 0.1449 0.1521 0.1946 -0.0017 -0.0079 0.0319  129 ALA   A N   
2757 N N   B ALA   A 129 ? 0.1787 0.1634 0.1533 0.0052  -0.0168 0.0118  129 ALA   A N   
2758 C CA  A ALA   A 129 ? 0.1436 0.1481 0.2204 0.0053  -0.0047 0.0238  129 ALA   A CA  
2759 C CA  B ALA   A 129 ? 0.1838 0.1664 0.1632 -0.0010 -0.0157 0.0166  129 ALA   A CA  
2760 C C   A ALA   A 129 ? 0.1442 0.1517 0.1950 0.0002  -0.0128 0.0120  129 ALA   A C   
2761 C C   B ALA   A 129 ? 0.1897 0.1706 0.1636 -0.0037 -0.0062 0.0207  129 ALA   A C   
2762 O O   A ALA   A 129 ? 0.1433 0.1505 0.2012 -0.0032 -0.0117 0.0235  129 ALA   A O   
2763 O O   B ALA   A 129 ? 0.1903 0.1717 0.1630 -0.0082 -0.0085 0.0303  129 ALA   A O   
2764 C CB  A ALA   A 129 ? 0.1512 0.1644 0.2505 0.0107  0.0034  0.0430  129 ALA   A CB  
2765 C CB  B ALA   A 129 ? 0.1846 0.1677 0.1663 -0.0090 -0.0199 0.0150  129 ALA   A CB  
2776 N N   A GLY   A 130 ? 0.1520 0.1464 0.2102 -0.0010 -0.0000 -0.0020 130 GLY   A N   
2777 N N   B GLY   A 130 ? 0.1953 0.1737 0.1625 -0.0027 -0.0045 0.0224  130 GLY   A N   
2778 C CA  A GLY   A 130 ? 0.1762 0.1522 0.2147 0.0020  0.0011  -0.0015 130 GLY   A CA  
2779 C CA  B GLY   A 130 ? 0.1992 0.1787 0.1648 -0.0072 -0.0013 0.0214  130 GLY   A CA  
2780 C C   A GLY   A 130 ? 0.1734 0.1462 0.2041 0.0041  -0.0169 -0.0033 130 GLY   A C   
2781 C C   B GLY   A 130 ? 0.2041 0.1840 0.1718 -0.0115 0.0053  0.0196  130 GLY   A C   
2782 O O   A GLY   A 130 ? 0.1829 0.1398 0.2147 0.0084  -0.0358 0.0009  130 GLY   A O   
2783 O O   B GLY   A 130 ? 0.2033 0.1831 0.1771 -0.0188 0.0033  0.0213  130 GLY   A O   
2790 N N   A ILE   A 131 ? 0.1824 0.1415 0.1917 -0.0006 -0.0167 0.0100  131 ILE   A N   
2791 N N   B ILE   A 131 ? 0.2096 0.1889 0.1740 -0.0099 0.0048  0.0180  131 ILE   A N   
2792 C CA  A ILE   A 131 ? 0.1988 0.1434 0.1746 -0.0071 -0.0334 0.0108  131 ILE   A CA  
2793 C CA  B ILE   A 131 ? 0.2122 0.1949 0.1824 -0.0108 0.0003  0.0124  131 ILE   A CA  
2794 C C   A ILE   A 131 ? 0.1870 0.1510 0.1476 -0.0103 -0.0237 0.0172  131 ILE   A C   
2795 C C   B ILE   A 131 ? 0.2127 0.1990 0.1843 -0.0079 -0.0005 0.0174  131 ILE   A C   
2796 O O   A ILE   A 131 ? 0.1977 0.1631 0.1668 -0.0073 -0.0213 0.0352  131 ILE   A O   
2797 O O   B ILE   A 131 ? 0.2121 0.2020 0.1875 -0.0086 0.0001  0.0190  131 ILE   A O   
2798 C CB  A ILE   A 131 ? 0.2239 0.1570 0.1807 -0.0190 -0.0353 0.0030  131 ILE   A CB  
2799 C CB  B ILE   A 131 ? 0.2141 0.1981 0.1887 -0.0113 -0.0012 0.0059  131 ILE   A CB  
2800 C CG1 A ILE   A 131 ? 0.2278 0.1920 0.2030 -0.0320 -0.0368 0.0030  131 ILE   A CG1 
2801 C CG1 B ILE   A 131 ? 0.2164 0.2031 0.1963 -0.0116 -0.0000 0.0029  131 ILE   A CG1 
2802 C CG2 A ILE   A 131 ? 0.2455 0.1421 0.2001 -0.0135 -0.0313 -0.0121 131 ILE   A CG2 
2803 C CG2 B ILE   A 131 ? 0.2129 0.1964 0.1888 -0.0109 -0.0036 0.0034  131 ILE   A CG2 
2804 C CD1 A ILE   A 131 ? 0.2342 0.2102 0.2381 -0.0372 -0.0303 -0.0018 131 ILE   A CD1 
2805 C CD1 B ILE   A 131 ? 0.2172 0.2066 0.2021 -0.0120 -0.0000 0.0038  131 ILE   A CD1 
2828 N N   A PHE   A 132 ? 0.1775 0.1461 0.1437 0.0015  -0.0237 0.0290  132 PHE   A N   
2829 N N   B PHE   A 132 ? 0.2138 0.1984 0.1816 -0.0044 -0.0031 0.0153  132 PHE   A N   
2830 C CA  A PHE   A 132 ? 0.1800 0.1525 0.1554 -0.0045 -0.0094 0.0128  132 PHE   A CA  
2831 C CA  B PHE   A 132 ? 0.2134 0.1998 0.1795 -0.0008 -0.0034 0.0121  132 PHE   A CA  
2832 C C   A PHE   A 132 ? 0.1883 0.1675 0.1568 -0.0046 -0.0076 0.0132  132 PHE   A C   
2833 C C   B PHE   A 132 ? 0.2155 0.2017 0.1831 0.0006  -0.0075 0.0179  132 PHE   A C   
2834 O O   A PHE   A 132 ? 0.1993 0.1838 0.1600 0.0014  -0.0100 0.0159  132 PHE   A O   
2835 O O   B PHE   A 132 ? 0.2168 0.2046 0.1811 0.0033  -0.0085 0.0279  132 PHE   A O   
2836 C CB  A PHE   A 132 ? 0.1717 0.1392 0.1545 -0.0023 -0.0135 0.0190  132 PHE   A CB  
2837 C CB  B PHE   A 132 ? 0.2110 0.1989 0.1758 0.0032  -0.0001 0.0031  132 PHE   A CB  
2838 C CG  A PHE   A 132 ? 0.1687 0.1423 0.1499 0.0013  -0.0151 0.0121  132 PHE   A CG  
2839 C CG  B PHE   A 132 ? 0.2082 0.1986 0.1720 0.0081  0.0045  -0.0058 132 PHE   A CG  
2840 C CD1 A PHE   A 132 ? 0.1718 0.1600 0.1646 0.0059  -0.0147 -0.0009 132 PHE   A CD1 
2841 C CD1 B PHE   A 132 ? 0.2061 0.1977 0.1716 0.0091  0.0066  -0.0118 132 PHE   A CD1 
2842 C CD2 A PHE   A 132 ? 0.1715 0.1551 0.1675 0.0034  -0.0105 0.0085  132 PHE   A CD2 
2843 C CD2 B PHE   A 132 ? 0.2059 0.1988 0.1693 0.0090  0.0080  -0.0092 132 PHE   A CD2 
2844 C CE1 A PHE   A 132 ? 0.1690 0.1673 0.1826 0.0022  -0.0249 -0.0037 132 PHE   A CE1 
2845 C CE1 B PHE   A 132 ? 0.2058 0.1981 0.1692 0.0104  0.0087  -0.0144 132 PHE   A CE1 
2846 C CE2 A PHE   A 132 ? 0.1660 0.1649 0.1802 0.0130  -0.0142 0.0078  132 PHE   A CE2 
2847 C CE2 B PHE   A 132 ? 0.2057 0.1993 0.1719 0.0112  0.0093  -0.0111 132 PHE   A CE2 
2848 C CZ  A PHE   A 132 ? 0.1622 0.1653 0.1874 0.0010  -0.0241 0.0069  132 PHE   A CZ  
2849 C CZ  B PHE   A 132 ? 0.2051 0.1978 0.1659 0.0112  0.0095  -0.0130 132 PHE   A CZ  
2868 N N   A GLY   A 133 ? 0.1904 0.1659 0.1549 -0.0058 -0.0300 0.0107  133 GLY   A N   
2869 N N   B GLY   A 133 ? 0.2149 0.2012 0.1867 0.0007  -0.0155 0.0130  133 GLY   A N   
2870 C CA  A GLY   A 133 ? 0.1988 0.1774 0.1807 -0.0090 -0.0336 0.0045  133 GLY   A CA  
2871 C CA  B GLY   A 133 ? 0.2138 0.2024 0.1907 -0.0011 -0.0195 0.0054  133 GLY   A CA  
2872 C C   A GLY   A 133 ? 0.2028 0.1863 0.1666 -0.0137 -0.0386 -0.0083 133 GLY   A C   
2873 C C   B GLY   A 133 ? 0.2127 0.2043 0.2005 -0.0040 -0.0201 0.0013  133 GLY   A C   
2874 O O   A GLY   A 133 ? 0.2293 0.2080 0.1834 -0.0128 -0.0487 -0.0315 133 GLY   A O   
2875 O O   B GLY   A 133 ? 0.2194 0.2100 0.2052 -0.0028 -0.0210 -0.0018 133 GLY   A O   
2882 N N   A ALA   A 134 ? 0.1955 0.1766 0.1693 -0.0127 -0.0306 -0.0070 134 ALA   A N   
2883 N N   B ALA   A 134 ? 0.2067 0.2015 0.2006 -0.0068 -0.0186 0.0021  134 ALA   A N   
2884 C CA  A ALA   A 134 ? 0.1931 0.1782 0.1915 -0.0098 -0.0233 -0.0092 134 ALA   A CA  
2885 C CA  B ALA   A 134 ? 0.2034 0.2019 0.2033 -0.0078 -0.0185 0.0018  134 ALA   A CA  
2886 C C   A ALA   A 134 ? 0.1923 0.1868 0.1943 -0.0062 -0.0170 0.0056  134 ALA   A C   
2887 C C   B ALA   A 134 ? 0.1992 0.2037 0.2033 -0.0088 -0.0218 0.0025  134 ALA   A C   
2888 O O   A ALA   A 134 ? 0.2051 0.1914 0.2179 -0.0057 0.0086  0.0111  134 ALA   A O   
2889 O O   B ALA   A 134 ? 0.2030 0.2046 0.2029 -0.0078 -0.0230 0.0006  134 ALA   A O   
2890 C CB  A ALA   A 134 ? 0.2006 0.1786 0.2172 -0.0052 -0.0183 -0.0123 134 ALA   A CB  
2891 C CB  B ALA   A 134 ? 0.2047 0.2012 0.2061 -0.0075 -0.0168 0.0006  134 ALA   A CB  
2902 N N   A ASP   A 135 ? 0.1958 0.1935 0.2120 -0.0087 -0.0283 0.0207  135 ASP   A N   
2903 N N   B ASP   A 135 ? 0.1929 0.2033 0.2072 -0.0102 -0.0222 0.0027  135 ASP   A N   
2904 C CA  A ASP   A 135 ? 0.1966 0.2093 0.2408 -0.0197 -0.0397 0.0329  135 ASP   A CA  
2905 C CA  B ASP   A 135 ? 0.1884 0.2046 0.2149 -0.0099 -0.0235 0.0061  135 ASP   A CA  
2906 C C   A ASP   A 135 ? 0.1809 0.2018 0.2421 -0.0145 -0.0265 0.0462  135 ASP   A C   
2907 C C   B ASP   A 135 ? 0.1881 0.2017 0.2090 -0.0073 -0.0204 0.0097  135 ASP   A C   
2908 O O   A ASP   A 135 ? 0.1807 0.1863 0.2496 -0.0151 -0.0324 0.0483  135 ASP   A O   
2909 O O   B ASP   A 135 ? 0.1887 0.2000 0.2095 -0.0086 -0.0179 0.0095  135 ASP   A O   
2910 C CB  A ASP   A 135 ? 0.2229 0.2446 0.2812 -0.0451 -0.0693 0.0164  135 ASP   A CB  
2911 C CB  B ASP   A 135 ? 0.1868 0.2089 0.2306 -0.0135 -0.0300 0.0017  135 ASP   A CB  
2912 C CG  A ASP   A 135 ? 0.2440 0.2894 0.3402 -0.0616 -0.0738 0.0119  135 ASP   A CG  
2913 C CG  B ASP   A 135 ? 0.1823 0.2093 0.2389 -0.0179 -0.0370 -0.0060 135 ASP   A CG  
2914 O OD1 A ASP   A 135 ? 0.2407 0.3078 0.3492 -0.0668 -0.0759 0.0319  135 ASP   A OD1 
2915 O OD1 B ASP   A 135 ? 0.1799 0.2098 0.2376 -0.0255 -0.0334 -0.0147 135 ASP   A OD1 
2916 O OD2 A ASP   A 135 ? 0.2756 0.3132 0.3967 -0.0635 -0.0551 0.0115  135 ASP   A OD2 
2917 O OD2 B ASP   A 135 ? 0.1868 0.2106 0.2527 -0.0110 -0.0338 0.0008  135 ASP   A OD2 
2926 N N   A PRO   A 136 ? 0.1674 0.2107 0.2466 0.0030  -0.0143 0.0548  136 PRO   A N   
2927 N N   B PRO   A 136 ? 0.1867 0.2005 0.2046 -0.0004 -0.0216 0.0117  136 PRO   A N   
2928 C CA  A PRO   A 136 ? 0.1562 0.2103 0.2511 -0.0033 -0.0074 0.0447  136 PRO   A CA  
2929 C CA  B PRO   A 136 ? 0.1838 0.1991 0.2027 0.0026  -0.0212 0.0116  136 PRO   A CA  
2930 C C   A PRO   A 136 ? 0.1341 0.2060 0.2479 -0.0035 -0.0021 0.0400  136 PRO   A C   
2931 C C   B PRO   A 136 ? 0.1827 0.2000 0.2060 0.0052  -0.0164 0.0119  136 PRO   A C   
2932 O O   A PRO   A 136 ? 0.1319 0.2015 0.2397 -0.0013 0.0007  0.0367  136 PRO   A O   
2933 O O   B PRO   A 136 ? 0.1835 0.2028 0.2088 0.0053  -0.0173 0.0139  136 PRO   A O   
2934 C CB  A PRO   A 136 ? 0.1843 0.2112 0.2624 0.0047  -0.0128 0.0469  136 PRO   A CB  
2935 C CB  B PRO   A 136 ? 0.1844 0.1970 0.2008 0.0049  -0.0252 0.0141  136 PRO   A CB  
2936 C CG  A PRO   A 136 ? 0.2009 0.2242 0.2828 0.0146  -0.0125 0.0447  136 PRO   A CG  
2937 C CG  B PRO   A 136 ? 0.1858 0.1985 0.2023 0.0043  -0.0277 0.0118  136 PRO   A CG  
2938 C CD  A PRO   A 136 ? 0.1848 0.2175 0.2622 0.0149  -0.0009 0.0648  136 PRO   A CD  
2939 C CD  B PRO   A 136 ? 0.1872 0.1996 0.2028 0.0021  -0.0243 0.0117  136 PRO   A CD  
2954 N N   A ILE   A 137 ? 0.1367 0.1987 0.2563 -0.0016 -0.0153 0.0448  137 ILE   A N   
2955 N N   B ILE   A 137 ? 0.1825 0.1996 0.2083 0.0063  -0.0133 0.0121  137 ILE   A N   
2956 C CA  A ILE   A 137 ? 0.1416 0.2115 0.2666 -0.0102 -0.0182 0.0393  137 ILE   A CA  
2957 C CA  B ILE   A 137 ? 0.1831 0.2006 0.2126 0.0040  -0.0114 0.0113  137 ILE   A CA  
2958 C C   A ILE   A 137 ? 0.1424 0.2087 0.2526 -0.0204 -0.0269 0.0387  137 ILE   A C   
2959 C C   B ILE   A 137 ? 0.1803 0.1978 0.2079 0.0022  -0.0112 0.0124  137 ILE   A C   
2960 O O   A ILE   A 137 ? 0.1495 0.2047 0.2552 -0.0237 -0.0184 0.0314  137 ILE   A O   
2961 O O   B ILE   A 137 ? 0.1838 0.1950 0.2077 0.0048  -0.0090 0.0103  137 ILE   A O   
2962 C CB  A ILE   A 137 ? 0.1480 0.2309 0.2933 -0.0123 -0.0404 0.0299  137 ILE   A CB  
2963 C CB  B ILE   A 137 ? 0.1862 0.2036 0.2214 0.0042  -0.0122 0.0066  137 ILE   A CB  
2964 C CG1 A ILE   A 137 ? 0.1638 0.2594 0.3223 -0.0065 -0.0459 0.0272  137 ILE   A CG1 
2965 C CG1 B ILE   A 137 ? 0.1879 0.2051 0.2276 0.0044  -0.0107 0.0000  137 ILE   A CG1 
2966 C CG2 A ILE   A 137 ? 0.1639 0.2306 0.3064 -0.0153 -0.0595 0.0228  137 ILE   A CG2 
2967 C CG2 B ILE   A 137 ? 0.1886 0.2042 0.2238 0.0038  -0.0146 0.0055  137 ILE   A CG2 
2968 C CD1 A ILE   A 137 ? 0.1863 0.2781 0.3511 0.0001  -0.0362 0.0236  137 ILE   A CD1 
2969 C CD1 B ILE   A 137 ? 0.1913 0.2065 0.2324 0.0051  -0.0098 -0.0066 137 ILE   A CD1 
2992 N N   A HIS   A 138 ? 0.1464 0.2173 0.2376 -0.0130 -0.0118 0.0354  138 HIS   A N   
2993 N N   B HIS   A 138 ? 0.1730 0.1983 0.2060 0.0006  -0.0092 0.0142  138 HIS   A N   
2994 C CA  A HIS   A 138 ? 0.1543 0.2154 0.2190 -0.0129 -0.0078 0.0306  138 HIS   A CA  
2995 C CA  B HIS   A 138 ? 0.1656 0.1979 0.2060 -0.0042 -0.0086 0.0186  138 HIS   A CA  
2996 C C   A HIS   A 138 ? 0.1414 0.1972 0.2145 -0.0102 -0.0101 0.0380  138 HIS   A C   
2997 C C   B HIS   A 138 ? 0.1491 0.1908 0.2089 -0.0057 -0.0087 0.0276  138 HIS   A C   
2998 O O   A HIS   A 138 ? 0.1535 0.1973 0.2316 -0.0092 -0.0057 0.0301  138 HIS   A O   
2999 O O   B HIS   A 138 ? 0.1509 0.1911 0.2059 -0.0077 -0.0101 0.0236  138 HIS   A O   
3000 C CB  A HIS   A 138 ? 0.1713 0.2353 0.2231 -0.0086 -0.0193 0.0131  138 HIS   A CB  
3001 C CB  B HIS   A 138 ? 0.1768 0.2057 0.2116 -0.0070 -0.0121 0.0151  138 HIS   A CB  
3002 C CG  A HIS   A 138 ? 0.1938 0.2470 0.2260 -0.0154 -0.0204 0.0015  138 HIS   A CG  
3003 C CG  B HIS   A 138 ? 0.1862 0.2107 0.2173 -0.0108 -0.0107 0.0136  138 HIS   A CG  
3004 N ND1 A HIS   A 138 ? 0.2073 0.2562 0.2508 -0.0226 -0.0167 -0.0116 138 HIS   A ND1 
3005 N ND1 B HIS   A 138 ? 0.1908 0.2143 0.2247 -0.0126 -0.0084 0.0105  138 HIS   A ND1 
3006 C CD2 A HIS   A 138 ? 0.1973 0.2555 0.2326 -0.0127 -0.0219 0.0068  138 HIS   A CD2 
3007 C CD2 B HIS   A 138 ? 0.1890 0.2140 0.2203 -0.0116 -0.0121 0.0147  138 HIS   A CD2 
3008 C CE1 A HIS   A 138 ? 0.2099 0.2622 0.2503 -0.0136 -0.0213 -0.0106 138 HIS   A CE1 
3009 C CE1 B HIS   A 138 ? 0.1924 0.2165 0.2257 -0.0109 -0.0095 0.0108  138 HIS   A CE1 
3010 N NE2 A HIS   A 138 ? 0.2048 0.2649 0.2381 -0.0152 -0.0134 -0.0039 138 HIS   A NE2 
3011 N NE2 B HIS   A 138 ? 0.1912 0.2169 0.2225 -0.0115 -0.0096 0.0125  138 HIS   A NE2 
3026 N N   . SER   A 139 ? 0.1331 0.1836 0.2254 -0.0035 -0.0042 0.0403  139 SER   A N   
3027 C CA  . SER   A 139 ? 0.1327 0.1755 0.2301 -0.0095 -0.0065 0.0460  139 SER   A CA  
3028 C C   . SER   A 139 ? 0.1257 0.1626 0.2354 -0.0126 -0.0016 0.0297  139 SER   A C   
3029 O O   . SER   A 139 ? 0.1261 0.1602 0.2326 -0.0127 0.0022  0.0336  139 SER   A O   
3030 C CB  . SER   A 139 ? 0.1325 0.1719 0.2265 -0.0180 -0.0117 0.0498  139 SER   A CB  
3031 O OG  . SER   A 139 ? 0.1471 0.1765 0.2302 -0.0159 -0.0081 0.0497  139 SER   A OG  
3038 N N   . LEU   A 140 ? 0.1229 0.1721 0.2248 -0.0035 0.0004  0.0476  140 LEU   A N   
3039 C CA  . LEU   A 140 ? 0.1266 0.1653 0.2226 -0.0084 -0.0035 0.0424  140 LEU   A CA  
3040 C C   . LEU   A 140 ? 0.1180 0.1750 0.2258 -0.0157 -0.0068 0.0405  140 LEU   A C   
3041 O O   . LEU   A 140 ? 0.1305 0.1741 0.2408 -0.0089 -0.0046 0.0405  140 LEU   A O   
3042 C CB  . LEU   A 140 ? 0.1330 0.1669 0.2293 -0.0048 0.0055  0.0355  140 LEU   A CB  
3043 C CG  . LEU   A 140 ? 0.1342 0.1859 0.2436 -0.0160 0.0067  0.0494  140 LEU   A CG  
3044 C CD1 . LEU   A 140 ? 0.1394 0.1944 0.2466 -0.0119 0.0026  0.0516  140 LEU   A CD1 
3045 C CD2 . LEU   A 140 ? 0.1407 0.2020 0.2660 -0.0179 0.0148  0.0511  140 LEU   A CD2 
3057 N N   . ARG   A 141 ? 0.1264 0.1772 0.2312 -0.0125 -0.0119 0.0401  141 ARG   A N   
3058 C CA  . ARG   A 141 ? 0.1451 0.1872 0.2495 -0.0233 -0.0193 0.0144  141 ARG   A CA  
3059 C C   . ARG   A 141 ? 0.1499 0.1618 0.2380 -0.0146 -0.0127 0.0068  141 ARG   A C   
3060 O O   . ARG   A 141 ? 0.1475 0.1607 0.2509 -0.0152 -0.0004 0.0073  141 ARG   A O   
3061 C CB  . ARG   A 141 ? 0.1582 0.2223 0.2751 -0.0288 -0.0301 -0.0083 141 ARG   A CB  
3062 C CG  . ARG   A 141 ? 0.1976 0.2631 0.3128 -0.0289 -0.0154 -0.0147 141 ARG   A CG  
3063 C CD  . ARG   A 141 ? 0.2305 0.2946 0.3356 -0.0376 -0.0154 -0.0160 141 ARG   A CD  
3064 N NE  . ARG   A 141 ? 0.2208 0.3254 0.3431 -0.0409 -0.0212 -0.0119 141 ARG   A NE  
3065 C CZ  . ARG   A 141 ? 0.2251 0.3476 0.3471 -0.0544 -0.0152 -0.0060 141 ARG   A CZ  
3066 N NH1 . ARG   A 141 ? 0.2193 0.3561 0.3439 -0.0606 0.0032  -0.0154 141 ARG   A NH1 
3067 N NH2 . ARG   A 141 ? 0.2319 0.3552 0.3592 -0.0555 -0.0311 0.0022  141 ARG   A NH2 
3081 N N   . VAL   A 142 ? 0.1384 0.1629 0.2282 -0.0094 -0.0061 0.0067  142 VAL   A N   
3082 C CA  . VAL   A 142 ? 0.1440 0.1620 0.2240 -0.0094 0.0084  0.0055  142 VAL   A CA  
3083 C C   . VAL   A 142 ? 0.1306 0.1530 0.2153 -0.0148 0.0036  0.0126  142 VAL   A C   
3084 O O   . VAL   A 142 ? 0.1341 0.1553 0.2280 -0.0002 0.0009  0.0191  142 VAL   A O   
3085 C CB  . VAL   A 142 ? 0.1499 0.1697 0.2176 -0.0105 0.0082  0.0176  142 VAL   A CB  
3086 C CG1 . VAL   A 142 ? 0.1535 0.1618 0.2218 -0.0142 0.0024  0.0110  142 VAL   A CG1 
3087 C CG2 . VAL   A 142 ? 0.1646 0.1926 0.2396 0.0055  0.0082  0.0259  142 VAL   A CG2 
3097 N N   . CYS   A 143 ? 0.1283 0.1529 0.2115 -0.0142 -0.0035 0.0212  143 CYS   A N   
3098 C CA  . CYS   A 143 ? 0.1361 0.1470 0.2180 -0.0074 0.0031  0.0148  143 CYS   A CA  
3099 C C   . CYS   A 143 ? 0.1331 0.1458 0.2169 -0.0055 0.0015  0.0214  143 CYS   A C   
3100 O O   . CYS   A 143 ? 0.1324 0.1503 0.2267 -0.0047 0.0012  0.0290  143 CYS   A O   
3101 C CB  . CYS   A 143 ? 0.1447 0.1499 0.2208 -0.0073 0.0201  0.0303  143 CYS   A CB  
3102 S SG  . CYS   A 143 ? 0.1654 0.1662 0.1996 0.0045  0.0134  0.0220  143 CYS   A SG  
3108 N N   . VAL   A 144 ? 0.1282 0.1490 0.2401 -0.0055 0.0049  0.0323  144 VAL   A N   
3109 C CA  . VAL   A 144 ? 0.1437 0.1537 0.2879 -0.0104 0.0207  0.0324  144 VAL   A CA  
3110 C C   . VAL   A 144 ? 0.1414 0.1496 0.2833 -0.0179 -0.0104 0.0285  144 VAL   A C   
3111 O O   . VAL   A 144 ? 0.1580 0.1563 0.2803 -0.0051 -0.0109 0.0364  144 VAL   A O   
3112 C CB  . VAL   A 144 ? 0.1692 0.1841 0.3395 0.0047  0.0370  0.0451  144 VAL   A CB  
3113 C CG1 . VAL   A 144 ? 0.1805 0.2052 0.3714 -0.0063 0.0161  0.0386  144 VAL   A CG1 
3114 C CG2 . VAL   A 144 ? 0.1603 0.1933 0.3378 0.0073  0.0524  0.0643  144 VAL   A CG2 
3124 N N   . ASP   A 145 ? 0.1453 0.1463 0.2823 -0.0194 -0.0068 0.0137  145 ASP   A N   
3125 C CA  . ASP   A 145 ? 0.1642 0.1543 0.2989 -0.0191 -0.0079 0.0064  145 ASP   A CA  
3126 C C   . ASP   A 145 ? 0.1637 0.1469 0.2803 -0.0128 0.0007  -0.0052 145 ASP   A C   
3127 O O   . ASP   A 145 ? 0.1785 0.1581 0.3380 -0.0152 -0.0085 -0.0389 145 ASP   A O   
3128 C CB  . ASP   A 145 ? 0.1814 0.1799 0.3196 -0.0182 -0.0265 0.0028  145 ASP   A CB  
3129 C CG  . ASP   A 145 ? 0.2033 0.2203 0.3491 -0.0380 -0.0331 0.0121  145 ASP   A CG  
3130 O OD1 . ASP   A 145 ? 0.2006 0.2305 0.3595 -0.0541 -0.0378 0.0133  145 ASP   A OD1 
3131 O OD2 . ASP   A 145 ? 0.2239 0.2501 0.3548 -0.0479 -0.0480 0.0076  145 ASP   A OD2 
3136 N N   . THR   A 146 ? 0.1448 0.1416 0.2400 -0.0136 0.0077  0.0056  146 THR   A N   
3137 C CA  . THR   A 146 ? 0.1381 0.1408 0.2298 0.0011  0.0062  0.0106  146 THR   A CA  
3138 C C   . THR   A 146 ? 0.1361 0.1426 0.2349 0.0039  0.0074  0.0160  146 THR   A C   
3139 O O   . THR   A 146 ? 0.1430 0.1493 0.2511 0.0026  0.0005  0.0089  146 THR   A O   
3140 C CB  . THR   A 146 ? 0.1367 0.1507 0.2266 0.0038  0.0013  0.0154  146 THR   A CB  
3141 O OG1 . THR   A 146 ? 0.1358 0.1625 0.2402 0.0013  -0.0059 0.0071  146 THR   A OG1 
3142 C CG2 . THR   A 146 ? 0.1372 0.1531 0.2340 0.0003  -0.0006 0.0090  146 THR   A CG2 
3150 N N   . VAL   A 147 ? 0.1270 0.1473 0.2318 0.0003  0.0051  0.0130  147 VAL   A N   
3151 C CA  . VAL   A 147 ? 0.1248 0.1482 0.2322 -0.0078 0.0197  0.0224  147 VAL   A CA  
3152 C C   . VAL   A 147 ? 0.1286 0.1406 0.2285 -0.0058 0.0156  0.0261  147 VAL   A C   
3153 O O   . VAL   A 147 ? 0.1357 0.1484 0.2552 -0.0104 0.0133  0.0279  147 VAL   A O   
3154 C CB  . VAL   A 147 ? 0.1443 0.1409 0.2213 -0.0087 0.0140  0.0276  147 VAL   A CB  
3155 C CG1 . VAL   A 147 ? 0.1878 0.1493 0.2181 -0.0074 0.0164  0.0384  147 VAL   A CG1 
3156 C CG2 . VAL   A 147 ? 0.1550 0.1449 0.2298 -0.0105 0.0032  0.0222  147 VAL   A CG2 
3166 N N   . ARG   A 148 ? 0.1345 0.1434 0.2432 -0.0071 0.0225  0.0357  148 ARG   A N   
3167 C CA  . ARG   A 148 ? 0.1428 0.1469 0.2297 -0.0088 0.0036  0.0441  148 ARG   A CA  
3168 C C   . ARG   A 148 ? 0.1545 0.1483 0.2217 -0.0145 0.0116  0.0585  148 ARG   A C   
3169 O O   . ARG   A 148 ? 0.1841 0.1606 0.2496 -0.0224 0.0215  0.0498  148 ARG   A O   
3170 C CB  . ARG   A 148 ? 0.1510 0.1498 0.2524 -0.0063 0.0186  0.0378  148 ARG   A CB  
3171 C CG  . ARG   A 148 ? 0.1660 0.1555 0.2885 -0.0060 0.0368  0.0250  148 ARG   A CG  
3172 C CD  . ARG   A 148 ? 0.1853 0.1485 0.3178 -0.0021 0.0492  0.0436  148 ARG   A CD  
3173 N NE  . ARG   A 148 ? 0.1778 0.1492 0.3204 0.0122  0.0549  0.0542  148 ARG   A NE  
3174 C CZ  . ARG   A 148 ? 0.1745 0.1409 0.3004 0.0071  0.0439  0.0445  148 ARG   A CZ  
3175 N NH1 . ARG   A 148 ? 0.1871 0.1363 0.3087 -0.0020 0.0443  0.0161  148 ARG   A NH1 
3176 N NH2 . ARG   A 148 ? 0.1662 0.1675 0.2956 0.0186  0.0509  0.0457  148 ARG   A NH2 
3190 N N   . THR   A 149 ? 0.1513 0.1572 0.2162 -0.0137 -0.0015 0.0509  149 THR   A N   
3191 C CA  . THR   A 149 ? 0.1532 0.1633 0.2143 -0.0113 0.0041  0.0465  149 THR   A CA  
3192 C C   . THR   A 149 ? 0.1473 0.1605 0.2130 -0.0228 0.0093  0.0435  149 THR   A C   
3193 O O   . THR   A 149 ? 0.1455 0.1702 0.2287 -0.0201 0.0146  0.0424  149 THR   A O   
3194 C CB  . THR   A 149 ? 0.1505 0.1774 0.2237 -0.0117 0.0073  0.0448  149 THR   A CB  
3195 O OG1 . THR   A 149 ? 0.1563 0.1603 0.2421 -0.0208 0.0065  0.0402  149 THR   A OG1 
3196 C CG2 . THR   A 149 ? 0.1558 0.1944 0.2347 -0.0067 0.0011  0.0376  149 THR   A CG2 
3204 N N   . ASN   A 150 ? 0.1482 0.1603 0.2147 -0.0078 0.0079  0.0489  150 ASN   A N   
3205 C CA  . ASN   A 150 ? 0.1660 0.1674 0.2134 -0.0085 0.0098  0.0456  150 ASN   A CA  
3206 C C   . ASN   A 150 ? 0.1472 0.1649 0.2181 -0.0197 0.0017  0.0391  150 ASN   A C   
3207 O O   . ASN   A 150 ? 0.1567 0.1770 0.2557 -0.0160 -0.0098 0.0396  150 ASN   A O   
3208 C CB  . ASN   A 150 ? 0.2158 0.1979 0.2339 -0.0168 0.0361  0.0588  150 ASN   A CB  
3209 C CG  . ASN   A 150 ? 0.2731 0.2317 0.2997 -0.0194 0.0181  0.0670  150 ASN   A CG  
3210 O OD1 . ASN   A 150 ? 0.3010 0.2420 0.3175 -0.0297 0.0143  0.0814  150 ASN   A OD1 
3211 N ND2 . ASN   A 150 ? 0.3040 0.2569 0.3348 -0.0106 0.0109  0.0622  150 ASN   A ND2 
3218 N N   . VAL   A 151 ? 0.1462 0.1489 0.2210 -0.0218 -0.0009 0.0371  151 VAL   A N   
3219 C CA  . VAL   A 151 ? 0.1550 0.1487 0.2187 -0.0208 0.0120  0.0386  151 VAL   A CA  
3220 C C   . VAL   A 151 ? 0.1466 0.1459 0.2248 -0.0189 0.0164  0.0423  151 VAL   A C   
3221 O O   . VAL   A 151 ? 0.1534 0.1561 0.2536 -0.0184 0.0131  0.0367  151 VAL   A O   
3222 C CB  . VAL   A 151 ? 0.1851 0.1722 0.2171 -0.0003 0.0127  0.0324  151 VAL   A CB  
3223 C CG1 . VAL   A 151 ? 0.1774 0.2033 0.2381 -0.0102 0.0059  0.0266  151 VAL   A CG1 
3224 C CG2 . VAL   A 151 ? 0.2023 0.1782 0.2161 0.0063  0.0252  0.0347  151 VAL   A CG2 
3234 N N   . TYR   A 152 ? 0.1426 0.1505 0.2187 -0.0139 0.0105  0.0435  152 TYR   A N   
3235 C CA  . TYR   A 152 ? 0.1420 0.1584 0.1888 -0.0159 0.0168  0.0411  152 TYR   A CA  
3236 C C   . TYR   A 152 ? 0.1405 0.1541 0.1827 -0.0190 0.0202  0.0376  152 TYR   A C   
3237 O O   . TYR   A 152 ? 0.1501 0.1540 0.1977 -0.0240 0.0135  0.0293  152 TYR   A O   
3238 C CB  . TYR   A 152 ? 0.1595 0.1637 0.1899 -0.0097 0.0187  0.0324  152 TYR   A CB  
3239 C CG  . TYR   A 152 ? 0.1753 0.1848 0.1731 -0.0143 0.0232  0.0437  152 TYR   A CG  
3240 C CD1 . TYR   A 152 ? 0.1916 0.2079 0.2016 -0.0046 0.0243  0.0488  152 TYR   A CD1 
3241 C CD2 . TYR   A 152 ? 0.1776 0.1984 0.1718 -0.0291 0.0188  0.0373  152 TYR   A CD2 
3242 C CE1 . TYR   A 152 ? 0.2167 0.2185 0.2115 -0.0039 0.0093  0.0516  152 TYR   A CE1 
3243 C CE2 . TYR   A 152 ? 0.2015 0.2078 0.1826 -0.0331 0.0246  0.0435  152 TYR   A CE2 
3244 C CZ  . TYR   A 152 ? 0.2279 0.2077 0.2041 -0.0225 0.0113  0.0624  152 TYR   A CZ  
3245 O OH  . TYR   A 152 ? 0.2627 0.2309 0.2483 -0.0171 0.0086  0.0680  152 TYR   A OH  
3255 N N   A LEU   A 153 ? 0.1333 0.1532 0.1907 -0.0214 0.0145  0.0441  153 LEU   A N   
3256 N N   B LEU   A 153 ? 0.1470 0.1619 0.1738 -0.0179 0.0161  0.0313  153 LEU   A N   
3257 C CA  A LEU   A 153 ? 0.1325 0.1501 0.2173 -0.0137 0.0158  0.0434  153 LEU   A CA  
3258 C CA  B LEU   A 153 ? 0.1538 0.1702 0.1709 -0.0152 0.0141  0.0235  153 LEU   A CA  
3259 C C   A LEU   A 153 ? 0.1337 0.1532 0.2284 -0.0057 0.0159  0.0408  153 LEU   A C   
3260 C C   B LEU   A 153 ? 0.1572 0.1764 0.1718 -0.0155 0.0128  0.0158  153 LEU   A C   
3261 O O   A LEU   A 153 ? 0.1379 0.1677 0.2548 -0.0064 0.0296  0.0350  153 LEU   A O   
3262 O O   B LEU   A 153 ? 0.1580 0.1779 0.1788 -0.0187 0.0195  0.0154  153 LEU   A O   
3263 C CB  A LEU   A 153 ? 0.1337 0.1510 0.2193 -0.0127 0.0064  0.0467  153 LEU   A CB  
3264 C CB  B LEU   A 153 ? 0.1574 0.1731 0.1696 -0.0125 0.0105  0.0248  153 LEU   A CB  
3265 C CG  A LEU   A 153 ? 0.1405 0.1502 0.2164 -0.0128 0.0117  0.0346  153 LEU   A CG  
3266 C CG  B LEU   A 153 ? 0.1619 0.1748 0.1686 -0.0098 0.0101  0.0223  153 LEU   A CG  
3267 C CD1 A LEU   A 153 ? 0.1557 0.1598 0.2268 -0.0098 -0.0011 0.0425  153 LEU   A CD1 
3268 C CD1 B LEU   A 153 ? 0.1666 0.1754 0.1745 -0.0068 0.0072  0.0274  153 LEU   A CD1 
3269 C CD2 A LEU   A 153 ? 0.1455 0.1610 0.2217 -0.0122 0.0202  0.0110  153 LEU   A CD2 
3270 C CD2 B LEU   A 153 ? 0.1635 0.1783 0.1675 -0.0105 0.0107  0.0151  153 LEU   A CD2 
3293 N N   A ALA   A 154 ? 0.1378 0.1443 0.2352 -0.0022 0.0292  0.0402  154 ALA   A N   
3294 N N   B ALA   A 154 ? 0.1611 0.1817 0.1670 -0.0129 0.0105  0.0111  154 ALA   A N   
3295 C CA  A ALA   A 154 ? 0.1548 0.1542 0.2472 -0.0033 0.0368  0.0396  154 ALA   A CA  
3296 C CA  B ALA   A 154 ? 0.1684 0.1884 0.1722 -0.0101 0.0077  0.0073  154 ALA   A CA  
3297 C C   A ALA   A 154 ? 0.1494 0.1517 0.2551 -0.0002 0.0270  0.0440  154 ALA   A C   
3298 C C   B ALA   A 154 ? 0.1723 0.1924 0.1729 -0.0074 0.0004  0.0013  154 ALA   A C   
3299 O O   A ALA   A 154 ? 0.1545 0.1671 0.2432 -0.0041 0.0287  0.0460  154 ALA   A O   
3300 O O   B ALA   A 154 ? 0.1700 0.1917 0.1661 -0.0093 -0.0043 0.0012  154 ALA   A O   
3301 C CB  A ALA   A 154 ? 0.1659 0.1604 0.2528 0.0051  0.0292  0.0240  154 ALA   A CB  
3302 C CB  B ALA   A 154 ? 0.1688 0.1887 0.1682 -0.0109 0.0068  0.0060  154 ALA   A CB  
3313 N N   A VAL   A 155 ? 0.1552 0.1546 0.2686 0.0098  0.0307  0.0617  155 VAL   A N   
3314 N N   B VAL   A 155 ? 0.1795 0.1976 0.1840 -0.0038 -0.0021 -0.0011 155 VAL   A N   
3315 C CA  A VAL   A 155 ? 0.1638 0.1683 0.2864 0.0098  0.0254  0.0702  155 VAL   A CA  
3316 C CA  B VAL   A 155 ? 0.1864 0.2029 0.1971 -0.0032 -0.0023 0.0020  155 VAL   A CA  
3317 C C   A VAL   A 155 ? 0.1763 0.1755 0.3097 0.0184  0.0193  0.0827  155 VAL   A C   
3318 C C   B VAL   A 155 ? 0.1967 0.2095 0.2164 0.0000  -0.0062 0.0038  155 VAL   A C   
3319 O O   A VAL   A 155 ? 0.1764 0.1823 0.3184 0.0275  0.0290  0.0688  155 VAL   A O   
3320 O O   B VAL   A 155 ? 0.1958 0.2083 0.2162 0.0027  -0.0131 -0.0011 155 VAL   A O   
3321 C CB  A VAL   A 155 ? 0.1751 0.1790 0.2819 0.0128  0.0102  0.0575  155 VAL   A CB  
3322 C CB  B VAL   A 155 ? 0.1845 0.2025 0.2002 -0.0031 -0.0009 0.0017  155 VAL   A CB  
3323 C CG1 A VAL   A 155 ? 0.1905 0.1959 0.2901 0.0183  -0.0017 0.0604  155 VAL   A CG1 
3324 C CG1 B VAL   A 155 ? 0.1830 0.2041 0.2033 -0.0042 -0.0056 0.0039  155 VAL   A CG1 
3325 C CG2 A VAL   A 155 ? 0.1872 0.1853 0.2840 0.0195  -0.0057 0.0592  155 VAL   A CG2 
3326 C CG2 B VAL   A 155 ? 0.1866 0.2028 0.2020 -0.0012 0.0007  0.0013  155 VAL   A CG2 
3345 N N   A PHE   A 156 ? 0.1929 0.1849 0.3431 0.0236  0.0252  0.0897  156 PHE   A N   
3346 N N   B PHE   A 156 ? 0.2079 0.2186 0.2351 0.0024  0.0005  0.0092  156 PHE   A N   
