data_7HET
# 
_entry.id   7HET 
# 
_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   7HET         pdb_00007het 10.2210/pdb7het/pdb 
WWPDB D_1001407383 ?            ?                   
# 
_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                        7HET 
_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 '(2R)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' 294.351   1   ? ? 
? ?                                                                                    
3 non-polymer syn '(2S)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' 294.351   1   ? ? 
? ?                                                                                    
4 water       nat water                                                                                          18.015    431 ? ? 
? ?                                                                                    
# 
_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 '(2R)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' A1BAB 
3 '(2S)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' A1BAC 
4 water                                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAB non-polymer         . '(2R)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' ? 
'C17 H18 N4 O'   294.351 
A1BAC non-polymer         . '(2S)-2-[(1R)-2,3-dihydro-1H-inden-1-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' ? 
'C17 H18 N4 O'   294.351 
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 A1BAB 1   201 201  A1BAB LA1 A . 
D 3 A1BAC 1   202 301  A1BAC LA2 A . 
E 4 HOH   1   301 493  HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 1290 HOH   HOH A . 
E 4 HOH   4   304 9    HOH   HOH A . 
E 4 HOH   5   305 625  HOH   HOH A . 
E 4 HOH   6   306 18   HOH   HOH A . 
E 4 HOH   7   307 109  HOH   HOH A . 
E 4 HOH   8   308 1289 HOH   HOH A . 
E 4 HOH   9   309 209  HOH   HOH A . 
E 4 HOH   10  310 247  HOH   HOH A . 
E 4 HOH   11  311 196  HOH   HOH A . 
E 4 HOH   12  312 192  HOH   HOH A . 
E 4 HOH   13  313 229  HOH   HOH A . 
E 4 HOH   14  314 153  HOH   HOH A . 
E 4 HOH   15  315 1283 HOH   HOH A . 
E 4 HOH   16  316 1295 HOH   HOH A . 
E 4 HOH   17  317 14   HOH   HOH A . 
E 4 HOH   18  318 409  HOH   HOH A . 
E 4 HOH   19  319 76   HOH   HOH A . 
E 4 HOH   20  320 136  HOH   HOH A . 
E 4 HOH   21  321 281  HOH   HOH A . 
E 4 HOH   22  322 124  HOH   HOH A . 
E 4 HOH   23  323 11   HOH   HOH A . 
E 4 HOH   24  324 86   HOH   HOH A . 
E 4 HOH   25  325 36   HOH   HOH A . 
E 4 HOH   26  326 49   HOH   HOH A . 
E 4 HOH   27  327 15   HOH   HOH A . 
E 4 HOH   28  328 661  HOH   HOH A . 
E 4 HOH   29  329 241  HOH   HOH A . 
E 4 HOH   30  330 151  HOH   HOH A . 
E 4 HOH   31  331 39   HOH   HOH A . 
E 4 HOH   32  332 296  HOH   HOH A . 
E 4 HOH   33  333 96   HOH   HOH A . 
E 4 HOH   34  334 105  HOH   HOH A . 
E 4 HOH   35  335 8    HOH   HOH A . 
E 4 HOH   36  336 236  HOH   HOH A . 
E 4 HOH   37  337 225  HOH   HOH A . 
E 4 HOH   38  338 140  HOH   HOH A . 
E 4 HOH   39  339 396  HOH   HOH A . 
E 4 HOH   40  340 337  HOH   HOH A . 
E 4 HOH   41  341 92   HOH   HOH A . 
E 4 HOH   42  342 21   HOH   HOH A . 
E 4 HOH   43  343 662  HOH   HOH A . 
E 4 HOH   44  344 195  HOH   HOH A . 
E 4 HOH   45  345 469  HOH   HOH A . 
E 4 HOH   46  346 964  HOH   HOH A . 
E 4 HOH   47  347 165  HOH   HOH A . 
E 4 HOH   48  348 42   HOH   HOH A . 
E 4 HOH   49  349 24   HOH   HOH A . 
E 4 HOH   50  350 320  HOH   HOH A . 
E 4 HOH   51  351 68   HOH   HOH A . 
E 4 HOH   52  352 57   HOH   HOH A . 
E 4 HOH   53  353 162  HOH   HOH A . 
E 4 HOH   54  354 27   HOH   HOH A . 
E 4 HOH   55  355 102  HOH   HOH A . 
E 4 HOH   56  356 33   HOH   HOH A . 
E 4 HOH   57  357 169  HOH   HOH A . 
E 4 HOH   58  358 164  HOH   HOH A . 
E 4 HOH   59  359 939  HOH   HOH A . 
E 4 HOH   60  360 354  HOH   HOH A . 
E 4 HOH   61  361 81   HOH   HOH A . 
E 4 HOH   62  362 1308 HOH   HOH A . 
E 4 HOH   63  363 34   HOH   HOH A . 
E 4 HOH   64  364 630  HOH   HOH A . 
E 4 HOH   65  365 93   HOH   HOH A . 
E 4 HOH   66  366 155  HOH   HOH A . 
E 4 HOH   67  367 148  HOH   HOH A . 
E 4 HOH   68  368 139  HOH   HOH A . 
E 4 HOH   69  369 56   HOH   HOH A . 
E 4 HOH   70  370 2    HOH   HOH A . 
E 4 HOH   71  371 351  HOH   HOH A . 
E 4 HOH   72  372 19   HOH   HOH A . 
E 4 HOH   73  373 159  HOH   HOH A . 
E 4 HOH   74  374 18   HOH   HOH A . 
E 4 HOH   75  375 66   HOH   HOH A . 
E 4 HOH   76  376 12   HOH   HOH A . 
E 4 HOH   77  377 1300 HOH   HOH A . 
E 4 HOH   78  378 78   HOH   HOH A . 
E 4 HOH   79  379 35   HOH   HOH A . 
E 4 HOH   80  380 19   HOH   HOH A . 
E 4 HOH   81  381 5    HOH   HOH A . 
E 4 HOH   82  382 138  HOH   HOH A . 
E 4 HOH   83  383 366  HOH   HOH A . 
E 4 HOH   84  384 186  HOH   HOH A . 
E 4 HOH   85  385 393  HOH   HOH A . 
E 4 HOH   86  386 218  HOH   HOH A . 
E 4 HOH   87  387 8    HOH   HOH A . 
E 4 HOH   88  388 17   HOH   HOH A . 
E 4 HOH   89  389 22   HOH   HOH A . 
E 4 HOH   90  390 45   HOH   HOH A . 
E 4 HOH   91  391 1275 HOH   HOH A . 
E 4 HOH   92  392 46   HOH   HOH A . 
E 4 HOH   93  393 134  HOH   HOH A . 
E 4 HOH   94  394 6    HOH   HOH A . 
E 4 HOH   95  395 1309 HOH   HOH A . 
E 4 HOH   96  396 21   HOH   HOH A . 
E 4 HOH   97  397 58   HOH   HOH A . 
E 4 HOH   98  398 278  HOH   HOH A . 
E 4 HOH   99  399 26   HOH   HOH A . 
E 4 HOH   100 400 154  HOH   HOH A . 
E 4 HOH   101 401 405  HOH   HOH A . 
E 4 HOH   102 402 116  HOH   HOH A . 
E 4 HOH   103 403 74   HOH   HOH A . 
E 4 HOH   104 404 4    HOH   HOH A . 
E 4 HOH   105 405 1315 HOH   HOH A . 
E 4 HOH   106 406 132  HOH   HOH A . 
E 4 HOH   107 407 461  HOH   HOH A . 
E 4 HOH   108 408 1    HOH   HOH A . 
E 4 HOH   109 409 83   HOH   HOH A . 
E 4 HOH   110 410 115  HOH   HOH A . 
E 4 HOH   111 411 121  HOH   HOH A . 
E 4 HOH   112 412 303  HOH   HOH A . 
E 4 HOH   113 413 3    HOH   HOH A . 
E 4 HOH   114 414 85   HOH   HOH A . 
E 4 HOH   115 415 333  HOH   HOH A . 
E 4 HOH   116 416 1279 HOH   HOH A . 
E 4 HOH   117 417 67   HOH   HOH A . 
E 4 HOH   118 418 125  HOH   HOH A . 
E 4 HOH   119 419 6    HOH   HOH A . 
E 4 HOH   120 420 123  HOH   HOH A . 
E 4 HOH   121 421 20   HOH   HOH A . 
E 4 HOH   122 422 381  HOH   HOH A . 
E 4 HOH   123 423 25   HOH   HOH A . 
E 4 HOH   124 424 582  HOH   HOH A . 
E 4 HOH   125 425 53   HOH   HOH A . 
E 4 HOH   126 426 51   HOH   HOH A . 
E 4 HOH   127 427 1094 HOH   HOH A . 
E 4 HOH   128 428 24   HOH   HOH A . 
E 4 HOH   129 429 70   HOH   HOH A . 
E 4 HOH   130 430 1313 HOH   HOH A . 
E 4 HOH   131 431 95   HOH   HOH A . 
E 4 HOH   132 432 1296 HOH   HOH A . 
E 4 HOH   133 433 397  HOH   HOH A . 
E 4 HOH   134 434 7    HOH   HOH A . 
E 4 HOH   135 435 1222 HOH   HOH A . 
E 4 HOH   136 436 2    HOH   HOH A . 
E 4 HOH   137 437 156  HOH   HOH A . 
E 4 HOH   138 438 1068 HOH   HOH A . 
E 4 HOH   139 439 199  HOH   HOH A . 
E 4 HOH   140 440 16   HOH   HOH A . 
E 4 HOH   141 441 1238 HOH   HOH A . 
E 4 HOH   142 442 944  HOH   HOH A . 
E 4 HOH   143 443 16   HOH   HOH A . 
E 4 HOH   144 444 1310 HOH   HOH A . 
E 4 HOH   145 445 188  HOH   HOH A . 
E 4 HOH   146 446 122  HOH   HOH A . 
E 4 HOH   147 447 212  HOH   HOH A . 
E 4 HOH   148 448 80   HOH   HOH A . 
E 4 HOH   149 449 71   HOH   HOH A . 
E 4 HOH   150 450 1189 HOH   HOH A . 
E 4 HOH   151 451 104  HOH   HOH A . 
E 4 HOH   152 452 576  HOH   HOH A . 
E 4 HOH   153 453 5    HOH   HOH A . 
E 4 HOH   154 454 952  HOH   HOH A . 
E 4 HOH   155 455 40   HOH   HOH A . 
E 4 HOH   156 456 94   HOH   HOH A . 
E 4 HOH   157 457 4    HOH   HOH A . 
E 4 HOH   158 458 1301 HOH   HOH A . 
E 4 HOH   159 459 97   HOH   HOH A . 
E 4 HOH   160 460 1286 HOH   HOH A . 
E 4 HOH   161 461 73   HOH   HOH A . 
E 4 HOH   162 462 79   HOH   HOH A . 
E 4 HOH   163 463 15   HOH   HOH A . 
E 4 HOH   164 464 330  HOH   HOH A . 
E 4 HOH   165 465 1134 HOH   HOH A . 
E 4 HOH   166 466 1119 HOH   HOH A . 
E 4 HOH   167 467 107  HOH   HOH A . 
E 4 HOH   168 468 509  HOH   HOH A . 
E 4 HOH   169 469 163  HOH   HOH A . 
E 4 HOH   170 470 726  HOH   HOH A . 
E 4 HOH   171 471 12   HOH   HOH A . 
E 4 HOH   172 472 556  HOH   HOH A . 
E 4 HOH   173 473 408  HOH   HOH A . 
E 4 HOH   174 474 756  HOH   HOH A . 
E 4 HOH   175 475 126  HOH   HOH A . 
E 4 HOH   176 476 361  HOH   HOH A . 
E 4 HOH   177 477 319  HOH   HOH A . 
E 4 HOH   178 478 1276 HOH   HOH A . 
E 4 HOH   179 479 801  HOH   HOH A . 
E 4 HOH   180 480 342  HOH   HOH A . 
E 4 HOH   181 481 63   HOH   HOH A . 
E 4 HOH   182 482 250  HOH   HOH A . 
E 4 HOH   183 483 1307 HOH   HOH A . 
E 4 HOH   184 484 370  HOH   HOH A . 
E 4 HOH   185 485 280  HOH   HOH A . 
E 4 HOH   186 486 135  HOH   HOH A . 
E 4 HOH   187 487 267  HOH   HOH A . 
E 4 HOH   188 488 1287 HOH   HOH A . 
E 4 HOH   189 489 1306 HOH   HOH A . 
E 4 HOH   190 490 224  HOH   HOH A . 
E 4 HOH   191 491 202  HOH   HOH A . 
E 4 HOH   192 492 674  HOH   HOH A . 
E 4 HOH   193 493 711  HOH   HOH A . 
E 4 HOH   194 494 695  HOH   HOH A . 
E 4 HOH   195 495 1284 HOH   HOH A . 
E 4 HOH   196 496 919  HOH   HOH A . 
E 4 HOH   197 497 1314 HOH   HOH A . 
E 4 HOH   198 498 315  HOH   HOH A . 
E 4 HOH   199 499 3    HOH   HOH A . 
E 4 HOH   200 500 521  HOH   HOH A . 
E 4 HOH   201 501 309  HOH   HOH A . 
E 4 HOH   202 502 318  HOH   HOH A . 
E 4 HOH   203 503 331  HOH   HOH A . 
E 4 HOH   204 504 941  HOH   HOH A . 
E 4 HOH   205 505 1299 HOH   HOH A . 
E 4 HOH   206 506 805  HOH   HOH A . 
E 4 HOH   207 507 263  HOH   HOH A . 
E 4 HOH   208 508 208  HOH   HOH A . 
E 4 HOH   209 509 13   HOH   HOH A . 
E 4 HOH   210 510 356  HOH   HOH A . 
E 4 HOH   211 511 152  HOH   HOH A . 
E 4 HOH   212 512 180  HOH   HOH A . 
E 4 HOH   213 513 350  HOH   HOH A . 
E 4 HOH   214 514 10   HOH   HOH A . 
E 4 HOH   215 515 1071 HOH   HOH A . 
E 4 HOH   216 516 313  HOH   HOH A . 
E 4 HOH   217 517 363  HOH   HOH A . 
E 4 HOH   218 518 371  HOH   HOH A . 
E 4 HOH   219 519 326  HOH   HOH A . 
E 4 HOH   220 520 7    HOH   HOH A . 
E 4 HOH   221 521 185  HOH   HOH A . 
E 4 HOH   222 522 429  HOH   HOH A . 
E 4 HOH   223 523 23   HOH   HOH A . 
E 4 HOH   224 524 17   HOH   HOH A . 
E 4 HOH   225 525 772  HOH   HOH A . 
E 4 HOH   226 526 376  HOH   HOH A . 
E 4 HOH   227 527 1074 HOH   HOH A . 
E 4 HOH   228 528 1292 HOH   HOH A . 
E 4 HOH   229 529 346  HOH   HOH A . 
E 4 HOH   230 530 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 531  HOH   HOH B . 
F 4 HOH   3   203 549  HOH   HOH B . 
F 4 HOH   4   204 240  HOH   HOH B . 
F 4 HOH   5   205 358  HOH   HOH B . 
F 4 HOH   6   206 1249 HOH   HOH B . 
F 4 HOH   7   207 232  HOH   HOH B . 
F 4 HOH   8   208 398  HOH   HOH B . 
F 4 HOH   9   209 343  HOH   HOH B . 
F 4 HOH   10  210 120  HOH   HOH B . 
F 4 HOH   11  211 364  HOH   HOH B . 
F 4 HOH   12  212 264  HOH   HOH B . 
F 4 HOH   13  213 758  HOH   HOH B . 
F 4 HOH   14  214 50   HOH   HOH B . 
F 4 HOH   15  215 654  HOH   HOH B . 
F 4 HOH   16  216 452  HOH   HOH B . 
F 4 HOH   17  217 353  HOH   HOH B . 
F 4 HOH   18  218 743  HOH   HOH B . 
F 4 HOH   19  219 82   HOH   HOH B . 
F 4 HOH   20  220 900  HOH   HOH B . 
F 4 HOH   21  221 1140 HOH   HOH B . 
F 4 HOH   22  222 444  HOH   HOH B . 
F 4 HOH   23  223 131  HOH   HOH B . 
F 4 HOH   24  224 282  HOH   HOH B . 
F 4 HOH   25  225 1278 HOH   HOH B . 
F 4 HOH   26  226 205  HOH   HOH B . 
F 4 HOH   27  227 172  HOH   HOH B . 
F 4 HOH   28  228 75   HOH   HOH B . 
F 4 HOH   29  229 416  HOH   HOH B . 
F 4 HOH   30  230 54   HOH   HOH B . 
F 4 HOH   31  231 128  HOH   HOH B . 
F 4 HOH   32  232 300  HOH   HOH B . 
F 4 HOH   33  233 272  HOH   HOH B . 
F 4 HOH   34  234 332  HOH   HOH B . 
F 4 HOH   35  235 60   HOH   HOH B . 
F 4 HOH   36  236 1    HOH   HOH B . 
F 4 HOH   37  237 325  HOH   HOH B . 
F 4 HOH   38  238 69   HOH   HOH B . 
F 4 HOH   39  239 723  HOH   HOH B . 
F 4 HOH   40  240 133  HOH   HOH B . 
F 4 HOH   41  241 181  HOH   HOH B . 
F 4 HOH   42  242 127  HOH   HOH B . 
F 4 HOH   43  243 41   HOH   HOH B . 
F 4 HOH   44  244 276  HOH   HOH B . 
F 4 HOH   45  245 30   HOH   HOH B . 
F 4 HOH   46  246 143  HOH   HOH B . 
F 4 HOH   47  247 14   HOH   HOH B . 
F 4 HOH   48  248 72   HOH   HOH B . 
F 4 HOH   49  249 110  HOH   HOH B . 
F 4 HOH   50  250 9    HOH   HOH B . 
F 4 HOH   51  251 166  HOH   HOH B . 
F 4 HOH   52  252 129  HOH   HOH B . 
F 4 HOH   53  253 52   HOH   HOH B . 
F 4 HOH   54  254 1312 HOH   HOH B . 
F 4 HOH   55  255 271  HOH   HOH B . 
F 4 HOH   56  256 144  HOH   HOH B . 
F 4 HOH   57  257 391  HOH   HOH B . 
F 4 HOH   58  258 150  HOH   HOH B . 
F 4 HOH   59  259 10   HOH   HOH B . 
F 4 HOH   60  260 231  HOH   HOH B . 
F 4 HOH   61  261 243  HOH   HOH B . 
F 4 HOH   62  262 103  HOH   HOH B . 
F 4 HOH   63  263 242  HOH   HOH B . 
F 4 HOH   64  264 347  HOH   HOH B . 
F 4 HOH   65  265 47   HOH   HOH B . 
F 4 HOH   66  266 62   HOH   HOH B . 
F 4 HOH   67  267 11   HOH   HOH B . 
F 4 HOH   68  268 252  HOH   HOH B . 
F 4 HOH   69  269 31   HOH   HOH B . 
F 4 HOH   70  270 61   HOH   HOH B . 
F 4 HOH   71  271 1277 HOH   HOH B . 
F 4 HOH   72  272 221  HOH   HOH B . 
F 4 HOH   73  273 117  HOH   HOH B . 
F 4 HOH   74  274 59   HOH   HOH B . 
F 4 HOH   75  275 77   HOH   HOH B . 
F 4 HOH   76  276 84   HOH   HOH B . 
F 4 HOH   77  277 20   HOH   HOH B . 
F 4 HOH   78  278 147  HOH   HOH B . 
F 4 HOH   79  279 387  HOH   HOH B . 
F 4 HOH   80  280 43   HOH   HOH B . 
F 4 HOH   81  281 88   HOH   HOH B . 
F 4 HOH   82  282 114  HOH   HOH B . 
F 4 HOH   83  283 216  HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 106  HOH   HOH B . 
F 4 HOH   86  286 341  HOH   HOH B . 
F 4 HOH   87  287 287  HOH   HOH B . 
F 4 HOH   88  288 1305 HOH   HOH B . 
F 4 HOH   89  289 89   HOH   HOH B . 
F 4 HOH   90  290 175  HOH   HOH B . 
F 4 HOH   91  291 302  HOH   HOH B . 
F 4 HOH   92  292 220  HOH   HOH B . 
F 4 HOH   93  293 235  HOH   HOH B . 
F 4 HOH   94  294 13   HOH   HOH B . 
F 4 HOH   95  295 99   HOH   HOH B . 
F 4 HOH   96  296 1066 HOH   HOH B . 
F 4 HOH   97  297 137  HOH   HOH B . 
F 4 HOH   98  298 635  HOH   HOH B . 
F 4 HOH   99  299 112  HOH   HOH B . 
F 4 HOH   100 300 311  HOH   HOH B . 
F 4 HOH   101 301 101  HOH   HOH B . 
F 4 HOH   102 302 142  HOH   HOH B . 
F 4 HOH   103 303 32   HOH   HOH B . 
F 4 HOH   104 304 160  HOH   HOH B . 
F 4 HOH   105 305 1106 HOH   HOH B . 
F 4 HOH   106 306 170  HOH   HOH B . 
F 4 HOH   107 307 316  HOH   HOH B . 
F 4 HOH   108 308 38   HOH   HOH B . 
F 4 HOH   109 309 215  HOH   HOH B . 
F 4 HOH   110 310 1285 HOH   HOH B . 
F 4 HOH   111 311 91   HOH   HOH B . 
F 4 HOH   112 312 297  HOH   HOH B . 
F 4 HOH   113 313 48   HOH   HOH B . 
F 4 HOH   114 314 118  HOH   HOH B . 
F 4 HOH   115 315 299  HOH   HOH B . 
F 4 HOH   116 316 23   HOH   HOH B . 
F 4 HOH   117 317 37   HOH   HOH B . 
F 4 HOH   118 318 161  HOH   HOH B . 
F 4 HOH   119 319 28   HOH   HOH B . 
F 4 HOH   120 320 44   HOH   HOH B . 
F 4 HOH   121 321 197  HOH   HOH B . 
F 4 HOH   122 322 177  HOH   HOH B . 
F 4 HOH   123 323 1274 HOH   HOH B . 
F 4 HOH   124 324 141  HOH   HOH B . 
F 4 HOH   125 325 55   HOH   HOH B . 
F 4 HOH   126 326 1291 HOH   HOH B . 
F 4 HOH   127 327 29   HOH   HOH B . 
F 4 HOH   128 328 1126 HOH   HOH B . 
F 4 HOH   129 329 100  HOH   HOH B . 
F 4 HOH   130 330 704  HOH   HOH B . 
F 4 HOH   131 331 182  HOH   HOH B . 
F 4 HOH   132 332 334  HOH   HOH B . 
F 4 HOH   133 333 1294 HOH   HOH B . 
F 4 HOH   134 334 98   HOH   HOH B . 
F 4 HOH   135 335 717  HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 207  HOH   HOH B . 
F 4 HOH   138 338 1293 HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 445  HOH   HOH B . 
F 4 HOH   141 341 960  HOH   HOH B . 
F 4 HOH   142 342 339  HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 178  HOH   HOH B . 
F 4 HOH   147 347 1304 HOH   HOH B . 
F 4 HOH   148 348 463  HOH   HOH B . 
F 4 HOH   149 349 87   HOH   HOH B . 
F 4 HOH   150 350 335  HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 623  HOH   HOH B . 
F 4 HOH   154 354 304  HOH   HOH B . 
F 4 HOH   155 355 203  HOH   HOH B . 
F 4 HOH   156 356 1280 HOH   HOH B . 
F 4 HOH   157 357 541  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 1077 HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 373  HOH   HOH B . 
F 4 HOH   166 366 898  HOH   HOH B . 
F 4 HOH   167 367 615  HOH   HOH B . 
F 4 HOH   168 368 340  HOH   HOH B . 
F 4 HOH   169 369 1303 HOH   HOH B . 
F 4 HOH   170 370 1316 HOH   HOH B . 
F 4 HOH   171 371 291  HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 667  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 190  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1163 HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 183  HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 176  HOH   HOH B . 
F 4 HOH   182 382 418  HOH   HOH B . 
F 4 HOH   183 383 1311 HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 424  HOH   HOH B . 
F 4 HOH   186 386 248  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 470  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 981  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 184  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 274  HOH   HOH B . 
F 4 HOH   197 397 157  HOH   HOH B . 
F 4 HOH   198 398 314  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HET 
_cell.length_a           88.668 
_cell.length_b           88.668 
_cell.length_c           39.460 
_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                         7HET 
_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          7HET 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.45 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HET 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.330 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164645 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.200 
_reflns.B_iso_Wilson_estimate        11.870 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.047 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1056230 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33590 7409 ? 1.145 ? ? ? 4.500 ? 1.000  ? ? ? ? ? ? 91.200 1.292 0.583 0.647 
1 2 5.480 44.330 ? 7513  1091 ? 0.030 ? ? ? 6.900 ? 56.100 ? ? ? ? ? ? 99.800 0.033 0.012 0.999 
# 
_refine.entry_id                                 7HET 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.6500 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4400 
_refine.ls_number_reflns_obs                     164573 
_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                          0.1420 
_refine.ls_R_factor_R_work                       0.1413 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1550 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7931 
_refine.ls_number_reflns_R_work                  156642 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9482 
_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                            0.1000 
_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                                72.200 
_refine.B_iso_min                                8.540 
_refine.pdbx_overall_phase_error                 16.5000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.6500 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.number_atoms_solvent             431 
_refine_hist.number_atoms_total               3053 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.34 
_refine_hist.pdbx_B_iso_mean_solvent          30.47 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 89.0000  4719 . 0.3640 0.3364 . 244 0.0000 4963 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  4935 . 0.3017 0.3294 . 207 0.0000 5142 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5294 . 0.2548 0.2662 . 273 0.0000 5567 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5118 . 0.2170 0.2177 . 267 0.0000 5385 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5209 . 0.2013 0.2177 . 325 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5230 . 0.1918 0.2108 . 249 0.0000 5479 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5248 . 0.1835 0.2145 . 256 0.0000 5504 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5194 . 0.1667 0.1935 . 246 0.0000 5440 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5248 . 0.1602 0.1696 . 279 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5198 . 0.1502 0.1700 . 242 0.0000 5440 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5288 . 0.1353 0.1563 . 270 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5216 . 0.1285 0.1505 . 261 0.0000 5477 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5167 . 0.1224 0.1488 . 287 0.0000 5454 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5337 . 0.1182 0.1504 . 223 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5169 . 0.1217 0.1350 . 262 0.0000 5431 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5235 . 0.1255 0.1389 . 277 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5223 . 0.1259 0.1423 . 285 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5235 . 0.1332 0.1528 . 280 0.0000 5515 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5232 . 0.1324 0.1583 . 249 0.0000 5481 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5242 . 0.1274 0.1505 . 267 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5269 . 0.1205 0.1227 . 243 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5217 . 0.1166 0.1272 . 286 0.0000 5503 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5291 . 0.1158 0.1350 . 263 0.0000 5554 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5267 . 0.1251 0.1438 . 255 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5265 . 0.1316 0.1334 . 253 0.0000 5518 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5258 . 0.1327 0.1318 . 283 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5278 . 0.1349 0.1429 . 286 0.0000 5564 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5279 . 0.1352 0.1432 . 287 0.0000 5566 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5309 . 0.1472 0.1660 . 256 0.0000 5565 . 'X-RAY DIFFRACTION' 
3.1100 39.6500 30 100.0000 5472 . 0.1478 0.1666 . 270 0.0000 5742 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HET 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003693' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HET 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HET A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HET 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 7HET SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HET MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HET SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HET MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O LEU A 93  ? O LEU A 93  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HET 
_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    HH 
_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              1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 54.56 -132.69 
2 1 HIS B 86 ? ? 57.20 -128.47 
# 
_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 528 ? 5.87 . 
2 1 O ? A HOH 529 ? 6.05 . 
3 1 O ? A HOH 530 ? 7.63 . 
4 1 O ? B HOH 401 ? 6.30 . 
# 
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 
A1BAB N2   N Y N 1   
A1BAB C3   C N R 2   
A1BAB C6   C Y N 3   
A1BAB C9   C Y N 4   
A1BAB C12  C Y N 5   
A1BAB C14  C Y N 6   
A1BAB C17  C Y N 7   
A1BAB C1   C N N 8   
A1BAB C10  C Y N 9   
A1BAB C11  C Y N 10  
A1BAB C13  C Y N 11  
A1BAB C15  C Y N 12  
A1BAB C16  C Y N 13  
A1BAB C2   C N R 14  
A1BAB C4   C N N 15  
A1BAB C5   C N N 16  
A1BAB C7   C Y N 17  
A1BAB C8   C Y N 18  
A1BAB N1   N N N 19  
A1BAB N3   N Y N 20  
A1BAB N4   N Y N 21  
A1BAB O1   O N N 22  
A1BAB H17  H N N 23  
A1BAB H2   H N N 24  
A1BAB H11  H N N 25  
A1BAB H15  H N N 26  
A1BAB H18  H N N 27  
A1BAB H5   H N N 28  
A1BAB H4   H N N 29  
A1BAB H12  H N N 30  
A1BAB H13  H N N 31  
A1BAB H16  H N N 32  
A1BAB H1   H N N 33  
A1BAB H7   H N N 34  
A1BAB H6   H N N 35  
A1BAB H8   H N N 36  
A1BAB H9   H N N 37  
A1BAB H10  H N N 38  
A1BAB H14  H N N 39  
A1BAB H3   H N N 40  
A1BAC O1   O N N 41  
A1BAC C1   C N N 42  
A1BAC C2   C N S 43  
A1BAC C3   C N R 44  
A1BAC C4   C N N 45  
A1BAC C5   C N N 46  
A1BAC C6   C Y N 47  
A1BAC C7   C Y N 48  
A1BAC C8   C Y N 49  
A1BAC C10  C Y N 50  
A1BAC C11  C Y N 51  
A1BAC C12  C Y N 52  
A1BAC C13  C Y N 53  
A1BAC C14  C Y N 54  
A1BAC C15  C Y N 55  
A1BAC C16  C Y N 56  
A1BAC C17  C Y N 57  
A1BAC C9   C Y N 58  
A1BAC N1   N N N 59  
A1BAC N2   N Y N 60  
A1BAC N3   N Y N 61  
A1BAC N4   N Y N 62  
A1BAC H3   H N N 63  
A1BAC H5   H N N 64  
A1BAC H4   H N N 65  
A1BAC H1   H N N 66  
A1BAC H2   H N N 67  
A1BAC H7   H N N 68  
A1BAC H6   H N N 69  
A1BAC H9   H N N 70  
A1BAC H8   H N N 71  
A1BAC H10  H N N 72  
A1BAC H12  H N N 73  
A1BAC H13  H N N 74  
A1BAC H15  H N N 75  
A1BAC H16  H N N 76  
A1BAC H18  H N N 77  
A1BAC H11  H N N 78  
A1BAC H14  H N N 79  
A1BAC H17  H N N 80  
ALA   N    N N N 81  
ALA   CA   C N S 82  
ALA   C    C N N 83  
ALA   O    O N N 84  
ALA   CB   C N N 85  
ALA   OXT  O N N 86  
ALA   H    H N N 87  
ALA   H2   H N N 88  
ALA   HA   H N N 89  
ALA   HB1  H N N 90  
ALA   HB2  H N N 91  
ALA   HB3  H N N 92  
ALA   HXT  H N N 93  
ARG   N    N N N 94  
ARG   CA   C N S 95  
ARG   C    C N N 96  
ARG   O    O N N 97  
ARG   CB   C N N 98  
ARG   CG   C N N 99  
ARG   CD   C N N 100 
ARG   NE   N N N 101 
ARG   CZ   C N N 102 
ARG   NH1  N N N 103 
ARG   NH2  N N N 104 
ARG   OXT  O N N 105 
ARG   H    H N N 106 
ARG   H2   H N N 107 
ARG   HA   H N N 108 
ARG   HB2  H N N 109 
ARG   HB3  H N N 110 
ARG   HG2  H N N 111 
ARG   HG3  H N N 112 
ARG   HD2  H N N 113 
ARG   HD3  H N N 114 
ARG   HE   H N N 115 
ARG   HH11 H N N 116 
ARG   HH12 H N N 117 
ARG   HH21 H N N 118 
ARG   HH22 H N N 119 
ARG   HXT  H N N 120 
ASN   N    N N N 121 
ASN   CA   C N S 122 
ASN   C    C N N 123 
ASN   O    O N N 124 
ASN   CB   C N N 125 
ASN   CG   C N N 126 
ASN   OD1  O N N 127 
ASN   ND2  N N N 128 
ASN   OXT  O N N 129 
ASN   H    H N N 130 
ASN   H2   H N N 131 
ASN   HA   H N N 132 
ASN   HB2  H N N 133 
ASN   HB3  H N N 134 
ASN   HD21 H N N 135 
ASN   HD22 H N N 136 
ASN   HXT  H N N 137 
ASP   N    N N N 138 
ASP   CA   C N S 139 
ASP   C    C N N 140 
ASP   O    O N N 141 
ASP   CB   C N N 142 
ASP   CG   C N N 143 
ASP   OD1  O N N 144 
ASP   OD2  O N N 145 
ASP   OXT  O N N 146 
ASP   H    H N N 147 
ASP   H2   H N N 148 
ASP   HA   H N N 149 
ASP   HB2  H N N 150 
ASP   HB3  H N N 151 
ASP   HD2  H N N 152 
ASP   HXT  H N N 153 
CYS   N    N N N 154 
CYS   CA   C N R 155 
CYS   C    C N N 156 
CYS   O    O N N 157 
CYS   CB   C N N 158 
CYS   SG   S N N 159 
CYS   OXT  O N N 160 
CYS   H    H N N 161 
CYS   H2   H N N 162 
CYS   HA   H N N 163 
CYS   HB2  H N N 164 
CYS   HB3  H N N 165 
CYS   HG   H N N 166 
CYS   HXT  H N N 167 
GLN   N    N N N 168 
GLN   CA   C N S 169 
GLN   C    C N N 170 
GLN   O    O N N 171 
GLN   CB   C N N 172 
GLN   CG   C N N 173 
GLN   CD   C N N 174 
GLN   OE1  O N N 175 
GLN   NE2  N N N 176 
GLN   OXT  O N N 177 
GLN   H    H N N 178 
GLN   H2   H N N 179 
GLN   HA   H N N 180 
GLN   HB2  H N N 181 
GLN   HB3  H N N 182 
GLN   HG2  H N N 183 
GLN   HG3  H N N 184 
GLN   HE21 H N N 185 
GLN   HE22 H N N 186 
GLN   HXT  H N N 187 
GLU   N    N N N 188 
GLU   CA   C N S 189 
GLU   C    C N N 190 
GLU   O    O N N 191 
GLU   CB   C N N 192 
GLU   CG   C N N 193 
GLU   CD   C N N 194 
GLU   OE1  O N N 195 
GLU   OE2  O N N 196 
GLU   OXT  O N N 197 
GLU   H    H N N 198 
GLU   H2   H N N 199 
GLU   HA   H N N 200 
GLU   HB2  H N N 201 
GLU   HB3  H N N 202 
GLU   HG2  H N N 203 
GLU   HG3  H N N 204 
GLU   HE2  H N N 205 
GLU   HXT  H N N 206 
GLY   N    N N N 207 
GLY   CA   C N N 208 
GLY   C    C N N 209 
GLY   O    O N N 210 
GLY   OXT  O N N 211 
GLY   H    H N N 212 
GLY   H2   H N N 213 
GLY   HA2  H N N 214 
GLY   HA3  H N N 215 
GLY   HXT  H N N 216 
HIS   N    N N N 217 
HIS   CA   C N S 218 
HIS   C    C N N 219 
HIS   O    O N N 220 
HIS   CB   C N N 221 
HIS   CG   C Y N 222 
HIS   ND1  N Y N 223 
HIS   CD2  C Y N 224 
HIS   CE1  C Y N 225 
HIS   NE2  N Y N 226 
HIS   OXT  O N N 227 
HIS   H    H N N 228 
HIS   H2   H N N 229 
HIS   HA   H N N 230 
HIS   HB2  H N N 231 
HIS   HB3  H N N 232 
HIS   HD1  H N N 233 
HIS   HD2  H N N 234 
HIS   HE1  H N N 235 
HIS   HE2  H N N 236 
HIS   HXT  H N N 237 
HOH   O    O N N 238 
HOH   H1   H N N 239 
HOH   H2   H N N 240 
ILE   N    N N N 241 
ILE   CA   C N S 242 
ILE   C    C N N 243 
ILE   O    O N N 244 
ILE   CB   C N S 245 
ILE   CG1  C N N 246 
ILE   CG2  C N N 247 
ILE   CD1  C N N 248 
ILE   OXT  O N N 249 
ILE   H    H N N 250 
ILE   H2   H N N 251 
ILE   HA   H N N 252 
ILE   HB   H N N 253 
ILE   HG12 H N N 254 
ILE   HG13 H N N 255 
ILE   HG21 H N N 256 
ILE   HG22 H N N 257 
ILE   HG23 H N N 258 
ILE   HD11 H N N 259 
ILE   HD12 H N N 260 
ILE   HD13 H N N 261 
ILE   HXT  H N N 262 
LEU   N    N N N 263 
LEU   CA   C N S 264 
LEU   C    C N N 265 
LEU   O    O N N 266 
LEU   CB   C N N 267 
LEU   CG   C N N 268 
LEU   CD1  C N N 269 
LEU   CD2  C N N 270 
LEU   OXT  O N N 271 
LEU   H    H N N 272 
LEU   H2   H N N 273 
LEU   HA   H N N 274 
LEU   HB2  H N N 275 
LEU   HB3  H N N 276 
LEU   HG   H N N 277 
LEU   HD11 H N N 278 
LEU   HD12 H N N 279 
LEU   HD13 H N N 280 
LEU   HD21 H N N 281 
LEU   HD22 H N N 282 
LEU   HD23 H N N 283 
LEU   HXT  H N N 284 
LYS   N    N N N 285 
LYS   CA   C N S 286 
LYS   C    C N N 287 
LYS   O    O N N 288 
LYS   CB   C N N 289 
LYS   CG   C N N 290 
LYS   CD   C N N 291 
LYS   CE   C N N 292 
LYS   NZ   N N N 293 
LYS   OXT  O N N 294 
LYS   H    H N N 295 
LYS   H2   H N N 296 
LYS   HA   H N N 297 
LYS   HB2  H N N 298 
LYS   HB3  H N N 299 
LYS   HG2  H N N 300 
LYS   HG3  H N N 301 
LYS   HD2  H N N 302 
LYS   HD3  H N N 303 
LYS   HE2  H N N 304 
LYS   HE3  H N N 305 
LYS   HZ1  H N N 306 
LYS   HZ2  H N N 307 
LYS   HZ3  H N N 308 
LYS   HXT  H N N 309 
MET   N    N N N 310 
MET   CA   C N S 311 
MET   C    C N N 312 
MET   O    O N N 313 
MET   CB   C N N 314 
MET   CG   C N N 315 
MET   SD   S N N 316 
MET   CE   C N N 317 
MET   OXT  O N N 318 
MET   H    H N N 319 
MET   H2   H N N 320 
MET   HA   H N N 321 
MET   HB2  H N N 322 
MET   HB3  H N N 323 
MET   HG2  H N N 324 
MET   HG3  H N N 325 
MET   HE1  H N N 326 
MET   HE2  H N N 327 
MET   HE3  H N N 328 
MET   HXT  H N N 329 
PHE   N    N N N 330 
PHE   CA   C N S 331 
PHE   C    C N N 332 
PHE   O    O N N 333 
PHE   CB   C N N 334 
PHE   CG   C Y N 335 
PHE   CD1  C Y N 336 
PHE   CD2  C Y N 337 
PHE   CE1  C Y N 338 
PHE   CE2  C Y N 339 
PHE   CZ   C Y N 340 
PHE   OXT  O N N 341 
PHE   H    H N N 342 
PHE   H2   H N N 343 
PHE   HA   H N N 344 
PHE   HB2  H N N 345 
PHE   HB3  H N N 346 
PHE   HD1  H N N 347 
PHE   HD2  H N N 348 
PHE   HE1  H N N 349 
PHE   HE2  H N N 350 
PHE   HZ   H N N 351 
PHE   HXT  H N N 352 
PRO   N    N N N 353 
PRO   CA   C N S 354 
PRO   C    C N N 355 
PRO   O    O N N 356 
PRO   CB   C N N 357 
PRO   CG   C N N 358 
PRO   CD   C N N 359 
PRO   OXT  O N N 360 
PRO   H    H N N 361 
PRO   HA   H N N 362 
PRO   HB2  H N N 363 
PRO   HB3  H N N 364 
PRO   HG2  H N N 365 
PRO   HG3  H N N 366 
PRO   HD2  H N N 367 
PRO   HD3  H N N 368 
PRO   HXT  H N N 369 
SER   N    N N N 370 
SER   CA   C N S 371 
SER   C    C N N 372 
SER   O    O N N 373 
SER   CB   C N N 374 
SER   OG   O N N 375 
SER   OXT  O N N 376 
SER   H    H N N 377 
SER   H2   H N N 378 
SER   HA   H N N 379 
SER   HB2  H N N 380 
SER   HB3  H N N 381 
SER   HG   H N N 382 
SER   HXT  H N N 383 
THR   N    N N N 384 
THR   CA   C N S 385 
THR   C    C N N 386 
THR   O    O N N 387 
THR   CB   C N R 388 
THR   OG1  O N N 389 
THR   CG2  C N N 390 
THR   OXT  O N N 391 
THR   H    H N N 392 
THR   H2   H N N 393 
THR   HA   H N N 394 
THR   HB   H N N 395 
THR   HG1  H N N 396 
THR   HG21 H N N 397 
THR   HG22 H N N 398 
THR   HG23 H N N 399 
THR   HXT  H N N 400 
TYR   N    N N N 401 
TYR   CA   C N S 402 
TYR   C    C N N 403 
TYR   O    O N N 404 
TYR   CB   C N N 405 
TYR   CG   C Y N 406 
TYR   CD1  C Y N 407 
TYR   CD2  C Y N 408 
TYR   CE1  C Y N 409 
TYR   CE2  C Y N 410 
TYR   CZ   C Y N 411 
TYR   OH   O N N 412 
TYR   OXT  O N N 413 
TYR   H    H N N 414 
TYR   H2   H N N 415 
TYR   HA   H N N 416 
TYR   HB2  H N N 417 
TYR   HB3  H N N 418 
TYR   HD1  H N N 419 
TYR   HD2  H N N 420 
TYR   HE1  H N N 421 
TYR   HE2  H N N 422 
TYR   HH   H N N 423 
TYR   HXT  H N N 424 
VAL   N    N N N 425 
VAL   CA   C N S 426 
VAL   C    C N N 427 
VAL   O    O N N 428 
VAL   CB   C N N 429 
VAL   CG1  C N N 430 
VAL   CG2  C N N 431 
VAL   OXT  O N N 432 
VAL   H    H N N 433 
VAL   H2   H N N 434 
VAL   HA   H N N 435 
VAL   HB   H N N 436 
VAL   HG11 H N N 437 
VAL   HG12 H N N 438 
VAL   HG13 H N N 439 
VAL   HG21 H N N 440 
VAL   HG22 H N N 441 
VAL   HG23 H N N 442 
VAL   HXT  H N N 443 
# 
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 
A1BAB C10 C9   doub Y N 1   
A1BAB C10 C11  sing Y N 2   
A1BAB C9  C8   sing Y N 3   
A1BAB C11 C6   doub Y N 4   
A1BAB C8  C7   doub Y N 5   
A1BAB C6  C7   sing Y N 6   
A1BAB C6  C5   sing N N 7   
A1BAB C7  C3   sing N N 8   
A1BAB C5  C4   sing N N 9   
A1BAB C3  C4   sing N N 10  
A1BAB C3  C2   sing N N 11  
A1BAB C1  C2   sing N N 12  
A1BAB C1  O1   sing N N 13  
A1BAB C2  N1   sing N N 14  
A1BAB N1  C12  sing N N 15  
A1BAB C12 C13  doub Y N 16  
A1BAB C12 N4   sing Y N 17  
A1BAB C14 C13  sing Y N 18  
A1BAB C14 C15  doub Y N 19  
A1BAB C13 C16  sing Y N 20  
A1BAB N4  C17  doub Y N 21  
A1BAB C15 N2   sing Y N 22  
A1BAB C16 N2   sing Y N 23  
A1BAB C16 N3   doub Y N 24  
A1BAB C17 N3   sing Y N 25  
A1BAB N2  H17  sing N N 26  
A1BAB C3  H2   sing N N 27  
A1BAB C9  H11  sing N N 28  
A1BAB C14 H15  sing N N 29  
A1BAB C17 H18  sing N N 30  
A1BAB C1  H5   sing N N 31  
A1BAB C1  H4   sing N N 32  
A1BAB C10 H12  sing N N 33  
A1BAB C11 H13  sing N N 34  
A1BAB C15 H16  sing N N 35  
A1BAB C2  H1   sing N N 36  
A1BAB C4  H7   sing N N 37  
A1BAB C4  H6   sing N N 38  
A1BAB C5  H8   sing N N 39  
A1BAB C5  H9   sing N N 40  
A1BAB C8  H10  sing N N 41  
A1BAB N1  H14  sing N N 42  
A1BAB O1  H3   sing N N 43  
A1BAC C11 C10  doub Y N 44  
A1BAC C11 C6   sing Y N 45  
A1BAC C10 C9   sing Y N 46  
A1BAC C6  C5   sing N N 47  
A1BAC C6  C7   doub Y N 48  
A1BAC C5  C4   sing N N 49  
A1BAC C9  C8   doub Y N 50  
A1BAC C1  O1   sing N N 51  
A1BAC C1  C2   sing N N 52  
A1BAC C7  C8   sing Y N 53  
A1BAC C7  C3   sing N N 54  
A1BAC C4  C3   sing N N 55  
A1BAC C3  C2   sing N N 56  
A1BAC C2  N1   sing N N 57  
A1BAC N1  C12  sing N N 58  
A1BAC C12 C13  doub Y N 59  
A1BAC C12 N4   sing Y N 60  
A1BAC C14 C13  sing Y N 61  
A1BAC C14 C15  doub Y N 62  
A1BAC C13 C16  sing Y N 63  
A1BAC N4  C17  doub Y N 64  
A1BAC C15 N2   sing Y N 65  
A1BAC C16 N2   sing Y N 66  
A1BAC C16 N3   doub Y N 67  
A1BAC C17 N3   sing Y N 68  
A1BAC O1  H3   sing N N 69  
A1BAC C1  H5   sing N N 70  
A1BAC C1  H4   sing N N 71  
A1BAC C2  H1   sing N N 72  
A1BAC C3  H2   sing N N 73  
A1BAC C4  H7   sing N N 74  
A1BAC C4  H6   sing N N 75  
A1BAC C5  H9   sing N N 76  
A1BAC C5  H8   sing N N 77  
A1BAC C8  H10  sing N N 78  
A1BAC C10 H12  sing N N 79  
A1BAC C11 H13  sing N N 80  
A1BAC C14 H15  sing N N 81  
A1BAC C15 H16  sing N N 82  
A1BAC C17 H18  sing N N 83  
A1BAC C9  H11  sing N N 84  
A1BAC N1  H14  sing N N 85  
A1BAC N2  H17  sing N N 86  
ALA   N   CA   sing N N 87  
ALA   N   H    sing N N 88  
ALA   N   H2   sing N N 89  
ALA   CA  C    sing N N 90  
ALA   CA  CB   sing N N 91  
ALA   CA  HA   sing N N 92  
ALA   C   O    doub N N 93  
ALA   C   OXT  sing N N 94  
ALA   CB  HB1  sing N N 95  
ALA   CB  HB2  sing N N 96  
ALA   CB  HB3  sing N N 97  
ALA   OXT HXT  sing N N 98  
ARG   N   CA   sing N N 99  
ARG   N   H    sing N N 100 
ARG   N   H2   sing N N 101 
ARG   CA  C    sing N N 102 
ARG   CA  CB   sing N N 103 
ARG   CA  HA   sing N N 104 
ARG   C   O    doub N N 105 
ARG   C   OXT  sing N N 106 
ARG   CB  CG   sing N N 107 
ARG   CB  HB2  sing N N 108 
ARG   CB  HB3  sing N N 109 
ARG   CG  CD   sing N N 110 
ARG   CG  HG2  sing N N 111 
ARG   CG  HG3  sing N N 112 
ARG   CD  NE   sing N N 113 
ARG   CD  HD2  sing N N 114 
ARG   CD  HD3  sing N N 115 
ARG   NE  CZ   sing N N 116 
ARG   NE  HE   sing N N 117 
ARG   CZ  NH1  sing N N 118 
ARG   CZ  NH2  doub N N 119 
ARG   NH1 HH11 sing N N 120 
ARG   NH1 HH12 sing N N 121 
ARG   NH2 HH21 sing N N 122 
ARG   NH2 HH22 sing N N 123 
ARG   OXT HXT  sing N N 124 
ASN   N   CA   sing N N 125 
ASN   N   H    sing N N 126 
ASN   N   H2   sing N N 127 
ASN   CA  C    sing N N 128 
ASN   CA  CB   sing N N 129 
ASN   CA  HA   sing N N 130 
ASN   C   O    doub N N 131 
ASN   C   OXT  sing N N 132 
ASN   CB  CG   sing N N 133 
ASN   CB  HB2  sing N N 134 
ASN   CB  HB3  sing N N 135 
ASN   CG  OD1  doub N N 136 
ASN   CG  ND2  sing N N 137 
ASN   ND2 HD21 sing N N 138 
ASN   ND2 HD22 sing N N 139 
ASN   OXT HXT  sing N N 140 
ASP   N   CA   sing N N 141 
ASP   N   H    sing N N 142 
ASP   N   H2   sing N N 143 
ASP   CA  C    sing N N 144 
ASP   CA  CB   sing N N 145 
ASP   CA  HA   sing N N 146 
ASP   C   O    doub N N 147 
ASP   C   OXT  sing N N 148 
ASP   CB  CG   sing N N 149 
ASP   CB  HB2  sing N N 150 
ASP   CB  HB3  sing N N 151 
ASP   CG  OD1  doub N N 152 
ASP   CG  OD2  sing N N 153 
ASP   OD2 HD2  sing N N 154 
ASP   OXT HXT  sing N N 155 
CYS   N   CA   sing N N 156 
CYS   N   H    sing N N 157 
CYS   N   H2   sing N N 158 
CYS   CA  C    sing N N 159 
CYS   CA  CB   sing N N 160 
CYS   CA  HA   sing N N 161 
CYS   C   O    doub N N 162 
CYS   C   OXT  sing N N 163 
CYS   CB  SG   sing N N 164 
CYS   CB  HB2  sing N N 165 
CYS   CB  HB3  sing N N 166 
CYS   SG  HG   sing N N 167 
CYS   OXT HXT  sing N N 168 
GLN   N   CA   sing N N 169 
GLN   N   H    sing N N 170 
GLN   N   H2   sing N N 171 
GLN   CA  C    sing N N 172 
GLN   CA  CB   sing N N 173 
GLN   CA  HA   sing N N 174 
GLN   C   O    doub N N 175 
GLN   C   OXT  sing N N 176 
GLN   CB  CG   sing N N 177 
GLN   CB  HB2  sing N N 178 
GLN   CB  HB3  sing N N 179 
GLN   CG  CD   sing N N 180 
GLN   CG  HG2  sing N N 181 
GLN   CG  HG3  sing N N 182 
GLN   CD  OE1  doub N N 183 
GLN   CD  NE2  sing N N 184 
GLN   NE2 HE21 sing N N 185 
GLN   NE2 HE22 sing N N 186 
GLN   OXT HXT  sing N N 187 
GLU   N   CA   sing N N 188 
GLU   N   H    sing N N 189 
GLU   N   H2   sing N N 190 
GLU   CA  C    sing N N 191 
GLU   CA  CB   sing N N 192 
GLU   CA  HA   sing N N 193 
GLU   C   O    doub N N 194 
GLU   C   OXT  sing N N 195 
GLU   CB  CG   sing N N 196 
GLU   CB  HB2  sing N N 197 
GLU   CB  HB3  sing N N 198 
GLU   CG  CD   sing N N 199 
GLU   CG  HG2  sing N N 200 
GLU   CG  HG3  sing N N 201 
GLU   CD  OE1  doub N N 202 
GLU   CD  OE2  sing N N 203 
GLU   OE2 HE2  sing N N 204 
GLU   OXT HXT  sing N N 205 
GLY   N   CA   sing N N 206 
GLY   N   H    sing N N 207 
GLY   N   H2   sing N N 208 
GLY   CA  C    sing N N 209 
GLY   CA  HA2  sing N N 210 
GLY   CA  HA3  sing N N 211 
GLY   C   O    doub N N 212 
GLY   C   OXT  sing N N 213 
GLY   OXT HXT  sing N N 214 
HIS   N   CA   sing N N 215 
HIS   N   H    sing N N 216 
HIS   N   H2   sing N N 217 
HIS   CA  C    sing N N 218 
HIS   CA  CB   sing N N 219 
HIS   CA  HA   sing N N 220 
HIS   C   O    doub N N 221 
HIS   C   OXT  sing N N 222 
HIS   CB  CG   sing N N 223 
HIS   CB  HB2  sing N N 224 
HIS   CB  HB3  sing N N 225 
HIS   CG  ND1  sing Y N 226 
HIS   CG  CD2  doub Y N 227 
HIS   ND1 CE1  doub Y N 228 
HIS   ND1 HD1  sing N N 229 
HIS   CD2 NE2  sing Y N 230 
HIS   CD2 HD2  sing N N 231 
HIS   CE1 NE2  sing Y N 232 
HIS   CE1 HE1  sing N N 233 
HIS   NE2 HE2  sing N N 234 
HIS   OXT HXT  sing N N 235 
HOH   O   H1   sing N N 236 
HOH   O   H2   sing N N 237 
ILE   N   CA   sing N N 238 
ILE   N   H    sing N N 239 
ILE   N   H2   sing N N 240 
ILE   CA  C    sing N N 241 
ILE   CA  CB   sing N N 242 
ILE   CA  HA   sing N N 243 
ILE   C   O    doub N N 244 
ILE   C   OXT  sing N N 245 
ILE   CB  CG1  sing N N 246 
ILE   CB  CG2  sing N N 247 
ILE   CB  HB   sing N N 248 
ILE   CG1 CD1  sing N N 249 
ILE   CG1 HG12 sing N N 250 
ILE   CG1 HG13 sing N N 251 
ILE   CG2 HG21 sing N N 252 
ILE   CG2 HG22 sing N N 253 
ILE   CG2 HG23 sing N N 254 
ILE   CD1 HD11 sing N N 255 
ILE   CD1 HD12 sing N N 256 
ILE   CD1 HD13 sing N N 257 
ILE   OXT HXT  sing N N 258 
LEU   N   CA   sing N N 259 
LEU   N   H    sing N N 260 
LEU   N   H2   sing N N 261 
LEU   CA  C    sing N N 262 
LEU   CA  CB   sing N N 263 
LEU   CA  HA   sing N N 264 
LEU   C   O    doub N N 265 
LEU   C   OXT  sing N N 266 
LEU   CB  CG   sing N N 267 
LEU   CB  HB2  sing N N 268 
LEU   CB  HB3  sing N N 269 
LEU   CG  CD1  sing N N 270 
LEU   CG  CD2  sing N N 271 
LEU   CG  HG   sing N N 272 
LEU   CD1 HD11 sing N N 273 
LEU   CD1 HD12 sing N N 274 
LEU   CD1 HD13 sing N N 275 
LEU   CD2 HD21 sing N N 276 
LEU   CD2 HD22 sing N N 277 
LEU   CD2 HD23 sing N N 278 
LEU   OXT HXT  sing N N 279 
LYS   N   CA   sing N N 280 
LYS   N   H    sing N N 281 
LYS   N   H2   sing N N 282 
LYS   CA  C    sing N N 283 
LYS   CA  CB   sing N N 284 
LYS   CA  HA   sing N N 285 
LYS   C   O    doub N N 286 
LYS   C   OXT  sing N N 287 
LYS   CB  CG   sing N N 288 
LYS   CB  HB2  sing N N 289 
LYS   CB  HB3  sing N N 290 
LYS   CG  CD   sing N N 291 
LYS   CG  HG2  sing N N 292 
LYS   CG  HG3  sing N N 293 
LYS   CD  CE   sing N N 294 
LYS   CD  HD2  sing N N 295 
LYS   CD  HD3  sing N N 296 
LYS   CE  NZ   sing N N 297 
LYS   CE  HE2  sing N N 298 
LYS   CE  HE3  sing N N 299 
LYS   NZ  HZ1  sing N N 300 
LYS   NZ  HZ2  sing N N 301 
LYS   NZ  HZ3  sing N N 302 
LYS   OXT HXT  sing N N 303 
MET   N   CA   sing N N 304 
MET   N   H    sing N N 305 
MET   N   H2   sing N N 306 
MET   CA  C    sing N N 307 
MET   CA  CB   sing N N 308 
MET   CA  HA   sing N N 309 
MET   C   O    doub N N 310 
MET   C   OXT  sing N N 311 
MET   CB  CG   sing N N 312 
MET   CB  HB2  sing N N 313 
MET   CB  HB3  sing N N 314 
MET   CG  SD   sing N N 315 
MET   CG  HG2  sing N N 316 
MET   CG  HG3  sing N N 317 
MET   SD  CE   sing N N 318 
MET   CE  HE1  sing N N 319 
MET   CE  HE2  sing N N 320 
MET   CE  HE3  sing N N 321 
MET   OXT HXT  sing N N 322 
PHE   N   CA   sing N N 323 
PHE   N   H    sing N N 324 
PHE   N   H2   sing N N 325 
PHE   CA  C    sing N N 326 
PHE   CA  CB   sing N N 327 
PHE   CA  HA   sing N N 328 
PHE   C   O    doub N N 329 
PHE   C   OXT  sing N N 330 
PHE   CB  CG   sing N N 331 
PHE   CB  HB2  sing N N 332 
PHE   CB  HB3  sing N N 333 
PHE   CG  CD1  doub Y N 334 
PHE   CG  CD2  sing Y N 335 
PHE   CD1 CE1  sing Y N 336 
PHE   CD1 HD1  sing N N 337 
PHE   CD2 CE2  doub Y N 338 
PHE   CD2 HD2  sing N N 339 
PHE   CE1 CZ   doub Y N 340 
PHE   CE1 HE1  sing N N 341 
PHE   CE2 CZ   sing Y N 342 
PHE   CE2 HE2  sing N N 343 
PHE   CZ  HZ   sing N N 344 
PHE   OXT HXT  sing N N 345 
PRO   N   CA   sing N N 346 
PRO   N   CD   sing N N 347 
PRO   N   H    sing N N 348 
PRO   CA  C    sing N N 349 
PRO   CA  CB   sing N N 350 
PRO   CA  HA   sing N N 351 
PRO   C   O    doub N N 352 
PRO   C   OXT  sing N N 353 
PRO   CB  CG   sing N N 354 
PRO   CB  HB2  sing N N 355 
PRO   CB  HB3  sing N N 356 
PRO   CG  CD   sing N N 357 
PRO   CG  HG2  sing N N 358 
PRO   CG  HG3  sing N N 359 
PRO   CD  HD2  sing N N 360 
PRO   CD  HD3  sing N N 361 
PRO   OXT HXT  sing N N 362 
SER   N   CA   sing N N 363 
SER   N   H    sing N N 364 
SER   N   H2   sing N N 365 
SER   CA  C    sing N N 366 
SER   CA  CB   sing N N 367 
SER   CA  HA   sing N N 368 
SER   C   O    doub N N 369 
SER   C   OXT  sing N N 370 
SER   CB  OG   sing N N 371 
SER   CB  HB2  sing N N 372 
SER   CB  HB3  sing N N 373 
SER   OG  HG   sing N N 374 
SER   OXT HXT  sing N N 375 
THR   N   CA   sing N N 376 
THR   N   H    sing N N 377 
THR   N   H2   sing N N 378 
THR   CA  C    sing N N 379 
THR   CA  CB   sing N N 380 
THR   CA  HA   sing N N 381 
THR   C   O    doub N N 382 
THR   C   OXT  sing N N 383 
THR   CB  OG1  sing N N 384 
THR   CB  CG2  sing N N 385 
THR   CB  HB   sing N N 386 
THR   OG1 HG1  sing N N 387 
THR   CG2 HG21 sing N N 388 
THR   CG2 HG22 sing N N 389 
THR   CG2 HG23 sing N N 390 
THR   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_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                    7HET 
_atom_sites.fract_transf_matrix[1][1]   0.011278 
_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]   0.011278 
_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]   0.025342 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.626 -16.176 22.268  0.40 54.60 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.594 -15.888 22.371  0.60 55.76 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.651 -15.102 22.418  0.40 54.17 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.592 -14.840 22.518  0.60 55.25 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.302 -13.755 22.122  0.40 52.38 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.216 -13.474 22.244  0.60 53.32 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.412 -13.481 22.578  0.40 52.74 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.281 -13.154 22.773  0.60 53.75 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.008 -15.122 23.821  0.40 55.18 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.931 -14.890 23.911  0.60 56.26 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.981 -14.006 23.956  0.40 55.38 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.872 -13.804 24.038  0.60 56.42 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.367 -16.476 24.095  0.40 55.44 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.325 -16.265 24.163  0.60 56.54 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.943 -15.233 21.773  0.40 65.00 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.895 -14.981 21.863  0.60 66.29 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.695 -14.978 24.490  0.40 66.22 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.605 -14.732 24.590  0.60 67.51 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.467 -14.146 24.767  0.40 66.46 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.353 -13.964 24.842  0.60 67.71 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.442 -13.154 24.002  0.40 66.46 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.308 -12.940 24.092  0.60 67.71 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.393 -14.025 23.185  0.40 66.46 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.293 -13.837 23.260  0.60 67.71 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.909 -16.442 24.950  0.40 66.52 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.847 -16.250 25.007  0.60 67.84 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.733 -16.673 23.388  0.40 66.52 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.712 -16.476 23.441  0.60 67.84 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.060 -17.155 24.117  0.40 66.52 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.035 -16.924 24.197  0.60 67.84 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.610 -12.920 21.347  0.40 49.91 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.553 -12.675 21.408  0.60 50.57 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.055 -11.563 21.055  0.40 47.13 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.003 -11.327 21.084  0.60 47.46 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.903 -10.593 21.301  0.40 44.36 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.867 -10.338 21.339  0.60 44.45 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.780 -10.993 21.622  0.40 44.32 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.770 -10.713 21.765  0.60 44.34 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.622 -11.442 19.633  0.40 46.87 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.544 -11.235 19.650  0.60 47.09 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.629 -11.850 18.565  0.40 46.47 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.536 -11.675 18.612  0.60 46.55 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.480 -11.410 18.564  0.40 46.40 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.377 -11.261 18.635  0.60 46.40 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.073 -12.699 17.644  0.40 46.35 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.975 -12.525 17.690  0.60 46.43 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.864 -13.127 20.972  0.40 59.88 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.823 -12.902 21.011  0.60 60.68 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.767 -11.337 21.667  0.40 56.56 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.731 -11.099 21.676  0.60 56.95 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.874 -10.517 19.473  0.40 56.24 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.786 -10.313 19.462  0.60 56.51 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.400 -12.014 19.553  0.40 56.24 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.325 -11.803 19.570  0.60 56.51 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.552 -12.961 17.012  0.40 55.62 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.445 -12.805 17.074  0.60 55.72 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.883 -12.987 17.679  0.40 55.62 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.793 -12.794 17.708  0.60 55.72 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.190 -9.301  21.144  0.40 41.36 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.137 -9.061  21.069  0.60 41.25 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.263 -8.239  21.514  0.40 38.22 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.245 -7.972  21.447  0.60 37.91 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.414 -7.747  20.346  0.40 34.54 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.392 -7.458  20.291  0.60 33.78 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.719 -6.735  20.486  0.40 34.35 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.788 -6.387  20.413  0.60 33.60 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.020 -7.069  22.146  0.40 39.01 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.044 -6.819  22.061  0.60 39.03 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.016 -6.572  21.269  0.40 39.33 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.963 -6.279  21.129  0.60 39.48 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.930 -9.013  20.814  0.40 49.63 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.844 -8.800  20.655  0.60 49.50 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.659 -8.584  22.188  0.40 45.86 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.643 -8.296  22.132  0.60 45.49 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.391 -6.356  22.343  0.40 46.81 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.428 -6.121  22.336  0.60 46.84 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.442 -7.372  22.966  0.40 46.81 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.533 -7.148  22.832  0.60 46.84 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.423 -5.932  21.631  0.40 47.19 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.393 -5.648  21.482  0.60 47.38 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.451 -8.427  19.204  0.40 30.86 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.325 -8.185  19.179  0.60 29.62 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.558 -8.081  18.106  0.40 27.23 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.433 -7.796  18.094  0.60 25.50 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.128 -8.461  18.473  0.40 26.22 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.991 -8.098  18.489  0.60 25.09 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.873 -9.575  18.939  0.40 26.75 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.699 -9.174  19.014  0.60 25.82 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.983 -8.809  16.833  0.40 25.01 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.806 -8.547  16.816  0.60 22.81 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.251 -8.278  16.219  0.40 23.16 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.116 -8.105  16.212  0.60 20.94 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.244 -7.094  15.500  0.40 22.30 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.182 -6.963  15.432  0.60 19.89 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.445 -8.969  16.349  0.40 22.77 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.278 -8.834  16.420  0.60 21.23 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.405 -6.604  14.930  0.40 22.12 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.380 -6.554  14.872  0.60 19.88 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.609 -8.484  15.780  0.40 22.45 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.479 -8.429  15.862  0.60 21.11 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.589 -7.300  15.069  0.40 22.20 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.529 -7.286  15.087  0.60 20.57 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.979 -9.086  19.042  0.40 37.03 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.774 -8.905  19.034  0.60 35.54 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.596 -7.125  17.947  0.40 32.68 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.513 -6.848  17.935  0.60 30.60 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.125 -9.746  17.043  0.40 30.01 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.875 -9.495  17.018  0.60 27.37 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.276 -8.723  16.175  0.40 30.01 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.111 -8.403  16.156  0.60 27.37 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.450 -6.620  15.403  0.40 26.76 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.410 -6.465  15.283  0.60 23.86 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.463 -9.767  16.828  0.40 27.33 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.248 -9.605  16.945  0.60 25.48 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.389 -5.807  14.451  0.40 26.54 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.410 -5.785  14.350  0.60 23.86 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.405 -8.956  15.877  0.40 26.94 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.252 -8.926  16.012  0.60 25.32 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.370 -6.972  14.686  0.40 26.64 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.333 -7.012  14.712  0.60 24.68 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.193 -7.534  18.260  0.40 24.72 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.090 -7.147  18.243  0.60 24.16 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.820 -7.688  18.721  0.40 23.67 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.725 -7.196  18.756  0.60 24.26 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.843 -7.348  17.603  0.40 22.05 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.720 -7.107  17.616  0.60 22.62 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.085 -6.433  16.810  0.40 22.19 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.866 -6.275  16.713  0.60 22.38 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.559 -6.773  19.928  0.40 24.09 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.487 -6.047  19.743  0.60 25.54 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.221 -6.880  20.381  0.40 24.58 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.104 -5.761  19.871  0.60 27.06 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.338 -6.794  17.845  0.40 29.66 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.255 -6.448  17.769  0.60 28.99 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.670 -8.605  18.996  0.40 28.40 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.585 -8.032  19.225  0.60 29.11 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.158 -7.025  20.650  0.40 28.90 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 11.822 -6.306  20.615  0.60 30.65 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.730 -5.853  19.668  0.40 28.90 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.963 -5.259  19.429  0.60 30.65 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.102 -6.372  21.041  0.40 29.50 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.997  -5.110  20.390  0.60 32.47 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.738  -8.092  17.543  0.40 20.71 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.700  -7.962  17.661  0.60 21.91 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.666  -7.774  16.620  0.40 19.33 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.591  -7.847  16.739  0.60 21.18 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.845  -8.271  15.202  0.40 17.94 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.843  -8.349  15.340  0.60 19.82 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.147  -7.794  14.301  0.40 18.33 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.088  -7.996  14.428  0.60 20.19 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.594  -8.783  18.034  0.40 24.85 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.639  -8.615  18.215  0.60 26.29 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.840  -8.145  16.973  0.40 23.20 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.841  -8.344  17.095  0.60 25.42 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.564  -6.810  16.586  0.40 23.20 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.334  -6.915  16.678  0.60 25.42 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.754  -9.213  14.970  0.40 16.44 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.869  -9.168  15.132  0.60 18.45 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 9.987  -9.750  13.639  0.40 14.84 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.160 -9.687  13.806  0.60 17.03 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.093  -10.953 13.365  0.40 13.90 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.338  -10.937 13.522  0.60 15.98 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.719  -11.702 14.273  0.40 14.52 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.131  -11.781 14.401  0.60 16.86 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.445 -10.191 13.480  0.40 14.58 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.652 -9.991  13.653  0.60 16.57 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.411 -9.047  13.331  0.40 14.32 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.491 -8.749  13.437  0.60 16.12 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.800 -8.301  14.431  0.40 14.36 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.746 -7.871  14.482  0.60 16.52 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.927 -8.708  12.089  0.40 14.24 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.011 -8.447  12.185  0.60 15.50 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.672 -7.242  14.301  0.40 14.67 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.500 -6.730  14.287  0.60 16.11 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.799 -7.652  11.946  0.40 14.54 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.765 -7.306  11.981  0.60 15.20 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.170 -6.921  13.055  0.40 15.07 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.007 -6.456  13.035  0.60 15.41 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 15.037 -5.868  12.919  0.40 15.92 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.752 -5.321  12.832  0.60 15.61 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.250 -9.560  15.576  0.40 19.72 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.407 -9.449  15.746  0.60 22.14 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.799  -9.066  12.973  0.40 17.81 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.923  -9.019  13.149  0.60 20.43 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.709 -10.710 14.256  0.40 17.49 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.968 -10.437 14.457  0.60 19.89 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.501 -10.734 12.682  0.40 17.49 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.769 -10.573 12.886  0.60 19.89 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.457 -8.513  15.269  0.40 17.23 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.401 -8.055  15.326  0.60 19.82 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.675 -9.201  11.338  0.40 17.09 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.846 -9.020  11.471  0.60 18.60 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.923 -6.749  15.047  0.40 17.60 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.665 -6.150  14.995  0.60 19.32 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.141 -7.440  11.107  0.40 17.45 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.111 -7.114  11.136  0.60 18.24 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.179 -5.520  13.669  0.40 19.10 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.824 -4.884  13.549  0.60 18.73 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.759  -11.128 12.091  0.40 13.83 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.868  -11.038 12.282  0.60 15.47 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.183  -12.367 11.596  0.40 13.55 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.192  -12.225 11.785  0.60 14.80 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.315  -13.302 11.185  0.40 13.08 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.248  -13.210 11.290  0.60 13.98 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.333 -12.861 10.641  0.40 12.27 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.079 -12.865 10.439  0.60 13.49 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.301  -12.069 10.385  0.40 14.45 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.249  -11.829 10.650  0.60 15.26 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.604  -13.275 9.759   0.40 16.18 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.591  -12.983 9.895   0.60 16.53 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.537  -13.820 10.696  0.40 17.06 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.659  -13.772 10.801  0.60 17.89 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.008  -12.911 8.412   0.40 16.93 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 5.848  -12.459 8.677   0.60 17.40 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.856  -10.525 11.479  0.40 16.59 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.936  -10.413 11.690  0.60 18.57 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.645  -12.785 12.290  0.40 16.26 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.671  -12.636 12.495  0.60 17.76 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.607  -11.444 10.653  0.40 17.34 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.531  -11.278 11.017  0.60 18.31 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.850  -11.665 9.698   0.40 17.34 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.746  -11.304 10.001  0.60 18.31 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.256  -13.977 9.612   0.40 19.42 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.280  -13.585 9.581   0.60 19.84 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.099  -14.574 10.271  0.40 20.48 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.324  -14.542 10.314  0.60 21.46 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.958  -14.107 11.523  0.40 20.48 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.150  -14.065 11.584  0.60 21.46 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.890  -13.122 10.880  0.40 20.48 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 4.921  -13.203 11.070  0.60 21.46 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.571  -13.693 8.042   0.40 20.31 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.439  -13.208 8.214   0.60 20.87 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.364  -12.198 8.536   0.40 20.31 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.164  -11.836 8.967   0.60 20.87 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.721  -12.618 7.824   0.40 20.31 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.479  -12.012 8.092   0.60 20.87 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.132  -14.596 11.442  0.40 13.47 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.224  -14.423 11.835  0.60 13.75 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.142 -15.609 11.157  0.40 13.66 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.154 -15.456 11.403  0.60 13.83 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.804  -16.232 9.807   0.40 14.44 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.757  -15.963 10.022  0.60 13.30 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.805  -16.945 9.682   0.40 15.47 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.603  -16.346 9.796   0.60 13.50 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.155 -16.654 12.273  0.40 13.40 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.155 -16.602 12.416  0.60 14.43 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.241 -17.719 12.173  0.40 13.21 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.121 -17.739 12.114  0.60 14.71 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.304 -18.558 13.454  0.40 12.85 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.171 -18.699 13.300  0.60 15.08 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.301 -19.709 13.342  0.40 12.80 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.180 -19.821 13.108  0.60 15.36 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.690 -19.236 13.098  0.40 12.95 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.571 -19.317 12.953  0.60 15.76 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.403  -14.921 11.771  0.40 16.17 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.672  -14.662 12.453  0.60 16.50 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.015 -15.192 11.103  0.40 16.39 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.042 -15.073 11.351  0.60 16.59 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.279 -16.189 13.117  0.40 16.08 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.392 -16.234 13.285  0.60 17.31 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.300  -17.106 12.275  0.40 16.08 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.261  -16.971 12.456  0.60 17.31 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.044 -18.310 11.432  0.40 15.85 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.816 -18.226 11.332  0.60 17.65 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.103 -17.292 12.047  0.40 15.85 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.012 -17.382 11.966  0.60 17.65 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.578 -17.992 14.194  0.40 15.42 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.417 -18.202 14.097  0.60 18.09 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.427 -18.935 13.632  0.40 15.42 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.293 -19.098 13.418  0.60 18.09 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.299 -20.215 14.171  0.40 15.36 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.157 -20.403 13.884  0.60 18.43 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.044 -20.282 12.603  0.40 15.36 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.950 -20.321 12.310  0.60 18.43 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.241 -19.930 13.027  0.40 15.54 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.135 -20.000 12.863  0.60 18.92 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.722 -18.764 12.343  0.40 15.54 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.629 -18.798 12.232  0.60 18.92 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.961 -18.721 13.771  0.40 15.54 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.805 -18.842 13.669  0.60 18.92 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.619 -15.945 8.788   0.40 13.50 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.716 -15.980 9.097   0.60 13.21 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.403 -16.573 7.489   0.40 13.29 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.471 -16.473 7.745   0.60 13.88 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.022 -17.959 7.442   0.40 13.01 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.027 -17.874 7.506   0.60 14.36 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.460 -18.876 6.831   0.40 13.74 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.338 -18.710 6.913   0.60 14.77 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.005 -15.723 6.372   0.40 13.05 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.018 -15.496 6.698   0.60 14.35 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.370 -14.354 6.141   0.40 13.55 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.364 -14.111 6.630   0.60 14.61 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.141 -13.611 5.069   0.40 13.91 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 10.976 -13.308 5.492   0.60 15.55 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.902  -14.483 5.756   0.40 13.87 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.847  -14.208 6.471   0.60 14.86 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.285 -15.400 8.820   0.40 16.20 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.517 -15.692 9.232   0.60 15.86 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.451  -16.661 7.331   0.40 15.95 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.515  -16.525 7.618   0.60 16.66 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 11.943 -15.579 6.575   0.40 15.66 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.960 -15.353 6.875   0.60 17.22 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 10.932 -16.223 5.542   0.40 15.66 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.912 -15.902 5.826   0.60 17.22 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.421 -13.839 6.959   0.40 16.26 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.544 -13.634 7.455   0.60 17.53 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.729 -12.744 4.929   0.40 16.70 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.525 -12.450 5.425   0.60 18.65 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.059 -13.499 5.362   0.40 16.70 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.919 -13.170 5.673   0.60 18.65 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.116 -14.126 4.247   0.40 16.70 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.867 -13.800 4.663   0.60 18.65 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.554  -13.605 5.542   0.40 16.64 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.491  -13.325 6.277   0.60 17.82 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.830  -15.064 4.982   0.40 16.64 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.643  -14.813 5.743   0.60 17.82 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.410  -14.863 6.500   0.40 16.64 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.464  -14.541 7.298   0.60 17.82 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.195 -18.107 8.046   0.40 12.64 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.267 -18.136 7.923   0.60 14.50 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 12.923 -19.360 8.029   0.40 12.21 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.908 -19.442 7.776   0.60 14.26 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.640 -19.530 9.359   0.40 11.99 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.705 -19.721 9.046   0.60 14.02 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.522 -18.712 10.276  0.40 12.71 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.620 -18.985 10.034  0.60 14.15 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 13.954 -19.395 6.897   0.40 12.44 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.826 -19.501 6.546   0.60 14.51 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 14.909 -18.355 7.113   0.40 12.17 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.989 -18.698 6.780   0.60 14.63 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.299 -19.236 5.524   0.40 13.30 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.119 -18.997 5.300   0.60 15.06 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.607 -17.472 8.461   0.40 15.17 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.781 -17.554 8.300   0.60 17.39 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.306 -20.094 7.909   0.40 14.65 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.227 -20.129 7.678   0.60 17.11 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.424 -20.237 6.910   0.40 14.92 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.098 -20.424 6.391   0.60 17.41 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.472 -18.333 6.487   0.40 14.60 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.510 -18.738 6.114   0.60 17.55 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.965 -19.347 4.823   0.40 15.96 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.607 -19.279 4.508   0.60 18.07 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.611 -19.912 5.408   0.40 15.96 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.223 -19.361 5.262   0.60 18.07 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 12.897 -18.359 5.439   0.40 15.96 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.071 -18.030 5.315   0.60 18.07 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.406 -20.611 9.436   0.40 11.68 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.513 -20.783 9.012   0.60 14.23 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.247 -20.879 10.588  0.40 12.43 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.367 -21.086 10.152  0.60 15.09 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.073 -19.660 10.976  0.40 12.01 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.211 -19.887 10.570  0.60 13.60 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.239 -19.371 12.167  0.40 12.84 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.490 -19.713 11.762  0.60 14.05 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.157 -22.055 10.243  0.40 14.42 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.286 -22.262 9.818   0.60 18.30 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.074 -22.427 11.379  0.40 16.84 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.354 -22.473 10.863  0.60 22.21 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.582 -22.998 12.374  0.40 16.71 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 17.004 -22.589 12.057  0.60 23.49 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.283 -22.135 11.282  0.40 18.40 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.542 -22.522 10.492  0.60 23.92 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.453 -21.198 8.830   0.40 14.01 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.577 -21.341 8.355   0.60 17.08 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.700 -21.120 11.351  0.40 14.91 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.816 -21.355 10.906  0.60 18.10 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.593 -22.819 10.014  0.40 17.30 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.763 -23.082 9.770   0.60 21.95 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.698 -21.815 9.471   0.40 17.30 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.723 -22.101 8.967   0.60 21.95 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.587 -18.922 9.988   0.40 12.08 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.645 -19.055 9.611   0.60 12.72 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.557 -17.868 10.246  0.40 12.29 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.647 -18.031 9.900   0.60 13.20 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.170 -16.504 9.701   0.40 12.59 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.311 -16.622 9.424   0.60 13.44 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 17.853 -15.530 10.035  0.40 12.36 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.146 -15.727 9.580   0.60 13.85 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 18.940 -18.244 9.679   0.40 12.30 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.013 -18.444 9.325   0.60 12.49 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 18.938 -18.376 8.166   0.40 12.74 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.001 -18.540 7.813   0.60 13.39 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.275 -19.252 7.612   0.40 14.00 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.235 -19.308 7.232   0.60 14.56 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.683 -17.503 7.488   0.40 12.68 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.837 -17.740 7.166   0.60 13.70 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.379 -19.002 9.161   0.40 14.49 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.380 -19.088 8.791   0.60 15.27 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.666 -17.776 11.207  0.40 14.75 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.749 -17.984 10.856  0.60 15.83 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.581 -17.551 9.919   0.40 14.76 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.675 -17.781 9.585   0.60 14.99 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.218 -19.092 10.057  0.40 14.76 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.264 -19.314 9.687   0.60 14.99 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.720 -17.539 6.626   0.40 15.22 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.868 -17.761 6.307   0.60 16.44 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.135 -16.902 7.907   0.40 15.22 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.358 -17.213 7.602   0.60 16.44 ?  15  ASN   A HD22 1 
ATOM   399  N N    . VAL   A 1 16  ? 16.121 -16.388 8.883   1.00 13.33 ?  16  VAL   A N    1 
ATOM   400  C CA   . VAL   A 1 16  ? 15.734 -15.107 8.298   1.00 13.70 ?  16  VAL   A CA   1 
ATOM   401  C C    . VAL   A 1 16  ? 14.453 -14.611 8.956   1.00 13.28 ?  16  VAL   A C    1 
ATOM   402  O O    . VAL   A 1 16  ? 13.454 -15.344 9.040   1.00 13.48 ?  16  VAL   A O    1 
ATOM   403  C CB   . VAL   A 1 16  ? 15.569 -15.178 6.771   1.00 14.17 ?  16  VAL   A CB   1 
ATOM   404  C CG1  . VAL   A 1 16  ? 15.133 -13.808 6.214   1.00 14.91 ?  16  VAL   A CG1  1 
ATOM   405  C CG2  . VAL   A 1 16  ? 16.854 -15.641 6.102   1.00 15.44 ?  16  VAL   A CG2  1 
ATOM   406  H H    A VAL   A 1 16  ? 15.618 -17.045 8.658   0.40 16.00 ?  16  VAL   A H    1 
ATOM   407  H H    B VAL   A 1 16  ? 15.490 -16.972 8.867   0.60 16.00 ?  16  VAL   A H    1 
ATOM   408  H HA   . VAL   A 1 16  ? 16.428 -14.457 8.488   1.00 16.44 ?  16  VAL   A HA   1 
ATOM   409  H HB   . VAL   A 1 16  ? 14.878 -15.817 6.562   1.00 17.01 ?  16  VAL   A HB   1 
ATOM   410  H HG11 . VAL   A 1 16  ? 15.232 -13.819 5.249   1.00 17.89 ?  16  VAL   A HG11 1 
ATOM   411  H HG12 . VAL   A 1 16  ? 14.202 -13.655 6.446   1.00 17.89 ?  16  VAL   A HG12 1 
ATOM   412  H HG13 . VAL   A 1 16  ? 15.690 -13.116 6.597   1.00 17.89 ?  16  VAL   A HG13 1 
ATOM   413  H HG21 . VAL   A 1 16  ? 16.760 -15.558 5.140   1.00 18.53 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 . VAL   A 1 16  ? 17.593 -15.089 6.408   1.00 18.53 ?  16  VAL   A HG22 1 
ATOM   415  H HG23 . VAL   A 1 16  ? 17.019 -16.566 6.341   1.00 18.53 ?  16  VAL   A HG23 1 
ATOM   416  N N    A TYR   A 1 17  ? 14.500 -13.369 9.426   0.40 12.90 ?  17  TYR   A N    1 
ATOM   417  N N    B TYR   A 1 17  ? 14.479 -13.341 9.364   0.60 13.15 ?  17  TYR   A N    1 
ATOM   418  C CA   A TYR   A 1 17  ? 13.386 -12.679 10.052  0.40 13.01 ?  17  TYR   A CA   1 
ATOM   419  C CA   B TYR   A 1 17  ? 13.415 -12.660 10.088  0.60 13.30 ?  17  TYR   A CA   1 
ATOM   420  C C    A TYR   A 1 17  ? 13.118 -11.388 9.289   0.40 12.75 ?  17  TYR   A C    1 
ATOM   421  C C    B TYR   A 1 17  ? 13.165 -11.308 9.430   0.60 13.25 ?  17  TYR   A C    1 
ATOM   422  O O    A TYR   A 1 17  ? 13.989 -10.886 8.574   0.40 12.48 ?  17  TYR   A O    1 
ATOM   423  O O    B TYR   A 1 17  ? 14.098 -10.695 8.913   0.60 12.95 ?  17  TYR   A O    1 
ATOM   424  C CB   A TYR   A 1 17  ? 13.719 -12.357 11.514  0.40 13.66 ?  17  TYR   A CB   1 
ATOM   425  C CB   B TYR   A 1 17  ? 13.854 -12.443 11.539  0.60 13.92 ?  17  TYR   A CB   1 
ATOM   426  C CG   A TYR   A 1 17  ? 13.895 -13.594 12.370  0.40 14.25 ?  17  TYR   A CG   1 
ATOM   427  C CG   B TYR   A 1 17  ? 14.062 -13.730 12.301  0.60 14.74 ?  17  TYR   A CG   1 
ATOM   428  C CD1  A TYR   A 1 17  ? 15.069 -14.345 12.323  0.40 15.23 ?  17  TYR   A CD1  1 
ATOM   429  C CD1  B TYR   A 1 17  ? 15.245 -14.462 12.187  0.60 15.36 ?  17  TYR   A CD1  1 
ATOM   430  C CD2  A TYR   A 1 17  ? 12.881 -14.021 13.214  0.40 14.45 ?  17  TYR   A CD2  1 
ATOM   431  C CD2  B TYR   A 1 17  ? 13.069 -14.224 13.130  0.60 15.37 ?  17  TYR   A CD2  1 
ATOM   432  C CE1  A TYR   A 1 17  ? 15.226 -15.490 13.103  0.40 15.81 ?  17  TYR   A CE1  1 
ATOM   433  C CE1  B TYR   A 1 17  ? 15.424 -15.655 12.885  0.60 15.81 ?  17  TYR   A CE1  1 
ATOM   434  C CE2  A TYR   A 1 17  ? 13.025 -15.165 13.993  0.40 15.30 ?  17  TYR   A CE2  1 
ATOM   435  C CE2  B TYR   A 1 17  ? 13.236 -15.414 13.828  0.60 15.83 ?  17  TYR   A CE2  1 
ATOM   436  C CZ   A TYR   A 1 17  ? 14.198 -15.894 13.935  0.40 15.52 ?  17  TYR   A CZ   1 
ATOM   437  C CZ   B TYR   A 1 17  ? 14.414 -16.123 13.707  0.60 15.78 ?  17  TYR   A CZ   1 
ATOM   438  O OH   A TYR   A 1 17  ? 14.340 -17.027 14.711  0.40 16.19 ?  17  TYR   A OH   1 
ATOM   439  O OH   B TYR   A 1 17  ? 14.578 -17.301 14.407  0.60 16.30 ?  17  TYR   A OH   1 
ATOM   440  H H    A TYR   A 1 17  ? 15.213 -12.879 9.384   0.40 15.47 ?  17  TYR   A H    1 
ATOM   441  H H    B TYR   A 1 17  ? 15.148 -12.816 9.209   0.60 15.78 ?  17  TYR   A H    1 
ATOM   442  H HA   A TYR   A 1 17  ? 12.600 -13.246 10.016  0.40 15.61 ?  17  TYR   A HA   1 
ATOM   443  H HA   B TYR   A 1 17  ? 12.598 -13.180 10.070  0.60 15.96 ?  17  TYR   A HA   1 
ATOM   444  H HB2  A TYR   A 1 17  ? 14.540 -11.844 11.543  0.40 16.39 ?  17  TYR   A HB2  1 
ATOM   445  H HB2  B TYR   A 1 17  ? 14.691 -11.957 11.544  0.60 16.71 ?  17  TYR   A HB2  1 
ATOM   446  H HB3  A TYR   A 1 17  ? 12.993 -11.835 11.883  0.40 16.39 ?  17  TYR   A HB3  1 
ATOM   447  H HB3  B TYR   A 1 17  ? 13.171 -11.937 12.000  0.60 16.71 ?  17  TYR   A HB3  1 
ATOM   448  H HD1  A TYR   A 1 17  ? 15.762 -14.075 11.762  0.40 18.28 ?  17  TYR   A HD1  1 
ATOM   449  H HD1  B TYR   A 1 17  ? 15.927 -14.150 11.633  0.60 18.42 ?  17  TYR   A HD1  1 
ATOM   450  H HD2  A TYR   A 1 17  ? 12.086 -13.541 13.258  0.40 17.33 ?  17  TYR   A HD2  1 
ATOM   451  H HD2  B TYR   A 1 17  ? 12.270 -13.754 13.215  0.60 18.44 ?  17  TYR   A HD2  1 
ATOM   452  H HE1  A TYR   A 1 17  ? 16.020 -15.979 13.063  0.40 18.97 ?  17  TYR   A HE1  1 
ATOM   453  H HE1  B TYR   A 1 17  ? 16.222 -16.130 12.803  0.60 18.97 ?  17  TYR   A HE1  1 
ATOM   454  H HE2  A TYR   A 1 17  ? 12.337 -15.439 14.556  0.40 18.36 ?  17  TYR   A HE2  1 
ATOM   455  H HE2  B TYR   A 1 17  ? 12.557 -15.724 14.381  0.60 19.00 ?  17  TYR   A HE2  1 
ATOM   456  H HH   A TYR   A 1 17  ? 13.586 -17.305 14.949  0.40 19.42 ?  17  TYR   A HH   1 
ATOM   457  H HH   B TYR   A 1 17  ? 15.336 -17.618 14.247  0.60 19.55 ?  17  TYR   A HH   1 
ATOM   458  N N    . ILE   A 1 18  ? 11.913 -10.835 9.447   1.00 13.16 ?  18  ILE   A N    1 
ATOM   459  C CA   . ILE   A 1 18  ? 11.536 -9.617  8.725   1.00 13.32 ?  18  ILE   A CA   1 
ATOM   460  C C    . ILE   A 1 18  ? 10.586 -8.742  9.541   1.00 13.99 ?  18  ILE   A C    1 
ATOM   461  O O    . ILE   A 1 18  ? 9.759  -9.240  10.312  1.00 14.42 ?  18  ILE   A O    1 
ATOM   462  C CB   . ILE   A 1 18  ? 10.963 -9.978  7.336   1.00 13.49 ?  18  ILE   A CB   1 
ATOM   463  C CG1  . ILE   A 1 18  ? 10.953 -8.765  6.407   1.00 14.27 ?  18  ILE   A CG1  1 
ATOM   464  C CG2  . ILE   A 1 18  ? 9.596  -10.641 7.468   1.00 14.63 ?  18  ILE   A CG2  1 
ATOM   465  C CD1  . ILE   A 1 18  ? 10.689 -9.126  4.972   1.00 16.02 ?  18  ILE   A CD1  1 
ATOM   466  H H    A ILE   A 1 18  ? 11.308 -11.139 9.972   0.40 15.79 ?  18  ILE   A H    1 
ATOM   467  H H    B ILE   A 1 18  ? 11.256 -11.225 9.839   0.60 15.79 ?  18  ILE   A H    1 
ATOM   468  H HA   . ILE   A 1 18  ? 12.349 -9.099  8.571   1.00 15.98 ?  18  ILE   A HA   1 
ATOM   469  H HB   . ILE   A 1 18  ? 11.560 -10.625 6.939   1.00 16.19 ?  18  ILE   A HB   1 
ATOM   470  H HG12 . ILE   A 1 18  ? 10.267 -8.147  6.688   1.00 17.12 ?  18  ILE   A HG12 1 
ATOM   471  H HG13 . ILE   A 1 18  ? 11.825 -8.329  6.440   1.00 17.12 ?  18  ILE   A HG13 1 
ATOM   472  H HG21 . ILE   A 1 18  ? 9.314  -10.954 6.595   1.00 17.56 ?  18  ILE   A HG21 1 
ATOM   473  H HG22 . ILE   A 1 18  ? 9.668  -11.381 8.083   1.00 17.56 ?  18  ILE   A HG22 1 
ATOM   474  H HG23 . ILE   A 1 18  ? 8.959  -9.988  7.803   1.00 17.56 ?  18  ILE   A HG23 1 
ATOM   475  H HD11 . ILE   A 1 18  ? 10.774 -8.328  4.421   1.00 19.22 ?  18  ILE   A HD11 1 
ATOM   476  H HD12 . ILE   A 1 18  ? 11.332 -9.792  4.685   1.00 19.22 ?  18  ILE   A HD12 1 
ATOM   477  H HD13 . ILE   A 1 18  ? 9.789  -9.480  4.896   1.00 19.22 ?  18  ILE   A HD13 1 
ATOM   478  N N    A LYS   A 1 19  ? 10.718 -7.423  9.374   0.40 14.01 ?  19  LYS   A N    1 
ATOM   479  N N    B LYS   A 1 19  ? 10.701 -7.426  9.329   0.60 13.86 ?  19  LYS   A N    1 
ATOM   480  C CA   A LYS   A 1 19  ? 9.951  -6.473  10.171  0.40 14.68 ?  19  LYS   A CA   1 
ATOM   481  C CA   B LYS   A 1 19  ? 9.871  -6.441  10.009  0.60 14.72 ?  19  LYS   A CA   1 
ATOM   482  C C    A LYS   A 1 19  ? 9.769  -5.185  9.383   0.40 14.25 ?  19  LYS   A C    1 
ATOM   483  C C    B LYS   A 1 19  ? 9.667  -5.239  9.098   0.60 14.46 ?  19  LYS   A C    1 
ATOM   484  O O    A LYS   A 1 19  ? 10.703 -4.724  8.724   0.40 13.88 ?  19  LYS   A O    1 
ATOM   485  O O    B LYS   A 1 19  ? 10.540 -4.906  8.293   0.60 13.83 ?  19  LYS   A O    1 
ATOM   486  C CB   A LYS   A 1 19  ? 10.685 -6.178  11.486  0.40 15.63 ?  19  LYS   A CB   1 
ATOM   487  C CB   B LYS   A 1 19  ? 10.557 -5.971  11.295  0.60 15.37 ?  19  LYS   A CB   1 
ATOM   488  C CG   A LYS   A 1 19  ? 10.006 -5.195  12.426  0.40 15.96 ?  19  LYS   A CG   1 
ATOM   489  C CG   B LYS   A 1 19  ? 9.725  -5.071  12.185  0.60 16.41 ?  19  LYS   A CG   1 
ATOM   490  C CD   A LYS   A 1 19  ? 10.883 -4.984  13.652  0.40 16.35 ?  19  LYS   A CD   1 
ATOM   491  C CD   B LYS   A 1 19  ? 10.510 -4.713  13.433  0.60 17.48 ?  19  LYS   A CD   1 
ATOM   492  C CE   A LYS   A 1 19  ? 10.242 -4.067  14.674  0.40 16.38 ?  19  LYS   A CE   1 
ATOM   493  C CE   B LYS   A 1 19  ? 9.744  -3.785  14.355  0.60 18.20 ?  19  LYS   A CE   1 
ATOM   494  N NZ   A LYS   A 1 19  ? 11.139 -3.868  15.846  0.40 16.30 ?  19  LYS   A NZ   1 
ATOM   495  N NZ   B LYS   A 1 19  ? 10.584 -3.402  15.521  0.60 18.21 ?  19  LYS   A NZ   1 
ATOM   496  H H    A LYS   A 1 19  ? 11.255 -7.047  8.804   0.40 16.81 ?  19  LYS   A H    1 
ATOM   497  H H    B LYS   A 1 19  ? 11.277 -7.075  8.782   0.60 16.63 ?  19  LYS   A H    1 
ATOM   498  H HA   A LYS   A 1 19  ? 9.082  -6.837  10.373  0.40 17.61 ?  19  LYS   A HA   1 
ATOM   499  H HA   B LYS   A 1 19  ? 9.014  -6.834  10.222  0.60 17.66 ?  19  LYS   A HA   1 
ATOM   500  H HB2  A LYS   A 1 19  ? 10.782 -7.011  11.971  0.40 18.75 ?  19  LYS   A HB2  1 
ATOM   501  H HB2  B LYS   A 1 19  ? 10.799 -6.753  11.813  0.60 18.44 ?  19  LYS   A HB2  1 
ATOM   502  H HB3  A LYS   A 1 19  ? 11.562 -5.819  11.280  0.40 18.75 ?  19  LYS   A HB3  1 
ATOM   503  H HB3  B LYS   A 1 19  ? 11.359 -5.482  11.051  0.60 18.44 ?  19  LYS   A HB3  1 
ATOM   504  H HG2  A LYS   A 1 19  ? 9.886  -4.340  11.982  0.40 19.15 ?  19  LYS   A HG2  1 
ATOM   505  H HG2  B LYS   A 1 19  ? 9.507  -4.254  11.711  0.60 19.69 ?  19  LYS   A HG2  1 
ATOM   506  H HG3  A LYS   A 1 19  ? 9.151  -5.554  12.715  0.40 19.15 ?  19  LYS   A HG3  1 
ATOM   507  H HG3  B LYS   A 1 19  ? 8.915  -5.536  12.451  0.60 19.69 ?  19  LYS   A HG3  1 
ATOM   508  H HD2  A LYS   A 1 19  ? 11.045 -5.841  14.076  0.40 19.62 ?  19  LYS   A HD2  1 
ATOM   509  H HD2  B LYS   A 1 19  ? 10.713 -5.527  13.924  0.60 20.98 ?  19  LYS   A HD2  1 
ATOM   510  H HD3  A LYS   A 1 19  ? 11.723 -4.585  13.374  0.40 19.62 ?  19  LYS   A HD3  1 
ATOM   511  H HD3  B LYS   A 1 19  ? 11.334 -4.270  13.173  0.60 20.98 ?  19  LYS   A HD3  1 
ATOM   512  H HE2  A LYS   A 1 19  ? 10.072 -3.202  14.268  0.40 19.66 ?  19  LYS   A HE2  1 
ATOM   513  H HE2  B LYS   A 1 19  ? 9.501  -2.979  13.873  0.60 21.83 ?  19  LYS   A HE2  1 
ATOM   514  H HE3  A LYS   A 1 19  ? 9.413  -4.463  14.986  0.40 19.66 ?  19  LYS   A HE3  1 
ATOM   515  H HE3  B LYS   A 1 19  ? 8.951  -4.237  14.683  0.60 21.83 ?  19  LYS   A HE3  1 
ATOM   516  H HZ1  A LYS   A 1 19  ? 10.747 -3.336  16.441  0.40 19.56 ?  19  LYS   A HZ1  1 
ATOM   517  H HZ1  B LYS   A 1 19  ? 10.129 -2.857  16.058  0.60 21.84 ?  19  LYS   A HZ1  1 
ATOM   518  H HZ2  A LYS   A 1 19  ? 11.316 -4.651  16.229  0.40 19.56 ?  19  LYS   A HZ2  1 
ATOM   519  H HZ2  B LYS   A 1 19  ? 10.821 -4.127  15.978  0.60 21.84 ?  19  LYS   A HZ2  1 
ATOM   520  H HZ3  A LYS   A 1 19  ? 11.903 -3.495  15.584  0.40 19.56 ?  19  LYS   A HZ3  1 
ATOM   521  H HZ3  B LYS   A 1 19  ? 11.319 -2.983  15.242  0.60 21.84 ?  19  LYS   A HZ3  1 
ATOM   522  N N    A ASN   A 1 20  ? 8.565  -4.612  9.443   0.40 14.48 ?  20  ASN   A N    1 
ATOM   523  N N    B ASN   A 1 20  ? 8.507  -4.590  9.233   0.60 15.27 ?  20  ASN   A N    1 
ATOM   524  C CA   A ASN   A 1 20  ? 8.331  -3.283  8.882   0.40 14.59 ?  20  ASN   A CA   1 
ATOM   525  C CA   B ASN   A 1 20  ? 8.233  -3.315  8.563   0.60 15.63 ?  20  ASN   A CA   1 
ATOM   526  C C    A ASN   A 1 20  ? 8.920  -2.264  9.846   0.40 14.46 ?  20  ASN   A C    1 
ATOM   527  C C    B ASN   A 1 20  ? 8.791  -2.202  9.444   0.60 16.19 ?  20  ASN   A C    1 
ATOM   528  O O    A ASN   A 1 20  ? 8.365  -2.024  10.923  0.40 14.09 ?  20  ASN   A O    1 
ATOM   529  O O    B ASN   A 1 20  ? 8.140  -1.764  10.398  0.60 16.91 ?  20  ASN   A O    1 
ATOM   530  C CB   A ASN   A 1 20  ? 6.839  -3.048  8.663   0.40 15.06 ?  20  ASN   A CB   1 
ATOM   531  C CB   B ASN   A 1 20  ? 6.728  -3.160  8.347   0.60 15.53 ?  20  ASN   A CB   1 
ATOM   532  C CG   A ASN   A 1 20  ? 6.509  -1.610  8.279   0.40 15.92 ?  20  ASN   A CG   1 
ATOM   533  C CG   B ASN   A 1 20  ? 6.334  -1.836  7.689   0.60 15.16 ?  20  ASN   A CG   1 
ATOM   534  O OD1  A ASN   A 1 20  ? 5.535  -1.046  8.771   0.40 17.43 ?  20  ASN   A OD1  1 
ATOM   535  O OD1  B ASN   A 1 20  ? 5.188  -1.387  7.837   0.60 15.32 ?  20  ASN   A OD1  1 
ATOM   536  N ND2  A ASN   A 1 20  ? 7.313  -1.014  7.404   0.40 15.79 ?  20  ASN   A ND2  1 
ATOM   537  N ND2  B ASN   A 1 20  ? 7.255  -1.222  6.947   0.60 15.88 ?  20  ASN   A ND2  1 
ATOM   538  H H    A ASN   A 1 20  ? 7.871  -4.973  9.796   0.40 17.38 ?  20  ASN   A H    1 
ATOM   539  H H    B ASN   A 1 20  ? 7.854  -4.880  9.706   0.60 18.32 ?  20  ASN   A H    1 
ATOM   540  H HA   A ASN   A 1 20  ? 8.785  -3.207  8.033   0.40 17.50 ?  20  ASN   A HA   1 
ATOM   541  H HA   B ASN   A 1 20  ? 8.678  -3.292  7.700   0.60 18.76 ?  20  ASN   A HA   1 
ATOM   542  H HB2  A ASN   A 1 20  ? 6.532  -3.626  7.947   0.40 18.07 ?  20  ASN   A HB2  1 
ATOM   543  H HB2  B ASN   A 1 20  ? 6.407  -3.875  7.780   0.60 18.64 ?  20  ASN   A HB2  1 
ATOM   544  H HB3  A ASN   A 1 20  ? 6.362  -3.255  9.481   0.40 18.07 ?  20  ASN   A HB3  1 
ATOM   545  H HB3  B ASN   A 1 20  ? 6.280  -3.205  9.204   0.60 18.64 ?  20  ASN   A HB3  1 
ATOM   546  H HD21 A ASN   A 1 20  ? 7.154  -0.204  7.157   0.40 18.95 ?  20  ASN   A HD21 1 
ATOM   547  H HD21 B ASN   A 1 20  ? 7.067  -0.481  6.562   0.60 19.05 ?  20  ASN   A HD21 1 
ATOM   548  H HD22 A ASN   A 1 20  ? 7.989  -1.435  7.082   0.40 18.95 ?  20  ASN   A HD22 1 
ATOM   549  H HD22 B ASN   A 1 20  ? 8.037  -1.568  6.852   0.60 19.05 ?  20  ASN   A HD22 1 
ATOM   550  N N    A ALA   A 1 21  ? 10.058 -1.683  9.476   0.40 15.17 ?  21  ALA   A N    1 
ATOM   551  N N    B ALA   A 1 21  ? 10.003 -1.742  9.129   0.60 16.27 ?  21  ALA   A N    1 
ATOM   552  C CA   A ALA   A 1 21  ? 10.758 -0.808  10.398  0.40 15.59 ?  21  ALA   A CA   1 
ATOM   553  C CA   B ALA   A 1 21  ? 10.664 -0.736  9.948   0.60 16.10 ?  21  ALA   A CA   1 
ATOM   554  C C    A ALA   A 1 21  ? 11.780 0.015   9.638   0.40 15.59 ?  21  ALA   A C    1 
ATOM   555  C C    B ALA   A 1 21  ? 11.738 -0.034  9.132   0.60 14.82 ?  21  ALA   A C    1 
ATOM   556  O O    A ALA   A 1 21  ? 12.324 -0.426  8.623   0.40 15.96 ?  21  ALA   A O    1 
ATOM   557  O O    B ALA   A 1 21  ? 12.195 -0.539  8.103   0.60 14.56 ?  21  ALA   A O    1 
ATOM   558  C CB   A ALA   A 1 21  ? 11.457 -1.614  11.496  0.40 16.65 ?  21  ALA   A CB   1 
ATOM   559  C CB   B ALA   A 1 21  ? 11.295 -1.347  11.203  0.60 17.28 ?  21  ALA   A CB   1 
ATOM   560  H H    A ALA   A 1 21  ? 10.440 -1.782  8.708   0.40 18.20 ?  21  ALA   A H    1 
ATOM   561  H H    B ALA   A 1 21  ? 10.455 -2.007  8.448   0.60 19.52 ?  21  ALA   A H    1 
ATOM   562  H HA   A ALA   A 1 21  ? 10.123 -0.204  10.812  0.40 18.70 ?  21  ALA   A HA   1 
ATOM   563  H HA   B ALA   A 1 21  ? 10.006 -0.081  10.226  0.60 19.31 ?  21  ALA   A HA   1 
ATOM   564  H HB1  A ALA   A 1 21  ? 11.872 -0.998  12.116  0.40 19.98 ?  21  ALA   A HB1  1 
ATOM   565  H HB1  B ALA   A 1 21  ? 11.722 -0.641  11.714  0.60 20.73 ?  21  ALA   A HB1  1 
ATOM   566  H HB2  A ALA   A 1 21  ? 10.795 -2.153  11.956  0.40 19.98 ?  21  ALA   A HB2  1 
ATOM   567  H HB2  B ALA   A 1 21  ? 10.601 -1.767  11.736  0.60 20.73 ?  21  ALA   A HB2  1 
ATOM   568  H HB3  A ALA   A 1 21  ? 12.126 -2.185  11.090  0.40 19.98 ?  21  ALA   A HB3  1 
ATOM   569  H HB3  B ALA   A 1 21  ? 11.954 -2.007  10.937  0.60 20.73 ?  21  ALA   A HB3  1 
ATOM   570  N N    A ASP   A 1 22  ? 12.020 1.220   10.147  0.40 15.72 ?  22  ASP   A N    1 
ATOM   571  N N    B ASP   A 1 22  ? 12.122 1.149   9.618   0.60 14.94 ?  22  ASP   A N    1 
ATOM   572  C CA   A ASP   A 1 22  ? 13.091 2.076   9.661   0.40 15.74 ?  22  ASP   A CA   1 
ATOM   573  C CA   B ASP   A 1 22  ? 13.288 1.882   9.131   0.60 14.81 ?  22  ASP   A CA   1 
ATOM   574  C C    A ASP   A 1 22  ? 14.415 1.533   10.182  0.40 14.92 ?  22  ASP   A C    1 
ATOM   575  C C    B ASP   A 1 22  ? 14.531 1.283   9.781   0.60 13.50 ?  22  ASP   A C    1 
ATOM   576  O O    A ASP   A 1 22  ? 14.643 1.511   11.395  0.40 15.41 ?  22  ASP   A O    1 
ATOM   577  O O    B ASP   A 1 22  ? 14.621 1.227   11.011  0.60 14.23 ?  22  ASP   A O    1 
ATOM   578  C CB   A ASP   A 1 22  ? 12.874 3.493   10.183  0.40 16.87 ?  22  ASP   A CB   1 
ATOM   579  C CB   B ASP   A 1 22  ? 13.146 3.354   9.532   0.60 16.18 ?  22  ASP   A CB   1 
ATOM   580  C CG   A ASP   A 1 22  ? 13.850 4.497   9.585   0.40 17.77 ?  22  ASP   A CG   1 
ATOM   581  C CG   B ASP   A 1 22  ? 14.232 4.255   8.948   0.60 16.78 ?  22  ASP   A CG   1 
ATOM   582  O OD1  A ASP   A 1 22  ? 14.917 4.084   9.086   0.40 17.71 ?  22  ASP   A OD1  1 
ATOM   583  O OD1  B ASP   A 1 22  ? 15.270 3.742   8.482   0.60 15.80 ?  22  ASP   A OD1  1 
ATOM   584  O OD2  A ASP   A 1 22  ? 13.549 5.709   9.619   0.40 18.55 -1 22  ASP   A OD2  1 
ATOM   585  O OD2  B ASP   A 1 22  ? 14.050 5.494   8.975   0.60 18.62 -1 22  ASP   A OD2  1 
ATOM   586  H H    A ASP   A 1 22  ? 11.561 1.570   10.785  0.40 18.86 ?  22  ASP   A H    1 
ATOM   587  H H    B ASP   A 1 22  ? 11.698 1.560   10.246  0.60 17.92 ?  22  ASP   A H    1 
ATOM   588  H HA   A ASP   A 1 22  ? 13.107 2.086   8.690   0.40 18.88 ?  22  ASP   A HA   1 
ATOM   589  H HA   B ASP   A 1 22  ? 13.355 1.808   8.166   0.60 17.78 ?  22  ASP   A HA   1 
ATOM   590  H HB2  A ASP   A 1 22  ? 11.973 3.776   9.962   0.40 20.24 ?  22  ASP   A HB2  1 
ATOM   591  H HB2  B ASP   A 1 22  ? 12.294 3.683   9.218   0.60 19.41 ?  22  ASP   A HB2  1 
ATOM   592  H HB3  A ASP   A 1 22  ? 12.984 3.487   11.152  0.40 20.24 ?  22  ASP   A HB3  1 
ATOM   593  H HB3  B ASP   A 1 22  ? 13.192 3.416   10.500  0.60 19.41 ?  22  ASP   A HB3  1 
ATOM   594  N N    A ILE   A 1 23  ? 15.287 1.100   9.269   0.40 14.12 ?  23  ILE   A N    1 
ATOM   595  N N    B ILE   A 1 23  ? 15.486 0.830   8.962   0.60 12.87 ?  23  ILE   A N    1 
ATOM   596  C CA   A ILE   A 1 23  ? 16.556 0.507   9.683   0.40 13.37 ?  23  ILE   A CA   1 
ATOM   597  C CA   B ILE   A 1 23  ? 16.702 0.210   9.487   0.60 12.62 ?  23  ILE   A CA   1 
ATOM   598  C C    A ILE   A 1 23  ? 17.358 1.476   10.542  0.40 13.29 ?  23  ILE   A C    1 
ATOM   599  C C    B ILE   A 1 23  ? 17.434 1.162   10.422  0.60 13.31 ?  23  ILE   A C    1 
ATOM   600  O O    A ILE   A 1 23  ? 18.123 1.053   11.416  0.40 13.70 ?  23  ILE   A O    1 
ATOM   601  O O    B ILE   A 1 23  ? 18.076 0.725   11.386  0.60 13.88 ?  23  ILE   A O    1 
ATOM   602  C CB   A ILE   A 1 23  ? 17.350 0.006   8.459   0.40 12.73 ?  23  ILE   A CB   1 
ATOM   603  C CB   B ILE   A 1 23  ? 17.605 -0.309  8.341   0.60 11.81 ?  23  ILE   A CB   1 
ATOM   604  C CG1  A ILE   A 1 23  ? 18.516 -0.874  8.913   0.40 12.45 ?  23  ILE   A CG1  1 
ATOM   605  C CG1  B ILE   A 1 23  ? 18.675 -1.266  8.887   0.60 12.10 ?  23  ILE   A CG1  1 
ATOM   606  C CG2  A ILE   A 1 23  ? 17.823 1.180   7.602   0.40 12.84 ?  23  ILE   A CG2  1 
ATOM   607  C CG2  B ILE   A 1 23  ? 18.244 0.842   7.573   0.60 11.81 ?  23  ILE   A CG2  1 
ATOM   608  C CD1  A ILE   A 1 23  ? 19.219 -1.599  7.788   0.40 12.18 ?  23  ILE   A CD1  1 
ATOM   609  C CD1  B ILE   A 1 23  ? 19.539 -1.921  7.810   0.60 12.39 ?  23  ILE   A CD1  1 
ATOM   610  H H    A ILE   A 1 23  ? 15.167 1.143   8.422   0.40 16.95 ?  23  ILE   A H    1 
ATOM   611  H H    B ILE   A 1 23  ? 15.462 0.874   8.118   0.60 15.44 ?  23  ILE   A H    1 
ATOM   612  H HA   A ILE   A 1 23  ? 16.363 -0.268  10.229  0.40 16.04 ?  23  ILE   A HA   1 
ATOM   613  H HA   B ILE   A 1 23  ? 16.444 -0.563  10.009  0.60 15.14 ?  23  ILE   A HA   1 
ATOM   614  H HB   A ILE   A 1 23  ? 16.758 -0.534  7.917   0.40 15.27 ?  23  ILE   A HB   1 
ATOM   615  H HB   B ILE   A 1 23  ? 17.054 -0.810  7.720   0.60 14.17 ?  23  ILE   A HB   1 
ATOM   616  H HG12 A ILE   A 1 23  ? 19.172 -0.320  9.362   0.40 14.93 ?  23  ILE   A HG12 1 
ATOM   617  H HG12 B ILE   A 1 23  ? 19.266 -0.774  9.478   0.60 14.52 ?  23  ILE   A HG12 1 
ATOM   618  H HG13 A ILE   A 1 23  ? 18.177 -1.544  9.528   0.40 14.93 ?  23  ILE   A HG13 1 
ATOM   619  H HG13 B ILE   A 1 23  ? 18.235 -1.977  9.381   0.60 14.52 ?  23  ILE   A HG13 1 
ATOM   620  H HG21 A ILE   A 1 23  ? 18.180 0.839   6.765   0.40 15.40 ?  23  ILE   A HG21 1 
ATOM   621  H HG21 B ILE   A 1 23  ? 18.636 0.500   6.750   0.60 14.17 ?  23  ILE   A HG21 1 
ATOM   622  H HG22 A ILE   A 1 23  ? 17.069 1.765   7.420   0.40 15.40 ?  23  ILE   A HG22 1 
ATOM   623  H HG22 B ILE   A 1 23  ? 17.564 1.498   7.365   0.60 14.17 ?  23  ILE   A HG22 1 
ATOM   624  H HG23 A ILE   A 1 23  ? 18.511 1.669   8.078   0.40 15.40 ?  23  ILE   A HG23 1 
ATOM   625  H HG23 B ILE   A 1 23  ? 18.938 1.246   8.120   0.60 14.17 ?  23  ILE   A HG23 1 
ATOM   626  H HD11 A ILE   A 1 23  ? 19.909 -2.168  8.164   0.40 14.62 ?  23  ILE   A HD11 1 
ATOM   627  H HD11 B ILE   A 1 23  ? 20.130 -2.571  8.230   0.60 14.87 ?  23  ILE   A HD11 1 
ATOM   628  H HD12 A ILE   A 1 23  ? 18.572 -2.137  7.307   0.40 14.62 ?  23  ILE   A HD12 1 
ATOM   629  H HD12 B ILE   A 1 23  ? 18.965 -2.366  7.169   0.60 14.87 ?  23  ILE   A HD12 1 
ATOM   630  H HD13 A ILE   A 1 23  ? 19.616 -0.946  7.192   0.40 14.62 ?  23  ILE   A HD13 1 
ATOM   631  H HD13 B ILE   A 1 23  ? 20.067 -1.239  7.367   0.60 14.87 ?  23  ILE   A HD13 1 
ATOM   632  N N    A VAL   A 1 24  ? 17.196 2.781   10.316  0.40 13.96 ?  24  VAL   A N    1 
ATOM   633  N N    B VAL   A 1 24  ? 17.344 2.468   10.166  0.60 14.28 ?  24  VAL   A N    1 
ATOM   634  C CA   A VAL   A 1 24  ? 17.873 3.769   11.154  0.40 15.09 ?  24  VAL   A CA   1 
ATOM   635  C CA   B VAL   A 1 24  ? 18.007 3.448   11.022  0.60 15.63 ?  24  VAL   A CA   1 
ATOM   636  C C    A VAL   A 1 24  ? 17.366 3.689   12.587  0.40 16.07 ?  24  VAL   A C    1 
ATOM   637  C C    B VAL   A 1 24  ? 17.416 3.410   12.424  0.60 16.48 ?  24  VAL   A C    1 
ATOM   638  O O    A VAL   A 1 24  ? 18.152 3.628   13.541  0.40 16.22 ?  24  VAL   A O    1 
ATOM   639  O O    B VAL   A 1 24  ? 18.144 3.411   13.425  0.60 16.90 ?  24  VAL   A O    1 
ATOM   640  C CB   A VAL   A 1 24  ? 17.700 5.182   10.569  0.40 15.52 ?  24  VAL   A CB   1 
ATOM   641  C CB   B VAL   A 1 24  ? 17.909 4.851   10.397  0.60 16.63 ?  24  VAL   A CB   1 
ATOM   642  C CG1  A VAL   A 1 24  ? 18.172 6.232   11.569  0.40 15.70 ?  24  VAL   A CG1  1 
ATOM   643  C CG1  B VAL   A 1 24  ? 18.538 5.883   11.317  0.60 18.13 ?  24  VAL   A CG1  1 
ATOM   644  C CG2  A VAL   A 1 24  ? 18.451 5.310   9.255   0.40 15.82 ?  24  VAL   A CG2  1 
ATOM   645  C CG2  B VAL   A 1 24  ? 18.572 4.858   9.030   0.60 16.93 ?  24  VAL   A CG2  1 
ATOM   646  H H    A VAL   A 1 24  ? 16.715 3.115   9.687   0.40 16.75 ?  24  VAL   A H    1 
ATOM   647  H H    B VAL   A 1 24  ? 16.903 2.808   9.514   0.60 17.14 ?  24  VAL   A H    1 
ATOM   648  H HA   A VAL   A 1 24  ? 18.821 3.572   11.167  0.40 18.11 ?  24  VAL   A HA   1 
ATOM   649  H HA   B VAL   A 1 24  ? 18.947 3.221   11.092  0.60 18.75 ?  24  VAL   A HA   1 
ATOM   650  H HB   A VAL   A 1 24  ? 16.759 5.341   10.393  0.40 18.63 ?  24  VAL   A HB   1 
ATOM   651  H HB   B VAL   A 1 24  ? 16.974 5.082   10.277  0.60 19.96 ?  24  VAL   A HB   1 
ATOM   652  H HG11 A VAL   A 1 24  ? 18.328 7.066   11.099  0.40 18.84 ?  24  VAL   A HG11 1 
ATOM   653  H HG11 B VAL   A 1 24  ? 18.664 6.708   10.824  0.60 21.75 ?  24  VAL   A HG11 1 
ATOM   654  H HG12 A VAL   A 1 24  ? 17.490 6.358   12.246  0.40 18.84 ?  24  VAL   A HG12 1 
ATOM   655  H HG12 B VAL   A 1 24  ? 17.947 6.036   12.072  0.60 21.75 ?  24  VAL   A HG12 1 
ATOM   656  H HG13 A VAL   A 1 24  ? 18.998 5.928   11.979  0.40 18.84 ?  24  VAL   A HG13 1 
ATOM   657  H HG13 B VAL   A 1 24  ? 19.394 5.548   11.626  0.60 21.75 ?  24  VAL   A HG13 1 
ATOM   658  H HG21 A VAL   A 1 24  ? 18.135 6.099   8.787   0.40 18.98 ?  24  VAL   A HG21 1 
ATOM   659  H HG21 B VAL   A 1 24  ? 18.606 5.768   8.701   0.60 20.31 ?  24  VAL   A HG21 1 
ATOM   660  H HG22 A VAL   A 1 24  ? 19.399 5.395   9.440   0.40 18.98 ?  24  VAL   A HG22 1 