3347 C CA  A PHE   A 156 ? 0.2144 0.1859 0.3788 0.0333  0.0308  0.0894  156 PHE   A CA  
3348 C CA  B PHE   A 156 ? 0.2187 0.2272 0.2541 0.0048  0.0063  0.0135  156 PHE   A CA  
3349 C C   A PHE   A 156 ? 0.2144 0.1903 0.3933 0.0474  0.0388  0.0947  156 PHE   A C   
3350 C C   B PHE   A 156 ? 0.2204 0.2326 0.2609 0.0061  0.0110  0.0195  156 PHE   A C   
3351 O O   A PHE   A 156 ? 0.2298 0.1964 0.4128 0.0427  0.0491  0.0651  156 PHE   A O   
3352 O O   B PHE   A 156 ? 0.2239 0.2348 0.2681 0.0041  0.0132  0.0200  156 PHE   A O   
3353 C CB  A PHE   A 156 ? 0.2377 0.1932 0.3910 0.0243  0.0205  0.1040  156 PHE   A CB  
3354 C CB  B PHE   A 156 ? 0.2287 0.2326 0.2659 0.0063  0.0051  0.0123  156 PHE   A CB  
3355 C CG  A PHE   A 156 ? 0.2723 0.2080 0.4148 0.0339  0.0050  0.0964  156 PHE   A CG  
3356 C CG  B PHE   A 156 ? 0.2400 0.2388 0.2807 0.0093  0.0031  0.0064  156 PHE   A CG  
3357 C CD1 A PHE   A 156 ? 0.2878 0.2220 0.4307 0.0379  0.0065  0.0783  156 PHE   A CD1 
3358 C CD1 B PHE   A 156 ? 0.2460 0.2408 0.2853 0.0121  0.0020  0.0061  156 PHE   A CD1 
3359 C CD2 A PHE   A 156 ? 0.2856 0.2138 0.4228 0.0442  0.0028  0.1046  156 PHE   A CD2 
3360 C CD2 B PHE   A 156 ? 0.2445 0.2420 0.2869 0.0120  0.0030  0.0037  156 PHE   A CD2 
3361 C CE1 A PHE   A 156 ? 0.3030 0.2345 0.4463 0.0393  0.0079  0.0732  156 PHE   A CE1 
3362 C CE1 B PHE   A 156 ? 0.2497 0.2434 0.2897 0.0139  0.0013  0.0055  156 PHE   A CE1 
3363 C CE2 A PHE   A 156 ? 0.3015 0.2277 0.4360 0.0464  0.0057  0.0888  156 PHE   A CE2 
3364 C CE2 B PHE   A 156 ? 0.2486 0.2435 0.2917 0.0129  0.0027  0.0010  156 PHE   A CE2 
3365 C CZ  A PHE   A 156 ? 0.3060 0.2336 0.4480 0.0460  0.0073  0.0690  156 PHE   A CZ  
3366 C CZ  B PHE   A 156 ? 0.2503 0.2439 0.2914 0.0151  0.0009  0.0037  156 PHE   A CZ  
3385 N N   A ASP   A 157 ? 0.2099 0.1903 0.3756 0.0423  0.0400  0.1188  157 ASP   A N   
3386 N N   B ASP   A 157 ? 0.2181 0.2353 0.2537 0.0063  0.0115  0.0231  157 ASP   A N   
3387 C CA  A ASP   A 157 ? 0.2267 0.2109 0.3890 0.0453  0.0302  0.1294  157 ASP   A CA  
3388 C CA  B ASP   A 157 ? 0.2178 0.2389 0.2503 0.0092  0.0126  0.0288  157 ASP   A CA  
3389 C C   A ASP   A 157 ? 0.2056 0.2262 0.3929 0.0515  0.0477  0.1303  157 ASP   A C   
3390 C C   B ASP   A 157 ? 0.2327 0.2528 0.2562 0.0128  0.0093  0.0282  157 ASP   A C   
3391 O O   A ASP   A 157 ? 0.1930 0.2183 0.3882 0.0470  0.0469  0.1280  157 ASP   A O   
3392 O O   B ASP   A 157 ? 0.2316 0.2532 0.2559 0.0141  0.0108  0.0252  157 ASP   A O   
3393 C CB  A ASP   A 157 ? 0.2592 0.2302 0.4182 0.0507  0.0107  0.1164  157 ASP   A CB  
3394 C CB  B ASP   A 157 ? 0.2014 0.2293 0.2433 0.0101  0.0165  0.0351  157 ASP   A CB  
3395 C CG  A ASP   A 157 ? 0.2926 0.2447 0.4577 0.0535  -0.0149 0.1072  157 ASP   A CG  
3396 C CG  B ASP   A 157 ? 0.1828 0.2180 0.2346 0.0117  0.0185  0.0432  157 ASP   A CG  
3397 O OD1 A ASP   A 157 ? 0.3298 0.2587 0.4896 0.0446  -0.0454 0.0891  157 ASP   A OD1 
3398 O OD1 B ASP   A 157 ? 0.1787 0.2144 0.2401 0.0068  0.0155  0.0358  157 ASP   A OD1 
3399 O OD2 A ASP   A 157 ? 0.2800 0.2455 0.4768 0.0511  -0.0065 0.1174  157 ASP   A OD2 
3400 O OD2 B ASP   A 157 ? 0.1688 0.2110 0.2207 0.0171  0.0220  0.0586  157 ASP   A OD2 
3409 N N   A LYS   A 158 ? 0.2109 0.2576 0.4137 0.0555  0.0575  0.1154  158 LYS   A N   
3410 N N   B LYS   A 158 ? 0.2480 0.2646 0.2647 0.0152  0.0047  0.0280  158 LYS   A N   
3411 C CA  A LYS   A 158 ? 0.2156 0.2869 0.4239 0.0622  0.0695  0.1154  158 LYS   A CA  
3412 C CA  B LYS   A 158 ? 0.2607 0.2752 0.2786 0.0169  0.0015  0.0253  158 LYS   A CA  
3413 C C   A LYS   A 158 ? 0.1883 0.2989 0.4105 0.0659  0.0651  0.1405  158 LYS   A C   
3414 C C   B LYS   A 158 ? 0.2658 0.2812 0.2838 0.0173  0.0024  0.0258  158 LYS   A C   
3415 O O   A LYS   A 158 ? 0.1824 0.3046 0.4219 0.0598  0.0754  0.1407  158 LYS   A O   
3416 O O   B LYS   A 158 ? 0.2676 0.2843 0.2839 0.0181  0.0038  0.0250  158 LYS   A O   
3417 C CB  A LYS   A 158 ? 0.2460 0.2986 0.4463 0.0620  0.0914  0.1102  158 LYS   A CB  
3418 C CB  B LYS   A 158 ? 0.2682 0.2788 0.2893 0.0165  -0.0015 0.0222  158 LYS   A CB  
3419 C CG  A LYS   A 158 ? 0.2710 0.3194 0.4703 0.0629  0.1097  0.1009  158 LYS   A CG  
3420 C CG  B LYS   A 158 ? 0.2741 0.2810 0.3006 0.0159  -0.0062 0.0212  158 LYS   A CG  
3421 C CD  A LYS   A 158 ? 0.2940 0.3370 0.4870 0.0594  0.1267  0.1045  158 LYS   A CD  
3422 C CD  B LYS   A 158 ? 0.2786 0.2837 0.3111 0.0152  -0.0091 0.0214  158 LYS   A CD  
3423 C CE  A LYS   A 158 ? 0.3085 0.3456 0.5023 0.0554  0.1351  0.1116  158 LYS   A CE  
3424 C CE  B LYS   A 158 ? 0.2821 0.2857 0.3193 0.0145  -0.0125 0.0229  158 LYS   A CE  
3425 N NZ  A LYS   A 158 ? 0.3153 0.3505 0.5109 0.0499  0.1419  0.1211  158 LYS   A NZ  
3426 N NZ  B LYS   A 158 ? 0.2838 0.2869 0.3220 0.0142  -0.0148 0.0243  158 LYS   A NZ  
3453 N N   A ASN   A 159 ? 0.1823 0.3086 0.4215 0.0656  0.0414  0.1434  159 ASN   A N   
3454 N N   B ASN   A 159 ? 0.2686 0.2830 0.2943 0.0153  0.0020  0.0248  159 ASN   A N   
3455 C CA  A ASN   A 159 ? 0.1872 0.3146 0.4210 0.0592  0.0165  0.1545  159 ASN   A CA  
3456 C CA  B ASN   A 159 ? 0.2710 0.2835 0.3034 0.0119  0.0025  0.0236  159 ASN   A CA  
3457 C C   A ASN   A 159 ? 0.1756 0.3117 0.3849 0.0404  0.0269  0.1371  159 ASN   A C   
3458 C C   B ASN   A 159 ? 0.2639 0.2759 0.2822 0.0086  0.0040  0.0182  159 ASN   A C   
3459 O O   A ASN   A 159 ? 0.1567 0.3162 0.3608 0.0394  0.0123  0.1214  159 ASN   A O   
3460 O O   B ASN   A 159 ? 0.2623 0.2744 0.2781 0.0055  0.0031  0.0167  159 ASN   A O   
3461 C CB  A ASN   A 159 ? 0.2088 0.3280 0.4786 0.0613  0.0066  0.1686  159 ASN   A CB  
3462 C CB  B ASN   A 159 ? 0.2810 0.2918 0.3351 0.0112  0.0024  0.0260  159 ASN   A CB  
3463 C CG  A ASN   A 159 ? 0.2362 0.3448 0.5420 0.0505  0.0080  0.1665  159 ASN   A CG  
3464 C CG  B ASN   A 159 ? 0.2893 0.2990 0.3649 0.0101  0.0032  0.0267  159 ASN   A CG  
3465 O OD1 A ASN   A 159 ? 0.2406 0.3554 0.5661 0.0458  0.0177  0.1614  159 ASN   A OD1 
3466 O OD1 B ASN   A 159 ? 0.2907 0.3025 0.3749 0.0103  0.0068  0.0274  159 ASN   A OD1 
3467 N ND2 A ASN   A 159 ? 0.2512 0.3550 0.5705 0.0492  0.0056  0.1619  159 ASN   A ND2 
3468 N ND2 B ASN   A 159 ? 0.2935 0.3026 0.3767 0.0098  0.0020  0.0265  159 ASN   A ND2 
3481 N N   A LEU   A 160 ? 0.1628 0.2909 0.3714 0.0320  0.0126  0.1384  160 LEU   A N   
3482 N N   B LEU   A 160 ? 0.2554 0.2683 0.2661 0.0092  0.0030  0.0147  160 LEU   A N   
3483 C CA  A LEU   A 160 ? 0.1622 0.2757 0.3557 0.0205  0.0141  0.1264  160 LEU   A CA  
3484 C CA  B LEU   A 160 ? 0.2465 0.2610 0.2484 0.0079  -0.0005 0.0148  160 LEU   A CA  
3485 C C   A LEU   A 160 ? 0.1479 0.2667 0.3347 0.0128  0.0259  0.1148  160 LEU   A C   
3486 C C   B LEU   A 160 ? 0.2401 0.2574 0.2393 0.0057  0.0020  0.0197  160 LEU   A C   
3487 O O   A LEU   A 160 ? 0.1442 0.2786 0.3487 0.0071  0.0293  0.1085  160 LEU   A O   
3488 O O   B LEU   A 160 ? 0.2390 0.2593 0.2405 0.0048  0.0034  0.0208  160 LEU   A O   
3489 C CB  A LEU   A 160 ? 0.1689 0.2678 0.3372 0.0089  0.0124  0.1266  160 LEU   A CB  
3490 C CB  B LEU   A 160 ? 0.2442 0.2581 0.2412 0.0064  -0.0042 0.0108  160 LEU   A CB  
3491 C CG  A LEU   A 160 ? 0.1814 0.2679 0.3378 -0.0014 0.0190  0.1049  160 LEU   A CG  
3492 C CG  B LEU   A 160 ? 0.2412 0.2561 0.2354 0.0044  -0.0088 0.0066  160 LEU   A CG  
3493 C CD1 A LEU   A 160 ? 0.1979 0.2749 0.3408 -0.0065 0.0215  0.0894  160 LEU   A CD1 
3494 C CD1 B LEU   A 160 ? 0.2396 0.2563 0.2315 0.0025  -0.0106 0.0060  160 LEU   A CD1 
3495 C CD2 A LEU   A 160 ? 0.1866 0.2692 0.3437 -0.0112 0.0282  0.0908  160 LEU   A CD2 
3496 C CD2 B LEU   A 160 ? 0.2401 0.2551 0.2320 0.0027  -0.0097 0.0046  160 LEU   A CD2 
3519 N N   A TYR   A 161 ? 0.1503 0.2421 0.3181 0.0190  0.0267  0.1062  161 TYR   A N   
3520 N N   B TYR   A 161 ? 0.2354 0.2516 0.2321 0.0051  0.0030  0.0217  161 TYR   A N   
3521 C CA  A TYR   A 161 ? 0.1472 0.2339 0.3195 0.0189  0.0265  0.0957  161 TYR   A CA  
3522 C CA  B TYR   A 161 ? 0.2319 0.2489 0.2300 0.0037  0.0021  0.0243  161 TYR   A CA  
3523 C C   A TYR   A 161 ? 0.1403 0.2471 0.3296 0.0157  0.0225  0.0918  161 TYR   A C   
3524 C C   B TYR   A 161 ? 0.2337 0.2563 0.2308 0.0060  0.0001  0.0318  161 TYR   A C   
3525 O O   A TYR   A 161 ? 0.1308 0.2458 0.3367 0.0084  0.0275  0.0799  161 TYR   A O   
3526 O O   B TYR   A 161 ? 0.2317 0.2550 0.2255 0.0052  -0.0017 0.0348  161 TYR   A O   
3527 C CB  A TYR   A 161 ? 0.1605 0.2240 0.3383 0.0078  0.0324  0.0779  161 TYR   A CB  
3528 C CB  B TYR   A 161 ? 0.2286 0.2406 0.2309 -0.0002 0.0023  0.0185  161 TYR   A CB  
3529 C CG  A TYR   A 161 ? 0.1568 0.2098 0.3365 0.0066  0.0243  0.0667  161 TYR   A CG  
3530 C CG  B TYR   A 161 ? 0.2244 0.2331 0.2287 -0.0031 -0.0003 0.0139  161 TYR   A CG  
3531 C CD1 A TYR   A 161 ? 0.1517 0.1969 0.3382 0.0000  0.0167  0.0565  161 TYR   A CD1 
3532 C CD1 B TYR   A 161 ? 0.2239 0.2321 0.2294 -0.0043 -0.0032 0.0106  161 TYR   A CD1 
3533 C CD2 A TYR   A 161 ? 0.1612 0.2162 0.3358 0.0092  0.0168  0.0532  161 TYR   A CD2 
3534 C CD2 B TYR   A 161 ? 0.2218 0.2285 0.2255 -0.0048 -0.0025 0.0101  161 TYR   A CD2 
3535 C CE1 A TYR   A 161 ? 0.1587 0.1978 0.3357 0.0024  0.0118  0.0619  161 TYR   A CE1 
3536 C CE1 B TYR   A 161 ? 0.2238 0.2298 0.2274 -0.0050 -0.0060 0.0104  161 TYR   A CE1 
3537 C CE2 A TYR   A 161 ? 0.1667 0.2105 0.3309 0.0014  0.0148  0.0637  161 TYR   A CE2 
3538 C CE2 B TYR   A 161 ? 0.2219 0.2277 0.2251 -0.0055 -0.0054 0.0098  161 TYR   A CE2 
3539 C CZ  A TYR   A 161 ? 0.1761 0.2073 0.3342 -0.0003 0.0093  0.0694  161 TYR   A CZ  
3540 C CZ  B TYR   A 161 ? 0.2244 0.2286 0.2269 -0.0059 -0.0072 0.0102  161 TYR   A CZ  
3541 O OH  A TYR   A 161 ? 0.1985 0.2168 0.3383 -0.0033 0.0068  0.0790  161 TYR   A OH  
3542 O OH  B TYR   A 161 ? 0.2287 0.2299 0.2318 -0.0066 -0.0098 0.0107  161 TYR   A OH  
3561 N N   A ASP   A 162 ? 0.1382 0.2637 0.3376 0.0202  0.0340  0.0996  162 ASP   A N   
3562 N N   B ASP   A 162 ? 0.2385 0.2649 0.2382 0.0108  0.0017  0.0370  162 ASP   A N   
3563 C CA  A ASP   A 162 ? 0.1409 0.2931 0.3343 0.0120  0.0420  0.1019  162 ASP   A CA  
3564 C CA  B ASP   A 162 ? 0.2444 0.2749 0.2460 0.0153  0.0007  0.0382  162 ASP   A CA  
3565 C C   A ASP   A 162 ? 0.1334 0.3084 0.3216 0.0019  0.0398  0.1061  162 ASP   A C   
3566 C C   B ASP   A 162 ? 0.2568 0.2844 0.2505 0.0126  0.0022  0.0324  162 ASP   A C   
3567 O O   A ASP   A 162 ? 0.1360 0.3096 0.3379 -0.0056 0.0387  0.0948  162 ASP   A O   
3568 O O   B ASP   A 162 ? 0.2562 0.2847 0.2452 0.0129  0.0005  0.0312  162 ASP   A O   
3569 C CB  A ASP   A 162 ? 0.1536 0.3080 0.3576 0.0193  0.0459  0.0950  162 ASP   A CB  
3570 C CB  B ASP   A 162 ? 0.2385 0.2753 0.2562 0.0213  -0.0028 0.0451  162 ASP   A CB  
3571 C CG  A ASP   A 162 ? 0.1705 0.3299 0.3868 0.0227  0.0545  0.0794  162 ASP   A CG  
3572 C CG  B ASP   A 162 ? 0.2344 0.2761 0.2619 0.0262  -0.0084 0.0535  162 ASP   A CG  
3573 O OD1 A ASP   A 162 ? 0.1916 0.3389 0.3968 0.0120  0.0541  0.0728  162 ASP   A OD1 
3574 O OD1 B ASP   A 162 ? 0.2330 0.2753 0.2654 0.0275  -0.0088 0.0590  162 ASP   A OD1 
3575 O OD2 A ASP   A 162 ? 0.1913 0.3412 0.4145 0.0433  0.0455  0.0662  162 ASP   A OD2 
3576 O OD2 B ASP   A 162 ? 0.2338 0.2780 0.2644 0.0308  -0.0127 0.0576  162 ASP   A OD2 
3585 N N   A LYS   A 163 ? 0.1454 0.3281 0.3269 -0.0000 0.0126  0.1072  163 LYS   A N   
3586 N N   B LYS   A 163 ? 0.2703 0.2949 0.2666 0.0100  0.0035  0.0287  163 LYS   A N   
3587 C CA  A LYS   A 163 ? 0.1591 0.3450 0.3212 -0.0050 0.0029  0.1064  163 LYS   A CA  
3588 C CA  B LYS   A 163 ? 0.2815 0.3032 0.2825 0.0075  0.0055  0.0234  163 LYS   A CA  
3589 C C   A LYS   A 163 ? 0.1556 0.3295 0.3143 -0.0123 0.0127  0.1006  163 LYS   A C   
3590 C C   B LYS   A 163 ? 0.2724 0.2926 0.2578 0.0049  0.0110  0.0212  163 LYS   A C   
3591 O O   A LYS   A 163 ? 0.1504 0.3407 0.3245 -0.0206 0.0017  0.0937  163 LYS   A O   
3592 O O   B LYS   A 163 ? 0.2721 0.2922 0.2533 0.0046  0.0118  0.0187  163 LYS   A O   
3593 C CB  A LYS   A 163 ? 0.2054 0.3774 0.3615 0.0092  -0.0178 0.1012  163 LYS   A CB  
3594 C CB  B LYS   A 163 ? 0.3018 0.3208 0.3255 0.0084  0.0032  0.0213  163 LYS   A CB  
3595 C CG  A LYS   A 163 ? 0.2550 0.4089 0.4128 0.0101  -0.0150 0.0948  163 LYS   A CG  
3596 C CG  B LYS   A 163 ? 0.3206 0.3368 0.3703 0.0084  0.0007  0.0189  163 LYS   A CG  
3597 C CD  A LYS   A 163 ? 0.3076 0.4382 0.4727 0.0124  -0.0158 0.0877  163 LYS   A CD  
3598 C CD  B LYS   A 163 ? 0.3361 0.3505 0.4104 0.0084  -0.0009 0.0166  163 LYS   A CD  
3599 C CE  A LYS   A 163 ? 0.3412 0.4568 0.5219 0.0113  -0.0124 0.0816  163 LYS   A CE  
3600 C CE  B LYS   A 163 ? 0.3472 0.3602 0.4399 0.0084  -0.0025 0.0156  163 LYS   A CE  
3601 N NZ  A LYS   A 163 ? 0.3555 0.4628 0.5501 0.0092  -0.0109 0.0805  163 LYS   A NZ  
3602 N NZ  B LYS   A 163 ? 0.3526 0.3655 0.4571 0.0081  -0.0038 0.0152  163 LYS   A NZ  
3629 N N   A LEU   A 164 ? 0.1365 0.2929 0.3028 -0.0204 0.0198  0.0922  164 LEU   A N   
3630 N N   B LEU   A 164 ? 0.2606 0.2805 0.2420 0.0023  0.0128  0.0205  164 LEU   A N   
3631 C CA  A LEU   A 164 ? 0.1439 0.2681 0.2974 -0.0235 0.0370  0.0811  164 LEU   A CA  
3632 C CA  B LEU   A 164 ? 0.2500 0.2694 0.2340 -0.0020 0.0131  0.0194  164 LEU   A CA  
3633 C C   A LEU   A 164 ? 0.1524 0.2656 0.3004 -0.0215 0.0405  0.0760  164 LEU   A C   
3634 C C   B LEU   A 164 ? 0.2393 0.2626 0.2268 -0.0043 0.0113  0.0219  164 LEU   A C   
3635 O O   A LEU   A 164 ? 0.1623 0.2693 0.3023 -0.0237 0.0570  0.0551  164 LEU   A O   
3636 O O   B LEU   A 164 ? 0.2386 0.2620 0.2286 -0.0045 0.0155  0.0190  164 LEU   A O   
3637 C CB  A LEU   A 164 ? 0.1384 0.2482 0.2860 -0.0206 0.0320  0.0819  164 LEU   A CB  
3638 C CB  B LEU   A 164 ? 0.2491 0.2656 0.2340 -0.0028 0.0118  0.0171  164 LEU   A CB  
3639 C CG  A LEU   A 164 ? 0.1421 0.2422 0.2996 -0.0093 0.0194  0.0691  164 LEU   A CG  
3640 C CG  B LEU   A 164 ? 0.2489 0.2629 0.2327 -0.0040 0.0110  0.0142  164 LEU   A CG  
3641 C CD1 A LEU   A 164 ? 0.1328 0.2352 0.3069 -0.0037 0.0161  0.0592  164 LEU   A CD1 
3642 C CD1 B LEU   A 164 ? 0.2482 0.2623 0.2317 -0.0033 0.0126  0.0122  164 LEU   A CD1 
3643 C CD2 A LEU   A 164 ? 0.1513 0.2399 0.3026 -0.0132 0.0255  0.0665  164 LEU   A CD2 
3644 C CD2 B LEU   A 164 ? 0.2490 0.2611 0.2330 -0.0066 0.0085  0.0129  164 LEU   A CD2 
3667 N N   A VAL   A 165 ? 0.1427 0.2607 0.2861 -0.0217 0.0339  0.0824  165 VAL   A N   
3668 N N   B VAL   A 165 ? 0.2279 0.2565 0.2185 -0.0069 0.0072  0.0288  165 VAL   A N   
3669 C CA  A VAL   A 165 ? 0.1572 0.2606 0.2741 -0.0161 0.0335  0.0835  165 VAL   A CA  
3670 C CA  B VAL   A 165 ? 0.2202 0.2514 0.2138 -0.0086 0.0013  0.0306  165 VAL   A CA  
3671 C C   A VAL   A 165 ? 0.1464 0.2746 0.2789 -0.0170 0.0411  0.0786  165 VAL   A C   
3672 C C   B VAL   A 165 ? 0.2152 0.2489 0.2174 -0.0089 0.0020  0.0324  165 VAL   A C   
3673 O O   A VAL   A 165 ? 0.1443 0.2752 0.2788 -0.0214 0.0358  0.0736  165 VAL   A O   
3674 O O   B VAL   A 165 ? 0.2149 0.2474 0.2220 -0.0094 0.0056  0.0301  165 VAL   A O   
3675 C CB  A VAL   A 165 ? 0.1696 0.2536 0.2884 -0.0184 0.0376  0.0746  165 VAL   A CB  
3676 C CB  B VAL   A 165 ? 0.2193 0.2506 0.2127 -0.0093 -0.0024 0.0309  165 VAL   A CB  
3677 C CG1 A VAL   A 165 ? 0.1818 0.2581 0.3010 -0.0159 0.0379  0.0674  165 VAL   A CG1 
3678 C CG1 B VAL   A 165 ? 0.2201 0.2517 0.2113 -0.0101 -0.0043 0.0297  165 VAL   A CG1 
3679 C CG2 A VAL   A 165 ? 0.1887 0.2559 0.3025 -0.0166 0.0264  0.0760  165 VAL   A CG2 
3680 C CG2 B VAL   A 165 ? 0.2195 0.2500 0.2123 -0.0074 -0.0075 0.0331  165 VAL   A CG2 
3699 N N   A SER   A 166 ? 0.1341 0.2869 0.2985 -0.0116 0.0411  0.0768  166 SER   A N   
3700 N N   B SER   A 166 ? 0.2120 0.2509 0.2165 -0.0069 -0.0012 0.0360  166 SER   A N   
3701 C CA  A SER   A 166 ? 0.1380 0.3098 0.3024 -0.0154 0.0384  0.0698  166 SER   A CA  
3702 C CA  B SER   A 166 ? 0.2137 0.2546 0.2193 -0.0046 -0.0058 0.0362  166 SER   A CA  
3703 C C   A SER   A 166 ? 0.1438 0.3247 0.2926 -0.0171 0.0170  0.0687  166 SER   A C   
3704 C C   B SER   A 166 ? 0.2264 0.2591 0.2264 -0.0021 -0.0095 0.0363  166 SER   A C   
3705 O O   A SER   A 166 ? 0.1711 0.3409 0.3209 -0.0252 0.0167  0.0493  166 SER   A O   
3706 O O   B SER   A 166 ? 0.2262 0.2581 0.2202 -0.0012 -0.0147 0.0404  166 SER   A O   
3707 C CB  A SER   A 166 ? 0.1527 0.3245 0.3479 -0.0036 0.0198  0.0441  166 SER   A CB  
3708 C CB  B SER   A 166 ? 0.2034 0.2551 0.2160 -0.0031 -0.0103 0.0346  166 SER   A CB  
3709 O OG  A SER   A 166 ? 0.1972 0.3343 0.3748 -0.0103 0.0168  0.0448  166 SER   A OG  
3710 O OG  B SER   A 166 ? 0.1935 0.2559 0.2125 -0.0060 -0.0113 0.0366  166 SER   A OG  
3721 N N   A SER   A 167 ? 0.1483 0.3285 0.2704 -0.0066 0.0110  0.0765  167 SER   A N   
3722 N N   B SER   A 167 ? 0.2402 0.2658 0.2356 -0.0005 -0.0065 0.0313  167 SER   A N   
3723 C CA  A SER   A 167 ? 0.1774 0.3329 0.2625 -0.0009 -0.0010 0.0604  167 SER   A CA  
3724 C CA  B SER   A 167 ? 0.2559 0.2721 0.2426 -0.0018 -0.0044 0.0253  167 SER   A CA  
3725 C C   A SER   A 167 ? 0.1828 0.3306 0.2539 0.0046  0.0137  0.0530  167 SER   A C   
3726 C C   B SER   A 167 ? 0.2709 0.2816 0.2539 -0.0015 -0.0014 0.0213  167 SER   A C   
3727 O O   A SER   A 167 ? 0.2044 0.3342 0.2751 0.0095  -0.0017 0.0468  167 SER   A O   
3728 O O   B SER   A 167 ? 0.2729 0.2801 0.2490 -0.0006 -0.0022 0.0224  167 SER   A O   
3729 C CB  A SER   A 167 ? 0.1933 0.3420 0.2799 0.0014  0.0039  0.0639  167 SER   A CB  
3730 C CB  B SER   A 167 ? 0.2561 0.2703 0.2390 -0.0029 -0.0044 0.0242  167 SER   A CB  
3731 O OG  A SER   A 167 ? 0.1973 0.3475 0.2798 -0.0013 0.0175  0.0694  167 SER   A OG  
3732 O OG  B SER   A 167 ? 0.2561 0.2700 0.2398 -0.0035 -0.0041 0.0225  167 SER   A OG  
3743 N N   A PHE   A 168 ? 0.1749 0.3255 0.2501 0.0123  0.0168  0.0474  168 PHE   A N   
3744 N N   B PHE   A 168 ? 0.2841 0.2928 0.2716 -0.0019 0.0005  0.0174  168 PHE   A N   
3745 C CA  A PHE   A 168 ? 0.1785 0.3226 0.2696 0.0069  0.0207  0.0379  168 PHE   A CA  
3746 C CA  B PHE   A 168 ? 0.2981 0.3047 0.2920 -0.0025 0.0013  0.0127  168 PHE   A CA  
3747 C C   A PHE   A 168 ? 0.1982 0.3452 0.3060 -0.0099 0.0610  0.0176  168 PHE   A C   
3748 C C   B PHE   A 168 ? 0.3223 0.3256 0.3322 -0.0059 0.0014  0.0090  168 PHE   A C   
3749 O O   A PHE   A 168 ? 0.2072 0.3383 0.3430 -0.0323 0.0603  0.0328  168 PHE   A O   
3750 O O   B PHE   A 168 ? 0.3240 0.3259 0.3319 -0.0084 -0.0008 0.0093  168 PHE   A O   
3751 C CB  A PHE   A 168 ? 0.1776 0.3016 0.2599 0.0045  -0.0015 0.0379  168 PHE   A CB  
3752 C CB  B PHE   A 168 ? 0.2881 0.2961 0.2747 0.0002  0.0016  0.0130  168 PHE   A CB  
3753 C CG  A PHE   A 168 ? 0.1713 0.2859 0.2488 -0.0054 -0.0014 0.0460  168 PHE   A CG  
3754 C CG  B PHE   A 168 ? 0.2789 0.2882 0.2604 0.0017  0.0030  0.0135  168 PHE   A CG  
3755 C CD1 A PHE   A 168 ? 0.1684 0.2893 0.2588 -0.0076 -0.0016 0.0554  168 PHE   A CD1 
3756 C CD1 B PHE   A 168 ? 0.2745 0.2858 0.2544 0.0028  0.0037  0.0143  168 PHE   A CD1 
3757 C CD2 A PHE   A 168 ? 0.1664 0.2778 0.2414 -0.0064 0.0112  0.0404  168 PHE   A CD2 
3758 C CD2 B PHE   A 168 ? 0.2754 0.2846 0.2557 0.0016  0.0033  0.0136  168 PHE   A CD2 
3759 C CE1 A PHE   A 168 ? 0.1599 0.2876 0.2570 -0.0073 -0.0057 0.0614  168 PHE   A CE1 
3760 C CE1 B PHE   A 168 ? 0.2719 0.2836 0.2517 0.0034  0.0035  0.0159  168 PHE   A CE1 
3761 C CE2 A PHE   A 168 ? 0.1665 0.2729 0.2539 -0.0088 0.0106  0.0524  168 PHE   A CE2 
3762 C CE2 B PHE   A 168 ? 0.2728 0.2822 0.2526 0.0013  0.0036  0.0141  168 PHE   A CE2 
3763 C CZ  A PHE   A 168 ? 0.1615 0.2804 0.2565 -0.0108 0.0002  0.0569  168 PHE   A CZ  
3764 C CZ  B PHE   A 168 ? 0.2713 0.2823 0.2509 0.0018  0.0031  0.0153  168 PHE   A CZ  
3783 N N   A LEU   A 169 ? 0.2583 0.3785 0.3728 -0.0166 0.0580  -0.0118 169 LEU   A N   
3784 N N   B LEU   A 169 ? 0.3457 0.3454 0.3728 -0.0077 0.0011  0.0062  169 LEU   A N   
3785 C CA  A LEU   A 169 ? 0.3453 0.4170 0.4723 -0.0159 0.0185  -0.0295 169 LEU   A CA  
3786 C CA  B LEU   A 169 ? 0.3687 0.3646 0.4138 -0.0085 -0.0022 0.0047  169 LEU   A CA  
3787 C C   A LEU   A 169 ? 0.3738 0.4266 0.5224 -0.0188 0.0046  -0.0235 169 LEU   A C   
3788 C C   B LEU   A 169 ? 0.3769 0.3705 0.4290 -0.0095 -0.0051 0.0093  169 LEU   A C   
3789 O O   A LEU   A 169 ? 0.3838 0.4297 0.5369 -0.0186 0.0034  -0.0262 169 LEU   A O   
3790 O O   B LEU   A 169 ? 0.3790 0.3725 0.4345 -0.0092 -0.0051 0.0115  169 LEU   A O   
3791 C CB  A LEU   A 169 ? 0.3949 0.4415 0.5046 -0.0146 -0.0025 -0.0493 169 LEU   A CB  
3792 C CB  B LEU   A 169 ? 0.3809 0.3757 0.4345 -0.0089 -0.0034 -0.0013 169 LEU   A CB  
3793 C CG  A LEU   A 169 ? 0.4300 0.4605 0.5283 -0.0184 -0.0166 -0.0691 169 LEU   A CG  
3794 C CG  B LEU   A 169 ? 0.3908 0.3841 0.4509 -0.0095 -0.0043 -0.0069 169 LEU   A CG  
3795 C CD1 A LEU   A 169 ? 0.4432 0.4667 0.5398 -0.0193 -0.0219 -0.0755 169 LEU   A CD1 
3796 C CD1 B LEU   A 169 ? 0.3938 0.3868 0.4571 -0.0096 -0.0041 -0.0084 169 LEU   A CD1 
3797 C CD2 A LEU   A 169 ? 0.4412 0.4671 0.5322 -0.0207 -0.0199 -0.0764 169 LEU   A CD2 
3798 C CD2 B LEU   A 169 ? 0.3943 0.3869 0.4559 -0.0099 -0.0047 -0.0091 169 LEU   A CD2 
3799 O OXT A LEU   A 169 ? 0.3712 0.4287 0.5365 -0.0193 0.0036  -0.0190 169 LEU   A OXT 
3800 O OXT B LEU   A 169 ? 0.3810 0.3722 0.4337 -0.0107 -0.0067 0.0113  169 LEU   A OXT 
3823 N N   A SER   B 1   ? 0.3809 0.3688 0.3908 -0.1317 -0.0933 0.0483  1   SER   B N   
3824 N N   B SER   B 1   ? 0.3757 0.3597 0.3558 -0.0300 -0.0188 0.0100  1   SER   B N   
3825 C CA  A SER   B 1   ? 0.3676 0.3663 0.3903 -0.1395 -0.1003 0.0454  1   SER   B CA  
3826 C CA  B SER   B 1   ? 0.3735 0.3593 0.3574 -0.0304 -0.0186 0.0102  1   SER   B CA  
3827 C C   A SER   B 1   ? 0.3337 0.3634 0.3621 -0.1372 -0.1072 0.0587  1   SER   B C   
3828 C C   B SER   B 1   ? 0.3672 0.3598 0.3597 -0.0304 -0.0200 0.0142  1   SER   B C   
3829 O O   A SER   B 1   ? 0.3390 0.3607 0.3350 -0.1262 -0.1022 0.0575  1   SER   B O   
3830 O O   B SER   B 1   ? 0.3682 0.3593 0.3545 -0.0290 -0.0203 0.0131  1   SER   B O   
3831 C CB  A SER   B 1   ? 0.3848 0.3694 0.4236 -0.1390 -0.0877 0.0286  1   SER   B CB  
3832 C CB  B SER   B 1   ? 0.3761 0.3578 0.3580 -0.0298 -0.0158 0.0059  1   SER   B CB  
3833 O OG  A SER   B 1   ? 0.4047 0.3812 0.4727 -0.1323 -0.0711 0.0195  1   SER   B OG  
3834 O OG  B SER   B 1   ? 0.3788 0.3567 0.3606 -0.0291 -0.0149 0.0035  1   SER   B OG  
3849 N N   A MET   B 2   ? 0.3087 0.3649 0.3672 -0.1320 -0.0989 0.0964  2   MET   B N   
3850 N N   B MET   B 2   ? 0.3595 0.3600 0.3643 -0.0311 -0.0200 0.0218  2   MET   B N   
3851 C CA  A MET   B 2   ? 0.2904 0.3646 0.3782 -0.1062 -0.0963 0.1157  2   MET   B CA  
3852 C CA  B MET   B 2   ? 0.3495 0.3576 0.3684 -0.0306 -0.0194 0.0275  2   MET   B CA  
3853 C C   A MET   B 2   ? 0.2551 0.3389 0.3422 -0.0820 -0.0966 0.1362  2   MET   B C   
3854 C C   B MET   B 2   ? 0.3258 0.3401 0.3323 -0.0337 -0.0201 0.0322  2   MET   B C   
3855 O O   A MET   B 2   ? 0.2482 0.3521 0.3456 -0.0607 -0.1105 0.1367  2   MET   B O   
3856 O O   B MET   B 2   ? 0.3276 0.3432 0.3329 -0.0321 -0.0176 0.0305  2   MET   B O   
3857 C CB  A MET   B 2   ? 0.3240 0.4011 0.4661 -0.0847 -0.0776 0.0918  2   MET   B CB  
3858 C CB  B MET   B 2   ? 0.3627 0.3721 0.4105 -0.0258 -0.0172 0.0273  2   MET   B CB  
3859 C CG  A MET   B 2   ? 0.3544 0.4341 0.5494 -0.0643 -0.0549 0.0813  2   MET   B CG  
3860 C CG  B MET   B 2   ? 0.3736 0.3843 0.4489 -0.0216 -0.0149 0.0286  2   MET   B CG  
3861 S SD  A MET   B 2   ? 0.3861 0.4671 0.6296 -0.0436 -0.0325 0.0709  2   MET   B SD  
3862 S SD  B MET   B 2   ? 0.3829 0.3950 0.4816 -0.0174 -0.0128 0.0301  2   MET   B SD  
3863 C CE  A MET   B 2   ? 0.3866 0.4694 0.6307 -0.0427 -0.0252 0.0699  2   MET   B CE  
3864 C CE  B MET   B 2   ? 0.3848 0.3971 0.4897 -0.0169 -0.0120 0.0290  2   MET   B CE  
3883 N N   A VAL   B 3   ? 0.2300 0.2961 0.3133 -0.0854 -0.0874 0.1447  3   VAL   B N   
3884 N N   B VAL   B 3   ? 0.2992 0.3181 0.2974 -0.0395 -0.0245 0.0385  3   VAL   B N   
3885 C CA  A VAL   B 3   ? 0.2258 0.2660 0.3077 -0.0775 -0.0781 0.1191  3   VAL   B CA  
3886 C CA  B VAL   B 3   ? 0.2727 0.2959 0.2680 -0.0444 -0.0311 0.0448  3   VAL   B CA  
3887 C C   A VAL   B 3   ? 0.2135 0.2610 0.2621 -0.0648 -0.0747 0.1104  3   VAL   B C   
3888 C C   B VAL   B 3   ? 0.2410 0.2733 0.2377 -0.0519 -0.0461 0.0598  3   VAL   B C   
3889 O O   A VAL   B 3   ? 0.2084 0.2697 0.2765 -0.0645 -0.0779 0.1203  3   VAL   B O   
3890 O O   B VAL   B 3   ? 0.2409 0.2769 0.2268 -0.0487 -0.0435 0.0567  3   VAL   B O   
3891 C CB  A VAL   B 3   ? 0.2497 0.2569 0.3513 -0.0756 -0.0668 0.1017  3   VAL   B CB  
3892 C CB  B VAL   B 3   ? 0.2778 0.2967 0.2728 -0.0433 -0.0248 0.0380  3   VAL   B CB  
3893 C CG1 A VAL   B 3   ? 0.2631 0.2505 0.3707 -0.0717 -0.0711 0.0934  3   VAL   B CG1 
3894 C CG1 B VAL   B 3   ? 0.2800 0.2967 0.2763 -0.0430 -0.0235 0.0347  3   VAL   B CG1 
3895 C CG2 A VAL   B 3   ? 0.2563 0.2630 0.3680 -0.0780 -0.0566 0.1016  3   VAL   B CG2 
3896 C CG2 B VAL   B 3   ? 0.2797 0.2977 0.2743 -0.0429 -0.0230 0.0370  3   VAL   B CG2 
3915 N N   . ASN   B 4   ? 0.2094 0.2456 0.2282 -0.0644 -0.0648 0.0769  4   ASN   B N   
3916 C CA  . ASN   B 4   ? 0.2015 0.2380 0.2017 -0.0669 -0.0547 0.0459  4   ASN   B CA  
3917 C C   . ASN   B 4   ? 0.2141 0.2423 0.1991 -0.0614 -0.0363 0.0324  4   ASN   B C   
3918 O O   . ASN   B 4   ? 0.2153 0.2423 0.2241 -0.0523 -0.0276 0.0189  4   ASN   B O   
3919 C CB  . ASN   B 4   ? 0.1956 0.2286 0.1856 -0.0596 -0.0631 0.0503  4   ASN   B CB  
3920 C CG  . ASN   B 4   ? 0.1960 0.2101 0.1743 -0.0545 -0.0613 0.0396  4   ASN   B CG  
3921 O OD1 . ASN   B 4   ? 0.1995 0.1907 0.1806 -0.0541 -0.0553 0.0356  4   ASN   B OD1 
3922 N ND2 . ASN   B 4   ? 0.2205 0.2184 0.1972 -0.0333 -0.0438 0.0323  4   ASN   B ND2 
3930 N N   . SER   B 5   ? 0.2301 0.2608 0.2173 -0.0627 -0.0252 0.0249  5   SER   B N   
3931 C CA  . SER   B 5   ? 0.2575 0.2991 0.2431 -0.0500 -0.0013 0.0262  5   SER   B CA  
3932 C C   . SER   B 5   ? 0.2730 0.3005 0.2711 -0.0682 0.0273  0.0231  5   SER   B C   
3933 O O   . SER   B 5   ? 0.2818 0.2928 0.3389 -0.0607 0.0599  0.0215  5   SER   B O   
3934 C CB  . SER   B 5   ? 0.2705 0.3264 0.2773 -0.0365 0.0016  0.0340  5   SER   B CB  