ATOM   661  H HG22 B VAL   A 1 24  ? 19.472 4.504   9.117   0.60 20.31 ?  24  VAL   A HG22 1 
ATOM   662  H HG23 A VAL   A 1 24  ? 18.285 4.520   8.716   0.40 18.98 ?  24  VAL   A HG23 1 
ATOM   663  H HG23 B VAL   A 1 24  ? 18.057 4.303   8.425   0.60 20.31 ?  24  VAL   A HG23 1 
ATOM   664  N N    A GLU   A 1 25  ? 16.041 3.702   12.760  0.40 17.00 ?  25  GLU   A N    1 
ATOM   665  N N    B GLU   A 1 25  ? 16.084 3.369   12.515  0.60 16.66 ?  25  GLU   A N    1 
ATOM   666  C CA   A GLU   A 1 25  ? 15.474 3.644   14.103  0.40 18.06 ?  25  GLU   A CA   1 
ATOM   667  C CA   B GLU   A 1 25  ? 15.426 3.298   13.815  0.60 18.03 ?  25  GLU   A CA   1 
ATOM   668  C C    A GLU   A 1 25  ? 15.695 2.285   14.749  0.40 17.17 ?  25  GLU   A C    1 
ATOM   669  C C    B GLU   A 1 25  ? 15.701 1.963   14.498  0.60 17.36 ?  25  GLU   A C    1 
ATOM   670  O O    A GLU   A 1 25  ? 15.869 2.206   15.971  0.40 17.60 ?  25  GLU   A O    1 
ATOM   671  O O    B GLU   A 1 25  ? 15.928 1.919   15.713  0.60 18.18 ?  25  GLU   A O    1 
ATOM   672  C CB   A GLU   A 1 25  ? 13.985 3.992   14.060  0.40 20.07 ?  25  GLU   A CB   1 
ATOM   673  C CB   B GLU   A 1 25  ? 13.924 3.551   13.655  0.60 20.18 ?  25  GLU   A CB   1 
ATOM   674  C CG   A GLU   A 1 25  ? 13.721 5.448   13.711  0.40 22.22 ?  25  GLU   A CG   1 
ATOM   675  C CG   B GLU   A 1 25  ? 13.600 4.949   13.150  0.60 23.03 ?  25  GLU   A CG   1 
ATOM   676  C CD   A GLU   A 1 25  ? 14.505 6.413   14.590  0.40 24.20 ?  25  GLU   A CD   1 
ATOM   677  C CD   B GLU   A 1 25  ? 14.163 6.027   14.047  0.60 25.66 ?  25  GLU   A CD   1 
ATOM   678  O OE1  A GLU   A 1 25  ? 14.571 6.186   15.817  0.40 24.74 ?  25  GLU   A OE1  1 
ATOM   679  O OE1  B GLU   A 1 25  ? 14.133 5.845   15.284  0.60 26.79 ?  25  GLU   A OE1  1 
ATOM   680  O OE2  A GLU   A 1 25  ? 15.077 7.384   14.051  0.40 25.31 -1 25  GLU   A OE2  1 
ATOM   681  O OE2  B GLU   A 1 25  ? 14.642 7.049   13.517  0.60 26.89 -1 25  GLU   A OE2  1 
ATOM   682  H H    A GLU   A 1 25  ? 15.461 3.758   12.126  0.40 20.40 ?  25  GLU   A H    1 
ATOM   683  H H    B GLU   A 1 25  ? 15.549 3.382   11.844  0.60 19.99 ?  25  GLU   A H    1 
ATOM   684  H HA   A GLU   A 1 25  ? 15.923 4.299   14.658  0.40 21.67 ?  25  GLU   A HA   1 
ATOM   685  H HA   B GLU   A 1 25  ? 15.785 3.990   14.386  0.60 21.64 ?  25  GLU   A HA   1 
ATOM   686  H HB2  A GLU   A 1 25  ? 13.550 3.440   13.387  0.40 24.09 ?  25  GLU   A HB2  1 
ATOM   687  H HB2  B GLU   A 1 25  ? 13.560 2.919   13.016  0.60 24.21 ?  25  GLU   A HB2  1 
ATOM   688  H HB3  A GLU   A 1 25  ? 13.593 3.818   14.930  0.40 24.09 ?  25  GLU   A HB3  1 
ATOM   689  H HB3  B GLU   A 1 25  ? 13.489 3.442   14.514  0.60 24.21 ?  25  GLU   A HB3  1 
ATOM   690  H HG2  A GLU   A 1 25  ? 13.983 5.602   12.791  0.40 26.67 ?  25  GLU   A HG2  1 
ATOM   691  H HG2  B GLU   A 1 25  ? 13.979 5.067   12.264  0.60 27.63 ?  25  GLU   A HG2  1 
ATOM   692  H HG3  A GLU   A 1 25  ? 12.774 5.630   13.825  0.40 26.67 ?  25  GLU   A HG3  1 
ATOM   693  H HG3  B GLU   A 1 25  ? 12.638 5.067   13.118  0.60 27.63 ?  25  GLU   A HG3  1 
ATOM   694  N N    A GLU   A 1 26  ? 15.692 1.212   13.955  0.40 16.68 ?  26  GLU   A N    1 
ATOM   695  N N    B GLU   A 1 26  ? 15.690 0.865   13.737  0.60 17.26 ?  26  GLU   A N    1 
ATOM   696  C CA   A GLU   A 1 26  ? 15.998 -0.108  14.497  0.40 16.38 ?  26  GLU   A CA   1 
ATOM   697  C CA   B GLU   A 1 26  ? 16.050 -0.429  14.312  0.60 17.35 ?  26  GLU   A CA   1 
ATOM   698  C C    A GLU   A 1 26  ? 17.420 -0.153  15.037  0.40 15.74 ?  26  GLU   A C    1 
ATOM   699  C C    B GLU   A 1 26  ? 17.471 -0.409  14.856  0.60 16.74 ?  26  GLU   A C    1 
ATOM   700  O O    A GLU   A 1 26  ? 17.656 -0.597  16.167  0.40 15.70 ?  26  GLU   A O    1 
ATOM   701  O O    B GLU   A 1 26  ? 17.745 -0.970  15.923  0.60 17.25 ?  26  GLU   A O    1 
ATOM   702  C CB   A GLU   A 1 26  ? 15.818 -1.175  13.416  0.40 16.99 ?  26  GLU   A CB   1 
ATOM   703  C CB   B GLU   A 1 26  ? 15.899 -1.536  13.268  0.60 18.21 ?  26  GLU   A CB   1 
ATOM   704  C CG   A GLU   A 1 26  ? 14.401 -1.657  13.224  0.40 18.45 ?  26  GLU   A CG   1 
ATOM   705  C CG   B GLU   A 1 26  ? 14.467 -1.912  12.968  0.60 19.71 ?  26  GLU   A CG   1 
ATOM   706  C CD   A GLU   A 1 26  ? 13.918 -2.532  14.364  0.40 19.21 ?  26  GLU   A CD   1 
ATOM   707  C CD   B GLU   A 1 26  ? 13.739 -2.442  14.178  0.60 20.35 ?  26  GLU   A CD   1 
ATOM   708  O OE1  A GLU   A 1 26  ? 14.383 -3.688  14.490  0.40 19.37 ?  26  GLU   A OE1  1 
ATOM   709  O OE1  B GLU   A 1 26  ? 14.238 -3.399  14.810  0.60 20.62 ?  26  GLU   A OE1  1 
ATOM   710  O OE2  A GLU   A 1 26  ? 13.073 -2.055  15.142  0.40 19.37 -1 26  GLU   A OE2  1 
ATOM   711  O OE2  B GLU   A 1 26  ? 12.676 -1.881  14.504  0.60 20.00 -1 26  GLU   A OE2  1 
ATOM   712  H H    A GLU   A 1 26  ? 15.519 1.227   13.113  0.40 20.02 ?  26  GLU   A H    1 
ATOM   713  H H    B GLU   A 1 26  ? 15.480 0.841   12.903  0.60 20.71 ?  26  GLU   A H    1 
ATOM   714  H HA   A GLU   A 1 26  ? 15.388 -0.300  15.224  0.40 19.66 ?  26  GLU   A HA   1 
ATOM   715  H HA   B GLU   A 1 26  ? 15.454 -0.625  15.050  0.60 20.82 ?  26  GLU   A HA   1 
ATOM   716  H HB2  A GLU   A 1 26  ? 16.117 -0.810  12.569  0.40 20.39 ?  26  GLU   A HB2  1 
ATOM   717  H HB2  B GLU   A 1 26  ? 16.304 -1.241  12.437  0.60 21.85 ?  26  GLU   A HB2  1 
ATOM   718  H HB3  A GLU   A 1 26  ? 16.359 -1.942  13.652  0.40 20.39 ?  26  GLU   A HB3  1 
ATOM   719  H HB3  B GLU   A 1 26  ? 16.354 -2.333  13.588  0.60 21.85 ?  26  GLU   A HB3  1 
ATOM   720  H HG2  A GLU   A 1 26  ? 13.815 -0.887  13.165  0.40 22.14 ?  26  GLU   A HG2  1 
ATOM   721  H HG2  B GLU   A 1 26  ? 13.989 -1.127  12.663  0.60 23.65 ?  26  GLU   A HG2  1 
ATOM   722  H HG3  A GLU   A 1 26  ? 14.352 -2.176  12.407  0.40 22.14 ?  26  GLU   A HG3  1 
ATOM   723  H HG3  B GLU   A 1 26  ? 14.451 -2.602  12.290  0.60 23.65 ?  26  GLU   A HG3  1 
ATOM   724  N N    A ALA   A 1 27  ? 18.385 0.315   14.240  0.40 15.34 ?  27  ALA   A N    1 
ATOM   725  N N    B ALA   A 1 27  ? 18.392 0.236   14.139  0.60 15.93 ?  27  ALA   A N    1 
ATOM   726  C CA   A ALA   A 1 27  ? 19.782 0.250   14.652  0.40 15.89 ?  27  ALA   A CA   1 
ATOM   727  C CA   B ALA   A 1 27  ? 19.766 0.317   14.622  0.60 16.28 ?  27  ALA   A CA   1 
ATOM   728  C C    A ALA   A 1 27  ? 20.009 1.023   15.944  0.40 17.02 ?  27  ALA   A C    1 
ATOM   729  C C    B ALA   A 1 27  ? 19.856 1.185   15.871  0.60 17.69 ?  27  ALA   A C    1 
ATOM   730  O O    A ALA   A 1 27  ? 20.688 0.538   16.856  0.40 17.17 ?  27  ALA   A O    1 
ATOM   731  O O    B ALA   A 1 27  ? 20.524 0.814   16.843  0.60 17.83 ?  27  ALA   A O    1 
ATOM   732  C CB   A ALA   A 1 27  ? 20.682 0.784   13.536  0.40 15.68 ?  27  ALA   A CB   1 
ATOM   733  C CB   B ALA   A 1 27  ? 20.681 0.843   13.514  0.60 15.75 ?  27  ALA   A CB   1 
ATOM   734  H H    A ALA   A 1 27  ? 18.254 0.680   13.472  0.40 18.40 ?  27  ALA   A H    1 
ATOM   735  H H    B ALA   A 1 27  ? 18.246 0.629   13.388  0.60 19.11 ?  27  ALA   A H    1 
ATOM   736  H HA   A ALA   A 1 27  ? 20.019 -0.674  14.811  0.40 19.07 ?  27  ALA   A HA   1 
ATOM   737  H HA   B ALA   A 1 27  ? 20.063 -0.572  14.857  0.60 19.54 ?  27  ALA   A HA   1 
ATOM   738  H HB1  A ALA   A 1 27  ? 21.608 0.733   13.824  0.40 18.82 ?  27  ALA   A HB1  1 
ATOM   739  H HB1  B ALA   A 1 27  ? 21.589 0.886   13.851  0.60 18.90 ?  27  ALA   A HB1  1 
ATOM   740  H HB2  A ALA   A 1 27  ? 20.553 0.242   12.741  0.40 18.82 ?  27  ALA   A HB2  1 
ATOM   741  H HB2  B ALA   A 1 27  ? 20.638 0.236   12.757  0.60 18.90 ?  27  ALA   A HB2  1 
ATOM   742  H HB3  A ALA   A 1 27  ? 20.445 1.706   13.349  0.40 18.82 ?  27  ALA   A HB3  1 
ATOM   743  H HB3  B ALA   A 1 27  ? 20.383 1.726   13.247  0.60 18.90 ?  27  ALA   A HB3  1 
ATOM   744  N N    A LYS   A 1 28  ? 19.439 2.226   16.045  0.40 18.37 ?  28  LYS   A N    1 
ATOM   745  N N    B LYS   A 1 28  ? 19.170 2.331   15.875  0.60 19.18 ?  28  LYS   A N    1 
ATOM   746  C CA   A LYS   A 1 28  ? 19.601 3.022   17.258  0.40 20.45 ?  28  LYS   A CA   1 
ATOM   747  C CA   B LYS   A 1 28  ? 19.207 3.221   17.032  0.60 21.25 ?  28  LYS   A CA   1 
ATOM   748  C C    A LYS   A 1 28  ? 19.029 2.298   18.470  0.40 22.09 ?  28  LYS   A C    1 
ATOM   749  C C    B LYS   A 1 28  ? 18.722 2.528   18.300  0.60 22.61 ?  28  LYS   A C    1 
ATOM   750  O O    A LYS   A 1 28  ? 19.612 2.341   19.559  0.40 22.66 ?  28  LYS   A O    1 
ATOM   751  O O    B LYS   A 1 28  ? 19.167 2.872   19.401  0.60 23.74 ?  28  LYS   A O    1 
ATOM   752  C CB   A LYS   A 1 28  ? 18.951 4.397   17.082  0.40 21.35 ?  28  LYS   A CB   1 
ATOM   753  C CB   B LYS   A 1 28  ? 18.363 4.467   16.758  0.60 22.38 ?  28  LYS   A CB   1 
ATOM   754  C CG   A LYS   A 1 28  ? 19.712 5.324   16.144  0.40 22.03 ?  28  LYS   A CG   1 
ATOM   755  C CG   B LYS   A 1 28  ? 19.029 5.482   15.846  0.60 23.59 ?  28  LYS   A CG   1 
ATOM   756  C CD   A LYS   A 1 28  ? 19.202 6.759   16.213  0.40 23.25 ?  28  LYS   A CD   1 
ATOM   757  C CD   B LYS   A 1 28  ? 18.091 6.643   15.545  0.60 25.67 ?  28  LYS   A CD   1 
ATOM   758  C CE   A LYS   A 1 28  ? 17.867 6.917   15.509  0.40 24.26 ?  28  LYS   A CE   1 
ATOM   759  C CE   B LYS   A 1 28  ? 18.800 7.764   14.802  0.60 27.25 ?  28  LYS   A CE   1 
ATOM   760  N NZ   A LYS   A 1 28  ? 17.433 8.341   15.471  0.40 24.76 ?  28  LYS   A NZ   1 
ATOM   761  N NZ   B LYS   A 1 28  ? 17.856 8.842   14.382  0.60 28.28 ?  28  LYS   A NZ   1 
ATOM   762  H H    A LYS   A 1 28  ? 18.964 2.595   15.436  0.40 22.05 ?  28  LYS   A H    1 
ATOM   763  H H    B LYS   A 1 28  ? 18.683 2.613   15.227  0.60 23.01 ?  28  LYS   A H    1 
ATOM   764  H HA   A LYS   A 1 28  ? 20.545 3.163   17.423  0.40 24.54 ?  28  LYS   A HA   1 
ATOM   765  H HA   B LYS   A 1 28  ? 20.117 3.510   17.186  0.60 25.50 ?  28  LYS   A HA   1 
ATOM   766  H HB2  A LYS   A 1 28  ? 18.061 4.281   16.717  0.40 25.62 ?  28  LYS   A HB2  1 
ATOM   767  H HB2  B LYS   A 1 28  ? 17.533 4.199   16.333  0.60 26.86 ?  28  LYS   A HB2  1 
ATOM   768  H HB3  A LYS   A 1 28  ? 18.898 4.836   17.946  0.40 25.62 ?  28  LYS   A HB3  1 
ATOM   769  H HB3  B LYS   A 1 28  ? 18.173 4.913   17.597  0.60 26.86 ?  28  LYS   A HB3  1 
ATOM   770  H HG2  A LYS   A 1 28  ? 20.650 5.327   16.391  0.40 26.43 ?  28  LYS   A HG2  1 
ATOM   771  H HG2  B LYS   A 1 28  ? 19.821 5.836   16.281  0.60 28.30 ?  28  LYS   A HG2  1 
ATOM   772  H HG3  A LYS   A 1 28  ? 19.607 5.012   15.232  0.40 26.43 ?  28  LYS   A HG3  1 
ATOM   773  H HG3  B LYS   A 1 28  ? 19.266 5.057   15.007  0.60 28.30 ?  28  LYS   A HG3  1 
ATOM   774  H HD2  A LYS   A 1 28  ? 19.086 7.014   17.142  0.40 27.90 ?  28  LYS   A HD2  1 
ATOM   775  H HD2  B LYS   A 1 28  ? 17.358 6.329   14.991  0.60 30.80 ?  28  LYS   A HD2  1 
ATOM   776  H HD3  A LYS   A 1 28  ? 19.843 7.347   15.783  0.40 27.90 ?  28  LYS   A HD3  1 
ATOM   777  H HD3  B LYS   A 1 28  ? 17.747 7.003   16.379  0.60 30.80 ?  28  LYS   A HD3  1 
ATOM   778  H HE2  A LYS   A 1 28  ? 17.948 6.601   14.595  0.40 29.11 ?  28  LYS   A HE2  1 
ATOM   779  H HE2  B LYS   A 1 28  ? 19.469 8.159   15.384  0.60 32.70 ?  28  LYS   A HE2  1 
ATOM   780  H HE3  A LYS   A 1 28  ? 17.192 6.407   15.982  0.40 29.11 ?  28  LYS   A HE3  1 
ATOM   781  H HE3  B LYS   A 1 28  ? 19.220 7.403   14.006  0.60 32.70 ?  28  LYS   A HE3  1 
ATOM   782  H HZ1  A LYS   A 1 28  ? 16.650 8.410   15.054  0.40 29.71 ?  28  LYS   A HZ1  1 
ATOM   783  H HZ1  B LYS   A 1 28  ? 18.298 9.483   13.951  0.60 33.94 ?  28  LYS   A HZ1  1 
ATOM   784  H HZ2  A LYS   A 1 28  ? 17.348 8.655   16.300  0.40 29.71 ?  28  LYS   A HZ2  1 
ATOM   785  H HZ2  B LYS   A 1 28  ? 17.233 8.507   13.842  0.60 33.94 ?  28  LYS   A HZ2  1 
ATOM   786  H HZ3  A LYS   A 1 28  ? 18.036 8.832   15.037  0.40 29.71 ?  28  LYS   A HZ3  1 
ATOM   787  H HZ3  B LYS   A 1 28  ? 17.460 9.195   15.097  0.60 33.94 ?  28  LYS   A HZ3  1 
ATOM   788  N N    A LYS   A 1 29  ? 17.898 1.612   18.298  0.40 23.67 ?  29  LYS   A N    1 
ATOM   789  N N    B LYS   A 1 29  ? 17.821 1.555   18.171  0.60 23.47 ?  29  LYS   A N    1 
ATOM   790  C CA   A LYS   A 1 29  ? 17.287 0.904   19.418  0.40 25.82 ?  29  LYS   A CA   1 
ATOM   791  C CA   B LYS   A 1 29  ? 17.220 0.889   19.323  0.60 25.57 ?  29  LYS   A CA   1 
ATOM   792  C C    A LYS   A 1 29  ? 18.098 -0.330  19.794  0.40 25.44 ?  29  LYS   A C    1 
ATOM   793  C C    B LYS   A 1 29  ? 18.020 -0.334  19.764  0.60 25.23 ?  29  LYS   A C    1 
ATOM   794  O O    A LYS   A 1 29  ? 18.429 -0.535  20.968  0.40 26.24 ?  29  LYS   A O    1 
ATOM   795  O O    B LYS   A 1 29  ? 18.255 -0.530  20.961  0.60 26.19 ?  29  LYS   A O    1 
ATOM   796  C CB   A LYS   A 1 29  ? 15.851 0.514   19.067  0.40 28.38 ?  29  LYS   A CB   1 
ATOM   797  C CB   B LYS   A 1 29  ? 15.787 0.470   18.978  0.60 28.29 ?  29  LYS   A CB   1 
ATOM   798  C CG   A LYS   A 1 29  ? 15.107 -0.213  20.182  0.40 31.03 ?  29  LYS   A CG   1 
ATOM   799  C CG   B LYS   A 1 29  ? 15.005 -0.125  20.138  0.60 31.38 ?  29  LYS   A CG   1 
ATOM   800  C CD   A LYS   A 1 29  ? 14.784 0.718   21.339  0.40 33.41 ?  29  LYS   A CD   1 
ATOM   801  C CD   B LYS   A 1 29  ? 14.663 0.932   21.174  0.60 34.25 ?  29  LYS   A CD   1 
ATOM   802  C CE   A LYS   A 1 29  ? 13.915 0.027   22.380  0.40 35.00 ?  29  LYS   A CE   1 
ATOM   803  C CE   B LYS   A 1 29  ? 13.792 0.360   22.281  0.60 36.23 ?  29  LYS   A CE   1 
ATOM   804  N NZ   A LYS   A 1 29  ? 13.444 0.972   23.432  0.40 35.91 ?  29  LYS   A NZ   1 
ATOM   805  N NZ   B LYS   A 1 29  ? 13.445 1.389   23.298  0.60 37.38 ?  29  LYS   A NZ   1 
ATOM   806  H H    A LYS   A 1 29  ? 17.477 1.536   17.553  0.40 28.40 ?  29  LYS   A H    1 
ATOM   807  H H    B LYS   A 1 29  ? 17.541 1.258   17.415  0.60 28.17 ?  29  LYS   A H    1 
ATOM   808  H HA   A LYS   A 1 29  ? 17.259 1.490   20.189  0.40 30.99 ?  29  LYS   A HA   1 
ATOM   809  H HA   B LYS   A 1 29  ? 17.181 1.511   20.065  0.60 30.68 ?  29  LYS   A HA   1 
ATOM   810  H HB2  A LYS   A 1 29  ? 15.351 1.319   18.860  0.40 34.06 ?  29  LYS   A HB2  1 
ATOM   811  H HB2  B LYS   A 1 29  ? 15.301 1.249   18.668  0.60 33.94 ?  29  LYS   A HB2  1 
ATOM   812  H HB3  A LYS   A 1 29  ? 15.865 -0.071  18.294  0.40 34.06 ?  29  LYS   A HB3  1 
ATOM   813  H HB3  B LYS   A 1 29  ? 15.819 -0.197  18.275  0.60 33.94 ?  29  LYS   A HB3  1 
ATOM   814  H HG2  A LYS   A 1 29  ? 14.273 -0.561  19.832  0.40 37.24 ?  29  LYS   A HG2  1 
ATOM   815  H HG2  B LYS   A 1 29  ? 14.175 -0.501  19.804  0.60 37.65 ?  29  LYS   A HG2  1 
ATOM   816  H HG3  A LYS   A 1 29  ? 15.654 -0.941  20.520  0.40 37.24 ?  29  LYS   A HG3  1 
ATOM   817  H HG3  B LYS   A 1 29  ? 15.534 -0.815  20.569  0.60 37.65 ?  29  LYS   A HG3  1 
ATOM   818  H HD2  A LYS   A 1 29  ? 15.608 0.998   21.768  0.40 40.09 ?  29  LYS   A HD2  1 
ATOM   819  H HD2  B LYS   A 1 29  ? 15.481 1.267   21.573  0.60 41.10 ?  29  LYS   A HD2  1 
ATOM   820  H HD3  A LYS   A 1 29  ? 14.301 1.490   21.003  0.40 40.09 ?  29  LYS   A HD3  1 
ATOM   821  H HD3  B LYS   A 1 29  ? 14.177 1.654   20.745  0.60 41.10 ?  29  LYS   A HD3  1 
ATOM   822  H HE2  A LYS   A 1 29  ? 13.136 -0.352  21.944  0.40 42.00 ?  29  LYS   A HE2  1 
ATOM   823  H HE2  B LYS   A 1 29  ? 12.967 0.023   21.896  0.60 43.47 ?  29  LYS   A HE2  1 
ATOM   824  H HE3  A LYS   A 1 29  ? 14.430 -0.673  22.811  0.40 42.00 ?  29  LYS   A HE3  1 
ATOM   825  H HE3  B LYS   A 1 29  ? 14.271 -0.358  22.725  0.60 43.47 ?  29  LYS   A HE3  1 
ATOM   826  H HZ1  A LYS   A 1 29  ? 12.940 0.540   24.025  0.40 43.09 ?  29  LYS   A HZ1  1 
ATOM   827  H HZ1  B LYS   A 1 29  ? 12.936 1.029   23.933  0.60 44.85 ?  29  LYS   A HZ1  1 
ATOM   828  H HZ2  A LYS   A 1 29  ? 14.141 1.331   23.852  0.40 43.09 ?  29  LYS   A HZ2  1 
ATOM   829  H HZ2  B LYS   A 1 29  ? 14.187 1.711   23.669  0.60 44.85 ?  29  LYS   A HZ2  1 
ATOM   830  H HZ3  A LYS   A 1 29  ? 12.963 1.623   23.062  0.40 43.09 ?  29  LYS   A HZ3  1 
ATOM   831  H HZ3  B LYS   A 1 29  ? 13.000 2.057   22.915  0.60 44.85 ?  29  LYS   A HZ3  1 
ATOM   832  N N    . VAL   A 1 30  ? 18.426 -1.168  18.810  1.00 24.26 ?  30  VAL   A N    1 
ATOM   833  C CA   . VAL   A 1 30  ? 19.084 -2.432  19.121  1.00 23.35 ?  30  VAL   A CA   1 
ATOM   834  C C    . VAL   A 1 30  ? 20.589 -2.278  19.320  1.00 21.71 ?  30  VAL   A C    1 
ATOM   835  O O    . VAL   A 1 30  ? 21.187 -3.017  20.110  1.00 22.49 ?  30  VAL   A O    1 
ATOM   836  C CB   . VAL   A 1 30  ? 18.777 -3.443  18.001  1.00 24.33 ?  30  VAL   A CB   1 
ATOM   837  C CG1  . VAL   A 1 30  ? 19.554 -4.738  18.205  1.00 24.87 ?  30  VAL   A CG1  1 
ATOM   838  C CG2  . VAL   A 1 30  ? 17.282 -3.718  17.931  1.00 25.32 ?  30  VAL   A CG2  1 
ATOM   839  H H    A VAL   A 1 30  ? 18.273 -1.036  17.974  0.40 29.11 ?  30  VAL   A H    1 
ATOM   840  H H    B VAL   A 1 30  ? 18.317 -1.031  17.968  0.60 29.11 ?  30  VAL   A H    1 
ATOM   841  H HA   . VAL   A 1 30  ? 18.704 -2.784  19.942  1.00 28.02 ?  30  VAL   A HA   1 
ATOM   842  H HB   . VAL   A 1 30  ? 19.049 -3.067  17.151  1.00 29.19 ?  30  VAL   A HB   1 
ATOM   843  H HG11 . VAL   A 1 30  ? 19.158 -5.433  17.654  1.00 29.84 ?  30  VAL   A HG11 1 
ATOM   844  H HG12 . VAL   A 1 30  ? 20.477 -4.599  17.947  1.00 29.84 ?  30  VAL   A HG12 1 
ATOM   845  H HG13 . VAL   A 1 30  ? 19.502 -4.992  19.140  1.00 29.84 ?  30  VAL   A HG13 1 
ATOM   846  H HG21 . VAL   A 1 30  ? 17.114 -4.395  17.255  1.00 30.38 ?  30  VAL   A HG21 1 
ATOM   847  H HG22 . VAL   A 1 30  ? 16.978 -4.037  18.797  1.00 30.38 ?  30  VAL   A HG22 1 
ATOM   848  H HG23 . VAL   A 1 30  ? 16.820 -2.899  17.701  1.00 30.38 ?  30  VAL   A HG23 1 
ATOM   849  N N    A LYS   A 1 31  ? 21.218 -1.333  18.630  0.40 21.64 ?  31  LYS   A N    1 
ATOM   850  N N    B LYS   A 1 31  ? 21.213 -1.330  18.629  0.60 20.84 ?  31  LYS   A N    1 
ATOM   851  C CA   A LYS   A 1 31  ? 22.671 -1.222  18.583  0.40 22.38 ?  31  LYS   A CA   1 
ATOM   852  C CA   B LYS   A 1 31  ? 22.665 -1.215  18.569  0.60 21.15 ?  31  LYS   A CA   1 
ATOM   853  C C    A LYS   A 1 31  ? 23.289 -2.580  18.243  0.40 20.13 ?  31  LYS   A C    1 
ATOM   854  C C    B LYS   A 1 31  ? 23.285 -2.576  18.242  0.60 19.62 ?  31  LYS   A C    1 
ATOM   855  O O    A LYS   A 1 31  ? 24.071 -3.129  19.027  0.40 20.98 ?  31  LYS   A O    1 
ATOM   856  O O    B LYS   A 1 31  ? 24.060 -3.122  19.035  0.60 20.44 ?  31  LYS   A O    1 
ATOM   857  C CB   A LYS   A 1 31  ? 23.242 -0.673  19.882  0.40 26.20 ?  31  LYS   A CB   1 
ATOM   858  C CB   B LYS   A 1 31  ? 23.246 -0.639  19.853  0.60 25.56 ?  31  LYS   A CB   1 
ATOM   859  C CG   A LYS   A 1 31  ? 22.546 0.578   20.390  0.40 30.12 ?  31  LYS   A CG   1 
ATOM   860  C CG   B LYS   A 1 31  ? 22.531 0.610   20.338  0.60 30.40 ?  31  LYS   A CG   1 
ATOM   861  C CD   A LYS   A 1 31  ? 23.549 1.617   20.865  0.40 33.05 ?  31  LYS   A CD   1 
ATOM   862  C CD   B LYS   A 1 31  ? 23.508 1.656   20.850  0.60 33.94 ?  31  LYS   A CD   1 
ATOM   863  C CE   A LYS   A 1 31  ? 22.890 2.655   21.759  0.40 34.86 ?  31  LYS   A CE   1 
ATOM   864  C CE   B LYS   A 1 31  ? 22.820 2.646   21.778  0.60 36.10 ?  31  LYS   A CE   1 
ATOM   865  N NZ   A LYS   A 1 31  ? 21.706 3.292   21.120  0.40 35.91 ?  31  LYS   A NZ   1 
ATOM   866  N NZ   B LYS   A 1 31  ? 21.573 3.213   21.193  0.60 37.35 ?  31  LYS   A NZ   1 
ATOM   867  H H    A LYS   A 1 31  ? 20.812 -0.729  18.173  0.40 25.96 ?  31  LYS   A H    1 
ATOM   868  H H    B LYS   A 1 31  ? 20.802 -0.725  18.177  0.60 25.00 ?  31  LYS   A H    1 
ATOM   869  H HA   A LYS   A 1 31  ? 22.903 -0.605  17.878  0.40 26.86 ?  31  LYS   A HA   1 
ATOM   870  H HA   B LYS   A 1 31  ? 22.888 -0.608  17.850  0.60 25.37 ?  31  LYS   A HA   1 
ATOM   871  H HB2  A LYS   A 1 31  ? 23.172 -1.353  20.567  0.40 31.43 ?  31  LYS   A HB2  1 
ATOM   872  H HB2  B LYS   A 1 31  ? 23.189 -1.306  20.552  0.60 30.67 ?  31  LYS   A HB2  1 
ATOM   873  H HB3  A LYS   A 1 31  ? 24.177 -0.451  19.737  0.40 31.43 ?  31  LYS   A HB3  1 
ATOM   874  H HB3  B LYS   A 1 31  ? 24.176 -0.406  19.693  0.60 30.67 ?  31  LYS   A HB3  1 
ATOM   875  H HG2  A LYS   A 1 31  ? 22.021 0.967   19.673  0.40 36.14 ?  31  LYS   A HG2  1 
ATOM   876  H HG2  B LYS   A 1 31  ? 22.030 0.999   19.604  0.60 36.47 ?  31  LYS   A HG2  1 
ATOM   877  H HG3  A LYS   A 1 31  ? 21.973 0.344   21.137  0.40 36.14 ?  31  LYS   A HG3  1 
ATOM   878  H HG3  B LYS   A 1 31  ? 21.933 0.374   21.064  0.60 36.47 ?  31  LYS   A HG3  1 
ATOM   879  H HD2  A LYS   A 1 31  ? 24.250 1.179   21.372  0.40 39.66 ?  31  LYS   A HD2  1 
ATOM   880  H HD2  B LYS   A 1 31  ? 24.219 1.218   21.344  0.60 40.72 ?  31  LYS   A HD2  1 
ATOM   881  H HD3  A LYS   A 1 31  ? 23.926 2.073   20.095  0.40 39.66 ?  31  LYS   A HD3  1 
ATOM   882  H HD3  B LYS   A 1 31  ? 23.876 2.148   20.098  0.60 40.72 ?  31  LYS   A HD3  1 
ATOM   883  H HE2  A LYS   A 1 31  ? 22.597 2.226   22.578  0.40 41.83 ?  31  LYS   A HE2  1 
ATOM   884  H HE2  B LYS   A 1 31  ? 22.585 2.193   22.603  0.60 43.31 ?  31  LYS   A HE2  1 
ATOM   885  H HE3  A LYS   A 1 31  ? 23.534 3.352   21.961  0.40 41.83 ?  31  LYS   A HE3  1 
ATOM   886  H HE3  B LYS   A 1 31  ? 23.426 3.380   21.963  0.60 43.31 ?  31  LYS   A HE3  1 
ATOM   887  H HZ1  A LYS   A 1 31  ? 21.367 3.913   21.660  0.40 43.09 ?  31  LYS   A HZ1  1 
ATOM   888  H HZ1  B LYS   A 1 31  ? 21.227 3.821   21.744  0.60 44.82 ?  31  LYS   A HZ1  1 
ATOM   889  H HZ2  A LYS   A 1 31  ? 21.944 3.675   20.353  0.40 43.09 ?  31  LYS   A HZ2  1 
ATOM   890  H HZ2  B LYS   A 1 31  ? 21.751 3.600   20.412  0.60 44.82 ?  31  LYS   A HZ2  1 
ATOM   891  H HZ3  A LYS   A 1 31  ? 21.082 2.679   20.956  0.40 43.09 ?  31  LYS   A HZ3  1 
ATOM   892  H HZ3  B LYS   A 1 31  ? 20.974 2.567   21.065  0.60 44.82 ?  31  LYS   A HZ3  1 
ATOM   893  N N    . PRO   A 1 32  ? 22.958 -3.144  17.086  1.00 17.76 ?  32  PRO   A N    1 
ATOM   894  C CA   . PRO   A 1 32  ? 23.437 -4.484  16.754  1.00 17.43 ?  32  PRO   A CA   1 
ATOM   895  C C    . PRO   A 1 32  ? 24.937 -4.497  16.545  1.00 17.13 ?  32  PRO   A C    1 
ATOM   896  O O    . PRO   A 1 32  ? 25.577 -3.467  16.329  1.00 17.03 ?  32  PRO   A O    1 
ATOM   897  C CB   . PRO   A 1 32  ? 22.712 -4.789  15.439  1.00 17.46 ?  32  PRO   A CB   1 
ATOM   898  C CG   . PRO   A 1 32  ? 22.540 -3.437  14.809  1.00 16.24 ?  32  PRO   A CG   1 
ATOM   899  C CD   . PRO   A 1 32  ? 22.237 -2.525  15.963  1.00 16.40 ?  32  PRO   A CD   1 
ATOM   900  H HA   . PRO   A 1 32  ? 23.187 -5.126  17.435  1.00 20.91 ?  32  PRO   A HA   1 
ATOM   901  H HB2  . PRO   A 1 32  ? 23.257 -5.372  14.885  1.00 20.95 ?  32  PRO   A HB2  1 
ATOM   902  H HB3  . PRO   A 1 32  ? 21.850 -5.202  15.627  1.00 20.95 ?  32  PRO   A HB3  1 
ATOM   903  H HG2  . PRO   A 1 32  ? 23.361 -3.184  14.363  1.00 19.49 ?  32  PRO   A HG2  1 
ATOM   904  H HG3  . PRO   A 1 32  ? 21.799 -3.468  14.180  1.00 19.49 ?  32  PRO   A HG3  1 
ATOM   905  H HD2  . PRO   A 1 32  ? 22.583 -1.639  15.772  1.00 19.68 ?  32  PRO   A HD2  1 
ATOM   906  H HD3  . PRO   A 1 32  ? 21.285 -2.510  16.131  1.00 19.68 ?  32  PRO   A HD3  1 
ATOM   907  N N    . THR   A 1 33  ? 25.494 -5.704  16.587  1.00 17.15 ?  33  THR   A N    1 
ATOM   908  C CA   . THR   A 1 33  ? 26.903 -5.869  16.258  1.00 17.16 ?  33  THR   A CA   1 
ATOM   909  C C    . THR   A 1 33  ? 27.193 -5.418  14.832  1.00 15.39 ?  33  THR   A C    1 
ATOM   910  O O    . THR   A 1 33  ? 28.222 -4.779  14.573  1.00 15.52 ?  33  THR   A O    1 
ATOM   911  C CB   . THR   A 1 33  ? 27.307 -7.327  16.462  1.00 18.98 ?  33  THR   A CB   1 
ATOM   912  O OG1  . THR   A 1 33  ? 27.032 -7.700  17.814  1.00 20.72 ?  33  THR   A OG1  1 
ATOM   913  C CG2  . THR   A 1 33  ? 28.785 -7.525  16.171  1.00 20.17 ?  33  THR   A CG2  1 
ATOM   914  H H    . THR   A 1 33  ? 25.084 -6.430  16.798  1.00 20.57 ?  33  THR   A H    1 
ATOM   915  H HA   . THR   A 1 33  ? 27.434 -5.327  16.862  1.00 20.58 ?  33  THR   A HA   1 
ATOM   916  H HB   . THR   A 1 33  ? 26.795 -7.897  15.863  1.00 22.77 ?  33  THR   A HB   1 
ATOM   917  H HG1  . THR   A 1 33  ? 27.482 -7.225  18.345  1.00 24.86 ?  33  THR   A HG1  1 
ATOM   918  H HG21 . THR   A 1 33  ? 29.068 -8.403  16.470  1.00 24.20 ?  33  THR   A HG21 1 
ATOM   919  H HG22 . THR   A 1 33  ? 28.949 -7.451  15.217  1.00 24.20 ?  33  THR   A HG22 1 
ATOM   920  H HG23 . THR   A 1 33  ? 29.305 -6.851  16.634  1.00 24.20 ?  33  THR   A HG23 1 
ATOM   921  N N    . VAL   A 1 34  ? 26.294 -5.731  13.898  1.00 13.86 ?  34  VAL   A N    1 
ATOM   922  C CA   . VAL   A 1 34  ? 26.485 -5.411  12.487  1.00 12.58 ?  34  VAL   A CA   1 
ATOM   923  C C    . VAL   A 1 34  ? 25.187 -4.852  11.921  1.00 11.80 ?  34  VAL   A C    1 
ATOM   924  O O    . VAL   A 1 34  ? 24.147 -5.524  11.961  1.00 12.82 ?  34  VAL   A O    1 
ATOM   925  C CB   . VAL   A 1 34  ? 26.920 -6.629  11.652  1.00 13.23 ?  34  VAL   A CB   1 
ATOM   926  C CG1  . VAL   A 1 34  ? 27.088 -6.231  10.190  1.00 13.38 ?  34  VAL   A CG1  1 
ATOM   927  C CG2  . VAL   A 1 34  ? 28.201 -7.238  12.205  1.00 14.56 ?  34  VAL   A CG2  1 
ATOM   928  H H    . VAL   A 1 34  ? 25.546 -6.132  14.064  1.00 16.63 ?  34  VAL   A H    1 
ATOM   929  H HA   . VAL   A 1 34  ? 27.165 -4.722  12.405  1.00 15.09 ?  34  VAL   A HA   1 
ATOM   930  H HB   . VAL   A 1 34  ? 26.223 -7.301  11.703  1.00 15.87 ?  34  VAL   A HB   1 
ATOM   931  H HG11 . VAL   A 1 34  ? 27.584 -6.927  9.735   1.00 16.05 ?  34  VAL   A HG11 1 
ATOM   932  H HG12 . VAL   A 1 34  ? 26.212 -6.130  9.786   1.00 16.05 ?  34  VAL   A HG12 1 
ATOM   933  H HG13 . VAL   A 1 34  ? 27.575 -5.394  10.146  1.00 16.05 ?  34  VAL   A HG13 1 
ATOM   934  H HG21 . VAL   A 1 34  ? 28.473 -7.970  11.632  1.00 17.47 ?  34  VAL   A HG21 1 
ATOM   935  H HG22 . VAL   A 1 34  ? 28.892 -6.557  12.226  1.00 17.47 ?  34  VAL   A HG22 1 
ATOM   936  H HG23 . VAL   A 1 34  ? 28.034 -7.566  13.104  1.00 17.47 ?  34  VAL   A HG23 1 
ATOM   937  N N    . VAL   A 1 35  ? 25.252 -3.643  11.361  1.00 11.18 ?  35  VAL   A N    1 
ATOM   938  C CA   . VAL   A 1 35  ? 24.214 -3.128  10.478  1.00 10.76 ?  35  VAL   A CA   1 
ATOM   939  C C    . VAL   A 1 35  ? 24.764 -3.138  9.060   1.00 10.05 ?  35  VAL   A C    1 
ATOM   940  O O    . VAL   A 1 35  ? 25.910 -2.734  8.826   1.00 10.95 ?  35  VAL   A O    1 
ATOM   941  C CB   . VAL   A 1 35  ? 23.689 -1.732  10.886  1.00 11.67 ?  35  VAL   A CB   1 
ATOM   942  C CG1  . VAL   A 1 35  ? 24.763 -0.640  10.742  1.00 12.29 ?  35  VAL   A CG1  1 
ATOM   943  C CG2  . VAL   A 1 35  ? 22.446 -1.381  10.073  1.00 12.16 ?  35  VAL   A CG2  1 
ATOM   944  H H    . VAL   A 1 35  ? 25.897 -3.085  11.483  1.00 13.41 ?  35  VAL   A H    1 
ATOM   945  H HA   . VAL   A 1 35  ? 23.456 -3.737  10.503  1.00 12.92 ?  35  VAL   A HA   1 
ATOM   946  H HB   . VAL   A 1 35  ? 23.419 -1.758  11.815  1.00 14.00 ?  35  VAL   A HB   1 
ATOM   947  H HG11 . VAL   A 1 35  ? 24.420 0.191   11.112  1.00 14.75 ?  35  VAL   A HG11 1 
ATOM   948  H HG12 . VAL   A 1 35  ? 25.555 -0.916  11.222  1.00 14.75 ?  35  VAL   A HG12 1 
ATOM   949  H HG13 . VAL   A 1 35  ? 24.968 -0.518  9.800   1.00 14.75 ?  35  VAL   A HG13 1 
ATOM   950  H HG21 . VAL   A 1 35  ? 22.093 -0.531  10.378  1.00 14.59 ?  35  VAL   A HG21 1 
ATOM   951  H HG22 . VAL   A 1 35  ? 22.686 -1.318  9.132   1.00 14.59 ?  35  VAL   A HG22 1 
ATOM   952  H HG23 . VAL   A 1 35  ? 21.779 -2.077  10.193  1.00 14.59 ?  35  VAL   A HG23 1 
ATOM   953  N N    . VAL   A 1 36  ? 23.947 -3.599  8.115   1.00 9.78  ?  36  VAL   A N    1 
ATOM   954  C CA   . VAL   A 1 36  ? 24.318 -3.618  6.710   1.00 9.51  ?  36  VAL   A CA   1 
ATOM   955  C C    . VAL   A 1 36  ? 23.856 -2.330  6.043   1.00 9.52  ?  36  VAL   A C    1 
ATOM   956  O O    . VAL   A 1 36  ? 22.691 -1.925  6.183   1.00 10.41 ?  36  VAL   A O    1 
ATOM   957  C CB   . VAL   A 1 36  ? 23.710 -4.833  5.995   1.00 9.67  ?  36  VAL   A CB   1 
ATOM   958  C CG1  . VAL   A 1 36  ? 23.969 -4.752  4.506   1.00 10.25 ?  36  VAL   A CG1  1 
ATOM   959  C CG2  . VAL   A 1 36  ? 24.252 -6.125  6.577   1.00 10.82 ?  36  VAL   A CG2  1 
ATOM   960  H H    . VAL   A 1 36  ? 23.155 -3.908  8.270   1.00 11.73 ?  36  VAL   A H    1 
ATOM   961  H HA   . VAL   A 1 36  ? 25.285 -3.672  6.636   1.00 11.41 ?  36  VAL   A HA   1 
ATOM   962  H HB   . VAL   A 1 36  ? 22.753 -4.825  6.131   1.00 11.60 ?  36  VAL   A HB   1 
ATOM   963  H HG11 . VAL   A 1 36  ? 23.848 -5.630  4.116   1.00 12.30 ?  36  VAL   A HG11 1 
ATOM   964  H HG12 . VAL   A 1 36  ? 23.341 -4.126  4.106   1.00 12.30 ?  36  VAL   A HG12 1 
ATOM   965  H HG13 . VAL   A 1 36  ? 24.879 -4.446  4.357   1.00 12.30 ?  36  VAL   A HG13 1 
ATOM   966  H HG21 . VAL   A 1 36  ? 23.864 -6.876  6.102   1.00 12.98 ?  36  VAL   A HG21 1 
ATOM   967  H HG22 . VAL   A 1 36  ? 25.219 -6.139  6.481   1.00 12.98 ?  36  VAL   A HG22 1 
ATOM   968  H HG23 . VAL   A 1 36  ? 24.017 -6.175  7.519   1.00 12.98 ?  36  VAL   A HG23 1 
ATOM   969  N N    A ASN   A 1 37  ? 24.767 -1.700  5.304   0.40 9.58  ?  37  ASN   A N    1 
ATOM   970  N N    B ASN   A 1 37  ? 24.768 -1.692  5.309   0.60 9.01  ?  37  ASN   A N    1 
ATOM   971  C CA   A ASN   A 1 37  ? 24.447 -0.557  4.468   0.40 9.72  ?  37  ASN   A CA   1 
ATOM   972  C CA   B ASN   A 1 37  ? 24.421 -0.594  4.422   0.60 8.57  ?  37  ASN   A CA   1 
ATOM   973  C C    A ASN   A 1 37  ? 24.262 -1.006  3.027   0.40 9.80  ?  37  ASN   A C    1 
ATOM   974  C C    B ASN   A 1 37  ? 24.291 -1.094  2.992   0.60 8.54  ?  37  ASN   A C    1 
ATOM   975  O O    A ASN   A 1 37  ? 24.995 -1.868  2.533   0.40 10.19 ?  37  ASN   A O    1 
ATOM   976  O O    B ASN   A 1 37  ? 25.109 -1.890  2.523   0.60 9.28  ?  37  ASN   A O    1 
ATOM   977  C CB   A ASN   A 1 37  ? 25.564 0.482   4.535   0.40 9.94  ?  37  ASN   A CB   1 
ATOM   978  C CB   B ASN   A 1 37  ? 25.473 0.511   4.490   0.60 9.12  ?  37  ASN   A CB   1 
ATOM   979  C CG   A ASN   A 1 37  ? 25.215 1.742   3.794   0.40 9.44  ?  37  ASN   A CG   1 
ATOM   980  C CG   B ASN   A 1 37  ? 25.158 1.662   3.567   0.60 8.97  ?  37  ASN   A CG   1 
ATOM   981  O OD1  A ASN   A 1 37  ? 24.043 2.104   3.702   0.40 9.39  ?  37  ASN   A OD1  1 
ATOM   982  O OD1  B ASN   A 1 37  ? 23.989 1.970   3.314   0.60 8.95  ?  37  ASN   A OD1  1 
ATOM   983  N ND2  A ASN   A 1 37  ? 26.226 2.423   3.261   0.40 9.68  ?  37  ASN   A ND2  1 
ATOM   984  N ND2  B ASN   A 1 37  ? 26.200 2.298   3.047   0.60 9.11  ?  37  ASN   A ND2  1 
ATOM   985  H H    A ASN   A 1 37  ? 25.599 -1.921  5.276   0.40 11.49 ?  37  ASN   A H    1 
ATOM   986  H H    B ASN   A 1 37  ? 25.611 -1.874  5.321   0.60 10.81 ?  37  ASN   A H    1 
ATOM   987  H HA   A ASN   A 1 37  ? 23.626 -0.144  4.773   0.40 11.66 ?  37  ASN   A HA   1 
ATOM   988  H HA   B ASN   A 1 37  ? 23.573 -0.215  4.694   0.60 10.28 ?  37  ASN   A HA   1 
ATOM   989  H HB2  A ASN   A 1 37  ? 25.719 0.721   5.462   0.40 11.93 ?  37  ASN   A HB2  1 
ATOM   990  H HB2  B ASN   A 1 37  ? 25.519 0.856   5.400   0.60 10.95 ?  37  ASN   A HB2  1 
ATOM   991  H HB3  A ASN   A 1 37  ? 26.375 0.111   4.148   0.40 11.93 ?  37  ASN   A HB3  1 
ATOM   992  H HB3  B ASN   A 1 37  ? 26.339 0.146   4.236   0.60 10.95 ?  37  ASN   A HB3  1 
ATOM   993  H HD21 A ASN   A 1 37  ? 26.076 3.148   2.825   0.40 11.61 ?  37  ASN   A HD21 1 
ATOM   994  H HD21 B ASN   A 1 37  ? 26.075 2.958   2.515   0.60 10.93 ?  37  ASN   A HD21 1 
ATOM   995  H HD22 A ASN   A 1 37  ? 27.031 2.143   3.348   0.40 11.61 ?  37  ASN   A HD22 1 
ATOM   996  H HD22 B ASN   A 1 37  ? 26.998 2.052   3.242   0.60 10.93 ?  37  ASN   A HD22 1 
ATOM   997  N N    A ALA   A 1 38  ? 23.271 -0.414  2.358   0.40 10.06 ?  38  ALA   A N    1 
ATOM   998  N N    B ALA   A 1 38  ? 23.250 -0.616  2.307   0.60 9.06  ?  38  ALA   A N    1 
ATOM   999  C CA   A ALA   A 1 38  ? 23.062 -0.592  0.922   0.40 9.67  ?  38  ALA   A CA   1 
ATOM   1000 C CA   B ALA   A 1 38  ? 23.069 -0.817  0.870   0.60 9.70  ?  38  ALA   A CA   1 
ATOM   1001 C C    A ALA   A 1 38  ? 23.994 0.377   0.192   0.40 9.52  ?  38  ALA   A C    1 
ATOM   1002 C C    B ALA   A 1 38  ? 23.894 0.239   0.136   0.60 9.99  ?  38  ALA   A C    1 
ATOM   1003 O O    A ALA   A 1 38  ? 23.608 1.471   -0.228  0.40 9.30  ?  38  ALA   A O    1 
ATOM   1004 O O    B ALA   A 1 38  ? 23.409 1.301   -0.263  0.60 10.21 ?  38  ALA   A O    1 
ATOM   1005 C CB   A ALA   A 1 38  ? 21.599 -0.348  0.572   0.40 10.07 ?  38  ALA   A CB   1 
ATOM   1006 C CB   B ALA   A 1 38  ? 21.593 -0.742  0.511   0.60 10.64 ?  38  ALA   A CB   1 
ATOM   1007 H H    A ALA   A 1 38  ? 22.699 0.109   2.725   0.40 12.06 ?  38  ALA   A H    1 
ATOM   1008 H H    B ALA   A 1 38  ? 22.629 -0.157  2.670   0.60 10.87 ?  38  ALA   A H    1 
ATOM   1009 H HA   A ALA   A 1 38  ? 23.294 -1.497  0.667   0.40 11.60 ?  38  ALA   A HA   1 
ATOM   1010 H HA   B ALA   A 1 38  ? 23.407 -1.695  0.620   0.60 11.64 ?  38  ALA   A HA   1 
ATOM   1011 H HB1  A ALA   A 1 38  ? 21.474 -0.472  -0.381  0.40 12.09 ?  38  ALA   A HB1  1 
ATOM   1012 H HB1  B ALA   A 1 38  ? 21.496 -0.880  -0.442  0.60 12.77 ?  38  ALA   A HB1  1 
ATOM   1013 H HB2  A ALA   A 1 38  ? 21.048 -0.980  1.063   0.40 12.09 ?  38  ALA   A HB2  1 
ATOM   1014 H HB2  B ALA   A 1 38  ? 21.115 -1.431  0.999   0.60 12.77 ?  38  ALA   A HB2  1 
ATOM   1015 H HB3  A ALA   A 1 38  ? 21.360 0.559   0.822   0.40 12.09 ?  38  ALA   A HB3  1 
ATOM   1016 H HB3  B ALA   A 1 38  ? 21.256 0.133   0.759   0.60 12.77 ?  38  ALA   A HB3  1 
ATOM   1017 N N    A ALA   A 1 39  ? 25.252 -0.038  0.052   0.40 9.44  ?  39  ALA   A N    1 
ATOM   1018 N N    B ALA   A 1 39  ? 25.175 -0.067  -0.030  0.60 10.18 ?  39  ALA   A N    1 
ATOM   1019 C CA   A ALA   A 1 39  ? 26.326 0.828   -0.412  0.40 9.56  ?  39  ALA   A CA   1 
ATOM   1020 C CA   B ALA   A 1 39  ? 26.162 0.872   -0.530  0.60 9.71  ?  39  ALA   A CA   1 
ATOM   1021 C C    A ALA   A 1 39  ? 26.493 0.773   -1.927  0.40 9.47  ?  39  ALA   A C    1 
ATOM   1022 C C    B ALA   A 1 39  ? 26.262 0.813   -2.052  0.60 9.42  ?  39  ALA   A C    1 
ATOM   1023 O O    A ALA   A 1 39  ? 26.015 -0.143  -2.602  0.40 9.60  ?  39  ALA   A O    1 
ATOM   1024 O O    B ALA   A 1 39  ? 25.739 -0.094  -2.708  0.60 10.39 ?  39  ALA   A O    1 
ATOM   1025 C CB   A ALA   A 1 39  ? 27.645 0.417   0.248   0.40 10.38 ?  39  ALA   A CB   1 
ATOM   1026 C CB   B ALA   A 1 39  ? 27.518 0.562   0.107   0.60 10.76 ?  39  ALA   A CB   1 
ATOM   1027 H H    A ALA   A 1 39  ? 25.513 -0.840  0.227   0.40 11.33 ?  39  ALA   A H    1 
ATOM   1028 H H    B ALA   A 1 39  ? 25.499 -0.842  0.149   0.60 12.21 ?  39  ALA   A H    1 
ATOM   1029 H HA   A ALA   A 1 39  ? 26.130 1.742   -0.161  0.40 11.47 ?  39  ALA   A HA   1 
ATOM   1030 H HA   B ALA   A 1 39  ? 25.901 1.771   -0.271  0.60 11.65 ?  39  ALA   A HA   1 
ATOM   1031 H HB1  A ALA   A 1 39  ? 28.350 1.004   -0.070  0.40 12.45 ?  39  ALA   A HB1  1 
ATOM   1032 H HB1  B ALA   A 1 39  ? 28.172 1.192   -0.225  0.60 12.90 ?  39  ALA   A HB1  1 
ATOM   1033 H HB2  A ALA   A 1 39  ? 27.552 0.504   1.210   0.40 12.45 ?  39  ALA   A HB2  1 
ATOM   1034 H HB2  B ALA   A 1 39  ? 27.440 0.647   1.076   0.60 12.90 ?  39  ALA   A HB2  1 
ATOM   1035 H HB3  A ALA   A 1 39  ? 27.844 -0.500  0.014   0.40 12.45 ?  39  ALA   A HB3  1 
ATOM   1036 H HB3  B ALA   A 1 39  ? 27.775 -0.343  -0.120  0.60 12.90 ?  39  ALA   A HB3  1 
ATOM   1037 N N    A ASN   A 1 40  ? 27.218 1.765   -2.451  0.40 9.33  ?  40  ASN   A N    1 
ATOM   1038 N N    B ASN   A 1 40  ? 26.951 1.808   -2.612  0.60 9.57  ?  40  ASN   A N    1 
ATOM   1039 C CA   A ASN   A 1 40  ? 27.762 1.727   -3.803  0.40 9.61  ?  40  ASN   A CA   1 
ATOM   1040 C CA   B ASN   A 1 40  ? 27.460 1.753   -3.976  0.60 9.66  ?  40  ASN   A CA   1 
ATOM   1041 C C    A ASN   A 1 40  ? 29.285 1.619   -3.742  0.40 9.35  ?  40  ASN   A C    1 
ATOM   1042 C C    B ASN   A 1 40  ? 28.983 1.635   -3.937  0.60 8.75  ?  40  ASN   A C    1 
ATOM   1043 O O    A ASN   A 1 40  ? 29.894 1.732   -2.674  0.40 9.80  ?  40  ASN   A O    1 
ATOM   1044 O O    B ASN   A 1 40  ? 29.603 1.732   -2.877  0.60 9.00  ?  40  ASN   A O    1 
ATOM   1045 C CB   A ASN   A 1 40  ? 27.279 2.909   -4.667  0.40 10.55 ?  40  ASN   A CB   1 
ATOM   1046 C CB   B ASN   A 1 40  ? 26.990 2.958   -4.807  0.60 10.60 ?  40  ASN   A CB   1 
ATOM   1047 C CG   A ASN   A 1 40  ? 27.659 4.267   -4.103  0.40 11.15 ?  40  ASN   A CG   1 
ATOM   1048 C CG   B ASN   A 1 40  ? 27.357 4.283   -4.184  0.60 11.38 ?  40  ASN   A CG   1 
ATOM   1049 O OD1  A ASN   A 1 40  ? 28.822 4.519   -3.776  0.40 10.98 ?  40  ASN   A OD1  1 
ATOM   1050 O OD1  B ASN   A 1 40  ? 28.530 4.572   -3.946  0.60 12.91 ?  40  ASN   A OD1  1 
ATOM   1051 N ND2  A ASN   A 1 40  ? 26.674 5.164   -4.015  0.40 12.22 ?  40  ASN   A ND2  1 
ATOM   1052 N ND2  B ASN   A 1 40  ? 26.352 5.117   -3.949  0.60 11.89 ?  40  ASN   A ND2  1 
ATOM   1053 H H    A ASN   A 1 40  ? 27.425 2.484   -2.026  0.40 11.20 ?  40  ASN   A H    1 
ATOM   1054 H H    B ASN   A 1 40  ? 27.134 2.540   -2.207  0.60 11.49 ?  40  ASN   A H    1 
ATOM   1055 H HA   A ASN   A 1 40  ? 27.447 0.923   -4.234  0.40 11.53 ?  40  ASN   A HA   1 
ATOM   1056 H HA   B ASN   A 1 40  ? 27.114 0.947   -4.400  0.60 11.59 ?  40  ASN   A HA   1 
ATOM   1057 H HB2  A ASN   A 1 40  ? 27.672 2.832   -5.557  0.40 12.66 ?  40  ASN   A HB2  1 
ATOM   1058 H HB2  B ASN   A 1 40  ? 27.401 2.905   -5.686  0.60 12.72 ?  40  ASN   A HB2  1 
ATOM   1059 H HB3  A ASN   A 1 40  ? 26.314 2.873   -4.736  0.40 12.66 ?  40  ASN   A HB3  1 
ATOM   1060 H HB3  B ASN   A 1 40  ? 26.023 2.919   -4.895  0.60 12.72 ?  40  ASN   A HB3  1 
ATOM   1061 H HD21 A ASN   A 1 40  ? 26.833 5.956   -3.715  0.40 14.66 ?  40  ASN   A HD21 1 
ATOM   1062 H HD21 B ASN   A 1 40  ? 26.509 5.887   -3.602  0.60 14.27 ?  40  ASN   A HD21 1 
ATOM   1063 H HD22 A ASN   A 1 40  ? 25.874 4.953   -4.256  0.40 14.66 ?  40  ASN   A HD22 1 
ATOM   1064 H HD22 B ASN   A 1 40  ? 25.546 4.884   -4.135  0.60 14.27 ?  40  ASN   A HD22 1 
ATOM   1065 N N    A VAL   A 1 41  ? 29.894 1.360   -4.905  0.40 9.66  ?  41  VAL   A N    1 
ATOM   1066 N N    B VAL   A 1 41  ? 29.587 1.391   -5.103  0.60 9.59  ?  41  VAL   A N    1 
ATOM   1067 C CA   A VAL   A 1 41  ? 31.321 1.036   -4.949  0.40 10.38 ?  41  VAL   A CA   1 
ATOM   1068 C CA   B VAL   A 1 41  ? 31.018 1.082   -5.140  0.60 10.31 ?  41  VAL   A CA   1 
ATOM   1069 C C    A VAL   A 1 41  ? 32.170 2.199   -4.471  0.40 10.01 ?  41  VAL   A C    1 
ATOM   1070 C C    B VAL   A 1 41  ? 31.893 2.223   -4.648  0.60 10.53 ?  41  VAL   A C    1 
ATOM   1071 O O    A VAL   A 1 41  ? 33.291 2.000   -3.985  0.40 10.26 ?  41  VAL   A O    1 
ATOM   1072 O O    B VAL   A 1 41  ? 33.046 1.983   -4.264  0.60 10.60 ?  41  VAL   A O    1 
ATOM   1073 C CB   A VAL   A 1 41  ? 31.756 0.556   -6.351  0.40 11.20 ?  41  VAL   A CB   1 
ATOM   1074 C CB   B VAL   A 1 41  ? 31.512 0.599   -6.523  0.60 12.08 ?  41  VAL   A CB   1 
ATOM   1075 C CG1  A VAL   A 1 41  ? 30.973 -0.683  -6.763  0.40 11.89 ?  41  VAL   A CG1  1 
ATOM   1076 C CG1  B VAL   A 1 41  ? 30.861 -0.728  -6.910  0.60 13.08 ?  41  VAL   A CG1  1 
ATOM   1077 C CG2  A VAL   A 1 41  ? 31.617 1.664   -7.391  0.40 11.38 ?  41  VAL   A CG2  1 
ATOM   1078 C CG2  B VAL   A 1 41  ? 31.314 1.662   -7.604  0.60 12.72 ?  41  VAL   A CG2  1 
ATOM   1079 H H    A VAL   A 1 41  ? 29.517 1.372   -5.675  0.40 11.59 ?  41  VAL   A H    1 
ATOM   1080 H H    B VAL   A 1 41  ? 29.191 1.389   -5.870  0.60 11.51 ?  41  VAL   A H    1 
ATOM   1081 H HA   A VAL   A 1 41  ? 31.491 0.303   -4.341  0.40 12.45 ?  41  VAL   A HA   1 
ATOM   1082 H HA   B VAL   A 1 41  ? 31.161 0.347   -4.528  0.60 12.37 ?  41  VAL   A HA   1 
ATOM   1083 H HB   A VAL   A 1 41  ? 32.696 0.308   -6.325  0.40 13.43 ?  41  VAL   A HB   1 
ATOM   1084 H HB   B VAL   A 1 41  ? 32.464 0.432   -6.455  0.60 14.50 ?  41  VAL   A HB   1 
ATOM   1085 H HG11 A VAL   A 1 41  ? 31.288 -0.989  -7.629  0.40 14.26 ?  41  VAL   A HG11 1 
ATOM   1086 H HG11 B VAL   A 1 41  ? 31.215 -1.016  -7.767  0.60 15.69 ?  41  VAL   A HG11 1 
ATOM   1087 H HG12 A VAL   A 1 41  ? 31.108 -1.377  -6.099  0.40 14.26 ?  41  VAL   A HG12 1 
ATOM   1088 H HG12 B VAL   A 1 41  ? 31.067 -1.392  -6.231  0.60 15.69 ?  41  VAL   A HG12 1 
ATOM   1089 H HG13 A VAL   A 1 41  ? 30.031 -0.456  -6.818  0.40 14.26 ?  41  VAL   A HG13 1 
ATOM   1090 H HG13 B VAL   A 1 41  ? 29.902 -0.606  -6.972  0.60 15.69 ?  41  VAL   A HG13 1 
ATOM   1091 H HG21 A VAL   A 1 41  ? 31.781 1.294   -8.276  0.40 13.65 ?  41  VAL   A HG21 1 
ATOM   1092 H HG21 B VAL   A 1 41  ? 31.591 1.293   -8.461  0.60 15.26 ?  41  VAL   A HG21 1 
ATOM   1093 H HG22 A VAL   A 1 41  ? 30.718 2.024   -7.349  0.40 13.65 ?  41  VAL   A HG22 1 
ATOM   1094 H HG22 B VAL   A 1 41  ? 30.383 1.915   -7.637  0.60 15.26 ?  41  VAL   A HG22 1 
ATOM   1095 H HG23 A VAL   A 1 41  ? 32.263 2.360   -7.202  0.40 13.65 ?  41  VAL   A HG23 1 
ATOM   1096 H HG23 B VAL   A 1 41  ? 31.864 2.433   -7.390  0.60 15.26 ?  41  VAL   A HG23 1 
ATOM   1097 N N    A TYR   A 1 42  ? 31.667 3.424   -4.616  0.40 10.09 ?  42  TYR   A N    1 
ATOM   1098 N N    B TYR   A 1 42  ? 31.395 3.464   -4.673  0.60 10.53 ?  42  TYR   A N    1 
ATOM   1099 C CA   A TYR   A 1 42  ? 32.359 4.628   -4.185  0.40 10.71 ?  42  TYR   A CA   1 
ATOM   1100 C CA   B TYR   A 1 42  ? 32.180 4.627   -4.269  0.60 10.64 ?  42  TYR   A CA   1 
ATOM   1101 C C    A TYR   A 1 42  ? 32.061 4.980   -2.736  0.40 10.15 ?  42  TYR   A C    1 
ATOM   1102 C C    B TYR   A 1 42  ? 31.949 5.027   -2.821  0.60 10.34 ?  42  TYR   A C    1 
ATOM   1103 O O    A TYR   A 1 42  ? 32.657 5.925   -2.202  0.40 10.47 ?  42  TYR   A O    1 
ATOM   1104 O O    B TYR   A 1 42  ? 32.497 6.043   -2.369  0.60 10.83 ?  42  TYR   A O    1 
ATOM   1105 C CB   A TYR   A 1 42  ? 31.954 5.809   -5.083  0.40 11.31 ?  42  TYR   A CB   1 
ATOM   1106 C CB   B TYR   A 1 42  ? 31.904 5.818   -5.197  0.60 11.27 ?  42  TYR   A CB   1 
ATOM   1107 C CG   A TYR   A 1 42  ? 32.048 5.517   -6.570  0.40 11.92 ?  42  TYR   A CG   1 
ATOM   1108 C CG   B TYR   A 1 42  ? 32.180 5.487   -6.641  0.60 12.23 ?  42  TYR   A CG   1 
ATOM   1109 C CD1  A TYR   A 1 42  ? 33.280 5.311   -7.178  0.40 12.05 ?  42  TYR   A CD1  1 
ATOM   1110 C CD1  B TYR   A 1 42  ? 33.476 5.270   -7.090  0.60 12.86 ?  42  TYR   A CD1  1 
ATOM   1111 C CD2  A TYR   A 1 42  ? 30.908 5.443   -7.366  0.40 13.24 ?  42  TYR   A CD2  1 
ATOM   1112 C CD2  B TYR   A 1 42  ? 31.144 5.346   -7.547  0.60 13.27 ?  42  TYR   A CD2  1 
ATOM   1113 C CE1  A TYR   A 1 42  ? 33.379 5.038   -8.533  0.40 11.81 ?  42  TYR   A CE1  1 
ATOM   1114 C CE1  B TYR   A 1 42  ? 33.725 4.938   -8.413  0.60 13.01 ?  42  TYR   A CE1  1 
ATOM   1115 C CE2  A TYR   A 1 42  ? 30.998 5.176   -8.730  0.40 13.24 ?  42  TYR   A CE2  1 
ATOM   1116 C CE2  B TYR   A 1 42  ? 31.383 5.025   -8.869  0.60 13.73 ?  42  TYR   A CE2  1 
ATOM   1117 C CZ   A TYR   A 1 42  ? 32.239 4.971   -9.304  0.40 12.60 ?  42  TYR   A CZ   1 
ATOM   1118 C CZ   B TYR   A 1 42  ? 32.674 4.820   -9.297  0.60 13.26 ?  42  TYR   A CZ   1 
ATOM   1119 O OH   A TYR   A 1 42  ? 32.360 4.706   -10.651 0.40 12.97 ?  42  TYR   A OH   1 
ATOM   1120 O OH   B TYR   A 1 42  ? 32.906 4.491   -10.610 0.60 14.25 ?  42  TYR   A OH   1 
ATOM   1121 H H    A TYR   A 1 42  ? 30.903 3.581   -4.961  0.40 12.11 ?  42  TYR   A H    1 
ATOM   1122 H H    B TYR   A 1 42  ? 30.586 3.659   -4.924  0.60 12.63 ?  42  TYR   A H    1 
ATOM   1123 H HA   A TYR   A 1 42  ? 33.318 4.502   -4.276  0.40 12.85 ?  42  TYR   A HA   1 
ATOM   1124 H HA   B TYR   A 1 42  ? 33.113 4.407   -4.360  0.60 12.77 ?  42  TYR   A HA   1 
ATOM   1125 H HB2  A TYR   A 1 42  ? 31.034 6.051   -4.886  0.40 13.57 ?  42  TYR   A HB2  1 
ATOM   1126 H HB2  B TYR   A 1 42  ? 30.970 6.076   -5.117  0.60 13.52 ?  42  TYR   A HB2  1 
ATOM   1127 H HB3  A TYR   A 1 42  ? 32.535 6.564   -4.893  0.40 13.57 ?  42  TYR   A HB3  1 
ATOM   1128 H HB3  B TYR   A 1 42  ? 32.475 6.559   -4.939  0.60 13.52 ?  42  TYR   A HB3  1 
ATOM   1129 H HD1  A TYR   A 1 42  ? 34.053 5.351   -6.666  0.40 14.46 ?  42  TYR   A HD1  1 
ATOM   1130 H HD1  B TYR   A 1 42  ? 34.189 5.348   -6.492  0.60 15.43 ?  42  TYR   A HD1  1 
ATOM   1131 H HD2  A TYR   A 1 42  ? 30.071 5.582   -6.986  0.40 15.88 ?  42  TYR   A HD2  1 
ATOM   1132 H HD2  B TYR   A 1 42  ? 30.267 5.486   -7.259  0.60 15.92 ?  42  TYR   A HD2  1 
ATOM   1133 H HE1  A TYR   A 1 42  ? 34.214 4.901   -8.922  0.40 14.17 ?  42  TYR   A HE1  1 
ATOM   1134 H HE1  B TYR   A 1 42  ? 34.599 4.805   -8.704  0.60 15.61 ?  42  TYR   A HE1  1 
ATOM   1135 H HE2  A TYR   A 1 42  ? 30.228 5.130   -9.254  0.40 15.89 ?  42  TYR   A HE2  1 
ATOM   1136 H HE2  B TYR   A 1 42  ? 30.671 4.946   -9.465  0.60 16.48 ?  42  TYR   A HE2  1 
ATOM   1137 H HH   A TYR   A 1 42  ? 31.603 4.690   -11.015 0.40 15.56 ?  42  TYR   A HH   1 
ATOM   1138 H HH   B TYR   A 1 42  ? 33.719 4.296   -10.713 0.60 17.10 ?  42  TYR   A HH   1 
ATOM   1139 N N    . LEU   A 1 43  ? 31.142 4.256   -2.095  1.00 10.23 ?  43  LEU   A N    1 
ATOM   1140 C CA   . LEU   A 1 43  ? 30.707 4.593   -0.744  1.00 9.94  ?  43  LEU   A CA   1 
ATOM   1141 C C    . LEU   A 1 43  ? 30.236 6.042   -0.651  1.00 9.84  ?  43  LEU   A C    1 
ATOM   1142 O O    . LEU   A 1 43  ? 30.508 6.747   0.324   1.00 10.91 ?  43  LEU   A O    1 
ATOM   1143 C CB   . LEU   A 1 43  ? 31.758 4.277   0.315   1.00 10.37 ?  43  LEU   A CB   1 
ATOM   1144 C CG   . LEU   A 1 43  ? 32.244 2.832   0.402   1.00 11.00 ?  43  LEU   A CG   1 
ATOM   1145 C CD1  . LEU   A 1 43  ? 33.286 2.714   1.496   1.00 11.80 ?  43  LEU   A CD1  1 
ATOM   1146 C CD2  . LEU   A 1 43  ? 31.097 1.871   0.655   1.00 11.55 ?  43  LEU   A CD2  1 
ATOM   1147 H H    A LEU   A 1 43  ? 30.751 3.562   -2.420  0.40 12.27 ?  43  LEU   A H    1 
ATOM   1148 H H    B LEU   A 1 43  ? 30.824 3.504   -2.368  0.60 12.27 ?  43  LEU   A H    1 
ATOM   1149 H HA   . LEU   A 1 43  ? 29.939 4.041   -0.537  1.00 11.93 ?  43  LEU   A HA   1 
ATOM   1150 H HB2  . LEU   A 1 43  ? 32.532 4.838   0.154   1.00 12.44 ?  43  LEU   A HB2  1 
ATOM   1151 H HB3  . LEU   A 1 43  ? 31.380 4.502   1.186   1.00 12.44 ?  43  LEU   A HB3  1 
ATOM   1152 H HG   . LEU   A 1 43  ? 32.667 2.589   -0.438  1.00 13.20 ?  43  LEU   A HG   1 
ATOM   1153 H HD11 . LEU   A 1 43  ? 33.595 1.796   1.546   1.00 14.16 ?  43  LEU   A HD11 1 
ATOM   1154 H HD12 . LEU   A 1 43  ? 34.030 3.303   1.294   1.00 14.16 ?  43  LEU   A HD12 1 
ATOM   1155 H HD13 . LEU   A 1 43  ? 32.885 2.972   2.344   1.00 14.16 ?  43  LEU   A HD13 1 
ATOM   1156 H HD21 . LEU   A 1 43  ? 31.460 0.987   0.814   1.00 13.86 ?  43  LEU   A HD21 1 
ATOM   1157 H HD22 . LEU   A 1 43  ? 30.604 2.174   1.431   1.00 13.86 ?  43  LEU   A HD22 1 
ATOM   1158 H HD23 . LEU   A 1 43  ? 30.523 1.862   -0.125  1.00 13.86 ?  43  LEU   A HD23 1 
ATOM   1159 N N    A LYS   A 1 44  ? 29.507 6.486   -1.675  0.40 10.70 ?  44  LYS   A N    1 
ATOM   1160 N N    B LYS   A 1 44  ? 29.496 6.480   -1.670  0.60 10.40 ?  44  LYS   A N    1 
ATOM   1161 C CA   A LYS   A 1 44  ? 28.863 7.799   -1.668  0.40 11.33 ?  44  LYS   A CA   1 
ATOM   1162 C CA   B LYS   A 1 44  ? 28.857 7.796   -1.667  0.60 10.55 ?  44  LYS   A CA   1 
ATOM   1163 C C    A LYS   A 1 44  ? 27.444 7.601   -1.156  0.40 10.35 ?  44  LYS   A C    1 
ATOM   1164 C C    B LYS   A 1 44  ? 27.437 7.606   -1.158  0.60 9.76  ?  44  LYS   A C    1 
ATOM   1165 O O    A LYS   A 1 44  ? 26.578 7.082   -1.865  0.40 11.11 ?  44  LYS   A O    1 
ATOM   1166 O O    B LYS   A 1 44  ? 26.569 7.091   -1.866  0.60 10.99 ?  44  LYS   A O    1 
ATOM   1167 C CB   A LYS   A 1 44  ? 28.891 8.425   -3.057  0.40 13.41 ?  44  LYS   A CB   1 
ATOM   1168 C CB   B LYS   A 1 44  ? 28.890 8.419   -3.056  0.60 12.36 ?  44  LYS   A CB   1 
ATOM   1169 C CG   A LYS   A 1 44  ? 30.275 8.871   -3.506  0.40 16.06 ?  44  LYS   A CG   1 
ATOM   1170 C CG   B LYS   A 1 44  ? 30.268 8.901   -3.477  0.60 15.47 ?  44  LYS   A CG   1 
ATOM   1171 C CD   A LYS   A 1 44  ? 30.923 9.820   -2.500  0.40 19.76 ?  44  LYS   A CD   1 
ATOM   1172 C CD   B LYS   A 1 44  ? 30.925 9.761   -2.398  0.60 20.55 ?  44  LYS   A CD   1 
ATOM   1173 C CE   A LYS   A 1 44  ? 32.261 10.329  -3.001  0.40 22.18 ?  44  LYS   A CE   1 
ATOM   1174 C CE   B LYS   A 1 44  ? 32.282 10.267  -2.835  0.60 23.62 ?  44  LYS   A CE   1 
ATOM   1175 N NZ   A LYS   A 1 44  ? 33.032 11.015  -1.929  0.40 23.48 ?  44  LYS   A NZ   1 
ATOM   1176 N NZ   B LYS   A 1 44  ? 33.079 10.766  -1.680  0.60 24.87 ?  44  LYS   A NZ   1 
ATOM   1177 H H    A LYS   A 1 44  ? 29.370 6.039   -2.397  0.40 12.84 ?  44  LYS   A H    1 
ATOM   1178 H H    B LYS   A 1 44  ? 29.351 6.029   -2.388  0.60 12.48 ?  44  LYS   A H    1 
ATOM   1179 H HA   A LYS   A 1 44  ? 29.320 8.380   -1.042  0.40 13.59 ?  44  LYS   A HA   1 
ATOM   1180 H HA   B LYS   A 1 44  ? 29.306 8.372   -1.032  0.60 12.66 ?  44  LYS   A HA   1 
ATOM   1181 H HB2  A LYS   A 1 44  ? 28.569 7.778   -3.703  0.40 16.09 ?  44  LYS   A HB2  1 
ATOM   1182 H HB2  B LYS   A 1 44  ? 28.598 7.763   -3.707  0.60 14.83 ?  44  LYS   A HB2  1 
ATOM   1183 H HB3  A LYS   A 1 44  ? 28.317 9.208   -3.062  0.40 16.09 ?  44  LYS   A HB3  1 
ATOM   1184 H HB3  B LYS   A 1 44  ? 28.295 9.187   -3.072  0.60 14.83 ?  44  LYS   A HB3  1 
ATOM   1185 H HG2  A LYS   A 1 44  ? 30.847 8.094   -3.600  0.40 19.27 ?  44  LYS   A HG2  1 
ATOM   1186 H HG2  B LYS   A 1 44  ? 30.839 8.136   -3.643  0.60 18.56 ?  44  LYS   A HG2  1 
ATOM   1187 H HG3  A LYS   A 1 44  ? 30.203 9.338   -4.355  0.40 19.27 ?  44  LYS   A HG3  1 
ATOM   1188 H HG3  B LYS   A 1 44  ? 30.189 9.441   -4.282  0.60 18.56 ?  44  LYS   A HG3  1 
ATOM   1189 H HD2  A LYS   A 1 44  ? 30.335 10.577  -2.349  0.40 23.71 ?  44  LYS   A HD2  1 
ATOM   1190 H HD2  B LYS   A 1 44  ? 30.351 10.518  -2.198  0.60 24.65 ?  44  LYS   A HD2  1 
ATOM   1191 H HD3  A LYS   A 1 44  ? 31.081 9.346   -1.666  0.40 23.71 ?  44  LYS   A HD3  1 
ATOM   1192 H HD3  B LYS   A 1 44  ? 31.067 9.226   -1.600  0.60 24.65 ?  44  LYS   A HD3  1 
ATOM   1193 H HE2  A LYS   A 1 44  ? 32.787 9.578   -3.319  0.40 26.61 ?  44  LYS   A HE2  1 
ATOM   1194 H HE2  B LYS   A 1 44  ? 32.774 9.541   -3.250  0.60 28.34 ?  44  LYS   A HE2  1 
ATOM   1195 H HE3  A LYS   A 1 44  ? 32.111 10.961  -3.719  0.40 26.61 ?  44  LYS   A HE3  1 
ATOM   1196 H HE3  B LYS   A 1 44  ? 32.163 10.995  -3.462  0.60 28.34 ?  44  LYS   A HE3  1 
ATOM   1197 H HZ1  A LYS   A 1 44  ? 33.810 11.301  -2.250  0.40 28.17 ?  44  LYS   A HZ1  1 
ATOM   1198 H HZ1  B LYS   A 1 44  ? 33.869 11.060  -1.961  0.60 29.84 ?  44  LYS   A HZ1  1 
ATOM   1199 H HZ2  A LYS   A 1 44  ? 32.570 11.711  -1.622  0.40 28.17 ?  44  LYS   A HZ2  1 
ATOM   1200 H HZ2  B LYS   A 1 44  ? 32.646 11.438  -1.283  0.60 29.84 ?  44  LYS   A HZ2  1 
ATOM   1201 H HZ3  A LYS   A 1 44  ? 33.185 10.451  -1.256  0.40 28.17 ?  44  LYS   A HZ3  1 
ATOM   1202 H HZ3  B LYS   A 1 44  ? 33.203 10.114  -1.089  0.60 29.84 ?  44  LYS   A HZ3  1 
ATOM   1203 N N    . HIS   A 1 45  ? 27.211 7.996   0.092   1.00 9.83  ?  45  HIS   A N    1 
ATOM   1204 C CA   . HIS   A 1 45  ? 25.978 7.659   0.796   1.00 10.08 ?  45  HIS   A CA   1 
ATOM   1205 C C    . HIS   A 1 45  ? 24.961 8.786   0.636   1.00 10.77 ?  45  HIS   A C    1 
ATOM   1206 O O    . HIS   A 1 45  ? 24.671 9.541   1.562   1.00 12.61 ?  45  HIS   A O    1 
ATOM   1207 C CB   . HIS   A 1 45  ? 26.283 7.414   2.261   1.00 9.89  ?  45  HIS   A CB   1 
ATOM   1208 C CG   . HIS   A 1 45  ? 27.387 6.436   2.489   1.00 9.62  ?  45  HIS   A CG   1 
ATOM   1209 N ND1  . HIS   A 1 45  ? 27.381 5.154   1.973   1.00 9.95  ?  45  HIS   A ND1  1 
ATOM   1210 C CD2  . HIS   A 1 45  ? 28.553 6.583   3.161   1.00 10.02 ?  45  HIS   A CD2  1 
ATOM   1211 C CE1  . HIS   A 1 45  ? 28.498 4.553   2.350   1.00 9.92  ?  45  HIS   A CE1  1 
ATOM   1212 N NE2  . HIS   A 1 45  ? 29.227 5.396   3.064   1.00 10.04 ?  45  HIS   A NE2  1 
ATOM   1213 H H    A HIS   A 1 45  ? 27.758 8.464   0.560   0.40 11.79 ?  45  HIS   A H    1 
ATOM   1214 H H    B HIS   A 1 45  ? 27.758 8.463   0.560   0.60 11.79 ?  45  HIS   A H    1 
ATOM   1215 H HA   . HIS   A 1 45  ? 25.593 6.851   0.417   1.00 12.09 ?  45  HIS   A HA   1 
ATOM   1216 H HB2  . HIS   A 1 45  ? 26.526 8.257   2.673   1.00 11.87 ?  45  HIS   A HB2  1 
ATOM   1217 H HB3  . HIS   A 1 45  ? 25.478 7.064   2.690   1.00 11.87 ?  45  HIS   A HB3  1 
ATOM   1218 H HD2  . HIS   A 1 45  ? 28.841 7.353   3.610   1.00 12.02 ?  45  HIS   A HD2  1 
ATOM   1219 H HE1  . HIS   A 1 45  ? 28.736 3.679   2.152   1.00 11.90 ?  45  HIS   A HE1  1 
ATOM   1220 H HE2  . HIS   A 1 45  ? 29.994 5.229   3.416   1.00 12.05 ?  45  HIS   A HE2  1 
ATOM   1221 N N    A GLY   A 1 46  ? 24.483 8.937   -0.595  0.40 11.62 ?  46  GLY   A N    1 
ATOM   1222 N N    B GLY   A 1 46  ? 24.324 8.823   -0.533  0.60 11.59 ?  46  GLY   A N    1 
ATOM   1223 C CA   A GLY   A 1 46  ? 23.733 10.126  -0.954  0.40 11.84 ?  46  GLY   A CA   1 
ATOM   1224 C CA   B GLY   A 1 46  ? 23.458 9.943   -0.867  0.60 11.63 ?  46  GLY   A CA   1 
ATOM   1225 C C    A GLY   A 1 46  ? 22.239 10.007  -0.742  0.40 11.68 ?  46  GLY   A C    1 
ATOM   1226 C C    B GLY   A 1 46  ? 21.997 9.815   -0.474  0.60 11.24 ?  46  GLY   A C    1 
ATOM   1227 O O    A GLY   A 1 46  ? 21.561 11.006  -0.488  0.40 12.29 ?  46  GLY   A O    1 
ATOM   1228 O O    B GLY   A 1 46  ? 21.375 10.794  -0.051  0.60 12.04 ?  46  GLY   A O    1 
ATOM   1229 H H    A GLY   A 1 46  ? 24.575 8.369   -1.234  0.40 13.94 ?  46  GLY   A H    1 
ATOM   1230 H H    B GLY   A 1 46  ? 24.370 8.220   -1.143  0.60 13.91 ?  46  GLY   A H    1 
ATOM   1231 H HA2  A GLY   A 1 46  ? 24.059 10.875  -0.426  0.40 14.20 ?  46  GLY   A HA2  1 
ATOM   1232 H HA2  B GLY   A 1 46  ? 23.797 10.742  -0.436  0.60 13.96 ?  46  GLY   A HA2  1 
ATOM   1233 H HA3  A GLY   A 1 46  ? 23.888 10.328  -1.889  0.40 14.20 ?  46  GLY   A HA3  1 
ATOM   1234 H HA3  B GLY   A 1 46  ? 23.485 10.088  -1.824  0.60 13.96 ?  46  GLY   A HA3  1 
ATOM   1235 N N    A GLY   A 1 47  ? 21.711 8.794   -0.854  0.40 10.77 ?  47  GLY   A N    1 
ATOM   1236 N N    B GLY   A 1 47  ? 21.421 8.627   -0.632  0.60 11.60 ?  47  GLY   A N    1 
ATOM   1237 C CA   A GLY   A 1 47  ? 20.277 8.597   -0.787  0.40 11.05 ?  47  GLY   A CA   1 
ATOM   1238 C CA   B GLY   A 1 47  ? 19.992 8.454   -0.465  0.60 11.96 ?  47  GLY   A CA   1 
ATOM   1239 C C    A GLY   A 1 47  ? 19.959 7.164   -0.418  0.40 10.80 ?  47  GLY   A C    1 
ATOM   1240 C C    B GLY   A 1 47  ? 19.666 7.033   -0.066  0.60 10.73 ?  47  GLY   A C    1 
ATOM   1241 O O    A GLY   A 1 47  ? 20.850 6.349   -0.169  0.40 11.30 ?  47  GLY   A O    1 
ATOM   1242 O O    B GLY   A 1 47  ? 20.551 6.191   0.101   0.60 10.81 ?  47  GLY   A O    1 
ATOM   1243 H H    A GLY   A 1 47  ? 22.165 8.074   -0.961  0.40 12.93 ?  47  GLY   A H    1 
ATOM   1244 H H    B GLY   A 1 47  ? 21.841 7.905   -0.830  0.60 13.92 ?  47  GLY   A H    1 
ATOM   1245 H HA2  A GLY   A 1 47  ? 19.889 9.193   -0.125  0.40 13.26 ?  47  GLY   A HA2  1 
ATOM   1246 H HA2  B GLY   A 1 47  ? 19.661 9.053   0.221   0.60 14.35 ?  47  GLY   A HA2  1 
ATOM   1247 H HA3  A GLY   A 1 47  ? 19.884 8.791   -1.652  0.40 13.26 ?  47  GLY   A HA3  1 
ATOM   1248 H HA3  B GLY   A 1 47  ? 19.536 8.655   -1.300  0.60 14.35 ?  47  GLY   A HA3  1 
ATOM   1249 N N    A GLY   A 1 48  ? 18.668 6.859   -0.395  0.40 10.95 ?  48  GLY   A N    1 
ATOM   1250 N N    B GLY   A 1 48  ? 18.370 6.770   0.088   0.60 11.02 ?  48  GLY   A N    1 
ATOM   1251 C CA   A GLY   A 1 48  ? 18.247 5.522   -0.028  0.40 10.85 ?  48  GLY   A CA   1 
ATOM   1252 C CA   B GLY   A 1 48  ? 17.940 5.453   0.504   0.60 10.72 ?  48  GLY   A CA   1 
ATOM   1253 C C    A GLY   A 1 48  ? 18.654 5.186   1.393   0.40 10.80 ?  48  GLY   A C    1 
ATOM   1254 C C    B GLY   A 1 48  ? 18.528 5.079   1.850   0.60 10.73 ?  48  GLY   A C    1 
ATOM   1255 O O    A GLY   A 1 48  ? 18.807 6.062   2.251   0.40 10.94 ?  48  GLY   A O    1 
ATOM   1256 O O    B GLY   A 1 48  ? 18.712 5.917   2.743   0.60 11.24 ?  48  GLY   A O    1 
ATOM   1257 H H    A GLY   A 1 48  ? 18.037 7.400   -0.584  0.40 13.14 ?  48  GLY   A H    1 
ATOM   1258 H H    B GLY   A 1 48  ? 17.728 7.333   -0.040  0.60 13.22 ?  48  GLY   A H    1 
ATOM   1259 H HA2  A GLY   A 1 48  ? 17.285 5.455   -0.099  0.40 13.02 ?  48  GLY   A HA2  1 
ATOM   1260 H HA2  B GLY   A 1 48  ? 16.966 5.414   0.557   0.60 12.86 ?  48  GLY   A HA2  1 
ATOM   1261 H HA3  A GLY   A 1 48  ? 18.653 4.874   -0.622  0.40 13.02 ?  48  GLY   A HA3  1 
ATOM   1262 H HA3  B GLY   A 1 48  ? 18.239 4.800   -0.143  0.60 12.86 ?  48  GLY   A HA3  1 
ATOM   1263 N N    A VAL   A 1 49  ? 18.843 3.888   1.645   0.40 10.78 ?  49  VAL   A N    1 
ATOM   1264 N N    B VAL   A 1 49  ? 18.823 3.786   1.996   0.60 10.10 ?  49  VAL   A N    1 
ATOM   1265 C CA   A VAL   A 1 49  ? 19.277 3.451   2.969   0.40 10.80 ?  49  VAL   A CA   1 
ATOM   1266 C CA   B VAL   A 1 49  ? 19.429 3.283   3.225   0.60 10.42 ?  49  VAL   A CA   1 
ATOM   1267 C C    A VAL   A 1 49  ? 20.607 4.095   3.335   0.40 10.42 ?  49  VAL   A C    1 
ATOM   1268 C C    B VAL   A 1 49  ? 20.710 4.043   3.549   0.60 9.77  ?  49  VAL   A C    1 
ATOM   1269 O O    A VAL   A 1 49  ? 20.804 4.534   4.471   0.40 10.99 ?  49  VAL   A O    1 
ATOM   1270 O O    B VAL   A 1 49  ? 20.939 4.432   4.697   0.60 9.67  ?  49  VAL   A O    1 
ATOM   1271 C CB   A VAL   A 1 49  ? 19.352 1.913   3.034   0.40 11.44 ?  49  VAL   A CB   1 
ATOM   1272 C CB   B VAL   A 1 49  ? 19.698 1.773   3.100   0.60 10.54 ?  49  VAL   A CB   1 
ATOM   1273 C CG1  A VAL   A 1 49  ? 20.074 1.465   4.297   0.40 11.38 ?  49  VAL   A CG1  1 
ATOM   1274 C CG1  B VAL   A 1 49  ? 20.565 1.297   4.250   0.60 10.25 ?  49  VAL   A CG1  1 
ATOM   1275 C CG2  A VAL   A 1 49  ? 17.955 1.312   2.978   0.40 12.53 ?  49  VAL   A CG2  1 
ATOM   1276 C CG2  B VAL   A 1 49  ? 18.390 0.991   3.032   0.60 11.65 ?  49  VAL   A CG2  1 
ATOM   1277 H H    A VAL   A 1 49  ? 18.734 3.253   1.076   0.40 12.94 ?  49  VAL   A H    1 
ATOM   1278 H H    B VAL   A 1 49  ? 18.681 3.180   1.401   0.60 12.12 ?  49  VAL   A H    1 
ATOM   1279 H HA   A VAL   A 1 49  ? 18.622 3.735   3.624   0.40 12.95 ?  49  VAL   A HA   1 
ATOM   1280 H HA   B VAL   A 1 49  ? 18.813 3.413   3.961   0.60 12.50 ?  49  VAL   A HA   1 
ATOM   1281 H HB   A VAL   A 1 49  ? 19.854 1.583   2.271   0.40 13.72 ?  49  VAL   A HB   1 
ATOM   1282 H HB   B VAL   A 1 49  ? 20.184 1.606   2.279   0.60 12.65 ?  49  VAL   A HB   1 
ATOM   1283 H HG11 A VAL   A 1 49  ? 19.865 0.534   4.467   0.40 13.66 ?  49  VAL   A HG11 1 
ATOM   1284 H HG11 B VAL   A 1 49  ? 20.478 0.335   4.336   0.60 12.30 ?  49  VAL   A HG11 1 
ATOM   1285 H HG12 A VAL   A 1 49  ? 21.030 1.571   4.175   0.40 13.66 ?  49  VAL   A HG12 1 
ATOM   1286 H HG12 B VAL   A 1 49  ? 21.492 1.526   4.069   0.60 12.30 ?  49  VAL   A HG12 1 
ATOM   1287 H HG13 A VAL   A 1 49  ? 19.771 2.010   5.043   0.40 13.66 ?  49  VAL   A HG13 1 
ATOM   1288 H HG13 B VAL   A 1 49  ? 20.271 1.727   5.069   0.60 12.30 ?  49  VAL   A HG13 1 
ATOM   1289 H HG21 A VAL   A 1 49  ? 18.026 0.344   3.013   0.40 15.04 ?  49  VAL   A HG21 1 
ATOM   1290 H HG21 B VAL   A 1 49  ? 18.584 0.043   2.955   0.60 13.98 ?  49  VAL   A HG21 1 
ATOM   1291 H HG22 A VAL   A 1 49  ? 17.444 1.633   3.738   0.40 15.04 ?  49  VAL   A HG22 1 
ATOM   1292 H HG22 B VAL   A 1 49  ? 17.876 1.155   3.842   0.60 13.98 ?  49  VAL   A HG22 1 
ATOM   1293 H HG23 A VAL   A 1 49  ? 17.529 1.584   2.152   0.40 15.04 ?  49  VAL   A HG23 1 
ATOM   1294 H HG23 B VAL   A 1 49  ? 17.882 1.286   2.258   0.60 13.98 ?  49  VAL   A HG23 1 
ATOM   1295 N N    A ALA   A 1 50  ? 21.546 4.134   2.387   0.40 9.99  ?  50  ALA   A N    1 
ATOM   1296 N N    B ALA   A 1 50  ? 21.589 4.200   2.557   0.60 9.62  ?  50  ALA   A N    1 
ATOM   1297 C CA   A ALA   A 1 50  ? 22.869 4.687   2.661   0.40 9.60  ?  50  ALA   A CA   1 
ATOM   1298 C CA   B ALA   A 1 50  ? 22.908 4.769   2.817   0.60 9.27  ?  50  ALA   A CA   1 
ATOM   1299 C C    A ALA   A 1 50  ? 22.780 6.149   3.072   0.40 9.93  ?  50  ALA   A C    1 
ATOM   1300 C C    B ALA   A 1 50  ? 22.804 6.220   3.264   0.60 9.14  ?  50  ALA   A C    1 
ATOM   1301 O O    A ALA   A 1 50  ? 23.434 6.579   4.028   0.40 10.13 ?  50  ALA   A O    1 
ATOM   1302 O O    B ALA   A 1 50  ? 23.423 6.620   4.256   0.60 9.45  ?  50  ALA   A O    1 
ATOM   1303 C CB   A ALA   A 1 50  ? 23.747 4.542   1.421   0.40 9.81  ?  50  ALA   A CB   1 
ATOM   1304 C CB   B ALA   A 1 50  ? 23.774 4.655   1.566   0.60 9.21  ?  50  ALA   A CB   1 
ATOM   1305 H H    A ALA   A 1 50  ? 21.442 3.842   1.588   0.40 11.99 ?  50  ALA   A H    1 
ATOM   1306 H H    B ALA   A 1 50  ? 21.449 3.983   1.735   0.60 11.54 ?  50  ALA   A H    1 
ATOM   1307 H HA   A ALA   A 1 50  ? 23.281 4.199   3.390   0.40 11.52 ?  50  ALA   A HA   1 
ATOM   1308 H HA   B ALA   A 1 50  ? 23.335 4.268   3.529   0.60 11.13 ?  50  ALA   A HA   1 
ATOM   1309 H HB1  A ALA   A 1 50  ? 24.620 4.916   1.610   0.40 11.77 ?  50  ALA   A HB1  1 
ATOM   1310 H HB1  B ALA   A 1 50  ? 24.644 5.040   1.752   0.60 11.05 ?  50  ALA   A HB1  1 
ATOM   1311 H HB2  A ALA   A 1 50  ? 23.824 3.605   1.197   0.40 11.77 ?  50  ALA   A HB2  1 
ATOM   1312 H HB2  B ALA   A 1 50  ? 23.864 3.722   1.329   0.60 11.05 ?  50  ALA   A HB2  1 
ATOM   1313 H HB3  A ALA   A 1 50  ? 23.331 5.027   0.689   0.40 11.77 ?  50  ALA   A HB3  1 
ATOM   1314 H HB3  B ALA   A 1 50  ? 23.345 5.143   0.844   0.60 11.05 ?  50  ALA   A HB3  1 
ATOM   1315 N N    A GLY   A 1 51  ? 21.982 6.934   2.352   0.40 9.99  ?  51  GLY   A N    1 
ATOM   1316 N N    B GLY   A 1 51  ? 22.024 7.024   2.544   0.60 9.82  ?  51  GLY   A N    1 
ATOM   1317 C CA   A GLY   A 1 51  ? 21.853 8.338   2.695   0.40 10.17 ?  51  GLY   A CA   1 
ATOM   1318 C CA   B GLY   A 1 51  ? 21.837 8.402   2.961   0.60 10.00 ?  51  GLY   A CA   1 
ATOM   1319 C C    A GLY   A 1 51  ? 21.244 8.545   4.068   0.40 9.70  ?  51  GLY   A C    1 
ATOM   1320 C C    B GLY   A 1 51  ? 21.227 8.493   4.345   0.60 9.81  ?  51  GLY   A C    1 
ATOM   1321 O O    A GLY   A 1 51  ? 21.640 9.453   4.803   0.40 9.83  ?  51  GLY   A O    1 
ATOM   1322 O O    B GLY   A 1 51  ? 21.597 9.359   5.144   0.60 10.24 ?  51  GLY   A O    1 
ATOM   1323 H H    A GLY   A 1 51  ? 21.522 6.679   1.673   0.40 11.98 ?  51  GLY   A H    1 
ATOM   1324 H H    B GLY   A 1 51  ? 21.599 6.797   1.828   0.60 11.79 ?  51  GLY   A H    1 
ATOM   1325 H HA2  A GLY   A 1 51  ? 22.730 8.754   2.685   0.40 12.20 ?  51  GLY   A HA2  1 
ATOM   1326 H HA2  B GLY   A 1 51  ? 22.696 8.854   2.968   0.60 12.00 ?  51  GLY   A HA2  1 
ATOM   1327 H HA3  A GLY   A 1 51  ? 21.293 8.780   2.041   0.40 12.20 ?  51  GLY   A HA3  1 
ATOM   1328 H HA3  B GLY   A 1 51  ? 21.256 8.856   2.328   0.60 12.00 ?  51  GLY   A HA3  1 
ATOM   1329 N N    A ALA   A 1 52  ? 20.263 7.711   4.428   0.40 10.10 ?  52  ALA   A N    1 
ATOM   1330 N N    B ALA   A 1 52  ? 20.285 7.596   4.647   0.60 10.19 ?  52  ALA   A N    1 
ATOM   1331 C CA   A ALA   A 1 52  ? 19.619 7.842   5.731   0.40 9.98  ?  52  ALA   A CA   1 
ATOM   1332 C CA   B ALA   A 1 52  ? 19.622 7.613   5.946   0.60 10.60 ?  52  ALA   A CA   1 
ATOM   1333 C C    A ALA   A 1 52  ? 20.548 7.410   6.861   0.40 9.70  ?  52  ALA   A C    1 
ATOM   1334 C C    B ALA   A 1 52  ? 20.578 7.214   7.066   0.60 9.97  ?  52  ALA   A C    1 
ATOM   1335 O O    A ALA   A 1 52  ? 20.636 8.087   7.892   0.40 10.60 ?  52  ALA   A O    1 
ATOM   1336 O O    B ALA   A 1 52  ? 20.629 7.868   8.115   0.60 10.82 ?  52  ALA   A O    1 
ATOM   1337 C CB   A ALA   A 1 52  ? 18.313 7.044   5.754   0.40 10.19 ?  52  ALA   A CB   1 
ATOM   1338 C CB   B ALA   A 1 52  ? 18.398 6.696   5.911   0.60 11.91 ?  52  ALA   A CB   1 
ATOM   1339 H H    A ALA   A 1 52  ? 19.966 7.064   3.943   0.40 12.11 ?  52  ALA   A H    1 
ATOM   1340 H H    B ALA   A 1 52  ? 20.025 6.964   4.115   0.60 12.23 ?  52  ALA   A H    1 
ATOM   1341 H HA   A ALA   A 1 52  ? 19.393 8.770   5.872   0.40 11.98 ?  52  ALA   A HA   1 
ATOM   1342 H HA   B ALA   A 1 52  ? 19.317 8.510   6.121   0.60 12.72 ?  52  ALA   A HA   1 
ATOM   1343 H HB1  A ALA   A 1 52  ? 17.895 7.143   6.625   0.40 12.22 ?  52  ALA   A HB1  1 
ATOM   1344 H HB1  B ALA   A 1 52  ? 17.946 6.744   6.766   0.60 14.29 ?  52  ALA   A HB1  1 
ATOM   1345 H HB2  A ALA   A 1 52  ? 17.720 7.385   5.064   0.40 12.22 ?  52  ALA   A HB2  1 
ATOM   1346 H HB2  B ALA   A 1 52  ? 17.801 6.995   5.205   0.60 14.29 ?  52  ALA   A HB2  1 
ATOM   1347 H HB3  A ALA   A 1 52  ? 18.507 6.107   5.587   0.40 12.22 ?  52  ALA   A HB3  1 
ATOM   1348 H HB3  B ALA   A 1 52  ? 18.684 5.786   5.735   0.60 14.29 ?  52  ALA   A HB3  1 
ATOM   1349 N N    A LEU   A 1 53  ? 21.250 6.287   6.688   0.40 9.63  ?  53  LEU   A N    1 
ATOM   1350 N N    B LEU   A 1 53  ? 21.330 6.125   6.879   0.60 9.84  ?  53  LEU   A N    1 
ATOM   1351 C CA   A LEU   A 1 53  ? 22.185 5.837   7.717   0.40 10.22 ?  53  LEU   A CA   1 
ATOM   1352 C CA   B LEU   A 1 53  ? 22.328 5.766   7.882   0.60 9.67  ?  53  LEU   A CA   1 
ATOM   1353 C C    A LEU   A 1 53  ? 23.290 6.860   7.935   0.40 10.45 ?  53  LEU   A C    1 
ATOM   1354 C C    B LEU   A 1 53  ? 23.340 6.890   8.056   0.60 9.88  ?  53  LEU   A C    1 
ATOM   1355 O O    A LEU   A 1 53  ? 23.679 7.135   9.075   0.40 10.87 ?  53  LEU   A O    1 
ATOM   1356 O O    B LEU   A 1 53  ? 23.635 7.308   9.180   0.60 10.69 ?  53  LEU   A O    1 
ATOM   1357 C CB   A LEU   A 1 53  ? 22.790 4.487   7.322   0.40 11.12 ?  53  LEU   A CB   1 
ATOM   1358 C CB   B LEU   A 1 53  ? 23.043 4.465   7.503   0.60 9.21  ?  53  LEU   A CB   1 
ATOM   1359 C CG   A LEU   A 1 53  ? 21.879 3.259   7.412   0.40 11.28 ?  53  LEU   A CG   1 
ATOM   1360 C CG   B LEU   A 1 53  ? 22.250 3.155   7.562   0.60 9.83  ?  53  LEU   A CG   1 
ATOM   1361 C CD1  A LEU   A 1 53  ? 22.590 2.033   6.862   0.40 11.09 ?  53  LEU   A CD1  1 
ATOM   1362 C CD1  B LEU   A 1 53  ? 23.041 2.055   6.879   0.60 10.44 ?  53  LEU   A CD1  1 
ATOM   1363 C CD2  A LEU   A 1 53  ? 21.436 3.025   8.847   0.40 11.97 ?  53  LEU   A CD2  1 
ATOM   1364 C CD2  B LEU   A 1 53  ? 21.937 2.764   8.990   0.60 10.67 ?  53  LEU   A CD2  1 
ATOM   1365 H H    A LEU   A 1 53  ? 21.208 5.781   5.998   0.40 11.55 ?  53  LEU   A H    1 
ATOM   1366 H H    B LEU   A 1 53  ? 21.279 5.584   6.204   0.60 11.80 ?  53  LEU   A H    1 
ATOM   1367 H HA   A LEU   A 1 53  ? 21.709 5.723   8.556   0.40 12.26 ?  53  LEU   A HA   1 
ATOM   1368 H HA   B LEU   A 1 53  ? 21.883 5.625   8.733   0.60 11.61 ?  53  LEU   A HA   1 
ATOM   1369 H HB2  A LEU   A 1 53  ? 23.092 4.550   6.403   0.40 13.34 ?  53  LEU   A HB2  1 
ATOM   1370 H HB2  B LEU   A 1 53  ? 23.367 4.556   6.596   0.60 11.06 ?  53  LEU   A HB2  1 
ATOM   1371 H HB3  A LEU   A 1 53  ? 23.551 4.316   7.897   0.40 13.34 ?  53  LEU   A HB3  1 
ATOM   1372 H HB3  B LEU   A 1 53  ? 23.800 4.357   8.101   0.60 11.06 ?  53  LEU   A HB3  1 
ATOM   1373 H HG   A LEU   A 1 53  ? 21.085 3.413   6.872   0.40 13.53 ?  53  LEU   A HG   1 
ATOM   1374 H HG   B LEU   A 1 53  ? 21.415 3.263   7.082   0.60 11.79 ?  53  LEU   A HG   1 
ATOM   1375 H HD11 A LEU   A 1 53  ? 21.998 1.269   6.927   0.40 13.31 ?  53  LEU   A HD11 1 
ATOM   1376 H HD11 B LEU   A 1 53  ? 22.538 1.227   6.929   0.60 12.53 ?  53  LEU   A HD11 1 
ATOM   1377 H HD12 A LEU   A 1 53  ? 22.825 2.194   5.934   0.40 13.31 ?  53  LEU   A HD12 1 
ATOM   1378 H HD12 B LEU   A 1 53  ? 23.186 2.299   5.951   0.60 12.53 ?  53  LEU   A HD12 1 
ATOM   1379 H HD13 A LEU   A 1 53  ? 23.394 1.877   7.383   0.40 13.31 ?  53  LEU   A HD13 1 
ATOM   1380 H HD13 B LEU   A 1 53  ? 23.893 1.953   7.331   0.60 12.53 ?  53  LEU   A HD13 1 
ATOM   1381 H HD21 A LEU   A 1 53  ? 20.955 2.186   8.897   0.40 14.36 ?  53  LEU   A HD21 1 
ATOM   1382 H HD21 B LEU   A 1 53  ? 21.376 1.970   8.985   0.60 12.80 ?  53  LEU   A HD21 1 
ATOM   1383 H HD22 A LEU   A 1 53  ? 22.223 2.991   9.415   0.40 14.36 ?  53  LEU   A HD22 1 
ATOM   1384 H HD22 B LEU   A 1 53  ? 22.764 2.583   9.459   0.60 12.80 ?  53  LEU   A HD22 1 
ATOM   1385 H HD23 A LEU   A 1 53  ? 20.861 3.754   9.126   0.40 14.36 ?  53  LEU   A HD23 1 
ATOM   1386 H HD23 B LEU   A 1 53  ? 21.464 3.495   9.420   0.60 12.80 ?  53  LEU   A HD23 1 
ATOM   1387 N N    A ASN   A 1 54  ? 23.817 7.427   6.854   0.40 10.09 ?  54  ASN   A N    1 
ATOM   1388 N N    B ASN   A 1 54  ? 23.873 7.403   6.948   0.60 9.72  ?  54  ASN   A N    1 
ATOM   1389 C CA   A ASN   A 1 54  ? 24.885 8.404   7.001   0.40 10.23 ?  54  ASN   A CA   1 
ATOM   1390 C CA   B ASN   A 1 54  ? 24.909 8.418   7.059   0.60 9.66  ?  54  ASN   A CA   1 
ATOM   1391 C C    A ASN   A 1 54  ? 24.382 9.674   7.679   0.40 10.56 ?  54  ASN   A C    1 
ATOM   1392 C C    B ASN   A 1 54  ? 24.396 9.647   7.806   0.60 9.81  ?  54  ASN   A C    1 
ATOM   1393 O O    A ASN   A 1 54  ? 25.110 10.298  8.458   0.40 10.81 ?  54  ASN   A O    1 
ATOM   1394 O O    B ASN   A 1 54  ? 25.054 10.150  8.724   0.60 9.63  ?  54  ASN   A O    1 
ATOM   1395 C CB   A ASN   A 1 54  ? 25.486 8.715   5.640   0.40 10.20 ?  54  ASN   A CB   1 
ATOM   1396 C CB   B ASN   A 1 54  ? 25.438 8.803   5.687   0.60 9.46  ?  54  ASN   A CB   1 
ATOM   1397 C CG   A ASN   A 1 54  ? 26.535 9.784   5.727   0.40 10.59 ?  54  ASN   A CG   1 
ATOM   1398 C CG   B ASN   A 1 54  ? 26.446 9.911   5.787   0.60 9.38  ?  54  ASN   A CG   1 
ATOM   1399 O OD1  A ASN   A 1 54  ? 27.530 9.628   6.437   0.40 11.05 ?  54  ASN   A OD1  1 
ATOM   1400 O OD1  B ASN   A 1 54  ? 27.462 9.765   6.476   0.60 9.52  ?  54  ASN   A OD1  1 
ATOM   1401 N ND2  A ASN   A 1 54  ? 26.321 10.889  5.029   0.40 11.05 ?  54  ASN   A ND2  1 
ATOM   1402 N ND2  B ASN   A 1 54  ? 26.165 11.045  5.158   0.60 10.28 ?  54  ASN   A ND2  1 
ATOM   1403 H H    A ASN   A 1 54  ? 23.582 7.256   6.048   0.40 12.11 ?  54  ASN   A H    1 
ATOM   1404 H H    B ASN   A 1 54  ? 23.657 7.177   6.145   0.60 11.66 ?  54  ASN   A H    1 
ATOM   1405 H HA   A ASN   A 1 54  ? 25.578 8.025   7.562   0.40 12.27 ?  54  ASN   A HA   1 
ATOM   1406 H HA   B ASN   A 1 54  ? 25.643 8.052   7.569   0.60 11.59 ?  54  ASN   A HA   1 
ATOM   1407 H HB2  A ASN   A 1 54  ? 25.898 7.910   5.290   0.40 12.23 ?  54  ASN   A HB2  1 
ATOM   1408 H HB2  B ASN   A 1 54  ? 25.873 8.031   5.286   0.60 11.34 ?  54  ASN   A HB2  1 
ATOM   1409 H HB3  A ASN   A 1 54  ? 24.785 9.020   5.047   0.40 12.23 ?  54  ASN   A HB3  1 
ATOM   1410 H HB3  B ASN   A 1 54  ? 24.706 9.103   5.130   0.60 11.34 ?  54  ASN   A HB3  1 
ATOM   1411 H HD21 A ASN   A 1 54  ? 26.893 11.528  5.054   0.40 13.26 ?  54  ASN   A HD21 1 
ATOM   1412 H HD21 B ASN   A 1 54  ? 26.713 11.709  5.201   0.60 12.33 ?  54  ASN   A HD21 1 
ATOM   1413 H HD22 A ASN   A 1 54  ? 25.610 10.962  4.551   0.40 13.26 ?  54  ASN   A HD22 1 
ATOM   1414 H HD22 B ASN   A 1 54  ? 25.442 11.115  4.700   0.60 12.33 ?  54  ASN   A HD22 1 
ATOM   1415 N N    A LYS   A 1 55  ? 23.139 10.070  7.394   0.40 10.67 ?  55  LYS   A N    1 
ATOM   1416 N N    B LYS   A 1 55  ? 23.210 10.136  7.431   0.60 10.58 ?  55  LYS   A N    1 
ATOM   1417 C CA   A LYS   A 1 55  ? 22.548 11.226  8.059   0.40 10.67 ?  55  LYS   A CA   1 
ATOM   1418 C CA   B LYS   A 1 55  ? 22.632 11.285  8.117   0.60 11.37 ?  55  LYS   A CA   1 
ATOM   1419 C C    A LYS   A 1 55  ? 22.497 11.022  9.569   0.40 11.15 ?  55  LYS   A C    1 
ATOM   1420 C C    B LYS   A 1 55  ? 22.527 11.030  9.616   0.60 11.36 ?  55  LYS   A C    1 
ATOM   1421 O O    A LYS   A 1 55  ? 22.791 11.943  10.344  0.40 11.90 ?  55  LYS   A O    1 
ATOM   1422 O O    B LYS   A 1 55  ? 22.816 11.919  10.431  0.60 12.00 ?  55  LYS   A O    1 
ATOM   1423 C CB   A LYS   A 1 55  ? 21.151 11.461  7.487   0.40 10.69 ?  55  LYS   A CB   1 
ATOM   1424 C CB   B LYS   A 1 55  ? 21.271 11.616  7.504   0.60 12.93 ?  55  LYS   A CB   1 
ATOM   1425 C CG   A LYS   A 1 55  ? 20.440 12.691  8.012   0.40 11.61 ?  55  LYS   A CG   1 
ATOM   1426 C CG   B LYS   A 1 55  ? 20.536 12.743  8.209   0.60 15.97 ?  55  LYS   A CG   1 
ATOM   1427 C CD   A LYS   A 1 55  ? 19.041 12.795  7.411   0.40 11.83 ?  55  LYS   A CD   1 
ATOM   1428 C CD   B LYS   A 1 55  ? 19.320 13.228  7.421   0.60 18.78 ?  55  LYS   A CD   1 
ATOM   1429 C CE   A LYS   A 1 55  ? 18.281 13.994  7.966   0.40 12.42 ?  55  LYS   A CE   1 
ATOM   1430 C CE   B LYS   A 1 55  ? 18.111 12.330  7.613   0.60 21.41 ?  55  LYS   A CE   1 
ATOM   1431 N NZ   A LYS   A 1 55  ? 16.921 14.115  7.359   0.40 12.70 ?  55  LYS   A NZ   1 
ATOM   1432 N NZ   B LYS   A 1 55  ? 16.849 13.025  7.224   0.60 22.64 ?  55  LYS   A NZ   1 
ATOM   1433 H H    A LYS   A 1 55  ? 22.617 9.683   6.825   0.40 12.81 ?  55  LYS   A H    1 
ATOM   1434 H H    B LYS   A 1 55  ? 22.719 9.813   6.797   0.60 12.70 ?  55  LYS   A H    1 
ATOM   1435 H HA   A LYS   A 1 55  ? 23.083 12.009  7.875   0.40 12.80 ?  55  LYS   A HA   1 
ATOM   1436 H HA   B LYS   A 1 55  ? 23.207 12.049  7.983   0.60 13.64 ?  55  LYS   A HA   1 
ATOM   1437 H HB2  A LYS   A 1 55  ? 21.217 11.551  6.523   0.40 12.82 ?  55  LYS   A HB2  1 
ATOM   1438 H HB2  B LYS   A 1 55  ? 21.397 11.882  6.578   0.60 15.51 ?  55  LYS   A HB2  1 
ATOM   1439 H HB3  A LYS   A 1 55  ? 20.591 10.690  7.698   0.40 12.82 ?  55  LYS   A HB3  1 
ATOM   1440 H HB3  B LYS   A 1 55  ? 20.705 10.827  7.540   0.60 15.51 ?  55  LYS   A HB3  1 
ATOM   1441 H HG2  A LYS   A 1 55  ? 20.348 12.633  8.975   0.40 13.93 ?  55  LYS   A HG2  1 
ATOM   1442 H HG2  B LYS   A 1 55  ? 20.220 12.429  9.071   0.60 19.16 ?  55  LYS   A HG2  1 
ATOM   1443 H HG3  A LYS   A 1 55  ? 20.934 13.485  7.762   0.40 13.93 ?  55  LYS   A HG3  1 
ATOM   1444 H HG3  B LYS   A 1 55  ? 21.134 13.493  8.323   0.60 19.16 ?  55  LYS   A HG3  1 
ATOM   1445 H HD2  A LYS   A 1 55  ? 19.110 12.898  6.449   0.40 14.19 ?  55  LYS   A HD2  1 
ATOM   1446 H HD2  B LYS   A 1 55  ? 19.081 14.122  7.721   0.60 22.54 ?  55  LYS   A HD2  1 
ATOM   1447 H HD3  A LYS   A 1 55  ? 18.537 11.991  7.626   0.40 14.19 ?  55  LYS   A HD3  1 
ATOM   1448 H HD3  B LYS   A 1 55  ? 19.536 13.245  6.475   0.60 22.54 ?  55  LYS   A HD3  1 
ATOM   1449 H HE2  A LYS   A 1 55  ? 18.175 13.890  8.924   0.40 14.90 ?  55  LYS   A HE2  1 
ATOM   1450 H HE2  B LYS   A 1 55  ? 18.207 11.542  7.057   0.60 25.69 ?  55  LYS   A HE2  1 
ATOM   1451 H HE3  A LYS   A 1 55  ? 18.773 14.804  7.766   0.40 14.90 ?  55  LYS   A HE3  1 
ATOM   1452 H HE3  B LYS   A 1 55  ? 18.043 12.079  8.547   0.60 25.69 ?  55  LYS   A HE3  1 
ATOM   1453 H HZ1  A LYS   A 1 55  ? 16.366 14.502  7.934   0.40 15.24 ?  55  LYS   A HZ1  1 
ATOM   1454 H HZ1  B LYS   A 1 55  ? 16.152 12.486  7.344   0.60 27.17 ?  55  LYS   A HZ1  1 
ATOM   1455 H HZ2  A LYS   A 1 55  ? 16.961 14.607  6.619   0.40 15.24 ?  55  LYS   A HZ2  1 
ATOM   1456 H HZ2  B LYS   A 1 55  ? 16.737 13.756  7.723   0.60 27.17 ?  55  LYS   A HZ2  1 
ATOM   1457 H HZ3  A LYS   A 1 55  ? 16.607 13.306  7.154   0.40 15.24 ?  55  LYS   A HZ3  1 
ATOM   1458 H HZ3  B LYS   A 1 55  ? 16.884 13.267  6.368   0.60 27.17 ?  55  LYS   A HZ3  1 
ATOM   1459 N N    . ALA   A 1 56  ? 22.133 9.813   10.003  1.00 11.75 ?  56  ALA   A N    1 
ATOM   1460 C CA   . ALA   A 1 56  ? 22.016 9.500   11.421  1.00 12.02 ?  56  ALA   A CA   1 
ATOM   1461 C C    . ALA   A 1 56  ? 23.361 9.508   12.135  1.00 12.09 ?  56  ALA   A C    1 
ATOM   1462 O O    . ALA   A 1 56  ? 23.390 9.674   13.357  1.00 13.55 ?  56  ALA   A O    1 
ATOM   1463 C CB   . ALA   A 1 56  ? 21.310 8.153   11.613  1.00 13.18 ?  56  ALA   A CB   1 
ATOM   1464 H H    A ALA   A 1 56  ? 21.948 9.152   9.485   0.40 14.09 ?  56  ALA   A H    1 
ATOM   1465 H H    B ALA   A 1 56  ? 21.931 9.167   9.472   0.60 14.09 ?  56  ALA   A H    1 
ATOM   1466 H HA   . ALA   A 1 56  ? 21.464 10.173  11.841  1.00 14.42 ?  56  ALA   A HA   1 
ATOM   1467 H HB1  . ALA   A 1 56  ? 21.246 7.961   12.565  1.00 15.81 ?  56  ALA   A HB1  1 
ATOM   1468 H HB2  . ALA   A 1 56  ? 20.419 8.203   11.231  1.00 15.81 ?  56  ALA   A HB2  1 
ATOM   1469 H HB3  . ALA   A 1 56  ? 21.820 7.456   11.172  1.00 15.81 ?  56  ALA   A HB3  1 
ATOM   1470 N N    . THR   A 1 57  ? 24.469 9.323   11.408  1.00 11.32 ?  57  THR   A N    1 
ATOM   1471 C CA   . THR   A 1 57  ? 25.814 9.448   11.975  1.00 11.22 ?  57  THR   A CA   1 
ATOM   1472 C C    . THR   A 1 57  ? 26.366 10.865  11.888  1.00 11.59 ?  57  THR   A C    1 
ATOM   1473 O O    . THR   A 1 57  ? 27.552 11.073  12.171  1.00 12.22 ?  57  THR   A O    1 
ATOM   1474 C CB   . THR   A 1 57  ? 26.818 8.495   11.301  1.00 11.38 ?  57  THR   A CB   1 
ATOM   1475 O OG1  . THR   A 1 57  ? 27.191 8.985   9.999   1.00 10.83 ?  57  THR   A OG1  1 
ATOM   1476 C CG2  . THR   A 1 57  ? 26.283 7.076   11.208  1.00 11.50 ?  57  THR   A CG2  1 
ATOM   1477 H H    . THR   A 1 57  ? 24.463 9.101   10.577  1.00 13.59 ?  57  THR   A H    1 
ATOM   1478 H HA   . THR   A 1 57  ? 25.772 9.194   12.915  1.00 13.46 ?  57  THR   A HA   1 
ATOM   1479 H HB   . THR   A 1 57  ? 27.617 8.456   11.855  1.00 13.65 ?  57  THR   A HB   1 
ATOM   1480 H HG1  . THR   A 1 57  ? 26.509 9.049   9.516   1.00 12.99 ?  57  THR   A HG1  1 
ATOM   1481 H HG21 . THR   A 1 57  ? 26.962 6.488   10.837  1.00 13.79 ?  57  THR   A HG21 1 
ATOM   1482 H HG22 . THR   A 1 57  ? 26.036 6.753   12.088  1.00 13.79 ?  57  THR   A HG22 1 
ATOM   1483 H HG23 . THR   A 1 57  ? 25.503 7.052   10.635  1.00 13.79 ?  57  THR   A HG23 1 
ATOM   1484 N N    . ASN   A 1 58  ? 25.552 11.840  11.490  1.00 12.20 ?  58  ASN   A N    1 
ATOM   1485 C CA   . ASN   A 1 58  ? 26.023 13.217  11.396  1.00 12.95 ?  58  ASN   A CA   1 
ATOM   1486 C C    . ASN   A 1 58  ? 27.159 13.338  10.377  1.00 11.68 ?  58  ASN   A C    1 
ATOM   1487 O O    . ASN   A 1 58  ? 28.058 14.167  10.524  1.00 12.59 ?  58  ASN   A O    1 
ATOM   1488 C CB   . ASN   A 1 58  ? 26.420 13.739  12.792  1.00 15.39 ?  58  ASN   A CB   1 
ATOM   1489 C CG   . ASN   A 1 58  ? 26.841 15.193  12.803  1.00 18.79 ?  58  ASN   A CG   1 
ATOM   1490 O OD1  . ASN   A 1 58  ? 26.213 16.029  12.167  1.00 20.55 ?  58  ASN   A OD1  1 
ATOM   1491 N ND2  . ASN   A 1 58  ? 27.907 15.503  13.548  1.00 20.01 ?  58  ASN   A ND2  1 
ATOM   1492 H H    . ASN   A 1 58  ? 24.728 11.719  11.260  1.00 14.64 ?  58  ASN   A H    1 
ATOM   1493 H HA   . ASN   A 1 58  ? 25.287 13.759  11.079  1.00 15.53 ?  58  ASN   A HA   1 
ATOM   1494 H HB2  . ASN   A 1 58  ? 25.653 13.639  13.390  1.00 18.46 ?  58  ASN   A HB2  1 
ATOM   1495 H HB3  . ASN   A 1 58  ? 27.160 13.217  13.130  1.00 18.46 ?  58  ASN   A HB3  1 
ATOM   1496 H HD21 . ASN   A 1 58  ? 28.178 16.318  13.594  1.00 24.01 ?  58  ASN   A HD21 1 
ATOM   1497 H HD22 . ASN   A 1 58  ? 28.319 14.886  13.977  1.00 24.01 ?  58  ASN   A HD22 1 
ATOM   1498 N N    . ASN   A 1 59  ? 27.123 12.515  9.324   1.00 10.98 ?  59  ASN   A N    1 
ATOM   1499 C CA   . ASN   A 1 59  ? 28.097 12.492  8.226   1.00 10.66 ?  59  ASN   A CA   1 
ATOM   1500 C C    . ASN   A 1 59  ? 29.417 11.811  8.605   1.00 10.57 ?  59  ASN   A C    1 
ATOM   1501 O O    . ASN   A 1 59  ? 30.329 11.764  7.769   1.00 10.79 ?  59  ASN   A O    1 
ATOM   1502 C CB   . ASN   A 1 59  ? 28.382 13.881  7.622   1.00 10.96 ?  59  ASN   A CB   1 
ATOM   1503 C CG   . ASN   A 1 59  ? 28.739 13.816  6.154   1.00 11.31 ?  59  ASN   A CG   1 
ATOM   1504 O OD1  . ASN   A 1 59  ? 28.035 13.189  5.357   1.00 11.41 ?  59  ASN   A OD1  1 
ATOM   1505 N ND2  . ASN   A 1 59  ? 29.827 14.480  5.781   1.00 11.82 ?  59  ASN   A ND2  1 
ATOM   1506 H H    . ASN   A 1 59  ? 26.500 11.929  9.212   1.00 13.17 ?  59  ASN   A H    1 
ATOM   1507 H HA   . ASN   A 1 59  ? 27.715 11.959  7.517   1.00 12.79 ?  59  ASN   A HA   1 
ATOM   1508 H HB2  . ASN   A 1 59  ? 27.589 14.432  7.705   1.00 13.14 ?  59  ASN   A HB2  1 
ATOM   1509 H HB3  . ASN   A 1 59  ? 29.124 14.288  8.091   1.00 13.14 ?  59  ASN   A HB3  1 
ATOM   1510 H HD21 . ASN   A 1 59  ? 30.075 14.477  4.958   1.00 14.19 ?  59  ASN   A HD21 1 
ATOM   1511 H HD22 . ASN   A 1 59  ? 30.296 14.908  6.366   1.00 14.19 ?  59  ASN   A HD22 1 
ATOM   1512 N N    . ALA   A 1 60  ? 29.548 11.264  9.815   1.00 10.73 ?  60  ALA   A N    1 
ATOM   1513 C CA   . ALA   A 1 60  ? 30.784 10.574  10.163  1.00 10.66 ?  60  ALA   A CA   1 
ATOM   1514 C C    . ALA   A 1 60  ? 31.000 9.341   9.296   1.00 10.39 ?  60  ALA   A C    1 
ATOM   1515 O O    . ALA   A 1 60  ? 32.141 9.026   8.945   1.00 11.06 ?  60  ALA   A O    1 
ATOM   1516 C CB   . ALA   A 1 60  ? 30.788 10.213  11.644  1.00 11.62 ?  60  ALA   A CB   1 
ATOM   1517 H H    . ALA   A 1 60  ? 28.951 11.270  10.434  1.00 12.87 ?  60  ALA   A H    1 
ATOM   1518 H HA   . ALA   A 1 60  ? 31.530 11.175  10.003  1.00 12.80 ?  60  ALA   A HA   1 
ATOM   1519 H HB1  . ALA   A 1 60  ? 31.620 9.757   11.855  1.00 13.95 ?  60  ALA   A HB1  1 
ATOM   1520 H HB2  . ALA   A 1 60  ? 30.719 11.029  12.166  1.00 13.95 ?  60  ALA   A HB2  1 
ATOM   1521 H HB3  . ALA   A 1 60  ? 30.037 9.634   11.830  1.00 13.95 ?  60  ALA   A HB3  1 
ATOM   1522 N N    . MET   A 1 61  ? 29.922 8.646   8.923   1.00 10.33 ?  61  MET   A N    1 
ATOM   1523 C CA   . MET   A 1 61  ? 30.056 7.509   8.015   1.00 10.26 ?  61  MET   A CA   1 
ATOM   1524 C C    . MET   A 1 61  ? 30.684 7.935   6.689   1.00 10.05 ?  61  MET   A C    1 
ATOM   1525 O O    . MET   A 1 61  ? 31.570 7.250   6.164   1.00 10.28 ?  61  MET   A O    1 
ATOM   1526 C CB   . MET   A 1 61  ? 28.690 6.855   7.805   1.00 10.05 ?  61  MET   A CB   1 
ATOM   1527 C CG   . MET   A 1 61  ? 28.697 5.697   6.834   1.00 10.63 ?  61  MET   A CG   1 
ATOM   1528 S SD   . MET   A 1 61  ? 27.071 4.940   6.647   1.00 11.75 ?  61  MET   A SD   1 
ATOM   1529 C CE   . MET   A 1 61  ? 26.962 4.046   8.205   1.00 13.08 ?  61  MET   A CE   1 
ATOM   1530 H H    . MET   A 1 61  ? 29.117 8.809   9.175   1.00 12.39 ?  61  MET   A H    1 
ATOM   1531 H HA   . MET   A 1 61  ? 30.629 6.848   8.431   1.00 12.31 ?  61  MET   A HA   1 
ATOM   1532 H HB2  . MET   A 1 61  ? 28.369 6.522   8.658   1.00 12.06 ?  61  MET   A HB2  1 
ATOM   1533 H HB3  . MET   A 1 61  ? 28.071 7.521   7.464   1.00 12.06 ?  61  MET   A HB3  1 
ATOM   1534 H HG2  . MET   A 1 61  ? 28.970 6.014   5.960   1.00 12.76 ?  61  MET   A HG2  1 
ATOM   1535 H HG3  . MET   A 1 61  ? 29.308 5.019   7.154   1.00 12.76 ?  61  MET   A HG3  1 
ATOM   1536 H HE1  . MET   A 1 61  ? 26.125 3.553   8.232   1.00 15.69 ?  61  MET   A HE1  1 
ATOM   1537 H HE2  . MET   A 1 61  ? 27.709 3.432   8.269   1.00 15.69 ?  61  MET   A HE2  1 
ATOM   1538 H HE3  . MET   A 1 61  ? 26.991 4.680   8.941   1.00 15.69 ?  61  MET   A HE3  1 
ATOM   1539 N N    . GLN   A 1 62  ? 30.239 9.065   6.134   1.00 10.05 ?  62  GLN   A N    1 
ATOM   1540 C CA   . GLN   A 1 62  ? 30.797 9.536   4.869   1.00 10.10 ?  62  GLN   A CA   1 
ATOM   1541 C C    . GLN   A 1 62  ? 32.268 9.913   5.010   1.00 10.06 ?  62  GLN   A C    1 
ATOM   1542 O O    . GLN   A 1 62  ? 33.076 9.596   4.129   1.00 10.44 ?  62  GLN   A O    1 
ATOM   1543 C CB   . GLN   A 1 62  ? 29.994 10.721  4.339   1.00 10.20 ?  62  GLN   A CB   1 
ATOM   1544 C CG   . GLN   A 1 62  ? 30.376 11.085  2.917   1.00 10.18 ?  62  GLN   A CG   1 
ATOM   1545 C CD   . GLN   A 1 62  ? 30.039 9.966   1.961   1.00 10.25 ?  62  GLN   A CD   1 
ATOM   1546 O OE1  . GLN   A 1 62  ? 28.858 9.665   1.759   1.00 11.03 ?  62  GLN   A OE1  1 
ATOM   1547 N NE2  . GLN   A 1 62  ? 31.053 9.296   1.420   1.00 11.19 ?  62  GLN   A NE2  1 
ATOM   1548 H H    . GLN   A 1 62  ? 29.625 9.565   6.467   1.00 12.05 ?  62  GLN   A H    1 
ATOM   1549 H HA   . GLN   A 1 62  ? 30.738 8.815   4.223   1.00 12.11 ?  62  GLN   A HA   1 
ATOM   1550 H HB2  . GLN   A 1 62  ? 29.053 10.505  4.356   1.00 12.23 ?  62  GLN   A HB2  1 
ATOM   1551 H HB3  . GLN   A 1 62  ? 30.169 11.497  4.904   1.00 12.23 ?  62  GLN   A HB3  1 
ATOM   1552 H HG2  . GLN   A 1 62  ? 29.882 11.871  2.643   1.00 12.21 ?  62  GLN   A HG2  1 
ATOM   1553 H HG3  . GLN   A 1 62  ? 31.332 11.253  2.867   1.00 12.21 ?  62  GLN   A HG3  1 
ATOM   1554 H HE21 . GLN   A 1 62  ? 31.863 9.525   1.601   1.00 13.43 ?  62  GLN   A HE21 1 
ATOM   1555 H HE22 . GLN   A 1 62  ? 30.901 8.645   0.882   1.00 13.43 ?  62  GLN   A HE22 1 
ATOM   1556 N N    . VAL   A 1 63  ? 32.635 10.597  6.097   1.00 10.69 ?  63  VAL   A N    1 
ATOM   1557 C CA   . VAL   A 1 63  ? 34.028 10.992  6.297   1.00 11.64 ?  63  VAL   A CA   1 
ATOM   1558 C C    . VAL   A 1 63  ? 34.924 9.757   6.360   1.00 11.01 ?  63  VAL   A C    1 
ATOM   1559 O O    . VAL   A 1 63  ? 35.972 9.691   5.705   1.00 11.33 ?  63  VAL   A O    1 
ATOM   1560 C CB   . VAL   A 1 63  ? 34.147 11.871  7.555   1.00 13.34 ?  63  VAL   A CB   1 
ATOM   1561 C CG1  . VAL   A 1 63  ? 35.595 12.127  7.897   1.00 15.24 ?  63  VAL   A CG1  1 
ATOM   1562 C CG2  . VAL   A 1 63  ? 33.404 13.193  7.349   1.00 13.61 ?  63  VAL   A CG2  1 
ATOM   1563 H H    . VAL   A 1 63  ? 32.092 10.844  6.725   1.00 12.82 ?  63  VAL   A H    1 
ATOM   1564 H HA   . VAL   A 1 63  ? 34.304 11.526  5.538   1.00 13.96 ?  63  VAL   A HA   1 
ATOM   1565 H HB   . VAL   A 1 63  ? 33.740 11.411  8.306   1.00 16.01 ?  63  VAL   A HB   1 
ATOM   1566 H HG11 . VAL   A 1 63  ? 35.643 12.864  8.526   1.00 18.29 ?  63  VAL   A HG11 1 
ATOM   1567 H HG12 . VAL   A 1 63  ? 35.974 11.329  8.292   1.00 18.29 ?  63  VAL   A HG12 1 
ATOM   1568 H HG13 . VAL   A 1 63  ? 36.072 12.357  7.084   1.00 18.29 ?  63  VAL   A HG13 1 
ATOM   1569 H HG21 . VAL   A 1 63  ? 33.502 13.740  8.146   1.00 16.33 ?  63  VAL   A HG21 1 
ATOM   1570 H HG22 . VAL   A 1 63  ? 33.782 13.655  6.585   1.00 16.33 ?  63  VAL   A HG22 1 
ATOM   1571 H HG23 . VAL   A 1 63  ? 32.465 13.008  7.192   1.00 16.33 ?  63  VAL   A HG23 1 
ATOM   1572 N N    . GLU   A 1 64  ? 34.506 8.750   7.132   1.00 10.90 ?  64  GLU   A N    1 
ATOM   1573 C CA   . GLU   A 1 64  ? 35.265 7.510   7.225   1.00 10.83 ?  64  GLU   A CA   1 
ATOM   1574 C C    . GLU   A 1 64  ? 35.343 6.819   5.872   1.00 10.67 ?  64  GLU   A C    1 
ATOM   1575 O O    . GLU   A 1 64  ? 36.388 6.268   5.494   1.00 11.23 ?  64  GLU   A O    1 
ATOM   1576 C CB   . GLU   A 1 64  ? 34.584 6.607   8.253   1.00 11.37 ?  64  GLU   A CB   1 
ATOM   1577 C CG   . GLU   A 1 64  ? 35.236 5.264   8.416   1.00 12.15 ?  64  GLU   A CG   1 
ATOM   1578 C CD   . GLU   A 1 64  ? 34.349 4.267   9.126   1.00 12.59 ?  64  GLU   A CD   1 
ATOM   1579 O OE1  . GLU   A 1 64  ? 33.106 4.366   8.997   1.00 13.49 ?  64  GLU   A OE1  1 
ATOM   1580 O OE2  . GLU   A 1 64  ? 34.894 3.369   9.810   1.00 13.00 -1 64  GLU   A OE2  1 
ATOM   1581 H H    . GLU   A 1 64  ? 33.783 8.762   7.601   1.00 13.07 ?  64  GLU   A H    1 
ATOM   1582 H HA   . GLU   A 1 64  ? 36.165 7.710   7.532   1.00 13.00 ?  64  GLU   A HA   1 
ATOM   1583 H HB2  . GLU   A 1 64  ? 34.606 7.055   9.120   1.00 13.64 ?  64  GLU   A HB2  1 
ATOM   1584 H HB3  . GLU   A 1 64  ? 33.666 6.471   7.982   1.00 13.64 ?  64  GLU   A HB3  1 
ATOM   1585 H HG2  . GLU   A 1 64  ? 35.450 4.896   7.542   1.00 14.57 ?  64  GLU   A HG2  1 
ATOM   1586 H HG3  . GLU   A 1 64  ? 36.047 5.368   8.935   1.00 14.57 ?  64  GLU   A HG3  1 
ATOM   1587 N N    . SER   A 1 65  ? 34.222 6.810   5.144   1.00 10.29 ?  65  SER   A N    1 
ATOM   1588 C CA   . SER   A 1 65  ? 34.167 6.149   3.846   1.00 10.14 ?  65  SER   A CA   1 
ATOM   1589 C C    . SER   A 1 65  ? 35.087 6.819   2.834   1.00 10.31 ?  65  SER   A C    1 
ATOM   1590 O O    . SER   A 1 65  ? 35.721 6.143   2.019   1.00 11.31 ?  65  SER   A O    1 
ATOM   1591 C CB   . SER   A 1 65  ? 32.731 6.159   3.320   1.00 10.37 ?  65  SER   A CB   1 
ATOM   1592 O OG   . SER   A 1 65  ? 31.879 5.349   4.117   1.00 10.92 ?  65  SER   A OG   1 
ATOM   1593 H H    . SER   A 1 65  ? 33.486 7.190   5.378   1.00 12.34 ?  65  SER   A H    1 
ATOM   1594 H HA   . SER   A 1 65  ? 34.449 5.227   3.946   1.00 12.17 ?  65  SER   A HA   1 
ATOM   1595 H HB2  . SER   A 1 65  ? 32.396 7.068   3.330   1.00 12.44 ?  65  SER   A HB2  1 
ATOM   1596 H HB3  . SER   A 1 65  ? 32.727 5.815   2.413   1.00 12.44 ?  65  SER   A HB3  1 
ATOM   1597 H HG   . SER   A 1 65  ? 31.877 5.635   4.911   1.00 13.11 ?  65  SER   A HG   1 
ATOM   1598 N N    . ASP   A 1 66  ? 35.168 8.154   2.857   1.00 10.61 ?  66  ASP   A N    1 
ATOM   1599 C CA   . ASP   A 1 66  ? 36.030 8.846   1.905   1.00 11.36 ?  66  ASP   A CA   1 
ATOM   1600 C C    . ASP   A 1 66  ? 37.491 8.487   2.137   1.00 11.15 ?  66  ASP   A C    1 
ATOM   1601 O O    . ASP   A 1 66  ? 38.256 8.308   1.183   1.00 12.31 ?  66  ASP   A O    1 
ATOM   1602 C CB   . ASP   A 1 66  ? 35.821 10.354  2.010   1.00 12.54 ?  66  ASP   A CB   1 
ATOM   1603 C CG   . ASP   A 1 66  ? 34.481 10.815  1.429   1.00 14.23 ?  66  ASP   A CG   1 
ATOM   1604 O OD1  . ASP   A 1 66  ? 33.752 10.024  0.791   1.00 14.51 ?  66  ASP   A OD1  1 
ATOM   1605 O OD2  . ASP   A 1 66  ? 34.186 12.018  1.589   1.00 16.65 -1 66  ASP   A OD2  1 
ATOM   1606 H H    . ASP   A 1 66  ? 34.735 8.666   3.400   1.00 12.73 ?  66  ASP   A H    1 
ATOM   1607 H HA   . ASP   A 1 66  ? 35.787 8.574   1.006   1.00 13.63 ?  66  ASP   A HA   1 
ATOM   1608 H HB2  . ASP   A 1 66  ? 35.843 10.613  2.945   1.00 15.04 ?  66  ASP   A HB2  1 
ATOM   1609 H HB3  . ASP   A 1 66  ? 36.531 10.804  1.525   1.00 15.04 ?  66  ASP   A HB3  1 
ATOM   1610 N N    . ASP   A 1 67  ? 37.893 8.355   3.399   1.00 11.57 ?  67  ASP   A N    1 
ATOM   1611 C CA   . ASP   A 1 67  ? 39.242 7.896   3.695   1.00 12.54 ?  67  ASP   A CA   1 
ATOM   1612 C C    . ASP   A 1 67  ? 39.451 6.460   3.223   1.00 12.21 ?  67  ASP   A C    1 
ATOM   1613 O O    . ASP   A 1 67  ? 40.505 6.133   2.665   1.00 12.98 ?  67  ASP   A O    1 
ATOM   1614 C CB   . ASP   A 1 67  ? 39.523 8.034   5.189   1.00 13.61 ?  67  ASP   A CB   1 
ATOM   1615 C CG   . ASP   A 1 67  ? 40.815 7.365   5.597   1.00 14.89 ?  67  ASP   A CG   1 
ATOM   1616 O OD1  . ASP   A 1 67  ? 41.893 7.984   5.431   1.00 17.56 ?  67  ASP   A OD1  1 
ATOM   1617 O OD2  . ASP   A 1 67  ? 40.763 6.206   6.073   1.00 14.47 -1 67  ASP   A OD2  1 
ATOM   1618 H H    . ASP   A 1 67  ? 37.411 8.530   4.089   1.00 13.88 ?  67  ASP   A H    1 
ATOM   1619 H HA   . ASP   A 1 67  ? 39.873 8.455   3.220   1.00 15.05 ?  67  ASP   A HA   1 
ATOM   1620 H HB2  . ASP   A 1 67  ? 39.592 8.970   5.409   1.00 16.33 ?  67  ASP   A HB2  1 
ATOM   1621 H HB3  . ASP   A 1 67  ? 38.799 7.620   5.685   1.00 16.33 ?  67  ASP   A HB3  1 
ATOM   1622 N N    A TYR   A 1 68  ? 38.453 5.596   3.415   0.40 11.83 ?  68  TYR   A N    1 
ATOM   1623 N N    B TYR   A 1 68  ? 38.455 5.586   3.430   0.60 12.02 ?  68  TYR   A N    1 
ATOM   1624 C CA   A TYR   A 1 68  ? 38.577 4.218   2.951   0.40 11.54 ?  68  TYR   A CA   1 
ATOM   1625 C CA   B TYR   A 1 68  ? 38.563 4.208   2.946   0.60 12.08 ?  68  TYR   A CA   1 
ATOM   1626 C C    A TYR   A 1 68  ? 38.804 4.159   1.440   0.40 11.29 ?  68  TYR   A C    1 
ATOM   1627 C C    B TYR   A 1 68  ? 38.814 4.170   1.440   0.60 11.63 ?  68  TYR   A C    1 
ATOM   1628 O O    A TYR   A 1 68  ? 39.667 3.413   0.959   0.40 11.70 ?  68  TYR   A O    1 
ATOM   1629 O O    B TYR   A 1 68  ? 39.696 3.444   0.962   0.60 12.35 ?  68  TYR   A O    1 
ATOM   1630 C CB   A TYR   A 1 68  ? 37.335 3.408   3.347   0.40 11.38 ?  68  TYR   A CB   1 
ATOM   1631 C CB   B TYR   A 1 68  ? 37.302 3.389   3.296   0.60 12.62 ?  68  TYR   A CB   1 
ATOM   1632 C CG   A TYR   A 1 68  ? 37.394 2.003   2.802   0.40 12.22 ?  68  TYR   A CG   1 
ATOM   1633 C CG   B TYR   A 1 68  ? 37.306 2.024   2.610   0.60 13.80 ?  68  TYR   A CG   1 
ATOM   1634 C CD1  A TYR   A 1 68  ? 36.929 1.719   1.525   0.40 13.15 ?  68  TYR   A CD1  1 
ATOM   1635 C CD1  B TYR   A 1 68  ? 36.839 1.883   1.303   0.60 14.49 ?  68  TYR   A CD1  1 
ATOM   1636 C CD2  A TYR   A 1 68  ? 37.973 0.975   3.530   0.40 13.52 ?  68  TYR   A CD2  1 
ATOM   1637 C CD2  B TYR   A 1 68  ? 37.834 0.901   3.237   0.60 14.72 ?  68  TYR   A CD2  1 
ATOM   1638 C CE1  A TYR   A 1 68  ? 37.017 0.455   0.993   0.40 14.81 ?  68  TYR   A CE1  1 
ATOM   1639 C CE1  B TYR   A 1 68  ? 36.884 0.675   0.648   0.60 14.49 ?  68  TYR   A CE1  1 
ATOM   1640 C CE2  A TYR   A 1 68  ? 38.062 -0.309  3.005   0.40 14.42 ?  68  TYR   A CE2  1 
ATOM   1641 C CE2  B TYR   A 1 68  ? 37.877 -0.328  2.589   0.60 14.14 ?  68  TYR   A CE2  1 
ATOM   1642 C CZ   A TYR   A 1 68  ? 37.585 -0.555  1.735   0.40 15.25 ?  68  TYR   A CZ   1 
ATOM   1643 C CZ   B TYR   A 1 68  ? 37.409 -0.423  1.297   0.60 13.90 ?  68  TYR   A CZ   1 
ATOM   1644 O OH   A TYR   A 1 68  ? 37.676 -1.812  1.191   0.40 16.90 ?  68  TYR   A OH   1 
ATOM   1645 O OH   B TYR   A 1 68  ? 37.476 -1.641  0.669   0.60 14.49 ?  68  TYR   A OH   1 
ATOM   1646 H H    A TYR   A 1 68  ? 37.705 5.774   3.805   0.40 14.20 ?  68  TYR   A H    1 
ATOM   1647 H H    B TYR   A 1 68  ? 37.716 5.760   3.836   0.60 14.42 ?  68  TYR   A H    1 
ATOM   1648 H HA   A TYR   A 1 68  ? 39.344 3.810   3.380   0.40 13.85 ?  68  TYR   A HA   1 
ATOM   1649 H HA   B TYR   A 1 68  ? 39.316 3.781   3.380   0.60 14.50 ?  68  TYR   A HA   1 
ATOM   1650 H HB2  A TYR   A 1 68  ? 37.285 3.350   4.312   0.40 13.65 ?  68  TYR   A HB2  1 
ATOM   1651 H HB2  B TYR   A 1 68  ? 37.271 3.240   4.254   0.60 15.14 ?  68  TYR   A HB2  1 
ATOM   1652 H HB3  A TYR   A 1 68  ? 36.544 3.834   2.988   0.40 13.65 ?  68  TYR   A HB3  1 
ATOM   1653 H HB3  B TYR   A 1 68  ? 36.513 3.870   3.004   0.60 15.14 ?  68  TYR   A HB3  1 
ATOM   1654 H HD1  A TYR   A 1 68  ? 36.551 2.400   1.014   0.40 15.77 ?  68  TYR   A HD1  1 
ATOM   1655 H HD1  B TYR   A 1 68  ? 36.492 2.620   0.857   0.60 17.39 ?  68  TYR   A HD1  1 
ATOM   1656 H HD2  A TYR   A 1 68  ? 38.311 1.145   4.378   0.40 16.22 ?  68  TYR   A HD2  1 
ATOM   1657 H HD2  B TYR   A 1 68  ? 38.165 0.975   4.100   0.60 17.66 ?  68  TYR   A HD2  1 
ATOM   1658 H HE1  A TYR   A 1 68  ? 36.689 0.287   0.138   0.40 17.77 ?  68  TYR   A HE1  1 
ATOM   1659 H HE1  B TYR   A 1 68  ? 36.559 0.588   -0.223  0.60 17.39 ?  68  TYR   A HE1  1 
ATOM   1660 H HE2  A TYR   A 1 68  ? 38.453 -0.993  3.497   0.40 17.30 ?  68  TYR   A HE2  1 
ATOM   1661 H HE2  B TYR   A 1 68  ? 38.233 -1.076  3.012   0.60 16.97 ?  68  TYR   A HE2  1 
ATOM   1662 H HH   A TYR   A 1 68  ? 38.028 -2.335  1.737   0.40 20.28 ?  68  TYR   A HH   1 
ATOM   1663 H HH   B TYR   A 1 68  ? 37.810 -2.220  1.186   0.60 17.39 ?  68  TYR   A HH   1 
ATOM   1664 N N    . ILE   A 1 69  ? 38.021 4.923   0.673   1.00 11.32 ?  69  ILE   A N    1 
ATOM   1665 C CA   . ILE   A 1 69  ? 38.161 4.913   -0.782  1.00 11.39 ?  69  ILE   A CA   1 
ATOM   1666 C C    . ILE   A 1 69  ? 39.500 5.512   -1.209  1.00 11.56 ?  69  ILE   A C    1 
ATOM   1667 O O    . ILE   A 1 69  ? 40.138 5.032   -2.152  1.00 11.86 ?  69  ILE   A O    1 
ATOM   1668 C CB   . ILE   A 1 69  ? 36.970 5.636   -1.442  1.00 12.24 ?  69  ILE   A CB   1 
ATOM   1669 C CG1  . ILE   A 1 69  ? 35.652 4.908   -1.166  1.00 12.76 ?  69  ILE   A CG1  1 
ATOM   1670 C CG2  . ILE   A 1 69  ? 37.212 5.843   -2.942  1.00 13.74 ?  69  ILE   A CG2  1 
ATOM   1671 C CD1  . ILE   A 1 69  ? 35.479 3.625   -1.931  1.00 13.22 ?  69  ILE   A CD1  1 
ATOM   1672 H H    A ILE   A 1 69  ? 37.409 5.448   0.967   0.40 13.58 ?  69  ILE   A H    1 
ATOM   1673 H H    B ILE   A 1 69  ? 37.406 5.445   0.967   0.60 13.58 ?  69  ILE   A H    1 
ATOM   1674 H HA   . ILE   A 1 69  ? 38.150 3.993   -1.086  1.00 13.66 ?  69  ILE   A HA   1 
ATOM   1675 H HB   . ILE   A 1 69  ? 36.903 6.510   -1.037  1.00 14.69 ?  69  ILE   A HB   1 
ATOM   1676 H HG12 . ILE   A 1 69  ? 35.611 4.691   -0.218  1.00 15.31 ?  69  ILE   A HG12 1 
ATOM   1677 H HG13 . ILE   A 1 69  ? 34.920 5.494   -1.397  1.00 15.31 ?  69  ILE   A HG13 1 
ATOM   1678 H HG21 . ILE   A 1 69  ? 36.367 6.061   -3.370  1.00 16.49 ?  69  ILE   A HG21 1 
ATOM   1679 H HG22 . ILE   A 1 69  ? 37.835 6.583   -3.062  1.00 16.49 ?  69  ILE   A HG22 1 
ATOM   1680 H HG23 . ILE   A 1 69  ? 37.579 5.036   -3.324  1.00 16.49 ?  69  ILE   A HG23 1 
ATOM   1681 H HD11 . ILE   A 1 69  ? 34.668 3.189   -1.627  1.00 15.86 ?  69  ILE   A HD11 1 
ATOM   1682 H HD12 . ILE   A 1 69  ? 35.407 3.832   -2.877  1.00 15.86 ?  69  ILE   A HD12 1 
ATOM   1683 H HD13 . ILE   A 1 69  ? 36.243 3.053   -1.772  1.00 15.86 ?  69  ILE   A HD13 1 
ATOM   1684 N N    . ALA   A 1 70  ? 39.925 6.593   -0.557  1.00 11.66 ?  70  ALA   A N    1 
ATOM   1685 C CA   . ALA   A 1 70  ? 41.204 7.200   -0.910  1.00 12.71 ?  70  ALA   A CA   1 
ATOM   1686 C C    . ALA   A 1 70  ? 42.347 6.213   -0.737  1.00 13.13 ?  70  ALA   A C    1 
ATOM   1687 O O    . ALA   A 1 70  ? 43.313 6.243   -1.502  1.00 15.00 ?  70  ALA   A O    1 
ATOM   1688 C CB   . ALA   A 1 70  ? 41.447 8.448   -0.059  1.00 13.48 ?  70  ALA   A CB   1 
ATOM   1689 H H    . ALA   A 1 70  ? 39.502 6.979   0.081   1.00 13.99 ?  70  ALA   A H    1 
ATOM   1690 H HA   . ALA   A 1 70  ? 41.175 7.477   -1.842  1.00 15.25 ?  70  ALA   A HA   1 
ATOM   1691 H HB1  . ALA   A 1 70  ? 42.303 8.835   -0.309  1.00 16.18 ?  70  ALA   A HB1  1 
ATOM   1692 H HB2  . ALA   A 1 70  ? 40.737 9.084   -0.214  1.00 16.18 ?  70  ALA   A HB2  1 
ATOM   1693 H HB3  . ALA   A 1 70  ? 41.467 8.188   0.877   1.00 16.18 ?  70  ALA   A HB3  1 
ATOM   1694 N N    . THR   A 1 71  ? 42.243 5.315   0.242   1.00 12.40 ?  71  THR   A N    1 
ATOM   1695 C CA   . THR   A 1 71  ? 43.295 4.337   0.493   1.00 13.75 ?  71  THR   A CA   1 
ATOM   1696 C C    . THR   A 1 71  ? 43.171 3.108   -0.399  1.00 14.05 ?  71  THR   A C    1 
ATOM   1697 O O    . THR   A 1 71  ? 44.181 2.594   -0.898  1.00 16.34 ?  71  THR   A O    1 
ATOM   1698 C CB   . THR   A 1 71  ? 43.225 3.900   1.951   1.00 15.76 ?  71  THR   A CB   1 
ATOM   1699 O OG1  . THR   A 1 71  ? 43.481 5.031   2.790   1.00 17.13 ?  71  THR   A OG1  1 
ATOM   1700 C CG2  . THR   A 1 71  ? 44.232 2.798   2.248   1.00 17.44 ?  71  THR   A CG2  1 
ATOM   1701 H H    . THR   A 1 71  ? 41.568 5.249   0.764   1.00 14.88 ?  71  THR   A H    1 
ATOM   1702 H HA   . THR   A 1 71  ? 44.160 4.745   0.329   1.00 16.50 ?  71  THR   A HA   1 
ATOM   1703 H HB   . THR   A 1 71  ? 42.335 3.550   2.130   1.00 18.91 ?  71  THR   A HB   1 
ATOM   1704 H HG1  . THR   A 1 71  ? 43.434 4.793   3.595   1.00 20.56 ?  71  THR   A HG1  1 
ATOM   1705 H HG21 . THR   A 1 71  ? 44.359 2.722   3.206   1.00 20.93 ?  71  THR   A HG21 1 
ATOM   1706 H HG22 . THR   A 1 71  ? 43.919 1.949   1.903   1.00 20.93 ?  71  THR   A HG22 1 
ATOM   1707 H HG23 . THR   A 1 71  ? 45.086 3.012   1.836   1.00 20.93 ?  71  THR   A HG23 1 
ATOM   1708 N N    . ASN   A 1 72  ? 41.947 2.609   -0.590  1.00 13.10 ?  72  ASN   A N    1 
ATOM   1709 C CA   . ASN   A 1 72  ? 41.718 1.283   -1.153  1.00 13.31 ?  72  ASN   A CA   1 
ATOM   1710 C C    . ASN   A 1 72  ? 41.086 1.273   -2.531  1.00 13.25 ?  72  ASN   A C    1 
ATOM   1711 O O    . ASN   A 1 72  ? 41.090 0.220   -3.181  1.00 14.68 ?  72  ASN   A O    1 
ATOM   1712 C CB   . ASN   A 1 72  ? 40.830 0.469   -0.208  1.00 13.91 ?  72  ASN   A CB   1 
ATOM   1713 C CG   . ASN   A 1 72  ? 41.452 0.315   1.151   1.00 15.16 ?  72  ASN   A CG   1 
ATOM   1714 O OD1  . ASN   A 1 72  ? 41.001 0.915   2.125   1.00 16.77 ?  72  ASN   A OD1  1 
ATOM   1715 N ND2  . ASN   A 1 72  ? 42.501 -0.476  1.227   1.00 15.71 ?  72  ASN   A ND2  1 
ATOM   1716 H H    . ASN   A 1 72  ? 41.221 3.035   -0.399  1.00 15.72 ?  72  ASN   A H    1 
ATOM   1717 H HA   . ASN   A 1 72  ? 42.571 0.832   -1.221  1.00 15.96 ?  72  ASN   A HA   1 
ATOM   1718 H HB2  . ASN   A 1 72  ? 39.978 0.915   -0.104  1.00 16.69 ?  72  ASN   A HB2  1 
ATOM   1719 H HB3  . ASN   A 1 72  ? 40.702 -0.419  -0.583  1.00 16.69 ?  72  ASN   A HB3  1 
ATOM   1720 H HD21 . ASN   A 1 72  ? 42.896 -0.598  1.984   1.00 18.85 ?  72  ASN   A HD21 1 
ATOM   1721 H HD22 . ASN   A 1 72  ? 42.796 -0.875  0.524   1.00 18.85 ?  72  ASN   A HD22 1 
ATOM   1722 N N    . GLY   A 1 73  ? 40.532 2.388   -2.988  1.00 12.95 ?  73  GLY   A N    1 
ATOM   1723 C CA   . GLY   A 1 73  ? 39.793 2.401   -4.224  1.00 12.72 ?  73  GLY   A CA   1 
ATOM   1724 C C    . GLY   A 1 73  ? 38.400 1.827   -4.057  1.00 12.25 ?  73  GLY   A C    1 
ATOM   1725 O O    . GLY   A 1 73  ? 38.013 1.363   -2.978  1.00 12.99 ?  73  GLY   A O    1 
ATOM   1726 H H    . GLY   A 1 73  ? 40.577 3.162   -2.601  1.00 15.54 ?  73  GLY   A H    1 
ATOM   1727 H HA2  . GLY   A 1 73  ? 39.722 3.317   -4.548  1.00 15.27 ?  73  GLY   A HA2  1 
ATOM   1728 H HA3  . GLY   A 1 73  ? 40.271 1.881   -4.894  1.00 15.27 ?  73  GLY   A HA3  1 
ATOM   1729 N N    . PRO   A 1 74  ? 37.624 1.855   -5.136  1.00 12.64 ?  74  PRO   A N    1 
ATOM   1730 C CA   . PRO   A 1 74  ? 36.228 1.423   -5.057  1.00 12.58 ?  74  PRO   A CA   1 
ATOM   1731 C C    . PRO   A 1 74  ? 36.075 -0.056  -4.733  1.00 11.87 ?  74  PRO   A C    1 
ATOM   1732 O O    . PRO   A 1 74  ? 36.943 -0.892  -5.009  1.00 12.96 ?  74  PRO   A O    1 
ATOM   1733 C CB   . PRO   A 1 74  ? 35.683 1.726   -6.458  1.00 14.16 ?  74  PRO   A CB   1 
ATOM   1734 C CG   . PRO   A 1 74  ? 36.634 2.707   -7.055  1.00 16.85 ?  74  PRO   A CG   1 
ATOM   1735 C CD   . PRO   A 1 74  ? 37.969 2.371   -6.470  1.00 14.48 ?  74  PRO   A CD   1 
ATOM   1736 H HA   . PRO   A 1 74  ? 35.748 1.949   -4.399  1.00 15.09 ?  74  PRO   A HA   1 
ATOM   1737 H HB2  . PRO   A 1 74  ? 35.654 0.912   -6.980  1.00 16.99 ?  74  PRO   A HB2  1 
ATOM   1738 H HB3  . PRO   A 1 74  ? 34.795 2.117   -6.382  1.00 16.99 ?  74  PRO   A HB3  1 
ATOM   1739 H HG2  . PRO   A 1 74  ? 36.650 2.602   -8.018  1.00 20.22 ?  74  PRO   A HG2  1 
ATOM   1740 H HG3  . PRO   A 1 74  ? 36.373 3.608   -6.811  1.00 20.22 ?  74  PRO   A HG3  1 
ATOM   1741 H HD2  . PRO   A 1 74  ? 38.414 1.686   -6.996  1.00 17.37 ?  74  PRO   A HD2  1 
ATOM   1742 H HD3  . PRO   A 1 74  ? 38.516 3.173   -6.402  1.00 17.37 ?  74  PRO   A HD3  1 
ATOM   1743 N N    . LEU   A 1 75  ? 34.924 -0.369  -4.141  1.00 11.42 ?  75  LEU   A N    1 
ATOM   1744 C CA   . LEU   A 1 75  ? 34.521 -1.756  -3.988  1.00 11.22 ?  75  LEU   A CA   1 
ATOM   1745 C C    . LEU   A 1 75  ? 34.133 -2.334  -5.346  1.00 11.97 ?  75  LEU   A C    1 
ATOM   1746 O O    . LEU   A 1 75  ? 33.999 -1.617  -6.343  1.00 13.50 ?  75  LEU   A O    1 
ATOM   1747 C CB   . LEU   A 1 75  ? 33.326 -1.871  -3.044  1.00 11.43 ?  75  LEU   A CB   1 
ATOM   1748 C CG   . LEU   A 1 75  ? 33.547 -1.436  -1.597  1.00 12.72 ?  75  LEU   A CG   1 
ATOM   1749 C CD1  . LEU   A 1 75  ? 32.270 -1.611  -0.783  1.00 14.83 ?  75  LEU   A CD1  1 
ATOM   1750 C CD2  . LEU   A 1 75  ? 34.688 -2.158  -0.947  1.00 16.02 ?  75  LEU   A CD2  1 
ATOM   1751 H H    . LEU   A 1 75  ? 34.361 0.201   -3.830  1.00 13.70 ?  75  LEU   A H    1 
ATOM   1752 H HA   . LEU   A 1 75  ? 35.257 -2.273  -3.631  1.00 13.46 ?  75  LEU   A HA   1 
ATOM   1753 H HB2  . LEU   A 1 75  ? 32.602 -1.333  -3.396  1.00 13.71 ?  75  LEU   A HB2  1 
ATOM   1754 H HB3  . LEU   A 1 75  ? 33.047 -2.802  -3.019  1.00 13.71 ?  75  LEU   A HB3  1 
ATOM   1755 H HG   . LEU   A 1 75  ? 33.774 -0.489  -1.595  1.00 15.26 ?  75  LEU   A HG   1 
ATOM   1756 H HD11 . LEU   A 1 75  ? 32.436 -1.322  0.129   1.00 17.80 ?  75  LEU   A HD11 1 
ATOM   1757 H HD12 . LEU   A 1 75  ? 31.572 -1.069  -1.180  1.00 17.80 ?  75  LEU   A HD12 1 