3935 O OG  . SER   B 5   ? 0.2958 0.3502 0.3335 -0.0228 0.0031  0.0385  5   SER   B OG  
3941 N N   . PHE   B 6   ? 0.2913 0.3194 0.2425 -0.0753 0.0406  0.0263  6   PHE   B N   
3942 C CA  . PHE   B 6   ? 0.2984 0.3228 0.2124 -0.0937 0.0415  0.0107  6   PHE   B CA  
3943 C C   . PHE   B 6   ? 0.3475 0.3544 0.2529 -0.0983 0.0608  -0.0217 6   PHE   B C   
3944 O O   . PHE   B 6   ? 0.3627 0.3835 0.2829 -0.0883 0.0434  -0.0360 6   PHE   B O   
3945 C CB  . PHE   B 6   ? 0.2659 0.2991 0.1918 -0.0873 0.0176  0.0139  6   PHE   B CB  
3946 C CG  . PHE   B 6   ? 0.2343 0.2638 0.1839 -0.0773 0.0047  0.0053  6   PHE   B CG  
3947 C CD1 . PHE   B 6   ? 0.2285 0.2363 0.1699 -0.0699 -0.0097 0.0067  6   PHE   B CD1 
3948 C CD2 . PHE   B 6   ? 0.2139 0.2557 0.1854 -0.0661 0.0119  0.0303  6   PHE   B CD2 
3949 C CE1 . PHE   B 6   ? 0.2233 0.2135 0.1759 -0.0528 -0.0106 0.0038  6   PHE   B CE1 
3950 C CE2 . PHE   B 6   ? 0.2146 0.2435 0.2123 -0.0444 0.0133  0.0245  6   PHE   B CE2 
3951 C CZ  . PHE   B 6   ? 0.2147 0.2188 0.1872 -0.0441 0.0061  0.0064  6   PHE   B CZ  
3961 N N   . SER   B 7   ? 0.3784 0.3453 0.2576 -0.1192 0.0917  -0.0477 7   SER   B N   
3962 C CA  . SER   B 7   ? 0.4120 0.3623 0.3128 -0.1205 0.1167  -0.0541 7   SER   B CA  
3963 C C   . SER   B 7   ? 0.4118 0.3381 0.3001 -0.1268 0.1320  -0.0729 7   SER   B C   
3964 O O   . SER   B 7   ? 0.4202 0.3349 0.3251 -0.1297 0.1370  -0.0728 7   SER   B O   
3965 C CB  . SER   B 7   ? 0.4358 0.3889 0.3831 -0.1146 0.1320  -0.0474 7   SER   B CB  
3966 O OG  . SER   B 7   ? 0.4509 0.3943 0.4401 -0.1121 0.1268  -0.0366 7   SER   B OG  
3972 N N   . GLY   B 8   ? 0.4108 0.3271 0.3093 -0.1115 0.1355  -0.0834 8   GLY   B N   
3973 C CA  . GLY   B 8   ? 0.3967 0.3093 0.3126 -0.1055 0.1367  -0.0900 8   GLY   B CA  
3974 C C   . GLY   B 8   ? 0.3757 0.2793 0.3066 -0.1064 0.1395  -0.0780 8   GLY   B C   
3975 O O   . GLY   B 8   ? 0.3877 0.2903 0.3420 -0.0961 0.1405  -0.0883 8   GLY   B O   
3979 N N   . TYR   B 9   ? 0.3549 0.2530 0.2794 -0.0979 0.1125  -0.0815 9   TYR   B N   
3980 C CA  . TYR   B 9   ? 0.3326 0.2273 0.2494 -0.0804 0.0829  -0.0627 9   TYR   B CA  
3981 C C   . TYR   B 9   ? 0.3282 0.2325 0.2376 -0.0756 0.0473  -0.0547 9   TYR   B C   
3982 O O   . TYR   B 9   ? 0.3431 0.2533 0.2711 -0.0747 0.0507  -0.0340 9   TYR   B O   
3983 C CB  . TYR   B 9   ? 0.3212 0.2045 0.2552 -0.0692 0.0729  -0.0524 9   TYR   B CB  
3984 C CG  . TYR   B 9   ? 0.3092 0.1891 0.2507 -0.0690 0.0675  -0.0583 9   TYR   B CG  
3985 C CD1 . TYR   B 9   ? 0.3090 0.1912 0.2637 -0.0827 0.0686  -0.0538 9   TYR   B CD1 
3986 C CD2 . TYR   B 9   ? 0.2971 0.1826 0.2461 -0.0599 0.0606  -0.0631 9   TYR   B CD2 
3987 C CE1 . TYR   B 9   ? 0.3032 0.2042 0.2726 -0.0868 0.0704  -0.0656 9   TYR   B CE1 
3988 C CE2 . TYR   B 9   ? 0.2958 0.1842 0.2600 -0.0644 0.0596  -0.0568 9   TYR   B CE2 
3989 C CZ  . TYR   B 9   ? 0.2979 0.2061 0.2733 -0.0763 0.0638  -0.0744 9   TYR   B CZ  
3990 O OH  . TYR   B 9   ? 0.2928 0.2150 0.2841 -0.0860 0.0632  -0.0859 9   TYR   B OH  
4000 N N   . LEU   B 10  ? 0.3100 0.2102 0.2209 -0.0688 0.0256  -0.0548 10  LEU   B N   
4001 C CA  . LEU   B 10  ? 0.3018 0.2081 0.2219 -0.0788 -0.0074 -0.0469 10  LEU   B CA  
4002 C C   . LEU   B 10  ? 0.2770 0.2105 0.2279 -0.0805 -0.0269 -0.0379 10  LEU   B C   
4003 O O   . LEU   B 10  ? 0.2566 0.2152 0.2302 -0.0611 -0.0251 -0.0252 10  LEU   B O   
4004 C CB  . LEU   B 10  ? 0.3245 0.2015 0.2426 -0.0842 -0.0213 -0.0255 10  LEU   B CB  
4005 C CG  . LEU   B 10  ? 0.3478 0.2089 0.2765 -0.0773 -0.0519 -0.0118 10  LEU   B CG  
4006 C CD1 . LEU   B 10  ? 0.3639 0.2211 0.2931 -0.0676 -0.0538 -0.0119 10  LEU   B CD1 
4007 C CD2 . LEU   B 10  ? 0.3565 0.2135 0.3034 -0.0815 -0.0468 0.0079  10  LEU   B CD2 
4019 N N   . LYS   B 11  ? 0.2965 0.2420 0.2299 -0.0694 -0.0302 -0.0280 11  LYS   B N   
4020 C CA  . LYS   B 11  ? 0.3177 0.2693 0.2665 -0.0572 -0.0363 -0.0268 11  LYS   B CA  
4021 C C   . LYS   B 11  ? 0.3015 0.2425 0.2751 -0.0773 -0.0296 -0.0417 11  LYS   B C   
4022 O O   . LYS   B 11  ? 0.3211 0.2583 0.3084 -0.0954 -0.0231 -0.0776 11  LYS   B O   
4023 C CB  . LYS   B 11  ? 0.3522 0.3218 0.3254 -0.0289 -0.0456 -0.0194 11  LYS   B CB  
4024 C CG  . LYS   B 11  ? 0.3848 0.3577 0.3923 -0.0121 -0.0550 -0.0216 11  LYS   B CG  
4025 C CD  . LYS   B 11  ? 0.4102 0.3812 0.4525 -0.0013 -0.0578 -0.0231 11  LYS   B CD  
4026 C CE  . LYS   B 11  ? 0.4298 0.3961 0.4989 0.0018  -0.0567 -0.0240 11  LYS   B CE  
4027 N NZ  . LYS   B 11  ? 0.4412 0.4051 0.5218 0.0032  -0.0573 -0.0221 11  LYS   B NZ  
4041 N N   . LEU   B 12  ? 0.2571 0.2111 0.2679 -0.0693 -0.0307 -0.0382 12  LEU   B N   
4042 C CA  . LEU   B 12  ? 0.2404 0.1951 0.2770 -0.0610 -0.0343 -0.0362 12  LEU   B CA  
4043 C C   . LEU   B 12  ? 0.2298 0.1986 0.2856 -0.0584 -0.0517 -0.0355 12  LEU   B C   
4044 O O   . LEU   B 12  ? 0.2297 0.1977 0.3078 -0.0669 -0.0611 -0.0301 12  LEU   B O   
4045 C CB  . LEU   B 12  ? 0.2417 0.1707 0.2718 -0.0465 -0.0256 -0.0406 12  LEU   B CB  
4046 C CG  . LEU   B 12  ? 0.2455 0.1683 0.2723 -0.0450 -0.0137 -0.0277 12  LEU   B CG  
4047 C CD1 . LEU   B 12  ? 0.2596 0.1681 0.2810 -0.0308 -0.0067 -0.0170 12  LEU   B CD1 
4048 C CD2 . LEU   B 12  ? 0.2511 0.1732 0.2776 -0.0409 -0.0044 -0.0330 12  LEU   B CD2 
4060 N N   . THR   B 13  ? 0.2231 0.2033 0.2891 -0.0620 -0.0510 -0.0459 13  THR   B N   
4061 C CA  . THR   B 13  ? 0.2277 0.2080 0.2775 -0.0727 -0.0597 -0.0316 13  THR   B CA  
4062 C C   . THR   B 13  ? 0.2717 0.2286 0.3006 -0.0807 -0.0689 -0.0294 13  THR   B C   
4063 O O   . THR   B 13  ? 0.2899 0.2288 0.3111 -0.0764 -0.0287 -0.0336 13  THR   B O   
4064 C CB  . THR   B 13  ? 0.2106 0.2030 0.2834 -0.0611 -0.0515 -0.0232 13  THR   B CB  
4065 O OG1 . THR   B 13  ? 0.2023 0.2004 0.2830 -0.0478 -0.0423 -0.0229 13  THR   B OG1 
4066 C CG2 . THR   B 13  ? 0.2179 0.2116 0.2946 -0.0513 -0.0416 -0.0105 13  THR   B CG2 
4074 N N   A ASP   B 14  ? 0.2901 0.2461 0.3243 -0.0882 -0.1037 -0.0098 14  ASP   B N   
4075 N N   B ASP   B 14  ? 0.2790 0.2380 0.3144 -0.0788 -0.0692 -0.0207 14  ASP   B N   
4076 C CA  A ASP   B 14  ? 0.3060 0.2701 0.3499 -0.0870 -0.1136 0.0148  14  ASP   B CA  
4077 C CA  B ASP   B 14  ? 0.2832 0.2460 0.3284 -0.0759 -0.0689 -0.0106 14  ASP   B CA  
4078 C C   A ASP   B 14  ? 0.2912 0.2481 0.3044 -0.0934 -0.1000 0.0118  14  ASP   B C   
4079 C C   B ASP   B 14  ? 0.2685 0.2299 0.2950 -0.0762 -0.0771 -0.0031 14  ASP   B C   
4080 O O   A ASP   B 14  ? 0.3242 0.2718 0.3109 -0.0959 -0.0949 0.0227  14  ASP   B O   
4081 O O   B ASP   B 14  ? 0.2749 0.2315 0.2928 -0.0747 -0.0765 -0.0054 14  ASP   B O   
4082 C CB  A ASP   B 14  ? 0.3304 0.3144 0.4219 -0.0786 -0.1296 0.0224  14  ASP   B CB  
4083 C CB  B ASP   B 14  ? 0.2993 0.2670 0.3743 -0.0721 -0.0605 -0.0105 14  ASP   B CB  
4084 C CG  A ASP   B 14  ? 0.3622 0.3529 0.4965 -0.0699 -0.1264 0.0108  14  ASP   B CG  
4085 C CG  B ASP   B 14  ? 0.3150 0.2838 0.4124 -0.0675 -0.0520 -0.0131 14  ASP   B CG  
4086 O OD1 A ASP   B 14  ? 0.3808 0.3684 0.5142 -0.0687 -0.1264 -0.0042 14  ASP   B OD1 
4087 O OD1 B ASP   B 14  ? 0.3212 0.2909 0.4247 -0.0653 -0.0488 -0.0160 14  ASP   B OD1 
4088 O OD2 A ASP   B 14  ? 0.3690 0.3701 0.5364 -0.0691 -0.1216 0.0143  14  ASP   B OD2 
4089 O OD2 B ASP   B 14  ? 0.3196 0.2887 0.4272 -0.0685 -0.0504 -0.0129 14  ASP   B OD2 
4098 N N   . ASN   B 15  ? 0.2476 0.2115 0.2687 -0.0725 -0.0872 0.0086  15  ASN   B N   
4099 C CA  . ASN   B 15  ? 0.2030 0.1839 0.2480 -0.0451 -0.0586 0.0041  15  ASN   B CA  
4100 C C   . ASN   B 15  ? 0.1810 0.1710 0.2333 -0.0228 -0.0529 -0.0038 15  ASN   B C   
4101 O O   . ASN   B 15  ? 0.1801 0.1610 0.2453 -0.0245 -0.0521 -0.0171 15  ASN   B O   
4102 C CB  . ASN   B 15  ? 0.1886 0.1770 0.2587 -0.0230 -0.0581 0.0068  15  ASN   B CB  
4103 C CG  . ASN   B 15  ? 0.1678 0.1789 0.2780 -0.0269 -0.0343 0.0086  15  ASN   B CG  
4104 O OD1 . ASN   B 15  ? 0.1771 0.2080 0.3054 -0.0450 -0.0356 0.0128  15  ASN   B OD1 
4105 N ND2 . ASN   B 15  ? 0.1710 0.1490 0.2693 -0.0141 -0.0082 -0.0115 15  ASN   B ND2 
4113 N N   . VAL   B 16  ? 0.1796 0.1613 0.2316 -0.0364 -0.0573 -0.0112 16  VAL   B N   
4114 C CA  . VAL   B 16  ? 0.1743 0.1628 0.2146 -0.0326 -0.0336 -0.0276 16  VAL   B CA  
4115 C C   . VAL   B 16  ? 0.1704 0.1755 0.2185 -0.0371 -0.0392 -0.0146 16  VAL   B C   
4116 O O   . VAL   B 16  ? 0.1797 0.1906 0.2444 -0.0355 -0.0318 -0.0304 16  VAL   B O   
4117 C CB  . VAL   B 16  ? 0.1807 0.1581 0.2303 -0.0190 -0.0157 -0.0230 16  VAL   B CB  
4118 C CG1 . VAL   B 16  ? 0.1976 0.1554 0.2267 -0.0004 -0.0156 -0.0124 16  VAL   B CG1 
4119 C CG2 . VAL   B 16  ? 0.1809 0.1586 0.2552 -0.0124 -0.0115 -0.0187 16  VAL   B CG2 
4129 N N   . TYR   B 17  ? 0.1838 0.1806 0.2174 -0.0337 -0.0281 -0.0233 17  TYR   B N   
4130 C CA  . TYR   B 17  ? 0.1908 0.1945 0.2051 -0.0396 -0.0257 0.0008  17  TYR   B CA  
4131 C C   . TYR   B 17  ? 0.1874 0.1650 0.2131 -0.0457 -0.0202 -0.0187 17  TYR   B C   
4132 O O   . TYR   B 17  ? 0.1859 0.1682 0.2222 -0.0314 -0.0389 -0.0369 17  TYR   B O   
4133 C CB  . TYR   B 17  ? 0.2275 0.2440 0.2418 -0.0277 -0.0280 0.0302  17  TYR   B CB  
4134 C CG  . TYR   B 17  ? 0.2660 0.3003 0.3024 -0.0169 -0.0415 0.0353  17  TYR   B CG  
4135 C CD1 . TYR   B 17  ? 0.2855 0.3188 0.3249 -0.0138 -0.0550 0.0435  17  TYR   B CD1 
4136 C CD2 . TYR   B 17  ? 0.2913 0.3329 0.3304 -0.0051 -0.0550 0.0351  17  TYR   B CD2 
4137 C CE1 . TYR   B 17  ? 0.3061 0.3475 0.3455 -0.0050 -0.0676 0.0430  17  TYR   B CE1 
4138 C CE2 . TYR   B 17  ? 0.3082 0.3562 0.3511 0.0058  -0.0734 0.0426  17  TYR   B CE2 
4139 C CZ  . TYR   B 17  ? 0.3179 0.3636 0.3614 0.0058  -0.0787 0.0445  17  TYR   B CZ  
4140 O OH  . TYR   B 17  ? 0.3358 0.3789 0.3766 0.0143  -0.0859 0.0475  17  TYR   B OH  
4150 N N   . ILE   B 18  ? 0.1953 0.1641 0.1990 -0.0394 -0.0142 -0.0216 18  ILE   B N   
4151 C CA  . ILE   B 18  ? 0.2015 0.1652 0.1962 -0.0430 -0.0074 -0.0280 18  ILE   B CA  
4152 C C   . ILE   B 18  ? 0.2105 0.1678 0.1990 -0.0492 -0.0017 -0.0391 18  ILE   B C   
4153 O O   . ILE   B 18  ? 0.2278 0.1813 0.2161 -0.0456 0.0113  -0.0436 18  ILE   B O   
4154 C CB  . ILE   B 18  ? 0.2096 0.1666 0.2095 -0.0450 -0.0041 -0.0181 18  ILE   B CB  
4155 C CG1 . ILE   B 18  ? 0.2109 0.1737 0.2227 -0.0447 -0.0037 -0.0073 18  ILE   B CG1 
4156 C CG2 . ILE   B 18  ? 0.2128 0.1666 0.2162 -0.0476 -0.0187 -0.0133 18  ILE   B CG2 
4157 C CD1 . ILE   B 18  ? 0.2225 0.2001 0.2441 -0.0457 -0.0166 0.0199  18  ILE   B CD1 
4169 N N   . LYS   B 19  ? 0.2072 0.1652 0.2216 -0.0339 0.0288  -0.0467 19  LYS   B N   
4170 C CA  . LYS   B 19  ? 0.2142 0.1698 0.2429 -0.0363 0.0230  -0.0483 19  LYS   B CA  
4171 C C   . LYS   B 19  ? 0.2022 0.1683 0.2515 -0.0313 0.0368  -0.0528 19  LYS   B C   
4172 O O   . LYS   B 19  ? 0.1954 0.1721 0.2363 -0.0147 0.0250  -0.0503 19  LYS   B O   
4173 C CB  . LYS   B 19  ? 0.2357 0.1916 0.2517 -0.0412 0.0286  -0.0448 19  LYS   B CB  
4174 C CG  . LYS   B 19  ? 0.2614 0.2152 0.2748 -0.0480 0.0432  -0.0478 19  LYS   B CG  
4175 C CD  . LYS   B 19  ? 0.2898 0.2496 0.2893 -0.0550 0.0535  -0.0374 19  LYS   B CD  
4176 C CE  . LYS   B 19  ? 0.3193 0.2791 0.3131 -0.0565 0.0507  -0.0400 19  LYS   B CE  
4177 N NZ  . LYS   B 19  ? 0.3375 0.2962 0.3227 -0.0597 0.0537  -0.0372 19  LYS   B NZ  
4191 N N   . ASN   B 20  ? 0.2013 0.1769 0.2877 -0.0284 0.0468  -0.0665 20  ASN   B N   
4192 C CA  . ASN   B 20  ? 0.2081 0.1916 0.3118 -0.0153 0.0494  -0.0786 20  ASN   B CA  
4193 C C   . ASN   B 20  ? 0.1976 0.2081 0.3195 -0.0176 0.0611  -0.0908 20  ASN   B C   
4194 O O   . ASN   B 20  ? 0.2183 0.2480 0.3436 -0.0367 0.0595  -0.0873 20  ASN   B O   
4195 C CB  . ASN   B 20  ? 0.2374 0.1928 0.3357 0.0053  0.0391  -0.0750 20  ASN   B CB  
4196 C CG  . ASN   B 20  ? 0.2700 0.2027 0.3606 0.0373  0.0399  -0.0778 20  ASN   B CG  
4197 O OD1 . ASN   B 20  ? 0.3029 0.2349 0.3850 0.0551  0.0385  -0.0828 20  ASN   B OD1 
4198 N ND2 . ASN   B 20  ? 0.2637 0.2037 0.3563 0.0339  0.0285  -0.0744 20  ASN   B ND2 
4205 N N   . ALA   B 21  ? 0.2003 0.1852 0.3187 -0.0207 0.0593  -0.0749 21  ALA   B N   
4206 C CA  . ALA   B 21  ? 0.2137 0.1940 0.3273 -0.0290 0.0443  -0.0631 21  ALA   B CA  
4207 C C   . ALA   B 21  ? 0.2130 0.1734 0.3139 -0.0221 0.0504  -0.0390 21  ALA   B C   
4208 O O   . ALA   B 21  ? 0.2177 0.1653 0.3199 -0.0356 0.0516  -0.0309 21  ALA   B O   
4209 C CB  . ALA   B 21  ? 0.2260 0.2252 0.3394 -0.0491 0.0406  -0.0399 21  ALA   B CB  
4215 N N   . ASP   B 22  ? 0.2038 0.1615 0.3013 -0.0215 0.0374  -0.0352 22  ASP   B N   
4216 C CA  . ASP   B 22  ? 0.2032 0.1578 0.2938 -0.0107 0.0239  -0.0308 22  ASP   B CA  
4217 C C   . ASP   B 22  ? 0.1974 0.1600 0.2450 -0.0187 0.0180  -0.0159 22  ASP   B C   
4218 O O   . ASP   B 22  ? 0.2018 0.1623 0.2484 -0.0101 0.0125  -0.0110 22  ASP   B O   
4219 C CB  . ASP   B 22  ? 0.2113 0.1656 0.3391 -0.0071 0.0211  -0.0148 22  ASP   B CB  
4220 C CG  . ASP   B 22  ? 0.2152 0.1859 0.3897 -0.0040 0.0019  -0.0142 22  ASP   B CG  
4221 O OD1 . ASP   B 22  ? 0.2319 0.1839 0.3923 -0.0002 -0.0196 -0.0169 22  ASP   B OD1 
4222 O OD2 . ASP   B 22  ? 0.2277 0.2192 0.4408 0.0090  -0.0157 -0.0211 22  ASP   B OD2 
4227 N N   . ILE   B 23  ? 0.1965 0.1509 0.2286 -0.0128 0.0063  0.0046  23  ILE   B N   
4228 C CA  . ILE   B 23  ? 0.1885 0.1528 0.2059 -0.0132 0.0045  -0.0029 23  ILE   B CA  
4229 C C   . ILE   B 23  ? 0.1778 0.1524 0.2037 -0.0059 -0.0060 -0.0061 23  ILE   B C   
4230 O O   . ILE   B 23  ? 0.1685 0.1483 0.1998 -0.0105 -0.0008 0.0036  23  ILE   B O   
4231 C CB  . ILE   B 23  ? 0.1831 0.1564 0.2161 -0.0215 -0.0001 0.0073  23  ILE   B CB  
4232 C CG1 . ILE   B 23  ? 0.1864 0.1689 0.2249 -0.0124 0.0064  0.0143  23  ILE   B CG1 
4233 C CG2 . ILE   B 23  ? 0.1966 0.1785 0.2276 -0.0209 -0.0029 -0.0001 23  ILE   B CG2 
4234 C CD1 . ILE   B 23  ? 0.1862 0.1770 0.2372 -0.0020 -0.0020 0.0183  23  ILE   B CD1 
4246 N N   . VAL   B 24  ? 0.1785 0.1503 0.2182 -0.0076 -0.0105 -0.0080 24  VAL   B N   
4247 C CA  . VAL   B 24  ? 0.1735 0.1526 0.2394 -0.0073 -0.0148 -0.0023 24  VAL   B CA  
4248 C C   . VAL   B 24  ? 0.1673 0.1569 0.2451 -0.0119 -0.0134 -0.0013 24  VAL   B C   
4249 O O   . VAL   B 24  ? 0.1680 0.1694 0.2542 -0.0162 -0.0120 0.0100  24  VAL   B O   
4250 C CB  . VAL   B 24  ? 0.1840 0.1725 0.2474 0.0051  -0.0276 0.0016  24  VAL   B CB  
4251 C CG1 . VAL   B 24  ? 0.1846 0.1808 0.2742 0.0009  -0.0290 -0.0005 24  VAL   B CG1 
4252 C CG2 . VAL   B 24  ? 0.1919 0.1964 0.2506 0.0103  -0.0252 -0.0052 24  VAL   B CG2 
4262 N N   . GLU   B 25  ? 0.1957 0.1710 0.2526 -0.0143 0.0017  0.0045  25  GLU   B N   
4263 C CA  . GLU   B 25  ? 0.2155 0.2049 0.2771 -0.0061 0.0167  -0.0069 25  GLU   B CA  
4264 C C   . GLU   B 25  ? 0.2039 0.1957 0.2390 -0.0140 0.0165  -0.0012 25  GLU   B C   
4265 O O   . GLU   B 25  ? 0.2014 0.2122 0.2555 -0.0116 0.0286  0.0022  25  GLU   B O   
4266 C CB  . GLU   B 25  ? 0.2663 0.2621 0.3585 0.0143  0.0265  -0.0134 25  GLU   B CB  
4267 C CG  . GLU   B 25  ? 0.3135 0.3284 0.4699 0.0224  0.0213  -0.0178 25  GLU   B CG  
4268 C CD  . GLU   B 25  ? 0.3670 0.3875 0.5586 0.0234  0.0181  -0.0224 25  GLU   B CD  
4269 O OE1 . GLU   B 25  ? 0.3885 0.4078 0.5887 0.0298  0.0215  -0.0219 25  GLU   B OE1 
4270 O OE2 . GLU   B 25  ? 0.3820 0.4034 0.5892 0.0236  0.0149  -0.0314 25  GLU   B OE2 
4277 N N   A GLU   B 26  ? 0.2012 0.1864 0.2058 -0.0304 0.0123  0.0030  26  GLU   B N   
4278 N N   B GLU   B 26  ? 0.2009 0.1950 0.2237 -0.0217 0.0119  0.0016  26  GLU   B N   
4279 C CA  A GLU   B 26  ? 0.2015 0.1994 0.2180 -0.0418 0.0009  0.0005  26  GLU   B CA  
4280 C CA  B GLU   B 26  ? 0.1988 0.1953 0.2202 -0.0273 0.0078  0.0056  26  GLU   B CA  
4281 C C   A GLU   B 26  ? 0.1815 0.1933 0.1938 -0.0321 0.0107  0.0165  26  GLU   B C   
4282 C C   B GLU   B 26  ? 0.1828 0.1879 0.2028 -0.0260 0.0071  0.0132  26  GLU   B C   
4283 O O   A GLU   B 26  ? 0.2010 0.2180 0.2080 -0.0268 0.0035  0.0246  26  GLU   B O   
4284 O O   B GLU   B 26  ? 0.1874 0.1946 0.2024 -0.0248 0.0040  0.0139  26  GLU   B O   
4285 C CB  A GLU   B 26  ? 0.2328 0.2184 0.2474 -0.0574 0.0102  0.0035  26  GLU   B CB  
4286 C CB  B GLU   B 26  ? 0.2126 0.2025 0.2367 -0.0335 0.0114  0.0061  26  GLU   B CB  
4287 C CG  A GLU   B 26  ? 0.2717 0.2595 0.3031 -0.0576 0.0155  -0.0200 26  GLU   B CG  
4288 C CG  B GLU   B 26  ? 0.2263 0.2136 0.2563 -0.0384 0.0176  0.0047  26  GLU   B CG  
4289 C CD  A GLU   B 26  ? 0.2926 0.2784 0.3160 -0.0692 0.0308  -0.0512 26  GLU   B CD  
4290 C CD  B GLU   B 26  ? 0.2354 0.2209 0.2658 -0.0471 0.0299  0.0032  26  GLU   B CD  
4291 O OE1 A GLU   B 26  ? 0.3045 0.2667 0.3260 -0.0882 0.0578  -0.0540 26  GLU   B OE1 
4292 O OE1 B GLU   B 26  ? 0.2418 0.2203 0.2664 -0.0489 0.0418  0.0064  26  GLU   B OE1 
4293 O OE2 A GLU   B 26  ? 0.2978 0.3068 0.3596 -0.0552 0.0270  -0.0512 26  GLU   B OE2 
4294 O OE2 B GLU   B 26  ? 0.2346 0.2242 0.2761 -0.0523 0.0331  0.0104  26  GLU   B OE2 
4307 N N   . ALA   B 27  ? 0.1653 0.1753 0.2005 -0.0257 0.0065  0.0179  27  ALA   B N   
4308 C CA  . ALA   B 27  ? 0.1704 0.1681 0.2202 -0.0147 0.0081  0.0328  27  ALA   B CA  
4309 C C   . ALA   B 27  ? 0.1730 0.1807 0.2416 -0.0162 0.0153  0.0391  27  ALA   B C   
4310 O O   . ALA   B 27  ? 0.1815 0.1842 0.2580 -0.0087 0.0149  0.0396  27  ALA   B O   
4311 C CB  . ALA   B 27  ? 0.1934 0.1487 0.2309 -0.0161 0.0083  0.0210  27  ALA   B CB  
4318 N N   . LYS   B 28  ? 0.1675 0.2040 0.2848 -0.0236 0.0184  0.0560  28  LYS   B N   
4319 C CA  . LYS   B 28  ? 0.1896 0.2477 0.3093 -0.0140 0.0545  0.0744  28  LYS   B CA  
4320 C C   . LYS   B 28  ? 0.2244 0.2743 0.2925 -0.0063 0.0643  0.0701  28  LYS   B C   
4321 O O   . LYS   B 28  ? 0.2407 0.2777 0.3022 -0.0098 0.0658  0.0674  28  LYS   B O   
4322 C CB  . LYS   B 28  ? 0.2095 0.2795 0.3576 0.0007  0.0746  0.0977  28  LYS   B CB  
4323 C CG  . LYS   B 28  ? 0.2387 0.3233 0.4004 0.0168  0.0702  0.1124  28  LYS   B CG  
4324 C CD  . LYS   B 28  ? 0.2883 0.3793 0.4553 0.0249  0.0809  0.1139  28  LYS   B CD  
4325 C CE  . LYS   B 28  ? 0.3246 0.4165 0.4970 0.0328  0.0854  0.1185  28  LYS   B CE  
4326 N NZ  . LYS   B 28  ? 0.3536 0.4285 0.5201 0.0414  0.0825  0.1217  28  LYS   B NZ  
4340 N N   A LYS   B 29  ? 0.2426 0.2922 0.2920 0.0098  0.0690  0.0570  29  LYS   B N   
4341 N N   B LYS   B 29  ? 0.2470 0.2954 0.3007 -0.0039 0.0547  0.0623  29  LYS   B N   
4342 C CA  A LYS   B 29  ? 0.2835 0.3218 0.3199 0.0102  0.0648  0.0522  29  LYS   B CA  
4343 C CA  B LYS   B 29  ? 0.2705 0.3166 0.3188 -0.0033 0.0445  0.0572  29  LYS   B CA  
4344 C C   A LYS   B 29  ? 0.2765 0.3232 0.2851 0.0099  0.0487  0.0613  29  LYS   B C   
4345 C C   B LYS   B 29  ? 0.2637 0.3149 0.2879 -0.0032 0.0395  0.0628  29  LYS   B C   
4346 O O   A LYS   B 29  ? 0.2934 0.3432 0.2953 0.0176  0.0511  0.0626  29  LYS   B O   
4347 O O   B LYS   B 29  ? 0.2697 0.3201 0.2887 -0.0019 0.0400  0.0634  29  LYS   B O   
4348 C CB  A LYS   B 29  ? 0.3356 0.3537 0.3966 0.0089  0.0626  0.0380  29  LYS   B CB  
4349 C CB  B LYS   B 29  ? 0.3005 0.3385 0.3725 -0.0027 0.0364  0.0450  29  LYS   B CB  
4350 C CG  A LYS   B 29  ? 0.3792 0.3789 0.4779 0.0064  0.0627  0.0319  29  LYS   B CG  
4351 C CG  B LYS   B 29  ? 0.3266 0.3567 0.4250 -0.0022 0.0296  0.0353  29  LYS   B CG  
4352 C CD  A LYS   B 29  ? 0.4147 0.3957 0.5429 0.0013  0.0697  0.0269  29  LYS   B CD  
4353 C CD  B LYS   B 29  ? 0.3470 0.3707 0.4673 -0.0024 0.0254  0.0273  29  LYS   B CD  
4354 C CE  A LYS   B 29  ? 0.4392 0.4064 0.5901 -0.0036 0.0771  0.0239  29  LYS   B CE  
4355 C CE  B LYS   B 29  ? 0.3608 0.3799 0.4977 -0.0030 0.0234  0.0215  29  LYS   B CE  
4356 N NZ  A LYS   B 29  ? 0.4487 0.4124 0.6196 -0.0063 0.0801  0.0236  29  LYS   B NZ  
4357 N NZ  B LYS   B 29  ? 0.3672 0.3840 0.5151 -0.0033 0.0223  0.0189  29  LYS   B NZ  
4384 N N   . VAL   B 30  ? 0.2485 0.3065 0.2639 -0.0055 0.0360  0.0669  30  VAL   B N   
4385 C CA  . VAL   B 30  ? 0.2265 0.2881 0.2856 -0.0148 -0.0038 0.0722  30  VAL   B CA  
4386 C C   . VAL   B 30  ? 0.2017 0.2775 0.2818 -0.0116 0.0039  0.1016  30  VAL   B C   
4387 O O   . VAL   B 30  ? 0.2147 0.2936 0.2895 -0.0056 0.0142  0.1156  30  VAL   B O   
4388 C CB  . VAL   B 30  ? 0.2264 0.2776 0.3143 -0.0357 -0.0295 0.0585  30  VAL   B CB  
4389 C CG1 . VAL   B 30  ? 0.2247 0.2808 0.3134 -0.0416 -0.0215 0.0547  30  VAL   B CG1 
4390 C CG2 . VAL   B 30  ? 0.2398 0.2778 0.3309 -0.0414 -0.0421 0.0392  30  VAL   B CG2 
4401 N N   . LYS   B 31  ? 0.1822 0.2422 0.3188 -0.0215 0.0042  0.1019  31  LYS   B N   
4402 C CA  . LYS   B 31  ? 0.1750 0.2405 0.3495 -0.0378 -0.0041 0.1072  31  LYS   B CA  
4403 C C   . LYS   B 31  ? 0.1700 0.2022 0.3112 -0.0391 -0.0242 0.0845  31  LYS   B C   
4404 O O   . LYS   B 31  ? 0.1733 0.2187 0.3196 -0.0302 -0.0205 0.1053  31  LYS   B O   
4405 C CB  . LYS   B 31  ? 0.2009 0.2926 0.4088 -0.0328 0.0123  0.1253  31  LYS   B CB  
4406 C CG  . LYS   B 31  ? 0.2479 0.3482 0.4593 -0.0318 0.0254  0.1296  31  LYS   B CG  
4407 C CD  . LYS   B 31  ? 0.2928 0.3975 0.5025 -0.0226 0.0205  0.1231  31  LYS   B CD  
4408 C CE  . LYS   B 31  ? 0.3206 0.4269 0.5384 -0.0173 0.0115  0.1147  31  LYS   B CE  
4409 N NZ  . LYS   B 31  ? 0.3296 0.4450 0.5541 -0.0094 0.0031  0.1052  31  LYS   B NZ  
4423 N N   . PRO   B 32  ? 0.1808 0.1629 0.2461 -0.0333 -0.0424 0.0519  32  PRO   B N   
4424 C CA  . PRO   B 32  ? 0.1883 0.1612 0.2032 -0.0320 -0.0425 0.0295  32  PRO   B CA  
4425 C C   . PRO   B 32  ? 0.2003 0.1535 0.1937 -0.0381 -0.0548 0.0309  32  PRO   B C   
4426 O O   . PRO   B 32  ? 0.2130 0.1559 0.2280 -0.0385 -0.0750 0.0291  32  PRO   B O   
4427 C CB  . PRO   B 32  ? 0.2022 0.1574 0.2092 -0.0357 -0.0266 0.0177  32  PRO   B CB  
4428 C CG  . PRO   B 32  ? 0.2157 0.1487 0.2233 -0.0337 -0.0439 0.0209  32  PRO   B CG  
4429 C CD  . PRO   B 32  ? 0.2000 0.1528 0.2371 -0.0276 -0.0593 0.0260  32  PRO   B CD  
4437 N N   . THR   B 33  ? 0.2030 0.1495 0.1860 -0.0340 -0.0522 0.0232  33  THR   B N   
4438 C CA  . THR   B 33  ? 0.2089 0.1511 0.1879 -0.0364 -0.0496 0.0284  33  THR   B CA  
4439 C C   . THR   B 33  ? 0.2125 0.1385 0.1874 -0.0298 -0.0429 0.0186  33  THR   B C   
4440 O O   . THR   B 33  ? 0.2347 0.1429 0.1905 -0.0445 -0.0482 0.0186  33  THR   B O   
4441 C CB  . THR   B 33  ? 0.2182 0.1639 0.1932 -0.0220 -0.0524 0.0370  33  THR   B CB  
4442 O OG1 . THR   B 33  ? 0.2115 0.1753 0.1979 -0.0192 -0.0504 0.0321  33  THR   B OG1 
4443 C CG2 . THR   B 33  ? 0.2391 0.1641 0.2193 -0.0160 -0.0556 0.0202  33  THR   B CG2 
4451 N N   . VAL   B 34  ? 0.1850 0.1379 0.1731 -0.0278 -0.0339 0.0123  34  VAL   B N   
4452 C CA  . VAL   B 34  ? 0.1751 0.1378 0.1685 -0.0248 -0.0340 0.0058  34  VAL   B CA  
4453 C C   . VAL   B 34  ? 0.1574 0.1314 0.1603 -0.0289 -0.0189 0.0044  34  VAL   B C   
4454 O O   . VAL   B 34  ? 0.1810 0.1349 0.1641 -0.0236 -0.0330 0.0095  34  VAL   B O   
4455 C CB  . VAL   B 34  ? 0.1802 0.1511 0.1994 -0.0091 -0.0271 0.0038  34  VAL   B CB  
4456 C CG1 . VAL   B 34  ? 0.1818 0.1693 0.2032 -0.0022 -0.0139 -0.0141 34  VAL   B CG1 
4457 C CG2 . VAL   B 34  ? 0.1792 0.1610 0.2237 -0.0039 -0.0228 0.0004  34  VAL   B CG2 
4467 N N   . VAL   B 35  ? 0.1538 0.1239 0.1522 -0.0264 -0.0167 0.0072  35  VAL   B N   
4468 C CA  . VAL   B 35  ? 0.1470 0.1250 0.1529 -0.0277 -0.0142 0.0067  35  VAL   B CA  
4469 C C   . VAL   B 35  ? 0.1395 0.1198 0.1537 -0.0207 -0.0137 0.0119  35  VAL   B C   
4470 O O   . VAL   B 35  ? 0.1450 0.1225 0.1673 -0.0239 -0.0017 -0.0033 35  VAL   B O   
4471 C CB  . VAL   B 35  ? 0.1476 0.1445 0.1656 -0.0222 0.0019  0.0028  35  VAL   B CB  
4472 C CG1 . VAL   B 35  ? 0.1403 0.1593 0.2024 -0.0233 -0.0013 -0.0042 35  VAL   B CG1 
4473 C CG2 . VAL   B 35  ? 0.1490 0.1466 0.1735 -0.0112 0.0027  -0.0003 35  VAL   B CG2 
4483 N N   . VAL   B 36  ? 0.1427 0.1204 0.1470 -0.0162 -0.0136 0.0099  36  VAL   B N   
4484 C CA  . VAL   B 36  ? 0.1391 0.1147 0.1523 -0.0134 -0.0052 0.0030  36  VAL   B CA  
4485 C C   . VAL   B 36  ? 0.1315 0.1179 0.1340 -0.0087 -0.0053 0.0027  36  VAL   B C   
4486 O O   . VAL   B 36  ? 0.1376 0.1327 0.1662 -0.0082 -0.0006 -0.0041 36  VAL   B O   
4487 C CB  . VAL   B 36  ? 0.1359 0.1250 0.1531 -0.0134 -0.0059 0.0052  36  VAL   B CB  
4488 C CG1 . VAL   B 36  ? 0.1369 0.1430 0.1784 -0.0198 -0.0064 0.0034  36  VAL   B CG1 
4489 C CG2 . VAL   B 36  ? 0.1452 0.1296 0.1643 -0.0110 -0.0150 0.0055  36  VAL   B CG2 
4499 N N   . ASN   B 37  ? 0.1349 0.1282 0.1466 -0.0010 -0.0101 0.0047  37  ASN   B N   
4500 C CA  . ASN   B 37  ? 0.1330 0.1288 0.1676 -0.0041 -0.0075 0.0111  37  ASN   B CA  
4501 C C   . ASN   B 37  ? 0.1318 0.1335 0.1614 0.0026  -0.0117 0.0063  37  ASN   B C   
4502 O O   . ASN   B 37  ? 0.1425 0.1443 0.1512 0.0024  -0.0018 0.0061  37  ASN   B O   
4503 C CB  . ASN   B 37  ? 0.1335 0.1375 0.1563 0.0001  -0.0129 0.0106  37  ASN   B CB  
4504 C CG  . ASN   B 37  ? 0.1434 0.1375 0.1665 -0.0073 -0.0134 0.0030  37  ASN   B CG  
4505 O OD1 . ASN   B 37  ? 0.1464 0.1436 0.1816 0.0068  -0.0161 0.0038  37  ASN   B OD1 
4506 N ND2 . ASN   B 37  ? 0.1523 0.1368 0.1623 -0.0076 -0.0197 0.0070  37  ASN   B ND2 
4513 N N   . ALA   B 38  ? 0.1448 0.1281 0.1601 0.0042  0.0017  0.0033  38  ALA   B N   
4514 C CA  . ALA   B 38  ? 0.1589 0.1321 0.1684 -0.0030 0.0068  0.0103  38  ALA   B CA  
4515 C C   . ALA   B 38  ? 0.1527 0.1288 0.1609 -0.0008 0.0039  0.0132  38  ALA   B C   
4516 O O   . ALA   B 38  ? 0.1610 0.1400 0.1775 0.0074  0.0015  0.0126  38  ALA   B O   
4517 C CB  . ALA   B 38  ? 0.1835 0.1409 0.1876 -0.0146 0.0165  0.0111  38  ALA   B CB  
4523 N N   . ALA   B 39  ? 0.1549 0.1320 0.1546 0.0079  -0.0085 -0.0010 39  ALA   B N   
4524 C CA  . ALA   B 39  ? 0.1619 0.1436 0.1546 0.0062  -0.0025 0.0051  39  ALA   B CA  
4525 C C   . ALA   B 39  ? 0.1612 0.1517 0.1417 0.0065  -0.0061 -0.0052 39  ALA   B C   
4526 O O   . ALA   B 39  ? 0.1656 0.1555 0.1671 -0.0029 -0.0064 0.0114  39  ALA   B O   
4527 C CB  . ALA   B 39  ? 0.1604 0.1462 0.1652 -0.0036 -0.0026 0.0073  39  ALA   B CB  
4533 N N   . ASN   B 40  ? 0.1661 0.1713 0.1455 -0.0050 -0.0001 -0.0023 40  ASN   B N   
4534 C CA  . ASN   B 40  ? 0.1743 0.1778 0.1548 0.0027  -0.0011 -0.0035 40  ASN   B CA  
4535 C C   . ASN   B 40  ? 0.1790 0.1784 0.1507 0.0054  -0.0102 -0.0002 40  ASN   B C   