ATOM   1758 H HD13 . LEU   A 1 75  ? 32.017 -2.545  -0.795  1.00 17.80 ?  75  LEU   A HD13 1 
ATOM   1759 H HD21 . LEU   A 1 75  ? 34.731 -1.909  -0.010  1.00 19.22 ?  75  LEU   A HD21 1 
ATOM   1760 H HD22 . LEU   A 1 75  ? 34.548 -3.113  -1.030  1.00 19.22 ?  75  LEU   A HD22 1 
ATOM   1761 H HD23 . LEU   A 1 75  ? 35.521 -1.909  -1.389  1.00 19.22 ?  75  LEU   A HD23 1 
ATOM   1762 N N    . LYS   A 1 76  ? 33.956 -3.656  -5.370  1.00 12.25 ?  76  LYS   A N    1 
ATOM   1763 C CA   . LYS   A 1 76  ? 33.353 -4.371  -6.490  1.00 12.95 ?  76  LYS   A CA   1 
ATOM   1764 C C    . LYS   A 1 76  ? 31.840 -4.449  -6.298  1.00 11.34 ?  76  LYS   A C    1 
ATOM   1765 O O    . LYS   A 1 76  ? 31.357 -4.571  -5.176  1.00 11.40 ?  76  LYS   A O    1 
ATOM   1766 C CB   . LYS   A 1 76  ? 33.887 -5.814  -6.542  1.00 14.67 ?  76  LYS   A CB   1 
ATOM   1767 C CG   . LYS   A 1 76  ? 35.395 -5.922  -6.716  1.00 16.39 ?  76  LYS   A CG   1 
ATOM   1768 C CD   . LYS   A 1 76  ? 35.915 -7.321  -6.475  1.00 17.82 ?  76  LYS   A CD   1 
ATOM   1769 C CE   . LYS   A 1 76  ? 37.408 -7.376  -6.689  1.00 20.65 ?  76  LYS   A CE   1 
ATOM   1770 N NZ   . LYS   A 1 76  ? 37.950 -8.715  -6.394  1.00 21.56 ?  76  LYS   A NZ   1 
ATOM   1771 H H    . LYS   A 1 76  ? 34.182 -4.176  -4.721  1.00 14.70 ?  76  LYS   A H    1 
ATOM   1772 H HA   . LYS   A 1 76  ? 33.554 -3.920  -7.326  1.00 15.53 ?  76  LYS   A HA   1 
ATOM   1773 H HB2  . LYS   A 1 76  ? 33.649 -6.258  -5.713  1.00 17.61 ?  76  LYS   A HB2  1 
ATOM   1774 H HB3  . LYS   A 1 76  ? 33.466 -6.268  -7.288  1.00 17.61 ?  76  LYS   A HB3  1 
ATOM   1775 H HG2  . LYS   A 1 76  ? 35.626 -5.666  -7.622  1.00 19.67 ?  76  LYS   A HG2  1 
ATOM   1776 H HG3  . LYS   A 1 76  ? 35.829 -5.328  -6.082  1.00 19.67 ?  76  LYS   A HG3  1 
ATOM   1777 H HD2  . LYS   A 1 76  ? 35.722 -7.585  -5.561  1.00 21.38 ?  76  LYS   A HD2  1 
ATOM   1778 H HD3  . LYS   A 1 76  ? 35.489 -7.934  -7.098  1.00 21.38 ?  76  LYS   A HD3  1 
ATOM   1779 H HE2  . LYS   A 1 76  ? 37.603 -7.166  -7.615  1.00 24.78 ?  76  LYS   A HE2  1 
ATOM   1780 H HE3  . LYS   A 1 76  ? 37.836 -6.739  -6.099  1.00 24.78 ?  76  LYS   A HE3  1 
ATOM   1781 H HZ1  . LYS   A 1 76  ? 38.829 -8.727  -6.527  1.00 25.87 ?  76  LYS   A HZ1  1 
ATOM   1782 H HZ2  . LYS   A 1 76  ? 37.783 -8.936  -5.547  1.00 25.87 ?  76  LYS   A HZ2  1 
ATOM   1783 H HZ3  . LYS   A 1 76  ? 37.571 -9.325  -6.926  1.00 25.87 ?  76  LYS   A HZ3  1 
ATOM   1784 N N    . VAL   A 1 77  ? 31.088 -4.418  -7.402  1.00 11.90 ?  77  VAL   A N    1 
ATOM   1785 C CA   . VAL   A 1 77  ? 29.680 -4.805  -7.313  1.00 11.94 ?  77  VAL   A CA   1 
ATOM   1786 C C    . VAL   A 1 77  ? 29.616 -6.258  -6.867  1.00 11.35 ?  77  VAL   A C    1 
ATOM   1787 O O    . VAL   A 1 77  ? 30.281 -7.126  -7.446  1.00 11.74 ?  77  VAL   A O    1 
ATOM   1788 C CB   . VAL   A 1 77  ? 28.950 -4.584  -8.646  1.00 13.21 ?  77  VAL   A CB   1 
ATOM   1789 C CG1  . VAL   A 1 77  ? 27.484 -5.010  -8.521  1.00 14.03 ?  77  VAL   A CG1  1 
ATOM   1790 C CG2  . VAL   A 1 77  ? 29.049 -3.130  -9.082  1.00 14.55 ?  77  VAL   A CG2  1 
ATOM   1791 H H    . VAL   A 1 77  ? 31.364 -4.179  -8.182  1.00 14.28 ?  77  VAL   A H    1 
ATOM   1792 H HA   . VAL   A 1 77  ? 29.248 -4.257  -6.637  1.00 14.33 ?  77  VAL   A HA   1 
ATOM   1793 H HB   . VAL   A 1 77  ? 29.370 -5.129  -9.329  1.00 15.85 ?  77  VAL   A HB   1 
ATOM   1794 H HG11 . VAL   A 1 77  ? 27.007 -4.739  -9.319  1.00 16.83 ?  77  VAL   A HG11 1 
ATOM   1795 H HG12 . VAL   A 1 77  ? 27.440 -5.975  -8.421  1.00 16.83 ?  77  VAL   A HG12 1 
ATOM   1796 H HG13 . VAL   A 1 77  ? 27.096 -4.580  -7.741  1.00 16.83 ?  77  VAL   A HG13 1 
ATOM   1797 H HG21 . VAL   A 1 77  ? 28.532 -3.010  -9.894  1.00 17.46 ?  77  VAL   A HG21 1 
ATOM   1798 H HG22 . VAL   A 1 77  ? 28.697 -2.565  -8.378  1.00 17.46 ?  77  VAL   A HG22 1 
ATOM   1799 H HG23 . VAL   A 1 77  ? 29.980 -2.910  -9.249  1.00 17.46 ?  77  VAL   A HG23 1 
ATOM   1800 N N    . GLY   A 1 78  ? 28.828 -6.526  -5.824  1.00 11.17 ?  78  GLY   A N    1 
ATOM   1801 C CA   . GLY   A 1 78  ? 28.811 -7.814  -5.163  1.00 11.24 ?  78  GLY   A CA   1 
ATOM   1802 C C    . GLY   A 1 78  ? 29.732 -7.902  -3.968  1.00 10.71 ?  78  GLY   A C    1 
ATOM   1803 O O    . GLY   A 1 78  ? 29.677 -8.901  -3.232  1.00 11.55 ?  78  GLY   A O    1 
ATOM   1804 H H    . GLY   A 1 78  ? 28.273 -5.954  -5.487  1.00 13.40 ?  78  GLY   A H    1 
ATOM   1805 H HA2  . GLY   A 1 78  ? 27.907 -8.004  -4.871  1.00 13.49 ?  78  GLY   A HA2  1 
ATOM   1806 H HA3  . GLY   A 1 78  ? 29.074 -8.495  -5.800  1.00 13.49 ?  78  GLY   A HA3  1 
ATOM   1807 N N    . GLY   A 1 79  ? 30.578 -6.891  -3.753  1.00 10.79 ?  79  GLY   A N    1 
ATOM   1808 C CA   . GLY   A 1 79  ? 31.550 -6.900  -2.686  1.00 11.13 ?  79  GLY   A CA   1 
ATOM   1809 C C    . GLY   A 1 79  ? 31.110 -6.108  -1.465  1.00 10.44 ?  79  GLY   A C    1 
ATOM   1810 O O    . GLY   A 1 79  ? 29.990 -5.606  -1.373  1.00 11.05 ?  79  GLY   A O    1 
ATOM   1811 H H    . GLY   A 1 79  ? 30.598 -6.172  -4.225  1.00 12.94 ?  79  GLY   A H    1 
ATOM   1812 H HA2  . GLY   A 1 79  ? 31.716 -7.821  -2.413  1.00 13.35 ?  79  GLY   A HA2  1 
ATOM   1813 H HA3  . GLY   A 1 79  ? 32.385 -6.529  -3.009  1.00 13.35 ?  79  GLY   A HA3  1 
ATOM   1814 N N    . SER   A 1 80  ? 32.026 -6.017  -0.503  1.00 11.22 ?  80  SER   A N    1 
ATOM   1815 C CA   . SER   A 1 80  ? 31.721 -5.380  0.767   1.00 10.56 ?  80  SER   A CA   1 
ATOM   1816 C C    . SER   A 1 80  ? 32.999 -4.935  1.457   1.00 10.71 ?  80  SER   A C    1 
ATOM   1817 O O    . SER   A 1 80  ? 34.104 -5.372  1.124   1.00 12.09 ?  80  SER   A O    1 
ATOM   1818 C CB   . SER   A 1 80  ? 30.969 -6.336  1.700   1.00 11.79 ?  80  SER   A CB   1 
ATOM   1819 O OG   . SER   A 1 80  ? 31.794 -7.399  2.148   1.00 13.63 ?  80  SER   A OG   1 
ATOM   1820 H H    . SER   A 1 80  ? 32.834 -6.313  -0.562  1.00 13.47 ?  80  SER   A H    1 
ATOM   1821 H HA   . SER   A 1 80  ? 31.169 -4.599  0.595   1.00 12.67 ?  80  SER   A HA   1 
ATOM   1822 H HB2  . SER   A 1 80  ? 30.655 -5.835  2.471   1.00 14.14 ?  80  SER   A HB2  1 
ATOM   1823 H HB3  . SER   A 1 80  ? 30.209 -6.705  1.220   1.00 14.14 ?  80  SER   A HB3  1 
ATOM   1824 H HG   . SER   A 1 80  ? 32.072 -7.835  1.481   1.00 16.35 ?  80  SER   A HG   1 
ATOM   1825 N N    . CYS   A 1 81  ? 32.817 -4.093  2.470   1.00 10.39 ?  81  CYS   A N    1 
ATOM   1826 C CA   . CYS   A 1 81  ? 33.870 -3.810  3.429   1.00 10.44 ?  81  CYS   A CA   1 
ATOM   1827 C C    . CYS   A 1 81  ? 33.231 -3.572  4.790   1.00 10.23 ?  81  CYS   A C    1 
ATOM   1828 O O    . CYS   A 1 81  ? 32.063 -3.172  4.883   1.00 11.58 ?  81  CYS   A O    1 
ATOM   1829 C CB   . CYS   A 1 81  ? 34.739 -2.613  3.014   1.00 11.18 ?  81  CYS   A CB   1 
ATOM   1830 S SG   . CYS   A 1 81  ? 33.846 -1.048  3.034   1.00 11.14 ?  81  CYS   A SG   1 
ATOM   1831 H H    . CYS   A 1 81  ? 32.082 -3.665  2.624   1.00 12.47 ?  81  CYS   A H    1 
ATOM   1832 H HA   . CYS   A 1 81  ? 34.447 -4.584  3.501   1.00 12.52 ?  81  CYS   A HA   1 
ATOM   1833 H HB2  . CYS   A 1 81  ? 35.490 -2.541  3.630   1.00 13.41 ?  81  CYS   A HB2  1 
ATOM   1834 H HB3  . CYS   A 1 81  ? 35.072 -2.764  2.113   1.00 13.41 ?  81  CYS   A HB3  1 
ATOM   1835 H HG   . CYS   A 1 81  ? 34.592 -0.170  2.698   1.00 13.36 ?  81  CYS   A HG   1 
ATOM   1836 N N    . VAL   A 1 82  ? 34.003 -3.834  5.841   1.00 10.73 ?  82  VAL   A N    1 
ATOM   1837 C CA   . VAL   A 1 82  ? 33.580 -3.588  7.212   1.00 11.10 ?  82  VAL   A CA   1 
ATOM   1838 C C    . VAL   A 1 82  ? 34.187 -2.278  7.678   1.00 11.43 ?  82  VAL   A C    1 
ATOM   1839 O O    . VAL   A 1 82  ? 35.412 -2.113  7.667   1.00 12.18 ?  82  VAL   A O    1 
ATOM   1840 C CB   . VAL   A 1 82  ? 33.999 -4.723  8.155   1.00 12.49 ?  82  VAL   A CB   1 
ATOM   1841 C CG1  . VAL   A 1 82  ? 33.542 -4.420  9.572   1.00 14.10 ?  82  VAL   A CG1  1 
ATOM   1842 C CG2  . VAL   A 1 82  ? 33.447 -6.051  7.684   1.00 13.45 ?  82  VAL   A CG2  1 
ATOM   1843 H H    . VAL   A 1 82  ? 34.800 -4.168  5.781   1.00 12.87 ?  82  VAL   A H    1 
ATOM   1844 H HA   . VAL   A 1 82  ? 32.614 -3.499  7.236   1.00 13.32 ?  82  VAL   A HA   1 
ATOM   1845 H HB   . VAL   A 1 82  ? 34.965 -4.778  8.163   1.00 14.98 ?  82  VAL   A HB   1 
ATOM   1846 H HG11 . VAL   A 1 82  ? 33.623 -5.225  10.105  1.00 16.92 ?  82  VAL   A HG11 1 
ATOM   1847 H HG12 . VAL   A 1 82  ? 34.093 -3.717  9.948   1.00 16.92 ?  82  VAL   A HG12 1 
ATOM   1848 H HG13 . VAL   A 1 82  ? 32.611 -4.135  9.551   1.00 16.92 ?  82  VAL   A HG13 1 
ATOM   1849 H HG21 . VAL   A 1 82  ? 33.694 -6.736  8.323   1.00 16.14 ?  82  VAL   A HG21 1 
ATOM   1850 H HG22 . VAL   A 1 82  ? 32.481 -5.987  7.621   1.00 16.14 ?  82  VAL   A HG22 1 
ATOM   1851 H HG23 . VAL   A 1 82  ? 33.823 -6.256  6.814   1.00 16.14 ?  82  VAL   A HG23 1 
ATOM   1852 N N    . LEU   A 1 83  ? 33.336 -1.356  8.107   1.00 10.83 ?  83  LEU   A N    1 
ATOM   1853 C CA   . LEU   A 1 83  ? 33.759 -0.089  8.679   1.00 10.97 ?  83  LEU   A CA   1 
ATOM   1854 C C    . LEU   A 1 83  ? 33.047 0.095   10.016  1.00 10.82 ?  83  LEU   A C    1 
ATOM   1855 O O    . LEU   A 1 83  ? 32.324 -0.796  10.484  1.00 11.43 ?  83  LEU   A O    1 
ATOM   1856 C CB   . LEU   A 1 83  ? 33.511 1.064   7.693   1.00 11.44 ?  83  LEU   A CB   1 
ATOM   1857 C CG   . LEU   A 1 83  ? 34.407 1.061   6.449   1.00 11.83 ?  83  LEU   A CG   1 
ATOM   1858 C CD1  . LEU   A 1 83  ? 33.959 2.107   5.450   1.00 12.53 ?  83  LEU   A CD1  1 
ATOM   1859 C CD2  . LEU   A 1 83  ? 35.870 1.300   6.829   1.00 12.68 ?  83  LEU   A CD2  1 
ATOM   1860 H H    . LEU   A 1 83  ? 32.481 -1.443  8.070   1.00 13.00 ?  83  LEU   A H    1 
ATOM   1861 H HA   . LEU   A 1 83  ? 34.712 -0.123  8.854   1.00 13.16 ?  83  LEU   A HA   1 
ATOM   1862 H HB2  . LEU   A 1 83  ? 32.594 1.018   7.382   1.00 13.73 ?  83  LEU   A HB2  1 
ATOM   1863 H HB3  . LEU   A 1 83  ? 33.657 1.905   8.151   1.00 13.73 ?  83  LEU   A HB3  1 
ATOM   1864 H HG   . LEU   A 1 83  ? 34.357 0.189   6.023   1.00 14.19 ?  83  LEU   A HG   1 
ATOM   1865 H HD11 . LEU   A 1 83  ? 34.548 2.069   4.676   1.00 15.03 ?  83  LEU   A HD11 1 
ATOM   1866 H HD12 . LEU   A 1 83  ? 33.051 1.909   5.183   1.00 15.03 ?  83  LEU   A HD12 1 
ATOM   1867 H HD13 . LEU   A 1 83  ? 34.010 2.977   5.864   1.00 15.03 ?  83  LEU   A HD13 1 
ATOM   1868 H HD21 . LEU   A 1 83  ? 36.394 1.436   6.020   1.00 15.21 ?  83  LEU   A HD21 1 
ATOM   1869 H HD22 . LEU   A 1 83  ? 35.930 2.090   7.391   1.00 15.21 ?  83  LEU   A HD22 1 
ATOM   1870 H HD23 . LEU   A 1 83  ? 36.212 0.529   7.310   1.00 15.21 ?  83  LEU   A HD23 1 
ATOM   1871 N N    . SER   A 1 84  ? 33.267 1.242   10.648  1.00 11.56 ?  84  SER   A N    1 
ATOM   1872 C CA   . SER   A 1 84  ? 32.626 1.500   11.928  1.00 11.66 ?  84  SER   A CA   1 
ATOM   1873 C C    . SER   A 1 84  ? 31.107 1.591   11.788  1.00 11.47 ?  84  SER   A C    1 
ATOM   1874 O O    . SER   A 1 84  ? 30.582 2.062   10.781  1.00 11.93 ?  84  SER   A O    1 
ATOM   1875 C CB   . SER   A 1 84  ? 33.132 2.815   12.508  1.00 12.82 ?  84  SER   A CB   1 
ATOM   1876 O OG   . SER   A 1 84  ? 32.503 3.087   13.743  1.00 13.83 ?  84  SER   A OG   1 
ATOM   1877 H H    . SER   A 1 84  ? 33.771 1.878   10.355  1.00 13.87 ?  84  SER   A H    1 
ATOM   1878 H HA   . SER   A 1 84  ? 32.844 0.785   12.542  1.00 13.99 ?  84  SER   A HA   1 
ATOM   1879 H HB2  . SER   A 1 84  ? 34.093 2.748   12.650  1.00 15.38 ?  84  SER   A HB2  1 
ATOM   1880 H HB3  . SER   A 1 84  ? 32.945 3.532   11.879  1.00 15.38 ?  84  SER   A HB3  1 
ATOM   1881 H HG   . SER   A 1 84  ? 32.780 3.815   14.051  1.00 16.60 ?  84  SER   A HG   1 
ATOM   1882 N N    . GLY   A 1 85  ? 30.404 1.177   12.837  1.00 12.53 ?  85  GLY   A N    1 
ATOM   1883 C CA   . GLY   A 1 85  ? 28.981 1.420   12.936  1.00 13.27 ?  85  GLY   A CA   1 
ATOM   1884 C C    . GLY   A 1 85  ? 28.624 2.738   13.583  1.00 12.59 ?  85  GLY   A C    1 
ATOM   1885 O O    . GLY   A 1 85  ? 27.438 3.060   13.705  1.00 13.22 ?  85  GLY   A O    1 
ATOM   1886 H H    . GLY   A 1 85  ? 30.740 0.753   13.509  1.00 15.04 ?  85  GLY   A H    1 
ATOM   1887 H HA2  . GLY   A 1 85  ? 28.599 1.407   12.047  1.00 15.92 ?  85  GLY   A HA2  1 
ATOM   1888 H HA3  . GLY   A 1 85  ? 28.577 0.712   13.453  1.00 15.92 ?  85  GLY   A HA3  1 
ATOM   1889 N N    . HIS   A 1 86  ? 29.619 3.510   14.011  1.00 12.58 ?  86  HIS   A N    1 
ATOM   1890 C CA   . HIS   A 1 86  ? 29.414 4.839   14.596  1.00 13.15 ?  86  HIS   A CA   1 
ATOM   1891 C C    . HIS   A 1 86  ? 28.435 4.714   15.756  1.00 13.88 ?  86  HIS   A C    1 
ATOM   1892 O O    . HIS   A 1 86  ? 28.615 3.833   16.608  1.00 15.12 ?  86  HIS   A O    1 
ATOM   1893 C CB   . HIS   A 1 86  ? 29.033 5.825   13.504  1.00 13.24 ?  86  HIS   A CB   1 
ATOM   1894 C CG   . HIS   A 1 86  ? 30.078 5.921   12.454  1.00 13.13 ?  86  HIS   A CG   1 
ATOM   1895 N ND1  . HIS   A 1 86  ? 31.178 6.744   12.576  1.00 14.42 ?  86  HIS   A ND1  1 
ATOM   1896 C CD2  . HIS   A 1 86  ? 30.240 5.236   11.302  1.00 12.70 ?  86  HIS   A CD2  1 
ATOM   1897 C CE1  . HIS   A 1 86  ? 31.958 6.575   11.525  1.00 13.96 ?  86  HIS   A CE1  1 
ATOM   1898 N NE2  . HIS   A 1 86  ? 31.419 5.657   10.744  1.00 13.13 ?  86  HIS   A NE2  1 
ATOM   1899 H H    . HIS   A 1 86  ? 30.447 3.284   13.979  1.00 15.10 ?  86  HIS   A H    1 
ATOM   1900 H HA   . HIS   A 1 86  ? 30.260 5.148   14.961  1.00 15.78 ?  86  HIS   A HA   1 
ATOM   1901 H HB2  . HIS   A 1 86  ? 28.206 5.543   13.082  1.00 15.89 ?  86  HIS   A HB2  1 
ATOM   1902 H HB3  . HIS   A 1 86  ? 28.917 6.714   13.890  1.00 15.89 ?  86  HIS   A HB3  1 
ATOM   1903 H HD2  . HIS   A 1 86  ? 29.667 4.586   10.956  1.00 15.24 ?  86  HIS   A HD2  1 
ATOM   1904 H HE1  . HIS   A 1 86  ? 32.753 7.029   11.350  1.00 16.75 ?  86  HIS   A HE1  1 
ATOM   1905 H HE2  . HIS   A 1 86  ? 31.741 5.385   9.986   1.00 15.76 ?  86  HIS   A HE2  1 
ATOM   1906 N N    . ASN   A 1 87  ? 27.432 5.569   15.835  1.00 15.01 ?  87  ASN   A N    1 
ATOM   1907 C CA   . ASN   A 1 87  ? 26.467 5.556   16.914  1.00 15.85 ?  87  ASN   A CA   1 
ATOM   1908 C C    . ASN   A 1 87  ? 25.332 4.573   16.680  1.00 16.61 ?  87  ASN   A C    1 
ATOM   1909 O O    . ASN   A 1 87  ? 24.426 4.501   17.514  1.00 18.83 ?  87  ASN   A O    1 
ATOM   1910 C CB   . ASN   A 1 87  ? 25.889 6.966   17.083  1.00 16.57 ?  87  ASN   A CB   1 
ATOM   1911 C CG   . ASN   A 1 87  ? 25.371 7.550   15.774  1.00 17.57 ?  87  ASN   A CG   1 
ATOM   1912 O OD1  . ASN   A 1 87  ? 26.012 7.444   14.732  1.00 18.00 ?  87  ASN   A OD1  1 
ATOM   1913 N ND2  . ASN   A 1 87  ? 24.207 8.168   15.827  1.00 18.73 ?  87  ASN   A ND2  1 
ATOM   1914 H H    . ASN   A 1 87  ? 27.279 6.179   15.256  1.00 18.01 ?  87  ASN   A H    1 
ATOM   1915 H HA   . ASN   A 1 87  ? 26.906 5.305   17.745  1.00 19.02 ?  87  ASN   A HA   1 
ATOM   1916 H HB2  . ASN   A 1 87  ? 25.150 6.931   17.717  1.00 19.88 ?  87  ASN   A HB2  1 
ATOM   1917 H HB3  . ASN   A 1 87  ? 26.585 7.550   17.425  1.00 19.88 ?  87  ASN   A HB3  1 
ATOM   1918 H HD21 . ASN   A 1 87  ? 23.875 8.508   15.114  1.00 22.48 ?  87  ASN   A HD21 1 
ATOM   1919 H HD22 . ASN   A 1 87  ? 23.787 8.230   16.574  1.00 22.48 ?  87  ASN   A HD22 1 
ATOM   1920 N N    A LEU   A 1 88  ? 25.365 3.810   15.591  0.40 15.74 ?  88  LEU   A N    1 
ATOM   1921 N N    B LEU   A 1 88  ? 25.361 3.808   15.592  0.60 15.49 ?  88  LEU   A N    1 
ATOM   1922 C CA   A LEU   A 1 88  ? 24.249 2.956   15.201  0.40 15.65 ?  88  LEU   A CA   1 
ATOM   1923 C CA   B LEU   A 1 88  ? 24.238 2.956   15.214  0.60 15.59 ?  88  LEU   A CA   1 
ATOM   1924 C C    A LEU   A 1 88  ? 24.462 1.484   15.524  0.40 15.28 ?  88  LEU   A C    1 
ATOM   1925 C C    B LEU   A 1 88  ? 24.458 1.474   15.484  0.60 15.38 ?  88  LEU   A C    1 
ATOM   1926 O O    A LEU   A 1 88  ? 23.487 0.771   15.780  0.40 15.92 ?  88  LEU   A O    1 
ATOM   1927 O O    B LEU   A 1 88  ? 23.480 0.737   15.646  0.60 16.26 ?  88  LEU   A O    1 
ATOM   1928 C CB   A LEU   A 1 88  ? 24.002 3.088   13.694  0.40 16.05 ?  88  LEU   A CB   1 
ATOM   1929 C CB   B LEU   A 1 88  ? 23.930 3.140   13.725  0.60 15.92 ?  88  LEU   A CB   1 
ATOM   1930 C CG   A LEU   A 1 88  ? 23.701 4.487   13.154  0.40 17.06 ?  88  LEU   A CG   1 
ATOM   1931 C CG   B LEU   A 1 88  ? 23.610 4.578   13.317  0.60 16.96 ?  88  LEU   A CG   1 
ATOM   1932 C CD1  A LEU   A 1 88  ? 23.567 4.440   11.642  0.40 17.38 ?  88  LEU   A CD1  1 
ATOM   1933 C CD1  B LEU   A 1 88  ? 23.389 4.667   11.817  0.60 17.34 ?  88  LEU   A CD1  1 
ATOM   1934 C CD2  A LEU   A 1 88  ? 22.442 5.059   13.788  0.40 18.32 ?  88  LEU   A CD2  1 
ATOM   1935 C CD2  B LEU   A 1 88  ? 22.394 5.095   14.078  0.60 18.48 ?  88  LEU   A CD2  1 
ATOM   1936 H H    A LEU   A 1 88  ? 26.039 3.761   15.063  0.40 18.89 ?  88  LEU   A H    1 
ATOM   1937 H H    B LEU   A 1 88  ? 26.026 3.769   15.052  0.60 18.59 ?  88  LEU   A H    1 
ATOM   1938 H HA   A LEU   A 1 88  ? 23.449 3.244   15.662  0.40 18.78 ?  88  LEU   A HA   1 
ATOM   1939 H HA   B LEU   A 1 88  ? 23.456 3.227   15.713  0.60 18.71 ?  88  LEU   A HA   1 
ATOM   1940 H HB2  A LEU   A 1 88  ? 24.790 2.772   13.228  0.40 19.25 ?  88  LEU   A HB2  1 
ATOM   1941 H HB2  B LEU   A 1 88  ? 24.699 2.854   13.207  0.60 19.11 ?  88  LEU   A HB2  1 
ATOM   1942 H HB3  A LEU   A 1 88  ? 23.246 2.529   13.462  0.40 19.25 ?  88  LEU   A HB3  1 
ATOM   1943 H HB3  B LEU   A 1 88  ? 23.161 2.593   13.495  0.60 19.11 ?  88  LEU   A HB3  1 
ATOM   1944 H HG   A LEU   A 1 88  ? 24.439 5.077   13.369  0.40 20.47 ?  88  LEU   A HG   1 
ATOM   1945 H HG   B LEU   A 1 88  ? 24.364 5.144   13.539  0.60 20.35 ?  88  LEU   A HG   1 
ATOM   1946 H HD11 A LEU   A 1 88  ? 23.405 5.337   11.309  0.40 20.85 ?  88  LEU   A HD11 1 
ATOM   1947 H HD11 B LEU   A 1 88  ? 23.197 5.588   11.579  0.60 20.81 ?  88  LEU   A HD11 1 
ATOM   1948 H HD12 A LEU   A 1 88  ? 24.387 4.089   11.261  0.40 20.85 ?  88  LEU   A HD12 1 
ATOM   1949 H HD12 B LEU   A 1 88  ? 24.192 4.369   11.360  0.60 20.81 ?  88  LEU   A HD12 1 
ATOM   1950 H HD13 A LEU   A 1 88  ? 22.821 3.863   11.410  0.40 20.85 ?  88  LEU   A HD13 1 
ATOM   1951 H HD13 B LEU   A 1 88  ? 22.641 4.099   11.572  0.60 20.81 ?  88  LEU   A HD13 1 
ATOM   1952 H HD21 A LEU   A 1 88  ? 22.238 5.912   13.373  0.40 21.98 ?  88  LEU   A HD21 1 
ATOM   1953 H HD21 B LEU   A 1 88  ? 22.111 5.935   13.686  0.60 22.18 ?  88  LEU   A HD21 1 
ATOM   1954 H HD22 A LEU   A 1 88  ? 21.709 4.439   13.649  0.40 21.98 ?  88  LEU   A HD22 1 
ATOM   1955 H HD22 B LEU   A 1 88  ? 21.681 4.440   14.013  0.60 22.18 ?  88  LEU   A HD22 1 
ATOM   1956 H HD23 A LEU   A 1 88  ? 22.596 5.182   14.738  0.40 21.98 ?  88  LEU   A HD23 1 
ATOM   1957 H HD23 B LEU   A 1 88  ? 22.638 5.228   15.007  0.60 22.18 ?  88  LEU   A HD23 1 
ATOM   1958 N N    . ALA   A 1 89  ? 25.708 1.022   15.512  1.00 14.66 ?  89  ALA   A N    1 
ATOM   1959 C CA   . ALA   A 1 89  ? 26.040 -0.391  15.619  1.00 14.05 ?  89  ALA   A CA   1 
ATOM   1960 C C    . ALA   A 1 89  ? 27.526 -0.461  15.931  1.00 14.38 ?  89  ALA   A C    1 
ATOM   1961 O O    . ALA   A 1 89  ? 28.242 0.534   15.808  1.00 15.24 ?  89  ALA   A O    1 
ATOM   1962 C CB   . ALA   A 1 89  ? 25.758 -1.105  14.298  1.00 13.32 ?  89  ALA   A CB   1 
ATOM   1963 H H    A ALA   A 1 89  ? 26.403 1.527   15.433  0.40 17.60 ?  89  ALA   A H    1 
ATOM   1964 H H    B ALA   A 1 89  ? 26.402 1.530   15.453  0.60 17.60 ?  89  ALA   A H    1 
ATOM   1965 H HA   . ALA   A 1 89  ? 25.534 -0.806  16.336  1.00 16.85 ?  89  ALA   A HA   1 
ATOM   1966 H HB1  . ALA   A 1 89  ? 26.001 -2.042  14.386  1.00 15.98 ?  89  ALA   A HB1  1 
ATOM   1967 H HB2  . ALA   A 1 89  ? 24.811 -1.031  14.091  1.00 15.98 ?  89  ALA   A HB2  1 
ATOM   1968 H HB3  . ALA   A 1 89  ? 26.283 -0.694  13.595  1.00 15.98 ?  89  ALA   A HB3  1 
ATOM   1969 N N    . LYS   A 1 90  ? 28.003 -1.643  16.317  1.00 14.84 ?  90  LYS   A N    1 
ATOM   1970 C CA   . LYS   A 1 90  ? 29.448 -1.797  16.453  1.00 15.68 ?  90  LYS   A CA   1 
ATOM   1971 C C    . LYS   A 1 90  ? 30.139 -1.606  15.105  1.00 14.55 ?  90  LYS   A C    1 
ATOM   1972 O O    . LYS   A 1 90  ? 31.074 -0.799  14.972  1.00 15.59 ?  90  LYS   A O    1 
ATOM   1973 C CB   . LYS   A 1 90  ? 29.794 -3.155  17.066  1.00 17.87 ?  90  LYS   A CB   1 
ATOM   1974 C CG   . LYS   A 1 90  ? 31.278 -3.298  17.372  1.00 22.56 ?  90  LYS   A CG   1 
ATOM   1975 C CD   . LYS   A 1 90  ? 31.545 -4.491  18.273  1.00 27.34 ?  90  LYS   A CD   1 
ATOM   1976 C CE   . LYS   A 1 90  ? 32.977 -4.498  18.786  1.00 31.37 ?  90  LYS   A CE   1 
ATOM   1977 N NZ   . LYS   A 1 90  ? 33.954 -4.906  17.741  1.00 33.71 ?  90  LYS   A NZ   1 
ATOM   1978 H H    . LYS   A 1 90  ? 27.528 -2.334  16.505  1.00 17.81 ?  90  LYS   A H    1 
ATOM   1979 H HA   . LYS   A 1 90  ? 29.776 -1.112  17.051  1.00 18.81 ?  90  LYS   A HA   1 
ATOM   1980 H HB2  . LYS   A 1 90  ? 29.302 -3.261  17.898  1.00 21.45 ?  90  LYS   A HB2  1 
ATOM   1981 H HB3  . LYS   A 1 90  ? 29.544 -3.858  16.445  1.00 21.45 ?  90  LYS   A HB3  1 
ATOM   1982 H HG2  . LYS   A 1 90  ? 31.766 -3.427  16.544  1.00 27.07 ?  90  LYS   A HG2  1 
ATOM   1983 H HG3  . LYS   A 1 90  ? 31.591 -2.499  17.826  1.00 27.07 ?  90  LYS   A HG3  1 
ATOM   1984 H HD2  . LYS   A 1 90  ? 30.949 -4.457  19.038  1.00 32.81 ?  90  LYS   A HD2  1 
ATOM   1985 H HD3  . LYS   A 1 90  ? 31.399 -5.310  17.773  1.00 32.81 ?  90  LYS   A HD3  1 
ATOM   1986 H HE2  . LYS   A 1 90  ? 33.212 -3.605  19.084  1.00 37.64 ?  90  LYS   A HE2  1 
ATOM   1987 H HE3  . LYS   A 1 90  ? 33.048 -5.123  19.525  1.00 37.64 ?  90  LYS   A HE3  1 
ATOM   1988 H HZ1  . LYS   A 1 90  ? 34.775 -4.933  18.086  1.00 40.45 ?  90  LYS   A HZ1  1 
ATOM   1989 H HZ2  . LYS   A 1 90  ? 33.746 -5.714  17.430  1.00 40.45 ?  90  LYS   A HZ2  1 
ATOM   1990 H HZ3  . LYS   A 1 90  ? 33.942 -4.324  17.069  1.00 40.45 ?  90  LYS   A HZ3  1 
ATOM   1991 N N    . HIS   A 1 91  ? 29.667 -2.324  14.086  1.00 13.03 ?  91  HIS   A N    1 
ATOM   1992 C CA   . HIS   A 1 91  ? 30.239 -2.312  12.755  1.00 12.56 ?  91  HIS   A CA   1 
ATOM   1993 C C    . HIS   A 1 91  ? 29.150 -2.036  11.735  1.00 11.20 ?  91  HIS   A C    1 
ATOM   1994 O O    . HIS   A 1 91  ? 27.983 -2.391  11.937  1.00 11.80 ?  91  HIS   A O    1 
ATOM   1995 C CB   . HIS   A 1 91  ? 30.823 -3.686  12.390  1.00 15.14 ?  91  HIS   A CB   1 
ATOM   1996 C CG   . HIS   A 1 91  ? 31.825 -4.203  13.370  1.00 19.30 ?  91  HIS   A CG   1 
ATOM   1997 N ND1  . HIS   A 1 91  ? 33.098 -3.687  13.475  1.00 21.68 ?  91  HIS   A ND1  1 
ATOM   1998 C CD2  . HIS   A 1 91  ? 31.748 -5.203  14.279  1.00 21.32 ?  91  HIS   A CD2  1 
ATOM   1999 C CE1  . HIS   A 1 91  ? 33.761 -4.342  14.412  1.00 22.71 ?  91  HIS   A CE1  1 
ATOM   2000 N NE2  . HIS   A 1 91  ? 32.965 -5.269  14.914  1.00 22.95 ?  91  HIS   A NE2  1 
ATOM   2001 H H    . HIS   A 1 91  ? 28.987 -2.860  14.155  1.00 15.63 ?  91  HIS   A H    1 
ATOM   2002 H HA   . HIS   A 1 91  ? 30.931 -1.641  12.687  1.00 15.07 ?  91  HIS   A HA   1 
ATOM   2003 H HB2  . HIS   A 1 91  ? 30.100 -4.335  12.344  1.00 18.17 ?  91  HIS   A HB2  1 
ATOM   2004 H HB3  . HIS   A 1 91  ? 31.259 -3.624  11.527  1.00 18.17 ?  91  HIS   A HB3  1 
ATOM   2005 H HD1  . HIS   A 1 91  ? 33.412 -3.037  13.002  1.00 26.02 ?  91  HIS   A HD1  1 
ATOM   2006 H HD2  . HIS   A 1 91  ? 31.018 -5.748  14.447  1.00 25.58 ?  91  HIS   A HD2  1 
ATOM   2007 H HE1  . HIS   A 1 91  ? 34.642 -4.174  14.670  1.00 27.25 ?  91  HIS   A HE1  1 
ATOM   2008 N N    . CYS   A 1 92  ? 29.549 -1.443  10.613  1.00 10.99 ?  92  CYS   A N    1 
ATOM   2009 C CA   . CYS   A 1 92  ? 28.707 -1.365  9.429   1.00 10.92 ?  92  CYS   A CA   1 
ATOM   2010 C C    . CYS   A 1 92  ? 29.347 -2.186  8.320   1.00 10.38 ?  92  CYS   A C    1 
ATOM   2011 O O    . CYS   A 1 92  ? 30.505 -1.940  7.947   1.00 11.10 ?  92  CYS   A O    1 
ATOM   2012 C CB   . CYS   A 1 92  ? 28.493 0.077   8.967   1.00 11.17 ?  92  CYS   A CB   1 
ATOM   2013 S SG   . CYS   A 1 92  ? 27.475 0.179   7.469   1.00 10.61 ?  92  CYS   A SG   1 
ATOM   2014 H H    . CYS   A 1 92  ? 30.324 -1.078  10.510  1.00 13.18 ?  92  CYS   A H    1 
ATOM   2015 H HA   . CYS   A 1 92  ? 27.840 -1.750  9.631   1.00 13.10 ?  92  CYS   A HA   1 
ATOM   2016 H HB2  . CYS   A 1 92  ? 28.043 0.572   9.672   1.00 13.40 ?  92  CYS   A HB2  1 
ATOM   2017 H HB3  . CYS   A 1 92  ? 29.352 0.479   8.775   1.00 13.40 ?  92  CYS   A HB3  1 
ATOM   2018 H HG   . CYS   A 1 92  ? 27.335 1.336   7.177   1.00 12.73 ?  92  CYS   A HG   1 
ATOM   2019 N N    . LEU   A 1 93  ? 28.606 -3.175  7.823   1.00 10.19 ?  93  LEU   A N    1 
ATOM   2020 C CA   . LEU   A 1 93  ? 29.009 -3.933  6.646   1.00 9.76  ?  93  LEU   A CA   1 
ATOM   2021 C C    . LEU   A 1 93  ? 28.410 -3.241  5.428   1.00 9.48  ?  93  LEU   A C    1 
ATOM   2022 O O    . LEU   A 1 93  ? 27.194 -3.292  5.208   1.00 9.72  ?  93  LEU   A O    1 
ATOM   2023 C CB   . LEU   A 1 93  ? 28.525 -5.375  6.756   1.00 10.61 ?  93  LEU   A CB   1 
ATOM   2024 C CG   . LEU   A 1 93  ? 28.909 -6.276  5.582   1.00 10.73 ?  93  LEU   A CG   1 
ATOM   2025 C CD1  . LEU   A 1 93  ? 30.410 -6.540  5.565   1.00 11.71 ?  93  LEU   A CD1  1 
ATOM   2026 C CD2  . LEU   A 1 93  ? 28.136 -7.591  5.613   1.00 11.68 ?  93  LEU   A CD2  1 
ATOM   2027 H H    . LEU   A 1 93  ? 27.852 -3.421  8.158   1.00 12.22 ?  93  LEU   A H    1 
ATOM   2028 H HA   . LEU   A 1 93  ? 29.972 -3.928  6.571   1.00 11.70 ?  93  LEU   A HA   1 
ATOM   2029 H HB2  . LEU   A 1 93  ? 28.898 -5.763  7.563   1.00 12.72 ?  93  LEU   A HB2  1 
ATOM   2030 H HB3  . LEU   A 1 93  ? 27.557 -5.374  6.814   1.00 12.72 ?  93  LEU   A HB3  1 
ATOM   2031 H HG   . LEU   A 1 93  ? 28.692 -5.832  4.756   1.00 12.88 ?  93  LEU   A HG   1 
ATOM   2032 H HD11 . LEU   A 1 93  ? 30.625 -7.158  4.847   1.00 14.05 ?  93  LEU   A HD11 1 
ATOM   2033 H HD12 . LEU   A 1 93  ? 30.885 -5.705  5.434   1.00 14.05 ?  93  LEU   A HD12 1 
ATOM   2034 H HD13 . LEU   A 1 93  ? 30.679 -6.935  6.419   1.00 14.05 ?  93  LEU   A HD13 1 
ATOM   2035 H HD21 . LEU   A 1 93  ? 28.413 -8.138  4.857   1.00 14.02 ?  93  LEU   A HD21 1 
ATOM   2036 H HD22 . LEU   A 1 93  ? 28.329 -8.056  6.442   1.00 14.02 ?  93  LEU   A HD22 1 
ATOM   2037 H HD23 . LEU   A 1 93  ? 27.190 -7.398  5.551   1.00 14.02 ?  93  LEU   A HD23 1 
ATOM   2038 N N    . HIS   A 1 94  ? 29.260 -2.552  4.664   1.00 9.22  ?  94  HIS   A N    1 
ATOM   2039 C CA   . HIS   A 1 94  ? 28.828 -1.879  3.444   1.00 9.13  ?  94  HIS   A CA   1 
ATOM   2040 C C    . HIS   A 1 94  ? 28.827 -2.912  2.332   1.00 9.37  ?  94  HIS   A C    1 
ATOM   2041 O O    . HIS   A 1 94  ? 29.887 -3.428  1.979   1.00 10.96 ?  94  HIS   A O    1 
ATOM   2042 C CB   . HIS   A 1 94  ? 29.785 -0.737  3.102   1.00 9.56  ?  94  HIS   A CB   1 
ATOM   2043 C CG   . HIS   A 1 94  ? 29.782 0.357   4.112   1.00 9.45  ?  94  HIS   A CG   1 
ATOM   2044 N ND1  . HIS   A 1 94  ? 28.903 1.418   4.065   1.00 9.59  ?  94  HIS   A ND1  1 
ATOM   2045 C CD2  . HIS   A 1 94  ? 30.523 0.521   5.231   1.00 10.15 ?  94  HIS   A CD2  1 
ATOM   2046 C CE1  . HIS   A 1 94  ? 29.121 2.196   5.108   1.00 9.84  ?  94  HIS   A CE1  1 
ATOM   2047 N NE2  . HIS   A 1 94  ? 30.099 1.677   5.830   1.00 10.27 ?  94  HIS   A NE2  1 
ATOM   2048 H H    . HIS   A 1 94  ? 30.103 -2.460  4.829   1.00 11.06 ?  94  HIS   A H    1 
ATOM   2049 H HA   . HIS   A 1 94  ? 27.928 -1.531  3.557   1.00 10.95 ?  94  HIS   A HA   1 
ATOM   2050 H HB2  . HIS   A 1 94  ? 30.679 -1.085  3.043   1.00 11.47 ?  94  HIS   A HB2  1 
ATOM   2051 H HB3  . HIS   A 1 94  ? 29.513 -0.350  2.254   1.00 11.47 ?  94  HIS   A HB3  1 
ATOM   2052 H HD2  . HIS   A 1 94  ? 31.199 -0.034  5.538   1.00 12.18 ?  94  HIS   A HD2  1 
ATOM   2053 H HE1  . HIS   A 1 94  ? 28.657 2.983   5.299   1.00 11.81 ?  94  HIS   A HE1  1 
ATOM   2054 H HE2  . HIS   A 1 94  ? 30.415 2.021   6.554   1.00 12.32 ?  94  HIS   A HE2  1 
ATOM   2055 N N    . VAL   A 1 95  ? 27.654 -3.233  1.791   1.00 9.00  ?  95  VAL   A N    1 
ATOM   2056 C CA   . VAL   A 1 95  ? 27.508 -4.270  0.772   1.00 9.33  ?  95  VAL   A CA   1 
ATOM   2057 C C    . VAL   A 1 95  ? 26.958 -3.636  -0.490  1.00 8.94  ?  95  VAL   A C    1 
ATOM   2058 O O    . VAL   A 1 95  ? 25.962 -2.906  -0.432  1.00 9.87  ?  95  VAL   A O    1 
ATOM   2059 C CB   . VAL   A 1 95  ? 26.570 -5.400  1.231   1.00 10.02 ?  95  VAL   A CB   1 
ATOM   2060 C CG1  . VAL   A 1 95  ? 26.427 -6.443  0.127   1.00 10.95 ?  95  VAL   A CG1  1 
ATOM   2061 C CG2  . VAL   A 1 95  ? 27.084 -6.030  2.503   1.00 10.32 ?  95  VAL   A CG2  1 
ATOM   2062 H H    . VAL   A 1 95  ? 26.904 -2.860  2.003   1.00 10.79 ?  95  VAL   A H    1 
ATOM   2063 H HA   . VAL   A 1 95  ? 28.369 -4.655  0.570   1.00 11.19 ?  95  VAL   A HA   1 
ATOM   2064 H HB   . VAL   A 1 95  ? 25.688 -5.038  1.409   1.00 12.03 ?  95  VAL   A HB   1 
ATOM   2065 H HG11 . VAL   A 1 95  ? 26.037 -7.252  0.501   1.00 13.13 ?  95  VAL   A HG11 1 
ATOM   2066 H HG12 . VAL   A 1 95  ? 25.849 -6.096  -0.571  1.00 13.13 ?  95  VAL   A HG12 1 
ATOM   2067 H HG13 . VAL   A 1 95  ? 27.304 -6.642  -0.237  1.00 13.13 ?  95  VAL   A HG13 1 
ATOM   2068 H HG21 . VAL   A 1 95  ? 26.514 -6.785  2.733   1.00 12.38 ?  95  VAL   A HG21 1 
ATOM   2069 H HG22 . VAL   A 1 95  ? 27.991 -6.334  2.359   1.00 12.38 ?  95  VAL   A HG22 1 
ATOM   2070 H HG23 . VAL   A 1 95  ? 27.057 -5.370  3.209   1.00 12.38 ?  95  VAL   A HG23 1 
ATOM   2071 N N    . VAL   A 1 96  ? 27.576 -3.934  -1.629  1.00 9.12  ?  96  VAL   A N    1 
ATOM   2072 C CA   . VAL   A 1 96  ? 27.160 -3.384  -2.912  1.00 9.76  ?  96  VAL   A CA   1 
ATOM   2073 C C    . VAL   A 1 96  ? 26.351 -4.433  -3.668  1.00 10.34 ?  96  VAL   A C    1 
ATOM   2074 O O    . VAL   A 1 96  ? 26.904 -5.376  -4.238  1.00 11.22 ?  96  VAL   A O    1 
ATOM   2075 C CB   . VAL   A 1 96  ? 28.352 -2.903  -3.741  1.00 10.18 ?  96  VAL   A CB   1 
ATOM   2076 C CG1  . VAL   A 1 96  ? 27.851 -2.268  -5.020  1.00 10.57 ?  96  VAL   A CG1  1 
ATOM   2077 C CG2  . VAL   A 1 96  ? 29.208 -1.916  -2.955  1.00 10.83 ?  96  VAL   A CG2  1 
ATOM   2078 H H    . VAL   A 1 96  ? 28.269 -4.448  -1.682  1.00 10.94 ?  96  VAL   A H    1 
ATOM   2079 H HA   . VAL   A 1 96  ? 26.588 -2.618  -2.756  1.00 11.71 ?  96  VAL   A HA   1 
ATOM   2080 H HB   . VAL   A 1 96  ? 28.908 -3.655  -3.979  1.00 12.21 ?  96  VAL   A HB   1 
ATOM   2081 H HG11 . VAL   A 1 96  ? 28.586 -1.793  -5.445  1.00 12.69 ?  96  VAL   A HG11 1 
ATOM   2082 H HG12 . VAL   A 1 96  ? 27.523 -2.960  -5.611  1.00 12.69 ?  96  VAL   A HG12 1 
ATOM   2083 H HG13 . VAL   A 1 96  ? 27.140 -1.643  -4.807  1.00 12.69 ?  96  VAL   A HG13 1 
ATOM   2084 H HG21 . VAL   A 1 96  ? 29.915 -1.571  -3.524  1.00 13.00 ?  96  VAL   A HG21 1 
ATOM   2085 H HG22 . VAL   A 1 96  ? 28.650 -1.177  -2.647  1.00 13.00 ?  96  VAL   A HG22 1 
ATOM   2086 H HG23 . VAL   A 1 96  ? 29.596 -2.367  -2.188  1.00 13.00 ?  96  VAL   A HG23 1 
ATOM   2087 N N    A GLY   A 1 97  ? 25.033 -4.274  -3.677  0.40 10.46 ?  97  GLY   A N    1 
ATOM   2088 N N    B GLY   A 1 97  ? 25.033 -4.271  -3.693  0.60 10.36 ?  97  GLY   A N    1 
ATOM   2089 C CA   A GLY   A 1 97  ? 24.199 -5.013  -4.589  0.40 10.94 ?  97  GLY   A CA   1 
ATOM   2090 C CA   B GLY   A 1 97  ? 24.202 -5.040  -4.583  0.60 10.97 ?  97  GLY   A CA   1 
ATOM   2091 C C    A GLY   A 1 97  ? 24.239 -4.351  -5.949  0.40 11.19 ?  97  GLY   A C    1 
ATOM   2092 C C    B GLY   A 1 97  ? 24.172 -4.394  -5.951  0.60 11.30 ?  97  GLY   A C    1 
ATOM   2093 O O    A GLY   A 1 97  ? 24.619 -3.183  -6.076  0.40 11.88 ?  97  GLY   A O    1 
ATOM   2094 O O    B GLY   A 1 97  ? 24.386 -3.187  -6.090  0.60 11.88 ?  97  GLY   A O    1 
ATOM   2095 H H    A GLY   A 1 97  ? 24.603 -3.735  -3.159  0.40 12.55 ?  97  GLY   A H    1 
ATOM   2096 H H    B GLY   A 1 97  ? 24.600 -3.715  -3.194  0.60 12.43 ?  97  GLY   A H    1 
ATOM   2097 H HA2  A GLY   A 1 97  ? 24.525 -5.922  -4.664  0.40 13.13 ?  97  GLY   A HA2  1 
ATOM   2098 H HA2  B GLY   A 1 97  ? 24.558 -5.937  -4.659  0.60 13.17 ?  97  GLY   A HA2  1 
ATOM   2099 H HA3  A GLY   A 1 97  ? 23.284 -5.029  -4.263  0.40 13.13 ?  97  GLY   A HA3  1 
ATOM   2100 H HA3  B GLY   A 1 97  ? 23.298 -5.087  -4.232  0.60 13.17 ?  97  GLY   A HA3  1 
ATOM   2101 N N    A PRO   A 1 98  ? 23.857 -5.077  -6.996  0.40 11.27 ?  98  PRO   A N    1 
ATOM   2102 N N    B PRO   A 1 98  ? 23.889 -5.175  -6.989  0.60 11.57 ?  98  PRO   A N    1 
ATOM   2103 C CA   A PRO   A 1 98  ? 23.759 -4.446  -8.317  0.40 12.01 ?  98  PRO   A CA   1 
ATOM   2104 C CA   B PRO   A 1 98  ? 23.777 -4.592  -8.330  0.60 13.09 ?  98  PRO   A CA   1 
ATOM   2105 C C    A PRO   A 1 98  ? 22.651 -3.402  -8.355  0.40 12.41 ?  98  PRO   A C    1 
ATOM   2106 C C    B PRO   A 1 98  ? 22.637 -3.585  -8.406  0.60 14.05 ?  98  PRO   A C    1 
ATOM   2107 O O    A PRO   A 1 98  ? 21.580 -3.577  -7.768  0.40 12.27 ?  98  PRO   A O    1 
ATOM   2108 O O    B PRO   A 1 98  ? 21.557 -3.785  -7.846  0.60 14.38 ?  98  PRO   A O    1 
ATOM   2109 C CB   A PRO   A 1 98  ? 23.447 -5.623  -9.249  0.40 12.66 ?  98  PRO   A CB   1 
ATOM   2110 C CB   B PRO   A 1 98  ? 23.516 -5.811  -9.224  0.60 13.33 ?  98  PRO   A CB   1 
ATOM   2111 C CG   A PRO   A 1 98  ? 22.835 -6.664  -8.361  0.40 12.66 ?  98  PRO   A CG   1 
ATOM   2112 C CG   B PRO   A 1 98  ? 22.898 -6.828  -8.306  0.60 13.20 ?  98  PRO   A CG   1 
ATOM   2113 C CD   A PRO   A 1 98  ? 23.544 -6.517  -7.041  0.40 11.96 ?  98  PRO   A CD   1 
ATOM   2114 C CD   B PRO   A 1 98  ? 23.594 -6.620  -6.984  0.60 11.86 ?  98  PRO   A CD   1 
ATOM   2115 H HA   A PRO   A 1 98  ? 24.606 -4.045  -8.565  0.40 14.41 ?  98  PRO   A HA   1 
ATOM   2116 H HA   B PRO   A 1 98  ? 24.609 -4.167  -8.586  0.60 15.71 ?  98  PRO   A HA   1 
ATOM   2117 H HB2  A PRO   A 1 98  ? 22.816 -5.342  -9.930  0.40 15.19 ?  98  PRO   A HB2  1 
ATOM   2118 H HB2  B PRO   A 1 98  ? 22.901 -5.569  -9.936  0.60 15.99 ?  98  PRO   A HB2  1 
ATOM   2119 H HB3  A PRO   A 1 98  ? 24.266 -5.952  -9.650  0.40 15.19 ?  98  PRO   A HB3  1 
ATOM   2120 H HB3  B PRO   A 1 98  ? 24.353 -6.135  -9.588  0.60 15.99 ?  98  PRO   A HB3  1 
ATOM   2121 H HG2  A PRO   A 1 98  ? 21.887 -6.492  -8.261  0.40 15.19 ?  98  PRO   A HG2  1 
ATOM   2122 H HG2  B PRO   A 1 98  ? 21.946 -6.661  -8.226  0.60 15.84 ?  98  PRO   A HG2  1 
ATOM   2123 H HG3  A PRO   A 1 98  ? 22.990 -7.544  -8.736  0.40 15.19 ?  98  PRO   A HG3  1 
ATOM   2124 H HG3  B PRO   A 1 98  ? 23.065 -7.720  -8.647  0.60 15.84 ?  98  PRO   A HG3  1 
ATOM   2125 H HD2  A PRO   A 1 98  ? 22.954 -6.765  -6.309  0.40 14.35 ?  98  PRO   A HD2  1 
ATOM   2126 H HD2  B PRO   A 1 98  ? 23.000 -6.849  -6.250  0.60 14.23 ?  98  PRO   A HD2  1 
ATOM   2127 H HD3  A PRO   A 1 98  ? 24.361 -7.040  -7.030  0.40 14.35 ?  98  PRO   A HD3  1 
ATOM   2128 H HD3  B PRO   A 1 98  ? 24.418 -7.128  -6.948  0.60 14.23 ?  98  PRO   A HD3  1 
ATOM   2129 N N    A ASN   A 1 99  ? 22.925 -2.303  -9.054  0.40 13.49 ?  99  ASN   A N    1 
ATOM   2130 N N    B ASN   A 1 99  ? 22.899 -2.480  -9.093  0.60 15.68 ?  99  ASN   A N    1 
ATOM   2131 C CA   A ASN   A 1 99  ? 21.954 -1.235  -9.268  0.40 14.06 ?  99  ASN   A CA   1 
ATOM   2132 C CA   B ASN   A 1 99  ? 21.896 -1.454  -9.369  0.60 17.46 ?  99  ASN   A CA   1 
ATOM   2133 C C    A ASN   A 1 99  ? 21.357 -1.433  -10.658 0.40 14.05 ?  99  ASN   A C    1 
ATOM   2134 C C    B ASN   A 1 99  ? 21.515 -1.623  -10.836 0.60 19.89 ?  99  ASN   A C    1 
ATOM   2135 O O    A ASN   A 1 99  ? 22.043 -1.245  -11.666 0.40 15.12 ?  99  ASN   A O    1 
ATOM   2136 O O    B ASN   A 1 99  ? 22.263 -1.224  -11.731 0.60 20.73 ?  99  ASN   A O    1 
ATOM   2137 C CB   A ASN   A 1 99  ? 22.635 0.129   -9.145  0.40 15.01 ?  99  ASN   A CB   1 
ATOM   2138 C CB   B ASN   A 1 99  ? 22.478 -0.071  -9.086  0.60 18.28 ?  99  ASN   A CB   1 
ATOM   2139 C CG   A ASN   A 1 99  ? 21.643 1.289   -9.116  0.40 15.70 ?  99  ASN   A CG   1 
ATOM   2140 C CG   B ASN   A 1 99  ? 21.431 1.035   -9.124  0.60 19.65 ?  99  ASN   A CG   1 
ATOM   2141 O OD1  A ASN   A 1 99  ? 20.633 1.280   -9.819  0.40 16.29 ?  99  ASN   A OD1  1 
ATOM   2142 O OD1  B ASN   A 1 99  ? 20.482 0.981   -9.909  0.60 20.36 ?  99  ASN   A OD1  1 
ATOM   2143 N ND2  A ASN   A 1 99  ? 21.942 2.300   -8.305  0.40 15.94 ?  99  ASN   A ND2  1 
ATOM   2144 N ND2  B ASN   A 1 99  ? 21.609 2.050   -8.274  0.60 19.69 ?  99  ASN   A ND2  1 
ATOM   2145 H H    A ASN   A 1 99  ? 23.691 -2.148  -9.415  0.40 16.18 ?  99  ASN   A H    1 
ATOM   2146 H H    B ASN   A 1 99  ? 23.676 -2.287  -9.407  0.60 18.81 ?  99  ASN   A H    1 
ATOM   2147 H HA   A ASN   A 1 99  ? 21.248 -1.294  -8.604  0.40 16.87 ?  99  ASN   A HA   1 
ATOM   2148 H HA   B ASN   A 1 99  ? 21.110 -1.590  -8.812  0.60 20.95 ?  99  ASN   A HA   1 
ATOM   2149 H HB2  A ASN   A 1 99  ? 23.153 0.154   -8.323  0.40 18.01 ?  99  ASN   A HB2  1 
ATOM   2150 H HB2  B ASN   A 1 99  ? 22.887 -0.072  -8.206  0.60 21.94 ?  99  ASN   A HB2  1 
ATOM   2151 H HB3  A ASN   A 1 99  ? 23.222 0.257   -9.907  0.40 18.01 ?  99  ASN   A HB3  1 
ATOM   2152 H HB3  B ASN   A 1 99  ? 23.147 0.129   -9.760  0.60 21.94 ?  99  ASN   A HB3  1 
ATOM   2153 H HD21 A ASN   A 1 99  ? 21.420 2.979   -8.251  0.40 19.13 ?  99  ASN   A HD21 1 
ATOM   2154 H HD21 B ASN   A 1 99  ? 21.050 2.703   -8.251  0.60 23.62 ?  99  ASN   A HD21 1 
ATOM   2155 H HD22 A ASN   A 1 99  ? 22.665 2.276   -7.834  0.40 19.13 ?  99  ASN   A HD22 1 
ATOM   2156 H HD22 B ASN   A 1 99  ? 22.287 2.051   -7.736  0.60 23.62 ?  99  ASN   A HD22 1 
ATOM   2157 N N    A VAL   A 1 100 ? 20.086 -1.840  -10.710 0.40 13.18 ?  100 VAL   A N    1 
ATOM   2158 N N    B VAL   A 1 100 ? 20.361 -2.250  -11.087 0.60 21.57 ?  100 VAL   A N    1 
ATOM   2159 C CA   A VAL   A 1 100 ? 19.440 -2.072  -12.000 0.40 13.69 ?  100 VAL   A CA   1 
ATOM   2160 C CA   B VAL   A 1 100 ? 19.978 -2.509  -12.471 0.60 24.42 ?  100 VAL   A CA   1 
ATOM   2161 C C    A VAL   A 1 100 ? 19.345 -0.774  -12.796 0.40 14.10 ?  100 VAL   A C    1 
ATOM   2162 C C    B VAL   A 1 100 ? 19.622 -1.221  -13.204 0.60 25.63 ?  100 VAL   A C    1 
ATOM   2163 O O    A VAL   A 1 100 ? 19.431 -0.783  -14.030 0.40 14.70 ?  100 VAL   A O    1 
ATOM   2164 O O    B VAL   A 1 100 ? 19.567 -1.215  -14.439 0.60 26.63 ?  100 VAL   A O    1 
ATOM   2165 C CB   A VAL   A 1 100 ? 18.070 -2.758  -11.804 0.40 15.44 ?  100 VAL   A CB   1 
ATOM   2166 C CB   B VAL   A 1 100 ? 18.881 -3.586  -12.606 0.60 26.04 ?  100 VAL   A CB   1 
ATOM   2167 C CG1  A VAL   A 1 100 ? 17.372 -2.965  -13.142 0.40 16.25 ?  100 VAL   A CG1  1 
ATOM   2168 C CG1  B VAL   A 1 100 ? 19.046 -4.660  -11.540 0.60 26.25 ?  100 VAL   A CG1  1 
ATOM   2169 C CG2  A VAL   A 1 100 ? 18.239 -4.089  -11.081 0.40 16.30 ?  100 VAL   A CG2  1 
ATOM   2170 C CG2  B VAL   A 1 100 ? 17.495 -2.964  -12.565 0.60 26.86 ?  100 VAL   A CG2  1 
ATOM   2171 H H    A VAL   A 1 100 ? 19.587 -1.983  -10.020 0.40 15.81 ?  100 VAL   A H    1 
ATOM   2172 H H    B VAL   A 1 100 ? 19.805 -2.530  -10.489 0.60 25.88 ?  100 VAL   A H    1 
ATOM   2173 H HA   A VAL   A 1 100 ? 19.993 -2.686  -12.503 0.40 16.42 ?  100 VAL   A HA   1 
ATOM   2174 H HA   B VAL   A 1 100 ? 20.754 -2.865  -12.921 0.60 29.30 ?  100 VAL   A HA   1 
ATOM   2175 H HB   A VAL   A 1 100 ? 17.505 -2.193  -11.253 0.40 18.53 ?  100 VAL   A HB   1 
ATOM   2176 H HB   B VAL   A 1 100 ? 18.982 -4.018  -13.471 0.60 31.25 ?  100 VAL   A HB   1 
ATOM   2177 H HG11 A VAL   A 1 100 ? 16.610 -3.552  -13.010 0.40 19.50 ?  100 VAL   A HG11 1 
ATOM   2178 H HG11 B VAL   A 1 100 ? 18.513 -5.432  -11.785 0.60 31.50 ?  100 VAL   A HG11 1 
ATOM   2179 H HG12 A VAL   A 1 100 ? 17.076 -2.108  -13.479 0.40 19.50 ?  100 VAL   A HG12 1 
ATOM   2180 H HG12 B VAL   A 1 100 ? 19.983 -4.909  -11.488 0.60 31.50 ?  100 VAL   A HG12 1 
ATOM   2181 H HG13 A VAL   A 1 100 ? 17.998 -3.372  -13.760 0.40 19.50 ?  100 VAL   A HG13 1 
ATOM   2182 H HG13 B VAL   A 1 100 ? 18.749 -4.308  -10.688 0.60 31.50 ?  100 VAL   A HG13 1 
ATOM   2183 H HG21 A VAL   A 1 100 ? 17.377 -4.529  -11.017 0.40 19.56 ?  100 VAL   A HG21 1 
ATOM   2184 H HG21 B VAL   A 1 100 ? 16.844 -3.661  -12.393 0.60 32.23 ?  100 VAL   A HG21 1 
ATOM   2185 H HG22 A VAL   A 1 100 ? 18.858 -4.644  -11.582 0.40 19.56 ?  100 VAL   A HG22 1 
ATOM   2186 H HG22 B VAL   A 1 100 ? 17.468 -2.302  -11.860 0.60 32.23 ?  100 VAL   A HG22 1 
ATOM   2187 H HG23 A VAL   A 1 100 ? 18.591 -3.925  -10.190 0.40 19.56 ?  100 VAL   A HG23 1 
ATOM   2188 H HG23 B VAL   A 1 100 ? 17.310 -2.546  -13.423 0.60 32.23 ?  100 VAL   A HG23 1 
ATOM   2189 N N    A ASN   A 1 101 ? 19.181 0.359   -12.115 0.40 14.81 ?  101 ASN   A N    1 
ATOM   2190 N N    B ASN   A 1 101 ? 19.373 -0.126  -12.477 0.60 26.22 ?  101 ASN   A N    1 
ATOM   2191 C CA   A ASN   A 1 101 ? 19.131 1.639   -12.810 0.40 16.78 ?  101 ASN   A CA   1 
ATOM   2192 C CA   B ASN   A 1 101 ? 19.267 1.177   -13.125 0.60 26.89 ?  101 ASN   A CA   1 
ATOM   2193 C C    A ASN   A 1 101 ? 20.491 2.071   -13.354 0.40 19.54 ?  101 ASN   A C    1 
ATOM   2194 C C    B ASN   A 1 101 ? 20.617 1.653   -13.645 0.60 28.28 ?  101 ASN   A C    1 
ATOM   2195 O O    A ASN   A 1 101 ? 20.584 3.153   -13.949 0.40 21.08 ?  101 ASN   A O    1 
ATOM   2196 O O    B ASN   A 1 101 ? 20.658 2.506   -14.540 0.60 29.13 ?  101 ASN   A O    1 
ATOM   2197 C CB   A ASN   A 1 101 ? 18.538 2.701   -11.886 0.40 16.77 ?  101 ASN   A CB   1 
ATOM   2198 C CB   B ASN   A 1 101 ? 18.669 2.213   -12.165 0.60 25.83 ?  101 ASN   A CB   1 
ATOM   2199 C CG   A ASN   A 1 101 ? 17.153 2.323   -11.389 0.40 16.76 ?  101 ASN   A CG   1 
ATOM   2200 C CG   B ASN   A 1 101 ? 17.280 1.830   -11.679 0.60 25.41 ?  101 ASN   A CG   1 
ATOM   2201 O OD1  A ASN   A 1 101 ? 16.308 1.857   -12.160 0.40 17.31 ?  101 ASN   A OD1  1 
ATOM   2202 O OD1  B ASN   A 1 101 ? 16.497 1.219   -12.407 0.60 25.86 ?  101 ASN   A OD1  1 
ATOM   2203 N ND2  A ASN   A 1 101 ? 16.921 2.499   -10.091 0.40 17.01 ?  101 ASN   A ND2  1 
ATOM   2204 N ND2  B ASN   A 1 101 ? 16.969 2.191   -10.438 0.60 25.27 ?  101 ASN   A ND2  1 
ATOM   2205 H H    A ASN   A 1 101 ? 19.088 0.406   -11.262 0.40 17.77 ?  101 ASN   A H    1 
ATOM   2206 H H    B ASN   A 1 101 ? 19.262 -0.113  -11.623 0.60 31.46 ?  101 ASN   A H    1 
ATOM   2207 H HA   A ASN   A 1 101 ? 18.527 1.541   -13.563 0.40 20.14 ?  101 ASN   A HA   1 
ATOM   2208 H HA   B ASN   A 1 101 ? 18.677 1.105   -13.886 0.60 32.27 ?  101 ASN   A HA   1 
ATOM   2209 H HB2  A ASN   A 1 101 ? 19.121 2.814   -11.120 0.40 20.12 ?  101 ASN   A HB2  1 
ATOM   2210 H HB2  B ASN   A 1 101 ? 19.244 2.308   -11.391 0.60 31.00 ?  101 ASN   A HB2  1 
ATOM   2211 H HB3  A ASN   A 1 101 ? 18.468 3.536   -12.377 0.40 20.12 ?  101 ASN   A HB3  1 
ATOM   2212 H HB3  B ASN   A 1 101 ? 18.597 3.064   -12.626 0.60 31.00 ?  101 ASN   A HB3  1 
ATOM   2213 H HD21 A ASN   A 1 101 ? 16.156 2.301   -9.758  0.40 20.41 ?  101 ASN   A HD21 1 
ATOM   2214 H HD21 B ASN   A 1 101 ? 16.195 2.000   -10.116 0.60 30.33 ?  101 ASN   A HD21 1 
ATOM   2215 H HD22 A ASN   A 1 101 ? 17.539 2.826   -9.583  0.40 20.41 ?  101 ASN   A HD22 1 
ATOM   2216 H HD22 B ASN   A 1 101 ? 17.541 2.619   -9.958  0.60 30.33 ?  101 ASN   A HD22 1 
ATOM   2217 N N    A LYS   A 1 102 ? 21.536 1.261   -13.155 0.40 21.38 ?  102 LYS   A N    1 
ATOM   2218 N N    B LYS   A 1 102 ? 21.714 1.114   -13.112 0.60 29.27 ?  102 LYS   A N    1 
ATOM   2219 C CA   A LYS   A 1 102 ? 22.818 1.419   -13.831 0.40 23.31 ?  102 LYS   A CA   1 
ATOM   2220 C CA   B LYS   A 1 102 ? 23.053 1.368   -13.626 0.60 29.90 ?  102 LYS   A CA   1 
ATOM   2221 C C    A LYS   A 1 102 ? 23.100 0.303   -14.829 0.40 23.79 ?  102 LYS   A C    1 
ATOM   2222 C C    B LYS   A 1 102 ? 23.493 0.320   -14.643 0.60 30.02 ?  102 LYS   A C    1 
ATOM   2223 O O    A LYS   A 1 102 ? 24.184 0.282   -15.419 0.40 24.31 ?  102 LYS   A O    1 
ATOM   2224 O O    B LYS   A 1 102 ? 24.601 0.426   -15.179 0.60 30.28 ?  102 LYS   A O    1 
ATOM   2225 C CB   A LYS   A 1 102 ? 23.963 1.465   -12.810 0.40 24.99 ?  102 LYS   A CB   1 
ATOM   2226 C CB   B LYS   A 1 102 ? 24.069 1.415   -12.475 0.60 30.73 ?  102 LYS   A CB   1 
ATOM   2227 C CG   A LYS   A 1 102 ? 23.901 2.619   -11.829 0.40 26.38 ?  102 LYS   A CG   1 
ATOM   2228 C CG   B LYS   A 1 102 ? 23.822 2.512   -11.445 0.60 31.40 ?  102 LYS   A CG   1 
ATOM   2229 C CD   A LYS   A 1 102 ? 25.079 2.568   -10.866 0.40 27.64 ?  102 LYS   A CD   1 
ATOM   2230 C CD   B LYS   A 1 102 ? 24.870 2.480   -10.334 0.60 31.90 ?  102 LYS   A CD   1 
ATOM   2231 C CE   A LYS   A 1 102 ? 25.014 3.682   -9.835  0.40 28.60 ?  102 LYS   A CE   1 
ATOM   2232 C CE   B LYS   A 1 102 ? 24.649 3.597   -9.321  0.60 32.37 ?  102 LYS   A CE   1 
ATOM   2233 N NZ   A LYS   A 1 102 ? 26.128 3.583   -8.849  0.40 29.15 ?  102 LYS   A NZ   1 
ATOM   2234 N NZ   B LYS   A 1 102 ? 25.653 3.567   -8.214  0.60 32.40 ?  102 LYS   A NZ   1 
ATOM   2235 H H    A LYS   A 1 102 ? 21.527 0.595   -12.607 0.40 25.66 ?  102 LYS   A H    1 
ATOM   2236 H H    B LYS   A 1 102 ? 21.705 0.573   -12.440 0.60 35.12 ?  102 LYS   A H    1 
ATOM   2237 H HA   A LYS   A 1 102 ? 22.818 2.253   -14.317 0.40 27.97 ?  102 LYS   A HA   1 
ATOM   2238 H HA   B LYS   A 1 102 ? 23.061 2.234   -14.059 0.60 35.87 ?  102 LYS   A HA   1 
ATOM   2239 H HB2  A LYS   A 1 102 ? 23.954 0.642   -12.297 0.40 29.99 ?  102 LYS   A HB2  1 
ATOM   2240 H HB2  B LYS   A 1 102 ? 24.049 0.566   -12.006 0.60 36.87 ?  102 LYS   A HB2  1 
ATOM   2241 H HB3  A LYS   A 1 102 ? 24.803 1.536   -13.293 0.40 29.99 ?  102 LYS   A HB3  1 
ATOM   2242 H HB3  B LYS   A 1 102 ? 24.953 1.560   -12.848 0.60 36.87 ?  102 LYS   A HB3  1 
ATOM   2243 H HG2  A LYS   A 1 102 ? 23.938 3.458   -12.315 0.40 31.66 ?  102 LYS   A HG2  1 
ATOM   2244 H HG2  B LYS   A 1 102 ? 23.870 3.377   -11.880 0.60 37.67 ?  102 LYS   A HG2  1 
ATOM   2245 H HG3  A LYS   A 1 102 ? 23.081 2.561   -11.315 0.40 31.66 ?  102 LYS   A HG3  1 
ATOM   2246 H HG3  B LYS   A 1 102 ? 22.949 2.385   -11.043 0.60 37.67 ?  102 LYS   A HG3  1 
ATOM   2247 H HD2  A LYS   A 1 102 ? 25.071 1.719   -10.396 0.40 33.17 ?  102 LYS   A HD2  1 
ATOM   2248 H HD2  B LYS   A 1 102 ? 24.816 1.631   -9.865  0.60 38.28 ?  102 LYS   A HD2  1 
ATOM   2249 H HD3  A LYS   A 1 102 ? 25.906 2.665   -11.366 0.40 33.17 ?  102 LYS   A HD3  1 
ATOM   2250 H HD3  B LYS   A 1 102 ? 25.752 2.592   -10.721 0.60 38.28 ?  102 LYS   A HD3  1 
ATOM   2251 H HE2  A LYS   A 1 102 ? 25.081 4.538   -10.286 0.40 34.31 ?  102 LYS   A HE2  1 
ATOM   2252 H HE2  B LYS   A 1 102 ? 24.723 4.453   -9.771  0.60 38.84 ?  102 LYS   A HE2  1 
ATOM   2253 H HE3  A LYS   A 1 102 ? 24.174 3.622   -9.353  0.40 34.31 ?  102 LYS   A HE3  1 
ATOM   2254 H HE3  B LYS   A 1 102 ? 23.766 3.502   -8.929  0.60 38.84 ?  102 LYS   A HE3  1 
ATOM   2255 H HZ1  A LYS   A 1 102 ? 26.069 4.245   -8.257  0.40 34.97 ?  102 LYS   A HZ1  1 
ATOM   2256 H HZ1  B LYS   A 1 102 ? 25.495 4.231   -7.642  0.60 38.88 ?  102 LYS   A HZ1  1 
ATOM   2257 H HZ2  A LYS   A 1 102 ? 26.085 2.805   -8.419  0.40 34.97 ?  102 LYS   A HZ2  1 
ATOM   2258 H HZ2  B LYS   A 1 102 ? 25.602 2.793   -7.777  0.60 38.88 ?  102 LYS   A HZ2  1 
ATOM   2259 H HZ3  A LYS   A 1 102 ? 26.911 3.639   -9.268  0.40 34.97 ?  102 LYS   A HZ3  1 
ATOM   2260 H HZ3  B LYS   A 1 102 ? 26.474 3.659   -8.545  0.60 38.88 ?  102 LYS   A HZ3  1 
ATOM   2261 N N    A GLY   A 1 103 ? 22.170 -0.630  -15.023 0.40 24.12 ?  103 GLY   A N    1 
ATOM   2262 N N    B GLY   A 1 103 ? 22.663 -0.687  -14.910 0.60 30.00 ?  103 GLY   A N    1 
ATOM   2263 C CA   A GLY   A 1 103 ? 22.386 -1.740  -15.931 0.40 24.30 ?  103 GLY   A CA   1 
ATOM   2264 C CA   B GLY   A 1 103 ? 22.987 -1.707  -15.888 0.60 29.26 ?  103 GLY   A CA   1 
ATOM   2265 C C    A GLY   A 1 103 ? 23.217 -2.873  -15.374 0.40 24.51 ?  103 GLY   A C    1 
ATOM   2266 C C    B GLY   A 1 103 ? 23.781 -2.886  -15.369 0.60 28.69 ?  103 GLY   A C    1 
ATOM   2267 O O    A GLY   A 1 103 ? 23.654 -3.736  -16.143 0.40 24.98 ?  103 GLY   A O    1 
ATOM   2268 O O    B GLY   A 1 103 ? 24.473 -3.544  -16.155 0.60 29.39 ?  103 GLY   A O    1 
ATOM   2269 H H    A GLY   A 1 103 ? 21.405 -0.646  -14.634 0.40 28.94 ?  103 GLY   A H    1 
ATOM   2270 H H    B GLY   A 1 103 ? 21.902 -0.797  -14.532 0.60 35.99 ?  103 GLY   A H    1 
ATOM   2271 H HA2  A GLY   A 1 103 ? 21.531 -2.110  -16.193 0.40 29.16 ?  103 GLY   A HA2  1 
ATOM   2272 H HA2  B GLY   A 1 103 ? 22.160 -2.038  -16.275 0.60 35.11 ?  103 GLY   A HA2  1 
ATOM   2273 H HA3  A GLY   A 1 103 ? 22.827 -1.407  -16.731 0.40 29.16 ?  103 GLY   A HA3  1 
ATOM   2274 H HA3  B GLY   A 1 103 ? 23.504 -1.302  -16.603 0.60 35.11 ?  103 GLY   A HA3  1 
ATOM   2275 N N    A GLU   A 1 104 ? 23.437 -2.911  -14.064 0.40 23.67 ?  104 GLU   A N    1 
ATOM   2276 N N    B GLU   A 1 104 ? 23.697 -3.191  -14.078 0.60 26.50 ?  104 GLU   A N    1 
ATOM   2277 C CA   A GLU   A 1 104 ? 24.332 -3.895  -13.473 0.40 22.60 ?  104 GLU   A CA   1 
ATOM   2278 C CA   B GLU   A 1 104 ? 24.555 -4.190  -13.455 0.60 24.56 ?  104 GLU   A CA   1 
ATOM   2279 C C    A GLU   A 1 104 ? 23.653 -5.255  -13.348 0.40 22.98 ?  104 GLU   A C    1 
ATOM   2280 C C    B GLU   A 1 104 ? 23.880 -5.563  -13.383 0.60 23.84 ?  104 GLU   A C    1 
ATOM   2281 O O    A GLU   A 1 104 ? 22.450 -5.351  -13.088 0.40 23.20 ?  104 GLU   A O    1 
ATOM   2282 O O    B GLU   A 1 104 ? 22.653 -5.688  -13.385 0.60 24.08 ?  104 GLU   A O    1 
ATOM   2283 C CB   A GLU   A 1 104 ? 24.840 -3.397  -12.118 0.40 20.92 ?  104 GLU   A CB   1 
ATOM   2284 C CB   B GLU   A 1 104 ? 25.000 -3.703  -12.071 0.60 24.07 ?  104 GLU   A CB   1 
ATOM   2285 C CG   A GLU   A 1 104 ? 25.741 -2.174  -12.267 0.40 19.75 ?  104 GLU   A CG   1 
ATOM   2286 C CG   B GLU   A 1 104 ? 25.902 -2.463  -12.159 0.60 24.38 ?  104 GLU   A CG   1 
ATOM   2287 C CD   A GLU   A 1 104 ? 26.170 -1.541  -10.961 0.40 18.25 ?  104 GLU   A CD   1 
ATOM   2288 C CD   B GLU   A 1 104 ? 25.966 -1.636  -10.889 0.60 24.66 ?  104 GLU   A CD   1 
ATOM   2289 O OE1  A GLU   A 1 104 ? 25.573 -1.832  -9.905  0.40 16.53 ?  104 GLU   A OE1  1 
ATOM   2290 O OE1  B GLU   A 1 104 ? 25.344 -2.012  -9.878  0.60 24.21 ?  104 GLU   A OE1  1 
ATOM   2291 O OE2  A GLU   A 1 104 ? 27.114 -0.723  -11.006 0.40 18.46 -1 104 GLU   A OE2  1 
ATOM   2292 O OE2  B GLU   A 1 104 ? 26.640 -0.583  -10.916 0.60 25.33 -1 104 GLU   A OE2  1 
ATOM   2293 H H    A GLU   A 1 104 ? 23.076 -2.376  -13.500 0.40 28.41 ?  104 GLU   A H    1 
ATOM   2294 H H    B GLU   A 1 104 ? 23.146 -2.817  -13.531 0.60 31.80 ?  104 GLU   A H    1 
ATOM   2295 H HA   A GLU   A 1 104 ? 25.098 -4.004  -14.053 0.40 27.11 ?  104 GLU   A HA   1 
ATOM   2296 H HA   B GLU   A 1 104 ? 25.352 -4.281  -13.998 0.60 29.47 ?  104 GLU   A HA   1 
ATOM   2297 H HB2  A GLU   A 1 104 ? 24.084 -3.153  -11.563 0.40 25.10 ?  104 GLU   A HB2  1 
ATOM   2298 H HB2  B GLU   A 1 104 ? 24.218 -3.474  -11.547 0.60 28.88 ?  104 GLU   A HB2  1 
ATOM   2299 H HB3  A GLU   A 1 104 ? 25.353 -4.103  -11.694 0.40 25.10 ?  104 GLU   A HB3  1 
ATOM   2300 H HB3  B GLU   A 1 104 ? 25.501 -4.410  -11.635 0.60 28.88 ?  104 GLU   A HB3  1 
ATOM   2301 H HG2  A GLU   A 1 104 ? 26.546 -2.434  -12.739 0.40 23.70 ?  104 GLU   A HG2  1 
ATOM   2302 H HG2  B GLU   A 1 104 ? 26.804 -2.745  -12.370 0.60 29.25 ?  104 GLU   A HG2  1 
ATOM   2303 H HG3  A GLU   A 1 104 ? 25.268 -1.496  -12.770 0.40 23.70 ?  104 GLU   A HG3  1 
ATOM   2304 H HG3  B GLU   A 1 104 ? 25.568 -1.879  -12.855 0.60 29.25 ?  104 GLU   A HG3  1 
ATOM   2305 N N    A ASP   A 1 105 ? 24.446 -6.306  -13.539 0.40 23.12 ?  105 ASP   A N    1 
ATOM   2306 N N    B ASP   A 1 105 ? 24.720 -6.598  -13.304 0.60 23.90 ?  105 ASP   A N    1 