4536 O O   . ASN   B 40  ? 0.1723 0.1657 0.1581 0.0035  -0.0102 0.0027  40  ASN   B O   
4537 C CB  . ASN   B 40  ? 0.1860 0.1799 0.1752 0.0101  -0.0110 0.0102  40  ASN   B CB  
4538 C CG  . ASN   B 40  ? 0.1886 0.1832 0.2140 0.0052  -0.0242 0.0107  40  ASN   B CG  
4539 O OD1 . ASN   B 40  ? 0.1832 0.1803 0.2883 -0.0011 -0.0346 0.0050  40  ASN   B OD1 
4540 N ND2 . ASN   B 40  ? 0.1929 0.1795 0.2171 0.0099  -0.0191 0.0132  40  ASN   B ND2 
4547 N N   . VAL   B 41  ? 0.1875 0.1816 0.1493 0.0127  0.0072  0.0026  41  VAL   B N   
4548 C CA  . VAL   B 41  ? 0.1952 0.1967 0.1616 0.0068  0.0083  -0.0112 41  VAL   B CA  
4549 C C   . VAL   B 41  ? 0.1862 0.1939 0.1553 0.0171  0.0010  -0.0112 41  VAL   B C   
4550 O O   . VAL   B 41  ? 0.1834 0.1953 0.1656 0.0157  -0.0081 -0.0197 41  VAL   B O   
4551 C CB  . VAL   B 41  ? 0.2051 0.2180 0.1837 -0.0039 0.0269  -0.0194 41  VAL   B CB  
4552 C CG1 . VAL   B 41  ? 0.1994 0.2278 0.1947 -0.0092 0.0382  -0.0184 41  VAL   B CG1 
4553 C CG2 . VAL   B 41  ? 0.2181 0.2409 0.1976 -0.0077 0.0284  -0.0145 41  VAL   B CG2 
4563 N N   . TYR   B 42  ? 0.1910 0.1941 0.1606 0.0157  -0.0200 0.0033  42  TYR   B N   
4564 C CA  . TYR   B 42  ? 0.1956 0.2076 0.1648 0.0160  -0.0246 -0.0139 42  TYR   B CA  
4565 C C   . TYR   B 42  ? 0.1798 0.1853 0.1695 0.0205  -0.0180 -0.0149 42  TYR   B C   
4566 O O   . TYR   B 42  ? 0.1786 0.1893 0.2063 0.0155  -0.0227 -0.0211 42  TYR   B O   
4567 C CB  . TYR   B 42  ? 0.2218 0.2473 0.1834 0.0103  -0.0256 -0.0017 42  TYR   B CB  
4568 C CG  . TYR   B 42  ? 0.2294 0.2686 0.1749 0.0050  -0.0275 0.0088  42  TYR   B CG  
4569 C CD1 . TYR   B 42  ? 0.2262 0.2707 0.1626 0.0044  -0.0147 0.0049  42  TYR   B CD1 
4570 C CD2 . TYR   B 42  ? 0.2487 0.2872 0.2163 0.0063  -0.0073 0.0203  42  TYR   B CD2 
4571 C CE1 . TYR   B 42  ? 0.2417 0.2899 0.1787 0.0098  -0.0028 0.0116  42  TYR   B CE1 
4572 C CE2 . TYR   B 42  ? 0.2554 0.2998 0.2111 0.0082  0.0204  0.0344  42  TYR   B CE2 
4573 C CZ  . TYR   B 42  ? 0.2621 0.3053 0.2076 0.0212  0.0258  0.0223  42  TYR   B CZ  
4574 O OH  . TYR   B 42  ? 0.2993 0.3268 0.2591 0.0306  0.0396  0.0287  42  TYR   B OH  
4584 N N   . LEU   B 43  ? 0.1712 0.1654 0.1602 0.0150  -0.0102 -0.0147 43  LEU   B N   
4585 C CA  . LEU   B 43  ? 0.1703 0.1637 0.1625 0.0050  -0.0059 -0.0041 43  LEU   B CA  
4586 C C   . LEU   B 43  ? 0.1735 0.1662 0.1736 0.0086  -0.0125 0.0016  43  LEU   B C   
4587 O O   . LEU   B 43  ? 0.1624 0.1768 0.1867 0.0064  -0.0231 0.0042  43  LEU   B O   
4588 C CB  . LEU   B 43  ? 0.1667 0.1566 0.1808 -0.0077 -0.0232 -0.0107 43  LEU   B CB  
4589 C CG  . LEU   B 43  ? 0.1746 0.1573 0.1789 0.0024  -0.0254 -0.0111 43  LEU   B CG  
4590 C CD1 . LEU   B 43  ? 0.1827 0.1618 0.2076 -0.0046 -0.0348 -0.0102 43  LEU   B CD1 
4591 C CD2 . LEU   B 43  ? 0.1706 0.1576 0.1813 -0.0020 -0.0221 -0.0078 43  LEU   B CD2 
4603 N N   . LYS   B 44  ? 0.1713 0.1597 0.1769 0.0120  -0.0053 -0.0089 44  LYS   B N   
4604 C CA  . LYS   B 44  ? 0.1830 0.1778 0.1779 0.0172  -0.0125 0.0102  44  LYS   B CA  
4605 C C   . LYS   B 44  ? 0.1703 0.1697 0.1719 0.0166  -0.0127 0.0063  44  LYS   B C   
4606 O O   . LYS   B 44  ? 0.1939 0.1697 0.1961 0.0076  -0.0091 0.0075  44  LYS   B O   
4607 C CB  . LYS   B 44  ? 0.2160 0.1963 0.1951 0.0260  -0.0216 0.0112  44  LYS   B CB  
4608 C CG  . LYS   B 44  ? 0.2588 0.2288 0.2289 0.0226  -0.0451 0.0092  44  LYS   B CG  
4609 C CD  . LYS   B 44  ? 0.2961 0.2496 0.2801 0.0011  -0.0524 0.0032  44  LYS   B CD  
4610 C CE  . LYS   B 44  ? 0.3271 0.2765 0.3262 -0.0090 -0.0521 0.0126  44  LYS   B CE  
4611 N NZ  . LYS   B 44  ? 0.3391 0.2886 0.3586 -0.0069 -0.0571 0.0252  44  LYS   B NZ  
4625 N N   . HIS   B 45  ? 0.1662 0.1738 0.1653 0.0044  -0.0150 0.0128  45  HIS   B N   
4626 C CA  . HIS   B 45  ? 0.1673 0.1681 0.1706 0.0073  -0.0065 0.0001  45  HIS   B CA  
4627 C C   . HIS   B 45  ? 0.1888 0.1908 0.1997 0.0179  -0.0120 -0.0062 45  HIS   B C   
4628 O O   . HIS   B 45  ? 0.2017 0.2225 0.2516 0.0418  0.0122  0.0010  45  HIS   B O   
4629 C CB  . HIS   B 45  ? 0.1592 0.1742 0.1654 -0.0002 -0.0087 -0.0026 45  HIS   B CB  
4630 C CG  . HIS   B 45  ? 0.1598 0.1669 0.1717 -0.0034 -0.0117 -0.0072 45  HIS   B CG  
4631 N ND1 . HIS   B 45  ? 0.1681 0.1624 0.1872 0.0049  -0.0212 -0.0038 45  HIS   B ND1 
4632 C CD2 . HIS   B 45  ? 0.1708 0.1658 0.1908 -0.0107 -0.0194 -0.0009 45  HIS   B CD2 
4633 C CE1 . HIS   B 45  ? 0.1772 0.1510 0.1722 0.0053  -0.0297 -0.0009 45  HIS   B CE1 
4634 N NE2 . HIS   B 45  ? 0.1792 0.1580 0.1839 0.0000  -0.0256 -0.0031 45  HIS   B NE2 
4642 N N   . GLY   B 46  ? 0.2054 0.1880 0.2410 0.0239  -0.0294 0.0005  46  GLY   B N   
4643 C CA  . GLY   B 46  ? 0.2222 0.2003 0.2749 0.0226  -0.0367 -0.0009 46  GLY   B CA  
4644 C C   . GLY   B 46  ? 0.2229 0.2176 0.3172 0.0280  -0.0344 0.0084  46  GLY   B C   
4645 O O   . GLY   B 46  ? 0.2348 0.2403 0.4064 0.0308  -0.0104 -0.0158 46  GLY   B O   
4649 N N   . GLY   B 47  ? 0.2158 0.2210 0.2884 0.0105  -0.0192 0.0072  47  GLY   B N   
4650 C CA  . GLY   B 47  ? 0.2006 0.1954 0.2484 0.0068  -0.0142 0.0058  47  GLY   B CA  
4651 C C   . GLY   B 47  ? 0.1769 0.1690 0.2163 0.0078  -0.0048 0.0103  47  GLY   B C   
4652 O O   . GLY   B 47  ? 0.1844 0.1596 0.2169 0.0055  -0.0153 0.0159  47  GLY   B O   
4656 N N   . GLY   B 48  ? 0.1625 0.1569 0.2215 0.0077  -0.0088 0.0225  48  GLY   B N   
4657 C CA  . GLY   B 48  ? 0.1608 0.1482 0.2181 0.0001  -0.0056 0.0166  48  GLY   B CA  
4658 C C   . GLY   B 48  ? 0.1477 0.1468 0.2044 0.0061  0.0045  -0.0010 48  GLY   B C   
4659 O O   . GLY   B 48  ? 0.1504 0.1525 0.2247 0.0083  -0.0094 0.0041  48  GLY   B O   
4663 N N   . VAL   B 49  ? 0.1496 0.1547 0.1905 0.0108  0.0026  0.0088  49  VAL   B N   
4664 C CA  . VAL   B 49  ? 0.1580 0.1636 0.1852 0.0038  -0.0116 -0.0050 49  VAL   B CA  
4665 C C   . VAL   B 49  ? 0.1503 0.1568 0.1715 0.0112  -0.0064 0.0100  49  VAL   B C   
4666 O O   . VAL   B 49  ? 0.1625 0.1599 0.1774 0.0055  -0.0085 0.0066  49  VAL   B O   
4667 C CB  . VAL   B 49  ? 0.1588 0.1773 0.2142 -0.0037 -0.0237 -0.0015 49  VAL   B CB  
4668 C CG1 . VAL   B 49  ? 0.1565 0.1866 0.2245 0.0048  -0.0286 0.0035  49  VAL   B CG1 
4669 C CG2 . VAL   B 49  ? 0.1820 0.1932 0.2505 -0.0082 -0.0412 0.0021  49  VAL   B CG2 
4679 N N   . ALA   B 50  ? 0.1452 0.1482 0.1777 0.0057  0.0027  0.0142  50  ALA   B N   
4680 C CA  . ALA   B 50  ? 0.1445 0.1402 0.1798 0.0078  -0.0069 0.0052  50  ALA   B CA  
4681 C C   . ALA   B 50  ? 0.1525 0.1436 0.1736 0.0041  -0.0093 0.0007  50  ALA   B C   
4682 O O   . ALA   B 50  ? 0.1502 0.1485 0.1744 0.0030  -0.0028 -0.0015 50  ALA   B O   
4683 C CB  . ALA   B 50  ? 0.1450 0.1422 0.1855 -0.0024 -0.0034 0.0103  50  ALA   B CB  
4689 N N   . GLY   B 51  ? 0.1517 0.1521 0.1861 0.0143  -0.0153 0.0058  51  GLY   B N   
4690 C CA  . GLY   B 51  ? 0.1595 0.1586 0.2033 0.0138  -0.0153 0.0112  51  GLY   B CA  
4691 C C   . GLY   B 51  ? 0.1502 0.1595 0.2038 0.0169  -0.0096 0.0061  51  GLY   B C   
4692 O O   . GLY   B 51  ? 0.1521 0.1703 0.2318 0.0079  -0.0178 -0.0009 51  GLY   B O   
4696 N N   . ALA   B 52  ? 0.1495 0.1468 0.1968 0.0155  -0.0036 0.0097  52  ALA   B N   
4697 C CA  . ALA   B 52  ? 0.1572 0.1550 0.1970 0.0159  0.0072  -0.0024 52  ALA   B CA  
4698 C C   . ALA   B 52  ? 0.1465 0.1518 0.1879 0.0101  0.0007  0.0068  52  ALA   B C   
4699 O O   . ALA   B 52  ? 0.1494 0.1588 0.2120 0.0118  0.0098  0.0031  52  ALA   B O   
4700 C CB  . ALA   B 52  ? 0.1808 0.1545 0.1998 0.0100  0.0112  0.0004  52  ALA   B CB  
4706 N N   . LEU   B 53  ? 0.1410 0.1473 0.1811 0.0150  0.0009  0.0003  53  LEU   B N   
4707 C CA  . LEU   B 53  ? 0.1467 0.1573 0.1786 0.0111  -0.0051 0.0023  53  LEU   B CA  
4708 C C   . LEU   B 53  ? 0.1491 0.1510 0.1812 0.0148  0.0047  0.0052  53  LEU   B C   
4709 O O   . LEU   B 53  ? 0.1573 0.1662 0.1892 0.0040  0.0023  0.0108  53  LEU   B O   
4710 C CB  . LEU   B 53  ? 0.1446 0.1667 0.1970 0.0073  0.0010  0.0135  53  LEU   B CB  
4711 C CG  . LEU   B 53  ? 0.1460 0.1778 0.1978 0.0052  0.0024  0.0292  53  LEU   B CG  
4712 C CD1 . LEU   B 53  ? 0.1511 0.2028 0.2295 0.0142  0.0024  0.0107  53  LEU   B CD1 
4713 C CD2 . LEU   B 53  ? 0.1589 0.2042 0.2113 -0.0060 -0.0088 -0.0028 53  LEU   B CD2 
4725 N N   . ASN   B 54  ? 0.1463 0.1419 0.1775 0.0047  -0.0009 0.0089  54  ASN   B N   
4726 C CA  . ASN   B 54  ? 0.1512 0.1626 0.1777 0.0043  -0.0062 -0.0026 54  ASN   B CA  
4727 C C   . ASN   B 54  ? 0.1436 0.1605 0.1994 -0.0001 -0.0094 -0.0067 54  ASN   B C   
4728 O O   . ASN   B 54  ? 0.1462 0.1692 0.2129 -0.0074 -0.0017 -0.0042 54  ASN   B O   
4729 C CB  . ASN   B 54  ? 0.1567 0.1719 0.1914 0.0046  0.0027  -0.0063 54  ASN   B CB  
4730 C CG  . ASN   B 54  ? 0.1527 0.1800 0.1937 0.0020  0.0005  -0.0057 54  ASN   B CG  
4731 O OD1 . ASN   B 54  ? 0.1510 0.1723 0.2003 -0.0025 -0.0076 -0.0080 54  ASN   B OD1 
4732 N ND2 . ASN   B 54  ? 0.1654 0.1980 0.2295 0.0024  -0.0290 0.0072  54  ASN   B ND2 
4739 N N   . LYS   B 55  ? 0.1432 0.1684 0.2187 0.0099  -0.0059 0.0027  55  LYS   B N   
4740 C CA  . LYS   B 55  ? 0.1543 0.1815 0.2317 0.0195  -0.0060 0.0068  55  LYS   B CA  
4741 C C   . LYS   B 55  ? 0.1466 0.1769 0.2287 0.0164  0.0025  -0.0009 55  LYS   B C   
4742 O O   . LYS   B 55  ? 0.1395 0.1969 0.2509 0.0155  0.0048  -0.0020 55  LYS   B O   
4743 C CB  . LYS   B 55  ? 0.1711 0.1968 0.2689 0.0297  0.0112  0.0210  55  LYS   B CB  
4744 C CG  . LYS   B 55  ? 0.2202 0.2324 0.3594 0.0364  0.0273  0.0327  55  LYS   B CG  
4745 C CD  . LYS   B 55  ? 0.2583 0.2618 0.4334 0.0457  0.0435  0.0392  55  LYS   B CD  
4746 C CE  . LYS   B 55  ? 0.2860 0.2868 0.4965 0.0453  0.0645  0.0375  55  LYS   B CE  
4747 N NZ  . LYS   B 55  ? 0.2996 0.3039 0.5336 0.0452  0.0597  0.0424  55  LYS   B NZ  
4761 N N   . ALA   B 56  ? 0.1445 0.1776 0.2078 0.0081  0.0065  -0.0081 56  ALA   B N   
4762 C CA  . ALA   B 56  ? 0.1636 0.1956 0.2153 0.0045  0.0072  -0.0050 56  ALA   B CA  
4763 C C   . ALA   B 56  ? 0.1673 0.1879 0.2028 0.0008  0.0164  0.0018  56  ALA   B C   
4764 O O   . ALA   B 56  ? 0.1814 0.2011 0.2243 0.0052  0.0328  0.0046  56  ALA   B O   
4765 C CB  . ALA   B 56  ? 0.1801 0.2175 0.2296 -0.0057 0.0020  -0.0120 56  ALA   B CB  
4771 N N   . THR   B 57  ? 0.1567 0.1830 0.2124 0.0027  0.0180  0.0015  57  THR   B N   
4772 C CA  . THR   B 57  ? 0.1621 0.1806 0.2122 -0.0011 0.0225  0.0037  57  THR   B CA  
4773 C C   . THR   B 57  ? 0.1630 0.1951 0.2290 -0.0027 0.0225  0.0058  57  THR   B C   
4774 O O   . THR   B 57  ? 0.1653 0.1983 0.2452 -0.0265 0.0079  0.0076  57  THR   B O   
4775 C CB  . THR   B 57  ? 0.1725 0.1632 0.2005 -0.0018 0.0232  0.0111  57  THR   B CB  
4776 O OG1 . THR   B 57  ? 0.1690 0.1676 0.2269 -0.0051 0.0166  0.0051  57  THR   B OG1 
4777 C CG2 . THR   B 57  ? 0.1640 0.1658 0.2170 -0.0078 0.0210  0.0116  57  THR   B CG2 
4785 N N   . ASN   B 58  ? 0.1465 0.2161 0.2508 -0.0165 0.0091  -0.0109 58  ASN   B N   
4786 C CA  . ASN   B 58  ? 0.1749 0.2639 0.2875 -0.0238 0.0364  -0.0114 58  ASN   B CA  
4787 C C   . ASN   B 58  ? 0.1507 0.2389 0.2493 -0.0198 0.0037  -0.0139 58  ASN   B C   
4788 O O   . ASN   B 58  ? 0.1567 0.2514 0.2711 -0.0221 -0.0009 -0.0267 58  ASN   B O   
4789 C CB  . ASN   B 58  ? 0.2738 0.3449 0.4104 -0.0370 0.0755  -0.0062 58  ASN   B CB  
4790 C CG  . ASN   B 58  ? 0.3842 0.4204 0.5564 -0.0441 0.0925  0.0132  58  ASN   B CG  
4791 O OD1 . ASN   B 58  ? 0.4071 0.4425 0.6126 -0.0476 0.0936  0.0187  58  ASN   B OD1 
4792 N ND2 . ASN   B 58  ? 0.4938 0.4938 0.6065 -0.0476 0.0990  0.0186  58  ASN   B ND2 
4799 N N   . ASN   B 59  ? 0.1478 0.2182 0.2270 -0.0162 -0.0042 0.0094  59  ASN   B N   
4800 C CA  . ASN   B 59  ? 0.1502 0.2171 0.2307 -0.0100 -0.0100 0.0128  59  ASN   B CA  
4801 C C   . ASN   B 59  ? 0.1480 0.2050 0.2173 -0.0148 -0.0166 -0.0021 59  ASN   B C   
4802 O O   . ASN   B 59  ? 0.1615 0.2076 0.2215 -0.0150 -0.0035 -0.0042 59  ASN   B O   
4803 C CB  . ASN   B 59  ? 0.1577 0.2338 0.2477 -0.0055 -0.0241 0.0116  59  ASN   B CB  
4804 C CG  . ASN   B 59  ? 0.1715 0.2555 0.2535 -0.0012 -0.0411 0.0093  59  ASN   B CG  
4805 O OD1 . ASN   B 59  ? 0.1735 0.2584 0.2551 0.0008  -0.0243 0.0218  59  ASN   B OD1 
4806 N ND2 . ASN   B 59  ? 0.1788 0.2665 0.2574 -0.0102 -0.0400 0.0090  59  ASN   B ND2 
4813 N N   . ALA   B 60  ? 0.1544 0.1961 0.2216 -0.0139 -0.0058 0.0012  60  ALA   B N   
4814 C CA  . ALA   B 60  ? 0.1642 0.1813 0.2214 -0.0257 -0.0044 0.0073  60  ALA   B CA  
4815 C C   . ALA   B 60  ? 0.1644 0.1681 0.2067 -0.0124 -0.0103 0.0061  60  ALA   B C   
4816 O O   . ALA   B 60  ? 0.1684 0.1705 0.2156 -0.0114 0.0004  -0.0037 60  ALA   B O   
4817 C CB  . ALA   B 60  ? 0.1728 0.1831 0.2413 -0.0197 0.0098  0.0096  60  ALA   B CB  
4823 N N   . MET   B 61  ? 0.1535 0.1595 0.2035 -0.0077 -0.0085 0.0057  61  MET   B N   
4824 C CA  . MET   B 61  ? 0.1476 0.1583 0.1945 -0.0057 -0.0180 0.0052  61  MET   B CA  
4825 C C   . MET   B 61  ? 0.1558 0.1588 0.1946 -0.0092 -0.0128 0.0062  61  MET   B C   
4826 O O   . MET   B 61  ? 0.1562 0.1594 0.1935 -0.0023 -0.0038 -0.0076 61  MET   B O   
4827 C CB  . MET   B 61  ? 0.1478 0.1603 0.2000 0.0027  -0.0116 -0.0024 61  MET   B CB  
4828 C CG  . MET   B 61  ? 0.1532 0.1644 0.1922 -0.0025 -0.0166 0.0034  61  MET   B CG  
4829 S SD  . MET   B 61  ? 0.1536 0.1650 0.2144 -0.0020 -0.0055 -0.0106 61  MET   B SD  
4830 C CE  . MET   B 61  ? 0.1687 0.1894 0.2256 -0.0026 -0.0004 -0.0174 61  MET   B CE  
4840 N N   . GLN   B 62  ? 0.1522 0.1632 0.1783 -0.0056 -0.0108 0.0013  62  GLN   B N   
4841 C CA  . GLN   B 62  ? 0.1543 0.1695 0.1870 0.0038  -0.0179 -0.0034 62  GLN   B CA  
4842 C C   . GLN   B 62  ? 0.1545 0.1749 0.1967 -0.0042 -0.0227 -0.0048 62  GLN   B C   
4843 O O   . GLN   B 62  ? 0.1767 0.1772 0.1922 -0.0067 -0.0325 -0.0162 62  GLN   B O   
4844 C CB  . GLN   B 62  ? 0.1557 0.1785 0.1964 0.0053  -0.0109 0.0009  62  GLN   B CB  
4845 C CG  . GLN   B 62  ? 0.1627 0.1818 0.2106 0.0038  -0.0175 -0.0041 62  GLN   B CG  
4846 C CD  . GLN   B 62  ? 0.1669 0.1803 0.1916 0.0044  -0.0227 -0.0001 62  GLN   B CD  
4847 O OE1 . GLN   B 62  ? 0.1632 0.1793 0.2053 0.0007  -0.0291 -0.0066 62  GLN   B OE1 
4848 N NE2 . GLN   B 62  ? 0.1673 0.1850 0.2024 0.0049  -0.0162 -0.0131 62  GLN   B NE2 
4857 N N   . VAL   B 63  ? 0.1554 0.1808 0.2180 -0.0129 -0.0185 -0.0160 63  VAL   B N   
4858 C CA  . VAL   B 63  ? 0.1659 0.1853 0.2399 -0.0150 -0.0302 -0.0106 63  VAL   B CA  
4859 C C   . VAL   B 63  ? 0.1714 0.1694 0.2171 -0.0232 -0.0293 -0.0161 63  VAL   B C   
4860 O O   . VAL   B 63  ? 0.1861 0.1736 0.2337 -0.0221 -0.0441 -0.0206 63  VAL   B O   
4861 C CB  . VAL   B 63  ? 0.1719 0.1997 0.2914 -0.0223 -0.0314 -0.0168 63  VAL   B CB  
4862 C CG1 . VAL   B 63  ? 0.1843 0.2048 0.3005 -0.0285 -0.0242 -0.0134 63  VAL   B CG1 
4863 C CG2 . VAL   B 63  ? 0.1662 0.2167 0.3106 -0.0128 -0.0317 -0.0182 63  VAL   B CG2 
4873 N N   . GLU   B 64  ? 0.1730 0.1575 0.2220 -0.0118 -0.0221 -0.0149 64  GLU   B N   
4874 C CA  . GLU   B 64  ? 0.1701 0.1482 0.2114 -0.0070 -0.0314 -0.0087 64  GLU   B CA  
4875 C C   . GLU   B 64  ? 0.1656 0.1527 0.2025 -0.0031 -0.0287 -0.0182 64  GLU   B C   
4876 O O   . GLU   B 64  ? 0.1811 0.1679 0.1931 -0.0116 -0.0310 -0.0170 64  GLU   B O   
4877 C CB  . GLU   B 64  ? 0.1754 0.1627 0.1985 -0.0176 -0.0189 0.0029  64  GLU   B CB  
4878 C CG  . GLU   B 64  ? 0.1809 0.1717 0.2070 -0.0292 -0.0239 -0.0060 64  GLU   B CG  
4879 C CD  . GLU   B 64  ? 0.1886 0.1931 0.2219 -0.0316 -0.0297 -0.0151 64  GLU   B CD  
4880 O OE1 . GLU   B 64  ? 0.1948 0.2165 0.2300 -0.0405 -0.0198 -0.0351 64  GLU   B OE1 
4881 O OE2 . GLU   B 64  ? 0.1990 0.2021 0.2306 -0.0292 -0.0407 -0.0174 64  GLU   B OE2 
4888 N N   . SER   B 65  ? 0.1632 0.1501 0.1879 -0.0094 -0.0132 -0.0173 65  SER   B N   
4889 C CA  . SER   B 65  ? 0.1625 0.1550 0.1890 0.0014  -0.0127 -0.0152 65  SER   B CA  
4890 C C   . SER   B 65  ? 0.1655 0.1597 0.1882 -0.0028 -0.0174 -0.0161 65  SER   B C   
4891 O O   . SER   B 65  ? 0.1698 0.1655 0.1911 -0.0026 -0.0195 -0.0260 65  SER   B O   
4892 C CB  . SER   B 65  ? 0.1668 0.1564 0.1913 -0.0086 -0.0175 -0.0096 65  SER   B CB  
4893 O OG  . SER   B 65  ? 0.1707 0.1645 0.1961 -0.0068 -0.0194 -0.0267 65  SER   B OG  
4899 N N   . ASP   B 66  ? 0.1737 0.1646 0.1853 0.0003  -0.0232 -0.0192 66  ASP   B N   
4900 C CA  . ASP   B 66  ? 0.1875 0.1801 0.1835 0.0058  -0.0314 -0.0125 66  ASP   B CA  
4901 C C   . ASP   B 66  ? 0.1877 0.1835 0.1902 -0.0078 -0.0296 -0.0194 66  ASP   B C   
4902 O O   . ASP   B 66  ? 0.1890 0.1868 0.1999 0.0027  -0.0277 -0.0224 66  ASP   B O   
4903 C CB  . ASP   B 66  ? 0.2124 0.2024 0.2060 0.0181  -0.0435 -0.0159 66  ASP   B CB  
4904 C CG  . ASP   B 66  ? 0.2374 0.2233 0.2210 0.0238  -0.0593 -0.0006 66  ASP   B CG  
4905 O OD1 . ASP   B 66  ? 0.2622 0.2183 0.2221 0.0159  -0.0597 -0.0104 66  ASP   B OD1 
4906 O OD2 . ASP   B 66  ? 0.2551 0.2532 0.2834 0.0394  -0.0526 0.0022  66  ASP   B OD2 
4911 N N   . ASP   B 67  ? 0.1863 0.1748 0.1900 -0.0108 -0.0257 -0.0233 67  ASP   B N   
4912 C CA  . ASP   B 67  ? 0.2014 0.1663 0.2092 -0.0149 -0.0277 -0.0175 67  ASP   B CA  
4913 C C   . ASP   B 67  ? 0.1932 0.1619 0.2163 0.0004  -0.0282 -0.0245 67  ASP   B C   
4914 O O   . ASP   B 67  ? 0.2033 0.1742 0.2160 -0.0007 -0.0181 -0.0350 67  ASP   B O   
4915 C CB  . ASP   B 67  ? 0.2319 0.1751 0.2291 -0.0136 -0.0345 -0.0166 67  ASP   B CB  
4916 C CG  . ASP   B 67  ? 0.2720 0.1888 0.2440 -0.0062 -0.0603 -0.0180 67  ASP   B CG  
4917 O OD1 . ASP   B 67  ? 0.2959 0.1965 0.2568 -0.0086 -0.0642 -0.0153 67  ASP   B OD1 
4918 O OD2 . ASP   B 67  ? 0.2863 0.1980 0.2718 0.0094  -0.0683 -0.0149 67  ASP   B OD2 
4923 N N   . TYR   B 68  ? 0.1885 0.1619 0.2053 -0.0003 -0.0426 -0.0335 68  TYR   B N   
4924 C CA  . TYR   B 68  ? 0.1873 0.1788 0.2228 0.0088  -0.0411 -0.0370 68  TYR   B CA  
4925 C C   . TYR   B 68  ? 0.1804 0.1768 0.2207 0.0053  -0.0342 -0.0447 68  TYR   B C   
4926 O O   . TYR   B 68  ? 0.1888 0.1919 0.2200 0.0070  -0.0301 -0.0654 68  TYR   B O   
4927 C CB  . TYR   B 68  ? 0.1880 0.2088 0.2321 0.0085  -0.0480 -0.0550 68  TYR   B CB  
4928 C CG  . TYR   B 68  ? 0.2018 0.2331 0.2392 0.0179  -0.0365 -0.0799 68  TYR   B CG  
4929 C CD1 . TYR   B 68  ? 0.1995 0.2418 0.2612 -0.0039 -0.0343 -0.0935 68  TYR   B CD1 
4930 C CD2 . TYR   B 68  ? 0.2058 0.2588 0.2572 0.0229  -0.0500 -0.0784 68  TYR   B CD2 
4931 C CE1 . TYR   B 68  ? 0.2039 0.2609 0.2843 0.0017  -0.0290 -0.0910 68  TYR   B CE1 
4932 C CE2 . TYR   B 68  ? 0.2076 0.2712 0.2725 0.0220  -0.0383 -0.0944 68  TYR   B CE2 
4933 C CZ  . TYR   B 68  ? 0.1989 0.2715 0.2886 0.0100  -0.0363 -0.0938 68  TYR   B CZ  
4934 O OH  . TYR   B 68  ? 0.1959 0.2899 0.3317 0.0031  -0.0256 -0.0756 68  TYR   B OH  
4944 N N   . ILE   B 69  ? 0.1766 0.1646 0.2156 0.0010  -0.0295 -0.0456 69  ILE   B N   
4945 C CA  . ILE   B 69  ? 0.1906 0.1764 0.2143 -0.0018 -0.0206 -0.0503 69  ILE   B CA  
4946 C C   . ILE   B 69  ? 0.1881 0.1758 0.2151 0.0066  -0.0322 -0.0325 69  ILE   B C   
4947 O O   . ILE   B 69  ? 0.1898 0.1860 0.2139 0.0013  -0.0190 -0.0385 69  ILE   B O   
4948 C CB  . ILE   B 69  ? 0.1964 0.1868 0.2336 -0.0067 0.0079  -0.0394 69  ILE   B CB  
4949 C CG1 . ILE   B 69  ? 0.2002 0.1936 0.2410 -0.0071 0.0179  -0.0434 69  ILE   B CG1 
4950 C CG2 . ILE   B 69  ? 0.2133 0.1940 0.2495 -0.0053 0.0053  -0.0296 69  ILE   B CG2 
4951 C CD1 . ILE   B 69  ? 0.1908 0.1973 0.2498 -0.0226 0.0219  -0.0448 69  ILE   B CD1 
4963 N N   . ALA   B 70  ? 0.1869 0.1740 0.2161 0.0068  -0.0431 -0.0348 70  ALA   B N   
4964 C CA  . ALA   B 70  ? 0.1895 0.1773 0.1962 0.0053  -0.0488 -0.0330 70  ALA   B CA  
4965 C C   . ALA   B 70  ? 0.1955 0.1821 0.2167 -0.0004 -0.0484 -0.0381 70  ALA   B C   
4966 O O   . ALA   B 70  ? 0.2024 0.1789 0.2163 0.0020  -0.0416 -0.0425 70  ALA   B O   
4967 C CB  . ALA   B 70  ? 0.1917 0.1967 0.1835 -0.0052 -0.0489 -0.0217 70  ALA   B CB  
4973 N N   . THR   B 71  ? 0.2009 0.1817 0.2176 0.0043  -0.0530 -0.0433 71  THR   B N   
4974 C CA  . THR   B 71  ? 0.2154 0.1839 0.2276 0.0126  -0.0664 -0.0446 71  THR   B CA  
4975 C C   . THR   B 71  ? 0.2105 0.1827 0.2603 0.0305  -0.0611 -0.0538 71  THR   B C   
4976 O O   . THR   B 71  ? 0.2265 0.1913 0.2971 0.0323  -0.0562 -0.0690 71  THR   B O   
4977 C CB  . THR   B 71  ? 0.2432 0.2060 0.2474 0.0015  -0.0729 -0.0262 71  THR   B CB  
4978 O OG1 . THR   B 71  ? 0.2614 0.2345 0.2737 -0.0220 -0.0662 -0.0032 71  THR   B OG1 
4979 C CG2 . THR   B 71  ? 0.2617 0.2066 0.2727 0.0073  -0.0631 -0.0125 71  THR   B CG2 
4987 N N   . ASN   B 72  ? 0.1942 0.1913 0.2492 0.0211  -0.0586 -0.0751 72  ASN   B N   
4988 C CA  . ASN   B 72  ? 0.1949 0.2114 0.2390 0.0138  -0.0440 -0.0798 72  ASN   B CA  
4989 C C   . ASN   B 72  ? 0.1978 0.2229 0.2485 -0.0027 -0.0218 -0.0805 72  ASN   B C   
4990 O O   . ASN   B 72  ? 0.2002 0.2374 0.2737 0.0108  -0.0078 -0.0780 72  ASN   B O   
4991 C CB  . ASN   B 72  ? 0.1999 0.2252 0.2543 0.0164  -0.0523 -0.0669 72  ASN   B CB  
4992 C CG  . ASN   B 72  ? 0.2174 0.2357 0.2681 0.0296  -0.0593 -0.0436 72  ASN   B CG  
4993 O OD1 . ASN   B 72  ? 0.2432 0.2488 0.2847 0.0165  -0.0421 -0.0487 72  ASN   B OD1 
4994 N ND2 . ASN   B 72  ? 0.2293 0.2445 0.3097 0.0399  -0.0482 -0.0125 72  ASN   B ND2 
5001 N N   . GLY   B 73  ? 0.1992 0.2224 0.2287 -0.0091 -0.0218 -0.0744 73  GLY   B N   
5002 C CA  . GLY   B 73  ? 0.1974 0.2324 0.1994 -0.0044 -0.0206 -0.0625 73  GLY   B CA  
5003 C C   . GLY   B 73  ? 0.1855 0.2285 0.1613 0.0055  -0.0148 -0.0492 73  GLY   B C   
5004 O O   . GLY   B 73  ? 0.1803 0.2132 0.1922 0.0058  -0.0201 -0.0418 73  GLY   B O   
5008 N N   . PRO   B 74  ? 0.1919 0.2356 0.1678 0.0035  -0.0236 -0.0399 74  PRO   B N   
5009 C CA  . PRO   B 74  ? 0.1825 0.2359 0.1615 0.0096  -0.0228 -0.0310 74  PRO   B CA  
5010 C C   . PRO   B 74  ? 0.1690 0.2138 0.1662 0.0067  -0.0138 -0.0255 74  PRO   B C   
5011 O O   . PRO   B 74  ? 0.1727 0.2135 0.2085 0.0087  -0.0091 -0.0428 74  PRO   B O   
5012 C CB  . PRO   B 74  ? 0.2038 0.2545 0.1820 0.0057  -0.0291 -0.0213 74  PRO   B CB  
5013 C CG  . PRO   B 74  ? 0.2232 0.2649 0.2081 0.0068  -0.0193 -0.0147 74  PRO   B CG  
5014 C CD  . PRO   B 74  ? 0.2201 0.2550 0.1900 0.0080  -0.0116 -0.0321 74  PRO   B CD  
5022 N N   . LEU   B 75  ? 0.1660 0.1974 0.1607 0.0068  -0.0208 -0.0263 75  LEU   B N   
5023 C CA  . LEU   B 75  ? 0.1692 0.1947 0.1574 0.0034  -0.0090 -0.0060 75  LEU   B CA  
5024 C C   . LEU   B 75  ? 0.1706 0.2015 0.1577 0.0043  -0.0040 -0.0075 75  LEU   B C   
5025 O O   . LEU   B 75  ? 0.1857 0.2205 0.1820 -0.0010 -0.0109 0.0024  75  LEU   B O   
5026 C CB  . LEU   B 75  ? 0.1759 0.2018 0.1487 -0.0106 -0.0155 0.0101  75  LEU   B CB  
5027 C CG  . LEU   B 75  ? 0.2158 0.2161 0.1827 -0.0382 -0.0030 0.0025  75  LEU   B CG  
5028 C CD1 . LEU   B 75  ? 0.2472 0.2332 0.1777 -0.0452 0.0102  -0.0042 75  LEU   B CD1 
5029 C CD2 . LEU   B 75  ? 0.2533 0.2343 0.2580 -0.0311 0.0043  0.0038  75  LEU   B CD2 
5041 N N   . LYS   B 76  ? 0.1663 0.2149 0.1907 0.0037  0.0063  -0.0034 76  LYS   B N   
5042 C CA  . LYS   B 76  ? 0.1812 0.2279 0.2196 -0.0039 0.0235  -0.0038 76  LYS   B CA  
5043 C C   . LYS   B 76  ? 0.1757 0.2115 0.1929 0.0040  0.0103  0.0166  76  LYS   B C   
5044 O O   . LYS   B 76  ? 0.1785 0.1910 0.1966 0.0015  0.0017  0.0141  76  LYS   B O   
5045 C CB  . LYS   B 76  ? 0.1967 0.2334 0.2812 -0.0124 0.0484  -0.0337 76  LYS   B CB  
5046 C CG  . LYS   B 76  ? 0.2117 0.2542 0.3386 0.0012  0.0341  -0.0364 76  LYS   B CG  
5047 C CD  . LYS   B 76  ? 0.2195 0.2652 0.3848 0.0084  0.0183  -0.0450 76  LYS   B CD  
5048 C CE  . LYS   B 76  ? 0.2310 0.2809 0.4374 0.0099  0.0045  -0.0510 76  LYS   B CE  
5049 N NZ  . LYS   B 76  ? 0.2304 0.2869 0.4621 0.0068  -0.0153 -0.0648 76  LYS   B NZ  
5063 N N   . VAL   B 77  ? 0.1827 0.2231 0.1825 0.0171  0.0131  0.0155  77  VAL   B N   
5064 C CA  . VAL   B 77  ? 0.1816 0.2138 0.1921 0.0149  0.0165  0.0401  77  VAL   B CA  
5065 C C   . VAL   B 77  ? 0.1666 0.1912 0.1805 0.0134  0.0206  0.0292  77  VAL   B C   
5066 O O   . VAL   B 77  ? 0.1720 0.1896 0.1915 0.0278  0.0278  0.0203  77  VAL   B O   
5067 C CB  . VAL   B 77  ? 0.1921 0.2208 0.2263 0.0158  0.0342  0.0554  77  VAL   B CB  
5068 C CG1 . VAL   B 77  ? 0.2045 0.2113 0.2599 0.0065  0.0307  0.0686  77  VAL   B CG1 
5069 C CG2 . VAL   B 77  ? 0.2086 0.2447 0.2486 0.0183  0.0220  0.0559  77  VAL   B CG2 
5079 N N   . GLY   B 78  ? 0.1661 0.1772 0.1759 0.0124  0.0168  0.0206  78  GLY   B N   
5080 C CA  . GLY   B 78  ? 0.1681 0.1729 0.1702 0.0148  0.0287  0.0101  78  GLY   B CA  
5081 C C   . GLY   B 78  ? 0.1651 0.1705 0.1656 0.0132  0.0201  0.0207  78  GLY   B C   
5082 O O   . GLY   B 78  ? 0.1718 0.1680 0.1849 0.0195  0.0175  0.0239  78  GLY   B O   
5086 N N   . GLY   B 79  ? 0.1561 0.1703 0.1829 0.0121  0.0145  0.0065  79  GLY   B N   
5087 C CA  . GLY   B 79  ? 0.1593 0.1601 0.1743 0.0165  0.0110  0.0074  79  GLY   B CA  
5088 C C   . GLY   B 79  ? 0.1483 0.1554 0.1828 0.0158  0.0122  0.0014  79  GLY   B C   
5089 O O   . GLY   B 79  ? 0.1559 0.1573 0.1897 0.0129  0.0188  0.0149  79  GLY   B O   
5093 N N   . SER   B 80  ? 0.1478 0.1442 0.1917 0.0087  0.0199  0.0042  80  SER   B N   
5094 C CA  . SER   B 80  ? 0.1458 0.1487 0.1925 0.0040  0.0084  0.0024  80  SER   B CA  
5095 C C   . SER   B 80  ? 0.1460 0.1411 0.1908 0.0094  -0.0054 -0.0027 80  SER   B C   
5096 O O   . SER   B 80  ? 0.1570 0.1441 0.2227 0.0086  0.0025  -0.0098 80  SER   B O   
5097 C CB  . SER   B 80  ? 0.1469 0.1551 0.1889 -0.0028 0.0048  0.0064  80  SER   B CB  
5098 O OG  . SER   B 80  ? 0.1562 0.1685 0.2130 0.0008  -0.0142 0.0135  80  SER   B OG  
5104 N N   . CYS   B 81  ? 0.1439 0.1321 0.1848 0.0027  -0.0045 -0.0096 81  CYS   B N   
5105 C CA  . CYS   B 81  ? 0.1509 0.1323 0.1913 0.0057  -0.0134 -0.0099 81  CYS   B CA  
5106 C C   . CYS   B 81  ? 0.1502 0.1327 0.1622 0.0007  -0.0083 -0.0037 81  CYS   B C   
5107 O O   . CYS   B 81  ? 0.1747 0.1306 0.1921 0.0054  -0.0060 -0.0081 81  CYS   B O   
5108 C CB  . CYS   B 81  ? 0.1704 0.1480 0.1922 -0.0022 -0.0090 -0.0063 81  CYS   B CB  
5109 S SG  . CYS   B 81  ? 0.1716 0.1699 0.1860 -0.0049 -0.0261 -0.0124 81  CYS   B SG  
5115 N N   . VAL   B 82  ? 0.1526 0.1240 0.1828 0.0001  -0.0035 -0.0056 82  VAL   B N   
5116 C CA  . VAL   B 82  ? 0.1570 0.1350 0.1849 -0.0067 -0.0104 0.0016  82  VAL   B CA  
5117 C C   . VAL   B 82  ? 0.1676 0.1254 0.1868 -0.0040 -0.0037 -0.0067 82  VAL   B C   
5118 O O   . VAL   B 82  ? 0.1756 0.1275 0.2230 -0.0020 -0.0129 -0.0161 82  VAL   B O   
5119 C CB  . VAL   B 82  ? 0.1635 0.1552 0.2021 -0.0024 -0.0094 0.0084  82  VAL   B CB  
5120 C CG1 . VAL   B 82  ? 0.1859 0.1808 0.2043 0.0020  -0.0116 0.0207  82  VAL   B CG1 
5121 C CG2 . VAL   B 82  ? 0.1778 0.1776 0.2215 -0.0085 -0.0300 0.0109  82  VAL   B CG2 
5131 N N   . LEU   B 83  ? 0.1540 0.1304 0.1914 -0.0128 -0.0212 -0.0078 83  LEU   B N   
5132 C CA  . LEU   B 83  ? 0.1590 0.1363 0.1739 -0.0123 -0.0178 -0.0031 83  LEU   B CA  
5133 C C   . LEU   B 83  ? 0.1606 0.1322 0.1760 -0.0171 -0.0166 -0.0013 83  LEU   B C   
5134 O O   . LEU   B 83  ? 0.1593 0.1421 0.1607 -0.0236 -0.0161 0.0050  83  LEU   B O   
5135 C CB  . LEU   B 83  ? 0.1644 0.1573 0.1732 -0.0170 -0.0253 -0.0081 83  LEU   B CB  
5136 C CG  . LEU   B 83  ? 0.1834 0.1776 0.1856 -0.0176 -0.0115 -0.0091 83  LEU   B CG  
5137 C CD1 . LEU   B 83  ? 0.1931 0.1828 0.1987 -0.0146 -0.0255 -0.0038 83  LEU   B CD1 
5138 C CD2 . LEU   B 83  ? 0.2069 0.1829 0.2174 -0.0076 -0.0061 -0.0297 83  LEU   B CD2 
5150 N N   . SER   B 84  ? 0.1575 0.1467 0.2011 -0.0212 -0.0186 -0.0060 84  SER   B N   
5151 C CA  . SER   B 84  ? 0.1662 0.1653 0.1896 -0.0224 -0.0068 0.0079  84  SER   B CA  
5152 C C   . SER   B 84  ? 0.1538 0.1829 0.1418 -0.0195 -0.0186 0.0159  84  SER   B C   
5153 O O   . SER   B 84  ? 0.1642 0.1720 0.1444 -0.0174 -0.0153 0.0015  84  SER   B O   
5154 C CB  . SER   B 84  ? 0.1877 0.1681 0.2452 -0.0298 0.0097  0.0064  84  SER   B CB  
5155 O OG  . SER   B 84  ? 0.1849 0.1847 0.2986 -0.0329 0.0179  0.0170  84  SER   B OG  
5161 N N   . GLY   B 85  ? 0.1567 0.2035 0.1583 -0.0272 -0.0172 0.0273  85  GLY   B N   
5162 C CA  . GLY   B 85  ? 0.1634 0.2061 0.1800 -0.0356 -0.0021 0.0006  85  GLY   B CA  
5163 C C   . GLY   B 85  ? 0.1584 0.1885 0.1623 -0.0399 -0.0074 0.0034  85  GLY   B C   
5164 O O   . GLY   B 85  ? 0.1648 0.1885 0.1757 -0.0532 0.0134  -0.0089 85  GLY   B O   
5168 N N   . HIS   B 86  ? 0.1577 0.1669 0.1845 -0.0295 -0.0250 0.0085  86  HIS   B N   
5169 C CA  . HIS   B 86  ? 0.1586 0.1656 0.1904 -0.0267 -0.0295 0.0151  86  HIS   B CA  
5170 C C   . HIS   B 86  ? 0.1616 0.1781 0.1843 -0.0380 -0.0143 0.0342  86  HIS   B C   
5171 O O   . HIS   B 86  ? 0.1718 0.1882 0.1839 -0.0298 0.0058  0.0359  86  HIS   B O   
5172 C CB  . HIS   B 86  ? 0.1664 0.1670 0.1983 -0.0207 -0.0344 0.0052  86  HIS   B CB  
5173 C CG  . HIS   B 86  ? 0.1700 0.1858 0.1884 -0.0099 -0.0251 0.0077  86  HIS   B CG  
5174 N ND1 . HIS   B 86  ? 0.1883 0.2130 0.2135 -0.0224 -0.0235 -0.0110 86  HIS   B ND1 
5175 C CD2 . HIS   B 86  ? 0.1777 0.1950 0.2075 -0.0083 -0.0225 0.0042  86  HIS   B CD2 
5176 C CE1 . HIS   B 86  ? 0.1943 0.2082 0.2082 -0.0112 -0.0104 -0.0309 86  HIS   B CE1 
5177 N NE2 . HIS   B 86  ? 0.1922 0.1981 0.2067 0.0037  -0.0135 -0.0044 86  HIS   B NE2 
5185 N N   . ASN   B 87  ? 0.1576 0.1850 0.1906 -0.0275 -0.0042 0.0324  87  ASN   B N   
5186 C CA  . ASN   B 87  ? 0.1660 0.2051 0.1867 -0.0290 0.0228  0.0256  87  ASN   B CA  
5187 C C   . ASN   B 87  ? 0.1803 0.1861 0.1785 -0.0341 0.0267  0.0153  87  ASN   B C   
5188 O O   . ASN   B 87  ? 0.2069 0.1967 0.2116 -0.0213 0.0525  0.0085  87  ASN   B O   
5189 C CB  . ASN   B 87  ? 0.1704 0.2416 0.2135 -0.0209 0.0258  0.0185  87  ASN   B CB  
5190 C CG  . ASN   B 87  ? 0.1776 0.2614 0.2264 0.0118  0.0326  0.0290  87  ASN   B CG  
5191 O OD1 . ASN   B 87  ? 0.1734 0.2454 0.2144 0.0159  0.0441  0.0462  87  ASN   B OD1 
5192 N ND2 . ASN   B 87  ? 0.2162 0.2709 0.2681 0.0162  0.0360  0.0254  87  ASN   B ND2 
5199 N N   . LEU   B 88  ? 0.1703 0.1764 0.1768 -0.0364 0.0134  0.0141  88  LEU   B N   
5200 C CA  . LEU   B 88  ? 0.1862 0.1722 0.1729 -0.0351 -0.0011 0.0075  88  LEU   B CA  
5201 C C   . LEU   B 88  ? 0.1868 0.1589 0.1704 -0.0411 0.0015  0.0087  88  LEU   B C   
5202 O O   . LEU   B 88  ? 0.2144 0.1666 0.2102 -0.0237 -0.0290 -0.0087 88  LEU   B O   
5203 C CB  . LEU   B 88  ? 0.1970 0.1805 0.1989 -0.0408 -0.0096 0.0132  88  LEU   B CB  
5204 C CG  . LEU   B 88  ? 0.2343 0.2117 0.2072 -0.0341 -0.0278 0.0257  88  LEU   B CG  
5205 C CD1 . LEU   B 88  ? 0.2454 0.2404 0.2326 -0.0472 -0.0216 0.0409  88  LEU   B CD1 
5206 C CD2 . LEU   B 88  ? 0.2696 0.2388 0.2547 0.0044  -0.0497 0.0083  88  LEU   B CD2 
5218 N N   . ALA   B 89  ? 0.1726 0.1536 0.1659 -0.0397 0.0177  0.0021  89  ALA   B N   
5219 C CA  . ALA   B 89  ? 0.1646 0.1559 0.1474 -0.0392 0.0016  0.0108  89  ALA   B CA  
5220 C C   . ALA   B 89  ? 0.1705 0.1578 0.1517 -0.0403 0.0114  0.0034  89  ALA   B C   
5221 O O   . ALA   B 89  ? 0.1557 0.1680 0.1951 -0.0404 0.0105  -0.0230 89  ALA   B O   
5222 C CB  . ALA   B 89  ? 0.1603 0.1555 0.1688 -0.0434 -0.0023 0.0128  89  ALA   B CB  
5228 N N   . LYS   B 90  ? 0.2091 0.1464 0.1570 -0.0411 -0.0099 0.0130  90  LYS   B N   
5229 C CA  . LYS   B 90  ? 0.2240 0.1422 0.1644 -0.0411 -0.0100 0.0129  90  LYS   B CA  
5230 C C   . LYS   B 90  ? 0.2075 0.1337 0.1768 -0.0380 -0.0111 -0.0014 90  LYS   B C   
5231 O O   . LYS   B 90  ? 0.2172 0.1561 0.1968 -0.0571 -0.0021 0.0011  90  LYS   B O   
5232 C CB  . LYS   B 90  ? 0.2511 0.1499 0.1937 -0.0366 0.0002  0.0233  90  LYS   B CB  
5233 C CG  . LYS   B 90  ? 0.2602 0.1752 0.2022 -0.0282 0.0225  0.0148  90  LYS   B CG  
5234 C CD  . LYS   B 90  ? 0.2832 0.2060 0.2482 -0.0192 0.0436  -0.0055 90  LYS   B CD  
5235 C CE  . LYS   B 90  ? 0.2938 0.2251 0.3001 -0.0255 0.0510  -0.0205 90  LYS   B CE  
5236 N NZ  . LYS   B 90  ? 0.3013 0.2202 0.3014 -0.0422 0.0711  -0.0233 90  LYS   B NZ  
5250 N N   . HIS   B 91  ? 0.1804 0.1319 0.1621 -0.0292 -0.0153 0.0125  91  HIS   B N   
5251 C CA  . HIS   B 91  ? 0.1677 0.1336 0.1686 -0.0212 -0.0171 0.0015  91  HIS   B CA  
5252 C C   . HIS   B 91  ? 0.1593 0.1344 0.1518 -0.0247 -0.0106 0.0077  91  HIS   B C   
5253 O O   . HIS   B 91  ? 0.1675 0.1371 0.1481 -0.0222 -0.0160 0.0002  91  HIS   B O   
5254 C CB  . HIS   B 91  ? 0.1902 0.1381 0.1974 -0.0074 -0.0196 0.0134  91  HIS   B CB  
5255 C CG  . HIS   B 91  ? 0.2333 0.1596 0.2596 0.0042  0.0147  0.0208  91  HIS   B CG  
5256 N ND1 . HIS   B 91  ? 0.2624 0.1616 0.3203 0.0036  0.0212  0.0141  91  HIS   B ND1 
5257 C CD2 . HIS   B 91  ? 0.2542 0.1906 0.3159 0.0201  -0.0007 0.0494  91  HIS   B CD2 
5258 C CE1 . HIS   B 91  ? 0.2691 0.1749 0.3340 0.0180  0.0171  0.0217  91  HIS   B CE1 
5259 N NE2 . HIS   B 91  ? 0.2657 0.1966 0.3433 0.0327  0.0097  0.0601  91  HIS   B NE2 
5267 N N   . CYS   B 92  ? 0.1470 0.1317 0.1509 -0.0240 -0.0131 0.0025  92  CYS   B N   
5268 C CA  . CYS   B 92  ? 0.1428 0.1279 0.1530 -0.0184 -0.0059 -0.0023 92  CYS   B CA  
5269 C C   . CYS   B 92  ? 0.1416 0.1186 0.1521 -0.0075 -0.0061 0.0033  92  CYS   B C   
5270 O O   . CYS   B 92  ? 0.1563 0.1320 0.1760 -0.0142 -0.0011 -0.0022 92  CYS   B O   
5271 C CB  . CYS   B 92  ? 0.1480 0.1433 0.1545 -0.0095 -0.0038 0.0117  92  CYS   B CB  
5272 S SG  . CYS   B 92  ? 0.1500 0.1444 0.1627 -0.0113 -0.0108 0.0072  92  CYS   B SG  
5278 N N   . LEU   B 93  ? 0.1308 0.1265 0.1533 -0.0137 -0.0091 -0.0090 93  LEU   B N   
5279 C CA  . LEU   B 93  ? 0.1333 0.1219 0.1552 -0.0039 -0.0157 0.0016  93  LEU   B CA  
5280 C C   . LEU   B 93  ? 0.1288 0.1267 0.1380 -0.0020 -0.0167 0.0094  93  LEU   B C   
5281 O O   . LEU   B 93  ? 0.1420 0.1252 0.1605 -0.0054 -0.0092 0.0021  93  LEU   B O   
5282 C CB  . LEU   B 93  ? 0.1367 0.1309 0.1739 -0.0015 -0.0072 0.0042  93  LEU   B CB  
5283 C CG  . LEU   B 93  ? 0.1362 0.1428 0.1848 -0.0004 -0.0094 0.0158  93  LEU   B CG  
5284 C CD1 . LEU   B 93  ? 0.1451 0.1584 0.1875 0.0094  -0.0013 -0.0011 93  LEU   B CD1 
5285 C CD2 . LEU   B 93  ? 0.1346 0.1542 0.1973 -0.0008 -0.0123 0.0007  93  LEU   B CD2 
5297 N N   . HIS   B 94  ? 0.1333 0.1275 0.1388 -0.0075 -0.0147 0.0064  94  HIS   B N   
5298 C CA  . HIS   B 94  ? 0.1369 0.1250 0.1417 -0.0030 -0.0073 0.0037  94  HIS   B CA  
5299 C C   . HIS   B 94  ? 0.1368 0.1240 0.1605 -0.0000 -0.0058 0.0105  94  HIS   B C   
5300 O O   . HIS   B 94  ? 0.1406 0.1314 0.2148 -0.0010 0.0122  -0.0056 94  HIS   B O   
5301 C CB  . HIS   B 94  ? 0.1386 0.1322 0.1506 -0.0030 -0.0146 0.0034  94  HIS   B CB  
5302 C CG  . HIS   B 94  ? 0.1390 0.1276 0.1590 -0.0025 -0.0259 -0.0002 94  HIS   B CG  
5303 N ND1 . HIS   B 94  ? 0.1401 0.1393 0.1641 -0.0046 -0.0245 0.0003  94  HIS   B ND1 
5304 C CD2 . HIS   B 94  ? 0.1449 0.1307 0.1686 -0.0033 -0.0228 0.0053  94  HIS   B CD2 
5305 C CE1 . HIS   B 94  ? 0.1395 0.1381 0.1685 -0.0076 -0.0264 -0.0012 94  HIS   B CE1 
5306 N NE2 . HIS   B 94  ? 0.1339 0.1458 0.1732 -0.0138 -0.0184 0.0026  94  HIS   B NE2 
5314 N N   . VAL   B 95  ? 0.1274 0.1208 0.1696 0.0016  -0.0014 0.0039  95  VAL   B N   
5315 C CA  . VAL   B 95  ? 0.1330 0.1316 0.1606 0.0049  -0.0032 0.0089  95  VAL   B CA  
5316 C C   . VAL   B 95  ? 0.1464 0.1316 0.1637 -0.0014 0.0094  0.0079  95  VAL   B C   
5317 O O   . VAL   B 95  ? 0.1461 0.1325 0.1887 0.0090  0.0063  0.0108  95  VAL   B O   
5318 C CB  . VAL   B 95  ? 0.1399 0.1307 0.1697 -0.0022 -0.0145 0.0017  95  VAL   B CB  
5319 C CG1 . VAL   B 95  ? 0.1531 0.1504 0.1920 -0.0109 -0.0075 0.0171  95  VAL   B CG1 
5320 C CG2 . VAL   B 95  ? 0.1453 0.1299 0.1761 0.0015  -0.0196 0.0012  95  VAL   B CG2 
5330 N N   . VAL   B 96  ? 0.1532 0.1395 0.1591 0.0101  0.0164  0.0204  96  VAL   B N   
5331 C CA  . VAL   B 96  ? 0.1579 0.1548 0.1496 0.0071  0.0077  0.0164  96  VAL   B CA  
5332 C C   . VAL   B 96  ? 0.1604 0.1534 0.1664 0.0098  0.0138  0.0228  96  VAL   B C   
5333 O O   . VAL   B 96  ? 0.1549 0.1607 0.1916 0.0018  0.0187  0.0009  96  VAL   B O   
5334 C CB  . VAL   B 96  ? 0.1600 0.1744 0.1574 0.0092  0.0073  0.0090  96  VAL   B CB  
5335 C CG1 . VAL   B 96  ? 0.1592 0.1875 0.1730 0.0139  0.0098  0.0032  96  VAL   B CG1 
5336 C CG2 . VAL   B 96  ? 0.1709 0.1792 0.1844 0.0041  0.0149  0.0041  96  VAL   B CG2 
5346 N N   . GLY   B 97  ? 0.1661 0.1504 0.1727 0.0054  0.0098  0.0232  97  GLY   B N   
5347 C CA  . GLY   B 97  ? 0.1816 0.1543 0.1787 0.0029  0.0178  0.0160  97  GLY   B CA  
5348 C C   . GLY   B 97  ? 0.1944 0.1638 0.1959 0.0125  0.0160  0.0175  97  GLY   B C   
5349 O O   . GLY   B 97  ? 0.2077 0.1752 0.1890 0.0097  0.0108  0.0137  97  GLY   B O   
5353 N N   . PRO   B 98  ? 0.2108 0.1680 0.1890 0.0138  0.0296  0.0278  98  PRO   B N   
5354 C CA  . PRO   B 98  ? 0.2235 0.1876 0.2000 0.0222  0.0425  0.0240  98  PRO   B CA  
5355 C C   . PRO   B 98  ? 0.2352 0.1835 0.1710 0.0323  0.0381  0.0410  98  PRO   B C   
5356 O O   . PRO   B 98  ? 0.2205 0.1808 0.2082 0.0266  0.0398  0.0422  98  PRO   B O   
5357 C CB  . PRO   B 98  ? 0.2066 0.1898 0.2158 0.0172  0.0585  0.0287  98  PRO   B CB  
5358 C CG  . PRO   B 98  ? 0.2019 0.1815 0.2162 0.0177  0.0403  0.0385  98  PRO   B CG  
5359 C CD  . PRO   B 98  ? 0.1932 0.1699 0.2084 0.0162  0.0365  0.0368  98  PRO   B CD  
5367 N N   . ASN   B 99  ? 0.2549 0.1957 0.1802 0.0534  0.0367  0.0217  99  ASN   B N   
5368 C CA  . ASN   B 99  ? 0.2763 0.2077 0.1823 0.0573  0.0328  0.0402  99  ASN   B CA  
5369 C C   . ASN   B 99  ? 0.3079 0.2498 0.2197 0.0524  0.0459  0.0726  99  ASN   B C   
5370 O O   . ASN   B 99  ? 0.3199 0.2568 0.2318 0.0557  0.0364  0.0692  99  ASN   B O   
5371 C CB  . ASN   B 99  ? 0.2863 0.2094 0.1936 0.0524  0.0118  0.0359  99  ASN   B CB  
5372 C CG  . ASN   B 99  ? 0.2906 0.2181 0.2155 0.0525  0.0021  0.0265  99  ASN   B CG  
5373 O OD1 . ASN   B 99  ? 0.2925 0.2181 0.2378 0.0628  0.0030  0.0291  99  ASN   B OD1 
5374 N ND2 . ASN   B 99  ? 0.2891 0.2193 0.2260 0.0535  -0.0215 0.0184  99  ASN   B ND2 
5381 N N   A VAL   B 100 ? 0.3201 0.2659 0.2493 0.0335  0.0605  0.0966  100 VAL   B N   
5382 N N   B VAL   B 100 ? 0.3308 0.2684 0.2594 0.0423  0.0377  0.0824  100 VAL   B N   
5383 C CA  A VAL   B 100 ? 0.3492 0.2848 0.3128 0.0236  0.0569  0.1107  100 VAL   B CA  
5384 C CA  B VAL   B 100 ? 0.3552 0.2856 0.3012 0.0337  0.0278  0.0899  100 VAL   B CA  
5385 C C   A VAL   B 100 ? 0.3729 0.2928 0.3067 0.0305  0.0506  0.1250  100 VAL   B C   
5386 C C   B VAL   B 100 ? 0.3736 0.2936 0.3036 0.0350  0.0272  0.1108  100 VAL   B C   
5387 O O   A VAL   B 100 ? 0.3822 0.3069 0.3196 0.0246  0.0661  0.1133  100 VAL   B O   
5388 O O   B VAL   B 100 ? 0.3758 0.2977 0.3077 0.0323  0.0277  0.1089  100 VAL   B O   
5389 C CB  A VAL   B 100 ? 0.3581 0.3024 0.3861 0.0012  0.0540  0.1171  100 VAL   B CB  
5390 C CB  B VAL   B 100 ? 0.3604 0.2942 0.3376 0.0239  0.0201  0.0795  100 VAL   B CB  
5391 C CG1 A VAL   B 100 ? 0.3638 0.3114 0.4174 -0.0042 0.0558  0.1160  100 VAL   B CG1 
5392 C CG1 B VAL   B 100 ? 0.3632 0.2982 0.3512 0.0211  0.0184  0.0760  100 VAL   B CG1 
5393 C CG2 A VAL   B 100 ? 0.3604 0.3069 0.4067 -0.0051 0.0569  0.1270  100 VAL   B CG2 
5394 C CG2 B VAL   B 100 ? 0.3612 0.2961 0.3496 0.0207  0.0181  0.0773  100 VAL   B CG2 
5413 N N   . ASN   B 101 ? 0.3884 0.2973 0.2992 0.0402  0.0295  0.1290  101 ASN   B N   
5414 C CA  . ASN   B 101 ? 0.4254 0.3166 0.3249 0.0470  0.0079  0.1368  101 ASN   B CA  
5415 C C   . ASN   B 101 ? 0.4653 0.3593 0.3272 0.0492  -0.0049 0.1392  101 ASN   B C   
5416 O O   . ASN   B 101 ? 0.4689 0.3720 0.3516 0.0537  -0.0012 0.1103  101 ASN   B O   
5417 C CB  . ASN   B 101 ? 0.4225 0.3012 0.3405 0.0413  0.0115  0.1245  101 ASN   B CB  
5418 C CG  . ASN   B 101 ? 0.4173 0.2846 0.3467 0.0371  0.0138  0.1203  101 ASN   B CG  
5419 O OD1 . ASN   B 101 ? 0.4198 0.2839 0.3786 0.0296  0.0285  0.1139  101 ASN   B OD1 
5420 N ND2 . ASN   B 101 ? 0.4107 0.2763 0.3407 0.0378  0.0078  0.1112  101 ASN   B ND2 
5428 N N   . LYS   B 102 ? 0.4984 0.3967 0.3451 0.0418  -0.0036 0.1323  102 LYS   B N   
5429 C CA  . LYS   B 102 ? 0.5292 0.4423 0.3742 0.0296  0.0067  0.1050  102 LYS   B CA  
5430 C C   . LYS   B 102 ? 0.5202 0.4385 0.3530 0.0290  0.0163  0.1037  102 LYS   B C   
5431 O O   . LYS   B 102 ? 0.5291 0.4414 0.3588 0.0306  0.0048  0.0961  102 LYS   B O   
5432 C CB  . LYS   B 102 ? 0.5648 0.4885 0.4467 0.0192  0.0179  0.0660  102 LYS   B CB  
5433 C CG  . LYS   B 102 ? 0.5932 0.5318 0.5258 0.0119  0.0297  0.0265  102 LYS   B CG  
5434 C CD  . LYS   B 102 ? 0.6172 0.5693 0.6029 0.0062  0.0411  -0.0049 102 LYS   B CD  
5435 C CE  . LYS   B 102 ? 0.6356 0.5935 0.6656 0.0013  0.0492  -0.0258 102 LYS   B CE  
5436 N NZ  . LYS   B 102 ? 0.6456 0.6056 0.7012 -0.0013 0.0529  -0.0394 102 LYS   B NZ  
5450 N N   A GLY   B 103 ? 0.5112 0.4320 0.3294 0.0311  0.0439  0.1115  103 GLY   B N   
5451 N N   B GLY   B 103 ? 0.5064 0.4345 0.3593 0.0237  0.0114  0.0936  103 GLY   B N   
5452 C CA  A GLY   B 103 ? 0.4997 0.4249 0.3315 0.0334  0.0721  0.1043  103 GLY   B CA  
5453 C CA  B GLY   B 103 ? 0.4901 0.4276 0.3687 0.0190  0.0091  0.0771  103 GLY   B CA  
5454 C C   A GLY   B 103 ? 0.4837 0.4137 0.3166 0.0326  0.0987  0.0922  103 GLY   B C   
5455 C C   B GLY   B 103 ? 0.4713 0.4184 0.3716 0.0141  0.0070  0.0586  103 GLY   B C   
5456 O O   A GLY   B 103 ? 0.4892 0.4217 0.3188 0.0299  0.1002  0.0924  103 GLY   B O   
5457 O O   B GLY   B 103 ? 0.4722 0.4196 0.3750 0.0141  0.0054  0.0586  103 GLY   B O   
5464 N N   A GLU   B 104 ? 0.4597 0.3915 0.3042 0.0352  0.1160  0.0677  104 GLU   B N   
5465 N N   B GLU   B 104 ? 0.4509 0.4069 0.3679 0.0092  0.0073  0.0391  104 GLU   B N   
5466 C CA  A GLU   B 104 ? 0.4358 0.3698 0.2910 0.0424  0.1183  0.0438  104 GLU   B CA  
5467 C CA  B GLU   B 104 ? 0.4305 0.3954 0.3623 0.0049  0.0075  0.0208  104 GLU   B CA  
5468 C C   A GLU   B 104 ? 0.4366 0.3712 0.3034 0.0260  0.1498  0.0441  104 GLU   B C   
5469 C C   B GLU   B 104 ? 0.4216 0.3926 0.3682 0.0013  0.0138  0.0125  104 GLU   B C   
5470 O O   A GLU   B 104 ? 0.4369 0.3735 0.3291 0.0223  0.1479  0.0392  104 GLU   B O   
5471 O O   B GLU   B 104 ? 0.4207 0.3923 0.3698 0.0009  0.0142  0.0097  104 GLU   B O   
5472 C CB  A GLU   B 104 ? 0.4173 0.3449 0.2837 0.0651  0.0786  0.0114  104 GLU   B CB  
5473 C CB  B GLU   B 104 ? 0.4203 0.3867 0.3516 0.0041  0.0024  0.0110  104 GLU   B CB  
5474 C CG  A GLU   B 104 ? 0.4026 0.3275 0.2745 0.0792  0.0309  -0.0213 104 GLU   B CG  
5475 C CG  B GLU   B 104 ? 0.4118 0.3794 0.3429 0.0027  -0.0027 0.0024  104 GLU   B CG  
5476 C CD  A GLU   B 104 ? 0.3900 0.3104 0.2642 0.0889  -0.0087 -0.0327 104 GLU   B CD  
5477 C CD  B GLU   B 104 ? 0.4051 0.3732 0.3356 0.0009  -0.0062 -0.0027 104 GLU   B CD  
5478 O OE1 A GLU   B 104 ? 0.3732 0.2942 0.2270 0.0976  -0.0101 -0.0293 104 GLU   B OE1 
5479 O OE1 B GLU   B 104 ? 0.4024 0.3705 0.3301 -0.0008 -0.0046 -0.0029 104 GLU   B OE1 
5480 O OE2 A GLU   B 104 ? 0.3951 0.3172 0.2816 0.0826  -0.0417 -0.0447 104 GLU   B OE2 
5481 O OE2 B GLU   B 104 ? 0.4033 0.3718 0.3351 0.0007  -0.0107 -0.0064 104 GLU   B OE2 
5494 N N   A ASP   B 105 ? 0.4328 0.3697 0.3041 0.0114  0.1780  0.0543  105 ASP   B N   
5495 N N   B ASP   B 105 ? 0.4139 0.3904 0.3743 -0.0020 0.0198  0.0090  105 ASP   B N   
5496 C CA  A ASP   B 105 ? 0.4330 0.3689 0.3319 -0.0022 0.1993  0.0448  105 ASP   B CA  
5497 C CA  B ASP   B 105 ? 0.4070 0.3881 0.3820 -0.0052 0.0249  0.0053  105 ASP   B CA  
5498 C C   A ASP   B 105 ? 0.4138 0.3300 0.3110 -0.0152 0.1960  0.0349  105 ASP   B C   
5499 C C   B ASP   B 105 ? 0.3976 0.3801 0.3654 -0.0067 0.0267  0.0026  105 ASP   B C   
5500 O O   A ASP   B 105 ? 0.3985 0.3205 0.3066 -0.0186 0.2010  0.0295  105 ASP   B O   
5501 O O   B ASP   B 105 ? 0.3969 0.3793 0.3601 -0.0073 0.0266  0.0020  105 ASP   B O   
5502 C CB  A ASP   B 105 ? 0.4471 0.3994 0.4037 0.0040  0.2091  0.0301  105 ASP   B CB  
5503 C CB  B ASP   B 105 ? 0.4087 0.3928 0.4068 -0.0057 0.0276  0.0040  105 ASP   B CB  
5504 C CG  A ASP   B 105 ? 0.4563 0.4227 0.4710 0.0082  0.2243  0.0195  105 ASP   B CG  
5505 C CG  B ASP   B 105 ? 0.4103 0.3962 0.4293 -0.0064 0.0299  0.0036  105 ASP   B CG  
5506 O OD1 A ASP   B 105 ? 0.4562 0.4281 0.4760 -0.0000 0.2434  0.0350  105 ASP   B OD1 
5507 O OD1 B ASP   B 105 ? 0.4101 0.3970 0.4363 -0.0076 0.0310  0.0048  105 ASP   B OD1 
5508 O OD2 A ASP   B 105 ? 0.4616 0.4351 0.5227 0.0173  0.2097  0.0004  105 ASP   B OD2 
5509 O OD2 B ASP   B 105 ? 0.4107 0.3982 0.4383 -0.0065 0.0305  0.0032  105 ASP   B OD2 
5518 N N   A ILE   B 106 ? 0.4080 0.3010 0.3266 -0.0176 0.1748  0.0302  106 ILE   B N   
5519 N N   B ILE   B 106 ? 0.3889 0.3725 0.3547 -0.0068 0.0273  0.0013  106 ILE   B N   
5520 C CA  A ILE   B 106 ? 0.3894 0.2711 0.3455 -0.0267 0.1769  0.0227  106 ILE   B CA  
5521 C CA  B ILE   B 106 ? 0.3787 0.3651 0.3486 -0.0066 0.0299  -0.0002 106 ILE   B CA  
5522 C C   A ILE   B 106 ? 0.3506 0.2611 0.3316 -0.0218 0.1792  -0.0067 106 ILE   B C   
5523 C C   B ILE   B 106 ? 0.3647 0.3584 0.3421 -0.0055 0.0341  -0.0037 106 ILE   B C   
5524 O O   A ILE   B 106 ? 0.3410 0.2328 0.3362 -0.0292 0.1741  -0.0180 106 ILE   B O   
5525 O O   B ILE   B 106 ? 0.3648 0.3581 0.3388 -0.0066 0.0314  -0.0048 106 ILE   B O   
5526 C CB  A ILE   B 106 ? 0.4122 0.2619 0.3682 -0.0370 0.1702  0.0428  106 ILE   B CB  
5527 C CB  B ILE   B 106 ? 0.3820 0.3647 0.3507 -0.0075 0.0286  0.0016  106 ILE   B CB  
5528 C CG1 A ILE   B 106 ? 0.4248 0.2618 0.3870 -0.0269 0.1525  0.0385  106 ILE   B CG1 
5529 C CG1 B ILE   B 106 ? 0.3830 0.3637 0.3530 -0.0067 0.0265  0.0026  106 ILE   B CG1 
5530 C CG2 A ILE   B 106 ? 0.4185 0.2664 0.3882 -0.0478 0.1722  0.0550  106 ILE   B CG2 
5531 C CG2 B ILE   B 106 ? 0.3833 0.3659 0.3532 -0.0082 0.0288  0.0019  106 ILE   B CG2 
5532 C CD1 A ILE   B 106 ? 0.4305 0.2630 0.3895 -0.0180 0.1445  0.0399  106 ILE   B CD1 
5533 C CD1 B ILE   B 106 ? 0.3834 0.3633 0.3540 -0.0057 0.0254  0.0033  106 ILE   B CD1 
5556 N N   A GLN   B 107 ? 0.3338 0.2881 0.3438 -0.0247 0.1600  -0.0131 107 GLN   B N   
5557 N N   B GLN   B 107 ? 0.3505 0.3515 0.3439 -0.0041 0.0396  -0.0057 107 GLN   B N   
5558 C CA  A GLN   B 107 ? 0.3128 0.3074 0.3532 -0.0295 0.1402  -0.0045 107 GLN   B CA  
5559 C CA  B GLN   B 107 ? 0.3346 0.3424 0.3492 -0.0021 0.0464  -0.0051 107 GLN   B CA  
5560 C C   A GLN   B 107 ? 0.2799 0.2908 0.3279 -0.0138 0.1029  -0.0075 107 GLN   B C   
5561 C C   B GLN   B 107 ? 0.2989 0.3126 0.3141 0.0025  0.0639  -0.0069 107 GLN   B C   
5562 O O   A GLN   B 107 ? 0.2649 0.2918 0.3628 -0.0053 0.0730  -0.0251 107 GLN   B O   
5563 O O   B GLN   B 107 ? 0.2999 0.3160 0.3134 0.0024  0.0582  -0.0103 107 GLN   B O   
5564 C CB  A GLN   B 107 ? 0.3443 0.3517 0.4247 -0.0350 0.1188  -0.0031 107 GLN   B CB  
5565 C CB  B GLN   B 107 ? 0.3543 0.3617 0.3951 -0.0036 0.0351  -0.0042 107 GLN   B CB  
5566 C CG  A GLN   B 107 ? 0.3804 0.3948 0.5064 -0.0321 0.0788  -0.0035 107 GLN   B CG  
5567 C CG  B GLN   B 107 ? 0.3714 0.3782 0.4414 -0.0037 0.0239  -0.0029 107 GLN   B CG  
5568 C CD  A GLN   B 107 ? 0.4076 0.4232 0.5718 -0.0323 0.0508  -0.0004 107 GLN   B CD  
5569 C CD  B GLN   B 107 ? 0.3843 0.3905 0.4789 -0.0041 0.0154  -0.0010 107 GLN   B CD  
5570 O OE1 A GLN   B 107 ? 0.4194 0.4344 0.5976 -0.0277 0.0467  -0.0015 107 GLN   B OE1 
5571 O OE1 B GLN   B 107 ? 0.3892 0.3954 0.4925 -0.0038 0.0138  -0.0007 107 GLN   B OE1 
5572 N NE2 A GLN   B 107 ? 0.4187 0.4322 0.5946 -0.0314 0.0389  0.0054  107 GLN   B NE2 
5573 N NE2 B GLN   B 107 ? 0.3889 0.3939 0.4922 -0.0039 0.0123  0.0007  107 GLN   B NE2 
5590 N N   . LEU   B 108 ? 0.2596 0.2772 0.2884 0.0076  0.0874  -0.0066 108 LEU   B N   
5591 C CA  . LEU   B 108 ? 0.2353 0.2437 0.2503 0.0262  0.0695  0.0104  108 LEU   B CA  
5592 C C   . LEU   B 108 ? 0.1978 0.1967 0.2519 0.0211  0.0391  0.0244  108 LEU   B C   
5593 O O   . LEU   B 108 ? 0.1975 0.1876 0.2479 0.0248  0.0304  0.0159  108 LEU   B O   
5594 C CB  . LEU   B 108 ? 0.2538 0.2696 0.2371 0.0283  0.0712  0.0184  108 LEU   B CB  
5595 C CG  . LEU   B 108 ? 0.2727 0.2984 0.2492 0.0291  0.0634  0.0010  108 LEU   B CG  
5596 C CD1 . LEU   B 108 ? 0.2828 0.3126 0.2424 0.0197  0.0578  0.0047  108 LEU   B CD1 
5597 C CD2 . LEU   B 108 ? 0.2899 0.3084 0.2629 0.0369  0.0493  -0.0118 108 LEU   B CD2 
5610 N N   . LEU   B 109 ? 0.1803 0.1738 0.2496 0.0136  0.0429  0.0240  109 LEU   B N   
5611 C CA  . LEU   B 109 ? 0.1618 0.1475 0.2574 0.0145  0.0364  0.0280  109 LEU   B CA  
5612 C C   . LEU   B 109 ? 0.1490 0.1360 0.2570 0.0027  0.0338  0.0126  109 LEU   B C   
5613 O O   . LEU   B 109 ? 0.1470 0.1371 0.2538 0.0050  0.0319  0.0221  109 LEU   B O   
5614 C CB  . LEU   B 109 ? 0.1729 0.1437 0.2641 0.0109  0.0244  0.0309  109 LEU   B CB  
5615 C CG  . LEU   B 109 ? 0.1747 0.1425 0.2584 0.0077  0.0135  0.0169  109 LEU   B CG  
5616 C CD1 . LEU   B 109 ? 0.1705 0.1561 0.2404 0.0146  0.0303  0.0188  109 LEU   B CD1 
5617 C CD2 . LEU   B 109 ? 0.1863 0.1472 0.2616 0.0020  0.0089  0.0147  109 LEU   B CD2 
5629 N N   . LYS   B 110 ? 0.1452 0.1363 0.2502 -0.0059 0.0348  0.0187  110 LYS   B N   
5630 C CA  . LYS   B 110 ? 0.1469 0.1358 0.2488 0.0018  0.0219  0.0171  110 LYS   B CA  
5631 C C   . LYS   B 110 ? 0.1432 0.1421 0.2325 0.0030  0.0255  0.0099  110 LYS   B C   
5632 O O   . LYS   B 110 ? 0.1416 0.1388 0.2313 -0.0047 0.0205  0.0038  110 LYS   B O   
5633 C CB  . LYS   B 110 ? 0.1505 0.1403 0.2641 -0.0011 0.0281  0.0133  110 LYS   B CB  
5634 C CG  . LYS   B 110 ? 0.1497 0.1417 0.2803 -0.0037 0.0128  0.0148  110 LYS   B CG  
5635 C CD  . LYS   B 110 ? 0.1601 0.1479 0.2868 -0.0021 0.0203  0.0056  110 LYS   B CD  
5636 C CE  . LYS   B 110 ? 0.1560 0.1579 0.3114 -0.0037 0.0114  0.0044  110 LYS   B CE  
5637 N NZ  . LYS   B 110 ? 0.1615 0.1742 0.3034 0.0037  -0.0057 -0.0068 110 LYS   B NZ  
5651 N N   . SER   B 111 ? 0.1511 0.1390 0.2397 -0.0016 0.0274  0.0144  111 SER   B N   
5652 C CA  . SER   B 111 ? 0.1581 0.1420 0.2359 0.0054  0.0210  0.0178  111 SER   B CA  
5653 C C   . SER   B 111 ? 0.1513 0.1306 0.2305 0.0023  0.0065  0.0051  111 SER   B C   
5654 O O   . SER   B 111 ? 0.1437 0.1362 0.2408 -0.0003 0.0097  0.0086  111 SER   B O   
5655 C CB  . SER   B 111 ? 0.1772 0.1632 0.2448 0.0073  0.0379  0.0233  111 SER   B CB  
5656 O OG  . SER   B 111 ? 0.1997 0.2003 0.2504 0.0063  0.0488  0.0221  111 SER   B OG  
5662 N N   . ALA   B 112 ? 0.1420 0.1365 0.2270 0.0055  0.0203  0.0119  112 ALA   B N   
5663 C CA  . ALA   B 112 ? 0.1361 0.1416 0.2059 0.0012  0.0107  0.0022  112 ALA   B CA  
5664 C C   . ALA   B 112 ? 0.1293 0.1344 0.1997 -0.0009 0.0139  -0.0020 112 ALA   B C   
5665 O O   . ALA   B 112 ? 0.1312 0.1362 0.2194 -0.0034 0.0082  0.0015  112 ALA   B O   
5666 C CB  . ALA   B 112 ? 0.1438 0.1499 0.2209 0.0077  0.0140  0.0075  112 ALA   B CB  
5672 N N   . TYR   B 113 ? 0.1342 0.1292 0.2062 -0.0015 0.0102  0.0090  113 TYR   B N   
5673 C CA  . TYR   B 113 ? 0.1261 0.1223 0.2025 -0.0057 0.0164  -0.0020 113 TYR   B CA  
5674 C C   . TYR   B 113 ? 0.1269 0.1171 0.2070 -0.0082 0.0107  -0.0025 113 TYR   B C   
5675 O O   . TYR   B 113 ? 0.1326 0.1274 0.2019 -0.0010 0.0007  -0.0029 113 TYR   B O   
5676 C CB  . TYR   B 113 ? 0.1295 0.1206 0.2256 -0.0026 0.0211  0.0090  113 TYR   B CB  
5677 C CG  . TYR   B 113 ? 0.1340 0.1206 0.2349 -0.0067 0.0102  0.0094  113 TYR   B CG  
5678 C CD1 . TYR   B 113 ? 0.1399 0.1260 0.2491 -0.0052 0.0082  0.0112  113 TYR   B CD1 
5679 C CD2 . TYR   B 113 ? 0.1390 0.1226 0.2425 -0.0041 0.0013  0.0056  113 TYR   B CD2 
5680 C CE1 . TYR   B 113 ? 0.1428 0.1301 0.2343 -0.0009 0.0108  0.0047  113 TYR   B CE1 
5681 C CE2 . TYR   B 113 ? 0.1452 0.1137 0.2525 -0.0034 0.0023  0.0097  113 TYR   B CE2 
5682 C CZ  . TYR   B 113 ? 0.1384 0.1240 0.2472 0.0048  0.0004  0.0061  113 TYR   B CZ  
5683 O OH  . TYR   B 113 ? 0.1497 0.1264 0.2668 0.0065  0.0146  0.0035  113 TYR   B OH  
5693 N N   . GLU   B 114 ? 0.1249 0.1184 0.2140 0.0000  0.0116  0.0049  114 GLU   B N   
5694 C CA  . GLU   B 114 ? 0.1299 0.1181 0.2239 0.0042  0.0086  0.0002  114 GLU   B CA  
5695 C C   . GLU   B 114 ? 0.1246 0.1182 0.2126 0.0014  0.0051  -0.0060 114 GLU   B C   
5696 O O   . GLU   B 114 ? 0.1327 0.1201 0.2348 0.0054  0.0018  0.0016  114 GLU   B O   
5697 C CB  . GLU   B 114 ? 0.1331 0.1224 0.2437 -0.0006 0.0126  0.0011  114 GLU   B CB  
5698 C CG  . GLU   B 114 ? 0.1332 0.1250 0.2439 0.0048  0.0072  0.0010  114 GLU   B CG  
5699 C CD  . GLU   B 114 ? 0.1336 0.1359 0.2420 -0.0040 0.0031  0.0065  114 GLU   B CD  