ATOM   2307 C CA   A ASP   A 1 105 ? 23.932 -7.666  -13.621 0.40 23.76 ?  105 ASP   A CA   1 
ATOM   2308 C CA   B ASP   A 1 105 ? 24.286 -7.984  -13.469 0.60 23.96 ?  105 ASP   A CA   1 
ATOM   2309 C C    A ASP   A 1 105 ? 23.237 -8.060  -12.325 0.40 21.79 ?  105 ASP   A C    1 
ATOM   2310 C C    B ASP   A 1 105 ? 23.538 -8.470  -12.229 0.60 22.00 ?  105 ASP   A C    1 
ATOM   2311 O O    A ASP   A 1 105 ? 23.864 -8.104  -11.264 0.40 20.84 ?  105 ASP   A O    1 
ATOM   2312 O O    B ASP   A 1 105 ? 24.096 -8.487  -11.130 0.60 19.68 ?  105 ASP   A O    1 
ATOM   2313 C CB   A ASP   A 1 105 ? 25.096 -8.617  -13.900 0.40 26.22 ?  105 ASP   A CB   1 
ATOM   2314 C CB   B ASP   A 1 105 ? 25.524 -8.847  -13.715 0.60 25.87 ?  105 ASP   A CB   1 
ATOM   2315 C CG   A ASP   A 1 105 ? 24.633 -10.032 -14.172 0.40 28.32 ?  105 ASP   A CG   1 
ATOM   2316 C CG   B ASP   A 1 105 ? 25.193 -10.302 -13.964 0.60 27.48 ?  105 ASP   A CG   1 
ATOM   2317 O OD1  A ASP   A 1 105 ? 23.407 -10.239 -14.291 0.40 28.74 ?  105 ASP   A OD1  1 
ATOM   2318 O OD1  B ASP   A 1 105 ? 23.998 -10.630 -14.108 0.60 27.53 ?  105 ASP   A OD1  1 
ATOM   2319 O OD2  A ASP   A 1 105 ? 25.489 -10.936 -14.271 0.40 29.68 -1 105 ASP   A OD2  1 
ATOM   2320 O OD2  B ASP   A 1 105 ? 26.141 -11.121 -14.013 0.60 28.43 -1 105 ASP   A OD2  1 
ATOM   2321 H H    A ASP   A 1 105 ? 25.299 -6.253  -13.621 0.40 27.74 ?  105 ASP   A H    1 
ATOM   2322 H H    B ASP   A 1 105 ? 25.562 -6.518  -13.149 0.60 28.68 ?  105 ASP   A H    1 
ATOM   2323 H HA   A ASP   A 1 105 ? 23.297 -7.741  -14.348 0.40 28.52 ?  105 ASP   A HA   1 
ATOM   2324 H HA   B ASP   A 1 105 ? 23.698 -8.057  -14.234 0.60 28.76 ?  105 ASP   A HA   1 
ATOM   2325 H HB2  A ASP   A 1 105 ? 25.583 -8.305  -14.683 0.40 31.46 ?  105 ASP   A HB2  1 
ATOM   2326 H HB2  B ASP   A 1 105 ? 25.998 -8.502  -14.489 0.60 31.05 ?  105 ASP   A HB2  1 
ATOM   2327 H HB3  A ASP   A 1 105 ? 25.695 -8.625  -13.131 0.40 31.46 ?  105 ASP   A HB3  1 
ATOM   2328 H HB3  B ASP   A 1 105 ? 26.094 -8.813  -12.934 0.60 31.05 ?  105 ASP   A HB3  1 
ATOM   2329 N N    A ILE   A 1 106 ? 21.940 -8.366  -12.417 0.40 20.96 ?  106 ILE   A N    1 
ATOM   2330 N N    B ILE   A 1 106 ? 22.287 -8.904  -12.414 0.60 22.54 ?  106 ILE   A N    1 
ATOM   2331 C CA   A ILE   A 1 106 ? 21.184 -8.789  -11.244 0.40 19.70 ?  106 ILE   A CA   1 
ATOM   2332 C CA   B ILE   A 1 106 ? 21.458 -9.321  -11.283 0.60 22.74 ?  106 ILE   A CA   1 
ATOM   2333 C C    A ILE   A 1 106 ? 21.717 -10.097 -10.681 0.40 18.50 ?  106 ILE   A C    1 
ATOM   2334 C C    B ILE   A 1 106 ? 22.044 -10.539 -10.585 0.60 22.10 ?  106 ILE   A C    1 
ATOM   2335 O O    A ILE   A 1 106 ? 21.524 -10.385 -9.495  0.40 17.78 ?  106 ILE   A O    1 
ATOM   2336 O O    B ILE   A 1 106 ? 21.821 -10.739 -9.384  0.60 21.76 ?  106 ILE   A O    1 
ATOM   2337 C CB   A ILE   A 1 106 ? 19.675 -8.880  -11.564 0.40 19.97 ?  106 ILE   A CB   1 
ATOM   2338 C CB   B ILE   A 1 106 ? 20.008 -9.570  -11.746 0.60 23.86 ?  106 ILE   A CB   1 
ATOM   2339 C CG1  A ILE   A 1 106 ? 18.855 -8.965  -10.276 0.40 20.18 ?  106 ILE   A CG1  1 
ATOM   2340 C CG1  B ILE   A 1 106 ? 19.060 -9.677  -10.549 0.60 24.21 ?  106 ILE   A CG1  1 
ATOM   2341 C CG2  A ILE   A 1 106 ? 19.383 -10.102 -12.420 0.40 20.19 ?  106 ILE   A CG2  1 
ATOM   2342 C CG2  B ILE   A 1 106 ? 19.924 -10.850 -12.547 0.60 24.24 ?  106 ILE   A CG2  1 
ATOM   2343 C CD1  A ILE   A 1 106 ? 19.088 -7.812  -9.327  0.40 20.09 ?  106 ILE   A CD1  1 
ATOM   2344 C CD1  B ILE   A 1 106 ? 18.964 -8.420  -9.723  0.60 24.44 ?  106 ILE   A CD1  1 
ATOM   2345 H H    A ILE   A 1 106 ? 21.485 -8.332  -13.142 0.40 25.15 ?  106 ILE   A H    1 
ATOM   2346 H H    B ILE   A 1 106 ? 21.903 -8.966  -13.176 0.60 27.04 ?  106 ILE   A H    1 
ATOM   2347 H HA   A ILE   A 1 106 ? 21.303 -8.118  -10.563 0.40 23.64 ?  106 ILE   A HA   1 
ATOM   2348 H HA   B ILE   A 1 106 ? 21.443 -8.606  -10.634 0.60 27.28 ?  106 ILE   A HA   1 
ATOM   2349 H HB   A ILE   A 1 106 ? 19.405 -8.086  -12.056 0.40 23.96 ?  106 ILE   A HB   1 
ATOM   2350 H HB   B ILE   A 1 106 ? 19.724 -8.831  -12.308 0.60 28.63 ?  106 ILE   A HB   1 
ATOM   2351 H HG12 A ILE   A 1 106 ? 17.912 -8.973  -10.505 0.40 24.21 ?  106 ILE   A HG12 1 
ATOM   2352 H HG12 B ILE   A 1 106 ? 18.170 -9.885  -10.875 0.60 29.05 ?  106 ILE   A HG12 1 
ATOM   2353 H HG13 A ILE   A 1 106 ? 19.086 -9.784  -9.812  0.40 24.21 ?  106 ILE   A HG13 1 
ATOM   2354 H HG13 B ILE   A 1 106 ? 19.369 -10.389 -9.969  0.60 29.05 ?  106 ILE   A HG13 1 
ATOM   2355 H HG21 A ILE   A 1 106 ? 18.506 -10.003 -12.822 0.40 24.22 ?  106 ILE   A HG21 1 
ATOM   2356 H HG21 B ILE   A 1 106 ? 19.063 -10.886 -12.987 0.60 29.09 ?  106 ILE   A HG21 1 
ATOM   2357 H HG22 A ILE   A 1 106 ? 20.059 -10.168 -13.111 0.40 24.22 ?  106 ILE   A HG22 1 
ATOM   2358 H HG22 B ILE   A 1 106 ? 20.637 -10.857 -13.203 0.60 29.09 ?  106 ILE   A HG22 1 
ATOM   2359 H HG23 A ILE   A 1 106 ? 19.403 -10.893 -11.859 0.40 24.22 ?  106 ILE   A HG23 1 
ATOM   2360 H HG23 B ILE   A 1 106 ? 20.018 -11.606 -11.945 0.60 29.09 ?  106 ILE   A HG23 1 
ATOM   2361 H HD11 A ILE   A 1 106 ? 18.341 -7.753  -8.715  0.40 24.11 ?  106 ILE   A HD11 1 
ATOM   2362 H HD11 B ILE   A 1 106 ? 18.187 -8.485  -9.149  0.60 29.32 ?  106 ILE   A HD11 1 
ATOM   2363 H HD12 A ILE   A 1 106 ? 19.909 -7.969  -8.833  0.40 24.11 ?  106 ILE   A HD12 1 
ATOM   2364 H HD12 B ILE   A 1 106 ? 19.767 -8.334  -9.187  0.60 29.32 ?  106 ILE   A HD12 1 
ATOM   2365 H HD13 A ILE   A 1 106 ? 19.162 -6.991  -9.840  0.40 24.11 ?  106 ILE   A HD13 1 
ATOM   2366 H HD13 B ILE   A 1 106 ? 18.876 -7.661  -10.319 0.60 29.32 ?  106 ILE   A HD13 1 
ATOM   2367 N N    A GLN   A 1 107 ? 22.385 -10.906 -11.509 0.40 19.20 ?  107 GLN   A N    1 
ATOM   2368 N N    B GLN   A 1 107 ? 22.797 -11.372 -11.312 0.60 22.54 ?  107 GLN   A N    1 
ATOM   2369 C CA   A GLN   A 1 107 ? 22.995 -12.135 -11.018 0.40 20.35 ?  107 GLN   A CA   1 
ATOM   2370 C CA   B GLN   A 1 107 ? 23.414 -12.543 -10.697 0.60 24.17 ?  107 GLN   A CA   1 
ATOM   2371 C C    A GLN   A 1 107 ? 23.991 -11.861 -9.903  0.40 18.19 ?  107 GLN   A C    1 
ATOM   2372 C C    B GLN   A 1 107 ? 24.337 -12.147 -9.554  0.60 21.00 ?  107 GLN   A C    1 
ATOM   2373 O O    A GLN   A 1 107 ? 24.259 -12.755 -9.093  0.40 19.54 ?  107 GLN   A O    1 
ATOM   2374 O O    B GLN   A 1 107 ? 24.566 -12.947 -8.640  0.60 21.04 ?  107 GLN   A O    1 
ATOM   2375 C CB   A GLN   A 1 107 ? 23.705 -12.870 -12.160 0.40 24.12 ?  107 GLN   A CB   1 
ATOM   2376 C CB   B GLN   A 1 107 ? 24.205 -13.337 -11.743 0.60 28.93 ?  107 GLN   A CB   1 
ATOM   2377 C CG   A GLN   A 1 107 ? 22.808 -13.236 -13.331 0.40 28.18 ?  107 GLN   A CG   1 
ATOM   2378 C CG   B GLN   A 1 107 ? 23.471 -13.550 -13.061 0.60 33.63 ?  107 GLN   A CG   1 
ATOM   2379 C CD   A GLN   A 1 107 ? 21.579 -14.009 -12.902 0.40 31.70 ?  107 GLN   A CD   1 
ATOM   2380 C CD   B GLN   A 1 107 ? 22.183 -14.330 -12.901 0.60 37.71 ?  107 GLN   A CD   1 
ATOM   2381 O OE1  A GLN   A 1 107 ? 21.677 -15.034 -12.228 0.40 32.97 ?  107 GLN   A OE1  1 
ATOM   2382 O OE1  B GLN   A 1 107 ? 22.076 -15.205 -12.041 0.60 39.04 ?  107 GLN   A OE1  1 
ATOM   2383 N NE2  A GLN   A 1 107 ? 20.410 -13.514 -13.284 0.40 32.64 ?  107 GLN   A NE2  1 
ATOM   2384 N NE2  B GLN   A 1 107 ? 21.194 -14.015 -13.733 0.60 38.89 ?  107 GLN   A NE2  1 
ATOM   2385 H H    A GLN   A 1 107 ? 22.491 -10.768 -12.349 0.40 23.04 ?  107 GLN   A H    1 
ATOM   2386 H H    B GLN   A 1 107 ? 22.973 -11.269 -12.148 0.60 27.04 ?  107 GLN   A H    1 
ATOM   2387 H HA   A GLN   A 1 107 ? 22.303 -12.723 -10.670 0.40 24.42 ?  107 GLN   A HA   1 
ATOM   2388 H HA   B GLN   A 1 107 ? 22.719 -13.125 -10.353 0.60 29.00 ?  107 GLN   A HA   1 
ATOM   2389 H HB2  A GLN   A 1 107 ? 24.414 -12.303 -12.501 0.40 28.94 ?  107 GLN   A HB2  1 
ATOM   2390 H HB2  B GLN   A 1 107 ? 25.030 -12.866 -11.939 0.60 34.72 ?  107 GLN   A HB2  1 
ATOM   2391 H HB3  A GLN   A 1 107 ? 24.084 -13.694 -11.815 0.40 28.94 ?  107 GLN   A HB3  1 
ATOM   2392 H HB3  B GLN   A 1 107 ? 24.410 -14.217 -11.382 0.60 34.72 ?  107 GLN   A HB3  1 
ATOM   2393 H HG2  A GLN   A 1 107 ? 22.514 -12.425 -13.772 0.40 33.81 ?  107 GLN   A HG2  1 
ATOM   2394 H HG2  B GLN   A 1 107 ? 23.255 -12.691 -13.454 0.60 40.35 ?  107 GLN   A HG2  1 
ATOM   2395 H HG3  A GLN   A 1 107 ? 23.311 -13.788 -13.954 0.40 33.81 ?  107 GLN   A HG3  1 
ATOM   2396 H HG3  B GLN   A 1 107 ? 24.048 -14.045 -13.660 0.60 40.35 ?  107 GLN   A HG3  1 
ATOM   2397 H HE21 A GLN   A 1 107 ? 20.382 -12.795 -13.752 0.40 39.16 ?  107 GLN   A HE21 1 
ATOM   2398 H HE21 B GLN   A 1 107 ? 21.305 -13.396 -14.321 0.60 46.66 ?  107 GLN   A HE21 1 
ATOM   2399 H HE22 A GLN   A 1 107 ? 19.685 -13.916 -13.064 0.40 39.16 ?  107 GLN   A HE22 1 
ATOM   2400 H HE22 B GLN   A 1 107 ? 20.442 -14.429 -13.685 0.60 46.66 ?  107 GLN   A HE22 1 
ATOM   2401 N N    A LEU   A 1 108 ? 24.540 -10.646 -9.839  0.40 14.66 ?  108 LEU   A N    1 
ATOM   2402 N N    B LEU   A 1 108 ? 24.859 -10.921 -9.579  0.60 17.72 ?  108 LEU   A N    1 
ATOM   2403 C CA   A LEU   A 1 108 ? 25.484 -10.306 -8.787  0.40 12.97 ?  108 LEU   A CA   1 
ATOM   2404 C CA   B LEU   A 1 108 ? 25.726 -10.451 -8.511  0.60 15.75 ?  108 LEU   A CA   1 
ATOM   2405 C C    A LEU   A 1 108 ? 24.822 -10.195 -7.420  0.40 11.61 ?  108 LEU   A C    1 
ATOM   2406 C C    B LEU   A 1 108 ? 24.977 -10.216 -7.209  0.60 14.06 ?  108 LEU   A C    1 
ATOM   2407 O O    A LEU   A 1 108 ? 25.533 -10.048 -6.422  0.40 11.60 ?  108 LEU   A O    1 
ATOM   2408 O O    B LEU   A 1 108 ? 25.622 -10.040 -6.172  0.60 14.51 ?  108 LEU   A O    1 
ATOM   2409 C CB   A LEU   A 1 108 ? 26.207 -9.007  -9.145  0.40 12.96 ?  108 LEU   A CB   1 
ATOM   2410 C CB   B LEU   A 1 108 ? 26.464 -9.189  -8.955  0.60 15.43 ?  108 LEU   A CB   1 
ATOM   2411 C CG   A LEU   A 1 108 ? 27.214 -9.148  -10.289 0.40 14.01 ?  108 LEU   A CG   1 
ATOM   2412 C CG   B LEU   A 1 108 ? 27.448 -9.430  -10.102 0.60 16.59 ?  108 LEU   A CG   1 
ATOM   2413 C CD1  A LEU   A 1 108 ? 27.588 -7.790  -10.860 0.40 14.31 ?  108 LEU   A CD1  1 
ATOM   2414 C CD1  B LEU   A 1 108 ? 28.067 -8.122  -10.567 0.60 16.82 ?  108 LEU   A CD1  1 
ATOM   2415 C CD2  A LEU   A 1 108 ? 28.461 -9.886  -9.817  0.40 14.83 ?  108 LEU   A CD2  1 
ATOM   2416 C CD2  B LEU   A 1 108 ? 28.532 -10.416 -9.685  0.60 17.88 ?  108 LEU   A CD2  1 
ATOM   2417 H H    A LEU   A 1 108 ? 24.377 -10.018 -10.399 0.40 17.58 ?  108 LEU   A H    1 
ATOM   2418 H H    B LEU   A 1 108 ? 24.726 -10.358 -10.208 0.60 21.26 ?  108 LEU   A H    1 
ATOM   2419 H HA   A LEU   A 1 108 ? 26.141 -11.012 -8.735  0.40 15.56 ?  108 LEU   A HA   1 
ATOM   2420 H HA   B LEU   A 1 108 ? 26.384 -11.136 -8.333  0.60 18.89 ?  108 LEU   A HA   1 
ATOM   2421 H HB2  A LEU   A 1 108 ? 25.546 -8.348  -9.413  0.40 15.55 ?  108 LEU   A HB2  1 
ATOM   2422 H HB2  B LEU   A 1 108 ? 25.813 -8.535  -9.252  0.60 18.51 ?  108 LEU   A HB2  1 
ATOM   2423 H HB3  A LEU   A 1 108 ? 26.683 -8.699  -8.364  0.40 15.55 ?  108 LEU   A HB3  1 
ATOM   2424 H HB3  B LEU   A 1 108 ? 26.963 -8.841  -8.202  0.60 18.51 ?  108 LEU   A HB3  1 
ATOM   2425 H HG   A LEU   A 1 108 ? 26.812 -9.670  -11.001 0.40 16.81 ?  108 LEU   A HG   1 
ATOM   2426 H HG   B LEU   A 1 108 ? 26.966 -9.814  -10.852 0.60 19.91 ?  108 LEU   A HG   1 
ATOM   2427 H HD11 A LEU   A 1 108 ? 28.163 -7.920  -11.632 0.40 17.17 ?  108 LEU   A HD11 1 
ATOM   2428 H HD11 B LEU   A 1 108 ? 28.676 -8.305  -11.300 0.60 20.19 ?  108 LEU   A HD11 1 
ATOM   2429 H HD12 A LEU   A 1 108 ? 26.780 -7.325  -11.125 0.40 17.17 ?  108 LEU   A HD12 1 
ATOM   2430 H HD12 B LEU   A 1 108 ? 27.362 -7.526  -10.864 0.60 20.19 ?  108 LEU   A HD12 1 
ATOM   2431 H HD13 A LEU   A 1 108 ? 28.057 -7.280  -10.182 0.40 17.17 ?  108 LEU   A HD13 1 
ATOM   2432 H HD13 B LEU   A 1 108 ? 28.550 -7.721  -9.827  0.60 20.19 ?  108 LEU   A HD13 1 
ATOM   2433 H HD21 A LEU   A 1 108 ? 29.117 -9.886  -10.531 0.40 17.80 ?  108 LEU   A HD21 1 
ATOM   2434 H HD21 B LEU   A 1 108 ? 29.263 -10.364 -10.317 0.60 21.45 ?  108 LEU   A HD21 1 
ATOM   2435 H HD22 A LEU   A 1 108 ? 28.818 -9.436  -9.037  0.40 17.80 ?  108 LEU   A HD22 1 
ATOM   2436 H HD22 B LEU   A 1 108 ? 28.843 -10.182 -8.796  0.60 21.45 ?  108 LEU   A HD22 1 
ATOM   2437 H HD23 A LEU   A 1 108 ? 28.221 -10.800 -9.590  0.40 17.80 ?  108 LEU   A HD23 1 
ATOM   2438 H HD23 B LEU   A 1 108 ? 28.159 -11.311 -9.679  0.60 21.45 ?  108 LEU   A HD23 1 
ATOM   2439 N N    A LEU   A 1 109 ? 23.491 -10.292 -7.346  0.40 11.52 ?  109 LEU   A N    1 
ATOM   2440 N N    B LEU   A 1 109 ? 23.642 -10.237 -7.225  0.60 13.22 ?  109 LEU   A N    1 
ATOM   2441 C CA   A LEU   A 1 109 ? 22.812 -10.157 -6.062  0.40 11.66 ?  109 LEU   A CA   1 
ATOM   2442 C CA   B LEU   A 1 109 ? 22.903 -10.117 -5.976  0.60 12.52 ?  109 LEU   A CA   1 
ATOM   2443 C C    A LEU   A 1 109 ? 23.212 -11.272 -5.100  0.40 11.54 ?  109 LEU   A C    1 
ATOM   2444 C C    B LEU   A 1 109 ? 23.197 -11.291 -5.052  0.60 11.71 ?  109 LEU   A C    1 
ATOM   2445 O O    A LEU   A 1 109 ? 23.399 -11.032 -3.901  0.40 11.84 ?  109 LEU   A O    1 
ATOM   2446 O O    B LEU   A 1 109 ? 23.291 -11.118 -3.831  0.60 11.84 ?  109 LEU   A O    1 
ATOM   2447 C CB   A LEU   A 1 109 ? 21.299 -10.134 -6.286  0.40 12.35 ?  109 LEU   A CB   1 
ATOM   2448 C CB   B LEU   A 1 109 ? 21.404 -9.982  -6.253  0.60 12.93 ?  109 LEU   A CB   1 
ATOM   2449 C CG   A LEU   A 1 109 ? 20.410 -9.843  -5.081  0.40 12.52 ?  109 LEU   A CG   1 
ATOM   2450 C CG   B LEU   A 1 109 ? 20.508 -9.716  -5.039  0.60 12.91 ?  109 LEU   A CG   1 
ATOM   2451 C CD1  A LEU   A 1 109 ? 20.767 -8.501  -4.460  0.40 12.52 ?  109 LEU   A CD1  1 
ATOM   2452 C CD1  B LEU   A 1 109 ? 21.016 -8.526  -4.232  0.60 12.68 ?  109 LEU   A CD1  1 
ATOM   2453 C CD2  A LEU   A 1 109 ? 18.947 -9.869  -5.501  0.40 13.00 ?  109 LEU   A CD2  1 
ATOM   2454 C CD2  B LEU   A 1 109 ? 19.055 -9.484  -5.465  0.60 13.30 ?  109 LEU   A CD2  1 
ATOM   2455 H H    A LEU   A 1 109 ? 22.959 -10.437 -8.013  0.40 13.82 ?  109 LEU   A H    1 
ATOM   2456 H H    B LEU   A 1 109 ? 23.153 -10.316 -7.925  0.60 15.87 ?  109 LEU   A H    1 
ATOM   2457 H HA   A LEU   A 1 109 ? 23.067 -9.314  -5.661  0.40 13.98 ?  109 LEU   A HA   1 
ATOM   2458 H HA   B LEU   A 1 109 ? 23.192 -9.310  -5.524  0.60 15.02 ?  109 LEU   A HA   1 
ATOM   2459 H HB2  A LEU   A 1 109 ? 21.105 -9.450  -6.948  0.40 14.82 ?  109 LEU   A HB2  1 
ATOM   2460 H HB2  B LEU   A 1 109 ? 21.272 -9.245  -6.871  0.60 15.52 ?  109 LEU   A HB2  1 
ATOM   2461 H HB3  A LEU   A 1 109 ? 21.029 -10.997 -6.631  0.40 14.82 ?  109 LEU   A HB3  1 
ATOM   2462 H HB3  B LEU   A 1 109 ? 21.091 -10.803 -6.662  0.60 15.52 ?  109 LEU   A HB3  1 
ATOM   2463 H HG   A LEU   A 1 109 ? 20.542 -10.530 -4.411  0.40 15.02 ?  109 LEU   A HG   1 
ATOM   2464 H HG   B LEU   A 1 109 ? 20.522 -10.491 -4.460  0.60 15.49 ?  109 LEU   A HG   1 
ATOM   2465 H HD11 A LEU   A 1 109 ? 20.112 -8.281  -3.779  0.40 15.02 ?  109 LEU   A HD11 1 
ATOM   2466 H HD11 B LEU   A 1 109 ? 20.342 -8.270  -3.582  0.60 15.21 ?  109 LEU   A HD11 1 
ATOM   2467 H HD12 A LEU   A 1 109 ? 21.649 -8.560  -4.061  0.40 15.02 ?  109 LEU   A HD12 1 
ATOM   2468 H HD12 B LEU   A 1 109 ? 21.834 -8.777  -3.777  0.60 15.21 ?  109 LEU   A HD12 1 
ATOM   2469 H HD13 A LEU   A 1 109 ? 20.762 -7.820  -5.153  0.40 15.02 ?  109 LEU   A HD13 1 
ATOM   2470 H HD13 B LEU   A 1 109 ? 21.186 -7.783  -4.836  0.60 15.21 ?  109 LEU   A HD13 1 
ATOM   2471 H HD21 A LEU   A 1 109 ? 18.413 -9.423  -4.824  0.40 15.60 ?  109 LEU   A HD21 1 
ATOM   2472 H HD21 B LEU   A 1 109 ? 18.521 -9.269  -4.681  0.60 15.96 ?  109 LEU   A HD21 1 
ATOM   2473 H HD22 A LEU   A 1 109 ? 18.852 -9.405  -6.349  0.40 15.60 ?  109 LEU   A HD22 1 
ATOM   2474 H HD22 B LEU   A 1 109 ? 19.019 -8.749  -6.097  0.60 15.96 ?  109 LEU   A HD22 1 
ATOM   2475 H HD23 A LEU   A 1 109 ? 18.659 -10.790 -5.597  0.40 15.60 ?  109 LEU   A HD23 1 
ATOM   2476 H HD23 B LEU   A 1 109 ? 18.712 -10.292 -5.881  0.60 15.96 ?  109 LEU   A HD23 1 
ATOM   2477 N N    . LYS   A 1 110 ? 23.352 -12.497 -5.606  1.00 11.54 ?  110 LYS   A N    1 
ATOM   2478 C CA   . LYS   A 1 110 ? 23.726 -13.620 -4.752  1.00 11.77 ?  110 LYS   A CA   1 
ATOM   2479 C C    . LYS   A 1 110 ? 25.105 -13.399 -4.141  1.00 11.11 ?  110 LYS   A C    1 
ATOM   2480 O O    . LYS   A 1 110 ? 25.298 -13.594 -2.938  1.00 11.27 ?  110 LYS   A O    1 
ATOM   2481 C CB   . LYS   A 1 110 ? 23.648 -14.940 -5.521  1.00 12.50 ?  110 LYS   A CB   1 
ATOM   2482 C CG   . LYS   A 1 110 ? 23.866 -16.153 -4.618  1.00 12.80 ?  110 LYS   A CG   1 
ATOM   2483 C CD   . LYS   A 1 110 ? 23.615 -17.476 -5.321  1.00 13.49 ?  110 LYS   A CD   1 
ATOM   2484 C CE   . LYS   A 1 110 ? 23.727 -18.650 -4.362  1.00 14.29 ?  110 LYS   A CE   1 
ATOM   2485 N NZ   . LYS   A 1 110 ? 22.540 -18.763 -3.479  1.00 14.82 ?  110 LYS   A NZ   1 
ATOM   2486 H H    A LYS   A 1 110 ? 23.229 -12.701 -6.430  0.40 13.85 ?  110 LYS   A H    1 
ATOM   2487 H H    B LYS   A 1 110 ? 23.237 -12.684 -6.435  0.60 13.85 ?  110 LYS   A H    1 
ATOM   2488 H HA   . LYS   A 1 110 ? 23.090 -13.678 -4.020  1.00 14.12 ?  110 LYS   A HA   1 
ATOM   2489 H HB2  . LYS   A 1 110 ? 22.768 -15.023 -5.924  1.00 15.00 ?  110 LYS   A HB2  1 
ATOM   2490 H HB3  . LYS   A 1 110 ? 24.330 -14.950 -6.208  1.00 15.00 ?  110 LYS   A HB3  1 
ATOM   2491 H HG2  . LYS   A 1 110 ? 24.785 -16.151 -4.304  1.00 15.36 ?  110 LYS   A HG2  1 
ATOM   2492 H HG3  . LYS   A 1 110 ? 23.261 -16.098 -3.863  1.00 15.36 ?  110 LYS   A HG3  1 
ATOM   2493 H HD2  . LYS   A 1 110 ? 22.725 -17.477 -5.696  1.00 16.18 ?  110 LYS   A HD2  1 
ATOM   2494 H HD3  . LYS   A 1 110 ? 24.278 -17.596 -6.021  1.00 16.18 ?  110 LYS   A HD3  1 
ATOM   2495 H HE2  . LYS   A 1 110 ? 23.807 -19.472 -4.870  1.00 17.14 ?  110 LYS   A HE2  1 
ATOM   2496 H HE3  . LYS   A 1 110 ? 24.512 -18.530 -3.799  1.00 17.14 ?  110 LYS   A HE3  1 
ATOM   2497 H HZ1  . LYS   A 1 110 ? 22.628 -19.453 -2.930  1.00 17.78 ?  110 LYS   A HZ1  1 
ATOM   2498 H HZ2  . LYS   A 1 110 ? 22.447 -18.017 -2.997  1.00 17.78 ?  110 LYS   A HZ2  1 
ATOM   2499 H HZ3  . LYS   A 1 110 ? 21.805 -18.875 -3.973  1.00 17.78 ?  110 LYS   A HZ3  1 
ATOM   2500 N N    . SER   A 1 111 ? 26.066 -12.955 -4.954  1.00 11.23 ?  111 SER   A N    1 
ATOM   2501 C CA   . SER   A 1 111 ? 27.395 -12.647 -4.436  1.00 11.23 ?  111 SER   A CA   1 
ATOM   2502 C C    . SER   A 1 111 ? 27.326 -11.598 -3.332  1.00 10.59 ?  111 SER   A C    1 
ATOM   2503 O O    . SER   A 1 111 ? 28.014 -11.703 -2.311  1.00 11.29 ?  111 SER   A O    1 
ATOM   2504 C CB   . SER   A 1 111 ? 28.290 -12.160 -5.576  1.00 12.81 ?  111 SER   A CB   1 
ATOM   2505 O OG   . SER   A 1 111 ? 28.376 -13.150 -6.588  1.00 14.91 ?  111 SER   A OG   1 
ATOM   2506 H H    . SER   A 1 111 ? 25.971 -12.823 -5.798  1.00 13.48 ?  111 SER   A H    1 
ATOM   2507 H HA   . SER   A 1 111 ? 27.789 -13.454 -4.067  1.00 13.48 ?  111 SER   A HA   1 
ATOM   2508 H HB2  . SER   A 1 111 ? 27.906 -11.354 -5.956  1.00 15.37 ?  111 SER   A HB2  1 
ATOM   2509 H HB3  . SER   A 1 111 ? 29.175 -11.979 -5.231  1.00 15.37 ?  111 SER   A HB3  1 
ATOM   2510 H HG   . SER   A 1 111 ? 28.872 -12.874 -7.215  1.00 17.88 ?  111 SER   A HG   1 
ATOM   2511 N N    . ALA   A 1 112 ? 26.478 -10.584 -3.511  1.00 10.89 ?  112 ALA   A N    1 
ATOM   2512 C CA   . ALA   A 1 112 ? 26.333 -9.548  -2.492  1.00 10.86 ?  112 ALA   A CA   1 
ATOM   2513 C C    . ALA   A 1 112 ? 25.853 -10.145 -1.171  1.00 10.57 ?  112 ALA   A C    1 
ATOM   2514 O O    . ALA   A 1 112 ? 26.398 -9.850  -0.101  1.00 10.94 ?  112 ALA   A O    1 
ATOM   2515 C CB   . ALA   A 1 112 ? 25.370 -8.463  -2.987  1.00 11.40 ?  112 ALA   A CB   1 
ATOM   2516 H H    . ALA   A 1 112 ? 25.991 -10.469 -4.207  1.00 13.07 ?  112 ALA   A H    1 
ATOM   2517 H HA   . ALA   A 1 112 ? 27.195 -9.127  -2.338  1.00 13.03 ?  112 ALA   A HA   1 
ATOM   2518 H HB1  . ALA   A 1 112 ? 25.293 -7.769  -2.303  1.00 13.67 ?  112 ALA   A HB1  1 
ATOM   2519 H HB2  . ALA   A 1 112 ? 25.724 -8.067  -3.803  1.00 13.67 ?  112 ALA   A HB2  1 
ATOM   2520 H HB3  . ALA   A 1 112 ? 24.503 -8.852  -3.156  1.00 13.67 ?  112 ALA   A HB3  1 
ATOM   2521 N N    . TYR   A 1 113 ? 24.815 -10.982 -1.222  1.00 10.81 ?  113 TYR   A N    1 
ATOM   2522 C CA   . TYR   A 1 113 ? 24.307 -11.592 0.004   1.00 10.54 ?  113 TYR   A CA   1 
ATOM   2523 C C    . TYR   A 1 113 ? 25.308 -12.547 0.647   1.00 10.35 ?  113 TYR   A C    1 
ATOM   2524 O O    . TYR   A 1 113 ? 25.271 -12.728 1.867   1.00 10.99 ?  113 TYR   A O    1 
ATOM   2525 C CB   . TYR   A 1 113 ? 22.988 -12.315 -0.266  1.00 10.90 ?  113 TYR   A CB   1 
ATOM   2526 C CG   . TYR   A 1 113 ? 21.771 -11.411 -0.200  1.00 10.89 ?  113 TYR   A CG   1 
ATOM   2527 C CD1  . TYR   A 1 113 ? 21.397 -10.802 0.993   1.00 11.06 ?  113 TYR   A CD1  1 
ATOM   2528 C CD2  . TYR   A 1 113 ? 20.973 -11.199 -1.318  1.00 11.33 ?  113 TYR   A CD2  1 
ATOM   2529 C CE1  . TYR   A 1 113 ? 20.271 -10.003 1.069   1.00 11.46 ?  113 TYR   A CE1  1 
ATOM   2530 C CE2  . TYR   A 1 113 ? 19.828 -10.398 -1.247  1.00 11.36 ?  113 TYR   A CE2  1 
ATOM   2531 C CZ   . TYR   A 1 113 ? 19.492 -9.806  -0.050  1.00 11.50 ?  113 TYR   A CZ   1 
ATOM   2532 O OH   . TYR   A 1 113 ? 18.368 -9.013  0.062   1.00 12.04 ?  113 TYR   A OH   1 
ATOM   2533 H H    . TYR   A 1 113 ? 24.400 -11.204 -1.941  1.00 12.97 ?  113 TYR   A H    1 
ATOM   2534 H HA   . TYR   A 1 113 ? 24.130 -10.885 0.642   1.00 12.65 ?  113 TYR   A HA   1 
ATOM   2535 H HB2  . TYR   A 1 113 ? 23.016 -12.698 -1.158  1.00 13.08 ?  113 TYR   A HB2  1 
ATOM   2536 H HB3  . TYR   A 1 113 ? 22.873 -13.013 0.391   1.00 13.08 ?  113 TYR   A HB3  1 
ATOM   2537 H HD1  . TYR   A 1 113 ? 21.917 -10.945 1.752   1.00 13.27 ?  113 TYR   A HD1  1 
ATOM   2538 H HD2  . TYR   A 1 113 ? 21.192 -11.606 -2.126  1.00 13.60 ?  113 TYR   A HD2  1 
ATOM   2539 H HE1  . TYR   A 1 113 ? 20.040 -9.607  1.878   1.00 13.75 ?  113 TYR   A HE1  1 
ATOM   2540 H HE2  . TYR   A 1 113 ? 19.296 -10.255 -2.000  1.00 13.63 ?  113 TYR   A HE2  1 
ATOM   2541 H HH   . TYR   A 1 113 ? 17.960 -8.999  -0.679  1.00 14.44 ?  113 TYR   A HH   1 
ATOM   2542 N N    . GLU   A 1 114 ? 26.205 -13.159 -0.138  1.00 10.55 ?  114 GLU   A N    1 
ATOM   2543 C CA   . GLU   A 1 114 ? 27.192 -14.061 0.457   1.00 10.94 ?  114 GLU   A CA   1 
ATOM   2544 C C    . GLU   A 1 114 ? 28.052 -13.353 1.498   1.00 10.88 ?  114 GLU   A C    1 
ATOM   2545 O O    . GLU   A 1 114 ? 28.533 -13.984 2.446   1.00 10.97 ?  114 GLU   A O    1 
ATOM   2546 C CB   . GLU   A 1 114 ? 28.060 -14.700 -0.635  1.00 11.16 ?  114 GLU   A CB   1 
ATOM   2547 C CG   . GLU   A 1 114 ? 27.297 -15.756 -1.419  1.00 11.77 ?  114 GLU   A CG   1 
ATOM   2548 C CD   . GLU   A 1 114 ? 28.013 -16.289 -2.656  1.00 11.74 ?  114 GLU   A CD   1 
ATOM   2549 O OE1  . GLU   A 1 114 ? 28.969 -15.659 -3.151  1.00 12.15 ?  114 GLU   A OE1  1 
ATOM   2550 O OE2  . GLU   A 1 114 ? 27.577 -17.348 -3.152  1.00 13.16 -1 114 GLU   A OE2  1 
ATOM   2551 H H    . GLU   A 1 114 ? 26.265 -13.063 -0.996  1.00 12.66 ?  114 GLU   A H    1 
ATOM   2552 H HA   . GLU   A 1 114 ? 26.723 -14.770 0.906   1.00 13.13 ?  114 GLU   A HA   1 
ATOM   2553 H HB2  . GLU   A 1 114 ? 28.352 -14.014 -1.262  1.00 13.39 ?  114 GLU   A HB2  1 
ATOM   2554 H HB3  . GLU   A 1 114 ? 28.830 -15.124 -0.227  1.00 13.39 ?  114 GLU   A HB3  1 
ATOM   2555 H HG2  . GLU   A 1 114 ? 27.127 -16.510 -0.832  1.00 14.12 ?  114 GLU   A HG2  1 
ATOM   2556 H HG3  . GLU   A 1 114 ? 26.453 -15.376 -1.710  1.00 14.12 ?  114 GLU   A HG3  1 
ATOM   2557 N N    . ASN   A 1 115 ? 28.243 -12.039 1.358   1.00 10.58 ?  115 ASN   A N    1 
ATOM   2558 C CA   . ASN   A 1 115 ? 29.017 -11.312 2.359   1.00 10.88 ?  115 ASN   A CA   1 
ATOM   2559 C C    . ASN   A 1 115 ? 28.406 -11.437 3.749   1.00 10.69 ?  115 ASN   A C    1 
ATOM   2560 O O    . ASN   A 1 115 ? 29.128 -11.365 4.753   1.00 11.10 ?  115 ASN   A O    1 
ATOM   2561 C CB   . ASN   A 1 115 ? 29.130 -9.835  1.976   1.00 11.14 ?  115 ASN   A CB   1 
ATOM   2562 C CG   . ASN   A 1 115 ? 29.912 -9.629  0.704   1.00 11.86 ?  115 ASN   A CG   1 
ATOM   2563 O OD1  . ASN   A 1 115 ? 31.129 -9.773  0.695   1.00 15.43 ?  115 ASN   A OD1  1 
ATOM   2564 N ND2  . ASN   A 1 115 ? 29.225 -9.302  -0.378  1.00 11.47 ?  115 ASN   A ND2  1 
ATOM   2565 H H    . ASN   A 1 115 ? 27.942 -11.547 0.714   1.00 12.69 ?  115 ASN   A H    1 
ATOM   2566 H HA   . ASN   A 1 115 ? 29.912 -11.679 2.397   1.00 13.05 ?  115 ASN   A HA   1 
ATOM   2567 H HB2  . ASN   A 1 115 ? 28.240 -9.471  1.855   1.00 13.37 ?  115 ASN   A HB2  1 
ATOM   2568 H HB3  . ASN   A 1 115 ? 29.586 -9.358  2.692   1.00 13.37 ?  115 ASN   A HB3  1 
ATOM   2569 H HD21 . ASN   A 1 115 ? 29.631 -9.177  -1.121  1.00 13.76 ?  115 ASN   A HD21 1 
ATOM   2570 H HD22 . ASN   A 1 115 ? 28.366 -9.235  -0.337  1.00 13.76 ?  115 ASN   A HD22 1 
ATOM   2571 N N    . PHE   A 1 116 ? 27.080 -11.605 3.833   1.00 10.76 ?  116 PHE   A N    1 
ATOM   2572 C CA   . PHE   A 1 116 ? 26.432 -11.691 5.138   1.00 10.51 ?  116 PHE   A CA   1 
ATOM   2573 C C    . PHE   A 1 116 ? 26.905 -12.919 5.913   1.00 10.87 ?  116 PHE   A C    1 
ATOM   2574 O O    . PHE   A 1 116 ? 26.836 -12.935 7.144   1.00 11.58 ?  116 PHE   A O    1 
ATOM   2575 C CB   . PHE   A 1 116 ? 24.906 -11.818 5.003   1.00 10.78 ?  116 PHE   A CB   1 
ATOM   2576 C CG   . PHE   A 1 116 ? 24.149 -10.575 4.531   1.00 10.53 ?  116 PHE   A CG   1 
ATOM   2577 C CD1  . PHE   A 1 116 ? 24.720 -9.558  3.773   1.00 10.76 ?  116 PHE   A CD1  1 
ATOM   2578 C CD2  . PHE   A 1 116 ? 22.803 -10.472 4.849   1.00 11.19 ?  116 PHE   A CD2  1 
ATOM   2579 C CE1  . PHE   A 1 116 ? 23.952 -8.482  3.352   1.00 10.99 ?  116 PHE   A CE1  1 
ATOM   2580 C CE2  . PHE   A 1 116 ? 22.035 -9.404  4.438   1.00 11.39 ?  116 PHE   A CE2  1 
ATOM   2581 C CZ   . PHE   A 1 116 ? 22.598 -8.409  3.683   1.00 10.85 ?  116 PHE   A CZ   1 
ATOM   2582 H H    . PHE   A 1 116 ? 26.544 -11.664 3.158   1.00 12.91 ?  116 PHE   A H    1 
ATOM   2583 H HA   . PHE   A 1 116 ? 26.629 -10.898 5.658   1.00 12.61 ?  116 PHE   A HA   1 
ATOM   2584 H HB2  . PHE   A 1 116 ? 24.714 -12.531 4.372   1.00 12.93 ?  116 PHE   A HB2  1 
ATOM   2585 H HB3  . PHE   A 1 116 ? 24.545 -12.060 5.872   1.00 12.93 ?  116 PHE   A HB3  1 
ATOM   2586 H HD1  . PHE   A 1 116 ? 25.614 -9.614  3.537   1.00 12.91 ?  116 PHE   A HD1  1 
ATOM   2587 H HD2  . PHE   A 1 116 ? 22.404 -11.155 5.347   1.00 13.43 ?  116 PHE   A HD2  1 
ATOM   2588 H HE1  . PHE   A 1 116 ? 24.344 -7.806  2.850   1.00 13.19 ?  116 PHE   A HE1  1 
ATOM   2589 H HE2  . PHE   A 1 116 ? 21.136 -9.370  4.673   1.00 13.66 ?  116 PHE   A HE2  1 
ATOM   2590 H HZ   . PHE   A 1 116 ? 22.089 -7.678  3.419   1.00 13.02 ?  116 PHE   A HZ   1 
ATOM   2591 N N    . ASN   A 1 117 ? 27.349 -13.968 5.211   1.00 11.17 ?  117 ASN   A N    1 
ATOM   2592 C CA   . ASN   A 1 117 ? 27.716 -15.215 5.877   1.00 11.63 ?  117 ASN   A CA   1 
ATOM   2593 C C    . ASN   A 1 117 ? 28.978 -15.096 6.710   1.00 11.99 ?  117 ASN   A C    1 
ATOM   2594 O O    . ASN   A 1 117 ? 29.271 -16.011 7.486   1.00 12.95 ?  117 ASN   A O    1 
ATOM   2595 C CB   . ASN   A 1 117 ? 27.826 -16.347 4.860   1.00 11.81 ?  117 ASN   A CB   1 
ATOM   2596 C CG   . ASN   A 1 117 ? 26.473 -16.731 4.326   1.00 11.78 ?  117 ASN   A CG   1 
ATOM   2597 O OD1  . ASN   A 1 117 ? 25.502 -16.752 5.077   1.00 12.71 ?  117 ASN   A OD1  1 
ATOM   2598 N ND2  . ASN   A 1 117 ? 26.383 -16.990 3.036   1.00 11.64 ?  117 ASN   A ND2  1 
ATOM   2599 H H    . ASN   A 1 117 ? 27.426 -13.987 4.350   1.00 13.40 ?  117 ASN   A H    1 
ATOM   2600 H HA   . ASN   A 1 117 ? 26.992 -15.447 6.482   1.00 13.95 ?  117 ASN   A HA   1 
ATOM   2601 H HB2  . ASN   A 1 117 ? 28.374 -16.057 4.115   1.00 14.17 ?  117 ASN   A HB2  1 
ATOM   2602 H HB3  . ASN   A 1 117 ? 28.212 -17.122 5.287   1.00 14.17 ?  117 ASN   A HB3  1 
ATOM   2603 H HD21 . ASN   A 1 117 ? 25.625 -17.209 2.700   1.00 13.97 ?  117 ASN   A HD21 1 
ATOM   2604 H HD22 . ASN   A 1 117 ? 27.085 -16.956 2.545   1.00 13.97 ?  117 ASN   A HD22 1 
ATOM   2605 N N    . GLN   A 1 118 ? 29.708 -13.991 6.587   1.00 11.77 ?  118 GLN   A N    1 
ATOM   2606 C CA   . GLN   A 1 118 ? 30.885 -13.758 7.407   1.00 12.31 ?  118 GLN   A CA   1 
ATOM   2607 C C    . GLN   A 1 118 ? 30.544 -13.185 8.777   1.00 12.37 ?  118 GLN   A C    1 
ATOM   2608 O O    . GLN   A 1 118 ? 31.461 -12.895 9.556   1.00 13.97 ?  118 GLN   A O    1 
ATOM   2609 C CB   . GLN   A 1 118 ? 31.883 -12.857 6.667   1.00 12.54 ?  118 GLN   A CB   1 
ATOM   2610 C CG   . GLN   A 1 118 ? 32.352 -13.435 5.349   1.00 12.54 ?  118 GLN   A CG   1 
ATOM   2611 C CD   . GLN   A 1 118 ? 33.181 -14.694 5.525   1.00 13.17 ?  118 GLN   A CD   1 
ATOM   2612 O OE1  . GLN   A 1 118 ? 34.046 -14.762 6.409   1.00 13.91 ?  118 GLN   A OE1  1 
ATOM   2613 N NE2  . GLN   A 1 118 ? 32.924 -15.699 4.681   1.00 13.42 ?  118 GLN   A NE2  1 
ATOM   2614 H H    . GLN   A 1 118 ? 29.531 -13.346 6.036   1.00 14.13 ?  118 GLN   A H    1 
ATOM   2615 H HA   . GLN   A 1 118 ? 31.317 -14.612 7.554   1.00 14.78 ?  118 GLN   A HA   1 
ATOM   2616 H HB2  . GLN   A 1 118 ? 31.462 -12.004 6.487   1.00 15.05 ?  118 GLN   A HB2  1 
ATOM   2617 H HB3  . GLN   A 1 118 ? 32.662 -12.730 7.232   1.00 15.05 ?  118 GLN   A HB3  1 
ATOM   2618 H HG2  . GLN   A 1 118 ? 31.583 -13.654 4.801   1.00 15.05 ?  118 GLN   A HG2  1 
ATOM   2619 H HG3  . GLN   A 1 118 ? 32.906 -12.780 4.893   1.00 15.05 ?  118 GLN   A HG3  1 
ATOM   2620 H HE21 . GLN   A 1 118 ? 32.311 -15.609 4.074   1.00 16.10 ?  118 GLN   A HE21 1 
ATOM   2621 H HE22 . GLN   A 1 118 ? 33.361 -16.436 4.731   1.00 16.10 ?  118 GLN   A HE22 1 
ATOM   2622 N N    . HIS   A 1 119 ? 29.257 -13.030 9.092   1.00 12.17 ?  119 HIS   A N    1 
ATOM   2623 C CA   . HIS   A 1 119 ? 28.806 -12.419 10.336  1.00 12.56 ?  119 HIS   A CA   1 
ATOM   2624 C C    . HIS   A 1 119 ? 27.672 -13.241 10.921  1.00 12.84 ?  119 HIS   A C    1 
ATOM   2625 O O    . HIS   A 1 119 ? 26.717 -13.570 10.216  1.00 13.32 ?  119 HIS   A O    1 
ATOM   2626 C CB   . HIS   A 1 119 ? 28.345 -10.989 10.051  1.00 12.89 ?  119 HIS   A CB   1 
ATOM   2627 C CG   . HIS   A 1 119 ? 29.427 -10.180 9.428   1.00 14.20 ?  119 HIS   A CG   1 
ATOM   2628 N ND1  . HIS   A 1 119 ? 30.415 -9.583  10.176  1.00 16.52 ?  119 HIS   A ND1  1 
ATOM   2629 C CD2  . HIS   A 1 119 ? 29.756 -9.980  8.132   1.00 15.20 ?  119 HIS   A CD2  1 
ATOM   2630 C CE1  . HIS   A 1 119 ? 31.281 -9.004  9.365   1.00 16.73 ?  119 HIS   A CE1  1 
ATOM   2631 N NE2  . HIS   A 1 119 ? 30.914 -9.240  8.119   1.00 16.40 ?  119 HIS   A NE2  1 
ATOM   2632 H H    . HIS   A 1 119 ? 28.607 -13.290 8.588   1.00 14.60 ?  119 HIS   A H    1 
ATOM   2633 H HA   . HIS   A 1 119 ? 29.536 -12.394 10.973  1.00 15.07 ?  119 HIS   A HA   1 
ATOM   2634 H HB2  . HIS   A 1 119 ? 27.590 -11.015 9.442   1.00 15.46 ?  119 HIS   A HB2  1 
ATOM   2635 H HB3  . HIS   A 1 119 ? 28.089 -10.568 10.886  1.00 15.46 ?  119 HIS   A HB3  1 
ATOM   2636 H HD1  . HIS   A 1 119 ? 30.451 -9.577  11.034  1.00 19.82 ?  119 HIS   A HD1  1 
ATOM   2637 H HD2  . HIS   A 1 119 ? 29.285 -10.286 7.388   1.00 18.24 ?  119 HIS   A HD2  1 
ATOM   2638 H HE1  . HIS   A 1 119 ? 32.022 -8.509  9.626   1.00 20.08 ?  119 HIS   A HE1  1 
ATOM   2639 N N    . GLU   A 1 120 ? 27.767 -13.553 12.213  1.00 13.65 ?  120 GLU   A N    1 
ATOM   2640 C CA   . GLU   A 1 120 ? 26.806 -14.475 12.817  1.00 16.58 ?  120 GLU   A CA   1 
ATOM   2641 C C    . GLU   A 1 120 ? 25.391 -13.904 12.877  1.00 14.75 ?  120 GLU   A C    1 
ATOM   2642 O O    . GLU   A 1 120 ? 24.414 -14.665 12.772  1.00 15.02 ?  120 GLU   A O    1 
ATOM   2643 C CB   . GLU   A 1 120 ? 27.274 -14.880 14.217  1.00 22.93 ?  120 GLU   A CB   1 
ATOM   2644 C CG   . GLU   A 1 120 ? 28.476 -15.810 14.223  1.00 31.79 ?  120 GLU   A CG   1 
ATOM   2645 C CD   . GLU   A 1 120 ? 28.676 -16.496 15.560  1.00 41.31 ?  120 GLU   A CD   1 
ATOM   2646 O OE1  . GLU   A 1 120 ? 28.042 -16.074 16.550  1.00 42.80 ?  120 GLU   A OE1  1 
ATOM   2647 O OE2  . GLU   A 1 120 ? 29.473 -17.456 15.622  1.00 45.61 -1 120 GLU   A OE2  1 
ATOM   2648 H H    . GLU   A 1 120 ? 28.367 -13.250 12.755  1.00 16.38 ?  120 GLU   A H    1 
ATOM   2649 H HA   . GLU   A 1 120 ? 26.774 -15.279 12.285  1.00 19.90 ?  120 GLU   A HA   1 
ATOM   2650 H HB2  . GLU   A 1 120 ? 27.521 -14.088 14.717  1.00 27.52 ?  120 GLU   A HB2  1 
ATOM   2651 H HB3  . GLU   A 1 120 ? 26.549 -15.341 14.674  1.00 27.52 ?  120 GLU   A HB3  1 
ATOM   2652 H HG2  . GLU   A 1 120 ? 28.360 -16.483 13.532  1.00 38.15 ?  120 GLU   A HG2  1 
ATOM   2653 H HG3  . GLU   A 1 120 ? 29.278 -15.297 14.060  1.00 38.15 ?  120 GLU   A HG3  1 
ATOM   2654 N N    . VAL   A 1 121 ? 25.261 -12.594 13.085  1.00 13.79 ?  121 VAL   A N    1 
ATOM   2655 C CA   . VAL   A 1 121 ? 23.969 -11.926 13.207  1.00 14.03 ?  121 VAL   A CA   1 
ATOM   2656 C C    . VAL   A 1 121 ? 24.084 -10.551 12.566  1.00 12.69 ?  121 VAL   A C    1 
ATOM   2657 O O    . VAL   A 1 121 ? 25.052 -9.826  12.814  1.00 13.27 ?  121 VAL   A O    1 
ATOM   2658 C CB   . VAL   A 1 121 ? 23.536 -11.766 14.684  1.00 17.01 ?  121 VAL   A CB   1 
ATOM   2659 C CG1  . VAL   A 1 121 ? 22.157 -11.117 14.772  1.00 17.33 ?  121 VAL   A CG1  1 
ATOM   2660 C CG2  . VAL   A 1 121 ? 23.535 -13.093 15.419  1.00 19.10 ?  121 VAL   A CG2  1 
ATOM   2661 H H    . VAL   A 1 121 ? 25.929 -12.053 13.168  1.00 16.54 ?  121 VAL   A H    1 
ATOM   2662 H HA   . VAL   A 1 121 ? 23.292 -12.437 12.743  1.00 16.83 ?  121 VAL   A HA   1 
ATOM   2663 H HB   . VAL   A 1 121 ? 24.163 -11.181 15.136  1.00 20.41 ?  121 VAL   A HB   1 
ATOM   2664 H HG11 . VAL   A 1 121 ? 21.835 -11.177 15.688  1.00 20.79 ?  121 VAL   A HG11 1 
ATOM   2665 H HG12 . VAL   A 1 121 ? 22.225 -10.185 14.511  1.00 20.79 ?  121 VAL   A HG12 1 
ATOM   2666 H HG13 . VAL   A 1 121 ? 21.548 -11.585 14.180  1.00 20.79 ?  121 VAL   A HG13 1 
ATOM   2667 H HG21 . VAL   A 1 121 ? 23.194 -12.957 16.322  1.00 22.92 ?  121 VAL   A HG21 1 
ATOM   2668 H HG22 . VAL   A 1 121 ? 22.961 -13.717 14.947  1.00 22.92 ?  121 VAL   A HG22 1 
ATOM   2669 H HG23 . VAL   A 1 121 ? 24.438 -13.436 15.459  1.00 22.92 ?  121 VAL   A HG23 1 
ATOM   2670 N N    . LEU   A 1 122 ? 23.079 -10.168 11.773  1.00 12.22 ?  122 LEU   A N    1 
ATOM   2671 C CA   . LEU   A 1 122 ? 23.080 -8.869  11.110  1.00 12.02 ?  122 LEU   A CA   1 
ATOM   2672 C C    . LEU   A 1 122 ? 21.680 -8.276  11.073  1.00 11.57 ?  122 LEU   A C    1 
ATOM   2673 O O    . LEU   A 1 122 ? 20.687 -8.993  10.941  1.00 12.67 ?  122 LEU   A O    1 
ATOM   2674 C CB   . LEU   A 1 122 ? 23.508 -8.958  9.640   1.00 13.23 ?  122 LEU   A CB   1 
ATOM   2675 C CG   . LEU   A 1 122 ? 24.711 -9.818  9.278   1.00 13.50 ?  122 LEU   A CG   1 
ATOM   2676 C CD1  . LEU   A 1 122 ? 24.320 -11.272 9.058   1.00 14.39 ?  122 LEU   A CD1  1 
ATOM   2677 C CD2  . LEU   A 1 122 ? 25.393 -9.252  8.039   1.00 12.46 ?  122 LEU   A CD2  1 
ATOM   2678 H H    . LEU   A 1 122 ? 22.381 -10.645 11.599  1.00 14.67 ?  122 LEU   A H    1 
ATOM   2679 H HA   . LEU   A 1 122 ? 23.672 -8.257  11.574  1.00 14.43 ?  122 LEU   A HA   1 
ATOM   2680 H HB2  . LEU   A 1 122 ? 22.768 -9.302  9.129   1.00 15.87 ?  122 LEU   A HB2  1 
ATOM   2681 H HB3  . LEU   A 1 122 ? 23.718 -8.061  9.335   1.00 15.87 ?  122 LEU   A HB3  1 
ATOM   2682 H HG   . LEU   A 1 122 ? 25.364 -9.793  9.996   1.00 16.20 ?  122 LEU   A HG   1 
ATOM   2683 H HD11 . LEU   A 1 122 ? 25.096 -11.777 8.761   1.00 17.27 ?  122 LEU   A HD11 1 
ATOM   2684 H HD12 . LEU   A 1 122 ? 23.992 -11.640 9.894   1.00 17.27 ?  122 LEU   A HD12 1 
ATOM   2685 H HD13 . LEU   A 1 122 ? 23.624 -11.316 8.383   1.00 17.27 ?  122 LEU   A HD13 1 
ATOM   2686 H HD21 . LEU   A 1 122 ? 26.137 -9.827  7.780   1.00 14.95 ?  122 LEU   A HD21 1 
ATOM   2687 H HD22 . LEU   A 1 122 ? 24.753 -9.204  7.311   1.00 14.95 ?  122 LEU   A HD22 1 
ATOM   2688 H HD23 . LEU   A 1 122 ? 25.731 -8.360  8.236   1.00 14.95 ?  122 LEU   A HD23 1 
ATOM   2689 N N    A LEU   A 1 123 ? 21.621 -6.951  11.187  0.40 11.34 ?  123 LEU   A N    1 
ATOM   2690 N N    B LEU   A 1 123 ? 21.627 -6.950  11.179  0.60 11.60 ?  123 LEU   A N    1 
ATOM   2691 C CA   A LEU   A 1 123 ? 20.468 -6.153  10.781  0.40 11.17 ?  123 LEU   A CA   1 
ATOM   2692 C CA   B LEU   A 1 123 ? 20.459 -6.145  10.846  0.60 11.67 ?  123 LEU   A CA   1 
ATOM   2693 C C    A LEU   A 1 123 ? 20.720 -5.650  9.368   0.40 10.44 ?  123 LEU   A C    1 
ATOM   2694 C C    B LEU   A 1 123 ? 20.694 -5.599  9.443   0.60 11.03 ?  123 LEU   A C    1 
ATOM   2695 O O    A LEU   A 1 123 ? 21.829 -5.200  9.062   0.40 10.04 ?  123 LEU   A O    1 
ATOM   2696 O O    B LEU   A 1 123 ? 21.690 -4.903  9.215   0.60 10.81 ?  123 LEU   A O    1 
ATOM   2697 C CB   A LEU   A 1 123 ? 20.325 -4.945  11.705  0.40 11.65 ?  123 LEU   A CB   1 
ATOM   2698 C CB   B LEU   A 1 123 ? 20.338 -4.988  11.840  0.60 11.80 ?  123 LEU   A CB   1 
ATOM   2699 C CG   A LEU   A 1 123 ? 19.243 -3.918  11.363  0.40 12.64 ?  123 LEU   A CG   1 
ATOM   2700 C CG   B LEU   A 1 123 ? 19.337 -3.887  11.484  0.60 12.30 ?  123 LEU   A CG   1 
ATOM   2701 C CD1  A LEU   A 1 123 ? 17.860 -4.550  11.384  0.40 13.40 ?  123 LEU   A CD1  1 
ATOM   2702 C CD1  B LEU   A 1 123 ? 17.923 -4.443  11.477  0.60 13.35 ?  123 LEU   A CD1  1 
ATOM   2703 C CD2  A LEU   A 1 123 ? 19.317 -2.750  12.334  0.40 13.07 ?  123 LEU   A CD2  1 
ATOM   2704 C CD2  B LEU   A 1 123 ? 19.447 -2.701  12.435  0.60 12.85 ?  123 LEU   A CD2  1 
ATOM   2705 H H    A LEU   A 1 123 ? 22.265 -6.476  11.513  0.40 13.61 ?  123 LEU   A H    1 
ATOM   2706 H H    B LEU   A 1 123 ? 22.292 -6.468  11.434  0.60 13.92 ?  123 LEU   A H    1 
ATOM   2707 H HA   A LEU   A 1 123 ? 19.662 -6.689  10.805  0.40 13.41 ?  123 LEU   A HA   1 
ATOM   2708 H HA   B LEU   A 1 123 ? 19.648 -6.681  10.860  0.60 14.00 ?  123 LEU   A HA   1 
ATOM   2709 H HB2  A LEU   A 1 123 ? 20.132 -5.271  12.594  0.40 13.97 ?  123 LEU   A HB2  1 
ATOM   2710 H HB2  B LEU   A 1 123 ? 20.065 -5.351  12.701  0.60 14.16 ?  123 LEU   A HB2  1 
ATOM   2711 H HB3  A LEU   A 1 123 ? 21.170 -4.474  11.710  0.40 13.97 ?  123 LEU   A HB3  1 
ATOM   2712 H HB3  B LEU   A 1 123 ? 21.205 -4.568  11.932  0.60 14.16 ?  123 LEU   A HB3  1 
ATOM   2713 H HG   A LEU   A 1 123 ? 19.400 -3.569  10.470  0.40 15.16 ?  123 LEU   A HG   1 
ATOM   2714 H HG   B LEU   A 1 123 ? 19.527 -3.557  10.592  0.60 14.76 ?  123 LEU   A HG   1 
ATOM   2715 H HD11 A LEU   A 1 123 ? 17.195 -3.862  11.226  0.40 16.08 ?  123 LEU   A HD11 1 
ATOM   2716 H HD11 B LEU   A 1 123 ? 17.300 -3.726  11.290  0.60 16.01 ?  123 LEU   A HD11 1 
ATOM   2717 H HD12 A LEU   A 1 123 ? 17.811 -5.225  10.690  0.40 16.08 ?  123 LEU   A HD12 1 
ATOM   2718 H HD12 B LEU   A 1 123 ? 17.857 -5.128  10.790  0.60 16.01 ?  123 LEU   A HD12 1 
ATOM   2719 H HD13 A LEU   A 1 123 ? 17.714 -4.957  12.253  0.40 16.08 ?  123 LEU   A HD13 1 
ATOM   2720 H HD13 B LEU   A 1 123 ? 17.732 -4.832  12.346  0.60 16.01 ?  123 LEU   A HD13 1 
ATOM   2721 H HD21 A LEU   A 1 123 ? 18.628 -2.106  12.110  0.40 15.68 ?  123 LEU   A HD21 1 
ATOM   2722 H HD21 B LEU   A 1 123 ? 18.797 -2.027  12.175  0.60 15.42 ?  123 LEU   A HD21 1 
ATOM   2723 H HD22 A LEU   A 1 123 ? 19.177 -3.082  13.236  0.40 15.68 ?  123 LEU   A HD22 1 
ATOM   2724 H HD22 B LEU   A 1 123 ? 19.262 -3.004  13.338  0.60 15.42 ?  123 LEU   A HD22 1 
ATOM   2725 H HD23 A LEU   A 1 123 ? 20.192 -2.337  12.267  0.40 15.68 ?  123 LEU   A HD23 1 
ATOM   2726 H HD23 B LEU   A 1 123 ? 20.341 -2.336  12.383  0.60 15.42 ?  123 LEU   A HD23 1 
ATOM   2727 N N    A ALA   A 1 124 ? 19.706 -5.705  8.504   0.40 10.19 ?  124 ALA   A N    1 
ATOM   2728 N N    B ALA   A 1 124 ? 19.799 -5.909  8.506   0.60 10.72 ?  124 ALA   A N    1 
ATOM   2729 C CA   A ALA   A 1 124 ? 19.986 -5.451  7.097   0.40 9.58  ?  124 ALA   A CA   1 
ATOM   2730 C CA   B ALA   A 1 124 ? 20.071 -5.632  7.103   0.60 10.89 ?  124 ALA   A CA   1 
ATOM   2731 C C    A ALA   A 1 124 ? 18.724 -4.993  6.375   0.40 9.66  ?  124 ALA   A C    1 
ATOM   2732 C C    B ALA   A 1 124 ? 18.843 -5.136  6.353   0.60 10.58 ?  124 ALA   A C    1 
ATOM   2733 O O    A ALA   A 1 124 ? 17.603 -5.283  6.814   0.40 10.30 ?  124 ALA   A O    1 
ATOM   2734 O O    B ALA   A 1 124 ? 17.705 -5.477  6.703   0.60 11.13 ?  124 ALA   A O    1 
ATOM   2735 C CB   A ALA   A 1 124 ? 20.561 -6.699  6.417   0.40 9.76  ?  124 ALA   A CB   1 
ATOM   2736 C CB   B ALA   A 1 124 ? 20.587 -6.893  6.393   0.60 11.59 ?  124 ALA   A CB   1 
ATOM   2737 H H    A ALA   A 1 124 ? 18.885 -5.879  8.707   0.40 12.22 ?  124 ALA   A H    1 
ATOM   2738 H H    B ALA   A 1 124 ? 19.038 -6.277  8.654   0.60 12.86 ?  124 ALA   A H    1 
ATOM   2739 H HA   A ALA   A 1 124 ? 20.634 -4.740  7.046   0.40 11.49 ?  124 ALA   A HA   1 
ATOM   2740 H HA   B ALA   A 1 124 ? 20.766 -4.957  7.054   0.60 13.07 ?  124 ALA   A HA   1 
ATOM   2741 H HB1  A ALA   A 1 124 ? 20.731 -6.494  5.487   0.40 11.71 ?  124 ALA   A HB1  1 
ATOM   2742 H HB1  B ALA   A 1 124 ? 20.763 -6.686  5.461   0.60 13.90 ?  124 ALA   A HB1  1 
ATOM   2743 H HB2  A ALA   A 1 124 ? 21.389 -6.936  6.864   0.40 11.71 ?  124 ALA   A HB2  1 
ATOM   2744 H HB2  B ALA   A 1 124 ? 21.410 -7.187  6.823   0.60 13.90 ?  124 ALA   A HB2  1 
ATOM   2745 H HB3  A ALA   A 1 124 ? 19.923 -7.422  6.493   0.40 11.71 ?  124 ALA   A HB3  1 
ATOM   2746 H HB3  B ALA   A 1 124 ? 19.917 -7.590  6.456   0.60 13.90 ?  124 ALA   A HB3  1 
ATOM   2747 N N    A PRO   A 1 125 ? 18.886 -4.280  5.258   0.40 10.21 ?  125 PRO   A N    1 
ATOM   2748 N N    B PRO   A 1 125 ? 19.055 -4.372  5.285   0.60 10.00 ?  125 PRO   A N    1 
ATOM   2749 C CA   A PRO   A 1 125 ? 17.807 -4.083  4.291   0.40 10.59 ?  125 PRO   A CA   1 
ATOM   2750 C CA   B PRO   A 1 125 ? 17.972 -4.001  4.379   0.60 10.24 ?  125 PRO   A CA   1 
ATOM   2751 C C    A PRO   A 1 125 ? 17.877 -5.142  3.194   0.40 10.09 ?  125 PRO   A C    1 
ATOM   2752 C C    B PRO   A 1 125 ? 17.882 -5.043  3.270   0.60 10.85 ?  125 PRO   A C    1 
ATOM   2753 O O    A PRO   A 1 125 ? 18.833 -5.913  3.096   0.40 10.41 ?  125 PRO   A O    1 
ATOM   2754 O O    B PRO   A 1 125 ? 18.727 -5.933  3.146   0.60 11.44 ?  125 PRO   A O    1 
ATOM   2755 C CB   A PRO   A 1 125 ? 18.157 -2.711  3.698   0.40 11.09 ?  125 PRO   A CB   1 
ATOM   2756 C CB   B PRO   A 1 125 ? 18.493 -2.680  3.804   0.60 9.91  ?  125 PRO   A CB   1 
ATOM   2757 C CG   A PRO   A 1 125 ? 19.662 -2.732  3.659   0.40 11.06 ?  125 PRO   A CG   1 
ATOM   2758 C CG   B PRO   A 1 125 ? 19.968 -2.970  3.608   0.60 9.33  ?  125 PRO   A CG   1 
ATOM   2759 C CD   A PRO   A 1 125 ? 20.094 -3.517  4.886   0.40 10.51 ?  125 PRO   A CD   1 
ATOM   2760 C CD   B PRO   A 1 125 ? 20.352 -3.873  4.784   0.60 9.42  ?  125 PRO   A CD   1 
ATOM   2761 H HA   A PRO   A 1 125 ? 16.935 -4.067  4.709   0.40 12.70 ?  125 PRO   A HA   1 
ATOM   2762 H HA   B PRO   A 1 125 ? 17.122 -3.888  4.846   0.60 12.28 ?  125 PRO   A HA   1 
ATOM   2763 H HB2  A PRO   A 1 125 ? 17.787 -2.625  2.802   0.40 13.31 ?  125 PRO   A HB2  1 
ATOM   2764 H HB2  B PRO   A 1 125 ? 18.050 -2.487  2.963   0.60 11.89 ?  125 PRO   A HB2  1 
ATOM   2765 H HB3  A PRO   A 1 125 ? 17.833 -2.003  4.277   0.40 13.31 ?  125 PRO   A HB3  1 
ATOM   2766 H HB3  B PRO   A 1 125 ? 18.357 -1.961  4.445   0.60 11.89 ?  125 PRO   A HB3  1 
ATOM   2767 H HG2  A PRO   A 1 125 ? 19.961 -3.176  2.849   0.40 13.27 ?  125 PRO   A HG2  1 
ATOM   2768 H HG2  B PRO   A 1 125 ? 20.096 -3.434  2.762   0.60 11.19 ?  125 PRO   A HG2  1 
ATOM   2769 H HG3  A PRO   A 1 125 ? 20.003 -1.824  3.694   0.40 13.27 ?  125 PRO   A HG3  1 
ATOM   2770 H HG3  B PRO   A 1 125 ? 20.468 -2.144  3.625   0.60 11.19 ?  125 PRO   A HG3  1 
ATOM   2771 H HD2  A PRO   A 1 125 ? 20.825 -4.114  4.666   0.40 12.61 ?  125 PRO   A HD2  1 
ATOM   2772 H HD2  B PRO   A 1 125 ? 20.910 -4.607  4.475   0.60 11.31 ?  125 PRO   A HD2  1 
ATOM   2773 H HD3  A PRO   A 1 125 ? 20.339 -2.908  5.604   0.40 12.61 ?  125 PRO   A HD3  1 
ATOM   2774 H HD3  B PRO   A 1 125 ? 20.802 -3.352  5.467   0.60 11.31 ?  125 PRO   A HD3  1 
ATOM   2775 N N    A LEU   A 1 126 ? 16.850 -5.143  2.344   0.40 10.10 ?  126 LEU   A N    1 
ATOM   2776 N N    B LEU   A 1 126 ? 16.859 -4.891  2.437   0.60 11.68 ?  126 LEU   A N    1 
ATOM   2777 C CA   A LEU   A 1 126 ? 16.881 -5.961  1.138   0.40 10.33 ?  126 LEU   A CA   1 
ATOM   2778 C CA   B LEU   A 1 126 ? 16.691 -5.754  1.273   0.60 11.90 ?  126 LEU   A CA   1 
ATOM   2779 C C    A LEU   A 1 126 ? 17.838 -5.347  0.124   0.40 10.33 ?  126 LEU   A C    1 
ATOM   2780 C C    B LEU   A 1 126 ? 17.582 -5.247  0.141   0.60 11.38 ?  126 LEU   A C    1 
ATOM   2781 O O    A LEU   A 1 126 ? 17.684 -4.187  -0.277  0.40 10.55 ?  126 LEU   A O    1 
ATOM   2782 O O    B LEU   A 1 126 ? 17.284 -4.223  -0.483  0.60 12.46 ?  126 LEU   A O    1 
ATOM   2783 C CB   A LEU   A 1 126 ? 15.483 -6.093  0.542   0.40 10.40 ?  126 LEU   A CB   1 
ATOM   2784 C CB   B LEU   A 1 126 ? 15.224 -5.766  0.860   0.60 14.25 ?  126 LEU   A CB   1 
ATOM   2785 C CG   A LEU   A 1 126 ? 14.530 -6.993  1.328   0.40 10.83 ?  126 LEU   A CG   1 
ATOM   2786 C CG   B LEU   A 1 126 ? 14.741 -6.875  -0.068  0.60 15.91 ?  126 LEU   A CG   1 
ATOM   2787 C CD1  A LEU   A 1 126 ? 13.118 -6.867  0.780   0.40 11.71 ?  126 LEU   A CD1  1 
ATOM   2788 C CD1  B LEU   A 1 126 ? 14.914 -8.245  0.565   0.60 16.07 ?  126 LEU   A CD1  1 
ATOM   2789 C CD2  A LEU   A 1 126 ? 14.994 -8.450  1.294   0.40 11.29 ?  126 LEU   A CD2  1 
ATOM   2790 C CD2  B LEU   A 1 126 ? 13.286 -6.631  -0.414  0.60 16.20 ?  126 LEU   A CD2  1 
ATOM   2791 H H    A LEU   A 1 126 ? 16.137 -4.674  2.431   0.40 12.12 ?  126 LEU   A H    1 
ATOM   2792 H H    B LEU   A 1 126 ? 16.247 -4.285  2.520   0.60 14.02 ?  126 LEU   A H    1 
ATOM   2793 H HA   A LEU   A 1 126 ? 17.206 -6.847  1.357   0.40 12.39 ?  126 LEU   A HA   1 
ATOM   2794 H HA   B LEU   A 1 126 ? 16.962 -6.656  1.504   0.60 14.28 ?  126 LEU   A HA   1 
ATOM   2795 H HB2  A LEU   A 1 126 ? 15.082 -5.214  0.496   0.40 12.48 ?  126 LEU   A HB2  1 
ATOM   2796 H HB2  B LEU   A 1 126 ? 14.690 -5.824  1.665   0.60 17.10 ?  126 LEU   A HB2  1 
ATOM   2797 H HB3  A LEU   A 1 126 ? 15.559 -6.464  -0.352  0.40 12.48 ?  126 LEU   A HB3  1 
ATOM   2798 H HB3  B LEU   A 1 126 ? 15.037 -4.926  0.414   0.60 17.10 ?  126 LEU   A HB3  1 
ATOM   2799 H HG   A LEU   A 1 126 ? 14.512 -6.706  2.253   0.40 12.99 ?  126 LEU   A HG   1 
ATOM   2800 H HG   B LEU   A 1 126 ? 15.254 -6.851  -0.893  0.60 19.09 ?  126 LEU   A HG   1 
ATOM   2801 H HD11 A LEU   A 1 126 ? 12.528 -7.443  1.288   0.40 14.05 ?  126 LEU   A HD11 1 
ATOM   2802 H HD11 B LEU   A 1 126 ? 14.459 -8.906  0.019   0.60 19.28 ?  126 LEU   A HD11 1 
ATOM   2803 H HD12 A LEU   A 1 126 ? 12.832 -5.944  0.858   0.40 14.05 ?  126 LEU   A HD12 1 
ATOM   2804 H HD12 B LEU   A 1 126 ? 15.860 -8.453  0.616   0.60 19.28 ?  126 LEU   A HD12 1 
ATOM   2805 H HD13 A LEU   A 1 126 ? 13.119 -7.135  -0.154  0.40 14.05 ?  126 LEU   A HD13 1 
ATOM   2806 H HD13 B LEU   A 1 126 ? 14.528 -8.232  1.455   0.60 19.28 ?  126 LEU   A HD13 1 
ATOM   2807 H HD21 A LEU   A 1 126 ? 14.294 -9.013  1.662   0.40 13.54 ?  126 LEU   A HD21 1 
ATOM   2808 H HD21 B LEU   A 1 126 ? 12.977 -7.337  -1.004  0.60 19.43 ?  126 LEU   A HD21 1 
ATOM   2809 H HD22 A LEU   A 1 126 ? 15.172 -8.703  0.375   0.40 13.54 ?  126 LEU   A HD22 1 
ATOM   2810 H HD22 B LEU   A 1 126 ? 12.764 -6.633  0.404   0.60 19.43 ?  126 LEU   A HD22 1 
ATOM   2811 H HD23 A LEU   A 1 126 ? 15.801 -8.536  1.824   0.40 13.54 ?  126 LEU   A HD23 1 
ATOM   2812 H HD23 B LEU   A 1 126 ? 13.205 -5.771  -0.856  0.60 19.43 ?  126 LEU   A HD23 1 
ATOM   2813 N N    A LEU   A 1 127 ? 18.830 -6.130  -0.286  0.40 11.13 ?  127 LEU   A N    1 
ATOM   2814 N N    B LEU   A 1 127 ? 18.665 -5.969  -0.144  0.60 11.79 ?  127 LEU   A N    1 
ATOM   2815 C CA   A LEU   A 1 127 ? 19.838 -5.646  -1.214  0.40 11.06 ?  127 LEU   A CA   1 
ATOM   2816 C CA   B LEU   A 1 127 ? 19.651 -5.482  -1.099  0.60 11.67 ?  127 LEU   A CA   1 
ATOM   2817 C C    A LEU   A 1 127 ? 19.234 -5.441  -2.593  0.40 11.18 ?  127 LEU   A C    1 
ATOM   2818 C C    B LEU   A 1 127 ? 19.055 -5.378  -2.493  0.60 11.04 ?  127 LEU   A C    1 
ATOM   2819 O O    A LEU   A 1 127 ? 18.412 -6.233  -3.066  0.40 11.32 ?  127 LEU   A O    1 
ATOM   2820 O O    B LEU   A 1 127 ? 18.213 -6.184  -2.908  0.60 11.65 ?  127 LEU   A O    1 
ATOM   2821 C CB   A LEU   A 1 127 ? 20.991 -6.643  -1.302  0.40 11.29 ?  127 LEU   A CB   1 
ATOM   2822 C CB   B LEU   A 1 127 ? 20.883 -6.391  -1.137  0.60 12.26 ?  127 LEU   A CB   1 
ATOM   2823 C CG   A LEU   A 1 127 ? 21.742 -6.932  -0.003  0.40 11.17 ?  127 LEU   A CG   1 
ATOM   2824 C CG   B LEU   A 1 127 ? 21.727 -6.450  0.141   0.60 12.75 ?  127 LEU   A CG   1 
ATOM   2825 C CD1  A LEU   A 1 127 ? 22.849 -7.924  -0.265  0.40 11.07 ?  127 LEU   A CD1  1 
ATOM   2826 C CD1  B LEU   A 1 127 ? 22.894 -7.409  -0.029  0.60 13.23 ?  127 LEU   A CD1  1 
ATOM   2827 C CD2  A LEU   A 1 127 ? 22.306 -5.654  0.585   0.40 11.38 ?  127 LEU   A CD2  1 
ATOM   2828 C CD2  B LEU   A 1 127 ? 22.226 -5.072  0.563   0.60 13.56 ?  127 LEU   A CD2  1 
ATOM   2829 H H    A LEU   A 1 127 ? 18.940 -6.950  -0.041  0.40 13.36 ?  127 LEU   A H    1 
ATOM   2830 H H    B LEU   A 1 127 ? 18.851 -6.744  0.186   0.60 14.15 ?  127 LEU   A H    1 
ATOM   2831 H HA   A LEU   A 1 127 ? 20.189 -4.799  -0.900  0.40 13.27 ?  127 LEU   A HA   1 
ATOM   2832 H HA   B LEU   A 1 127 ? 19.934 -4.602  -0.833  0.60 14.00 ?  127 LEU   A HA   1 
ATOM   2833 H HB2  A LEU   A 1 127 ? 20.642 -7.488  -1.625  0.40 13.54 ?  127 LEU   A HB2  1 
ATOM   2834 H HB2  B LEU   A 1 127 ? 20.590 -7.294  -1.336  0.60 14.70 ?  127 LEU   A HB2  1 
ATOM   2835 H HB3  A LEU   A 1 127 ? 21.643 -6.301  -1.934  0.40 13.54 ?  127 LEU   A HB3  1 
ATOM   2836 H HB3  B LEU   A 1 127 ? 21.463 -6.081  -1.855  0.60 14.70 ?  127 LEU   A HB3  1 
ATOM   2837 H HG   A LEU   A 1 127 ? 21.128 -7.323  0.644   0.40 13.40 ?  127 LEU   A HG   1 
ATOM   2838 H HG   B LEU   A 1 127 ? 21.173 -6.794  0.856   0.60 15.30 ?  127 LEU   A HG   1 
ATOM   2839 H HD11 A LEU   A 1 127 ? 23.267 -8.162  0.577   0.40 13.28 ?  127 LEU   A HD11 1 
ATOM   2840 H HD11 B LEU   A 1 127 ? 23.426 -7.403  0.785   0.60 15.88 ?  127 LEU   A HD11 1 
ATOM   2841 H HD12 A LEU   A 1 127 ? 22.469 -8.717  -0.680  0.40 13.28 ?  127 LEU   A HD12 1 
ATOM   2842 H HD12 B LEU   A 1 127 ? 22.550 -8.301  -0.191  0.60 15.88 ?  127 LEU   A HD12 1 
ATOM   2843 H HD13 A LEU   A 1 127 ? 23.498 -7.520  -0.859  0.40 13.28 ?  127 LEU   A HD13 1 
ATOM   2844 H HD13 B LEU   A 1 127 ? 23.436 -7.120  -0.778  0.60 15.88 ?  127 LEU   A HD13 1 
ATOM   2845 H HD21 A LEU   A 1 127 ? 22.891 -5.881  1.322   0.40 13.66 ?  127 LEU   A HD21 1 
ATOM   2846 H HD21 B LEU   A 1 127 ? 22.849 -5.174  1.301   0.60 16.27 ?  127 LEU   A HD21 1 
ATOM   2847 H HD22 A LEU   A 1 127 ? 22.802 -5.189  -0.105  0.40 13.66 ?  127 LEU   A HD22 1 
ATOM   2848 H HD22 B LEU   A 1 127 ? 22.672 -4.651  -0.188  0.60 16.27 ?  127 LEU   A HD22 1 
ATOM   2849 H HD23 A LEU   A 1 127 ? 21.573 -5.103  0.898   0.40 13.66 ?  127 LEU   A HD23 1 
ATOM   2850 H HD23 B LEU   A 1 127 ? 21.469 -4.533  0.843   0.60 16.27 ?  127 LEU   A HD23 1 
ATOM   2851 N N    A SER   A 1 128 ? 19.662 -4.365  -3.240  0.40 11.59 ?  128 SER   A N    1 
ATOM   2852 N N    B SER   A 1 128 ? 19.511 -4.359  -3.216  0.60 11.18 ?  128 SER   A N    1 
ATOM   2853 C CA   A SER   A 1 128 ? 19.256 -3.957  -4.576  0.40 11.75 ?  128 SER   A CA   1 
ATOM   2854 C CA   B SER   A 1 128 ? 19.152 -4.083  -4.596  0.60 11.80 ?  128 SER   A CA   1 