5700 O OE1 . GLU   B 114 ? 0.1327 0.1577 0.2428 -0.0063 0.0112  0.0037  114 GLU   B OE1 
5701 O OE2 . GLU   B 114 ? 0.1296 0.1569 0.2636 -0.0119 0.0106  0.0017  114 GLU   B OE2 
5708 N N   . ASN   B 115 ? 0.1284 0.1200 0.1975 -0.0003 -0.0049 0.0009  115 ASN   B N   
5709 C CA  . ASN   B 115 ? 0.1305 0.1207 0.1953 -0.0053 0.0079  0.0093  115 ASN   B CA  
5710 C C   . ASN   B 115 ? 0.1259 0.1194 0.2008 -0.0046 -0.0015 -0.0042 115 ASN   B C   
5711 O O   . ASN   B 115 ? 0.1420 0.1253 0.2067 -0.0148 0.0020  -0.0017 115 ASN   B O   
5712 C CB  . ASN   B 115 ? 0.1444 0.1364 0.1996 -0.0073 0.0058  0.0128  115 ASN   B CB  
5713 C CG  . ASN   B 115 ? 0.1570 0.1464 0.2050 0.0022  0.0071  0.0039  115 ASN   B CG  
5714 O OD1 . ASN   B 115 ? 0.2077 0.1595 0.2231 0.0027  0.0140  -0.0075 115 ASN   B OD1 
5715 N ND2 . ASN   B 115 ? 0.1504 0.1588 0.2096 -0.0072 0.0087  0.0086  115 ASN   B ND2 
5722 N N   . PHE   B 116 ? 0.1277 0.1193 0.1824 -0.0011 0.0055  -0.0015 116 PHE   B N   
5723 C CA  . PHE   B 116 ? 0.1359 0.1273 0.1946 -0.0095 -0.0008 0.0067  116 PHE   B CA  
5724 C C   . PHE   B 116 ? 0.1345 0.1149 0.1915 -0.0105 -0.0053 0.0050  116 PHE   B C   
5725 O O   . PHE   B 116 ? 0.1385 0.1276 0.2024 -0.0006 -0.0096 0.0012  116 PHE   B O   
5726 C CB  . PHE   B 116 ? 0.1325 0.1216 0.1834 -0.0040 -0.0107 0.0031  116 PHE   B CB  
5727 C CG  . PHE   B 116 ? 0.1253 0.1255 0.1915 -0.0061 -0.0029 0.0014  116 PHE   B CG  
5728 C CD1 . PHE   B 116 ? 0.1359 0.1279 0.2050 0.0002  -0.0063 0.0056  116 PHE   B CD1 
5729 C CD2 . PHE   B 116 ? 0.1335 0.1366 0.1855 0.0024  -0.0011 -0.0096 116 PHE   B CD2 
5730 C CE1 . PHE   B 116 ? 0.1404 0.1298 0.2080 0.0028  -0.0135 0.0095  116 PHE   B CE1 
5731 C CE2 . PHE   B 116 ? 0.1383 0.1350 0.1863 0.0006  0.0077  0.0009  116 PHE   B CE2 
5732 C CZ  . PHE   B 116 ? 0.1280 0.1337 0.2026 -0.0011 -0.0059 0.0064  116 PHE   B CZ  
5742 N N   . ASN   B 117 ? 0.1307 0.1242 0.2066 -0.0043 -0.0110 0.0004  117 ASN   B N   
5743 C CA  . ASN   B 117 ? 0.1418 0.1256 0.2198 0.0005  -0.0096 0.0067  117 ASN   B CA  
5744 C C   . ASN   B 117 ? 0.1410 0.1188 0.2265 -0.0004 -0.0045 0.0051  117 ASN   B C   
5745 O O   . ASN   B 117 ? 0.1501 0.1254 0.2530 -0.0038 -0.0260 0.0063  117 ASN   B O   
5746 C CB  . ASN   B 117 ? 0.1394 0.1283 0.2196 0.0040  -0.0023 -0.0052 117 ASN   B CB  
5747 C CG  . ASN   B 117 ? 0.1376 0.1325 0.2236 0.0026  -0.0023 -0.0099 117 ASN   B CG  
5748 O OD1 . ASN   B 117 ? 0.1619 0.1364 0.2335 -0.0148 0.0022  -0.0055 117 ASN   B OD1 
5749 N ND2 . ASN   B 117 ? 0.1351 0.1352 0.2154 -0.0021 -0.0040 -0.0099 117 ASN   B ND2 
5756 N N   . GLN   B 118 ? 0.1410 0.1183 0.2108 -0.0029 -0.0145 -0.0039 118 GLN   B N   
5757 C CA  . GLN   B 118 ? 0.1417 0.1265 0.2282 0.0054  -0.0104 -0.0053 118 GLN   B CA  
5758 C C   . GLN   B 118 ? 0.1475 0.1178 0.2366 0.0028  -0.0110 0.0011  118 GLN   B C   
5759 O O   . GLN   B 118 ? 0.1736 0.1164 0.2705 -0.0056 0.0008  -0.0009 118 GLN   B O   
5760 C CB  . GLN   B 118 ? 0.1552 0.1336 0.2333 0.0057  -0.0111 -0.0047 118 GLN   B CB  
5761 C CG  . GLN   B 118 ? 0.1649 0.1379 0.2269 0.0095  -0.0145 -0.0159 118 GLN   B CG  
5762 C CD  . GLN   B 118 ? 0.1705 0.1255 0.2293 0.0118  -0.0235 -0.0237 118 GLN   B CD  
5763 O OE1 . GLN   B 118 ? 0.1780 0.1247 0.2557 0.0089  -0.0036 0.0017  118 GLN   B OE1 
5764 N NE2 . GLN   B 118 ? 0.1782 0.1294 0.2400 0.0075  -0.0275 -0.0048 118 GLN   B NE2 
5773 N N   . HIS   B 119 ? 0.1471 0.1249 0.1962 -0.0057 -0.0087 0.0049  119 HIS   B N   
5774 C CA  . HIS   B 119 ? 0.1582 0.1398 0.1885 0.0031  -0.0143 0.0064  119 HIS   B CA  
5775 C C   . HIS   B 119 ? 0.1642 0.1375 0.1877 -0.0044 -0.0277 0.0125  119 HIS   B C   
5776 O O   . HIS   B 119 ? 0.1778 0.1382 0.2065 -0.0244 -0.0199 0.0064  119 HIS   B O   
5777 C CB  . HIS   B 119 ? 0.1649 0.1491 0.1868 0.0012  -0.0147 0.0068  119 HIS   B CB  
5778 C CG  . HIS   B 119 ? 0.1697 0.1727 0.2006 0.0046  -0.0358 -0.0091 119 HIS   B CG  
5779 N ND1 . HIS   B 119 ? 0.1843 0.1827 0.2344 -0.0021 -0.0499 -0.0277 119 HIS   B ND1 
5780 C CD2 . HIS   B 119 ? 0.1861 0.1915 0.2041 0.0332  -0.0556 -0.0102 119 HIS   B CD2 
5781 C CE1 . HIS   B 119 ? 0.2066 0.2009 0.2372 0.0143  -0.0488 -0.0351 119 HIS   B CE1 
5782 N NE2 . HIS   B 119 ? 0.2035 0.2180 0.2191 0.0277  -0.0515 -0.0337 119 HIS   B NE2 
5790 N N   . GLU   B 120 ? 0.1873 0.1441 0.1778 -0.0080 -0.0411 0.0177  120 GLU   B N   
5791 C CA  . GLU   B 120 ? 0.2160 0.1656 0.2009 -0.0023 -0.0483 0.0340  120 GLU   B CA  
5792 C C   . GLU   B 120 ? 0.1906 0.1548 0.1878 -0.0115 -0.0330 0.0255  120 GLU   B C   
5793 O O   . GLU   B 120 ? 0.1858 0.1645 0.1996 -0.0173 -0.0318 0.0079  120 GLU   B O   
5794 C CB  . GLU   B 120 ? 0.2847 0.2150 0.2728 0.0263  -0.0718 0.0595  120 GLU   B CB  
5795 C CG  . GLU   B 120 ? 0.3507 0.2914 0.3718 0.0296  -0.0905 0.0803  120 GLU   B CG  
5796 C CD  . GLU   B 120 ? 0.3988 0.3634 0.4816 0.0295  -0.0953 0.0919  120 GLU   B CD  
5797 O OE1 . GLU   B 120 ? 0.4235 0.3914 0.5211 0.0254  -0.0916 0.1016  120 GLU   B OE1 
5798 O OE2 . GLU   B 120 ? 0.4141 0.4012 0.5327 0.0304  -0.0957 0.0879  120 GLU   B OE2 
5805 N N   . VAL   B 121 ? 0.1802 0.1428 0.1944 -0.0207 -0.0191 0.0201  121 VAL   B N   
5806 C CA  . VAL   B 121 ? 0.1729 0.1553 0.1749 -0.0136 -0.0187 0.0155  121 VAL   B CA  
5807 C C   . VAL   B 121 ? 0.1630 0.1456 0.1680 -0.0219 -0.0159 0.0148  121 VAL   B C   
5808 O O   . VAL   B 121 ? 0.1727 0.1414 0.1952 -0.0261 -0.0247 0.0078  121 VAL   B O   
5809 C CB  . VAL   B 121 ? 0.1949 0.1963 0.1824 -0.0058 -0.0261 0.0200  121 VAL   B CB  
5810 C CG1 . VAL   B 121 ? 0.2068 0.2083 0.2192 -0.0138 -0.0071 0.0180  121 VAL   B CG1 
5811 C CG2 . VAL   B 121 ? 0.2157 0.2227 0.1865 0.0016  -0.0206 0.0117  121 VAL   B CG2 
5821 N N   . LEU   B 122 ? 0.1567 0.1345 0.1681 -0.0151 -0.0260 0.0077  122 LEU   B N   
5822 C CA  . LEU   B 122 ? 0.1463 0.1498 0.1599 -0.0184 -0.0127 0.0089  122 LEU   B CA  
5823 C C   . LEU   B 122 ? 0.1473 0.1367 0.1583 -0.0293 -0.0167 0.0057  122 LEU   B C   
5824 O O   . LEU   B 122 ? 0.1589 0.1426 0.1916 -0.0303 -0.0248 -0.0010 122 LEU   B O   
5825 C CB  . LEU   B 122 ? 0.1738 0.1612 0.1908 -0.0005 -0.0200 0.0027  122 LEU   B CB  
5826 C CG  . LEU   B 122 ? 0.1604 0.1644 0.2035 -0.0139 -0.0057 -0.0000 122 LEU   B CG  
5827 C CD1 . LEU   B 122 ? 0.1699 0.1892 0.2176 -0.0166 -0.0089 0.0045  122 LEU   B CD1 
5828 C CD2 . LEU   B 122 ? 0.1582 0.1704 0.1836 -0.0083 0.0063  -0.0136 122 LEU   B CD2 
5840 N N   . LEU   B 123 ? 0.1456 0.1231 0.1629 -0.0249 -0.0153 0.0076  123 LEU   B N   
5841 C CA  . LEU   B 123 ? 0.1514 0.1284 0.1665 -0.0240 -0.0152 0.0016  123 LEU   B CA  
5842 C C   . LEU   B 123 ? 0.1429 0.1267 0.1619 -0.0193 -0.0166 -0.0002 123 LEU   B C   
5843 O O   . LEU   B 123 ? 0.1558 0.1315 0.1772 -0.0288 -0.0166 -0.0028 123 LEU   B O   
5844 C CB  . LEU   B 123 ? 0.1599 0.1360 0.1748 -0.0279 -0.0068 -0.0057 123 LEU   B CB  
5845 C CG  . LEU   B 123 ? 0.1586 0.1403 0.1834 -0.0226 -0.0056 0.0086  123 LEU   B CG  
5846 C CD1 . LEU   B 123 ? 0.1663 0.1441 0.1809 -0.0230 0.0058  -0.0058 123 LEU   B CD1 
5847 C CD2 . LEU   B 123 ? 0.1666 0.1475 0.1985 -0.0110 0.0004  0.0125  123 LEU   B CD2 
5859 N N   . ALA   B 124 ? 0.1420 0.1283 0.1640 -0.0211 -0.0059 -0.0062 124 ALA   B N   
5860 C CA  . ALA   B 124 ? 0.1354 0.1291 0.1800 -0.0176 -0.0059 -0.0126 124 ALA   B CA  
5861 C C   . ALA   B 124 ? 0.1319 0.1263 0.1758 -0.0190 -0.0143 -0.0044 124 ALA   B C   
5862 O O   . ALA   B 124 ? 0.1430 0.1290 0.1801 -0.0146 -0.0133 -0.0064 124 ALA   B O   
5863 C CB  . ALA   B 124 ? 0.1443 0.1293 0.1906 -0.0062 0.0021  -0.0091 124 ALA   B CB  
5869 N N   . PRO   B 125 ? 0.1460 0.1287 0.1686 -0.0185 -0.0233 0.0058  125 PRO   B N   
5870 C CA  . PRO   B 125 ? 0.1505 0.1327 0.1861 -0.0156 -0.0212 0.0184  125 PRO   B CA  
5871 C C   . PRO   B 125 ? 0.1467 0.1236 0.2006 -0.0149 -0.0118 0.0049  125 PRO   B C   
5872 O O   . PRO   B 125 ? 0.1482 0.1251 0.2269 -0.0071 -0.0092 0.0141  125 PRO   B O   
5873 C CB  . PRO   B 125 ? 0.1491 0.1591 0.2024 -0.0220 -0.0116 0.0298  125 PRO   B CB  
5874 C CG  . PRO   B 125 ? 0.1571 0.1656 0.1957 -0.0251 -0.0218 0.0184  125 PRO   B CG  
5875 C CD  . PRO   B 125 ? 0.1532 0.1427 0.1763 -0.0335 -0.0152 0.0055  125 PRO   B CD  
5883 N N   . LEU   B 126 ? 0.1436 0.1251 0.2226 -0.0138 0.0059  0.0072  126 LEU   B N   
5884 C CA  . LEU   B 126 ? 0.1540 0.1356 0.2183 -0.0057 0.0087  0.0085  126 LEU   B CA  
5885 C C   . LEU   B 126 ? 0.1548 0.1436 0.2121 0.0061  0.0141  0.0212  126 LEU   B C   
5886 O O   . LEU   B 126 ? 0.1783 0.1736 0.2372 0.0245  -0.0013 -0.0045 126 LEU   B O   
5887 C CB  . LEU   B 126 ? 0.1793 0.1402 0.2503 -0.0166 0.0222  0.0032  126 LEU   B CB  
5888 C CG  . LEU   B 126 ? 0.1979 0.1497 0.2566 -0.0226 0.0249  -0.0150 126 LEU   B CG  
5889 C CD1 . LEU   B 126 ? 0.2183 0.1476 0.3089 -0.0216 0.0273  -0.0312 126 LEU   B CD1 
5890 C CD2 . LEU   B 126 ? 0.2027 0.1666 0.2625 -0.0322 0.0166  -0.0120 126 LEU   B CD2 
5902 N N   . LEU   B 127 ? 0.1472 0.1313 0.2198 0.0072  0.0193  0.0147  127 LEU   B N   
5903 C CA  . LEU   B 127 ? 0.1470 0.1430 0.2246 -0.0024 0.0263  0.0264  127 LEU   B CA  
5904 C C   . LEU   B 127 ? 0.1460 0.1363 0.2307 0.0011  0.0170  0.0204  127 LEU   B C   
5905 O O   . LEU   B 127 ? 0.1479 0.1405 0.2378 -0.0150 0.0104  0.0185  127 LEU   B O   
5906 C CB  . LEU   B 127 ? 0.1624 0.1420 0.2404 -0.0049 0.0195  0.0281  127 LEU   B CB  
5907 C CG  . LEU   B 127 ? 0.1796 0.1399 0.2654 0.0036  0.0258  0.0191  127 LEU   B CG  
5908 C CD1 . LEU   B 127 ? 0.1960 0.1407 0.2666 0.0113  0.0169  0.0102  127 LEU   B CD1 
5909 C CD2 . LEU   B 127 ? 0.1853 0.1570 0.2743 -0.0080 0.0304  0.0326  127 LEU   B CD2 
5921 N N   . SER   B 128 ? 0.1517 0.1324 0.2264 0.0012  -0.0011 0.0176  128 SER   B N   
5922 C CA  . SER   B 128 ? 0.1648 0.1462 0.2295 0.0107  -0.0039 0.0173  128 SER   B CA  
5923 C C   . SER   B 128 ? 0.1778 0.1488 0.2548 0.0085  -0.0198 0.0244  128 SER   B C   
5924 O O   . SER   B 128 ? 0.1971 0.1494 0.2902 0.0074  -0.0226 0.0306  128 SER   B O   
5925 C CB  . SER   B 128 ? 0.1721 0.1482 0.2329 0.0062  0.0009  0.0225  128 SER   B CB  
5926 O OG  . SER   B 128 ? 0.1773 0.1626 0.2336 0.0107  0.0201  0.0283  128 SER   B OG  
5932 N N   . ALA   B 129 ? 0.1896 0.1568 0.2709 0.0207  -0.0092 0.0099  129 ALA   B N   
5933 C CA  . ALA   B 129 ? 0.2070 0.1634 0.2946 0.0256  -0.0107 0.0003  129 ALA   B CA  
5934 C C   . ALA   B 129 ? 0.1895 0.1550 0.2791 0.0189  0.0080  0.0061  129 ALA   B C   
5935 O O   . ALA   B 129 ? 0.1788 0.1584 0.2840 0.0180  -0.0017 0.0043  129 ALA   B O   
5936 C CB  . ALA   B 129 ? 0.2283 0.1851 0.3307 0.0321  0.0039  -0.0107 129 ALA   B CB  
5942 N N   . GLY   B 130 ? 0.1838 0.1511 0.2751 0.0273  0.0132  -0.0046 130 GLY   B N   
5943 C CA  . GLY   B 130 ? 0.1884 0.1593 0.2894 0.0236  0.0405  -0.0000 130 GLY   B CA  
5944 C C   . GLY   B 130 ? 0.1951 0.1634 0.2818 0.0160  0.0230  0.0119  130 GLY   B C   
5945 O O   . GLY   B 130 ? 0.2144 0.1787 0.2776 0.0167  0.0151  0.0186  130 GLY   B O   
5949 N N   . ILE   B 131 ? 0.1894 0.1757 0.2859 0.0269  0.0132  0.0127  131 ILE   B N   
5950 C CA  . ILE   B 131 ? 0.2078 0.1936 0.2721 0.0207  0.0014  0.0272  131 ILE   B CA  
5951 C C   . ILE   B 131 ? 0.2236 0.1875 0.2492 0.0158  0.0027  0.0274  131 ILE   B C   
5952 O O   . ILE   B 131 ? 0.2551 0.2046 0.2625 0.0190  -0.0162 0.0282  131 ILE   B O   
5953 C CB  . ILE   B 131 ? 0.2115 0.2305 0.3064 0.0180  -0.0133 0.0340  131 ILE   B CB  
5954 C CG1 . ILE   B 131 ? 0.2183 0.2495 0.3128 -0.0101 -0.0056 0.0375  131 ILE   B CG1 
5955 C CG2 . ILE   B 131 ? 0.2095 0.2496 0.3278 0.0260  -0.0097 0.0256  131 ILE   B CG2 
5956 C CD1 . ILE   B 131 ? 0.2286 0.2672 0.3189 -0.0256 -0.0103 0.0470  131 ILE   B CD1 
5968 N N   . PHE   B 132 ? 0.2070 0.1694 0.2404 0.0088  0.0139  0.0285  132 PHE   B N   
5969 C CA  . PHE   B 132 ? 0.2172 0.1750 0.2352 0.0073  0.0330  0.0145  132 PHE   B CA  
5970 C C   . PHE   B 132 ? 0.2351 0.1888 0.2573 0.0077  0.0413  0.0166  132 PHE   B C   
5971 O O   . PHE   B 132 ? 0.2550 0.2060 0.2845 0.0037  0.0578  0.0195  132 PHE   B O   
5972 C CB  . PHE   B 132 ? 0.2000 0.1729 0.2272 0.0093  0.0336  0.0235  132 PHE   B CB  
5973 C CG  . PHE   B 132 ? 0.1982 0.1759 0.2245 0.0175  0.0260  0.0259  132 PHE   B CG  
5974 C CD1 . PHE   B 132 ? 0.2087 0.1791 0.2594 0.0122  0.0238  0.0248  132 PHE   B CD1 
5975 C CD2 . PHE   B 132 ? 0.2033 0.1769 0.2095 0.0229  0.0253  0.0289  132 PHE   B CD2 
5976 C CE1 . PHE   B 132 ? 0.2127 0.1847 0.2640 0.0125  0.0160  0.0336  132 PHE   B CE1 
5977 C CE2 . PHE   B 132 ? 0.2085 0.1839 0.2152 0.0229  0.0152  0.0293  132 PHE   B CE2 
5978 C CZ  . PHE   B 132 ? 0.2127 0.1843 0.2527 0.0173  -0.0007 0.0395  132 PHE   B CZ  
5988 N N   . GLY   B 133 ? 0.2304 0.1748 0.2535 0.0095  0.0254  0.0350  133 GLY   B N   
5989 C CA  . GLY   B 133 ? 0.2417 0.1888 0.2631 -0.0149 0.0229  0.0360  133 GLY   B CA  
5990 C C   . GLY   B 133 ? 0.2444 0.1959 0.2586 -0.0282 0.0324  0.0376  133 GLY   B C   
5991 O O   . GLY   B 133 ? 0.2692 0.2134 0.3034 -0.0468 0.0265  0.0510  133 GLY   B O   
5995 N N   . ALA   B 134 ? 0.2246 0.1975 0.2496 -0.0276 0.0341  0.0253  134 ALA   B N   
5996 C CA  . ALA   B 134 ? 0.2197 0.1966 0.2727 -0.0198 0.0414  0.0140  134 ALA   B CA  
5997 C C   . ALA   B 134 ? 0.2250 0.1812 0.2761 -0.0151 0.0359  0.0301  134 ALA   B C   
5998 O O   . ALA   B 134 ? 0.2312 0.1982 0.2947 -0.0011 0.0338  0.0177  134 ALA   B O   
5999 C CB  . ALA   B 134 ? 0.2186 0.1953 0.2929 -0.0139 0.0378  0.0014  134 ALA   B CB  
6005 N N   . ASP   B 135 ? 0.2403 0.1728 0.2771 -0.0162 0.0279  0.0333  135 ASP   B N   
6006 C CA  . ASP   B 135 ? 0.2595 0.1613 0.2891 -0.0121 0.0125  0.0344  135 ASP   B CA  
6007 C C   . ASP   B 135 ? 0.2396 0.1558 0.2711 0.0003  0.0071  0.0304  135 ASP   B C   
6008 O O   . ASP   B 135 ? 0.2346 0.1522 0.2922 0.0011  0.0095  0.0315  135 ASP   B O   
6009 C CB  . ASP   B 135 ? 0.2932 0.1745 0.3109 -0.0306 0.0165  0.0355  135 ASP   B CB  
6010 C CG  . ASP   B 135 ? 0.3237 0.1775 0.3491 -0.0542 0.0197  0.0261  135 ASP   B CG  
6011 O OD1 . ASP   B 135 ? 0.3359 0.1735 0.3459 -0.0363 0.0065  0.0198  135 ASP   B OD1 
6012 O OD2 . ASP   B 135 ? 0.3495 0.2154 0.4010 -0.0654 0.0216  0.0053  135 ASP   B OD2 
6017 N N   . PRO   B 136 ? 0.2258 0.1642 0.2816 0.0183  -0.0046 0.0275  136 PRO   B N   
6018 C CA  . PRO   B 136 ? 0.2029 0.1568 0.2846 0.0188  -0.0015 0.0096  136 PRO   B CA  
6019 C C   . PRO   B 136 ? 0.1808 0.1404 0.2936 0.0160  0.0015  -0.0030 136 PRO   B C   
6020 O O   . PRO   B 136 ? 0.1645 0.1332 0.2940 0.0057  -0.0019 0.0086  136 PRO   B O   
6021 C CB  . PRO   B 136 ? 0.2077 0.1807 0.2884 0.0296  -0.0118 -0.0009 136 PRO   B CB  
6022 C CG  . PRO   B 136 ? 0.2329 0.1877 0.3079 0.0321  -0.0071 0.0029  136 PRO   B CG  
6023 C CD  . PRO   B 136 ? 0.2338 0.1815 0.2985 0.0401  -0.0024 0.0148  136 PRO   B CD  
6031 N N   . ILE   B 137 ? 0.1937 0.1334 0.3068 0.0127  -0.0084 -0.0004 137 ILE   B N   
6032 C CA  . ILE   B 137 ? 0.2038 0.1344 0.3180 -0.0028 -0.0002 -0.0029 137 ILE   B CA  
6033 C C   . ILE   B 137 ? 0.1925 0.1445 0.3102 -0.0072 0.0035  0.0036  137 ILE   B C   
6034 O O   . ILE   B 137 ? 0.1802 0.1462 0.2984 -0.0141 0.0009  0.0073  137 ILE   B O   
6035 C CB  . ILE   B 137 ? 0.2276 0.1368 0.3587 -0.0095 -0.0010 -0.0071 137 ILE   B CB  
6036 C CG1 . ILE   B 137 ? 0.2546 0.1510 0.3969 -0.0005 0.0023  -0.0155 137 ILE   B CG1 
6037 C CG2 . ILE   B 137 ? 0.2368 0.1454 0.3696 -0.0353 -0.0041 -0.0002 137 ILE   B CG2 
6038 C CD1 . ILE   B 137 ? 0.2791 0.1842 0.4320 0.0113  -0.0060 -0.0027 137 ILE   B CD1 
6050 N N   . HIS   B 138 ? 0.1986 0.1340 0.3048 -0.0092 0.0098  0.0048  138 HIS   B N   
6051 C CA  . HIS   B 138 ? 0.2061 0.1461 0.3048 -0.0049 0.0284  0.0094  138 HIS   B CA  
6052 C C   . HIS   B 138 ? 0.1925 0.1423 0.2894 -0.0058 0.0234  0.0217  138 HIS   B C   
6053 O O   . HIS   B 138 ? 0.1812 0.1450 0.3109 -0.0027 0.0276  0.0301  138 HIS   B O   
6054 C CB  . HIS   B 138 ? 0.2300 0.1604 0.3175 -0.0106 0.0467  0.0110  138 HIS   B CB  
6055 C CG  . HIS   B 138 ? 0.2565 0.1756 0.3224 -0.0153 0.0644  0.0304  138 HIS   B CG  
6056 N ND1 . HIS   B 138 ? 0.2653 0.1947 0.3427 -0.0111 0.0808  0.0239  138 HIS   B ND1 
6057 C CD2 . HIS   B 138 ? 0.2743 0.1856 0.3092 -0.0154 0.0752  0.0244  138 HIS   B CD2 
6058 C CE1 . HIS   B 138 ? 0.2710 0.1961 0.3335 -0.0104 0.0798  0.0251  138 HIS   B CE1 
6059 N NE2 . HIS   B 138 ? 0.2805 0.1854 0.3187 -0.0062 0.0809  0.0213  138 HIS   B NE2 
6067 N N   . SER   B 139 ? 0.1875 0.1263 0.2794 0.0020  0.0197  0.0085  139 SER   B N   
6068 C CA  . SER   B 139 ? 0.1819 0.1197 0.2632 0.0005  0.0198  -0.0023 139 SER   B CA  
6069 C C   . SER   B 139 ? 0.1596 0.1167 0.2621 -0.0023 0.0126  -0.0041 139 SER   B C   
6070 O O   . SER   B 139 ? 0.1623 0.1175 0.2661 -0.0033 0.0038  -0.0008 139 SER   B O   
6071 C CB  . SER   B 139 ? 0.1868 0.1277 0.2715 0.0044  0.0105  -0.0093 139 SER   B CB  
6072 O OG  . SER   B 139 ? 0.1926 0.1351 0.2796 -0.0053 -0.0116 0.0086  139 SER   B OG  
6078 N N   . LEU   B 140 ? 0.1602 0.1132 0.2558 -0.0070 0.0166  -0.0080 140 LEU   B N   
6079 C CA  . LEU   B 140 ? 0.1584 0.1163 0.2693 0.0004  0.0154  -0.0056 140 LEU   B CA  
6080 C C   . LEU   B 140 ? 0.1543 0.1165 0.2842 -0.0086 0.0038  -0.0061 140 LEU   B C   
6081 O O   . LEU   B 140 ? 0.1536 0.1333 0.2771 -0.0065 -0.0016 -0.0000 140 LEU   B O   
6082 C CB  . LEU   B 140 ? 0.1589 0.1220 0.2707 -0.0063 0.0196  -0.0056 140 LEU   B CB  
6083 C CG  . LEU   B 140 ? 0.1673 0.1259 0.2694 -0.0113 0.0078  0.0046  140 LEU   B CG  
6084 C CD1 . LEU   B 140 ? 0.1806 0.1392 0.2857 -0.0161 0.0119  0.0038  140 LEU   B CD1 
6085 C CD2 . LEU   B 140 ? 0.1830 0.1396 0.2658 -0.0098 0.0052  -0.0123 140 LEU   B CD2 
6097 N N   . ARG   B 141 ? 0.1407 0.1247 0.2849 -0.0116 0.0073  -0.0056 141 ARG   B N   
6098 C CA  . ARG   B 141 ? 0.1461 0.1255 0.3240 -0.0201 0.0149  -0.0045 141 ARG   B CA  
6099 C C   . ARG   B 141 ? 0.1395 0.1276 0.3104 -0.0170 0.0107  -0.0027 141 ARG   B C   
6100 O O   . ARG   B 141 ? 0.1449 0.1330 0.3068 -0.0116 0.0051  -0.0152 141 ARG   B O   
6101 C CB  . ARG   B 141 ? 0.1610 0.1392 0.3466 -0.0211 0.0230  -0.0085 141 ARG   B CB  
6102 C CG  . ARG   B 141 ? 0.1915 0.1662 0.3698 -0.0203 0.0186  -0.0015 141 ARG   B CG  
6103 C CD  . ARG   B 141 ? 0.2282 0.1882 0.3758 -0.0184 0.0028  -0.0055 141 ARG   B CD  
6104 N NE  . ARG   B 141 ? 0.2485 0.1873 0.3688 -0.0315 0.0150  -0.0114 141 ARG   B NE  
6105 C CZ  . ARG   B 141 ? 0.2647 0.1805 0.3563 -0.0265 0.0301  -0.0225 141 ARG   B CZ  
6106 N NH1 . ARG   B 141 ? 0.2757 0.1730 0.3606 -0.0230 0.0255  -0.0226 141 ARG   B NH1 
6107 N NH2 . ARG   B 141 ? 0.2788 0.1986 0.3664 -0.0122 0.0223  -0.0179 141 ARG   B NH2 
6121 N N   . VAL   B 142 ? 0.1480 0.1228 0.2925 -0.0065 0.0152  -0.0080 142 VAL   B N   
6122 C CA  . VAL   B 142 ? 0.1483 0.1270 0.2841 -0.0055 0.0171  -0.0046 142 VAL   B CA  
6123 C C   . VAL   B 142 ? 0.1373 0.1231 0.2882 -0.0056 0.0077  -0.0110 142 VAL   B C   
6124 O O   . VAL   B 142 ? 0.1506 0.1204 0.2958 0.0024  0.0148  0.0003  142 VAL   B O   
6125 C CB  . VAL   B 142 ? 0.1595 0.1409 0.2765 -0.0050 0.0180  0.0046  142 VAL   B CB  
6126 C CG1 . VAL   B 142 ? 0.1576 0.1323 0.2730 0.0032  0.0237  0.0064  142 VAL   B CG1 
6127 C CG2 . VAL   B 142 ? 0.1865 0.1433 0.2759 -0.0020 0.0162  0.0054  142 VAL   B CG2 
6137 N N   . CYS   B 143 ? 0.1326 0.1192 0.2792 -0.0056 0.0039  -0.0046 143 CYS   B N   
6138 C CA  . CYS   B 143 ? 0.1295 0.1237 0.2808 -0.0130 0.0012  -0.0013 143 CYS   B CA  
6139 C C   . CYS   B 143 ? 0.1235 0.1300 0.2711 -0.0106 0.0099  -0.0077 143 CYS   B C   
6140 O O   . CYS   B 143 ? 0.1393 0.1288 0.2764 -0.0084 -0.0027 -0.0025 143 CYS   B O   
6141 C CB  . CYS   B 143 ? 0.1406 0.1361 0.2653 -0.0062 -0.0029 -0.0085 143 CYS   B CB  
6142 S SG  . CYS   B 143 ? 0.1473 0.1541 0.2608 -0.0043 0.0070  0.0016  143 CYS   B SG  
6148 N N   . VAL   B 144 ? 0.1446 0.1281 0.2759 -0.0089 -0.0016 -0.0167 144 VAL   B N   
6149 C CA  . VAL   B 144 ? 0.1514 0.1445 0.3011 -0.0164 -0.0149 -0.0206 144 VAL   B CA  
6150 C C   . VAL   B 144 ? 0.1474 0.1392 0.3072 -0.0085 -0.0106 -0.0000 144 VAL   B C   
6151 O O   . VAL   B 144 ? 0.1635 0.1641 0.3169 0.0025  -0.0184 0.0145  144 VAL   B O   
6152 C CB  . VAL   B 144 ? 0.1738 0.1551 0.3456 -0.0120 -0.0280 -0.0337 144 VAL   B CB  
6153 C CG1 . VAL   B 144 ? 0.1997 0.1984 0.3781 -0.0194 -0.0412 -0.0366 144 VAL   B CG1 
6154 C CG2 . VAL   B 144 ? 0.1931 0.1585 0.3404 0.0004  -0.0362 -0.0448 144 VAL   B CG2 
6164 N N   . ASP   B 145 ? 0.1399 0.1348 0.3231 -0.0146 -0.0063 -0.0157 145 ASP   B N   
6165 C CA  . ASP   B 145 ? 0.1427 0.1450 0.3416 -0.0104 0.0047  -0.0140 145 ASP   B CA  
6166 C C   . ASP   B 145 ? 0.1389 0.1496 0.3319 -0.0116 0.0003  -0.0169 145 ASP   B C   
6167 O O   . ASP   B 145 ? 0.1390 0.1633 0.3857 -0.0103 0.0029  -0.0307 145 ASP   B O   
6168 C CB  . ASP   B 145 ? 0.1609 0.1539 0.3856 -0.0140 0.0127  -0.0010 145 ASP   B CB  
6169 C CG  . ASP   B 145 ? 0.1802 0.1597 0.4392 -0.0183 0.0267  -0.0054 145 ASP   B CG  
6170 O OD1 . ASP   B 145 ? 0.1869 0.1620 0.4481 -0.0334 -0.0036 -0.0219 145 ASP   B OD1 
6171 O OD2 . ASP   B 145 ? 0.2080 0.1699 0.4862 -0.0277 0.0452  -0.0037 145 ASP   B OD2 
6176 N N   . THR   B 146 ? 0.1304 0.1342 0.2823 -0.0090 0.0011  -0.0048 146 THR   B N   
6177 C CA  . THR   B 146 ? 0.1461 0.1273 0.2673 -0.0091 0.0021  -0.0060 146 THR   B CA  
6178 C C   . THR   B 146 ? 0.1426 0.1281 0.2608 -0.0008 -0.0020 0.0022  146 THR   B C   
6179 O O   . THR   B 146 ? 0.1455 0.1310 0.2638 -0.0014 -0.0058 0.0061  146 THR   B O   
6180 C CB  . THR   B 146 ? 0.1491 0.1284 0.2623 -0.0061 0.0111  -0.0010 146 THR   B CB  
6181 O OG1 . THR   B 146 ? 0.1551 0.1328 0.2702 -0.0064 0.0110  0.0096  146 THR   B OG1 
6182 C CG2 . THR   B 146 ? 0.1584 0.1359 0.2636 -0.0093 0.0135  -0.0055 146 THR   B CG2 
6190 N N   . VAL   B 147 ? 0.1476 0.1258 0.2425 0.0019  0.0127  0.0033  147 VAL   B N   
6191 C CA  . VAL   B 147 ? 0.1480 0.1253 0.2303 -0.0126 -0.0069 -0.0045 147 VAL   B CA  
6192 C C   . VAL   B 147 ? 0.1410 0.1305 0.2495 -0.0178 -0.0152 -0.0078 147 VAL   B C   
6193 O O   . VAL   B 147 ? 0.1566 0.1406 0.2529 -0.0205 -0.0334 -0.0083 147 VAL   B O   
6194 C CB  . VAL   B 147 ? 0.1590 0.1358 0.2147 -0.0096 -0.0130 -0.0005 147 VAL   B CB  
6195 C CG1 . VAL   B 147 ? 0.1577 0.1582 0.2095 -0.0132 -0.0129 0.0109  147 VAL   B CG1 
6196 C CG2 . VAL   B 147 ? 0.1630 0.1366 0.2215 -0.0062 -0.0043 -0.0000 147 VAL   B CG2 
6206 N N   . ARG   B 148 ? 0.1437 0.1304 0.2496 -0.0092 -0.0241 -0.0104 148 ARG   B N   
6207 C CA  . ARG   B 148 ? 0.1481 0.1425 0.2392 -0.0040 -0.0255 -0.0138 148 ARG   B CA  
6208 C C   . ARG   B 148 ? 0.1551 0.1481 0.2247 -0.0057 -0.0231 -0.0062 148 ARG   B C   
6209 O O   . ARG   B 148 ? 0.1738 0.1817 0.2253 -0.0240 -0.0331 0.0022  148 ARG   B O   
6210 C CB  . ARG   B 148 ? 0.1542 0.1561 0.2494 -0.0087 -0.0298 -0.0228 148 ARG   B CB  
6211 C CG  . ARG   B 148 ? 0.1491 0.1713 0.2643 -0.0079 -0.0314 -0.0388 148 ARG   B CG  
6212 C CD  . ARG   B 148 ? 0.1580 0.1894 0.2694 0.0085  -0.0334 -0.0409 148 ARG   B CD  
6213 N NE  . ARG   B 148 ? 0.1663 0.1838 0.2587 0.0246  -0.0406 -0.0359 148 ARG   B NE  
6214 C CZ  . ARG   B 148 ? 0.1582 0.1746 0.2418 0.0184  -0.0333 -0.0250 148 ARG   B CZ  
6215 N NH1 . ARG   B 148 ? 0.1491 0.1749 0.2479 0.0092  -0.0075 -0.0142 148 ARG   B NH1 
6216 N NH2 . ARG   B 148 ? 0.1811 0.1637 0.2397 0.0142  -0.0212 -0.0153 148 ARG   B NH2 
6230 N N   . THR   B 149 ? 0.1569 0.1448 0.2234 -0.0098 -0.0238 -0.0017 149 THR   B N   
6231 C CA  . THR   B 149 ? 0.1609 0.1466 0.2164 -0.0117 -0.0263 -0.0003 149 THR   B CA  
6232 C C   . THR   B 149 ? 0.1580 0.1434 0.2109 -0.0201 -0.0299 0.0001  149 THR   B C   
6233 O O   . THR   B 149 ? 0.1667 0.1424 0.2208 -0.0180 -0.0119 0.0008  149 THR   B O   
6234 C CB  . THR   B 149 ? 0.1675 0.1476 0.2205 -0.0141 -0.0346 -0.0009 149 THR   B CB  
6235 O OG1 . THR   B 149 ? 0.1689 0.1538 0.2149 -0.0249 -0.0356 0.0007  149 THR   B OG1 
6236 C CG2 . THR   B 149 ? 0.1787 0.1544 0.2236 -0.0073 -0.0200 0.0070  149 THR   B CG2 
6244 N N   . ASN   B 150 ? 0.1615 0.1441 0.2038 -0.0169 -0.0335 -0.0002 150 ASN   B N   
6245 C CA  . ASN   B 150 ? 0.1757 0.1634 0.1923 -0.0177 -0.0261 -0.0053 150 ASN   B CA  
6246 C C   . ASN   B 150 ? 0.1607 0.1539 0.1915 -0.0129 -0.0295 -0.0047 150 ASN   B C   
6247 O O   . ASN   B 150 ? 0.1768 0.1560 0.2206 -0.0245 -0.0450 -0.0047 150 ASN   B O   
6248 C CB  . ASN   B 150 ? 0.1972 0.2035 0.2020 -0.0273 -0.0389 0.0077  150 ASN   B CB  
6249 C CG  . ASN   B 150 ? 0.2243 0.2452 0.2293 -0.0247 -0.0417 0.0239  150 ASN   B CG  
6250 O OD1 . ASN   B 150 ? 0.2309 0.2621 0.2526 -0.0312 -0.0596 0.0156  150 ASN   B OD1 
6251 N ND2 . ASN   B 150 ? 0.2387 0.2663 0.2714 -0.0150 -0.0419 0.0598  150 ASN   B ND2 
6258 N N   . VAL   B 151 ? 0.1574 0.1501 0.1941 -0.0196 -0.0304 -0.0033 151 VAL   B N   
6259 C CA  . VAL   B 151 ? 0.1577 0.1524 0.2011 -0.0258 -0.0299 -0.0016 151 VAL   B CA  
6260 C C   . VAL   B 151 ? 0.1618 0.1405 0.2053 -0.0309 -0.0288 -0.0016 151 VAL   B C   
6261 O O   . VAL   B 151 ? 0.1713 0.1514 0.2255 -0.0245 -0.0163 -0.0128 151 VAL   B O   
6262 C CB  . VAL   B 151 ? 0.1806 0.1644 0.2098 -0.0072 -0.0253 -0.0015 151 VAL   B CB  
6263 C CG1 . VAL   B 151 ? 0.1941 0.1698 0.2456 -0.0152 -0.0187 -0.0170 151 VAL   B CG1 
6264 C CG2 . VAL   B 151 ? 0.1913 0.1807 0.1989 0.0008  -0.0217 0.0058  151 VAL   B CG2 
6274 N N   . TYR   B 152 ? 0.1555 0.1287 0.2016 -0.0212 -0.0231 -0.0030 152 TYR   B N   
6275 C CA  . TYR   B 152 ? 0.1595 0.1479 0.1880 -0.0270 -0.0067 -0.0082 152 TYR   B CA  
6276 C C   . TYR   B 152 ? 0.1534 0.1350 0.1795 -0.0225 -0.0035 -0.0086 152 TYR   B C   
6277 O O   . TYR   B 152 ? 0.1587 0.1379 0.1920 -0.0283 -0.0117 -0.0023 152 TYR   B O   
6278 C CB  . TYR   B 152 ? 0.1792 0.1647 0.1843 -0.0290 -0.0180 0.0015  152 TYR   B CB  
6279 C CG  . TYR   B 152 ? 0.1982 0.1708 0.1811 -0.0439 -0.0219 -0.0026 152 TYR   B CG  
6280 C CD1 . TYR   B 152 ? 0.2132 0.1846 0.1702 -0.0312 -0.0274 0.0109  152 TYR   B CD1 
6281 C CD2 . TYR   B 152 ? 0.2230 0.1947 0.1882 -0.0409 -0.0139 -0.0082 152 TYR   B CD2 
6282 C CE1 . TYR   B 152 ? 0.2327 0.2061 0.1830 -0.0267 -0.0309 0.0207  152 TYR   B CE1 
6283 C CE2 . TYR   B 152 ? 0.2321 0.2172 0.1878 -0.0387 -0.0184 -0.0168 152 TYR   B CE2 