ATOM   2855 C C    A SER   A 1 128 ? 17.794 -3.519  -4.658  0.40 12.27 ?  128 SER   A C    1 
ATOM   2856 C C    B SER   A 1 128 ? 17.695 -3.661  -4.761  0.60 11.81 ?  128 SER   A C    1 
ATOM   2857 O O    A SER   A 1 128 ? 17.329 -3.190  -5.753  0.40 12.68 ?  128 SER   A O    1 
ATOM   2858 O O    B SER   A 1 128 ? 17.261 -3.434  -5.894  0.60 13.50 ?  128 SER   A O    1 
ATOM   2859 C CB   A SER   A 1 128 ? 19.589 -4.997  -5.657  0.40 11.26 ?  128 SER   A CB   1 
ATOM   2860 C CB   B SER   A 1 128 ? 19.517 -5.241  -5.533  0.60 12.56 ?  128 SER   A CB   1 
ATOM   2861 O OG   A SER   A 1 128 ? 20.988 -5.255  -5.689  0.40 11.53 ?  128 SER   A OG   1 
ATOM   2862 O OG   B SER   A 1 128 ? 20.930 -5.339  -5.677  0.60 13.29 ?  128 SER   A OG   1 
ATOM   2863 H H    A SER   A 1 128 ? 20.237 -3.822  -2.894  0.40 13.91 ?  128 SER   A H    1 
ATOM   2864 H H    B SER   A 1 128 ? 20.071 -3.774  -2.906  0.60 13.42 ?  128 SER   A H    1 
ATOM   2865 H HA   A SER   A 1 128 ? 19.787 -3.182  -4.790  0.40 14.10 ?  128 SER   A HA   1 
ATOM   2866 H HA   B SER   A 1 128 ? 19.676 -3.324  -4.890  0.60 14.16 ?  128 SER   A HA   1 
ATOM   2867 H HB2  A SER   A 1 128 ? 19.119 -5.821  -5.464  0.40 13.52 ?  128 SER   A HB2  1 
ATOM   2868 H HB2  B SER   A 1 128 ? 19.175 -6.066  -5.148  0.60 15.07 ?  128 SER   A HB2  1 
ATOM   2869 H HB3  A SER   A 1 128 ? 19.315 -4.650  -6.520  0.40 13.52 ?  128 SER   A HB3  1 
ATOM   2870 H HB3  B SER   A 1 128 ? 19.121 -5.084  -6.396  0.60 15.07 ?  128 SER   A HB3  1 
ATOM   2871 H HG   A SER   A 1 128 ? 21.407 -4.548  -5.853  0.40 13.84 ?  128 SER   A HG   1 
ATOM   2872 H HG   B SER   A 1 128 ? 21.236 -4.619  -5.983  0.60 15.94 ?  128 SER   A HG   1 
ATOM   2873 N N    A ALA   A 1 129 ? 17.067 -3.473  -3.540  0.40 13.33 ?  129 ALA   A N    1 
ATOM   2874 N N    B ALA   A 1 129 ? 16.944 -3.510  -3.672  0.60 12.76 ?  129 ALA   A N    1 
ATOM   2875 C CA   A ALA   A 1 129 ? 15.709 -2.951  -3.511  0.40 13.94 ?  129 ALA   A CA   1 
ATOM   2876 C CA   B ALA   A 1 129 ? 15.562 -3.057  -3.728  0.60 13.44 ?  129 ALA   A CA   1 
ATOM   2877 C C    A ALA   A 1 129 ? 15.731 -1.423  -3.498  0.40 13.89 ?  129 ALA   A C    1 
ATOM   2878 C C    B ALA   A 1 129 ? 15.519 -1.527  -3.669  0.60 14.06 ?  129 ALA   A C    1 
ATOM   2879 O O    A ALA   A 1 129 ? 16.788 -0.788  -3.529  0.40 14.64 ?  129 ALA   A O    1 
ATOM   2880 O O    B ALA   A 1 129 ? 16.549 -0.849  -3.717  0.60 14.55 ?  129 ALA   A O    1 
ATOM   2881 C CB   A ALA   A 1 129 ? 14.958 -3.502  -2.299  0.40 15.04 ?  129 ALA   A CB   1 
ATOM   2882 C CB   B ALA   A 1 129 ? 14.736 -3.746  -2.640  0.60 14.26 ?  129 ALA   A CB   1 
ATOM   2883 H H    A ALA   A 1 129 ? 17.347 -3.744  -2.774  0.40 16.00 ?  129 ALA   A H    1 
ATOM   2884 H H    B ALA   A 1 129 ? 17.230 -3.667  -2.873  0.60 15.31 ?  129 ALA   A H    1 
ATOM   2885 H HA   A ALA   A 1 129 ? 15.242 -3.229  -4.308  0.40 16.72 ?  129 ALA   A HA   1 
ATOM   2886 H HA   B ALA   A 1 129 ? 15.192 -3.324  -4.575  0.60 16.12 ?  129 ALA   A HA   1 
ATOM   2887 H HB1  A ALA   A 1 129 ? 14.054 -3.153  -2.299  0.40 18.05 ?  129 ALA   A HB1  1 
ATOM   2888 H HB1  B ALA   A 1 129 ? 13.823 -3.430  -2.688  0.60 17.10 ?  129 ALA   A HB1  1 
ATOM   2889 H HB2  A ALA   A 1 129 ? 14.937 -4.473  -2.358  0.40 18.05 ?  129 ALA   A HB2  1 
ATOM   2890 H HB2  B ALA   A 1 129 ? 14.763 -4.708  -2.784  0.60 17.10 ?  129 ALA   A HB2  1 
ATOM   2891 H HB3  A ALA   A 1 129 ? 15.418 -3.234  -1.488  0.40 18.05 ?  129 ALA   A HB3  1 
ATOM   2892 H HB3  B ALA   A 1 129 ? 15.115 -3.537  -1.769  0.60 17.10 ?  129 ALA   A HB3  1 
ATOM   2893 N N    A GLY   A 1 130 ? 14.548 -0.821  -3.449  0.40 14.38 ?  130 GLY   A N    1 
ATOM   2894 N N    B GLY   A 1 130 ? 14.318 -0.966  -3.584  0.60 14.70 ?  130 GLY   A N    1 
ATOM   2895 C CA   A GLY   A 1 130 ? 14.479 0.630   -3.404  0.40 15.19 ?  130 GLY   A CA   1 
ATOM   2896 C CA   B GLY   A 1 130 ? 14.189 0.480   -3.546  0.60 15.58 ?  130 GLY   A CA   1 
ATOM   2897 C C    A GLY   A 1 130 ? 15.098 1.241   -4.643  0.40 15.27 ?  130 GLY   A C    1 
ATOM   2898 C C    B GLY   A 1 130 ? 14.767 1.118   -4.789  0.60 15.58 ?  130 GLY   A C    1 
ATOM   2899 O O    A GLY   A 1 130 ? 14.860 0.796   -5.770  0.40 14.90 ?  130 GLY   A O    1 
ATOM   2900 O O    B GLY   A 1 130 ? 14.525 0.671   -5.915  0.60 15.70 ?  130 GLY   A O    1 
ATOM   2901 H H    A GLY   A 1 130 ? 13.790 -1.222  -3.437  0.40 17.25 ?  130 GLY   A H    1 
ATOM   2902 H H    B GLY   A 1 130 ? 13.576 -1.393  -3.540  0.60 17.63 ?  130 GLY   A H    1 
ATOM   2903 H HA2  A GLY   A 1 130 ? 13.553 0.909   -3.347  0.40 18.23 ?  130 GLY   A HA2  1 
ATOM   2904 H HA2  B GLY   A 1 130 ? 13.257 0.732   -3.449  0.60 18.69 ?  130 GLY   A HA2  1 
ATOM   2905 H HA3  A GLY   A 1 130 ? 14.954 0.960   -2.626  0.40 18.23 ?  130 GLY   A HA3  1 
ATOM   2906 H HA3  B GLY   A 1 130 ? 14.682 0.822   -2.798  0.60 18.69 ?  130 GLY   A HA3  1 
ATOM   2907 N N    A ILE   A 1 131 ? 15.917 2.277   -4.435  0.40 15.56 ?  131 ILE   A N    1 
ATOM   2908 N N    B ILE   A 1 131 ? 15.559 2.173   -4.587  0.60 16.28 ?  131 ILE   A N    1 
ATOM   2909 C CA   A ILE   A 1 131 ? 16.494 3.027   -5.547  0.40 15.08 ?  131 ILE   A CA   1 
ATOM   2910 C CA   B ILE   A 1 131 ? 16.081 2.957   -5.701  0.60 16.69 ?  131 ILE   A CA   1 
ATOM   2911 C C    A ILE   A 1 131 ? 17.490 2.224   -6.375  0.40 14.18 ?  131 ILE   A C    1 
ATOM   2912 C C    B ILE   A 1 131 ? 17.195 2.211   -6.427  0.60 15.78 ?  131 ILE   A C    1 
ATOM   2913 O O    A ILE   A 1 131 ? 17.902 2.700   -7.441  0.40 14.99 ?  131 ILE   A O    1 
ATOM   2914 O O    B ILE   A 1 131 ? 17.710 2.697   -7.441  0.60 16.26 ?  131 ILE   A O    1 
ATOM   2915 C CB   A ILE   A 1 131 ? 17.099 4.368   -5.076  0.40 16.00 ?  131 ILE   A CB   1 
ATOM   2916 C CB   B ILE   A 1 131 ? 16.509 4.377   -5.281  0.60 18.09 ?  131 ILE   A CB   1 
ATOM   2917 C CG1  A ILE   A 1 131 ? 18.357 4.145   -4.234  0.40 17.13 ?  131 ILE   A CG1  1 
ATOM   2918 C CG1  B ILE   A 1 131 ? 17.692 4.341   -4.315  0.60 19.80 ?  131 ILE   A CG1  1 
ATOM   2919 C CG2  A ILE   A 1 131 ? 16.071 5.169   -4.281  0.40 15.65 ?  131 ILE   A CG2  1 
ATOM   2920 C CG2  B ILE   A 1 131 ? 15.328 5.136   -4.681  0.60 18.09 ?  131 ILE   A CG2  1 
ATOM   2921 C CD1  A ILE   A 1 131 ? 19.021 5.440   -3.788  0.40 17.97 ?  131 ILE   A CD1  1 
ATOM   2922 C CD1  B ILE   A 1 131 ? 18.220 5.715   -3.985  0.60 20.54 ?  131 ILE   A CD1  1 
ATOM   2923 H H    A ILE   A 1 131 ? 16.141 2.567   -3.659  0.40 18.67 ?  131 ILE   A H    1 
ATOM   2924 H H    B ILE   A 1 131 ? 15.812 2.448   -3.813  0.60 19.54 ?  131 ILE   A H    1 
ATOM   2925 H HA   A ILE   A 1 131 ? 15.774 3.254   -6.148  0.40 18.10 ?  131 ILE   A HA   1 
ATOM   2926 H HA   B ILE   A 1 131 ? 15.369 3.063   -6.340  0.60 20.02 ?  131 ILE   A HA   1 
ATOM   2927 H HB   A ILE   A 1 131 ? 17.342 4.888   -5.860  0.40 19.20 ?  131 ILE   A HB   1 
ATOM   2928 H HB   B ILE   A 1 131 ? 16.788 4.848   -6.076  0.60 21.71 ?  131 ILE   A HB   1 
ATOM   2929 H HG12 A ILE   A 1 131 ? 18.118 3.647   -3.441  0.40 20.55 ?  131 ILE   A HG12 1 
ATOM   2930 H HG12 B ILE   A 1 131 ? 17.406 3.924   -3.490  0.60 23.76 ?  131 ILE   A HG12 1 
ATOM   2931 H HG13 A ILE   A 1 131 ? 19.005 3.653   -4.758  0.40 20.55 ?  131 ILE   A HG13 1 
ATOM   2932 H HG13 B ILE   A 1 131 ? 18.417 3.830   -4.709  0.60 23.76 ?  131 ILE   A HG13 1 
ATOM   2933 H HG21 A ILE   A 1 131 ? 16.391 6.079   -4.172  0.40 18.77 ?  131 ILE   A HG21 1 
ATOM   2934 H HG21 B ILE   A 1 131 ? 15.583 6.063   -4.545  0.60 21.71 ?  131 ILE   A HG21 1 
ATOM   2935 H HG22 A ILE   A 1 131 ? 15.232 5.171   -4.766  0.40 18.77 ?  131 ILE   A HG22 1 
ATOM   2936 H HG22 B ILE   A 1 131 ? 14.578 5.090   -5.294  0.60 21.71 ?  131 ILE   A HG22 1 
ATOM   2937 H HG23 A ILE   A 1 131 ? 15.952 4.753   -3.413  0.40 18.77 ?  131 ILE   A HG23 1 
ATOM   2938 H HG23 B ILE   A 1 131 ? 15.086 4.731   -3.834  0.60 21.71 ?  131 ILE   A HG23 1 
ATOM   2939 H HD11 A ILE   A 1 131 ? 19.885 5.233   -3.396  0.40 21.56 ?  131 ILE   A HD11 1 
ATOM   2940 H HD11 B ILE   A 1 131 ? 19.093 5.631   -3.581  0.60 24.65 ?  131 ILE   A HD11 1 
ATOM   2941 H HD12 A ILE   A 1 131 ? 19.142 6.019   -4.560  0.40 21.56 ?  131 ILE   A HD12 1 
ATOM   2942 H HD12 B ILE   A 1 131 ? 18.280 6.227   -4.806  0.60 24.65 ?  131 ILE   A HD12 1 
ATOM   2943 H HD13 A ILE   A 1 131 ? 18.458 5.881   -3.133  0.40 21.56 ?  131 ILE   A HD13 1 
ATOM   2944 H HD13 B ILE   A 1 131 ? 17.605 6.145   -3.371  0.60 24.65 ?  131 ILE   A HD13 1 
ATOM   2945 N N    A PHE   A 1 132 ? 17.895 1.027   -5.927  0.40 13.32 ?  132 PHE   A N    1 
ATOM   2946 N N    B PHE   A 1 132 ? 17.566 1.022   -5.931  0.60 14.79 ?  132 PHE   A N    1 
ATOM   2947 C CA   A PHE   A 1 132 ? 18.768 0.184   -6.740  0.40 13.27 ?  132 PHE   A CA   1 
ATOM   2948 C CA   B PHE   A 1 132 ? 18.459 0.155   -6.691  0.60 14.15 ?  132 PHE   A CA   1 
ATOM   2949 C C    A PHE   A 1 132 ? 18.015 -0.568  -7.836  0.40 14.28 ?  132 PHE   A C    1 
ATOM   2950 C C    B PHE   A 1 132 ? 17.741 -0.596  -7.811  0.60 14.62 ?  132 PHE   A C    1 
ATOM   2951 O O    A PHE   A 1 132 ? 18.657 -1.187  -8.693  0.40 15.59 ?  132 PHE   A O    1 
ATOM   2952 O O    B PHE   A 1 132 ? 18.404 -1.192  -8.664  0.60 14.87 ?  132 PHE   A O    1 
ATOM   2953 C CB   A PHE   A 1 132 ? 19.563 -0.799  -5.868  0.40 11.84 ?  132 PHE   A CB   1 
ATOM   2954 C CB   B PHE   A 1 132 ? 19.176 -0.842  -5.773  0.60 13.67 ?  132 PHE   A CB   1 
ATOM   2955 C CG   A PHE   A 1 132 ? 20.786 -0.197  -5.205  0.40 11.36 ?  132 PHE   A CG   1 
ATOM   2956 C CG   B PHE   A 1 132 ? 20.381 -0.279  -5.063  0.60 13.31 ?  132 PHE   A CG   1 
ATOM   2957 C CD1  A PHE   A 1 132 ? 20.667 0.821   -4.271  0.40 12.43 ?  132 PHE   A CD1  1 
ATOM   2958 C CD1  B PHE   A 1 132 ? 20.236 0.681   -4.075  0.60 14.00 ?  132 PHE   A CD1  1 
ATOM   2959 C CD2  A PHE   A 1 132 ? 22.057 -0.684  -5.490  0.40 11.80 ?  132 PHE   A CD2  1 
ATOM   2960 C CD2  B PHE   A 1 132 ? 21.655 -0.744  -5.356  0.60 13.57 ?  132 PHE   A CD2  1 
ATOM   2961 C CE1  A PHE   A 1 132 ? 21.790 1.357   -3.651  0.40 12.21 ?  132 PHE   A CE1  1 
ATOM   2962 C CE1  B PHE   A 1 132 ? 21.341 1.185   -3.409  0.60 14.18 ?  132 PHE   A CE1  1 
ATOM   2963 C CE2  A PHE   A 1 132 ? 23.183 -0.152  -4.870  0.40 12.27 ?  132 PHE   A CE2  1 
ATOM   2964 C CE2  B PHE   A 1 132 ? 22.763 -0.250  -4.689  0.60 13.58 ?  132 PHE   A CE2  1 
ATOM   2965 C CZ   A PHE   A 1 132 ? 23.046 0.872   -3.951  0.40 12.03 ?  132 PHE   A CZ   1 
ATOM   2966 C CZ   B PHE   A 1 132 ? 22.605 0.724   -3.718  0.60 13.42 ?  132 PHE   A CZ   1 
ATOM   2967 H H    A PHE   A 1 132 ? 17.690 0.697   -5.158  0.40 15.99 ?  132 PHE   A H    1 
ATOM   2968 H H    B PHE   A 1 132 ? 17.322 0.713   -5.161  0.60 17.74 ?  132 PHE   A H    1 
ATOM   2969 H HA   A PHE   A 1 132 ? 19.416 0.757   -7.176  0.40 15.93 ?  132 PHE   A HA   1 
ATOM   2970 H HA   B PHE   A 1 132 ? 19.141 0.714   -7.093  0.60 16.98 ?  132 PHE   A HA   1 
ATOM   2971 H HB2  A PHE   A 1 132 ? 18.989 -1.129  -5.164  0.40 14.21 ?  132 PHE   A HB2  1 
ATOM   2972 H HB2  B PHE   A 1 132 ? 18.557 -1.146  -5.094  0.60 16.40 ?  132 PHE   A HB2  1 
ATOM   2973 H HB3  A PHE   A 1 132 ? 19.866 -1.538  -6.423  0.40 14.21 ?  132 PHE   A HB3  1 
ATOM   2974 H HB3  B PHE   A 1 132 ? 19.478 -1.589  -6.308  0.60 16.40 ?  132 PHE   A HB3  1 
ATOM   2975 H HD1  A PHE   A 1 132 ? 19.828 1.154   -4.060  0.40 14.91 ?  132 PHE   A HD1  1 
ATOM   2976 H HD1  B PHE   A 1 132 ? 19.389 1.001   -3.859  0.60 16.79 ?  132 PHE   A HD1  1 
ATOM   2977 H HD2  A PHE   A 1 132 ? 22.162 -1.374  -6.105  0.40 14.16 ?  132 PHE   A HD2  1 
ATOM   2978 H HD2  B PHE   A 1 132 ? 21.765 -1.397  -6.008  0.60 16.28 ?  132 PHE   A HD2  1 
ATOM   2979 H HE1  A PHE   A 1 132 ? 21.697 2.044   -3.030  0.40 14.65 ?  132 PHE   A HE1  1 
ATOM   2980 H HE1  B PHE   A 1 132 ? 21.230 1.839   -2.751  0.60 17.01 ?  132 PHE   A HE1  1 
ATOM   2981 H HE2  A PHE   A 1 132 ? 24.030 -0.484  -5.076  0.40 14.72 ?  132 PHE   A HE2  1 
ATOM   2982 H HE2  B PHE   A 1 132 ? 23.612 -0.562  -4.904  0.60 16.30 ?  132 PHE   A HE2  1 
ATOM   2983 H HZ   A PHE   A 1 132 ? 23.799 1.231   -3.535  0.40 14.43 ?  132 PHE   A HZ   1 
ATOM   2984 H HZ   B PHE   A 1 132 ? 23.344 1.064   -3.268  0.60 16.10 ?  132 PHE   A HZ   1 
ATOM   2985 N N    A GLY   A 1 133 ? 16.683 -0.551  -7.822  0.40 14.18 ?  133 GLY   A N    1 
ATOM   2986 N N    B GLY   A 1 133 ? 16.413 -0.610  -7.821  0.60 15.12 ?  133 GLY   A N    1 
ATOM   2987 C CA   A GLY   A 1 133 ? 15.903 -0.910  -8.987  0.40 14.39 ?  133 GLY   A CA   1 
ATOM   2988 C CA   B GLY   A 1 133 ? 15.670 -0.971  -9.009  0.60 16.24 ?  133 GLY   A CA   1 
ATOM   2989 C C    A GLY   A 1 133 ? 15.518 -2.367  -9.141  0.40 14.47 ?  133 GLY   A C    1 
ATOM   2990 C C    B GLY   A 1 133 ? 15.335 -2.436  -9.216  0.60 17.08 ?  133 GLY   A C    1 
ATOM   2991 O O    A GLY   A 1 133 ? 14.905 -2.709  -10.159 0.40 15.44 ?  133 GLY   A O    1 
ATOM   2992 O O    B GLY   A 1 133 ? 14.624 -2.745  -10.181 0.60 18.51 ?  133 GLY   A O    1 
ATOM   2993 H H    A GLY   A 1 133 ? 16.210 -0.321  -7.141  0.40 17.02 ?  133 GLY   A H    1 
ATOM   2994 H H    B GLY   A 1 133 ? 15.924 -0.397  -7.147  0.60 18.15 ?  133 GLY   A H    1 
ATOM   2995 H HA2  A GLY   A 1 133 ? 15.085 -0.389  -8.981  0.40 17.26 ?  133 GLY   A HA2  1 
ATOM   2996 H HA2  B GLY   A 1 133 ? 14.834 -0.488  -9.000  0.60 19.49 ?  133 GLY   A HA2  1 
ATOM   2997 H HA3  A GLY   A 1 133 ? 16.401 -0.665  -9.782  0.40 17.26 ?  133 GLY   A HA3  1 
ATOM   2998 H HA3  B GLY   A 1 133 ? 16.174 -0.672  -9.785  0.60 19.49 ?  133 GLY   A HA3  1 
ATOM   2999 N N    A ALA   A 1 134 ? 15.849 -3.236  -8.189  0.40 13.64 ?  134 ALA   A N    1 
ATOM   3000 N N    B ALA   A 1 134 ? 15.803 -3.347  -8.365  0.60 16.51 ?  134 ALA   A N    1 
ATOM   3001 C CA   A ALA   A 1 134 ? 15.473 -4.638  -8.305  0.40 13.66 ?  134 ALA   A CA   1 
ATOM   3002 C CA   B ALA   A 1 134 ? 15.545 -4.762  -8.598  0.60 16.72 ?  134 ALA   A CA   1 
ATOM   3003 C C    A ALA   A 1 134 ? 14.127 -4.897  -7.635  0.40 13.57 ?  134 ALA   A C    1 
ATOM   3004 C C    B ALA   A 1 134 ? 14.191 -5.179  -8.019  0.60 16.98 ?  134 ALA   A C    1 
ATOM   3005 O O    A ALA   A 1 134 ? 13.667 -4.128  -6.788  0.40 14.08 ?  134 ALA   A O    1 
ATOM   3006 O O    B ALA   A 1 134 ? 13.560 -4.454  -7.247  0.60 17.70 ?  134 ALA   A O    1 
ATOM   3007 C CB   A ALA   A 1 134 ? 16.533 -5.546  -7.686  0.40 13.88 ?  134 ALA   A CB   1 
ATOM   3008 C CB   B ALA   A 1 134 ? 16.666 -5.628  -8.022  0.60 17.10 ?  134 ALA   A CB   1 
ATOM   3009 H H    A ALA   A 1 134 ? 16.292 -3.036  -7.476  0.40 16.37 ?  134 ALA   A H    1 
ATOM   3010 H H    B ALA   A 1 134 ? 16.266 -3.170  -7.656  0.60 19.81 ?  134 ALA   A H    1 
ATOM   3011 H HA   A ALA   A 1 134 ? 15.389 -4.861  -9.243  0.40 16.39 ?  134 ALA   A HA   1 
ATOM   3012 H HA   B ALA   A 1 134 ? 15.521 -4.914  -9.558  0.60 20.06 ?  134 ALA   A HA   1 
ATOM   3013 H HB1  A ALA   A 1 134 ? 16.257 -6.465  -7.798  0.40 16.66 ?  134 ALA   A HB1  1 
ATOM   3014 H HB1  B ALA   A 1 134 ? 16.485 -6.556  -8.230  0.60 20.52 ?  134 ALA   A HB1  1 
ATOM   3015 H HB2  A ALA   A 1 134 ? 17.375 -5.389  -8.138  0.40 16.66 ?  134 ALA   A HB2  1 
ATOM   3016 H HB2  B ALA   A 1 134 ? 17.511 -5.358  -8.420  0.60 20.52 ?  134 ALA   A HB2  1 
ATOM   3017 H HB3  A ALA   A 1 134 ? 16.616 -5.332  -6.744  0.40 16.66 ?  134 ALA   A HB3  1 
ATOM   3018 H HB3  B ALA   A 1 134 ? 16.701 -5.502  -7.062  0.60 20.52 ?  134 ALA   A HB3  1 
ATOM   3019 N N    A ASP   A 1 135 ? 13.499 -6.000  -8.038  0.40 13.88 ?  135 ASP   A N    1 
ATOM   3020 N N    B ASP   A 1 135 ? 13.746 -6.368  -8.421  0.60 17.14 ?  135 ASP   A N    1 
ATOM   3021 C CA   A ASP   A 1 135 ? 12.253 -6.454  -7.432  0.40 14.61 ?  135 ASP   A CA   1 
ATOM   3022 C CA   B ASP   A 1 135 ? 12.498 -6.953  -7.934  0.60 17.37 ?  135 ASP   A CA   1 
ATOM   3023 C C    A ASP   A 1 135 ? 12.529 -6.908  -6.003  0.40 14.04 ?  135 ASP   A C    1 
ATOM   3024 C C    B ASP   A 1 135 ? 12.656 -7.325  -6.464  0.60 16.21 ?  135 ASP   A C    1 
ATOM   3025 O O    A ASP   A 1 135 ? 13.282 -7.870  -5.807  0.40 13.90 ?  135 ASP   A O    1 
ATOM   3026 O O    B ASP   A 1 135 ? 13.488 -8.182  -6.142  0.60 15.95 ?  135 ASP   A O    1 
ATOM   3027 C CB   A ASP   A 1 135 ? 11.714 -7.623  -8.251  0.40 16.25 ?  135 ASP   A CB   1 
ATOM   3028 C CB   B ASP   A 1 135 ? 12.201 -8.205  -8.762  0.60 19.83 ?  135 ASP   A CB   1 
ATOM   3029 C CG   A ASP   A 1 135 ? 10.336 -8.081  -7.787  0.40 17.95 ?  135 ASP   A CG   1 
ATOM   3030 C CG   B ASP   A 1 135 ? 10.901 -8.888  -8.360  0.60 22.08 ?  135 ASP   A CG   1 
ATOM   3031 O OD1  A ASP   A 1 135 ? 9.900  -7.676  -6.689  0.40 17.95 ?  135 ASP   A OD1  1 
ATOM   3032 O OD1  B ASP   A 1 135 ? 10.367 -8.588  -7.271  0.60 22.62 ?  135 ASP   A OD1  1 
ATOM   3033 O OD2  A ASP   A 1 135 ? 9.677  -8.834  -8.536  0.40 19.69 -1 135 ASP   A OD2  1 
ATOM   3034 O OD2  B ASP   A 1 135 ? 10.420 -9.741  -9.133  0.60 23.68 -1 135 ASP   A OD2  1 
ATOM   3035 H H    A ASP   A 1 135 ? 13.772 -6.504  -8.674  0.40 16.65 ?  135 ASP   A H    1 
ATOM   3036 H H    B ASP   A 1 135 ? 14.157 -6.864  -8.989  0.60 20.57 ?  135 ASP   A H    1 
ATOM   3037 H HA   A ASP   A 1 135 ? 11.592 -5.739  -7.441  0.40 17.53 ?  135 ASP   A HA   1 
ATOM   3038 H HA   B ASP   A 1 135 ? 11.765 -6.328  -8.049  0.60 20.84 ?  135 ASP   A HA   1 
ATOM   3039 H HB2  A ASP   A 1 135 ? 11.622 -7.347  -9.175  0.40 19.50 ?  135 ASP   A HB2  1 
ATOM   3040 H HB2  B ASP   A 1 135 ? 12.153 -7.959  -9.704  0.60 23.80 ?  135 ASP   A HB2  1 
ATOM   3041 H HB3  A ASP   A 1 135 ? 12.352 -8.361  -8.195  0.40 19.50 ?  135 ASP   A HB3  1 
ATOM   3042 H HB3  B ASP   A 1 135 ? 12.919 -8.847  -8.634  0.60 23.80 ?  135 ASP   A HB3  1 
ATOM   3043 N N    A PRO   A 1 136 ? 11.966 -6.253  -4.983  0.40 13.57 ?  136 PRO   A N    1 
ATOM   3044 N N    B PRO   A 1 136 ? 11.895 -6.722  -5.545  0.60 15.61 ?  136 PRO   A N    1 
ATOM   3045 C CA   A PRO   A 1 136 ? 12.234 -6.691  -3.601  0.40 13.61 ?  136 PRO   A CA   1 
ATOM   3046 C CA   B PRO   A 1 136 ? 12.106 -7.034  -4.120  0.60 15.32 ?  136 PRO   A CA   1 
ATOM   3047 C C    A PRO   A 1 136 ? 11.800 -8.120  -3.309  0.40 12.67 ?  136 PRO   A C    1 
ATOM   3048 C C    B PRO   A 1 136 ? 11.733 -8.454  -3.734  0.60 14.64 ?  136 PRO   A C    1 
ATOM   3049 O O    A PRO   A 1 136 ? 12.384 -8.767  -2.430  0.40 11.49 ?  136 PRO   A O    1 
ATOM   3050 O O    B PRO   A 1 136 ? 12.376 -9.030  -2.848  0.60 14.35 ?  136 PRO   A O    1 
ATOM   3051 C CB   A PRO   A 1 136 ? 11.478 -5.659  -2.749  0.40 14.26 ?  136 PRO   A CB   1 
ATOM   3052 C CB   B PRO   A 1 136 ? 11.248 -5.988  -3.396  0.60 15.78 ?  136 PRO   A CB   1 
ATOM   3053 C CG   A PRO   A 1 136 ? 10.482 -5.042  -3.679  0.40 14.87 ?  136 PRO   A CG   1 
ATOM   3054 C CG   B PRO   A 1 136 ? 10.205 -5.602  -4.390  0.60 16.18 ?  136 PRO   A CG   1 
ATOM   3055 C CD   A PRO   A 1 136 ? 11.097 -5.066  -5.032  0.40 14.18 ?  136 PRO   A CD   1 
ATOM   3056 C CD   B PRO   A 1 136 ? 10.863 -5.688  -5.738  0.60 15.86 ?  136 PRO   A CD   1 
ATOM   3057 H HA   A PRO   A 1 136 ? 13.182 -6.610  -3.407  0.40 16.33 ?  136 PRO   A HA   1 
ATOM   3058 H HA   B PRO   A 1 136 ? 13.039 -6.892  -3.890  0.60 18.38 ?  136 PRO   A HA   1 
ATOM   3059 H HB2  A PRO   A 1 136 ? 11.030 -6.101  -2.013  0.40 17.11 ?  136 PRO   A HB2  1 
ATOM   3060 H HB2  B PRO   A 1 136 ? 10.849 -6.388  -2.606  0.60 18.93 ?  136 PRO   A HB2  1 
ATOM   3061 H HB3  A PRO   A 1 136 ? 12.097 -4.985  -2.420  0.40 17.11 ?  136 PRO   A HB3  1 
ATOM   3062 H HB3  B PRO   A 1 136 ? 11.801 -5.229  -3.154  0.60 18.93 ?  136 PRO   A HB3  1 
ATOM   3063 H HG2  A PRO   A 1 136 ? 9.668  -5.569  -3.675  0.40 17.84 ?  136 PRO   A HG2  1 
ATOM   3064 H HG2  B PRO   A 1 136 ? 9.461  -6.221  -4.334  0.60 19.42 ?  136 PRO   A HG2  1 
ATOM   3065 H HG3  A PRO   A 1 136 ? 10.301 -4.131  -3.408  0.40 17.84 ?  136 PRO   A HG3  1 
ATOM   3066 H HG3  B PRO   A 1 136 ? 9.912  -4.696  -4.212  0.60 19.42 ?  136 PRO   A HG3  1 
ATOM   3067 H HD2  A PRO   A 1 136 ? 10.412 -5.178  -5.712  0.40 17.01 ?  136 PRO   A HD2  1 
ATOM   3068 H HD2  B PRO   A 1 136 ? 10.228 -5.976  -6.411  0.60 19.03 ?  136 PRO   A HD2  1 
ATOM   3069 H HD3  A PRO   A 1 136 ? 11.624 -4.265  -5.187  0.40 17.01 ?  136 PRO   A HD3  1 
ATOM   3070 H HD3  B PRO   A 1 136 ? 11.275 -4.842  -5.975  0.60 19.03 ?  136 PRO   A HD3  1 
ATOM   3071 N N    A ILE   A 1 137 ? 10.788 -8.631  -4.013  0.40 13.22 ?  137 ILE   A N    1 
ATOM   3072 N N    B ILE   A 1 137 ? 10.691 -9.029  -4.341  0.60 14.54 ?  137 ILE   A N    1 
ATOM   3073 C CA   A ILE   A 1 137 ? 10.384 -10.024 -3.828  0.40 13.83 ?  137 ILE   A CA   1 
ATOM   3074 C CA   B ILE   A 1 137 ? 10.388 -10.437 -4.102  0.60 15.39 ?  137 ILE   A CA   1 
ATOM   3075 C C    A ILE   A 1 137 ? 11.516 -10.960 -4.231  0.40 14.00 ?  137 ILE   A C    1 
ATOM   3076 C C    B ILE   A 1 137 ? 11.597 -11.285 -4.452  0.60 15.23 ?  137 ILE   A C    1 
ATOM   3077 O O    A ILE   A 1 137 ? 11.819 -11.936 -3.532  0.40 13.91 ?  137 ILE   A O    1 
ATOM   3078 O O    B ILE   A 1 137 ? 11.954 -12.226 -3.731  0.60 15.11 ?  137 ILE   A O    1 
ATOM   3079 C CB   A ILE   A 1 137 ? 9.091  -10.317 -4.614  0.40 14.44 ?  137 ILE   A CB   1 
ATOM   3080 C CB   B ILE   A 1 137 ? 9.138  -10.866 -4.897  0.60 16.45 ?  137 ILE   A CB   1 
ATOM   3081 C CG1  A ILE   A 1 137 ? 7.940  -9.451  -4.094  0.40 15.07 ?  137 ILE   A CG1  1 
ATOM   3082 C CG1  B ILE   A 1 137 ? 7.904  -10.087 -4.441  0.60 17.37 ?  137 ILE   A CG1  1 
ATOM   3083 C CG2  A ILE   A 1 137 ? 8.732  -11.795 -4.527  0.40 15.11 ?  137 ILE   A CG2  1 
ATOM   3084 C CG2  B ILE   A 1 137 ? 8.894  -12.368 -4.751  0.60 16.98 ?  137 ILE   A CG2  1 
ATOM   3085 C CD1  A ILE   A 1 137 ? 6.640  -9.663  -4.832  0.40 16.02 ?  137 ILE   A CD1  1 
ATOM   3086 C CD1  B ILE   A 1 137 ? 6.688  -10.296 -5.332  0.60 18.40 ?  137 ILE   A CD1  1 
ATOM   3087 H H    A ILE   A 1 137 ? 10.326 -8.191  -4.593  0.40 15.86 ?  137 ILE   A H    1 
ATOM   3088 H H    B ILE   A 1 137 ? 10.157 -8.637  -4.886  0.60 17.44 ?  137 ILE   A H    1 
ATOM   3089 H HA   A ILE   A 1 137 ? 10.195 -10.168 -2.890  0.40 16.59 ?  137 ILE   A HA   1 
ATOM   3090 H HA   B ILE   A 1 137 ? 10.200 -10.575 -3.165  0.60 18.47 ?  137 ILE   A HA   1 
ATOM   3091 H HB   A ILE   A 1 137 ? 9.240  -10.091 -5.544  0.40 17.33 ?  137 ILE   A HB   1 
ATOM   3092 H HB   B ILE   A 1 137 ? 9.283  -10.678 -5.836  0.60 19.74 ?  137 ILE   A HB   1 
ATOM   3093 H HG12 A ILE   A 1 137 ? 7.788  -9.656  -3.159  0.40 18.08 ?  137 ILE   A HG12 1 
ATOM   3094 H HG12 B ILE   A 1 137 ? 7.664  -10.373 -3.545  0.60 20.84 ?  137 ILE   A HG12 1 
ATOM   3095 H HG13 A ILE   A 1 137 ? 8.181  -8.515  -4.191  0.40 18.08 ?  137 ILE   A HG13 1 
ATOM   3096 H HG13 B ILE   A 1 137 ? 8.112  -9.141  -4.442  0.60 20.84 ?  137 ILE   A HG13 1 
ATOM   3097 H HG21 A ILE   A 1 137 ? 7.876  -11.949 -4.952  0.40 18.13 ?  137 ILE   A HG21 1 
ATOM   3098 H HG21 B ILE   A 1 137 ? 8.037  -12.598 -5.146  0.60 20.38 ?  137 ILE   A HG21 1 
ATOM   3099 H HG22 A ILE   A 1 137 ? 9.414  -12.310 -4.982  0.40 18.13 ?  137 ILE   A HG22 1 
ATOM   3100 H HG22 B ILE   A 1 137 ? 9.598  -12.851 -5.209  0.60 20.38 ?  137 ILE   A HG22 1 
ATOM   3101 H HG23 A ILE   A 1 137 ? 8.688  -12.050 -3.594  0.40 18.13 ?  137 ILE   A HG23 1 
ATOM   3102 H HG23 B ILE   A 1 137 ? 8.892  -12.596 -3.809  0.60 20.38 ?  137 ILE   A HG23 1 
ATOM   3103 H HD11 A ILE   A 1 137 ? 6.286  -8.799  -5.080  0.40 19.23 ?  137 ILE   A HD11 1 
ATOM   3104 H HD11 B ILE   A 1 137 ? 5.992  -9.681  -5.058  0.60 22.07 ?  137 ILE   A HD11 1 
ATOM   3105 H HD12 A ILE   A 1 137 ? 6.806  -10.189 -5.631  0.40 19.23 ?  137 ILE   A HD12 1 
ATOM   3106 H HD12 B ILE   A 1 137 ? 6.940  -10.121 -6.254  0.60 22.07 ?  137 ILE   A HD12 1 
ATOM   3107 H HD13 A ILE   A 1 137 ? 6.016  -10.131 -4.252  0.40 19.23 ?  137 ILE   A HD13 1 
ATOM   3108 H HD13 B ILE   A 1 137 ? 6.376  -11.208 -5.241  0.60 22.07 ?  137 ILE   A HD13 1 
ATOM   3109 N N    A HIS   A 1 138 ? 12.153 -10.679 -5.371  0.40 14.37 ?  138 HIS   A N    1 
ATOM   3110 N N    B HIS   A 1 138 ? 12.251 -10.956 -5.566  0.60 15.38 ?  138 HIS   A N    1 
ATOM   3111 C CA   A HIS   A 1 138 ? 13.268 -11.504 -5.826  0.40 14.37 ?  138 HIS   A CA   1 
ATOM   3112 C CA   B HIS   A 1 138 ? 13.475 -11.650 -5.932  0.60 15.49 ?  138 HIS   A CA   1 
ATOM   3113 C C    A HIS   A 1 138 ? 14.439 -11.421 -4.857  0.40 13.89 ?  138 HIS   A C    1 
ATOM   3114 C C    B HIS   A 1 138 ? 14.563 -11.446 -4.884  0.60 14.44 ?  138 HIS   A C    1 
ATOM   3115 O O    A HIS   A 1 138 ? 15.061 -12.435 -4.523  0.40 14.21 ?  138 HIS   A O    1 
ATOM   3116 O O    B HIS   A 1 138 ? 15.251 -12.401 -4.508  0.60 14.44 ?  138 HIS   A O    1 
ATOM   3117 C CB   A HIS   A 1 138 ? 13.689 -11.055 -7.226  0.40 14.71 ?  138 HIS   A CB   1 
ATOM   3118 C CB   B HIS   A 1 138 ? 13.946 -11.200 -7.313  0.60 16.62 ?  138 HIS   A CB   1 
ATOM   3119 C CG   A HIS   A 1 138 ? 14.990 -11.637 -7.682  0.40 15.22 ?  138 HIS   A CG   1 
ATOM   3120 C CG   B HIS   A 1 138 ? 15.196 -11.884 -7.766  0.60 17.78 ?  138 HIS   A CG   1 
ATOM   3121 N ND1  A HIS   A 1 138 ? 15.159 -12.983 -7.928  0.40 16.10 ?  138 HIS   A ND1  1 
ATOM   3122 N ND1  B HIS   A 1 138 ? 15.253 -13.236 -8.029  0.60 18.94 ?  138 HIS   A ND1  1 
ATOM   3123 C CD2  A HIS   A 1 138 ? 16.187 -11.055 -7.933  0.40 15.20 ?  138 HIS   A CD2  1 
ATOM   3124 C CD2  B HIS   A 1 138 ? 16.444 -11.405 -7.981  0.60 18.18 ?  138 HIS   A CD2  1 
ATOM   3125 C CE1  A HIS   A 1 138 ? 16.403 -13.204 -8.315  0.40 15.94 ?  138 HIS   A CE1  1 
ATOM   3126 C CE1  B HIS   A 1 138 ? 16.478 -13.557 -8.402  0.60 19.30 ?  138 HIS   A CE1  1 
ATOM   3127 N NE2  A HIS   A 1 138 ? 17.048 -12.052 -8.326  0.40 15.39 ?  138 HIS   A NE2  1 
ATOM   3128 N NE2  B HIS   A 1 138 ? 17.221 -12.465 -8.379  0.60 18.56 ?  138 HIS   A NE2  1 
ATOM   3129 H H    A HIS   A 1 138 ? 11.960 -10.019 -5.893  0.40 17.24 ?  138 HIS   A H    1 
ATOM   3130 H H    B HIS   A 1 138 ? 12.006 -10.340 -6.123  0.60 18.46 ?  138 HIS   A H    1 
ATOM   3131 H HA   A HIS   A 1 138 ? 12.981 -12.425 -5.875  0.40 17.25 ?  138 HIS   A HA   1 
ATOM   3132 H HA   B HIS   A 1 138 ? 13.289 -12.598 -5.987  0.60 18.59 ?  138 HIS   A HA   1 
ATOM   3133 H HB2  A HIS   A 1 138 ? 13.004 -11.327 -7.860  0.40 17.65 ?  138 HIS   A HB2  1 
ATOM   3134 H HB2  B HIS   A 1 138 ? 13.249 -11.391 -7.964  0.60 19.95 ?  138 HIS   A HB2  1 
ATOM   3135 H HB3  A HIS   A 1 138 ? 13.777 -10.089 -7.235  0.40 17.65 ?  138 HIS   A HB3  1 
ATOM   3136 H HB3  B HIS   A 1 138 ? 14.122 -10.247 -7.293  0.60 19.95 ?  138 HIS   A HB3  1 
ATOM   3137 H HD1  A HIS   A 1 138 ? 14.548 -13.583 -7.846  0.40 19.32 ?  138 HIS   A HD1  1 
ATOM   3138 H HD2  A HIS   A 1 138 ? 16.386 -10.150 -7.858  0.40 18.24 ?  138 HIS   A HD2  1 
ATOM   3139 H HD2  B HIS   A 1 138 ? 16.719 -10.524 -7.883  0.60 21.81 ?  138 HIS   A HD2  1 
ATOM   3140 H HE1  A HIS   A 1 138 ? 16.763 -14.031 -8.540  0.40 19.13 ?  138 HIS   A HE1  1 
ATOM   3141 H HE1  B HIS   A 1 138 ? 16.767 -14.408 -8.636  0.60 23.16 ?  138 HIS   A HE1  1 
ATOM   3142 H HE2  B HIS   A 1 138 ? 18.055 -12.425 -8.579  0.60 22.27 ?  138 HIS   A HE2  1 
ATOM   3143 N N    . SER   A 1 139 ? 14.748 -10.212 -4.397  1.00 13.81 ?  139 SER   A N    1 
ATOM   3144 C CA   . SER   A 1 139 ? 15.816 -10.008 -3.428  1.00 13.56 ?  139 SER   A CA   1 
ATOM   3145 C C    . SER   A 1 139 ? 15.595 -10.828 -2.164  1.00 12.79 ?  139 SER   A C    1 
ATOM   3146 O O    . SER   A 1 139 ? 16.546 -11.397 -1.618  1.00 12.56 ?  139 SER   A O    1 
ATOM   3147 C CB   . SER   A 1 139 ? 15.945 -8.526  -3.095  1.00 13.73 ?  139 SER   A CB   1 
ATOM   3148 O OG   . SER   A 1 139 ? 17.012 -8.343  -2.188  1.00 13.85 ?  139 SER   A OG   1 
ATOM   3149 H H    A SER   A 1 139 ? 14.345 -9.487  -4.630  0.40 16.57 ?  139 SER   A H    1 
ATOM   3150 H H    B SER   A 1 139 ? 14.294 -9.511  -4.605  0.60 16.57 ?  139 SER   A H    1 
ATOM   3151 H HA   . SER   A 1 139 ? 16.656 -10.290 -3.819  1.00 16.27 ?  139 SER   A HA   1 
ATOM   3152 H HB2  . SER   A 1 139 ? 16.125 -8.019  -3.906  1.00 16.47 ?  139 SER   A HB2  1 
ATOM   3153 H HB3  . SER   A 1 139 ? 15.122 -8.209  -2.684  1.00 16.47 ?  139 SER   A HB3  1 
ATOM   3154 H HG   . SER   A 1 139 ? 17.744 -8.557  -2.552  1.00 16.61 ?  139 SER   A HG   1 
ATOM   3155 N N    . LEU   A 1 140 ? 14.357 -10.884 -1.674  1.00 12.65 ?  140 LEU   A N    1 
ATOM   3156 C CA   . LEU   A 1 140 ? 14.082 -11.677 -0.480  1.00 12.32 ?  140 LEU   A CA   1 
ATOM   3157 C C    . LEU   A 1 140 ? 14.354 -13.157 -0.732  1.00 12.31 ?  140 LEU   A C    1 
ATOM   3158 O O    . LEU   A 1 140 ? 14.905 -13.854 0.130   1.00 12.73 ?  140 LEU   A O    1 
ATOM   3159 C CB   . LEU   A 1 140 ? 12.641 -11.447 -0.029  1.00 12.70 ?  140 LEU   A CB   1 
ATOM   3160 C CG   . LEU   A 1 140 ? 12.195 -12.250 1.190   1.00 13.39 ?  140 LEU   A CG   1 
ATOM   3161 C CD1  . LEU   A 1 140 ? 13.111 -12.046 2.392   1.00 13.76 ?  140 LEU   A CD1  1 
ATOM   3162 C CD2  . LEU   A 1 140 ? 10.745 -11.915 1.539   1.00 13.98 ?  140 LEU   A CD2  1 
ATOM   3163 H H    . LEU   A 1 140 ? 13.675 -10.474 -2.004  1.00 15.17 ?  140 LEU   A H    1 
ATOM   3164 H HA   . LEU   A 1 140 ? 14.668 -11.386 0.231   1.00 14.78 ?  140 LEU   A HA   1 
ATOM   3165 H HB2  . LEU   A 1 140 ? 12.530 -10.515 0.185   1.00 15.24 ?  140 LEU   A HB2  1 
ATOM   3166 H HB3  . LEU   A 1 140 ? 12.051 -11.690 -0.762  1.00 15.24 ?  140 LEU   A HB3  1 
ATOM   3167 H HG   . LEU   A 1 140 ? 12.216 -13.197 0.965   1.00 16.07 ?  140 LEU   A HG   1 
ATOM   3168 H HD11 . LEU   A 1 140 ? 12.736 -12.509 3.159   1.00 16.51 ?  140 LEU   A HD11 1 
ATOM   3169 H HD12 . LEU   A 1 140 ? 13.986 -12.414 2.185   1.00 16.51 ?  140 LEU   A HD12 1 
ATOM   3170 H HD13 . LEU   A 1 140 ? 13.182 -11.101 2.578   1.00 16.51 ?  140 LEU   A HD13 1 
ATOM   3171 H HD21 . LEU   A 1 140 ? 10.476 -12.435 2.317   1.00 16.77 ?  140 LEU   A HD21 1 
ATOM   3172 H HD22 . LEU   A 1 140 ? 10.678 -10.969 1.738   1.00 16.77 ?  140 LEU   A HD22 1 
ATOM   3173 H HD23 . LEU   A 1 140 ? 10.175 -12.138 0.785   1.00 16.77 ?  140 LEU   A HD23 1 
ATOM   3174 N N    . ARG   A 1 141 ? 13.967 -13.653 -1.913  1.00 12.98 ?  141 ARG   A N    1 
ATOM   3175 C CA   . ARG   A 1 141 ? 14.216 -15.047 -2.259  1.00 14.06 ?  141 ARG   A CA   1 
ATOM   3176 C C    . ARG   A 1 141 ? 15.712 -15.338 -2.273  1.00 13.48 ?  141 ARG   A C    1 
ATOM   3177 O O    . ARG   A 1 141 ? 16.170 -16.336 -1.702  1.00 13.72 ?  141 ARG   A O    1 
ATOM   3178 C CB   . ARG   A 1 141 ? 13.591 -15.343 -3.626  1.00 16.02 ?  141 ARG   A CB   1 
ATOM   3179 C CG   . ARG   A 1 141 ? 13.612 -16.798 -4.057  1.00 19.05 ?  141 ARG   A CG   1 
ATOM   3180 C CD   . ARG   A 1 141 ? 12.574 -17.576 -3.316  1.00 21.70 ?  141 ARG   A CD   1 
ATOM   3181 N NE   . ARG   A 1 141 ? 13.165 -18.351 -2.238  1.00 22.80 ?  141 ARG   A NE   1 
ATOM   3182 C CZ   . ARG   A 1 141 ? 12.470 -18.889 -1.245  1.00 23.39 ?  141 ARG   A CZ   1 
ATOM   3183 N NH1  . ARG   A 1 141 ? 11.183 -18.627 -1.081  1.00 23.09 ?  141 ARG   A NH1  1 
ATOM   3184 N NH2  . ARG   A 1 141 ? 13.084 -19.701 -0.390  1.00 24.40 ?  141 ARG   A NH2  1 
ATOM   3185 H H    . ARG   A 1 141 ? 13.574 -13.202 -2.535  1.00 15.58 ?  141 ARG   A H    1 
ATOM   3186 H HA   . ARG   A 1 141 ? 13.804 -15.623 -1.603  1.00 16.87 ?  141 ARG   A HA   1 
ATOM   3187 H HB2  . ARG   A 1 141 ? 12.667 -15.051 -3.612  1.00 19.22 ?  141 ARG   A HB2  1 
ATOM   3188 H HB3  . ARG   A 1 141 ? 14.076 -14.839 -4.300  1.00 19.22 ?  141 ARG   A HB3  1 
ATOM   3189 H HG2  . ARG   A 1 141 ? 13.424 -16.860 -5.008  1.00 22.85 ?  141 ARG   A HG2  1 
ATOM   3190 H HG3  . ARG   A 1 141 ? 14.483 -17.186 -3.863  1.00 22.85 ?  141 ARG   A HG3  1 
ATOM   3191 H HD2  . ARG   A 1 141 ? 11.930 -16.966 -2.921  1.00 26.04 ?  141 ARG   A HD2  1 
ATOM   3192 H HD3  . ARG   A 1 141 ? 12.122 -18.179 -3.931  1.00 26.04 ?  141 ARG   A HD3  1 
ATOM   3193 H HE   . ARG   A 1 141 ? 13.988 -18.583 -2.319  1.00 27.35 ?  141 ARG   A HE   1 
ATOM   3194 H HH11 . ARG   A 1 141 ? 10.768 -18.118 -1.636  1.00 27.70 ?  141 ARG   A HH11 1 
ATOM   3195 H HH12 . ARG   A 1 141 ? 10.751 -18.985 -0.426  1.00 27.70 ?  141 ARG   A HH12 1 
ATOM   3196 H HH21 . ARG   A 1 141 ? 13.920 -19.878 -0.488  1.00 29.28 ?  141 ARG   A HH21 1 
ATOM   3197 H HH22 . ARG   A 1 141 ? 12.647 -20.046 0.267   1.00 29.28 ?  141 ARG   A HH22 1 
ATOM   3198 N N    . VAL   A 1 142 ? 16.497 -14.471 -2.920  1.00 12.90 ?  142 VAL   A N    1 
ATOM   3199 C CA   . VAL   A 1 142 ? 17.943 -14.677 -2.950  1.00 12.99 ?  142 VAL   A CA   1 
ATOM   3200 C C    . VAL   A 1 142 ? 18.509 -14.643 -1.537  1.00 12.18 ?  142 VAL   A C    1 
ATOM   3201 O O    . VAL   A 1 142 ? 19.375 -15.450 -1.181  1.00 12.52 ?  142 VAL   A O    1 
ATOM   3202 C CB   . VAL   A 1 142 ? 18.638 -13.661 -3.877  1.00 13.17 ?  142 VAL   A CB   1 
ATOM   3203 C CG1  . VAL   A 1 142 ? 20.153 -13.873 -3.845  1.00 13.14 ?  142 VAL   A CG1  1 
ATOM   3204 C CG2  . VAL   A 1 142 ? 18.140 -13.793 -5.300  1.00 14.65 ?  142 VAL   A CG2  1 
ATOM   3205 H H    . VAL   A 1 142 ? 16.227 -13.763 -3.336  1.00 15.48 ?  142 VAL   A H    1 
ATOM   3206 H HA   . VAL   A 1 142 ? 18.122 -15.554 -3.313  1.00 15.58 ?  142 VAL   A HA   1 
ATOM   3207 H HB   . VAL   A 1 142 ? 18.461 -12.756 -3.570  1.00 15.80 ?  142 VAL   A HB   1 
ATOM   3208 H HG11 . VAL   A 1 142 ? 20.558 -13.390 -4.583  1.00 15.76 ?  142 VAL   A HG11 1 
ATOM   3209 H HG12 . VAL   A 1 142 ? 20.506 -13.543 -3.004  1.00 15.76 ?  142 VAL   A HG12 1 
ATOM   3210 H HG13 . VAL   A 1 142 ? 20.339 -14.822 -3.933  1.00 15.76 ?  142 VAL   A HG13 1 
ATOM   3211 H HG21 . VAL   A 1 142 ? 18.600 -13.143 -5.857  1.00 17.58 ?  142 VAL   A HG21 1 
ATOM   3212 H HG22 . VAL   A 1 142 ? 18.329 -14.689 -5.614  1.00 17.58 ?  142 VAL   A HG22 1 
ATOM   3213 H HG23 . VAL   A 1 142 ? 17.189 -13.626 -5.312  1.00 17.58 ?  142 VAL   A HG23 1 
ATOM   3214 N N    . CYS   A 1 143 ? 18.037 -13.710 -0.713  1.00 11.98 ?  143 CYS   A N    1 
ATOM   3215 C CA   . CYS   A 1 143 ? 18.496 -13.647 0.670   1.00 12.03 ?  143 CYS   A CA   1 
ATOM   3216 C C    . CYS   A 1 143 ? 18.279 -14.980 1.378   1.00 12.16 ?  143 CYS   A C    1 
ATOM   3217 O O    . CYS   A 1 143 ? 19.206 -15.552 1.958   1.00 12.42 ?  143 CYS   A O    1 
ATOM   3218 C CB   . CYS   A 1 143 ? 17.759 -12.530 1.406   1.00 12.54 ?  143 CYS   A CB   1 
ATOM   3219 S SG   . CYS   A 1 143 ? 18.254 -12.338 3.124   1.00 13.08 ?  143 CYS   A SG   1 
ATOM   3220 H H    . CYS   A 1 143 ? 17.465 -13.107 -0.929  1.00 14.37 ?  143 CYS   A H    1 
ATOM   3221 H HA   . CYS   A 1 143 ? 19.443 -13.454 0.687   1.00 14.44 ?  143 CYS   A HA   1 
ATOM   3222 H HB2  . CYS   A 1 143 ? 17.927 -11.692 0.951   1.00 15.05 ?  143 CYS   A HB2  1 
ATOM   3223 H HB3  . CYS   A 1 143 ? 16.808 -12.722 1.390   1.00 15.05 ?  143 CYS   A HB3  1 
ATOM   3224 H HG   . CYS   A 1 143 ? 17.668 -11.403 3.589   1.00 15.70 ?  143 CYS   A HG   1 
ATOM   3225 N N    . VAL   A 1 144 ? 17.049 -15.489 1.336   1.00 12.80 ?  144 VAL   A N    1 
ATOM   3226 C CA   . VAL   A 1 144 ? 16.718 -16.711 2.056   1.00 14.36 ?  144 VAL   A CA   1 
ATOM   3227 C C    . VAL   A 1 144 ? 17.525 -17.887 1.531   1.00 14.53 ?  144 VAL   A C    1 
ATOM   3228 O O    . VAL   A 1 144 ? 17.891 -18.793 2.291   1.00 15.01 ?  144 VAL   A O    1 
ATOM   3229 C CB   . VAL   A 1 144 ? 15.198 -16.944 1.954   1.00 17.72 ?  144 VAL   A CB   1 
ATOM   3230 C CG1  . VAL   A 1 144 ? 14.825 -18.385 2.259   1.00 19.82 ?  144 VAL   A CG1  1 
ATOM   3231 C CG2  . VAL   A 1 144 ? 14.465 -15.936 2.856   1.00 17.33 ?  144 VAL   A CG2  1 
ATOM   3232 H H    . VAL   A 1 144 ? 16.386 -15.141 0.898   1.00 15.36 ?  144 VAL   A H    1 
ATOM   3233 H HA   . VAL   A 1 144 ? 16.929 -16.590 2.989   1.00 17.23 ?  144 VAL   A HA   1 
ATOM   3234 H HB   . VAL   A 1 144 ? 14.914 -16.758 1.042   1.00 21.26 ?  144 VAL   A HB   1 
ATOM   3235 H HG11 . VAL   A 1 144 ? 13.867 -18.435 2.420   1.00 23.78 ?  144 VAL   A HG11 1 
ATOM   3236 H HG12 . VAL   A 1 144 ? 15.056 -18.939 1.498   1.00 23.78 ?  144 VAL   A HG12 1 
ATOM   3237 H HG13 . VAL   A 1 144 ? 15.307 -18.675 3.046   1.00 23.78 ?  144 VAL   A HG13 1 
ATOM   3238 H HG21 . VAL   A 1 144 ? 13.505 -16.096 2.809   1.00 20.79 ?  144 VAL   A HG21 1 
ATOM   3239 H HG22 . VAL   A 1 144 ? 14.768 -16.043 3.770   1.00 20.79 ?  144 VAL   A HG22 1 
ATOM   3240 H HG23 . VAL   A 1 144 ? 14.655 -15.031 2.551   1.00 20.79 ?  144 VAL   A HG23 1 
ATOM   3241 N N    . ASP   A 1 145 ? 17.785 -17.914 0.227   1.00 14.79 ?  145 ASP   A N    1 
ATOM   3242 C CA   . ASP   A 1 145 ? 18.495 -19.023 -0.401  1.00 15.31 ?  145 ASP   A CA   1 
ATOM   3243 C C    . ASP   A 1 145 ? 20.015 -18.877 -0.359  1.00 14.63 ?  145 ASP   A C    1 
ATOM   3244 O O    . ASP   A 1 145 ? 20.720 -19.774 -0.832  1.00 16.61 ?  145 ASP   A O    1 
ATOM   3245 C CB   . ASP   A 1 145 ? 18.050 -19.161 -1.858  1.00 17.41 ?  145 ASP   A CB   1 
ATOM   3246 C CG   . ASP   A 1 145 ? 16.607 -19.615 -1.992  1.00 19.91 ?  145 ASP   A CG   1 
ATOM   3247 O OD1  . ASP   A 1 145 ? 16.049 -20.158 -1.017  1.00 20.45 ?  145 ASP   A OD1  1 
ATOM   3248 O OD2  . ASP   A 1 145 ? 16.034 -19.423 -3.082  1.00 21.62 -1 145 ASP   A OD2  1 
ATOM   3249 H H    . ASP   A 1 145 ? 17.543 -17.299 -0.324  1.00 17.74 ?  145 ASP   A H    1 
ATOM   3250 H HA   . ASP   A 1 145 ? 18.260 -19.843 0.059   1.00 18.36 ?  145 ASP   A HA   1 
ATOM   3251 H HB2  . ASP   A 1 145 ? 18.137 -18.302 -2.299  1.00 20.89 ?  145 ASP   A HB2  1 
ATOM   3252 H HB3  . ASP   A 1 145 ? 18.605 -19.822 -2.296  1.00 20.89 ?  145 ASP   A HB3  1 
ATOM   3253 N N    . THR   A 1 146 ? 20.541 -17.781 0.179   1.00 12.84 ?  146 THR   A N    1 
ATOM   3254 C CA   . THR   A 1 146 ? 21.983 -17.533 0.196   1.00 12.41 ?  146 THR   A CA   1 
ATOM   3255 C C    . THR   A 1 146 ? 22.537 -17.341 1.593   1.00 12.35 ?  146 THR   A C    1 
ATOM   3256 O O    . THR   A 1 146 ? 23.618 -17.855 1.903   1.00 13.51 ?  146 THR   A O    1 
ATOM   3257 C CB   . THR   A 1 146 ? 22.309 -16.284 -0.645  1.00 12.41 ?  146 THR   A CB   1 
ATOM   3258 O OG1  . THR   A 1 146 ? 21.784 -16.451 -1.965  1.00 12.88 ?  146 THR   A OG1  1 
ATOM   3259 C CG2  . THR   A 1 146 ? 23.812 -16.049 -0.723  1.00 13.10 ?  146 THR   A CG2  1 
ATOM   3260 H H    . THR   A 1 146 ? 20.079 -17.152 0.543   1.00 15.40 ?  146 THR   A H    1 
ATOM   3261 H HA   . THR   A 1 146 ? 22.440 -18.287 -0.200  1.00 14.89 ?  146 THR   A HA   1 
ATOM   3262 H HB   . THR   A 1 146 ? 21.907 -15.507 -0.238  1.00 14.89 ?  146 THR   A HB   1 
ATOM   3263 H HG1  . THR   A 1 146 ? 20.949 -16.529 -1.935  1.00 15.45 ?  146 THR   A HG1  1 
ATOM   3264 H HG21 . THR   A 1 146 ? 24.007 -15.400 -1.412  1.00 15.71 ?  146 THR   A HG21 1 
ATOM   3265 H HG22 . THR   A 1 146 ? 24.139 -15.724 0.127   1.00 15.71 ?  146 THR   A HG22 1 
ATOM   3266 H HG23 . THR   A 1 146 ? 24.263 -16.884 -0.939  1.00 15.71 ?  146 THR   A HG23 1 
ATOM   3267 N N    . VAL   A 1 147 ? 21.860 -16.560 2.424   1.00 12.24 ?  147 VAL   A N    1 
ATOM   3268 C CA   . VAL   A 1 147 ? 22.354 -16.263 3.761   1.00 12.50 ?  147 VAL   A CA   1 
ATOM   3269 C C    . VAL   A 1 147 ? 22.034 -17.431 4.681   1.00 12.40 ?  147 VAL   A C    1 
ATOM   3270 O O    . VAL   A 1 147 ? 20.892 -17.899 4.739   1.00 13.33 ?  147 VAL   A O    1 
ATOM   3271 C CB   . VAL   A 1 147 ? 21.744 -14.954 4.283   1.00 12.22 ?  147 VAL   A CB   1 
ATOM   3272 C CG1  . VAL   A 1 147 ? 22.300 -14.638 5.649   1.00 13.48 ?  147 VAL   A CG1  1 
ATOM   3273 C CG2  . VAL   A 1 147 ? 21.991 -13.813 3.304   1.00 12.11 ?  147 VAL   A CG2  1 
ATOM   3274 H H    . VAL   A 1 147 ? 21.105 -16.189 2.239   1.00 14.68 ?  147 VAL   A H    1 
ATOM   3275 H HA   . VAL   A 1 147 ? 23.317 -16.154 3.724   1.00 14.99 ?  147 VAL   A HA   1 
ATOM   3276 H HB   . VAL   A 1 147 ? 20.787 -15.069 4.374   1.00 14.67 ?  147 VAL   A HB   1 
ATOM   3277 H HG11 . VAL   A 1 147 ? 22.058 -13.732 5.886   1.00 16.17 ?  147 VAL   A HG11 1 
ATOM   3278 H HG12 . VAL   A 1 147 ? 21.930 -15.260 6.295   1.00 16.17 ?  147 VAL   A HG12 1 
ATOM   3279 H HG13 . VAL   A 1 147 ? 23.268 -14.725 5.623   1.00 16.17 ?  147 VAL   A HG13 1 
ATOM   3280 H HG21 . VAL   A 1 147 ? 21.677 -12.988 3.703   1.00 14.54 ?  147 VAL   A HG21 1 
ATOM   3281 H HG22 . VAL   A 1 147 ? 22.938 -13.757 3.120   1.00 14.54 ?  147 VAL   A HG22 1 
ATOM   3282 H HG23 . VAL   A 1 147 ? 21.501 -13.993 2.486   1.00 14.54 ?  147 VAL   A HG23 1 
ATOM   3283 N N    . ARG   A 1 148 ? 23.055 -17.896 5.399   1.00 12.59 ?  148 ARG   A N    1 
ATOM   3284 C CA   . ARG   A 1 148 ? 22.931 -18.966 6.370   1.00 12.85 ?  148 ARG   A CA   1 
ATOM   3285 C C    . ARG   A 1 148 ? 23.050 -18.489 7.804   1.00 13.47 ?  148 ARG   A C    1 
ATOM   3286 O O    . ARG   A 1 148 ? 22.642 -19.216 8.719   1.00 15.09 ?  148 ARG   A O    1 
ATOM   3287 C CB   . ARG   A 1 148 ? 23.980 -20.053 6.094   1.00 13.81 ?  148 ARG   A CB   1 
ATOM   3288 C CG   . ARG   A 1 148 ? 23.799 -20.718 4.740   1.00 15.59 ?  148 ARG   A CG   1 
ATOM   3289 C CD   . ARG   A 1 148 ? 24.885 -21.744 4.437   1.00 16.29 ?  148 ARG   A CD   1 
ATOM   3290 N NE   . ARG   A 1 148 ? 26.225 -21.160 4.458   1.00 15.97 ?  148 ARG   A NE   1 
ATOM   3291 C CZ   . ARG   A 1 148 ? 26.736 -20.422 3.481   1.00 15.12 ?  148 ARG   A CZ   1 
ATOM   3292 N NH1  . ARG   A 1 148 ? 26.064 -20.192 2.365   1.00 15.52 ?  148 ARG   A NH1  1 
ATOM   3293 N NH2  . ARG   A 1 148 ? 27.950 -19.885 3.633   1.00 15.53 ?  148 ARG   A NH2  1 
ATOM   3294 H H    . ARG   A 1 148 ? 23.861 -17.583 5.332   1.00 15.10 ?  148 ARG   A H    1 
ATOM   3295 H HA   . ARG   A 1 148 ? 22.059 -19.366 6.269   1.00 15.41 ?  148 ARG   A HA   1 
ATOM   3296 H HB2  . ARG   A 1 148 ? 24.863 -19.663 6.119   1.00 16.57 ?  148 ARG   A HB2  1 
ATOM   3297 H HB3  . ARG   A 1 148 ? 23.900 -20.745 6.773   1.00 16.57 ?  148 ARG   A HB3  1 
ATOM   3298 H HG2  . ARG   A 1 148 ? 22.937 -21.165 4.722   1.00 18.71 ?  148 ARG   A HG2  1 
ATOM   3299 H HG3  . ARG   A 1 148 ? 23.825 -20.030 4.052   1.00 18.71 ?  148 ARG   A HG3  1 
ATOM   3300 H HD2  . ARG   A 1 148 ? 24.848 -22.443 5.105   1.00 19.55 ?  148 ARG   A HD2  1 
ATOM   3301 H HD3  . ARG   A 1 148 ? 24.727 -22.115 3.554   1.00 19.55 ?  148 ARG   A HD3  1 
ATOM   3302 H HE   . ARG   A 1 148 ? 26.708 -21.302 5.148   1.00 19.17 ?  148 ARG   A HE   1 
ATOM   3303 H HH11 . ARG   A 1 148 ? 25.279 -20.525 2.253   1.00 18.62 ?  148 ARG   A HH11 1 
ATOM   3304 H HH12 . ARG   A 1 148 ? 26.414 -19.706 1.746   1.00 18.62 ?  148 ARG   A HH12 1 
ATOM   3305 H HH21 . ARG   A 1 148 ? 28.385 -20.016 4.359   1.00 18.63 ?  148 ARG   A HH21 1 
ATOM   3306 H HH22 . ARG   A 1 148 ? 28.283 -19.397 3.009   1.00 18.63 ?  148 ARG   A HH22 1 
ATOM   3307 N N    . THR   A 1 149 ? 23.599 -17.298 8.017   1.00 13.31 ?  149 THR   A N    1 
ATOM   3308 C CA   . THR   A 1 149 ? 23.678 -16.701 9.335   1.00 13.60 ?  149 THR   A CA   1 
ATOM   3309 C C    . THR   A 1 149 ? 22.355 -16.002 9.644   1.00 12.94 ?  149 THR   A C    1 
ATOM   3310 O O    . THR   A 1 149 ? 21.422 -15.991 8.832   1.00 13.73 ?  149 THR   A O    1 
ATOM   3311 C CB   . THR   A 1 149 ? 24.879 -15.768 9.391   1.00 13.76 ?  149 THR   A CB   1 
ATOM   3312 O OG1  . THR   A 1 149 ? 24.752 -14.836 8.314   1.00 13.79 ?  149 THR   A OG1  1 
ATOM   3313 C CG2  . THR   A 1 149 ? 26.182 -16.567 9.259   1.00 14.43 ?  149 THR   A CG2  1 
ATOM   3314 H H    . THR   A 1 149 ? 23.945 -16.804 7.397   1.00 15.97 ?  149 THR   A H    1 
ATOM   3315 H HA   . THR   A 1 149 ? 23.805 -17.403 9.991   1.00 16.32 ?  149 THR   A HA   1 
ATOM   3316 H HB   . THR   A 1 149 ? 24.878 -15.296 10.238  1.00 16.51 ?  149 THR   A HB   1 
ATOM   3317 H HG1  . THR   A 1 149 ? 25.403 -14.304 8.319   1.00 16.55 ?  149 THR   A HG1  1 
ATOM   3318 H HG21 . THR   A 1 149 ? 26.946 -15.969 9.319   1.00 17.31 ?  149 THR   A HG21 1 
ATOM   3319 H HG22 . THR   A 1 149 ? 26.247 -17.227 9.969   1.00 17.31 ?  149 THR   A HG22 1 
ATOM   3320 H HG23 . THR   A 1 149 ? 26.212 -17.025 8.403   1.00 17.31 ?  149 THR   A HG23 1 
ATOM   3321 N N    . ASN   A 1 150 ? 22.236 -15.461 10.850  1.00 13.51 ?  150 ASN   A N    1 
ATOM   3322 C CA   . ASN   A 1 150 ? 20.953 -14.943 11.323  1.00 13.91 ?  150 ASN   A CA   1 
ATOM   3323 C C    . ASN   A 1 150 ? 20.778 -13.504 10.863  1.00 13.36 ?  150 ASN   A C    1 
ATOM   3324 O O    . ASN   A 1 150 ? 21.536 -12.616 11.273  1.00 14.53 ?  150 ASN   A O    1 
ATOM   3325 C CB   . ASN   A 1 150 ? 20.876 -15.042 12.841  1.00 16.54 ?  150 ASN   A CB   1 
ATOM   3326 C CG   . ASN   A 1 150 ? 20.784 -16.472 13.311  1.00 20.79 ?  150 ASN   A CG   1 
ATOM   3327 O OD1  . ASN   A 1 150 ? 20.195 -17.313 12.631  1.00 21.90 ?  150 ASN   A OD1  1 
ATOM   3328 N ND2  . ASN   A 1 150 ? 21.378 -16.766 14.464  1.00 23.24 ?  150 ASN   A ND2  1 
ATOM   3329 H H    . ASN   A 1 150 ? 22.874 -15.389 11.419  1.00 16.22 ?  150 ASN   A H    1 
ATOM   3330 H HA   . ASN   A 1 150 ? 20.230 -15.479 10.950  1.00 16.69 ?  150 ASN   A HA   1 
ATOM   3331 H HB2  . ASN   A 1 150 ? 21.671 -14.653 13.231  1.00 19.84 ?  150 ASN   A HB2  1 
ATOM   3332 H HB3  . ASN   A 1 150 ? 20.084 -14.580 13.157  1.00 19.84 ?  150 ASN   A HB3  1 
ATOM   3333 H HD21 . ASN   A 1 150 ? 21.357 -17.571 14.777  1.00 27.89 ?  150 ASN   A HD21 1 
ATOM   3334 H HD22 . ASN   A 1 150 ? 21.780 -16.149 14.911  1.00 27.89 ?  150 ASN   A HD22 1 
ATOM   3335 N N    . VAL   A 1 151 ? 19.787 -13.273 10.010  1.00 12.93 ?  151 VAL   A N    1 
ATOM   3336 C CA   . VAL   A 1 151 ? 19.577 -11.966 9.406   1.00 12.83 ?  151 VAL   A CA   1 
ATOM   3337 C C    . VAL   A 1 151 ? 18.193 -11.446 9.771   1.00 12.41 ?  151 VAL   A C    1 
ATOM   3338 O O    . VAL   A 1 151 ? 17.184 -12.152 9.621   1.00 14.09 ?  151 VAL   A O    1 
ATOM   3339 C CB   . VAL   A 1 151 ? 19.859 -11.971 7.888   1.00 14.42 ?  151 VAL   A CB   1 
ATOM   3340 C CG1  . VAL   A 1 151 ? 19.019 -12.994 7.155   1.00 15.69 ?  151 VAL   A CG1  1 
ATOM   3341 C CG2  . VAL   A 1 151 ? 19.679 -10.570 7.297   1.00 14.39 ?  151 VAL   A CG2  1 
ATOM   3342 H H    . VAL   A 1 151 ? 19.213 -13.866 9.761   1.00 15.51 ?  151 VAL   A H    1 
ATOM   3343 H HA   . VAL   A 1 151 ? 20.221 -11.352 9.790   1.00 15.40 ?  151 VAL   A HA   1 
ATOM   3344 H HB   . VAL   A 1 151 ? 20.789 -12.218 7.747   1.00 17.30 ?  151 VAL   A HB   1 
ATOM   3345 H HG11 . VAL   A 1 151 ? 19.208 -12.951 6.203   1.00 18.83 ?  151 VAL   A HG11 1 
ATOM   3346 H HG12 . VAL   A 1 151 ? 19.238 -13.884 7.489   1.00 18.83 ?  151 VAL   A HG12 1 
ATOM   3347 H HG13 . VAL   A 1 151 ? 18.079 -12.811 7.312   1.00 18.83 ?  151 VAL   A HG13 1 
ATOM   3348 H HG21 . VAL   A 1 151 ? 19.988 -10.573 6.374   1.00 17.27 ?  151 VAL   A HG21 1 
ATOM   3349 H HG22 . VAL   A 1 151 ? 18.739 -10.332 7.324   1.00 17.27 ?  151 VAL   A HG22 1 
ATOM   3350 H HG23 . VAL   A 1 151 ? 20.199 -9.939  7.815   1.00 17.27 ?  151 VAL   A HG23 1 
ATOM   3351 N N    . TYR   A 1 152 ? 18.179 -10.208 10.261  1.00 12.52 ?  152 TYR   A N    1 
ATOM   3352 C CA   . TYR   A 1 152 ? 16.987 -9.468  10.634  1.00 12.28 ?  152 TYR   A CA   1 
ATOM   3353 C C    . TYR   A 1 152 ? 16.808 -8.373  9.596   1.00 11.66 ?  152 TYR   A C    1 
ATOM   3354 O O    . TYR   A 1 152 ? 17.587 -7.413  9.549   1.00 12.14 ?  152 TYR   A O    1 
ATOM   3355 C CB   . TYR   A 1 152 ? 17.160 -8.910  12.042  1.00 13.38 ?  152 TYR   A CB   1 
ATOM   3356 C CG   . TYR   A 1 152 ? 17.114 -10.028 13.048  1.00 14.17 ?  152 TYR   A CG   1 
ATOM   3357 C CD1  . TYR   A 1 152 ? 18.237 -10.797 13.325  1.00 15.55 ?  152 TYR   A CD1  1 
ATOM   3358 C CD2  . TYR   A 1 152 ? 15.928 -10.365 13.682  1.00 14.84 ?  152 TYR   A CD2  1 
ATOM   3359 C CE1  . TYR   A 1 152 ? 18.197 -11.844 14.221  1.00 17.54 ?  152 TYR   A CE1  1 
ATOM   3360 C CE2  . TYR   A 1 152 ? 15.872 -11.425 14.587  1.00 16.91 ?  152 TYR   A CE2  1 
ATOM   3361 C CZ   . TYR   A 1 152 ? 17.016 -12.155 14.853  1.00 17.76 ?  152 TYR   A CZ   1 
ATOM   3362 O OH   . TYR   A 1 152 ? 16.983 -13.207 15.740  1.00 20.35 ?  152 TYR   A OH   1 
ATOM   3363 H H    . TYR   A 1 152 ? 18.905 -9.740  10.380  1.00 15.02 ?  152 TYR   A H    1 
ATOM   3364 H HA   . TYR   A 1 152 ? 16.221 -10.055 10.614  1.00 14.73 ?  152 TYR   A HA   1 
ATOM   3365 H HB2  . TYR   A 1 152 ? 18.018 -8.472  12.118  1.00 16.05 ?  152 TYR   A HB2  1 
ATOM   3366 H HB3  . TYR   A 1 152 ? 16.440 -8.291  12.237  1.00 16.05 ?  152 TYR   A HB3  1 
ATOM   3367 H HD1  . TYR   A 1 152 ? 19.039 -10.591 12.897  1.00 18.66 ?  152 TYR   A HD1  1 
ATOM   3368 H HD2  . TYR   A 1 152 ? 15.151 -9.875  13.503  1.00 17.80 ?  152 TYR   A HD2  1 
ATOM   3369 H HE1  . TYR   A 1 152 ? 18.964 -12.335 14.394  1.00 21.04 ?  152 TYR   A HE1  1 
ATOM   3370 H HE2  . TYR   A 1 152 ? 15.069 -11.633 15.013  1.00 20.29 ?  152 TYR   A HE2  1 
ATOM   3371 H HH   . TYR   A 1 152 ? 16.209 -13.286 16.056  1.00 24.42 ?  152 TYR   A HH   1 
ATOM   3372 N N    . LEU   A 1 153 ? 15.805 -8.546  8.743   1.00 11.81 ?  153 LEU   A N    1 
ATOM   3373 C CA   . LEU   A 1 153 ? 15.548 -7.636  7.640   1.00 11.77 ?  153 LEU   A CA   1 
ATOM   3374 C C    . LEU   A 1 153 ? 14.549 -6.569  8.046   1.00 12.41 ?  153 LEU   A C    1 
ATOM   3375 O O    . LEU   A 1 153 ? 13.448 -6.879  8.518   1.00 13.60 ?  153 LEU   A O    1 
ATOM   3376 C CB   . LEU   A 1 153 ? 14.989 -8.400  6.441   1.00 12.17 ?  153 LEU   A CB   1 
ATOM   3377 C CG   . LEU   A 1 153 ? 15.907 -9.420  5.767   1.00 12.51 ?  153 LEU   A CG   1 
ATOM   3378 C CD1  . LEU   A 1 153 ? 15.112 -10.266 4.778   1.00 13.02 ?  153 LEU   A CD1  1 
ATOM   3379 C CD2  . LEU   A 1 153 ? 17.053 -8.723  5.060   1.00 12.97 ?  153 LEU   A CD2  1 
ATOM   3380 H H    . LEU   A 1 153 ? 15.241 -9.202  8.789   1.00 14.17 ?  153 LEU   A H    1 
ATOM   3381 H HA   . LEU   A 1 153 ? 16.376 -7.213  7.385   1.00 14.12 ?  153 LEU   A HA   1 
ATOM   3382 H HB2  . LEU   A 1 153 ? 14.198 -8.873  6.729   1.00 14.60 ?  153 LEU   A HB2  1 
ATOM   3383 H HB3  . LEU   A 1 153 ? 14.745 -7.747  5.765   1.00 14.60 ?  153 LEU   A HB3  1 
ATOM   3384 H HG   . LEU   A 1 153 ? 16.283 -10.010 6.443   1.00 15.00 ?  153 LEU   A HG   1 
ATOM   3385 H HD11 . LEU   A 1 153 ? 15.667 -10.982 4.453   1.00 15.63 ?  153 LEU   A HD11 1 
ATOM   3386 H HD12 . LEU   A 1 153 ? 14.330 -10.618 5.227   1.00 15.63 ?  153 LEU   A HD12 1 
ATOM   3387 H HD13 . LEU   A 1 153 ? 14.834 -9.694  4.038   1.00 15.63 ?  153 LEU   A HD13 1 
ATOM   3388 H HD21 . LEU   A 1 153 ? 17.610 -9.388  4.634   1.00 15.56 ?  153 LEU   A HD21 1 
ATOM   3389 H HD22 . LEU   A 1 153 ? 16.687 -8.117  4.398   1.00 15.56 ?  153 LEU   A HD22 1 
ATOM   3390 H HD23 . LEU   A 1 153 ? 17.570 -8.224  5.714   1.00 15.56 ?  153 LEU   A HD23 1 
ATOM   3391 N N    A ALA   A 1 154 ? 14.932 -5.313  7.832   0.40 12.80 ?  154 ALA   A N    1 
ATOM   3392 N N    B ALA   A 1 154 ? 14.927 -5.308  7.867   0.60 12.46 ?  154 ALA   A N    1 
ATOM   3393 C CA   A ALA   A 1 154 ? 14.064 -4.165  8.037   0.40 13.54 ?  154 ALA   A CA   1 
ATOM   3394 C CA   B ALA   A 1 154 ? 14.049 -4.174  8.117   0.60 13.10 ?  154 ALA   A CA   1 
ATOM   3395 C C    A ALA   A 1 154 ? 13.572 -3.685  6.681   0.40 14.03 ?  154 ALA   A C    1 
ATOM   3396 C C    B ALA   A 1 154 ? 13.651 -3.600  6.766   0.60 13.37 ?  154 ALA   A C    1 
ATOM   3397 O O    A ALA   A 1 154 ? 14.378 -3.373  5.795   0.40 14.45 ?  154 ALA   A O    1 
ATOM   3398 O O    B ALA   A 1 154 ? 14.520 -3.198  5.982   0.60 13.66 ?  154 ALA   A O    1 
ATOM   3399 C CB   A ALA   A 1 154 ? 14.816 -3.038  8.741   0.40 14.07 ?  154 ALA   A CB   1 
ATOM   3400 C CB   B ALA   A 1 154 ? 14.762 -3.114  8.956   0.60 13.83 ?  154 ALA   A CB   1 
ATOM   3401 H H    A ALA   A 1 154 ? 15.721 -5.098  7.558   0.40 15.35 ?  154 ALA   A H    1 
ATOM   3402 H H    B ALA   A 1 154 ? 15.712 -5.075  7.594   0.60 14.95 ?  154 ALA   A H    1 
ATOM   3403 H HA   A ALA   A 1 154 ? 13.300 -4.422  8.572   0.40 16.25 ?  154 ALA   A HA   1 