6284 C CZ  . TYR   B 152 ? 0.2416 0.2320 0.1775 -0.0305 -0.0424 0.0056  152 TYR   B CZ  
6285 O OH  . TYR   B 152 ? 0.2642 0.2736 0.2068 -0.0185 -0.0403 0.0068  152 TYR   B OH  
6295 N N   . LEU   B 153 ? 0.1517 0.1327 0.1898 -0.0209 -0.0169 -0.0057 153 LEU   B N   
6296 C CA  . LEU   B 153 ? 0.1588 0.1316 0.1783 -0.0231 -0.0056 -0.0152 153 LEU   B CA  
6297 C C   . LEU   B 153 ? 0.1637 0.1266 0.1959 -0.0261 -0.0019 -0.0228 153 LEU   B C   
6298 O O   . LEU   B 153 ? 0.1728 0.1548 0.2122 -0.0190 -0.0086 -0.0410 153 LEU   B O   
6299 C CB  . LEU   B 153 ? 0.1608 0.1298 0.1948 -0.0250 -0.0048 -0.0064 153 LEU   B CB  
6300 C CG  . LEU   B 153 ? 0.1527 0.1440 0.2204 -0.0239 -0.0028 -0.0048 153 LEU   B CG  
6301 C CD1 . LEU   B 153 ? 0.1635 0.1612 0.2221 -0.0263 0.0096  0.0050  153 LEU   B CD1 
6302 C CD2 . LEU   B 153 ? 0.1617 0.1613 0.2218 -0.0260 0.0074  -0.0033 153 LEU   B CD2 
6314 N N   . ALA   B 154 ? 0.1529 0.1322 0.1941 -0.0072 -0.0140 -0.0207 154 ALA   B N   
6315 C CA  . ALA   B 154 ? 0.1694 0.1421 0.2171 -0.0021 -0.0171 -0.0238 154 ALA   B CA  
6316 C C   . ALA   B 154 ? 0.1862 0.1437 0.2307 0.0064  -0.0339 -0.0300 154 ALA   B C   
6317 O O   . ALA   B 154 ? 0.2260 0.1510 0.2511 0.0135  -0.0179 -0.0148 154 ALA   B O   
6318 C CB  . ALA   B 154 ? 0.1680 0.1615 0.2460 -0.0023 -0.0103 -0.0210 154 ALA   B CB  
6324 N N   . VAL   B 155 ? 0.1518 0.1295 0.2439 -0.0021 -0.0081 -0.0206 155 VAL   B N   
6325 C CA  . VAL   B 155 ? 0.1452 0.1346 0.2612 -0.0026 -0.0108 -0.0181 155 VAL   B CA  
6326 C C   . VAL   B 155 ? 0.1472 0.1405 0.2588 -0.0059 -0.0116 -0.0259 155 VAL   B C   
6327 O O   . VAL   B 155 ? 0.1705 0.1595 0.2737 0.0048  -0.0105 -0.0340 155 VAL   B O   
6328 C CB  . VAL   B 155 ? 0.1509 0.1513 0.2895 -0.0024 -0.0166 -0.0010 155 VAL   B CB  
6329 C CG1 . VAL   B 155 ? 0.1571 0.1558 0.2943 -0.0123 -0.0068 -0.0054 155 VAL   B CG1 
6330 C CG2 . VAL   B 155 ? 0.1494 0.1626 0.3251 -0.0055 -0.0166 0.0335  155 VAL   B CG2 
6340 N N   . PHE   B 156 ? 0.1361 0.1488 0.2763 0.0035  -0.0066 -0.0188 156 PHE   B N   
6341 C CA  . PHE   B 156 ? 0.1379 0.1631 0.3155 0.0040  -0.0054 -0.0232 156 PHE   B CA  
6342 C C   . PHE   B 156 ? 0.1404 0.1726 0.3422 0.0092  -0.0035 -0.0392 156 PHE   B C   
6343 O O   . PHE   B 156 ? 0.1689 0.1911 0.3701 0.0210  0.0100  -0.0472 156 PHE   B O   
6344 C CB  . PHE   B 156 ? 0.1506 0.1602 0.3163 -0.0059 -0.0144 -0.0089 156 PHE   B CB  
6345 C CG  . PHE   B 156 ? 0.1501 0.1660 0.3189 -0.0028 -0.0157 0.0039  156 PHE   B CG  
6346 C CD1 . PHE   B 156 ? 0.1532 0.1930 0.3562 0.0055  -0.0038 0.0361  156 PHE   B CD1 
6347 C CD2 . PHE   B 156 ? 0.1580 0.1792 0.3165 0.0034  -0.0230 -0.0011 156 PHE   B CD2 
6348 C CE1 . PHE   B 156 ? 0.1536 0.2127 0.3648 0.0072  -0.0108 0.0332  156 PHE   B CE1 
6349 C CE2 . PHE   B 156 ? 0.1629 0.2057 0.3353 0.0121  -0.0132 0.0048  156 PHE   B CE2 
6350 C CZ  . PHE   B 156 ? 0.1487 0.2126 0.3590 0.0173  -0.0214 0.0150  156 PHE   B CZ  
6360 N N   . ASP   B 157 ? 0.1406 0.1536 0.3527 0.0095  -0.0202 -0.0268 157 ASP   B N   
6361 C CA  . ASP   B 157 ? 0.1535 0.1602 0.3770 0.0071  -0.0226 -0.0346 157 ASP   B CA  
6362 C C   . ASP   B 157 ? 0.1575 0.1517 0.3805 0.0117  -0.0197 -0.0500 157 ASP   B C   
6363 O O   . ASP   B 157 ? 0.1477 0.1561 0.3670 0.0083  -0.0208 -0.0398 157 ASP   B O   
6364 C CB  . ASP   B 157 ? 0.1829 0.1837 0.3875 0.0059  -0.0468 -0.0181 157 ASP   B CB  
6365 C CG  . ASP   B 157 ? 0.2317 0.2040 0.4124 0.0030  -0.0283 -0.0170 157 ASP   B CG  
6366 O OD1 . ASP   B 157 ? 0.2437 0.1996 0.4309 0.0118  -0.0157 -0.0099 157 ASP   B OD1 
6367 O OD2 . ASP   B 157 ? 0.2762 0.2298 0.4454 -0.0012 -0.0099 -0.0174 157 ASP   B OD2 
6372 N N   . LYS   B 158 ? 0.1634 0.1796 0.3948 0.0113  -0.0013 -0.0704 158 LYS   B N   
6373 C CA  . LYS   B 158 ? 0.1827 0.2019 0.4037 0.0060  0.0030  -0.0902 158 LYS   B CA  
6374 C C   . LYS   B 158 ? 0.1807 0.1775 0.4072 0.0090  -0.0091 -0.0823 158 LYS   B C   
6375 O O   . LYS   B 158 ? 0.1877 0.1774 0.4221 0.0034  -0.0100 -0.0919 158 LYS   B O   
6376 C CB  . LYS   B 158 ? 0.2134 0.2589 0.4059 0.0060  0.0115  -0.1207 158 LYS   B CB  
6377 C CG  . LYS   B 158 ? 0.2613 0.3127 0.4201 0.0181  0.0159  -0.1327 158 LYS   B CG  
6378 C CD  . LYS   B 158 ? 0.2908 0.3627 0.4379 0.0187  0.0189  -0.1301 158 LYS   B CD  
6379 C CE  . LYS   B 158 ? 0.3121 0.4027 0.4554 0.0231  0.0197  -0.1254 158 LYS   B CE  
6380 N NZ  . LYS   B 158 ? 0.3222 0.4283 0.4615 0.0238  0.0209  -0.1201 158 LYS   B NZ  
6394 N N   . ASN   B 159 ? 0.1814 0.1698 0.4237 0.0105  -0.0141 -0.0667 159 ASN   B N   
6395 C CA  . ASN   B 159 ? 0.2022 0.1594 0.4376 0.0179  -0.0269 -0.0529 159 ASN   B CA  
6396 C C   . ASN   B 159 ? 0.1823 0.1468 0.4322 0.0106  -0.0400 -0.0458 159 ASN   B C   
6397 O O   . ASN   B 159 ? 0.1816 0.1515 0.4447 -0.0022 -0.0499 -0.0384 159 ASN   B O   
6398 C CB  . ASN   B 159 ? 0.2279 0.1774 0.4645 0.0274  -0.0299 -0.0419 159 ASN   B CB  
6399 C CG  . ASN   B 159 ? 0.2549 0.2098 0.4876 0.0317  -0.0412 -0.0465 159 ASN   B CG  
6400 O OD1 . ASN   B 159 ? 0.2695 0.2142 0.4916 0.0376  -0.0426 -0.0624 159 ASN   B OD1 
6401 N ND2 . ASN   B 159 ? 0.2558 0.2232 0.5043 0.0356  -0.0480 -0.0384 159 ASN   B ND2 
6408 N N   . LEU   B 160 ? 0.1700 0.1505 0.4125 0.0042  -0.0277 -0.0399 160 LEU   B N   
6409 C CA  . LEU   B 160 ? 0.1655 0.1558 0.3696 0.0026  -0.0254 -0.0256 160 LEU   B CA  
6410 C C   . LEU   B 160 ? 0.1598 0.1463 0.3601 -0.0011 -0.0215 -0.0316 160 LEU   B C   
6411 O O   . LEU   B 160 ? 0.1434 0.1564 0.3444 -0.0027 -0.0238 -0.0274 160 LEU   B O   
6412 C CB  . LEU   B 160 ? 0.1648 0.1657 0.3423 0.0044  -0.0339 -0.0178 160 LEU   B CB  
6413 C CG  . LEU   B 160 ? 0.1616 0.1799 0.3119 0.0075  -0.0287 -0.0081 160 LEU   B CG  
6414 C CD1 . LEU   B 160 ? 0.1796 0.1951 0.3098 -0.0004 -0.0218 -0.0052 160 LEU   B CD1 
6415 C CD2 . LEU   B 160 ? 0.1642 0.1877 0.3127 0.0180  -0.0269 -0.0254 160 LEU   B CD2 
6427 N N   . TYR   B 161 ? 0.1575 0.1492 0.3616 -0.0067 0.0016  -0.0415 161 TYR   B N   
6428 C CA  . TYR   B 161 ? 0.1637 0.1502 0.3492 -0.0145 0.0200  -0.0463 161 TYR   B CA  
6429 C C   . TYR   B 161 ? 0.1713 0.1493 0.3310 -0.0122 0.0180  -0.0433 161 TYR   B C   
6430 O O   . TYR   B 161 ? 0.1738 0.1516 0.3161 -0.0207 0.0031  -0.0403 161 TYR   B O   
6431 C CB  . TYR   B 161 ? 0.1799 0.1598 0.3461 -0.0265 0.0375  -0.0528 161 TYR   B CB  
6432 C CG  . TYR   B 161 ? 0.2046 0.1709 0.3351 -0.0337 0.0473  -0.0587 161 TYR   B CG  
6433 C CD1 . TYR   B 161 ? 0.2122 0.1677 0.3212 -0.0449 0.0492  -0.0612 161 TYR   B CD1 
6434 C CD2 . TYR   B 161 ? 0.2341 0.1815 0.3296 -0.0327 0.0350  -0.0584 161 TYR   B CD2 
6435 C CE1 . TYR   B 161 ? 0.2296 0.1922 0.3250 -0.0471 0.0469  -0.0606 161 TYR   B CE1 
6436 C CE2 . TYR   B 161 ? 0.2545 0.2004 0.3287 -0.0364 0.0326  -0.0569 161 TYR   B CE2 
6437 C CZ  . TYR   B 161 ? 0.2486 0.2027 0.3278 -0.0541 0.0333  -0.0473 161 TYR   B CZ  
6438 O OH  . TYR   B 161 ? 0.2840 0.2313 0.3486 -0.0532 0.0287  -0.0435 161 TYR   B OH  
6448 N N   . ASP   B 162 ? 0.1755 0.1470 0.3484 -0.0133 -0.0068 -0.0522 162 ASP   B N   
6449 C CA  . ASP   B 162 ? 0.1878 0.1566 0.3557 -0.0151 -0.0099 -0.0522 162 ASP   B CA  
6450 C C   . ASP   B 162 ? 0.1837 0.1499 0.3369 -0.0175 -0.0144 -0.0436 162 ASP   B C   
6451 O O   . ASP   B 162 ? 0.1853 0.1599 0.3449 -0.0236 -0.0289 -0.0415 162 ASP   B O   
6452 C CB  . ASP   B 162 ? 0.2069 0.1724 0.3802 -0.0037 -0.0060 -0.0652 162 ASP   B CB  
6453 C CG  . ASP   B 162 ? 0.2146 0.1962 0.3998 0.0064  -0.0060 -0.0803 162 ASP   B CG  
6454 O OD1 . ASP   B 162 ? 0.2117 0.2244 0.3951 0.0011  0.0055  -0.0797 162 ASP   B OD1 
6455 O OD2 . ASP   B 162 ? 0.2408 0.2203 0.4332 0.0264  0.0002  -0.0835 162 ASP   B OD2 
6460 N N   A LYS   B 163 ? 0.1779 0.1325 0.3267 -0.0131 -0.0212 -0.0329 163 LYS   B N   
6461 N N   B LYS   B 163 ? 0.1991 0.1706 0.3264 -0.0167 -0.0161 -0.0311 163 LYS   B N   
6462 C CA  A LYS   B 163 ? 0.1942 0.1425 0.3267 -0.0197 -0.0124 -0.0130 163 LYS   B CA  
6463 C CA  B LYS   B 163 ? 0.2152 0.1923 0.3275 -0.0164 -0.0137 -0.0179 163 LYS   B CA  
6464 C C   A LYS   B 163 ? 0.1633 0.1376 0.3231 -0.0199 -0.0192 -0.0067 163 LYS   B C   
6465 C C   B LYS   B 163 ? 0.1850 0.1648 0.3059 -0.0169 -0.0161 -0.0115 163 LYS   B C   
6466 O O   A LYS   B 163 ? 0.1590 0.1522 0.3543 -0.0278 -0.0205 -0.0080 163 LYS   B O   
6467 O O   B LYS   B 163 ? 0.1859 0.1666 0.3013 -0.0174 -0.0170 -0.0097 163 LYS   B O   
6468 C CB  A LYS   B 163 ? 0.2470 0.1706 0.3647 -0.0146 -0.0121 0.0070  163 LYS   B CB  
6469 C CB  B LYS   B 163 ? 0.2572 0.2395 0.3662 -0.0153 -0.0119 -0.0121 163 LYS   B CB  
6470 C CG  A LYS   B 163 ? 0.3317 0.2456 0.4176 -0.0198 0.0044  0.0136  163 LYS   B CG  
6471 C CG  B LYS   B 163 ? 0.2979 0.2857 0.4098 -0.0149 -0.0083 -0.0081 163 LYS   B CG  
6472 C CD  A LYS   B 163 ? 0.4021 0.3066 0.4768 -0.0331 0.0052  0.0108  163 LYS   B CD  
6473 C CD  B LYS   B 163 ? 0.3403 0.3318 0.4533 -0.0161 -0.0068 -0.0055 163 LYS   B CD  
6474 C CE  A LYS   B 163 ? 0.4512 0.3487 0.5155 -0.0424 0.0076  0.0154  163 LYS   B CE  
6475 C CE  B LYS   B 163 ? 0.3694 0.3621 0.4864 -0.0171 -0.0051 -0.0029 163 LYS   B CE  
6476 N NZ  A LYS   B 163 ? 0.4937 0.3754 0.5418 -0.0472 0.0098  0.0143  163 LYS   B NZ  
6477 N NZ  B LYS   B 163 ? 0.3730 0.3655 0.5062 -0.0176 -0.0040 -0.0024 163 LYS   B NZ  
6504 N N   . LEU   B 164 ? 0.1548 0.1354 0.2991 -0.0183 -0.0183 -0.0084 164 LEU   B N   
6505 C CA  . LEU   B 164 ? 0.1564 0.1364 0.2897 -0.0079 -0.0195 -0.0093 164 LEU   B CA  
6506 C C   . LEU   B 164 ? 0.1627 0.1436 0.2964 -0.0154 -0.0302 0.0015  164 LEU   B C   
6507 O O   . LEU   B 164 ? 0.1578 0.1661 0.3133 -0.0187 -0.0295 -0.0019 164 LEU   B O   
6508 C CB  . LEU   B 164 ? 0.1533 0.1390 0.2742 -0.0096 -0.0177 -0.0048 164 LEU   B CB  
6509 C CG  . LEU   B 164 ? 0.1598 0.1521 0.2831 -0.0050 -0.0137 -0.0040 164 LEU   B CG  
6510 C CD1 . LEU   B 164 ? 0.1633 0.1500 0.2794 -0.0143 -0.0191 -0.0061 164 LEU   B CD1 
6511 C CD2 . LEU   B 164 ? 0.1702 0.1893 0.2966 0.0013  -0.0026 -0.0216 164 LEU   B CD2 
6524 N N   . VAL   B 165 ? 0.1962 0.1496 0.3131 -0.0239 -0.0289 -0.0101 165 VAL   B N   
6525 C CA  . VAL   B 165 ? 0.2323 0.1602 0.3089 -0.0331 -0.0436 -0.0079 165 VAL   B CA  
6526 C C   . VAL   B 165 ? 0.2529 0.1717 0.3356 -0.0412 -0.0710 -0.0130 165 VAL   B C   
6527 O O   . VAL   B 165 ? 0.2716 0.1866 0.3410 -0.0462 -0.0688 -0.0091 165 VAL   B O   
6528 C CB  . VAL   B 165 ? 0.2563 0.1823 0.2904 -0.0239 -0.0220 -0.0232 165 VAL   B CB  
6529 C CG1 . VAL   B 165 ? 0.2712 0.1934 0.3101 -0.0246 -0.0088 -0.0101 165 VAL   B CG1 
6530 C CG2 . VAL   B 165 ? 0.2558 0.1935 0.2856 -0.0275 -0.0133 -0.0209 165 VAL   B CG2 
6540 N N   . SER   B 166 ? 0.2577 0.1595 0.3742 -0.0392 -0.0855 -0.0308 166 SER   B N   
6541 C CA  . SER   B 166 ? 0.2520 0.1686 0.4261 -0.0426 -0.0754 -0.0335 166 SER   B CA  
6542 C C   . SER   B 166 ? 0.2361 0.1769 0.4454 -0.0494 -0.0742 -0.0047 166 SER   B C   
6543 O O   . SER   B 166 ? 0.2451 0.2026 0.4751 -0.0591 -0.0967 -0.0217 166 SER   B O   
6544 C CB  . SER   B 166 ? 0.2507 0.1738 0.4543 -0.0349 -0.0749 -0.0467 166 SER   B CB  
6545 O OG  . SER   B 166 ? 0.2451 0.1684 0.4714 -0.0213 -0.0765 -0.0267 166 SER   B OG  
6551 N N   . SER   B 167 ? 0.2120 0.1659 0.4173 -0.0452 -0.0747 0.0290  167 SER   B N   
6552 C CA  . SER   B 167 ? 0.2113 0.1711 0.4052 -0.0375 -0.0514 0.0349  167 SER   B CA  
6553 C C   . SER   B 167 ? 0.2047 0.1787 0.3794 -0.0455 -0.0499 0.0504  167 SER   B C   
6554 O O   . SER   B 167 ? 0.2097 0.1945 0.3656 -0.0519 -0.0391 0.0448  167 SER   B O   
6555 C CB  . SER   B 167 ? 0.1998 0.1791 0.4161 -0.0319 -0.0310 0.0263  167 SER   B CB  
6556 O OG  . SER   B 167 ? 0.1872 0.1853 0.4127 -0.0205 -0.0211 0.0240  167 SER   B OG  
6562 N N   . PHE   B 168 ? 0.2046 0.1723 0.3712 -0.0438 -0.0354 0.0559  168 PHE   B N   
6563 C CA  . PHE   B 168 ? 0.2110 0.1775 0.3493 -0.0466 -0.0296 0.0390  168 PHE   B CA  
6564 C C   . PHE   B 168 ? 0.1843 0.1657 0.3078 -0.0260 -0.0154 0.0198  168 PHE   B C   
6565 O O   . PHE   B 168 ? 0.2099 0.1596 0.3082 -0.0021 -0.0144 0.0049  168 PHE   B O   
6566 C CB  . PHE   B 168 ? 0.2247 0.1856 0.3469 -0.0588 -0.0464 0.0492  168 PHE   B CB  
6567 C CG  . PHE   B 168 ? 0.2528 0.1731 0.3380 -0.0665 -0.0532 0.0246  168 PHE   B CG  
6568 C CD1 . PHE   B 168 ? 0.2849 0.1754 0.3449 -0.0611 -0.0593 0.0215  168 PHE   B CD1 
6569 C CD2 . PHE   B 168 ? 0.2441 0.1676 0.3333 -0.0629 -0.0531 0.0304  168 PHE   B CD2 
6570 C CE1 . PHE   B 168 ? 0.2958 0.1831 0.3270 -0.0457 -0.0555 0.0184  168 PHE   B CE1 
6571 C CE2 . PHE   B 168 ? 0.2701 0.1766 0.3374 -0.0469 -0.0594 0.0185  168 PHE   B CE2 
6572 C CZ  . PHE   B 168 ? 0.2842 0.1702 0.3294 -0.0362 -0.0660 0.0218  168 PHE   B CZ  
6582 N N   . LEU   B 169 ? 0.1950 0.1863 0.3187 -0.0002 -0.0055 0.0033  169 LEU   B N   
6583 C CA  . LEU   B 169 ? 0.2257 0.2169 0.3466 -0.0015 -0.0067 -0.0234 169 LEU   B CA  
6584 C C   . LEU   B 169 ? 0.2549 0.2375 0.4007 0.0119  -0.0163 -0.0471 169 LEU   B C   
6585 O O   . LEU   B 169 ? 0.2812 0.2623 0.4510 0.0115  -0.0115 -0.0708 169 LEU   B O   
6586 C CB  . LEU   B 169 ? 0.2531 0.2544 0.3497 -0.0100 -0.0085 0.0003  169 LEU   B CB  
6587 C CG  . LEU   B 169 ? 0.2935 0.2899 0.3804 -0.0057 -0.0067 0.0078  169 LEU   B CG  
6588 C CD1 . LEU   B 169 ? 0.3087 0.3076 0.3846 -0.0050 -0.0098 0.0211  169 LEU   B CD1 
6589 C CD2 . LEU   B 169 ? 0.2937 0.2986 0.3805 0.0054  0.0049  0.0017  169 LEU   B CD2 
6590 O OXT . LEU   B 169 ? 0.2760 0.2453 0.3976 0.0336  -0.0152 -0.0500 169 LEU   B OXT 
6602 N N2  B A1A5Y C .   ? 0.2657 0.2340 0.2419 -0.0204 0.0160  0.0038  201 A1A5Y A N2  
6603 C C3  B A1A5Y C .   ? 0.2626 0.2285 0.2311 -0.0200 0.0111  -0.0025 201 A1A5Y A C3  
6604 C C6  B A1A5Y C .   ? 0.2601 0.2328 0.2294 -0.0107 0.0141  0.0044  201 A1A5Y A C6  
6605 C C9  B A1A5Y C .   ? 0.2215 0.2101 0.2103 0.0141  -0.0061 0.0025  201 A1A5Y A C9  
6606 C C12 B A1A5Y C .   ? 0.2294 0.2160 0.2110 0.0213  0.0127  -0.0028 201 A1A5Y A C12 
6607 C C14 B A1A5Y C .   ? 0.2257 0.2193 0.1984 0.0252  0.0184  -0.0066 201 A1A5Y A C14 
6608 C C17 B A1A5Y C .   ? 0.2302 0.2237 0.2000 0.0217  0.0166  -0.0037 201 A1A5Y A C17 
6609 C C19 B A1A5Y C .   ? 0.2663 0.2345 0.2358 -0.0161 0.0112  0.0087  201 A1A5Y A C19 
6610 C C1  B A1A5Y C .   ? 0.2666 0.2342 0.2441 -0.0212 0.0161  0.0011  201 A1A5Y A C1  
6611 C C10 B A1A5Y C .   ? 0.2132 0.2087 0.2176 0.0138  -0.0287 -0.0011 201 A1A5Y A C10 
6612 C C11 B A1A5Y C .   ? 0.2256 0.2135 0.2075 0.0175  0.0054  0.0005  201 A1A5Y A C11 
6613 C C13 B A1A5Y C .   ? 0.2306 0.2187 0.2042 0.0216  0.0149  -0.0026 201 A1A5Y A C13 
6614 C C15 B A1A5Y C .   ? 0.2261 0.2220 0.1952 0.0244  0.0189  -0.0043 201 A1A5Y A C15 
6615 C C16 B A1A5Y C .   ? 0.2286 0.2244 0.1976 0.0231  0.0196  -0.0055 201 A1A5Y A C16 
6616 C C18 B A1A5Y C .   ? 0.2671 0.2355 0.2363 -0.0145 0.0105  0.0111  201 A1A5Y A C18 
6617 C C2  B A1A5Y C .   ? 0.2654 0.2303 0.2390 -0.0210 0.0153  -0.0021 201 A1A5Y A C2  
6618 C C20 B A1A5Y C .   ? 0.2666 0.2333 0.2379 -0.0176 0.0128  0.0037  201 A1A5Y A C20 
6619 C C4  B A1A5Y C .   ? 0.2655 0.2317 0.2354 -0.0148 0.0105  -0.0016 201 A1A5Y A C4  
6620 C C5  B A1A5Y C .   ? 0.2641 0.2345 0.2339 -0.0135 0.0136  -0.0012 201 A1A5Y A C5  
6621 C C7  B A1A5Y C .   ? 0.2479 0.2227 0.2170 -0.0056 0.0190  0.0069  201 A1A5Y A C7  
6622 C C8  B A1A5Y C .   ? 0.2283 0.2125 0.2120 0.0111  0.0074  0.0001  201 A1A5Y A C8  
6623 F F1  B A1A5Y C .   ? 0.2735 0.2388 0.2469 -0.0160 0.0079  0.0136  201 A1A5Y A F1  
6624 N N1  B A1A5Y C .   ? 0.2339 0.2145 0.2095 0.0088  0.0140  0.0030  201 A1A5Y A N1  
6625 O O1  B A1A5Y C .   ? 0.2696 0.2391 0.2524 -0.0208 0.0155  0.0025  201 A1A5Y A O1  
6626 O O2  B A1A5Y C .   ? 0.2471 0.2234 0.2169 -0.0156 0.0256  0.0120  201 A1A5Y A O2  
6627 O O3  B A1A5Y C .   ? 0.2114 0.2094 0.2225 0.0112  -0.0389 -0.0032 201 A1A5Y A O3  
6628 O O4  B A1A5Y C .   ? 0.2078 0.2051 0.2206 0.0191  -0.0447 -0.0024 201 A1A5Y A O4  
6651 O O   . HOH   D .   ? 0.3448 0.2509 0.3757 -0.0247 -0.0173 0.0400  301 HOH   A O   
6652 O O   . HOH   D .   ? 0.4215 0.6964 0.5047 -0.1144 0.0676  0.0108  302 HOH   A O   
6653 O O   . HOH   D .   ? 0.5523 0.6051 0.4786 -0.0853 -0.1258 -0.0820 303 HOH   A O   
6654 O O   . HOH   D .   ? 0.2389 0.1941 0.2695 0.0255  -0.0444 -0.0120 304 HOH   A O   
6655 O O   . HOH   D .   ? 0.2081 0.2342 0.2698 -0.0035 -0.0069 0.0741  305 HOH   A O   
6656 O O   . HOH   D .   ? 0.5372 0.4285 0.4998 -0.0775 0.1335  0.1546  306 HOH   A O   
6657 O O   . HOH   D .   ? 0.4562 0.4694 0.3542 0.1420  -0.0795 -0.1611 307 HOH   A O   
6658 O O   . HOH   D .   ? 0.7593 0.4406 0.3827 0.1945  -0.1537 0.0338  308 HOH   A O   
6659 O O   . HOH   D .   ? 0.4057 0.3714 0.5350 0.0177  0.1185  -0.0605 309 HOH   A O   
6660 O O   . HOH   D .   ? 0.2150 0.1853 0.3034 -0.0063 -0.0445 -0.0075 310 HOH   A O   
6661 O O   . HOH   D .   ? 0.2753 0.4956 0.5808 -0.0346 0.0927  0.2390  311 HOH   A O   
6662 O O   . HOH   D .   ? 0.1841 0.2220 0.2094 -0.0130 -0.0019 0.0559  312 HOH   A O   
6663 O O   . HOH   D .   ? 0.2540 0.2626 0.3341 -0.0113 0.0495  0.0811  313 HOH   A O   
6664 O O   . HOH   D .   ? 0.1802 0.2824 0.2840 0.0515  0.0429  0.0993  314 HOH   A O   
6665 O O   . HOH   D .   ? 0.2134 0.2252 0.3140 0.0009  -0.0306 0.0440  315 HOH   A O   
6666 O O   . HOH   D .   ? 0.2235 0.2031 0.3792 -0.0493 0.0130  -0.0304 316 HOH   A O   
6667 O O   . HOH   D .   ? 0.1896 0.5224 0.3562 0.0843  -0.0016 0.0797  317 HOH   A O   
6668 O O   . HOH   D .   ? 0.2835 0.2202 0.2817 -0.0295 0.0079  -0.0187 318 HOH   A O   
6669 O O   . HOH   D .   ? 0.1542 0.3484 0.3103 -0.0112 0.0244  0.0679  319 HOH   A O   
6670 O O   . HOH   D .   ? 0.6942 0.5699 0.3594 -0.0275 -0.0483 0.1001  320 HOH   A O   
6671 O O   . HOH   D .   ? 0.2474 0.3179 0.3073 0.0002  -0.0057 -0.0620 321 HOH   A O   
6672 O O   . HOH   D .   ? 0.5438 0.2252 0.5487 0.0690  -0.0387 -0.0180 322 HOH   A O   
6673 O O   . HOH   D .   ? 0.3120 0.3710 0.1768 -0.0554 0.0274  0.0353  323 HOH   A O   
6674 O O   . HOH   D .   ? 0.3918 0.4684 0.2680 -0.0549 0.0632  0.0345  324 HOH   A O   
6675 O O   . HOH   D .   ? 0.3728 0.2976 0.3292 -0.1174 0.0329  0.0424  325 HOH   A O   
6676 O O   . HOH   D .   ? 0.5185 0.6013 0.3436 -0.1101 0.1760  0.0684  326 HOH   A O   
6677 O O   A HOH   D .   ? 0.3742 0.3734 0.2805 -0.0535 -0.0783 -0.0117 327 HOH   A O   
6678 O O   . HOH   D .   ? 0.3960 0.3408 0.3764 -0.0263 0.1595  0.0215  328 HOH   A O   
6679 O O   . HOH   D .   ? 0.1970 0.3576 0.4844 -0.0351 0.0365  -0.1167 329 HOH   A O   
6680 O O   . HOH   D .   ? 0.1705 0.1657 0.2613 -0.0214 0.0118  -0.0043 330 HOH   A O   
6681 O O   . HOH   D .   ? 0.5616 0.4437 0.3374 0.0299  0.0463  0.1651  331 HOH   A O   
6682 O O   . HOH   D .   ? 0.6198 0.4498 0.5446 -0.0302 -0.0731 0.0458  332 HOH   A O   
6683 O O   . HOH   D .   ? 0.2375 0.2319 0.2845 0.0296  0.0337  0.0343  333 HOH   A O   
6684 O O   . HOH   D .   ? 0.5289 0.5402 0.4751 -0.1932 -0.0482 0.2569  334 HOH   A O   
6685 O O   . HOH   D .   ? 0.6324 0.5459 0.4841 -0.1199 0.1446  0.1882  335 HOH   A O   
6686 O O   . HOH   D .   ? 0.2765 0.4235 0.4432 -0.0100 -0.0848 0.1383  336 HOH   A O   
6687 O O   . HOH   D .   ? 0.3378 0.5097 0.4086 0.0173  -0.0832 0.0082  337 HOH   A O   
6688 O O   . HOH   D .   ? 0.6002 0.5559 0.4838 -0.1308 -0.1417 -0.0418 338 HOH   A O   
6689 O O   A HOH   D .   ? 0.3152 0.1725 0.2250 0.0339  0.0165  0.0145  339 HOH   A O   
6690 O O   . HOH   D .   ? 0.7905 0.3997 0.6098 -0.0078 -0.1375 -0.0500 340 HOH   A O   
6691 O O   A HOH   D .   ? 0.2820 0.2506 0.4059 -0.0211 -0.1078 0.0839  341 HOH   A O   
6692 O O   . HOH   D .   ? 0.3733 0.2476 0.4675 -0.0477 0.1245  0.0159  342 HOH   A O   
6693 O O   . HOH   D .   ? 0.7164 0.6232 0.3771 -0.1402 -0.0326 0.1956  343 HOH   A O   
6694 O O   . HOH   D .   ? 0.5611 0.5358 0.5181 0.0793  0.2530  -0.0991 344 HOH   A O   
6695 O O   . HOH   D .   ? 0.1798 0.1789 0.2644 -0.0189 0.0145  0.0369  345 HOH   A O   
6696 O O   . HOH   D .   ? 0.1998 0.2283 0.3717 0.0194  0.0732  -0.0179 346 HOH   A O   
6697 O O   . HOH   D .   ? 0.2518 0.4980 0.4251 0.0329  -0.0454 0.0810  347 HOH   A O   
6698 O O   . HOH   D .   ? 0.2545 0.4340 0.3656 -0.0367 0.0431  -0.0013 348 HOH   A O   
6699 O O   . HOH   D .   ? 0.3231 0.5059 0.2537 -0.1380 -0.0253 -0.0519 349 HOH   A O   
6700 O O   . HOH   D .   ? 0.1826 0.2818 0.3504 -0.0159 0.0549  0.0529  350 HOH   A O   
6701 O O   . HOH   D .   ? 0.1562 0.2563 0.2609 0.0067  -0.0075 0.0630  351 HOH   A O   
6702 O O   . HOH   D .   ? 0.1575 0.1787 0.3013 0.0083  -0.0304 -0.0453 352 HOH   A O   
6703 O O   . HOH   D .   ? 0.1431 0.1306 0.1660 -0.0010 0.0119  0.0090  353 HOH   A O   
6704 O O   . HOH   D .   ? 0.3882 0.2383 0.2538 0.1069  0.0314  0.0033  354 HOH   A O   
6705 O O   . HOH   D .   ? 0.2125 0.1768 0.1817 -0.0047 0.0050  0.0134  355 HOH   A O   
6706 O O   . HOH   D .   ? 0.4341 0.2281 0.4156 0.0425  -0.1126 0.0352  356 HOH   A O   
6707 O O   . HOH   D .   ? 0.3881 0.4989 0.3958 0.2077  0.0445  0.0231  357 HOH   A O   
6708 O O   . HOH   D .   ? 0.2616 0.4078 0.3523 0.0923  -0.0540 -0.0275 358 HOH   A O   
6709 O O   . HOH   D .   ? 0.5969 0.3026 0.4022 -0.1963 0.2029  -0.0974 359 HOH   A O   
6710 O O   . HOH   D .   ? 0.3913 0.2218 0.5126 -0.0904 0.0734  0.0297  360 HOH   A O   
6711 O O   . HOH   D .   ? 0.1596 0.2032 0.2778 0.0137  -0.0069 0.0070  361 HOH   A O   
6712 O O   . HOH   D .   ? 0.2870 0.3769 0.4590 -0.0396 -0.0635 0.0557  362 HOH   A O   
6713 O O   . HOH   D .   ? 0.4066 0.6878 0.5279 -0.0677 -0.1616 0.0541  363 HOH   A O   
6714 O O   . HOH   D .   ? 0.1736 0.1447 0.2742 -0.0048 0.0204  -0.0156 364 HOH   A O   
6715 O O   . HOH   D .   ? 0.4762 0.5031 0.5758 0.1351  0.1779  -0.0072 365 HOH   A O   
6716 O O   . HOH   D .   ? 0.4076 0.6007 0.4714 0.1341  -0.0470 0.1269  366 HOH   A O   
6717 O O   . HOH   D .   ? 0.3377 0.3783 0.5105 -0.0615 -0.1289 -0.0746 367 HOH   A O   
6718 O O   . HOH   D .   ? 0.5949 0.6109 0.4218 0.1838  -0.0110 -0.0042 368 HOH   A O   
6719 O O   . HOH   D .   ? 0.3659 0.2994 0.3933 -0.0818 -0.0217 0.0030  369 HOH   A O   
6720 O O   . HOH   D .   ? 0.1564 0.1634 0.1942 -0.0020 -0.0164 -0.0046 370 HOH   A O   
6721 O O   A HOH   D .   ? 0.2686 0.5470 0.5887 0.1134  0.0509  0.1075  371 HOH   A O   
6722 O O   B HOH   D .   ? 0.1030 0.1969 0.2194 -0.0470 0.0041  -0.0509 372 HOH   A O   
6723 O O   . HOH   D .   ? 0.2337 0.1969 0.2175 0.0002  0.0162  0.0112  373 HOH   A O   
6724 O O   . HOH   D .   ? 0.2471 0.2273 0.2840 0.0078  0.0000  0.0482  374 HOH   A O   
6725 O O   . HOH   D .   ? 0.3276 0.2998 0.2351 0.0236  0.0747  -0.0031 375 HOH   A O   
6726 O O   . HOH   D .   ? 0.2109 0.2092 0.2710 -0.0346 0.0087  0.0353  376 HOH   A O   
6727 O O   . HOH   D .   ? 0.2059 0.2386 0.2276 -0.0272 -0.0288 0.0338  377 HOH   A O   
6728 O O   . HOH   D .   ? 0.2065 0.2588 0.3945 0.0310  0.0701  -0.0539 378 HOH   A O   
6729 O O   . HOH   D .   ? 0.2842 0.4095 0.3024 0.0394  0.0420  0.1584  379 HOH   A O   
6730 O O   . HOH   D .   ? 0.1853 0.1985 0.2455 0.0143  -0.0106 0.0403  380 HOH   A O   
6731 O O   . HOH   D .   ? 0.2758 0.2710 0.4220 -0.0734 0.1051  -0.0073 381 HOH   A O   
6732 O O   A HOH   D .   ? 0.6114 0.4055 0.4876 -0.1484 0.0466  0.0587  382 HOH   A O   
6733 O O   . HOH   D .   ? 0.3867 0.2371 0.5707 -0.0558 -0.0194 -0.0009 383 HOH   A O   
6734 O O   . HOH   D .   ? 0.3323 0.2606 0.3517 -0.0033 -0.0316 0.0947  384 HOH   A O   
6735 O O   . HOH   D .   ? 0.3602 0.6383 0.4602 -0.1020 -0.0101 0.1634  385 HOH   A O   
6736 O O   . HOH   D .   ? 0.2289 0.3493 0.2741 0.0261  0.0259  0.0467  386 HOH   A O   
6737 O O   . HOH   D .   ? 0.2703 0.2093 0.2008 -0.0586 0.0240  0.0249  387 HOH   A O   
6738 O O   . HOH   D .   ? 0.2066 0.2864 0.3323 -0.0208 -0.0039 0.0075  388 HOH   A O   
6739 O O   . HOH   D .   ? 0.4112 0.3995 0.2595 0.0160  -0.1170 0.0179  389 HOH   A O   
6740 O O   . HOH   D .   ? 0.1946 0.1929 0.3950 0.0307  0.0946  0.0817  390 HOH   A O   
6741 O O   . HOH   D .   ? 0.1770 0.1954 0.2622 0.0166  -0.0257 0.0348  391 HOH   A O   
6742 O O   . HOH   D .   ? 0.3273 0.2995 0.2419 -0.0832 -0.0930 0.0514  392 HOH   A O   
6743 O O   . HOH   D .   ? 0.2691 0.1859 0.2977 -0.0042 0.0118  0.0196  393 HOH   A O   
6744 O O   . HOH   D .   ? 0.2904 0.3951 0.3830 -0.0366 0.0908  -0.0772 394 HOH   A O   
6745 O O   . HOH   D .   ? 0.2938 0.7068 0.5682 -0.0113 -0.0759 0.1389  395 HOH   A O   
6746 O O   . HOH   D .   ? 0.1563 0.1506 0.2157 0.0012  -0.0176 0.0076  396 HOH   A O   
6747 O O   A HOH   D .   ? 0.1632 0.1623 0.2029 0.0042  -0.0253 0.0015  397 HOH   A O   
6748 O O   . HOH   D .   ? 0.5901 0.4728 0.5544 -0.0559 -0.0805 0.0540  398 HOH   A O   
6749 O O   . HOH   D .   ? 0.5520 0.2905 0.4991 0.0662  -0.0208 -0.0197 399 HOH   A O   
6750 O O   . HOH   D .   ? 0.2978 0.6465 0.3964 0.0754  0.0636  -0.1033 400 HOH   A O   
6751 O O   . HOH   D .   ? 0.5684 0.6781 0.5583 -0.0362 0.0320  0.0073  401 HOH   A O   
6752 O O   . HOH   D .   ? 0.2397 0.1794 0.3506 0.0049  -0.0483 0.0111  402 HOH   A O   
6753 O O   . HOH   D .   ? 0.2766 0.3479 0.3529 -0.0276 0.1005  -0.0201 403 HOH   A O   
6754 O O   A HOH   D .   ? 0.1399 0.1765 0.2085 -0.0068 -0.0187 -0.0271 404 HOH   A O   
6755 O O   . HOH   D .   ? 0.3174 0.3770 0.6900 -0.0260 0.0842  -0.0844 405 HOH   A O   
6756 O O   . HOH   D .   ? 0.1988 0.1406 0.1951 -0.0180 0.0195  0.0053  406 HOH   A O   
6757 O O   . HOH   D .   ? 0.4907 0.4440 0.5325 0.0723  0.1234  -0.1176 407 HOH   A O   
6758 O O   . HOH   D .   ? 0.3481 0.3144 0.5500 0.0892  0.1007  0.0451  408 HOH   A O   
6759 O O   . HOH   D .   ? 0.6375 0.3923 0.5117 0.1740  -0.1242 0.1044  409 HOH   A O   
6760 O O   . HOH   D .   ? 0.5905 0.3517 0.3553 -0.1254 0.0804  0.1152  410 HOH   A O   
6761 O O   . HOH   D .   ? 0.4589 0.6756 0.3457 -0.0943 -0.0326 0.1553  411 HOH   A O   
6762 O O   . HOH   D .   ? 0.3444 0.5523 0.5524 0.1387  0.0893  0.0665  412 HOH   A O   
6763 O O   . HOH   D .   ? 0.3125 0.3977 0.5273 -0.0604 0.1199  -0.0144 413 HOH   A O   
6764 O O   . HOH   D .   ? 0.2535 0.4298 0.2902 0.1650  0.0030  0.0414  414 HOH   A O   
6765 O O   . HOH   D .   ? 0.6254 0.5882 0.6661 -0.1522 -0.0418 -0.1030 415 HOH   A O   
6766 O O   . HOH   D .   ? 0.2202 0.3068 0.2704 -0.0134 -0.0512 0.0399  416 HOH   A O   
6767 O O   . HOH   D .   ? 0.2645 0.2270 0.2846 -0.0511 -0.0030 0.0593  417 HOH   A O   
6768 O O   . HOH   D .   ? 0.1601 0.1893 0.3808 0.0123  -0.0019 0.0173  418 HOH   A O   
6769 O O   . HOH   D .   ? 0.3124 0.5787 0.1811 -0.0397 0.0449  0.0228  419 HOH   A O   
6770 O O   . HOH   D .   ? 0.3429 0.1450 0.2293 0.0099  -0.0392 0.0030  420 HOH   A O   
6771 O O   . HOH   D .   ? 0.5774 0.7016 0.4108 -0.0417 0.2511  -0.1080 421 HOH   A O   
6772 O O   . HOH   D .   ? 0.5206 0.4583 0.2367 0.0390  0.1088  0.0715  422 HOH   A O   
6773 O O   A HOH   D .   ? 0.2711 0.2382 0.3203 0.0312  0.0593  0.0883  423 HOH   A O   
6774 O O   . HOH   D .   ? 0.2249 0.2569 0.3644 0.0069  -0.0397 -0.0401 424 HOH   A O   
6775 O O   . HOH   D .   ? 0.1673 0.2227 0.3085 -0.0189 -0.0062 0.0480  425 HOH   A O   
6776 O O   . HOH   D .   ? 0.5038 0.5117 0.3361 -0.0351 -0.1201 0.0505  426 HOH   A O   
6777 O O   . HOH   D .   ? 0.4294 0.2531 0.5999 -0.1015 -0.2508 0.1241  427 HOH   A O   
6778 O O   . HOH   D .   ? 0.7025 0.5653 0.7230 -0.1392 0.0363  -0.1190 428 HOH   A O   
6779 O O   . HOH   D .   ? 0.4091 0.3153 0.2614 -0.0727 0.0204  0.0189  429 HOH   A O   
6780 O O   . HOH   D .   ? 0.9242 0.9788 0.7399 -0.0403 0.0359  -0.0993 430 HOH   A O   
6781 O O   . HOH   D .   ? 0.2233 0.1621 0.1967 0.0061  -0.0175 -0.0057 431 HOH   A O   
6782 O O   . HOH   D .   ? 0.3969 0.2993 0.2064 -0.0926 0.0387  0.0670  432 HOH   A O   
6783 O O   . HOH   D .   ? 0.4661 0.4343 0.5286 -0.1148 -0.1157 -0.1281 433 HOH   A O   
6784 O O   . HOH   D .   ? 0.6869 0.6512 0.5405 0.1364  -0.1260 0.0048  434 HOH   A O   
6785 O O   A HOH   D .   ? 0.2199 0.1663 0.2523 0.0164  -0.0554 -0.0258 435 HOH   A O   
6786 O O   . HOH   D .   ? 0.2744 0.1792 0.3323 0.0123  -0.0054 -0.0004 436 HOH   A O   
6787 O O   . HOH   D .   ? 0.5253 0.2805 0.7086 0.0127  0.0060  -0.1183 437 HOH   A O   
6788 O O   . HOH   D .   ? 0.4194 0.3634 0.3475 0.2265  -0.0202 -0.0252 438 HOH   A O   
6789 O O   . HOH   D .   ? 0.3275 0.3964 0.5981 -0.0213 0.1455  -0.1681 439 HOH   A O   
6790 O O   . HOH   D .   ? 0.1919 0.2046 0.5639 -0.0195 -0.0760 0.0702  440 HOH   A O   
6791 O O   . HOH   D .   ? 0.6030 0.7748 0.6076 0.0853  -0.0075 0.0555  441 HOH   A O   
6792 O O   . HOH   D .   ? 0.2600 0.2204 0.2933 0.0142  0.0264  0.0321  442 HOH   A O   
6793 O O   . HOH   D .   ? 0.7654 0.7901 0.5179 0.2348  -0.1092 0.2504  443 HOH   A O   
6794 O O   . HOH   D .   ? 0.6535 0.5389 0.7832 0.0578  -0.1151 0.1731  444 HOH   A O   
6795 O O   . HOH   D .   ? 0.2513 0.3034 0.2790 0.0186  -0.0090 -0.0614 445 HOH   A O   
6796 O O   A HOH   D .   ? 0.1550 0.1754 0.3396 -0.0078 0.0117  0.0726  446 HOH   A O   
6797 O O   . HOH   D .   ? 0.6169 0.4099 0.4904 0.0113  0.0719  0.1521  447 HOH   A O   
6798 O O   . HOH   D .   ? 0.4400 0.7875 0.2931 0.0411  0.1300  0.0140  448 HOH   A O   
6799 O O   . HOH   D .   ? 0.3679 0.5067 0.4849 0.1226  -0.0775 0.1994  449 HOH   A O   
6800 O O   . HOH   D .   ? 0.4786 0.4307 0.4589 0.0717  0.0078  0.0636  450 HOH   A O   
6801 O O   . HOH   D .   ? 0.5441 0.3158 0.4221 0.0670  0.0563  0.0377  451 HOH   A O   
6802 O O   . HOH   D .   ? 0.5137 0.3703 0.4925 0.0422  0.0426  0.0403  452 HOH   A O   
6803 O O   . HOH   D .   ? 0.6477 0.5568 0.5088 -0.0763 0.1217  0.0480  453 HOH   A O   
6804 O O   . HOH   D .   ? 0.3466 0.6032 0.5609 -0.1232 0.1152  -0.0872 454 HOH   A O   
6805 O O   . HOH   D .   ? 0.3050 0.2967 0.3908 -0.0491 0.0039  -0.0773 455 HOH   A O   
6806 O O   . HOH   D .   ? 0.5580 0.2920 0.3749 -0.0832 -0.1355 0.0574  456 HOH   A O   
6807 O O   . HOH   D .   ? 0.7252 0.7326 0.4908 0.0409  -0.1101 -0.0517 457 HOH   A O   
6808 O O   . HOH   D .   ? 0.3881 0.5306 0.5154 0.0679  -0.0443 0.1599  458 HOH   A O   
6809 O O   . HOH   D .   ? 0.3953 0.6738 0.3953 -0.1386 -0.0686 0.2322  459 HOH   A O   
6810 O O   . HOH   D .   ? 0.3407 0.4448 0.4161 -0.0726 -0.0045 -0.0031 460 HOH   A O   
6811 O O   . HOH   D .   ? 0.3381 0.2049 0.2631 0.0497  -0.0917 -0.0244 461 HOH   A O   
6812 O O   . HOH   D .   ? 0.4097 0.5936 0.3743 0.0609  -0.0561 -0.0760 462 HOH   A O   
6813 O O   . HOH   D .   ? 0.3059 0.2980 0.3819 -0.1043 0.0635  -0.0553 463 HOH   A O   
6814 O O   . HOH   D .   ? 0.3196 0.2931 0.6127 0.0749  -0.1434 -0.0606 464 HOH   A O   
6815 O O   . HOH   D .   ? 0.3246 0.4008 0.6947 0.0664  0.0707  -0.1809 465 HOH   A O   
6816 O O   . HOH   D .   ? 0.6332 0.3702 0.7916 0.0766  -0.0194 0.2458  466 HOH   A O   
6817 O O   . HOH   D .   ? 0.6310 0.4765 0.5054 0.0229  0.1514  0.0524  467 HOH   A O   
6818 O O   . HOH   D .   ? 0.6360 0.4644 0.5470 0.0951  0.2383  0.1285  468 HOH   A O   
6819 O O   . HOH   D .   ? 0.3338 0.3420 0.4145 -0.0003 0.0583  0.0067  469 HOH   A O   
6820 O O   . HOH   D .   ? 0.5491 0.5342 0.5330 0.1649  -0.1020 -0.1260 470 HOH   A O   
6821 O O   . HOH   D .   ? 0.4403 0.4474 0.4450 -0.2082 -0.0186 0.0134  471 HOH   A O   
6822 O O   . HOH   D .   ? 0.5337 0.5987 0.5969 -0.1762 -0.0851 0.1388  472 HOH   A O   
6823 O O   . HOH   D .   ? 0.4596 0.4964 0.2986 -0.0258 -0.0211 0.0315  473 HOH   A O   
6824 O O   . HOH   D .   ? 0.6369 0.5239 0.5077 -0.0908 -0.0669 -0.0760 474 HOH   A O   
6825 O O   . HOH   D .   ? 0.2483 0.2673 0.2793 0.0019  0.0008  -0.0048 475 HOH   A O   
6826 O O   . HOH   D .   ? 0.7608 0.6182 0.7159 -0.0732 0.1227  -0.0758 476 HOH   A O   
6827 O O   . HOH   D .   ? 0.5894 0.4637 0.4432 0.0068  0.0072  -0.1298 477 HOH   A O   
6828 O O   . HOH   D .   ? 0.8224 0.4066 0.3327 -0.0490 -0.0992 0.0148  478 HOH   A O   
6829 O O   . HOH   D .   ? 0.4577 0.4375 0.3843 -0.0753 -0.0513 -0.0171 479 HOH   A O   
6830 O O   . HOH   D .   ? 0.3303 0.4926 0.3948 -0.0098 -0.0213 -0.1097 480 HOH   A O   
6831 O O   . HOH   D .   ? 0.2674 0.5155 0.3974 0.1021  0.1031  0.2466  481 HOH   A O   
6832 O O   . HOH   D .   ? 0.3077 0.5236 0.5387 0.0466  0.1510  0.1666  482 HOH   A O   
6833 O O   . HOH   D .   ? 0.5920 0.6959 0.6915 0.0153  -0.1288 0.1311  483 HOH   A O   
6834 O O   . HOH   D .   ? 0.6807 0.7838 0.5167 -0.0203 0.1298  0.1789  484 HOH   A O   
6835 O O   . HOH   D .   ? 0.2827 0.2940 0.6682 -0.0176 -0.1163 0.0435  485 HOH   A O   
6836 O O   . HOH   D .   ? 0.6471 0.4069 0.4005 -0.0748 0.1429  -0.0142 486 HOH   A O   
6837 O O   . HOH   D .   ? 0.4834 0.5655 0.6676 0.0819  0.0719  -0.1276 487 HOH   A O   
6838 O O   . HOH   D .   ? 0.4490 0.3747 0.2842 -0.0784 0.1170  -0.0396 488 HOH   A O   
6839 O O   . HOH   D .   ? 0.3309 0.2392 0.6146 0.0238  0.0531  0.1056  489 HOH   A O   
6840 O O   . HOH   D .   ? 0.4517 0.3510 0.4887 -0.0125 0.2046  0.0418  490 HOH   A O   
6841 O O   . HOH   D .   ? 0.4412 0.3374 0.4802 -0.1061 0.0739  0.0680  491 HOH   A O   
6842 O O   . HOH   D .   ? 0.2944 0.3464 0.5065 -0.0215 0.1073  -0.0444 492 HOH   A O   
6843 O O   . HOH   D .   ? 0.3977 0.9846 0.5387 -0.1323 0.0404  0.2835  493 HOH   A O   
6844 O O   . HOH   D .   ? 0.2660 0.3994 0.3796 0.0577  -0.0396 0.0590  494 HOH   A O   
6845 O O   . HOH   D .   ? 0.5902 0.2869 0.4916 -0.0845 0.0447  0.0790  495 HOH   A O   
6846 O O   . HOH   D .   ? 0.4882 0.2840 0.4972 -0.1489 -0.0011 0.0620  496 HOH   A O   
6847 O O   . HOH   D .   ? 0.3206 0.4404 0.4462 0.0350  -0.0115 0.0494  497 HOH   A O   
6848 O O   . HOH   D .   ? 0.7526 0.4250 0.6166 -0.0056 -0.0125 0.0135  498 HOH   A O   
6849 O O   . HOH   D .   ? 0.6095 0.7548 0.5651 0.1651  -0.0899 0.0352  499 HOH   A O   
6850 O O   . HOH   D .   ? 0.6257 0.6452 0.4559 0.0531  -0.1415 0.0286  500 HOH   A O   
6851 O O   . HOH   D .   ? 0.3522 0.2970 0.4481 -0.0258 0.0202  0.0733  501 HOH   A O   
6852 O O   . HOH   D .   ? 0.5900 0.7639 0.5978 0.3455  -0.0688 0.1402  502 HOH   A O   
6853 O O   . HOH   D .   ? 0.5621 0.5280 0.4260 -0.0402 -0.0007 -0.1390 503 HOH   A O   
6854 O O   . HOH   D .   ? 0.3259 0.7737 0.3928 0.0873  0.0459  0.0066  504 HOH   A O   
6855 O O   . HOH   D .   ? 0.4612 0.6102 0.4623 0.0962  0.0243  0.0115  505 HOH   A O   
6856 O O   . HOH   D .   ? 0.4845 0.6927 0.5794 -0.0618 -0.0892 0.0991  506 HOH   A O   
6857 O O   . HOH   D .   ? 0.3282 0.5040 0.6355 -0.0644 -0.0625 0.2341  507 HOH   A O   
6858 O O   . HOH   E .   ? 0.2465 0.2161 0.3518 0.0181  0.0753  0.0290  201 HOH   B O   
6859 O O   . HOH   E .   ? 0.5769 0.3826 0.3969 -0.0019 -0.0398 -0.1478 202 HOH   B O   
6860 O O   . HOH   E .   ? 0.4241 0.3917 0.6415 -0.0651 0.1028  -0.0468 203 HOH   B O   
6861 O O   . HOH   E .   ? 0.3505 0.6061 0.4970 -0.0266 0.1844  -0.2003 204 HOH   B O   
6862 O O   . HOH   E .   ? 0.4277 0.3375 0.2614 -0.0566 -0.0252 -0.0722 205 HOH   B O   
6863 O O   . HOH   E .   ? 0.5404 0.6024 0.4289 0.2358  -0.1520 0.0049  206 HOH   B O   
6864 O O   . HOH   E .   ? 0.3202 0.7169 0.3673 0.0889  0.0222  0.2260  207 HOH   B O   
6865 O O   . HOH   E .   ? 0.5646 0.4076 0.3378 -0.0437 -0.1302 0.0528  208 HOH   B O   
6866 O O   . HOH   E .   ? 0.4142 0.6223 0.4011 0.2269  -0.0196 0.0240  209 HOH   B O   
6867 O O   . HOH   E .   ? 0.6393 0.5878 0.5864 0.1505  0.0332  0.0011  210 HOH   B O   
6868 O O   . HOH   E .   ? 0.2039 0.2809 0.3253 0.0051  0.0029  -0.0304 211 HOH   B O   
6869 O O   . HOH   E .   ? 0.7420 0.3679 0.5144 0.0561  0.1450  -0.0234 212 HOH   B O   
6870 O O   . HOH   E .   ? 0.2651 0.3001 0.6832 0.0423  -0.1007 0.0459  213 HOH   B O   
6871 O O   . HOH   E .   ? 0.5145 0.4058 0.6539 0.0670  -0.0885 0.2606  214 HOH   B O   
6872 O O   . HOH   E .   ? 0.1719 0.1886 0.3047 -0.0202 -0.0018 0.0153  215 HOH   B O   
6873 O O   . HOH   E .   ? 0.3292 0.2287 0.5594 0.0000  0.1887  0.0198  216 HOH   B O   
6874 O O   . HOH   E .   ? 0.3304 0.2177 0.5829 0.0146  0.2000  0.0923  217 HOH   B O   
6875 O O   . HOH   E .   ? 0.5805 0.3098 0.4477 -0.1728 -0.0113 0.0046  218 HOH   B O   
6876 O O   . HOH   E .   ? 0.3621 0.4988 0.5706 -0.1064 -0.0232 -0.1416 219 HOH   B O   
6877 O O   . HOH   E .   ? 0.2518 0.1920 0.2861 -0.0311 0.0895  0.0002  220 HOH   B O   
6878 O O   . HOH   E .   ? 0.4386 0.4984 0.4549 0.0333  0.0914  -0.1717 221 HOH   B O   
6879 O O   . HOH   E .   ? 0.3837 0.3904 0.5280 -0.1459 -0.0158 0.0941  222 HOH   B O   
6880 O O   . HOH   E .   ? 0.2832 0.4364 0.3537 -0.0936 0.0090  -0.0428 223 HOH   B O   
6881 O O   . HOH   E .   ? 0.1886 0.2147 0.3361 -0.0127 0.0213  -0.0133 224 HOH   B O   
6882 O O   . HOH   E .   ? 0.4882 0.2317 0.5013 -0.0071 -0.1362 0.0380  225 HOH   B O   
6883 O O   . HOH   E .   ? 0.2147 0.4658 0.2832 -0.0280 -0.0137 0.0750  226 HOH   B O   
6884 O O   . HOH   E .   ? 0.3477 0.3571 0.4884 0.0453  -0.1210 -0.0087 227 HOH   B O   
6885 O O   . HOH   E .   ? 0.6582 0.5742 0.3368 0.0357  -0.0426 0.0669  228 HOH   B O   
6886 O O   . HOH   E .   ? 0.4161 0.3552 0.2437 0.0557  0.0719  0.0407  229 HOH   B O   
6887 O O   . HOH   E .   ? 0.7078 0.5122 0.4968 0.1521  -0.0463 -0.0799 230 HOH   B O   
6888 O O   . HOH   E .   ? 0.5522 0.3269 0.4341 -0.2382 0.0116  0.0000  231 HOH   B O   
6889 O O   . HOH   E .   ? 0.3885 0.2582 0.4583 0.0357  -0.0791 -0.1311 232 HOH   B O   
6890 O O   . HOH   E .   ? 0.2912 0.2852 0.3166 0.0422  0.0088  -0.0877 233 HOH   B O   
6891 O O   . HOH   E .   ? 0.4185 0.6109 0.5804 0.2188  0.0570  -0.1216 234 HOH   B O   
6892 O O   . HOH   E .   ? 0.2443 0.2416 0.3989 -0.0427 0.0023  -0.0678 235 HOH   B O   
6893 O O   . HOH   E .   ? 0.5548 0.4615 0.6343 0.0374  -0.1616 -0.1117 236 HOH   B O   
6894 O O   . HOH   E .   ? 0.2366 0.2438 0.3451 -0.0499 0.0174  -0.0291 237 HOH   B O   
6895 O O   . HOH   E .   ? 0.1634 0.1522 0.2028 -0.0111 -0.0075 -0.0077 238 HOH   B O   
6896 O O   . HOH   E .   ? 0.2168 0.1475 0.3717 0.0134  -0.0676 -0.0257 239 HOH   B O   
6897 O O   . HOH   E .   ? 0.4562 0.7277 0.3956 0.2219  0.0683  0.0074  240 HOH   B O   
6898 O O   . HOH   E .   ? 0.2348 0.2057 0.2489 -0.0240 -0.0433 0.0053  241 HOH   B O   
6899 O O   . HOH   E .   ? 0.4261 0.2411 0.4347 0.0791  -0.0447 -0.0787 242 HOH   B O   
6900 O O   . HOH   E .   ? 0.3373 0.1899 0.6092 -0.0184 -0.1567 -0.0344 243 HOH   B O   
6901 O O   . HOH   E .   ? 0.1619 0.1661 0.3104 -0.0117 0.0051  -0.0124 244 HOH   B O   
6902 O O   . HOH   E .   ? 0.1508 0.1400 0.1916 -0.0018 -0.0047 0.0098  245 HOH   B O   
6903 O O   . HOH   E .   ? 0.2484 0.3719 0.3360 -0.0554 -0.0802 -0.0338 246 HOH   B O   
6904 O O   . HOH   E .   ? 0.3468 0.3698 0.2439 0.0178  0.0697  0.0197  247 HOH   B O   
6905 O O   . HOH   E .   ? 0.3168 0.4166 0.3987 -0.1069 -0.0319 -0.0712 248 HOH   B O   
6906 O O   . HOH   E .   ? 0.3261 0.3564 0.6971 -0.0154 0.0660  -0.0114 249 HOH   B O   
6907 O O   . HOH   E .   ? 0.2654 0.2170 0.2234 0.0201  -0.0025 -0.0016 250 HOH   B O   
6908 O O   . HOH   E .   ? 0.3005 0.2325 0.3439 0.0763  0.0972  0.0132  251 HOH   B O   
6909 O O   . HOH   E .   ? 0.3862 0.2033 0.2514 0.0178  -0.0427 -0.0113 252 HOH   B O   
6910 O O   . HOH   E .   ? 0.1780 0.1763 0.3360 -0.0245 -0.0221 0.0051  253 HOH   B O   
6911 O O   . HOH   E .   ? 0.3371 0.3758 0.5384 -0.0127 -0.0164 -0.1016 254 HOH   B O   
6912 O O   . HOH   E .   ? 0.5821 0.3888 0.2783 -0.0010 0.0758  -0.0430 255 HOH   B O   
6913 O O   . HOH   E .   ? 0.2504 0.3163 0.2707 -0.0554 0.0161  0.0711  256 HOH   B O   
6914 O O   . HOH   E .   ? 0.2307 0.1587 0.2362 -0.0277 -0.0437 0.0246  257 HOH   B O   
6915 O O   . HOH   E .   ? 0.2358 0.2089 0.3628 -0.0108 -0.0389 -0.0196 258 HOH   B O   
6916 O O   . HOH   E .   ? 0.3690 0.2569 0.3415 -0.0290 0.0131  -0.0677 259 HOH   B O   
6917 O O   . HOH   E .   ? 0.4448 0.4064 0.3869 -0.0936 0.0535  -0.1145 260 HOH   B O   
6918 O O   . HOH   E .   ? 0.1461 0.1809 0.2566 -0.0048 0.0055  0.0126  261 HOH   B O   
6919 O O   . HOH   E .   ? 0.3965 0.4153 0.4274 0.1555  -0.0551 -0.0804 262 HOH   B O   
6920 O O   . HOH   E .   ? 0.2384 0.2297 0.2792 0.0799  -0.0730 -0.0563 263 HOH   B O   
6921 O O   . HOH   E .   ? 0.3734 0.5360 0.3531 -0.0210 -0.1029 0.1144  264 HOH   B O   
6922 O O   . HOH   E .   ? 0.2011 0.2794 0.3012 0.0524  0.0420  0.0920  265 HOH   B O   
6923 O O   . HOH   E .   ? 0.2480 0.2359 0.2331 0.0254  0.0008  -0.0014 266 HOH   B O   
6924 O O   . HOH   E .   ? 0.1874 0.1482 0.4780 -0.0127 -0.0323 -0.0124 267 HOH   B O   
6925 O O   . HOH   E .   ? 0.3690 0.4212 0.6124 0.0538  0.0379  -0.1202 268 HOH   B O   
6926 O O   . HOH   E .   ? 0.2778 0.2063 0.3182 -0.0592 0.0142  -0.0044 269 HOH   B O   
6927 O O   . HOH   E .   ? 0.2204 0.1612 0.2598 -0.0260 -0.0121 0.0085  270 HOH   B O   
6928 O O   . HOH   E .   ? 0.2843 0.4007 0.3537 -0.0740 0.0665  -0.1386 271 HOH   B O   
6929 O O   . HOH   E .   ? 0.1962 0.1909 0.1884 -0.0443 -0.0439 0.0091  272 HOH   B O   
6930 O O   . HOH   E .   ? 0.2731 0.3689 0.5957 0.0849  -0.0499 -0.0563 273 HOH   B O   
6931 O O   . HOH   E .   ? 0.2324 0.4043 0.5215 -0.0727 -0.0175 -0.1454 274 HOH   B O   
6932 O O   . HOH   E .   ? 0.2568 0.2762 0.2840 -0.0466 -0.0623 -0.0273 275 HOH   B O   
6933 O O   . HOH   E .   ? 0.2873 0.2138 0.5232 0.0036  0.0635  0.0436  276 HOH   B O   
6934 O O   . HOH   E .   ? 0.4239 0.4378 0.5392 -0.0057 -0.1242 -0.0947 277 HOH   B O   
6935 O O   . HOH   E .   ? 0.2783 0.4171 0.4380 0.0341  0.1311  0.0482  278 HOH   B O   
6936 O O   . HOH   E .   ? 0.2789 0.3277 0.2512 0.1176  -0.0209 -0.0175 279 HOH   B O   
6937 O O   . HOH   E .   ? 0.2708 0.2981 0.2880 -0.0504 -0.0832 0.0168  280 HOH   B O   
6938 O O   . HOH   E .   ? 0.1687 0.1748 0.3642 -0.0185 -0.0008 -0.0037 281 HOH   B O   
6939 O O   . HOH   E .   ? 0.4405 0.6363 0.5329 -0.0024 -0.1439 -0.0320 282 HOH   B O   
6940 O O   . HOH   E .   ? 0.2604 0.2874 0.3138 0.0055  -0.0754 0.0243  283 HOH   B O   
6941 O O   . HOH   E .   ? 0.1737 0.1599 0.2124 -0.0022 0.0007  -0.0040 284 HOH   B O   
6942 O O   . HOH   E .   ? 0.1781 0.2095 0.3387 0.0222  -0.0099 0.0108  285 HOH   B O   
6943 O O   . HOH   E .   ? 0.4446 0.4463 0.2917 0.0542  -0.0030 -0.1006 286 HOH   B O   
6944 O O   . HOH   E .   ? 0.4955 0.5471 0.2934 -0.0025 -0.0387 0.1423  287 HOH   B O   
6945 O O   . HOH   E .   ? 0.4787 0.3374 0.5484 -0.0654 -0.0226 0.1066  288 HOH   B O   
6946 O O   . HOH   E .   ? 0.5398 0.4490 0.2696 0.1419  -0.0813 -0.0206 289 HOH   B O   
6947 O O   . HOH   E .   ? 0.3312 0.3136 0.3236 -0.0413 0.0175  -0.1434 290 HOH   B O   
6948 O O   . HOH   E .   ? 0.3344 0.6874 0.7892 0.1298  -0.0570 -0.0936 291 HOH   B O   
6949 O O   . HOH   E .   ? 0.1672 0.2141 0.1833 -0.0144 -0.0215 0.0082  292 HOH   B O   
6950 O O   . HOH   E .   ? 0.3922 0.3090 0.2436 0.0663  -0.0625 -0.0356 293 HOH   B O   
6951 O O   . HOH   E .   ? 0.3529 0.3529 0.4240 -0.1456 0.1352  -0.0586 294 HOH   B O   
6952 O O   . HOH   E .   ? 0.4871 0.4176 0.2821 0.1212  -0.1120 0.0556  295 HOH   B O   
6953 O O   . HOH   E .   ? 0.4297 0.2510 0.4447 -0.1212 -0.2214 0.1116  296 HOH   B O   
6954 O O   . HOH   E .   ? 0.1802 0.3253 0.4935 0.0312  -0.0097 -0.1090 297 HOH   B O   
6955 O O   . HOH   E .   ? 0.3884 0.7283 0.3836 0.1330  -0.1158 0.0908  298 HOH   B O   
6956 O O   . HOH   E .   ? 0.3011 0.5230 0.5267 -0.0826 -0.1350 0.1393  299 HOH   B O   
6957 O O   . HOH   E .   ? 0.1934 0.1709 0.2736 0.0118  0.0167  0.0125  300 HOH   B O   
6958 O O   . HOH   E .   ? 0.2319 0.1688 0.3029 -0.0231 -0.0285 -0.0003 301 HOH   B O   
6959 O O   . HOH   E .   ? 0.2233 0.3101 0.5930 0.0385  -0.0629 -0.0953 302 HOH   B O   
6960 O O   . HOH   E .   ? 0.2709 0.7890 0.2745 0.1109  -0.0484 -0.0755 303 HOH   B O   
6961 O O   . HOH   E .   ? 0.5977 0.4053 0.3531 0.2752  0.1190  0.0902  304 HOH   B O   
6962 O O   . HOH   E .   ? 0.3653 0.1985 0.3398 0.0766  0.1086  0.0414  305 HOH   B O   
6963 O O   . HOH   E .   ? 0.5321 0.3108 0.2516 -0.1641 0.0869  -0.0187 306 HOH   B O   
6964 O O   . HOH   E .   ? 0.3020 0.3117 0.3919 -0.0439 0.1113  -0.0800 307 HOH   B O   
6965 O O   . HOH   E .   ? 0.4751 0.4774 0.2240 0.0075  0.0856  0.0395  308 HOH   B O   
6966 O O   . HOH   E .   ? 0.3670 0.3159 0.5936 -0.0224 -0.0964 0.1415  309 HOH   B O   
6967 O O   . HOH   E .   ? 0.2162 0.1840 0.3596 0.0420  -0.0801 -0.0057 310 HOH   B O   
6968 O O   . HOH   E .   ? 0.2464 0.3295 0.4730 -0.0384 -0.0404 -0.0074 311 HOH   B O   
6969 O O   . HOH   E .   ? 0.7440 0.5655 0.5606 0.2728  -0.0629 -0.0116 312 HOH   B O   
6970 O O   . HOH   E .   ? 0.1750 0.1671 0.3581 0.0118  -0.0049 0.0004  313 HOH   B O   
6971 O O   . HOH   E .   ? 0.4451 0.2560 0.3026 0.1634  0.1131  0.0386  314 HOH   B O   
6972 O O   . HOH   E .   ? 0.2705 0.1614 0.2778 -0.0167 -0.0239 0.0302  315 HOH   B O   
6973 O O   . HOH   E .   ? 0.2117 0.3025 0.3750 0.0385  -0.0181 -0.0721 316 HOH   B O   
6974 O O   . HOH   E .   ? 0.1666 0.2015 0.3117 -0.0242 -0.0111 0.0021  317 HOH   B O   
6975 O O   . HOH   E .   ? 0.2299 0.2118 0.2222 0.0004  0.0137  0.0168  318 HOH   B O   
6976 O O   . HOH   E .   ? 0.5485 0.4417 0.6380 0.1087  0.0060  0.0752  319 HOH   B O   
6977 O O   . HOH   E .   ? 0.1812 0.2931 0.2559 -0.0051 -0.0100 0.0674  320 HOH   B O   
6978 O O   . HOH   E .   ? 0.4690 0.4722 0.3078 0.0332  -0.0519 -0.0895 321 HOH   B O   
6979 O O   . HOH   E .   ? 0.7136 0.5034 0.5172 0.1783  0.0724  0.0102  322 HOH   B O   
6980 O O   . HOH   E .   ? 0.3146 0.2310 0.2837 0.0097  -0.0130 0.0193  323 HOH   B O   
6981 O O   . HOH   E .   ? 0.6237 0.5180 0.5404 -0.1136 -0.0264 0.1269  324 HOH   B O   
6982 O O   . HOH   E .   ? 0.1727 0.1785 0.3387 -0.0107 -0.0208 -0.0276 325 HOH   B O   
6983 O O   . HOH   E .   ? 0.5688 0.5301 0.6246 0.0292  -0.1453 0.2341  326 HOH   B O   
6984 O O   . HOH   E .   ? 0.4523 0.3565 0.5371 0.1376  0.1829  0.1872  327 HOH   B O   
6985 O O   . HOH   E .   ? 0.3016 0.3962 0.5360 -0.0816 -0.1624 0.1775  328 HOH   B O   
6986 O O   . HOH   E .   ? 0.2171 0.2150 0.3352 0.0453  0.0670  0.0229  329 HOH   B O   
6987 O O   . HOH   E .   ? 0.6709 0.3506 0.3920 0.0138  0.1446  0.1154  330 HOH   B O   
6988 O O   . HOH   E .   ? 0.8349 0.2182 0.3297 0.0480  -0.0945 0.0005  331 HOH   B O   
6989 O O   . HOH   E .   ? 0.2888 0.2262 0.5432 0.0062  0.0111  0.0290  332 HOH   B O   
6990 O O   . HOH   E .   ? 0.5980 0.2800 0.3456 0.0945  0.0354  0.0687  333 HOH   B O   
6991 O O   . HOH   E .   ? 0.3372 0.4403 0.8770 -0.0277 -0.1064 0.2663  334 HOH   B O   
6992 O O   . HOH   E .   ? 0.1915 0.1599 0.2754 0.0025  -0.0223 0.0130  335 HOH   B O   
6993 O O   . HOH   E .   ? 0.5783 0.3904 0.4482 0.0145  0.0777  -0.1807 336 HOH   B O   
6994 O O   . HOH   E .   ? 0.5728 0.3532 0.3231 0.0577  -0.1128 -0.0787 337 HOH   B O   
6995 O O   . HOH   E .   ? 0.2344 0.5657 0.5857 -0.0833 -0.0370 0.0523  338 HOH   B O   
6996 O O   . HOH   E .   ? 0.2496 0.2371 0.5515 -0.0603 0.0006  0.1363  339 HOH   B O   
6997 O O   . HOH   E .   ? 0.3178 0.5599 0.7413 0.0739  -0.0614 -0.0418 340 HOH   B O   
6998 O O   . HOH   E .   ? 0.5447 0.6289 0.3434 -0.0503 -0.0218 0.1128  341 HOH   B O   
6999 O O   . HOH   E .   ? 0.6541 0.6063 0.3279 -0.0148 -0.0594 0.0990  342 HOH   B O   
7000 O O   . HOH   E .   ? 0.5587 0.5183 0.6063 -0.0849 -0.0657 -0.1382 343 HOH   B O   
7001 O O   . HOH   E .   ? 0.4056 0.6240 0.3954 -0.0540 -0.0771 -0.0642 344 HOH   B O   
7002 O O   . HOH   E .   ? 0.5342 0.6244 0.3649 -0.0593 -0.1176 0.0648  345 HOH   B O   
7003 O O   . HOH   E .   ? 0.2441 0.2269 0.3793 -0.0137 0.1058  -0.0220 346 HOH   B O   
7004 O O   . HOH   E .   ? 0.2587 0.6285 0.3219 0.1743  -0.0671 -0.1384 347 HOH   B O   
7005 O O   . HOH   E .   ? 0.3434 0.1967 0.4155 0.0515  -0.1289 -0.0531 348 HOH   B O   
7006 O O   . HOH   E .   ? 0.2296 0.4668 0.5849 0.0199  0.0234  0.0303  349 HOH   B O   
7007 O O   . HOH   E .   ? 0.3121 0.2524 0.4832 -0.0387 -0.0712 -0.0457 350 HOH   B O   
7008 O O   . HOH   E .   ? 0.4516 0.5874 0.4710 -0.0040 -0.0557 0.0644  351 HOH   B O   
7009 O O   . HOH   E .   ? 0.4088 0.4317 0.5481 -0.1741 -0.0606 0.0237  352 HOH   B O   
7010 O O   . HOH   E .   ? 0.4744 0.3174 0.6240 -0.1008 0.1432  0.0372  353 HOH   B O   
7011 O O   . HOH   E .   ? 0.4912 0.7569 0.6554 0.1524  0.0628  0.0753  354 HOH   B O   
7012 O O   . HOH   E .   ? 0.5126 0.6551 0.5286 -0.1274 -0.0099 0.0342  355 HOH   B O   
7013 O O   . HOH   E .   ? 0.3943 0.2525 0.3878 -0.0766 0.0346  -0.0943 356 HOH   B O   
7014 O O   . HOH   E .   ? 0.3668 0.3061 0.4820 -0.0890 -0.0198 -0.0741 357 HOH   B O   
7015 O O   . HOH   E .   ? 0.6088 0.3486 0.4975 0.0838  0.1646  -0.0295 358 HOH   B O   
7016 O O   . HOH   E .   ? 0.5375 0.5712 0.5583 -0.0696 -0.0037 0.0234  359 HOH   B O   
7017 O O   . HOH   E .   ? 0.4877 0.6477 0.5301 0.2002  -0.1224 0.1157  360 HOH   B O   
7018 O O   . HOH   E .   ? 0.4777 0.3795 0.5649 -0.0028 -0.1556 -0.0352 361 HOH   B O   
7019 O O   . HOH   E .   ? 0.4775 0.4454 0.6702 -0.0397 0.0223  0.0821  362 HOH   B O   
7020 O O   . HOH   E .   ? 0.2420 0.3731 0.6755 -0.0647 -0.0636 -0.0945 363 HOH   B O   
7021 O O   . HOH   E .   ? 0.4588 0.6836 0.3232 0.1722  -0.0317 0.0573  364 HOH   B O   
7022 O O   . HOH   E .   ? 0.6015 0.5660 0.3767 0.1339  -0.1543 0.0766  365 HOH   B O   
7023 O O   . HOH   E .   ? 0.5710 0.3197 0.5918 -0.1389 -0.0320 0.0443  366 HOH   B O   
7024 O O   . HOH   E .   ? 0.6795 0.2370 0.4305 -0.0063 0.0074  0.0785  367 HOH   B O   
7025 O O   . HOH   E .   ? 0.7072 0.4947 0.4402 0.1163  0.1019  0.0642  368 HOH   B O   
7026 O O   . HOH   E .   ? 0.5354 0.3605 0.5178 0.1256  -0.1353 0.0199  369 HOH   B O   
7027 O O   . HOH   E .   ? 0.5134 0.5996 0.4674 -0.0944 -0.0396 -0.1103 370 HOH   B O   
7028 O O   . HOH   E .   ? 0.4821 0.5527 0.6630 0.2646  0.1036  0.1106  371 HOH   B O   
7029 O O   . HOH   E .   ? 0.6923 0.5250 0.3802 -0.1402 -0.1188 -0.1325 372 HOH   B O   
7030 O O   . HOH   E .   ? 0.4553 0.4103 0.4573 0.0380  -0.1540 -0.0328 373 HOH   B O   
7031 O O   . HOH   E .   ? 0.8098 0.7592 0.5397 0.2428  -0.1380 0.0810  374 HOH   B O   
7032 O O   . HOH   E .   ? 0.4742 0.5025 0.4812 -0.0976 -0.0735 0.0193  375 HOH   B O   
7033 O O   . HOH   E .   ? 0.2518 0.4607 0.4765 0.0627  -0.0874 -0.0835 376 HOH   B O   
7034 O O   . HOH   E .   ? 0.3812 0.4549 0.2585 0.0592  0.0379  0.0197  377 HOH   B O   
7035 O O   . HOH   E .   ? 0.5104 0.7203 0.5698 0.1696  0.0608  0.2608  378 HOH   B O   
7036 O O   . HOH   E .   ? 0.7613 0.4074 0.5276 -0.0666 0.0533  -0.0313 379 HOH   B O   
7037 O O   . HOH   E .   ? 0.5235 0.7810 0.4439 -0.1313 0.0587  -0.1345 380 HOH   B O   
7038 O O   . HOH   E .   ? 0.3777 0.5137 0.5305 0.0967  -0.0046 0.0440  381 HOH   B O   
7039 O O   . HOH   E .   ? 0.6602 0.8255 0.7168 -0.1033 0.1981  0.1619  382 HOH   B O   
7040 O O   . HOH   E .   ? 0.3071 0.2655 0.3444 -0.0048 0.0302  0.0246  383 HOH   B O   
7041 O O   . HOH   E .   ? 0.5907 0.9160 0.6949 0.1702  0.2902  0.1087  384 HOH   B O   
7042 O O   . HOH   E .   ? 0.6510 0.4518 0.5123 0.0201  0.0889  -0.1165 385 HOH   B O   
7043 O O   . HOH   E .   ? 0.7534 0.6282 0.4441 0.2435  0.0325  -0.0114 386 HOH   B O   
7044 O O   . HOH   E .   ? 0.5466 0.5157 0.5031 -0.0256 -0.0876 -0.0566 387 HOH   B O   
7045 O O   . HOH   E .   ? 0.6203 0.3888 0.5730 -0.0503 0.0992  -0.0356 388 HOH   B O   
7046 O O   . HOH   E .   ? 0.2462 0.4418 0.4520 -0.0699 -0.0989 -0.0399 389 HOH   B O   
7047 O O   . HOH   E .   ? 0.5509 0.3993 0.3146 0.0026  0.0396  -0.0218 390 HOH   B O   
7048 O O   . HOH   E .   ? 0.5082 0.2450 0.3725 0.1031  -0.0571 0.0093  391 HOH   B O   
7049 O O   . HOH   E .   ? 0.6123 0.3647 0.4277 0.0299  0.0216  0.0056  392 HOH   B O   
7050 O O   . HOH   E .   ? 0.2607 0.5229 0.7140 -0.1406 -0.0466 -0.0394 393 HOH   B O   
7051 O O   . HOH   E .   ? 0.4664 0.2318 0.5472 -0.0581 0.0274  0.0475  394 HOH   B O   
7052 O O   . HOH   E .   ? 0.5212 0.5484 0.4074 0.1396  0.0084  -0.0881 395 HOH   B O   
7053 O O   . HOH   E .   ? 0.3132 0.4544 0.4097 0.0764  -0.0072 -0.0902 396 HOH   B O   
7054 O O   . HOH   E .   ? 0.2454 0.3002 0.5761 -0.0635 -0.0953 -0.0157 397 HOH   B O   
7055 O O   . HOH   E .   ? 0.4726 0.4446 0.4524 -0.0179 0.1079  0.0857  398 HOH   B O   
7056 O O   . HOH   E .   ? 0.6292 0.6625 0.7697 0.1467  -0.1163 0.2333  399 HOH   B O   
7057 O O   . HOH   E .   ? 0.5613 0.4239 0.3178 -0.1937 -0.0459 0.0820  400 HOH   B O   
7058 O O   . HOH   E .   ? 0.7058 0.6821 0.4446 0.1684  -0.0465 -0.0091 401 HOH   B O   
# 