ATOM   3404 H HA   B ALA   A 1 154 ? 13.251 -4.463  8.588   0.60 15.71 ?  154 ALA   A HA   1 
ATOM   3405 H HB1  A ALA   A 1 154 ? 14.212 -2.287  8.857   0.40 16.88 ?  154 ALA   A HB1  1 
ATOM   3406 H HB1  B ALA   A 1 154 ? 14.156 -2.368  9.108   0.60 16.59 ?  154 ALA   A HB1  1 
ATOM   3407 H HB2  A ALA   A 1 154 ? 15.123 -3.355  9.601   0.40 16.88 ?  154 ALA   A HB2  1 
ATOM   3408 H HB2  B ALA   A 1 154 ? 15.025 -3.501  9.805   0.60 16.59 ?  154 ALA   A HB2  1 
ATOM   3409 H HB3  A ALA   A 1 154 ? 15.571 -2.772  8.193   0.40 16.88 ?  154 ALA   A HB3  1 
ATOM   3410 H HB3  B ALA   A 1 154 ? 15.547 -2.804  8.476   0.60 16.59 ?  154 ALA   A HB3  1 
ATOM   3411 N N    A VAL   A 1 155 ? 12.255 -3.628  6.527   0.40 14.46 ?  155 VAL   A N    1 
ATOM   3412 N N    B VAL   A 1 155 ? 12.348 -3.565  6.496   0.60 13.61 ?  155 VAL   A N    1 
ATOM   3413 C CA   A VAL   A 1 155 ? 11.603 -3.102  5.336   0.40 14.83 ?  155 VAL   A CA   1 
ATOM   3414 C CA   B VAL   A 1 155 ? 11.807 -3.092  5.226   0.60 14.75 ?  155 VAL   A CA   1 
ATOM   3415 C C    A VAL   A 1 155 ? 10.890 -1.821  5.747   0.40 15.14 ?  155 VAL   A C    1 
ATOM   3416 C C    B VAL   A 1 155 ? 10.983 -1.842  5.506   0.60 14.89 ?  155 VAL   A C    1 
ATOM   3417 O O    A VAL   A 1 155 ? 9.993  -1.853  6.597   0.40 15.28 ?  155 VAL   A O    1 
ATOM   3418 O O    B VAL   A 1 155 ? 9.945  -1.910  6.175   0.60 14.52 ?  155 VAL   A O    1 
ATOM   3419 C CB   A VAL   A 1 155 ? 10.615 -4.123  4.751   0.40 14.68 ?  155 VAL   A CB   1 
ATOM   3420 C CB   B VAL   A 1 155 ? 10.981 -4.168  4.510   0.60 15.02 ?  155 VAL   A CB   1 
ATOM   3421 C CG1  A VAL   A 1 155 ? 9.936  -3.560  3.514   0.40 15.29 ?  155 VAL   A CG1  1 
ATOM   3422 C CG1  B VAL   A 1 155 ? 10.326 -3.598  3.258   0.60 15.76 ?  155 VAL   A CG1  1 
ATOM   3423 C CG2  A VAL   A 1 155 ? 11.328 -5.437  4.436   0.40 14.42 ?  155 VAL   A CG2  1 
ATOM   3424 C CG2  B VAL   A 1 155 ? 11.874 -5.345  4.154   0.60 15.52 ?  155 VAL   A CG2  1 
ATOM   3425 H H    A VAL   A 1 155 ? 11.701 -3.899  7.123   0.40 17.35 ?  155 VAL   A H    1 
ATOM   3426 H H    B VAL   A 1 155 ? 11.737 -3.808  7.053   0.60 16.33 ?  155 VAL   A H    1 
ATOM   3427 H HA   A VAL   A 1 155 ? 12.268 -2.886  4.665   0.40 17.80 ?  155 VAL   A HA   1 
ATOM   3428 H HA   B VAL   A 1 155 ? 12.538 -2.842  4.643   0.60 17.69 ?  155 VAL   A HA   1 
ATOM   3429 H HB   A VAL   A 1 155 ? 9.927  -4.304  5.413   0.40 17.62 ?  155 VAL   A HB   1 
ATOM   3430 H HB   B VAL   A 1 155 ? 10.281 -4.488  5.101   0.60 18.03 ?  155 VAL   A HB   1 
ATOM   3431 H HG11 A VAL   A 1 155 ? 9.421  -4.264  3.093   0.40 18.35 ?  155 VAL   A HG11 1 
ATOM   3432 H HG11 B VAL   A 1 155 ? 10.019 -4.331  2.700   0.60 18.91 ?  155 VAL   A HG11 1 
ATOM   3433 H HG12 A VAL   A 1 155 ? 9.350  -2.832  3.775   0.40 18.35 ?  155 VAL   A HG12 1 
ATOM   3434 H HG12 B VAL   A 1 155 ? 9.570  -3.046  3.518   0.60 18.91 ?  155 VAL   A HG12 1 
ATOM   3435 H HG13 A VAL   A 1 155 ? 10.616 -3.235  2.903   0.40 18.35 ?  155 VAL   A HG13 1 
ATOM   3436 H HG13 B VAL   A 1 155 ? 10.976 -3.066  2.775   0.60 18.91 ?  155 VAL   A HG13 1 
ATOM   3437 H HG21 A VAL   A 1 155 ? 10.706 -6.033  3.993   0.40 17.30 ?  155 VAL   A HG21 1 
ATOM   3438 H HG21 B VAL   A 1 155 ? 11.347 -6.011  3.687   0.60 18.62 ?  155 VAL   A HG21 1 
ATOM   3439 H HG22 A VAL   A 1 155 ? 12.084 -5.253  3.856   0.40 17.30 ?  155 VAL   A HG22 1 
ATOM   3440 H HG22 B VAL   A 1 155 ? 12.593 -5.031  3.584   0.60 18.62 ?  155 VAL   A HG22 1 
ATOM   3441 H HG23 A VAL   A 1 155 ? 11.638 -5.836  5.265   0.40 17.30 ?  155 VAL   A HG23 1 
ATOM   3442 H HG23 B VAL   A 1 155 ? 12.237 -5.721  4.970   0.60 18.62 ?  155 VAL   A HG23 1 
ATOM   3443 N N    A PHE   A 1 156 ? 11.296 -0.693  5.155   0.40 15.35 ?  156 PHE   A N    1 
ATOM   3444 N N    B PHE   A 1 156 ? 11.444 -0.708  4.971   0.60 16.12 ?  156 PHE   A N    1 
ATOM   3445 C CA   A PHE   A 1 156 ? 10.746 0.601   5.556   0.40 16.19 ?  156 PHE   A CA   1 
ATOM   3446 C CA   B PHE   A 1 156 ? 10.889 0.610   5.284   0.60 17.66 ?  156 PHE   A CA   1 
ATOM   3447 C C    A PHE   A 1 156 ? 9.298  0.756   5.105   0.40 16.47 ?  156 PHE   A C    1 
ATOM   3448 C C    B PHE   A 1 156 ? 9.456  0.760   4.786   0.60 16.98 ?  156 PHE   A C    1 
ATOM   3449 O O    A PHE   A 1 156 ? 8.456  1.264   5.857   0.40 16.81 ?  156 PHE   A O    1 
ATOM   3450 O O    B PHE   A 1 156 ? 8.582  1.265   5.504   0.60 17.53 ?  156 PHE   A O    1 
ATOM   3451 C CB   A PHE   A 1 156 ? 11.618 1.718   4.975   0.40 17.73 ?  156 PHE   A CB   1 
ATOM   3452 C CB   B PHE   A 1 156 ? 11.809 1.642   4.623   0.60 19.57 ?  156 PHE   A CB   1 
ATOM   3453 C CG   A PHE   A 1 156 ? 11.121 3.098   5.281   0.40 18.89 ?  156 PHE   A CG   1 
ATOM   3454 C CG   B PHE   A 1 156 ? 11.387 3.074   4.782   0.60 20.43 ?  156 PHE   A CG   1 
ATOM   3455 C CD1  A PHE   A 1 156 ? 11.011 3.523   6.589   0.40 19.31 ?  156 PHE   A CD1  1 
ATOM   3456 C CD1  B PHE   A 1 156 ? 10.529 3.672   3.869   0.60 21.22 ?  156 PHE   A CD1  1 
ATOM   3457 C CD2  A PHE   A 1 156 ? 10.779 3.974   4.259   0.40 19.74 ?  156 PHE   A CD2  1 
ATOM   3458 C CD2  B PHE   A 1 156 ? 11.918 3.846   5.804   0.60 20.89 ?  156 PHE   A CD2  1 
ATOM   3459 C CE1  A PHE   A 1 156 ? 10.557 4.792   6.881   0.40 20.10 ?  156 PHE   A CE1  1 
ATOM   3460 C CE1  B PHE   A 1 156 ? 10.167 5.000   4.009   0.60 21.59 ?  156 PHE   A CE1  1 
ATOM   3461 C CE2  A PHE   A 1 156 ? 10.325 5.244   4.544   0.40 20.32 ?  156 PHE   A CE2  1 
ATOM   3462 C CE2  B PHE   A 1 156 ? 11.565 5.172   5.947   0.60 21.17 ?  156 PHE   A CE2  1 
ATOM   3463 C CZ   A PHE   A 1 156 ? 10.217 5.656   5.858   0.40 20.56 ?  156 PHE   A CZ   1 
ATOM   3464 C CZ   B PHE   A 1 156 ? 10.696 5.755   5.048   0.60 21.24 ?  156 PHE   A CZ   1 
ATOM   3465 H H    A PHE   A 1 156 ? 11.887 -0.654  4.530   0.40 18.42 ?  156 PHE   A H    1 
ATOM   3466 H H    B PHE   A 1 156 ? 12.112 -0.680  4.426   0.60 19.34 ?  156 PHE   A H    1 
ATOM   3467 H HA   A PHE   A 1 156 ? 10.780 0.676   6.524   0.40 19.43 ?  156 PHE   A HA   1 
ATOM   3468 H HA   B PHE   A 1 156 ? 10.906 0.751   6.241   0.60 21.19 ?  156 PHE   A HA   1 
ATOM   3469 H HB2  A PHE   A 1 156 ? 12.517 1.643   5.338   0.40 21.27 ?  156 PHE   A HB2  1 
ATOM   3470 H HB2  B PHE   A 1 156 ? 12.684 1.558   5.022   0.60 23.48 ?  156 PHE   A HB2  1 
ATOM   3471 H HB3  A PHE   A 1 156 ? 11.649 1.622   4.010   0.40 21.27 ?  156 PHE   A HB3  1 
ATOM   3472 H HB3  B PHE   A 1 156 ? 11.871 1.466   3.675   0.60 23.48 ?  156 PHE   A HB3  1 
ATOM   3473 H HD1  A PHE   A 1 156 ? 11.242 2.946   7.280   0.40 23.17 ?  156 PHE   A HD1  1 
ATOM   3474 H HD1  B PHE   A 1 156 ? 10.176 3.171   3.169   0.60 25.46 ?  156 PHE   A HD1  1 
ATOM   3475 H HD2  A PHE   A 1 156 ? 10.851 3.697   3.373   0.40 23.69 ?  156 PHE   A HD2  1 
ATOM   3476 H HD2  B PHE   A 1 156 ? 12.504 3.456   6.413   0.60 25.07 ?  156 PHE   A HD2  1 
ATOM   3477 H HE1  A PHE   A 1 156 ? 10.486 5.069   7.765   0.40 24.12 ?  156 PHE   A HE1  1 
ATOM   3478 H HE1  B PHE   A 1 156 ? 9.579  5.393   3.400   0.60 25.90 ?  156 PHE   A HE1  1 
ATOM   3479 H HE2  A PHE   A 1 156 ? 10.094 5.822   3.851   0.40 24.38 ?  156 PHE   A HE2  1 
ATOM   3480 H HE2  B PHE   A 1 156 ? 11.912 5.673   6.647   0.60 25.41 ?  156 PHE   A HE2  1 
ATOM   3481 H HZ   A PHE   A 1 156 ? 9.910  6.512   6.054   0.40 24.67 ?  156 PHE   A HZ   1 
ATOM   3482 H HZ   B PHE   A 1 156 ? 10.449 6.647   5.147   0.60 25.48 ?  156 PHE   A HZ   1 
ATOM   3483 N N    A ASP   A 1 157 ? 8.988  0.315   3.891   0.40 16.88 ?  157 ASP   A N    1 
ATOM   3484 N N    B ASP   A 1 157 ? 9.206  0.353   3.552   0.60 16.89 ?  157 ASP   A N    1 
ATOM   3485 C CA   A ASP   A 1 157 ? 7.667  0.519   3.309   0.40 18.55 ?  157 ASP   A CA   1 
ATOM   3486 C CA   B ASP   A 1 157 ? 7.946  0.653   2.892   0.60 16.65 ?  157 ASP   A CA   1 
ATOM   3487 C C    A ASP   A 1 157 ? 6.701  -0.533  3.842   0.40 18.98 ?  157 ASP   A C    1 
ATOM   3488 C C    B ASP   A 1 157 ? 6.872  -0.318  3.373   0.60 16.18 ?  157 ASP   A C    1 
ATOM   3489 O O    A ASP   A 1 157 ? 6.910  -1.734  3.643   0.40 18.78 ?  157 ASP   A O    1 
ATOM   3490 O O    B ASP   A 1 157 ? 6.996  -1.532  3.181   0.60 16.37 ?  157 ASP   A O    1 
ATOM   3491 C CB   A ASP   A 1 157 ? 7.761  0.425   1.790   0.40 20.13 ?  157 ASP   A CB   1 
ATOM   3492 C CB   B ASP   A 1 157 ? 8.165  0.550   1.386   0.60 17.01 ?  157 ASP   A CB   1 
ATOM   3493 C CG   A ASP   A 1 157 ? 6.556  1.015   1.094   0.40 21.60 ?  157 ASP   A CG   1 
ATOM   3494 C CG   B ASP   A 1 157 ? 6.988  1.031   0.599   0.60 17.76 ?  157 ASP   A CG   1 
ATOM   3495 O OD1  A ASP   A 1 157 ? 6.488  2.257   0.970   0.40 22.36 ?  157 ASP   A OD1  1 
ATOM   3496 O OD1  B ASP   A 1 157 ? 5.979  0.308   0.555   0.60 18.42 ?  157 ASP   A OD1  1 
ATOM   3497 O OD2  A ASP   A 1 157 ? 5.671  0.239   0.678   0.40 22.33 -1 157 ASP   A OD2  1 
ATOM   3498 O OD2  B ASP   A 1 157 ? 7.073  2.135   0.030   0.60 18.14 -1 157 ASP   A OD2  1 
ATOM   3499 H H    A ASP   A 1 157 ? 9.537  -0.111  3.382   0.40 20.25 ?  157 ASP   A H    1 
ATOM   3500 H H    B ASP   A 1 157 ? 9.762  -0.101  3.065   0.60 20.26 ?  157 ASP   A H    1 
ATOM   3501 H HA   A ASP   A 1 157 ? 7.339  1.396   3.552   0.40 22.26 ?  157 ASP   A HA   1 
ATOM   3502 H HA   B ASP   A 1 157 ? 7.679  1.562   3.105   0.60 19.98 ?  157 ASP   A HA   1 
ATOM   3503 H HB2  A ASP   A 1 157 ? 8.548  0.902   1.494   0.40 24.15 ?  157 ASP   A HB2  1 
ATOM   3504 H HB2  B ASP   A 1 157 ? 8.933  1.091   1.133   0.60 20.41 ?  157 ASP   A HB2  1 
ATOM   3505 H HB3  A ASP   A 1 157 ? 7.828  -0.506  1.539   0.40 24.15 ?  157 ASP   A HB3  1 
ATOM   3506 H HB3  B ASP   A 1 157 ? 8.322  -0.376  1.147   0.60 20.41 ?  157 ASP   A HB3  1 
ATOM   3507 N N    A LYS   A 1 158 ? 5.639  -0.082  4.514   0.40 19.95 ?  158 LYS   A N    1 
ATOM   3508 N N    B LYS   A 1 158 ? 5.819  0.216   4.000   0.60 16.64 ?  158 LYS   A N    1 
ATOM   3509 C CA   A LYS   A 1 158 ? 4.670  -1.018  5.079   0.40 21.07 ?  158 LYS   A CA   1 
ATOM   3510 C CA   B LYS   A 1 158 ? 4.785  -0.645  4.566   0.60 17.20 ?  158 LYS   A CA   1 
ATOM   3511 C C    A LYS   A 1 158 ? 3.932  -1.782  3.987   0.40 20.66 ?  158 LYS   A C    1 
ATOM   3512 C C    B LYS   A 1 158 ? 4.120  -1.485  3.486   0.60 17.23 ?  158 LYS   A C    1 
ATOM   3513 O O    A LYS   A 1 158 ? 3.729  -2.996  4.102   0.40 20.39 ?  158 LYS   A O    1 
ATOM   3514 O O    B LYS   A 1 158 ? 3.894  -2.687  3.667   0.60 16.98 ?  158 LYS   A O    1 
ATOM   3515 C CB   A LYS   A 1 158 ? 3.691  -0.272  5.989   0.40 22.37 ?  158 LYS   A CB   1 
ATOM   3516 C CB   B LYS   A 1 158 ? 3.733  0.192   5.294   0.60 18.48 ?  158 LYS   A CB   1 
ATOM   3517 C CG   A LYS   A 1 158 ? 2.460  -1.074  6.413   0.40 23.56 ?  158 LYS   A CG   1 
ATOM   3518 C CG   B LYS   A 1 158 ? 2.535  -0.630  5.755   0.60 19.66 ?  158 LYS   A CG   1 
ATOM   3519 C CD   A LYS   A 1 158 ? 2.816  -2.326  7.207   0.40 24.43 ?  158 LYS   A CD   1 
ATOM   3520 C CD   B LYS   A 1 158 ? 1.459  0.229   6.381   0.60 21.45 ?  158 LYS   A CD   1 
ATOM   3521 C CE   A LYS   A 1 158 ? 1.563  -2.969  7.790   0.40 24.91 ?  158 LYS   A CE   1 
ATOM   3522 C CE   B LYS   A 1 158 ? 0.326  -0.616  6.944   0.60 22.27 ?  158 LYS   A CE   1 
ATOM   3523 N NZ   A LYS   A 1 158 ? 1.800  -4.340  8.326   0.40 25.12 ?  158 LYS   A NZ   1 
ATOM   3524 N NZ   B LYS   A 1 158 ? -0.336 -1.466  5.914   0.60 22.58 ?  158 LYS   A NZ   1 
ATOM   3525 H H    A LYS   A 1 158 ? 5.463  0.744   4.656   0.40 23.94 ?  158 LYS   A H    1 
ATOM   3526 H H    B LYS   A 1 158 ? 5.688  1.062   4.096   0.60 19.96 ?  158 LYS   A H    1 
ATOM   3527 H HA   A LYS   A 1 158 ? 5.140  -1.666  5.627   0.40 25.28 ?  158 LYS   A HA   1 
ATOM   3528 H HA   B LYS   A 1 158 ? 5.196  -1.243  5.206   0.60 20.64 ?  158 LYS   A HA   1 
ATOM   3529 H HB2  A LYS   A 1 158 ? 4.159  -0.012  6.800   0.40 26.84 ?  158 LYS   A HB2  1 
ATOM   3530 H HB2  B LYS   A 1 158 ? 4.143  0.598   6.075   0.60 22.17 ?  158 LYS   A HB2  1 
ATOM   3531 H HB3  A LYS   A 1 158 ? 3.378  0.519   5.527   0.40 26.84 ?  158 LYS   A HB3  1 
ATOM   3532 H HB3  B LYS   A 1 158 ? 3.414  0.885   4.692   0.60 22.17 ?  158 LYS   A HB3  1 
ATOM   3533 H HG2  A LYS   A 1 158 ? 1.903  -0.516  6.977   0.40 28.27 ?  158 LYS   A HG2  1 
ATOM   3534 H HG2  B LYS   A 1 158 ? 2.142  -1.086  4.995   0.60 23.59 ?  158 LYS   A HG2  1 
ATOM   3535 H HG3  A LYS   A 1 158 ? 1.958  -1.345  5.627   0.40 28.27 ?  158 LYS   A HG3  1 
ATOM   3536 H HG3  B LYS   A 1 158 ? 2.838  -1.277  6.411   0.60 23.59 ?  158 LYS   A HG3  1 
ATOM   3537 H HD2  A LYS   A 1 158 ? 3.245  -2.971  6.624   0.40 29.32 ?  158 LYS   A HD2  1 
ATOM   3538 H HD2  B LYS   A 1 158 ? 1.847  0.747   7.103   0.60 25.73 ?  158 LYS   A HD2  1 
ATOM   3539 H HD3  A LYS   A 1 158 ? 3.406  -2.087  7.940   0.40 29.32 ?  158 LYS   A HD3  1 
ATOM   3540 H HD3  B LYS   A 1 158 ? 1.094  0.821   5.702   0.60 25.73 ?  158 LYS   A HD3  1 
ATOM   3541 H HE2  A LYS   A 1 158 ? 1.227  -2.418  8.515   0.40 29.89 ?  158 LYS   A HE2  1 
ATOM   3542 H HE2  B LYS   A 1 158 ? 0.683  -1.201  7.629   0.60 26.73 ?  158 LYS   A HE2  1 
ATOM   3543 H HE3  A LYS   A 1 158 ? 0.892  -3.036  7.096   0.40 29.89 ?  158 LYS   A HE3  1 
ATOM   3544 H HE3  B LYS   A 1 158 ? -0.343 -0.028  7.323   0.60 26.73 ?  158 LYS   A HE3  1 
ATOM   3545 H HZ1  A LYS   A 1 158 ? 1.044  -4.675  8.656   0.40 30.15 ?  158 LYS   A HZ1  1 
ATOM   3546 H HZ1  B LYS   A 1 158 ? -0.998 -1.931  6.285   0.60 27.09 ?  158 LYS   A HZ1  1 
ATOM   3547 H HZ2  A LYS   A 1 158 ? 2.091  -4.874  7.675   0.40 30.15 ?  158 LYS   A HZ2  1 
ATOM   3548 H HZ2  B LYS   A 1 158 ? -0.670 -0.955  5.267   0.60 27.09 ?  158 LYS   A HZ2  1 
ATOM   3549 H HZ3  A LYS   A 1 158 ? 2.411  -4.316  8.973   0.40 30.15 ?  158 LYS   A HZ3  1 
ATOM   3550 H HZ3  B LYS   A 1 158 ? 0.253  -2.032  5.561   0.60 27.09 ?  158 LYS   A HZ3  1 
ATOM   3551 N N    A ASN   A 1 159 ? 3.515  -1.094  2.923   0.40 20.44 ?  159 ASN   A N    1 
ATOM   3552 N N    B ASN   A 1 159 ? 3.776  -0.862  2.358   0.60 18.17 ?  159 ASN   A N    1 
ATOM   3553 C CA   A ASN   A 1 159 ? 2.851  -1.791  1.826   0.40 20.31 ?  159 ASN   A CA   1 
ATOM   3554 C CA   B ASN   A 1 159 ? 3.050  -1.589  1.325   0.60 19.91 ?  159 ASN   A CA   1 
ATOM   3555 C C    A ASN   A 1 159 ? 3.779  -2.823  1.193   0.40 19.40 ?  159 ASN   A C    1 
ATOM   3556 C C    B ASN   A 1 159 ? 3.884  -2.722  0.741   0.60 20.54 ?  159 ASN   A C    1 
ATOM   3557 O O    A ASN   A 1 159 ? 3.347  -3.929  0.848   0.40 19.15 ?  159 ASN   A O    1 
ATOM   3558 O O    B ASN   A 1 159 ? 3.363  -3.811  0.480   0.60 20.64 ?  159 ASN   A O    1 
ATOM   3559 C CB   A ASN   A 1 159 ? 2.337  -0.787  0.791   0.40 21.15 ?  159 ASN   A CB   1 
ATOM   3560 C CB   B ASN   A 1 159 ? 2.570  -0.629  0.236   0.60 21.59 ?  159 ASN   A CB   1 
ATOM   3561 C CG   A ASN   A 1 159 ? 1.113  -0.024  1.276   0.40 21.89 ?  159 ASN   A CG   1 
ATOM   3562 C CG   B ASN   A 1 159 ? 1.387  0.215   0.682   0.60 23.16 ?  159 ASN   A CG   1 
ATOM   3563 O OD1  A ASN   A 1 159 ? 0.275  -0.569  1.994   0.40 22.58 ?  159 ASN   A OD1  1 
ATOM   3564 O OD1  B ASN   A 1 159 ? 1.284  1.395   0.333   0.60 24.14 ?  159 ASN   A OD1  1 
ATOM   3565 N ND2  A ASN   A 1 159 ? 1.007  1.241   0.885   0.40 22.46 ?  159 ASN   A ND2  1 
ATOM   3566 N ND2  B ASN   A 1 159 ? 0.485  -0.385  1.456   0.60 23.80 ?  159 ASN   A ND2  1 
ATOM   3567 H H    A ASN   A 1 159 ? 3.598  -0.248  2.818   0.40 24.53 ?  159 ASN   A H    1 
ATOM   3568 H H    B ASN   A 1 159 ? 3.951  -0.039  2.169   0.60 21.81 ?  159 ASN   A H    1 
ATOM   3569 H HA   A ASN   A 1 159 ? 2.080  -2.265  2.180   0.40 24.37 ?  159 ASN   A HA   1 
ATOM   3570 H HA   B ASN   A 1 159 ? 2.279  -2.004  1.731   0.60 23.89 ?  159 ASN   A HA   1 
ATOM   3571 H HB2  A ASN   A 1 159 ? 3.032  -0.143  0.599   0.40 25.38 ?  159 ASN   A HB2  1 
ATOM   3572 H HB2  B ASN   A 1 159 ? 3.287  -0.019  0.001   0.60 25.91 ?  159 ASN   A HB2  1 
ATOM   3573 H HB3  A ASN   A 1 159 ? 2.090  -1.265  -0.018  0.40 25.38 ?  159 ASN   A HB3  1 
ATOM   3574 H HB3  B ASN   A 1 159 ? 2.294  -1.134  -0.544  0.60 25.91 ?  159 ASN   A HB3  1 
ATOM   3575 H HD21 A ASN   A 1 159 ? 0.333  1.713   1.132   0.40 26.95 ?  159 ASN   A HD21 1 
ATOM   3576 H HD21 B ASN   A 1 159 ? -0.199 0.049   1.733   0.60 28.55 ?  159 ASN   A HD21 1 
ATOM   3577 H HD22 A ASN   A 1 159 ? 1.614  1.589   0.387   0.40 26.95 ?  159 ASN   A HD22 1 
ATOM   3578 H HD22 B ASN   A 1 159 ? 0.583  -1.211  1.684   0.60 28.55 ?  159 ASN   A HD22 1 
ATOM   3579 N N    A LEU   A 1 160 ? 5.065  -2.497  1.056   0.40 18.10 ?  160 LEU   A N    1 
ATOM   3580 N N    B LEU   A 1 160 ? 5.182  -2.503  0.540   0.60 20.67 ?  160 LEU   A N    1 
ATOM   3581 C CA   A LEU   A 1 160 ? 6.004  -3.491  0.549   0.40 17.35 ?  160 LEU   A CA   1 
ATOM   3582 C CA   B LEU   A 1 160 ? 5.994  -3.585  -0.005  0.60 21.80 ?  160 LEU   A CA   1 
ATOM   3583 C C    A LEU   A 1 160 ? 6.157  -4.645  1.531   0.40 16.49 ?  160 LEU   A C    1 
ATOM   3584 C C    B LEU   A 1 160 ? 6.253  -4.664  1.041   0.60 19.88 ?  160 LEU   A C    1 
ATOM   3585 O O    A LEU   A 1 160 ? 6.182  -5.810  1.124   0.40 16.75 ?  160 LEU   A O    1 
ATOM   3586 O O    B LEU   A 1 160 ? 6.292  -5.853  0.706   0.60 19.65 ?  160 LEU   A O    1 
ATOM   3587 C CB   A LEU   A 1 160 ? 7.360  -2.854  0.242   0.40 17.07 ?  160 LEU   A CB   1 
ATOM   3588 C CB   B LEU   A 1 160 ? 7.286  -3.050  -0.622  0.60 24.60 ?  160 LEU   A CB   1 
ATOM   3589 C CG   A LEU   A 1 160 ? 8.430  -3.851  -0.212  0.40 17.39 ?  160 LEU   A CG   1 
ATOM   3590 C CG   B LEU   A 1 160 ? 7.114  -2.511  -2.050  0.60 27.22 ?  160 LEU   A CG   1 
ATOM   3591 C CD1  A LEU   A 1 160 ? 7.937  -4.654  -1.405  0.40 17.42 ?  160 LEU   A CD1  1 
ATOM   3592 C CD1  B LEU   A 1 160 ? 8.383  -1.846  -2.558  0.60 28.14 ?  160 LEU   A CD1  1 
ATOM   3593 C CD2  A LEU   A 1 160 ? 9.736  -3.147  -0.535  0.40 17.20 ?  160 LEU   A CD2  1 
ATOM   3594 C CD2  B LEU   A 1 160 ? 6.673  -3.618  -3.006  0.60 27.96 ?  160 LEU   A CD2  1 
ATOM   3595 H H    A LEU   A 1 160 ? 5.405  -1.737  1.252   0.40 21.72 ?  160 LEU   A H    1 
ATOM   3596 H H    B LEU   A 1 160 ? 5.597  -1.767  0.704   0.60 24.81 ?  160 LEU   A H    1 
ATOM   3597 H HA   A LEU   A 1 160 ? 5.648  -3.853  -0.274  0.40 20.82 ?  160 LEU   A HA   1 
ATOM   3598 H HA   B LEU   A 1 160 ? 5.483  -4.000  -0.714  0.60 26.16 ?  160 LEU   A HA   1 
ATOM   3599 H HB2  A LEU   A 1 160 ? 7.247  -2.179  -0.453  0.40 20.48 ?  160 LEU   A HB2  1 
ATOM   3600 H HB2  B LEU   A 1 160 ? 7.620  -2.325  -0.073  0.60 29.52 ?  160 LEU   A HB2  1 
ATOM   3601 H HB3  A LEU   A 1 160 ? 7.687  -2.445  1.053   0.40 20.48 ?  160 LEU   A HB3  1 
ATOM   3602 H HB3  B LEU   A 1 160 ? 7.935  -3.769  -0.653  0.60 29.52 ?  160 LEU   A HB3  1 
ATOM   3603 H HG   A LEU   A 1 160 ? 8.604  -4.471  0.512   0.40 20.87 ?  160 LEU   A HG   1 
ATOM   3604 H HG   B LEU   A 1 160 ? 6.419  -1.838  -2.044  0.60 32.66 ?  160 LEU   A HG   1 
ATOM   3605 H HD11 A LEU   A 1 160 ? 8.656  -5.216  -1.719  0.40 20.90 ?  160 LEU   A HD11 1 
ATOM   3606 H HD11 B LEU   A 1 160 ? 8.224  -1.502  -3.453  0.60 33.76 ?  160 LEU   A HD11 1 
ATOM   3607 H HD12 A LEU   A 1 160 ? 7.186  -5.207  -1.131  0.40 20.90 ?  160 LEU   A HD12 1 
ATOM   3608 H HD12 B LEU   A 1 160 ? 8.616  -1.117  -1.963  0.60 33.76 ?  160 LEU   A HD12 1 
ATOM   3609 H HD13 A LEU   A 1 160 ? 7.657  -4.043  -2.105  0.40 20.90 ?  160 LEU   A HD13 1 
ATOM   3610 H HD13 B LEU   A 1 160 ? 9.098  -2.500  -2.579  0.60 33.76 ?  160 LEU   A HD13 1 
ATOM   3611 H HD21 A LEU   A 1 160 ? 10.387 -3.810  -0.814  0.40 20.63 ?  160 LEU   A HD21 1 
ATOM   3612 H HD21 B LEU   A 1 160 ? 6.872  -3.347  -3.916  0.60 33.55 ?  160 LEU   A HD21 1 
ATOM   3613 H HD22 A LEU   A 1 160 ? 9.583  -2.510  -1.249  0.40 20.63 ?  160 LEU   A HD22 1 
ATOM   3614 H HD22 B LEU   A 1 160 ? 7.155  -4.431  -2.790  0.60 33.55 ?  160 LEU   A HD22 1 
ATOM   3615 H HD23 A LEU   A 1 160 ? 10.050 -2.687  0.259   0.40 20.63 ?  160 LEU   A HD23 1 
ATOM   3616 H HD23 B LEU   A 1 160 ? 5.719  -3.763  -2.905  0.60 33.55 ?  160 LEU   A HD23 1 
ATOM   3617 N N    A TYR   A 1 161 ? 6.243  -4.343  2.828   0.40 15.53 ?  161 TYR   A N    1 
ATOM   3618 N N    B TYR   A 1 161 ? 6.409  -4.280  2.311   0.60 17.99 ?  161 TYR   A N    1 
ATOM   3619 C CA   A TYR   A 1 161 ? 6.382  -5.395  3.831   0.40 15.22 ?  161 TYR   A CA   1 
ATOM   3620 C CA   B TYR   A 1 161 ? 6.486  -5.279  3.374   0.60 17.42 ?  161 TYR   A CA   1 
ATOM   3621 C C    A TYR   A 1 161 ? 5.237  -6.400  3.745   0.40 15.93 ?  161 TYR   A C    1 
ATOM   3622 C C    B TYR   A 1 161 ? 5.276  -6.199  3.332   0.60 17.19 ?  161 TYR   A C    1 
ATOM   3623 O O    A TYR   A 1 161 ? 5.461  -7.614  3.784   0.40 15.50 ?  161 TYR   A O    1 
ATOM   3624 O O    B TYR   A 1 161 ? 5.411  -7.428  3.341   0.60 16.39 ?  161 TYR   A O    1 
ATOM   3625 C CB   A TYR   A 1 161 ? 6.457  -4.775  5.227   0.40 14.93 ?  161 TYR   A CB   1 
ATOM   3626 C CB   B TYR   A 1 161 ? 6.587  -4.611  4.748   0.60 17.13 ?  161 TYR   A CB   1 
ATOM   3627 C CG   A TYR   A 1 161 ? 6.384  -5.790  6.341   0.40 14.75 ?  161 TYR   A CG   1 
ATOM   3628 C CG   B TYR   A 1 161 ? 6.475  -5.612  5.878   0.60 16.65 ?  161 TYR   A CG   1 
ATOM   3629 C CD1  A TYR   A 1 161 ? 7.521  -6.452  6.781   0.40 14.83 ?  161 TYR   A CD1  1 
ATOM   3630 C CD1  B TYR   A 1 161 ? 7.580  -6.336  6.298   0.60 16.73 ?  161 TYR   A CD1  1 
ATOM   3631 C CD2  A TYR   A 1 161 ? 5.173  -6.092  6.949   0.40 14.59 ?  161 TYR   A CD2  1 
ATOM   3632 C CD2  B TYR   A 1 161 ? 5.257  -5.852  6.510   0.60 16.39 ?  161 TYR   A CD2  1 
ATOM   3633 C CE1  A TYR   A 1 161 ? 7.455  -7.386  7.795   0.40 15.14 ?  161 TYR   A CE1  1 
ATOM   3634 C CE1  B TYR   A 1 161 ? 7.486  -7.263  7.319   0.60 16.64 ?  161 TYR   A CE1  1 
ATOM   3635 C CE2  A TYR   A 1 161 ? 5.096  -7.023  7.964   0.40 15.28 ?  161 TYR   A CE2  1 
ATOM   3636 C CE2  B TYR   A 1 161 ? 5.151  -6.779  7.537   0.60 16.14 ?  161 TYR   A CE2  1 
ATOM   3637 C CZ   A TYR   A 1 161 ? 6.240  -7.669  8.384   0.40 15.79 ?  161 TYR   A CZ   1 
ATOM   3638 C CZ   B TYR   A 1 161 ? 6.271  -7.482  7.935   0.60 16.68 ?  161 TYR   A CZ   1 
ATOM   3639 O OH   A TYR   A 1 161 ? 6.168  -8.599  9.397   0.40 16.99 ?  161 TYR   A OH   1 
ATOM   3640 O OH   B TYR   A 1 161 ? 6.188  -8.408  8.951   0.60 17.46 ?  161 TYR   A OH   1 
ATOM   3641 H H    A TYR   A 1 161 ? 6.214  -3.548  3.150   0.40 18.63 ?  161 TYR   A H    1 
ATOM   3642 H H    B TYR   A 1 161 ? 6.471  -3.467  2.574   0.60 21.58 ?  161 TYR   A H    1 
ATOM   3643 H HA   A TYR   A 1 161 ? 7.207  -5.874  3.674   0.40 18.26 ?  161 TYR   A HA   1 
ATOM   3644 H HA   B TYR   A 1 161 ? 7.278  -5.821  3.247   0.60 20.90 ?  161 TYR   A HA   1 
ATOM   3645 H HB2  A TYR   A 1 161 ? 7.297  -4.301  5.313   0.40 17.92 ?  161 TYR   A HB2  1 
ATOM   3646 H HB2  B TYR   A 1 161 ? 7.448  -4.167  4.823   0.60 20.55 ?  161 TYR   A HB2  1 
ATOM   3647 H HB3  A TYR   A 1 161 ? 5.716  -4.158  5.338   0.40 17.92 ?  161 TYR   A HB3  1 
ATOM   3648 H HB3  B TYR   A 1 161 ? 5.871  -3.962  4.842   0.60 20.55 ?  161 TYR   A HB3  1 
ATOM   3649 H HD1  A TYR   A 1 161 ? 8.341  -6.264  6.384   0.40 17.80 ?  161 TYR   A HD1  1 
ATOM   3650 H HD1  B TYR   A 1 161 ? 8.399  -6.194  5.887   0.60 20.08 ?  161 TYR   A HD1  1 
ATOM   3651 H HD2  A TYR   A 1 161 ? 4.398  -5.659  6.668   0.40 17.51 ?  161 TYR   A HD2  1 
ATOM   3652 H HD2  B TYR   A 1 161 ? 4.499  -5.377  6.247   0.60 19.66 ?  161 TYR   A HD2  1 
ATOM   3653 H HE1  A TYR   A 1 161 ? 8.226  -7.822  8.079   0.40 18.16 ?  161 TYR   A HE1  1 
ATOM   3654 H HE1  B TYR   A 1 161 ? 8.238  -7.739  7.591   0.60 19.96 ?  161 TYR   A HE1  1 
ATOM   3655 H HE2  A TYR   A 1 161 ? 4.275  -7.214  8.363   0.40 18.33 ?  161 TYR   A HE2  1 
ATOM   3656 H HE2  B TYR   A 1 161 ? 4.330  -6.926  7.956   0.60 19.37 ?  161 TYR   A HE2  1 
ATOM   3657 H HH   A TYR   A 1 161 ? 5.370  -8.667  9.657   0.40 20.38 ?  161 TYR   A HH   1 
ATOM   3658 H HH   B TYR   A 1 161 ? 5.396  -8.447  9.248   0.60 20.95 ?  161 TYR   A HH   1 
ATOM   3659 N N    A ASP   A 1 162 ? 3.999  -5.915  3.629   0.40 16.74 ?  162 ASP   A N    1 
ATOM   3660 N N    B ASP   A 1 162 ? 4.075  -5.617  3.296   0.60 18.02 ?  162 ASP   A N    1 
ATOM   3661 C CA   A ASP   A 1 162 ? 2.852  -6.821  3.595   0.40 17.32 ?  162 ASP   A CA   1 
ATOM   3662 C CA   B ASP   A 1 162 ? 2.867  -6.432  3.217   0.60 18.64 ?  162 ASP   A CA   1 
ATOM   3663 C C    A ASP   A 1 162 ? 2.900  -7.727  2.370   0.40 17.45 ?  162 ASP   A C    1 
ATOM   3664 C C    B ASP   A 1 162 ? 2.907  -7.341  1.994   0.60 19.56 ?  162 ASP   A C    1 
ATOM   3665 O O    A ASP   A 1 162 ? 2.562  -8.913  2.454   0.40 17.50 ?  162 ASP   A O    1 
ATOM   3666 O O    B ASP   A 1 162 ? 2.527  -8.515  2.066   0.60 19.54 ?  162 ASP   A O    1 
ATOM   3667 C CB   A ASP   A 1 162 ? 1.544  -6.025  3.621   0.40 18.19 ?  162 ASP   A CB   1 
ATOM   3668 C CB   B ASP   A 1 162 ? 1.625  -5.538  3.171   0.60 19.39 ?  162 ASP   A CB   1 
ATOM   3669 C CG   A ASP   A 1 162 ? 1.251  -5.416  4.976   0.40 19.60 ?  162 ASP   A CG   1 
ATOM   3670 C CG   B ASP   A 1 162 ? 1.371  -4.793  4.481   0.60 19.89 ?  162 ASP   A CG   1 
ATOM   3671 O OD1  A ASP   A 1 162 ? 1.905  -5.805  5.964   0.40 19.92 ?  162 ASP   A OD1  1 
ATOM   3672 O OD1  B ASP   A 1 162 ? 1.913  -5.198  5.529   0.60 20.23 ?  162 ASP   A OD1  1 
ATOM   3673 O OD2  A ASP   A 1 162 ? 0.359  -4.543  5.047   0.40 20.40 -1 162 ASP   A OD2  1 
ATOM   3674 O OD2  B ASP   A 1 162 ? 0.609  -3.800  4.462   0.60 20.15 -1 162 ASP   A OD2  1 
ATOM   3675 H H    A ASP   A 1 162 ? 3.797  -5.086  3.564   0.40 20.08 ?  162 ASP   A H    1 
ATOM   3676 H H    B ASP   A 1 162 ? 3.938  -4.767  3.308   0.60 21.62 ?  162 ASP   A H    1 
ATOM   3677 H HA   A ASP   A 1 162 ? 2.871  -7.394  4.377   0.40 20.79 ?  162 ASP   A HA   1 
ATOM   3678 H HA   B ASP   A 1 162 ? 2.807  -6.989  4.007   0.60 22.36 ?  162 ASP   A HA   1 
ATOM   3679 H HB2  A ASP   A 1 162 ? 1.604  -5.293  2.998   0.40 21.83 ?  162 ASP   A HB2  1 
ATOM   3680 H HB2  B ASP   A 1 162 ? 1.732  -4.884  2.461   0.60 23.26 ?  162 ASP   A HB2  1 
ATOM   3681 H HB3  A ASP   A 1 162 ? 0.808  -6.613  3.385   0.40 21.83 ?  162 ASP   A HB3  1 
ATOM   3682 H HB3  B ASP   A 1 162 ? 0.846  -6.089  2.999   0.60 23.26 ?  162 ASP   A HB3  1 
ATOM   3683 N N    A LYS   A 1 163 ? 3.322  -7.190  1.224   0.40 18.13 ?  163 LYS   A N    1 
ATOM   3684 N N    B LYS   A 1 163 ? 3.373  -6.814  0.858   0.60 20.67 ?  163 LYS   A N    1 
ATOM   3685 C CA   A LYS   A 1 163 ? 3.387  -7.994  0.007   0.40 19.04 ?  163 LYS   A CA   1 
ATOM   3686 C CA   B LYS   A 1 163 ? 3.491  -7.628  -0.347  0.60 22.18 ?  163 LYS   A CA   1 
ATOM   3687 C C    A LYS   A 1 163 ? 4.506  -9.028  0.086   0.40 18.68 ?  163 LYS   A C    1 
ATOM   3688 C C    B LYS   A 1 163 ? 4.539  -8.722  -0.177  0.60 20.94 ?  163 LYS   A C    1 
ATOM   3689 O O    A LYS   A 1 163 ? 4.354  -10.155 -0.399  0.40 19.12 ?  163 LYS   A O    1 
ATOM   3690 O O    B LYS   A 1 163 ? 4.342  -9.853  -0.633  0.60 20.80 ?  163 LYS   A O    1 
ATOM   3691 C CB   A LYS   A 1 163 ? 3.580  -7.075  -1.200  0.40 20.95 ?  163 LYS   A CB   1 
ATOM   3692 C CB   B LYS   A 1 163 ? 3.851  -6.739  -1.537  0.60 25.14 ?  163 LYS   A CB   1 
ATOM   3693 C CG   A LYS   A 1 163 ? 3.536  -7.777  -2.544  0.40 23.04 ?  163 LYS   A CG   1 
ATOM   3694 C CG   B LYS   A 1 163 ? 4.062  -7.486  -2.847  0.60 28.10 ?  163 LYS   A CG   1 
ATOM   3695 C CD   A LYS   A 1 163 ? 3.929  -6.824  -3.663  0.40 25.22 ?  163 LYS   A CD   1 
ATOM   3696 C CD   B LYS   A 1 163 ? 4.892  -6.648  -3.803  0.60 30.96 ?  163 LYS   A CD   1 
ATOM   3697 C CE   A LYS   A 1 163 ? 3.835  -7.491  -5.024  0.40 26.91 ?  163 LYS   A CE   1 
ATOM   3698 C CE   B LYS   A 1 163 ? 4.584  -6.955  -5.257  0.60 33.02 ?  163 LYS   A CE   1 
ATOM   3699 N NZ   A LYS   A 1 163 ? 4.516  -6.693  -6.083  0.40 27.68 ?  163 LYS   A NZ   1 
ATOM   3700 N NZ   B LYS   A 1 163 ? 5.311  -6.023  -6.163  0.60 34.23 ?  163 LYS   A NZ   1 
ATOM   3701 H H    A LYS   A 1 163 ? 3.571  -6.373  1.130   0.40 21.75 ?  163 LYS   A H    1 
ATOM   3702 H H    B LYS   A 1 163 ? 3.619  -5.994  0.763   0.60 24.80 ?  163 LYS   A H    1 
ATOM   3703 H HA   A LYS   A 1 163 ? 2.543  -8.462  -0.109  0.40 22.84 ?  163 LYS   A HA   1 
ATOM   3704 H HA   B LYS   A 1 163 ? 2.635  -8.048  -0.532  0.60 26.61 ?  163 LYS   A HA   1 
ATOM   3705 H HB2  A LYS   A 1 163 ? 2.874  -6.405  -1.199  0.40 25.14 ?  163 LYS   A HB2  1 
ATOM   3706 H HB2  B LYS   A 1 163 ? 3.130  -6.101  -1.678  0.60 30.16 ?  163 LYS   A HB2  1 
ATOM   3707 H HB3  A LYS   A 1 163 ? 4.441  -6.638  -1.125  0.40 25.14 ?  163 LYS   A HB3  1 
ATOM   3708 H HB3  B LYS   A 1 163 ? 4.669  -6.263  -1.332  0.60 30.16 ?  163 LYS   A HB3  1 
ATOM   3709 H HG2  A LYS   A 1 163 ? 4.161  -8.518  -2.544  0.40 27.65 ?  163 LYS   A HG2  1 
ATOM   3710 H HG2  B LYS   A 1 163 ? 4.535  -8.319  -2.688  0.60 33.72 ?  163 LYS   A HG2  1 
ATOM   3711 H HG3  A LYS   A 1 163 ? 2.635  -8.094  -2.715  0.40 27.65 ?  163 LYS   A HG3  1 
ATOM   3712 H HG3  B LYS   A 1 163 ? 3.202  -7.662  -3.258  0.60 33.72 ?  163 LYS   A HG3  1 
ATOM   3713 H HD2  A LYS   A 1 163 ? 3.330  -6.060  -3.658  0.40 30.27 ?  163 LYS   A HD2  1 
ATOM   3714 H HD2  B LYS   A 1 163 ? 4.706  -5.711  -3.645  0.60 37.15 ?  163 LYS   A HD2  1 
ATOM   3715 H HD3  A LYS   A 1 163 ? 4.844  -6.532  -3.528  0.40 30.27 ?  163 LYS   A HD3  1 
ATOM   3716 H HD3  B LYS   A 1 163 ? 5.833  -6.832  -3.648  0.60 37.15 ?  163 LYS   A HD3  1 
ATOM   3717 H HE2  A LYS   A 1 163 ? 4.242  -8.369  -4.983  0.40 32.29 ?  163 LYS   A HE2  1 
ATOM   3718 H HE2  B LYS   A 1 163 ? 4.859  -7.861  -5.464  0.60 39.62 ?  163 LYS   A HE2  1 
ATOM   3719 H HE3  A LYS   A 1 163 ? 2.903  -7.572  -5.269  0.40 32.29 ?  163 LYS   A HE3  1 
ATOM   3720 H HE3  B LYS   A 1 163 ? 3.631  -6.850  -5.411  0.60 39.62 ?  163 LYS   A HE3  1 
ATOM   3721 H HZ1  A LYS   A 1 163 ? 4.447  -7.108  -6.867  0.40 33.22 ?  163 LYS   A HZ1  1 
ATOM   3722 H HZ1  B LYS   A 1 163 ? 5.247  -6.303  -7.004  0.60 41.07 ?  163 LYS   A HZ1  1 
ATOM   3723 H HZ2  A LYS   A 1 163 ? 4.139  -5.889  -6.146  0.40 33.22 ?  163 LYS   A HZ2  1 
ATOM   3724 H HZ2  B LYS   A 1 163 ? 4.961  -5.206  -6.102  0.60 41.07 ?  163 LYS   A HZ2  1 
ATOM   3725 H HZ3  A LYS   A 1 163 ? 5.378  -6.593  -5.884  0.40 33.22 ?  163 LYS   A HZ3  1 
ATOM   3726 H HZ3  B LYS   A 1 163 ? 6.170  -5.986  -5.933  0.60 41.07 ?  163 LYS   A HZ3  1 
ATOM   3727 N N    A LEU   A 1 164 ? 5.640  -8.664  0.686   0.40 17.26 ?  164 LEU   A N    1 
ATOM   3728 N N    B LEU   A 1 164 ? 5.667  -8.399  0.455   0.60 19.42 ?  164 LEU   A N    1 
ATOM   3729 C CA   A LEU   A 1 164 ? 6.733  -9.619  0.844   0.40 16.56 ?  164 LEU   A CA   1 
ATOM   3730 C CA   B LEU   A 1 164 ? 6.723  -9.388  0.646   0.60 18.80 ?  164 LEU   A CA   1 
ATOM   3731 C C    A LEU   A 1 164 ? 6.312  -10.789 1.723   0.40 16.98 ?  164 LEU   A C    1 
ATOM   3732 C C    B LEU   A 1 164 ? 6.229  -10.550 1.496   0.60 18.39 ?  164 LEU   A C    1 
ATOM   3733 O O    A LEU   A 1 164 ? 6.643  -11.945 1.435   0.40 16.93 ?  164 LEU   A O    1 
ATOM   3734 O O    B LEU   A 1 164 ? 6.460  -11.720 1.167   0.60 18.31 ?  164 LEU   A O    1 
ATOM   3735 C CB   A LEU   A 1 164 ? 7.944  -8.917  1.454   0.40 15.99 ?  164 LEU   A CB   1 
ATOM   3736 C CB   B LEU   A 1 164 ? 7.934  -8.726  1.300   0.60 18.92 ?  164 LEU   A CB   1 
ATOM   3737 C CG   A LEU   A 1 164 ? 8.691  -7.915  0.574   0.40 16.04 ?  164 LEU   A CG   1 
ATOM   3738 C CG   B LEU   A 1 164 ? 8.790  -7.823  0.411   0.60 19.32 ?  164 LEU   A CG   1 
ATOM   3739 C CD1  A LEU   A 1 164 ? 9.569  -7.025  1.440   0.40 16.29 ?  164 LEU   A CD1  1 
ATOM   3740 C CD1  B LEU   A 1 164 ? 9.752  -7.013  1.266   0.60 19.41 ?  164 LEU   A CD1  1 
ATOM   3741 C CD2  A LEU   A 1 164 ? 9.527  -8.633  -0.472  0.40 16.35 ?  164 LEU   A CD2  1 
ATOM   3742 C CD2  B LEU   A 1 164 ? 9.550  -8.635  -0.629  0.60 19.72 ?  164 LEU   A CD2  1 
ATOM   3743 H H    A LEU   A 1 164 ? 5.793  -7.883  1.007   0.40 20.70 ?  164 LEU   A H    1 
ATOM   3744 H H    B LEU   A 1 164 ? 5.841  -7.621  0.779   0.60 23.30 ?  164 LEU   A H    1 
ATOM   3745 H HA   A LEU   A 1 164 ? 6.983  -9.966  -0.025  0.40 19.87 ?  164 LEU   A HA   1 
ATOM   3746 H HA   B LEU   A 1 164 ? 6.993  -9.735  -0.217  0.60 22.56 ?  164 LEU   A HA   1 
ATOM   3747 H HB2  A LEU   A 1 164 ? 7.648  -8.437  2.241   0.40 19.19 ?  164 LEU   A HB2  1 
ATOM   3748 H HB2  B LEU   A 1 164 ? 7.620  -8.182  2.039   0.60 22.70 ?  164 LEU   A HB2  1 
ATOM   3749 H HB3  A LEU   A 1 164 ? 8.584  -9.596  1.713   0.40 19.19 ?  164 LEU   A HB3  1 
ATOM   3750 H HB3  B LEU   A 1 164 ? 8.513  -9.424  1.637   0.60 22.70 ?  164 LEU   A HB3  1 
ATOM   3751 H HG   A LEU   A 1 164 ? 8.050  -7.349  0.115   0.40 19.24 ?  164 LEU   A HG   1 
ATOM   3752 H HG   B LEU   A 1 164 ? 8.212  -7.201  -0.058  0.60 23.19 ?  164 LEU   A HG   1 
ATOM   3753 H HD11 A LEU   A 1 164 ? 10.051 -6.405  0.872   0.40 19.55 ?  164 LEU   A HD11 1 
ATOM   3754 H HD11 B LEU   A 1 164 ? 10.291 -6.451  0.689   0.60 23.29 ?  164 LEU   A HD11 1 
ATOM   3755 H HD12 A LEU   A 1 164 ? 9.007  -6.536  2.063   0.40 19.55 ?  164 LEU   A HD12 1 
ATOM   3756 H HD12 B LEU   A 1 164 ? 9.240  -6.463  1.881   0.60 23.29 ?  164 LEU   A HD12 1 
ATOM   3757 H HD13 A LEU   A 1 164 ? 10.196 -7.581  1.930   0.40 19.55 ?  164 LEU   A HD13 1 
ATOM   3758 H HD13 B LEU   A 1 164 ? 10.321 -7.622  1.763   0.60 23.29 ?  164 LEU   A HD13 1 
ATOM   3759 H HD21 A LEU   A 1 164 ? 9.997  -7.975  -1.008  0.40 19.62 ?  164 LEU   A HD21 1 
ATOM   3760 H HD21 B LEU   A 1 164 ? 10.141 -8.042  -1.121  0.60 23.66 ?  164 LEU   A HD21 1 
ATOM   3761 H HD22 A LEU   A 1 164 ? 10.166 -9.210  -0.024  0.40 19.62 ?  164 LEU   A HD22 1 
ATOM   3762 H HD22 B LEU   A 1 164 ? 10.069 -9.319  -0.179  0.60 23.66 ?  164 LEU   A HD22 1 
ATOM   3763 H HD23 A LEU   A 1 164 ? 8.941  -9.162  -1.035  0.40 19.62 ?  164 LEU   A HD23 1 
ATOM   3764 H HD23 B LEU   A 1 164 ? 8.916  -9.046  -1.236  0.60 23.66 ?  164 LEU   A HD23 1 
ATOM   3765 N N    A VAL   A 1 165 ? 5.592  -10.504 2.808   0.40 16.96 ?  165 VAL   A N    1 
ATOM   3766 N N    B VAL   A 1 165 ? 5.553  -10.243 2.603   0.60 17.44 ?  165 VAL   A N    1 
ATOM   3767 C CA   A VAL   A 1 165 ? 5.135  -11.564 3.701   0.40 17.67 ?  165 VAL   A CA   1 
ATOM   3768 C CA   B VAL   A 1 165 ? 5.041  -11.295 3.477   0.60 17.87 ?  165 VAL   A CA   1 
ATOM   3769 C C    A VAL   A 1 165 ? 4.104  -12.442 3.005   0.40 17.70 ?  165 VAL   A C    1 
ATOM   3770 C C    B VAL   A 1 165 ? 3.995  -12.129 2.747   0.60 17.82 ?  165 VAL   A C    1 
ATOM   3771 O O    A VAL   A 1 165 ? 4.216  -13.674 2.995   0.40 17.69 ?  165 VAL   A O    1 
ATOM   3772 O O    B VAL   A 1 165 ? 4.058  -13.364 2.726   0.60 17.37 ?  165 VAL   A O    1 
ATOM   3773 C CB   A VAL   A 1 165 ? 4.579  -10.954 5.001   0.40 18.18 ?  165 VAL   A CB   1 
ATOM   3774 C CB   B VAL   A 1 165 ? 4.489  -10.685 4.780   0.60 18.83 ?  165 VAL   A CB   1 
ATOM   3775 C CG1  A VAL   A 1 165 ? 3.804  -11.996 5.796   0.40 18.36 ?  165 VAL   A CG1  1 
ATOM   3776 C CG1  B VAL   A 1 165 ? 3.754  -11.735 5.601   0.60 19.06 ?  165 VAL   A CG1  1 
ATOM   3777 C CG2  A VAL   A 1 165 ? 5.706  -10.358 5.832   0.40 18.59 ?  165 VAL   A CG2  1 
ATOM   3778 C CG2  B VAL   A 1 165 ? 5.616  -10.061 5.590   0.60 19.17 ?  165 VAL   A CG2  1 
ATOM   3779 H H    A VAL   A 1 165 ? 5.361  -9.714  3.049   0.40 20.35 ?  165 VAL   A H    1 
ATOM   3780 H H    B VAL   A 1 165 ? 5.381  -9.442  2.868   0.60 20.92 ?  165 VAL   A H    1 
ATOM   3781 H HA   A VAL   A 1 165 ? 5.889  -12.125 3.940   0.40 21.20 ?  165 VAL   A HA   1 
ATOM   3782 H HA   B VAL   A 1 165 ? 5.773  -11.881 3.721   0.60 21.44 ?  165 VAL   A HA   1 
ATOM   3783 H HB   A VAL   A 1 165 ? 3.968  -10.236 4.776   0.40 21.81 ?  165 VAL   A HB   1 
ATOM   3784 H HB   B VAL   A 1 165 ? 3.860  -9.979  4.561   0.60 22.60 ?  165 VAL   A HB   1 
ATOM   3785 H HG11 A VAL   A 1 165 ? 3.714  -11.690 6.712   0.40 22.03 ?  165 VAL   A HG11 1 
ATOM   3786 H HG11 B VAL   A 1 165 ? 3.651  -11.412 6.511   0.60 22.87 ?  165 VAL   A HG11 1 
ATOM   3787 H HG12 A VAL   A 1 165 ? 2.923  -12.106 5.400   0.40 22.03 ?  165 VAL   A HG12 1 
ATOM   3788 H HG12 B VAL   A 1 165 ? 2.881  -11.891 5.208   0.60 22.87 ?  165 VAL   A HG12 1 
ATOM   3789 H HG13 A VAL   A 1 165 ? 4.287  -12.835 5.773   0.40 22.03 ?  165 VAL   A HG13 1 
ATOM   3790 H HG13 B VAL   A 1 165 ? 4.271  -12.555 5.601   0.60 22.87 ?  165 VAL   A HG13 1 
ATOM   3791 H HG21 A VAL   A 1 165 ? 5.334  -9.977  6.643   0.40 22.31 ?  165 VAL   A HG21 1 
ATOM   3792 H HG21 B VAL   A 1 165 ? 5.252  -9.695  6.413   0.60 23.00 ?  165 VAL   A HG21 1 
ATOM   3793 H HG22 A VAL   A 1 165 ? 6.339  -11.058 6.055   0.40 22.31 ?  165 VAL   A HG22 1 
ATOM   3794 H HG22 B VAL   A 1 165 ? 6.273  -10.745 5.797   0.60 23.00 ?  165 VAL   A HG22 1 
ATOM   3795 H HG23 A VAL   A 1 165 ? 6.147  -9.665  5.314   0.40 22.31 ?  165 VAL   A HG23 1 
ATOM   3796 H HG23 B VAL   A 1 165 ? 6.028  -9.353  5.070   0.60 23.00 ?  165 VAL   A HG23 1 
ATOM   3797 N N    A SER   A 1 166 ? 3.081  -11.819 2.413   0.40 17.84 ?  166 SER   A N    1 
ATOM   3798 N N    B SER   A 1 166 ? 3.024  -11.466 2.119   0.60 17.79 ?  166 SER   A N    1 
ATOM   3799 C CA   A SER   A 1 166 ? 1.973  -12.582 1.846   0.40 18.51 ?  166 SER   A CA   1 
ATOM   3800 C CA   B SER   A 1 166 ? 1.900  -12.183 1.527   0.60 18.84 ?  166 SER   A CA   1 
ATOM   3801 C C    A SER   A 1 166 ? 2.417  -13.450 0.679   0.40 18.97 ?  166 SER   A C    1 
ATOM   3802 C C    B SER   A 1 166 ? 2.309  -13.063 0.353   0.60 18.68 ?  166 SER   A C    1 
ATOM   3803 O O    A SER   A 1 166 ? 1.869  -14.542 0.477   0.40 19.48 ?  166 SER   A O    1 
ATOM   3804 O O    B SER   A 1 166 ? 1.563  -13.988 0.005   0.60 19.05 ?  166 SER   A O    1 
ATOM   3805 C CB   A SER   A 1 166 ? 0.858  -11.637 1.396   0.40 19.65 ?  166 SER   A CB   1 
ATOM   3806 C CB   B SER   A 1 166 ? 0.827  -11.195 1.068   0.60 20.66 ?  166 SER   A CB   1 
ATOM   3807 O OG   A SER   A 1 166 ? 0.245  -11.013 2.511   0.40 21.36 ?  166 SER   A OG   1 
ATOM   3808 O OG   B SER   A 1 166 ? 0.276  -10.473 2.157   0.60 23.13 ?  166 SER   A OG   1 
ATOM   3809 H H    A SER   A 1 166 ? 3.005  -10.967 2.334   0.40 21.40 ?  166 SER   A H    1 
ATOM   3810 H H    B SER   A 1 166 ? 2.991  -10.611 2.031   0.60 21.35 ?  166 SER   A H    1 
ATOM   3811 H HA   A SER   A 1 166 ? 1.606  -13.166 2.528   0.40 22.21 ?  166 SER   A HA   1 
ATOM   3812 H HA   B SER   A 1 166 ? 1.506  -12.757 2.200   0.60 22.60 ?  166 SER   A HA   1 
ATOM   3813 H HB2  A SER   A 1 166 ? 1.234  -10.959 0.812   0.40 23.58 ?  166 SER   A HB2  1 
ATOM   3814 H HB2  B SER   A 1 166 ? 1.219  -10.564 0.451   0.60 24.79 ?  166 SER   A HB2  1 
ATOM   3815 H HB3  A SER   A 1 166 ? 0.184  -12.146 0.916   0.40 23.58 ?  166 SER   A HB3  1 
ATOM   3816 H HB3  B SER   A 1 166 ? 0.114  -11.690 0.631   0.60 24.79 ?  166 SER   A HB3  1 
ATOM   3817 H HG   A SER   A 1 166 ? 0.810  -10.548 2.925   0.40 25.63 ?  166 SER   A HG   1 
ATOM   3818 H HG   B SER   A 1 166 ? 0.882  -10.052 2.559   0.60 27.75 ?  166 SER   A HG   1 
ATOM   3819 N N    A SER   A 1 167 ? 3.394  -12.987 -0.097  0.40 19.24 ?  167 SER   A N    1 
ATOM   3820 N N    B SER   A 1 167 ? 3.459  -12.795 -0.270  0.60 18.85 ?  167 SER   A N    1 
ATOM   3821 C CA   A SER   A 1 167 ? 3.855  -13.707 -1.276  0.40 20.09 ?  167 SER   A CA   1 
ATOM   3822 C CA   B SER   A 1 167 ? 3.902  -13.552 -1.434  0.60 19.74 ?  167 SER   A CA   1 
ATOM   3823 C C    A SER   A 1 167 ? 5.024  -14.637 -0.986  0.40 20.36 ?  167 SER   A C    1 
ATOM   3824 C C    B SER   A 1 167 ? 5.030  -14.524 -1.124  0.60 19.99 ?  167 SER   A C    1 
ATOM   3825 O O    A SER   A 1 167 ? 5.545  -15.261 -1.917  0.40 20.62 ?  167 SER   A O    1 
ATOM   3826 O O    B SER   A 1 167 ? 5.498  -15.220 -2.033  0.60 20.66 ?  167 SER   A O    1 
ATOM   3827 C CB   A SER   A 1 167 ? 4.254  -12.718 -2.380  0.40 20.81 ?  167 SER   A CB   1 
ATOM   3828 C CB   B SER   A 1 167 ? 4.333  -12.602 -2.561  0.60 20.28 ?  167 SER   A CB   1 
ATOM   3829 O OG   A SER   A 1 167 ? 5.371  -11.938 -1.987  0.40 21.41 ?  167 SER   A OG   1 
ATOM   3830 O OG   B SER   A 1 167 ? 5.424  -11.786 -2.162  0.60 20.84 ?  167 SER   A OG   1 
ATOM   3831 H H    A SER   A 1 167 ? 3.810  -12.244 0.043   0.40 23.08 ?  167 SER   A H    1 
ATOM   3832 H H    B SER   A 1 167 ? 4.005  -12.166 -0.033  0.60 22.62 ?  167 SER   A H    1 
ATOM   3833 H HA   A SER   A 1 167 ? 3.124  -14.241 -1.614  0.40 24.10 ?  167 SER   A HA   1 
ATOM   3834 H HA   B SER   A 1 167 ? 3.153  -14.067 -1.762  0.60 23.68 ?  167 SER   A HA   1 
ATOM   3835 H HB2  A SER   A 1 167 ? 4.485  -13.216 -3.180  0.40 24.97 ?  167 SER   A HB2  1 
ATOM   3836 H HB2  B SER   A 1 167 ? 4.598  -13.132 -3.329  0.60 24.33 ?  167 SER   A HB2  1 
ATOM   3837 H HB3  A SER   A 1 167 ? 3.500  -12.131 -2.566  0.40 24.97 ?  167 SER   A HB3  1 
ATOM   3838 H HB3  B SER   A 1 167 ? 3.576  -12.037 -2.801  0.60 24.33 ?  167 SER   A HB3  1 
ATOM   3839 H HG   A SER   A 1 167 ? 5.177  -11.485 -1.305  0.40 25.69 ?  167 SER   A HG   1 
ATOM   3840 H HG   B SER   A 1 167 ? 5.193  -11.313 -1.505  0.60 25.00 ?  167 SER   A HG   1 
ATOM   3841 N N    A PHE   A 1 168 ? 5.453  -14.750 0.268   0.40 20.65 ?  168 PHE   A N    1 
ATOM   3842 N N    B PHE   A 1 168 ? 5.480  -14.597 0.125   0.60 19.80 ?  168 PHE   A N    1 
ATOM   3843 C CA   A PHE   A 1 168 ? 6.639  -15.539 0.567   0.40 21.61 ?  168 PHE   A CA   1 
ATOM   3844 C CA   B PHE   A 1 168 ? 6.652  -15.404 0.437   0.60 20.93 ?  168 PHE   A CA   1 
ATOM   3845 C C    A PHE   A 1 168 ? 6.329  -17.026 0.479   0.40 23.89 ?  168 PHE   A C    1 
ATOM   3846 C C    B PHE   A 1 168 ? 6.313  -16.886 0.378   0.60 23.13 ?  168 PHE   A C    1 
ATOM   3847 O O    A PHE   A 1 168 ? 5.376  -17.511 1.096   0.40 23.96 ?  168 PHE   A O    1 
ATOM   3848 O O    B PHE   A 1 168 ? 5.314  -17.330 0.952   0.60 23.26 ?  168 PHE   A O    1 
ATOM   3849 C CB   A PHE   A 1 168 ? 7.176  -15.218 1.958   0.40 20.89 ?  168 PHE   A CB   1 
ATOM   3850 C CB   B PHE   A 1 168 ? 7.190  -15.064 1.823   0.60 20.57 ?  168 PHE   A CB   1 
ATOM   3851 C CG   A PHE   A 1 168 ? 8.434  -15.966 2.291   0.40 20.22 ?  168 PHE   A CG   1 
ATOM   3852 C CG   B PHE   A 1 168 ? 8.441  -15.815 2.167   0.60 19.92 ?  168 PHE   A CG   1 
ATOM   3853 C CD1  A PHE   A 1 168 ? 9.627  -15.630 1.678   0.40 20.18 ?  168 PHE   A CD1  1 
ATOM   3854 C CD1  B PHE   A 1 168 ? 9.647  -15.454 1.598   0.60 19.87 ?  168 PHE   A CD1  1 
ATOM   3855 C CD2  A PHE   A 1 168 ? 8.423  -17.020 3.191   0.40 20.08 ?  168 PHE   A CD2  1 
ATOM   3856 C CD2  B PHE   A 1 168 ? 8.413  -16.895 3.034   0.60 19.71 ?  168 PHE   A CD2  1 
ATOM   3857 C CE1  A PHE   A 1 168 ? 10.789 -16.319 1.965   0.40 19.91 ?  168 PHE   A CE1  1 
ATOM   3858 C CE1  B PHE   A 1 168 ? 10.803 -16.148 1.897   0.60 19.67 ?  168 PHE   A CE1  1 
ATOM   3859 C CE2  A PHE   A 1 168 ? 9.586  -17.712 3.485   0.40 20.08 ?  168 PHE   A CE2  1 
ATOM   3860 C CE2  B PHE   A 1 168 ? 9.571  -17.593 3.338   0.60 19.93 ?  168 PHE   A CE2  1 
ATOM   3861 C CZ   A PHE   A 1 168 ? 10.768 -17.361 2.870   0.40 19.87 ?  168 PHE   A CZ   1 
ATOM   3862 C CZ   B PHE   A 1 168 ? 10.764 -17.218 2.769   0.60 19.61 ?  168 PHE   A CZ   1 
ATOM   3863 H H    A PHE   A 1 168 ? 5.082  -14.384 0.952   0.40 24.78 ?  168 PHE   A H    1 
ATOM   3864 H H    B PHE   A 1 168 ? 5.135  -14.190 0.799   0.60 23.76 ?  168 PHE   A H    1 
ATOM   3865 H HA   A PHE   A 1 168 ? 7.330  -15.336 -0.081  0.40 25.93 ?  168 PHE   A HA   1 
ATOM   3866 H HA   B PHE   A 1 168 ? 7.350  -15.223 -0.213  0.60 25.11 ?  168 PHE   A HA   1 
ATOM   3867 H HB2  A PHE   A 1 168 ? 7.371  -14.270 2.009   0.40 25.07 ?  168 PHE   A HB2  1 
ATOM   3868 H HB2  B PHE   A 1 168 ? 7.393  -14.117 1.860   0.60 24.69 ?  168 PHE   A HB2  1 
ATOM   3869 H HB3  A PHE   A 1 168 ? 6.505  -15.455 2.617   0.40 25.07 ?  168 PHE   A HB3  1 
ATOM   3870 H HB3  B PHE   A 1 168 ? 6.519  -15.286 2.485   0.60 24.69 ?  168 PHE   A HB3  1 
ATOM   3871 H HD1  A PHE   A 1 168 ? 9.649  -14.929 1.067   0.40 24.21 ?  168 PHE   A HD1  1 
ATOM   3872 H HD1  B PHE   A 1 168 ? 9.686  -14.735 1.011   0.60 23.84 ?  168 PHE   A HD1  1 
ATOM   3873 H HD2  A PHE   A 1 168 ? 7.627  -17.261 3.609   0.40 24.09 ?  168 PHE   A HD2  1 
ATOM   3874 H HD2  B PHE   A 1 168 ? 7.606  -17.153 3.420   0.60 23.65 ?  168 PHE   A HD2  1 
ATOM   3875 H HE1  A PHE   A 1 168 ? 11.589 -16.081 1.551   0.40 23.88 ?  168 PHE   A HE1  1 
ATOM   3876 H HE1  B PHE   A 1 168 ? 11.616 -15.895 1.514   0.60 23.60 ?  168 PHE   A HE1  1 
ATOM   3877 H HE2  A PHE   A 1 168 ? 9.568  -18.416 4.094   0.40 24.09 ?  168 PHE   A HE2  1 
ATOM   3878 H HE2  B PHE   A 1 168 ? 9.535  -18.316 3.925   0.60 23.91 ?  168 PHE   A HE2  1 
ATOM   3879 H HZ   A PHE   A 1 168 ? 11.551 -17.826 3.065   0.40 23.84 ?  168 PHE   A HZ   1 
ATOM   3880 H HZ   B PHE   A 1 168 ? 11.545 -17.685 2.971   0.60 23.53 ?  168 PHE   A HZ   1 
ATOM   3881 N N    A LEU   A 1 169 ? 7.154  -17.753 -0.268  0.40 26.71 ?  169 LEU   A N    1 
ATOM   3882 N N    B LEU   A 1 169 ? 7.162  -17.656 -0.298  0.60 26.50 ?  169 LEU   A N    1 
ATOM   3883 C CA   A LEU   A 1 169 ? 6.967  -19.188 -0.422  0.40 30.12 ?  169 LEU   A CA   1 
ATOM   3884 C CA   B LEU   A 1 169 ? 6.938  -19.090 -0.425  0.60 30.59 ?  169 LEU   A CA   1 
ATOM   3885 C C    A LEU   A 1 169 ? 7.877  -19.950 0.532   0.40 31.23 ?  169 LEU   A C    1 
ATOM   3886 C C    B LEU   A 1 169 ? 7.745  -19.853 0.619   0.60 31.76 ?  169 LEU   A C    1 
ATOM   3887 O O    A LEU   A 1 169 ? 7.435  -20.423 1.580   0.40 31.45 ?  169 LEU   A O    1 
ATOM   3888 O O    B LEU   A 1 169 ? 7.180  -20.413 1.560   0.60 31.88 ?  169 LEU   A O    1 
ATOM   3889 C CB   A LEU   A 1 169 ? 7.242  -19.611 -1.866  0.40 31.85 ?  169 LEU   A CB   1 
ATOM   3890 C CB   B LEU   A 1 169 ? 7.293  -19.569 -1.836  0.60 32.66 ?  169 LEU   A CB   1 
ATOM   3891 C CG   A LEU   A 1 169 ? 6.934  -21.069 -2.213  0.40 33.41 ?  169 LEU   A CG   1 
ATOM   3892 C CG   B LEU   A 1 169 ? 7.020  -21.045 -2.144  0.60 34.54 ?  169 LEU   A CG   1 
ATOM   3893 C CD1  A LEU   A 1 169 ? 5.506  -21.423 -1.833  0.40 33.82 ?  169 LEU   A CD1  1 
ATOM   3894 C CD1  B LEU   A 1 169 ? 5.602  -21.430 -1.750  0.60 35.03 ?  169 LEU   A CD1  1 
ATOM   3895 C CD2  A LEU   A 1 169 ? 7.172  -21.325 -3.695  0.40 33.93 ?  169 LEU   A CD2  1 
ATOM   3896 C CD2  B LEU   A 1 169 ? 7.260  -21.337 -3.619  0.60 35.10 ?  169 LEU   A CD2  1 
ATOM   3897 O OXT  A LEU   A 1 169 ? 9.073  -20.106 0.282   0.40 31.26 -1 169 LEU   A OXT  1 
ATOM   3898 O OXT  B LEU   A 1 169 ? 8.975  -19.919 0.557   0.60 31.68 -1 169 LEU   A OXT  1 
ATOM   3899 H H    A LEU   A 1 169 ? 7.831  -17.437 -0.695  0.40 32.05 ?  169 LEU   A H    1 
ATOM   3900 H H    B LEU   A 1 169 ? 7.874  -17.371 -0.690  0.60 31.80 ?  169 LEU   A H    1 
ATOM   3901 H HA   A LEU   A 1 169 ? 6.050  -19.409 -0.206  0.40 36.14 ?  169 LEU   A HA   1 
ATOM   3902 H HA   B LEU   A 1 169 ? 6.001  -19.273 -0.271  0.60 36.71 ?  169 LEU   A HA   1 
ATOM   3903 H HB2  A LEU   A 1 169 ? 6.705  -19.057 -2.452  0.40 38.21 ?  169 LEU   A HB2  1 
ATOM   3904 H HB2  B LEU   A 1 169 ? 6.781  -19.046 -2.472  0.60 39.18 ?  169 LEU   A HB2  1 
ATOM   3905 H HB3  A LEU   A 1 169 ? 8.182  -19.464 -2.053  0.40 38.21 ?  169 LEU   A HB3  1 
ATOM   3906 H HB3  B LEU   A 1 169 ? 8.239  -19.417 -1.982  0.60 39.18 ?  169 LEU   A HB3  1 
ATOM   3907 H HG   A LEU   A 1 169 ? 7.530  -21.648 -1.711  0.40 40.10 ?  169 LEU   A HG   1 
ATOM   3908 H HG   B LEU   A 1 169 ? 7.632  -21.595 -1.630  0.60 41.44 ?  169 LEU   A HG   1 
ATOM   3909 H HD11 A LEU   A 1 169 ? 5.274  -22.273 -2.237  0.40 40.58 ?  169 LEU   A HD11 1 
ATOM   3910 H HD11 B LEU   A 1 169 ? 5.399  -22.305 -2.115  0.60 42.04 ?  169 LEU   A HD11 1 
ATOM   3911 H HD12 A LEU   A 1 169 ? 5.442  -21.487 -0.867  0.40 40.58 ?  169 LEU   A HD12 1 
ATOM   3912 H HD12 B LEU   A 1 169 ? 5.538  -21.453 -0.782  0.60 42.04 ?  169 LEU   A HD12 1 
ATOM   3913 H HD13 A LEU   A 1 169 ? 4.912  -20.728 -2.160  0.40 40.58 ?  169 LEU   A HD13 1 
ATOM   3914 H HD13 B LEU   A 1 169 ? 4.986  -20.772 -2.109  0.60 42.04 ?  169 LEU   A HD13 1 
ATOM   3915 H HD21 A LEU   A 1 169 ? 6.976  -22.255 -3.890  0.40 40.72 ?  169 LEU   A HD21 1 
ATOM   3916 H HD21 B LEU   A 1 169 ? 7.085  -22.277 -3.788  0.60 42.11 ?  169 LEU   A HD21 1 
ATOM   3917 H HD22 A LEU   A 1 169 ? 6.588  -20.748 -4.212  0.40 40.72 ?  169 LEU   A HD22 1 
ATOM   3918 H HD22 B LEU   A 1 169 ? 6.660  -20.790 -4.151  0.60 42.11 ?  169 LEU   A HD22 1 
ATOM   3919 H HD23 A LEU   A 1 169 ? 8.099  -21.131 -3.904  0.40 40.72 ?  169 LEU   A HD23 1 
ATOM   3920 H HD23 B LEU   A 1 169 ? 8.181  -21.128 -3.837  0.60 42.11 ?  169 LEU   A HD23 1 
ATOM   3921 N N    A SER   B 1 1   ? 50.698 -9.207  -23.716 0.40 29.03 ?  1   SER   B N    1 
ATOM   3922 N N    B SER   B 1 1   ? 50.756 -9.209  -23.723 0.60 28.00 ?  1   SER   B N    1 
ATOM   3923 C CA   A SER   B 1 1   ? 51.228 -10.272 -22.842 0.40 29.13 ?  1   SER   B CA   1 
ATOM   3924 C CA   B SER   B 1 1   ? 51.184 -10.219 -22.733 0.60 28.07 ?  1   SER   B CA   1 
ATOM   3925 C C    A SER   B 1 1   ? 50.167 -11.329 -22.590 0.40 28.11 ?  1   SER   B C    1 
ATOM   3926 C C    B SER   B 1 1   ? 50.069 -11.213 -22.449 0.60 26.36 ?  1   SER   B C    1 
ATOM   3927 O O    A SER   B 1 1   ? 48.976 -11.121 -22.843 0.40 28.07 ?  1   SER   B O    1 
ATOM   3928 O O    B SER   B 1 1   ? 48.898 -11.004 -22.794 0.60 25.81 ?  1   SER   B O    1 
ATOM   3929 C CB   A SER   B 1 1   ? 51.698 -9.693  -21.512 0.40 29.37 ?  1   SER   B CB   1 
ATOM   3930 C CB   B SER   B 1 1   ? 51.617 -9.561  -21.428 0.60 28.75 ?  1   SER   B CB   1 
ATOM   3931 O OG   A SER   B 1 1   ? 50.595 -9.354  -20.694 0.40 30.71 ?  1   SER   B OG   1 
ATOM   3932 O OG   B SER   B 1 1   ? 50.535 -9.509  -20.516 0.60 30.71 ?  1   SER   B OG   1 
ATOM   3933 H H1   A SER   B 1 1   ? 50.280 -9.579  -24.405 0.40 34.83 ?  1   SER   B H1   1 
ATOM   3934 H H1   B SER   B 1 1   ? 51.416 -8.626  -23.842 0.60 33.60 ?  1   SER   B H1   1 
ATOM   3935 H H2   A SER   B 1 1   ? 50.133 -8.707  -23.252 0.40 34.83 ?  1   SER   B H2   1 
ATOM   3936 H H2   B SER   B 1 1   ? 50.572 -9.616  -24.490 0.60 33.60 ?  1   SER   B H2   1 
ATOM   3937 H H3   A SER   B 1 1   ? 51.376 -8.712  -24.006 0.40 34.83 ?  1   SER   B H3   1 
ATOM   3938 H H3   B SER   B 1 1   ? 50.036 -8.794  -23.418 0.60 33.60 ?  1   SER   B H3   1 
ATOM   3939 H HA   A SER   B 1 1   ? 51.980 -10.686 -23.285 0.40 34.95 ?  1   SER   B HA   1 
ATOM   3940 H HA   B SER   B 1 1   ? 51.942 -10.696 -23.099 0.60 33.68 ?  1   SER   B HA   1 
ATOM   3941 H HB2  A SER   B 1 1   ? 52.242 -10.358 -21.063 0.40 35.25 ?  1   SER   B HB2  1 
ATOM   3942 H HB2  B SER   B 1 1   ? 52.334 -10.085 -21.040 0.60 34.50 ?  1   SER   B HB2  1 
ATOM   3943 H HB3  A SER   B 1 1   ? 52.219 -8.895  -21.681 0.40 35.25 ?  1   SER   B HB3  1 
ATOM   3944 H HB3  B SER   B 1 1   ? 51.923 -8.660  -21.611 0.60 34.50 ?  1   SER   B HB3  1 
ATOM   3945 H HG   A SER   B 1 1   ? 50.855 -8.890  -20.045 0.40 36.85 ?  1   SER   B HG   1 
ATOM   3946 H HG   B SER   B 1 1   ? 50.571 -8.795  -20.076 0.60 36.85 ?  1   SER   B HG   1 
ATOM   3947 N N    A MET   B 1 2   ? 50.615 -12.462 -22.067 0.40 26.95 ?  2   MET   B N    1 
ATOM   3948 N N    B MET   B 1 2   ? 50.458 -12.290 -21.782 0.60 25.21 ?  2   MET   B N    1 
ATOM   3949 C CA   A MET   B 1 2   ? 49.784 -13.642 -21.892 0.40 26.20 ?  2   MET   B CA   1 
ATOM   3950 C CA   B MET   B 1 2   ? 49.643 -13.489 -21.638 0.60 25.06 ?  2   MET   B CA   1 
ATOM   3951 C C    A MET   B 1 2   ? 49.553 -13.847 -20.404 0.40 23.17 ?  2   MET   B C    1 
ATOM   3952 C C    B MET   B 1 2   ? 49.383 -13.702 -20.153 0.60 22.83 ?  2   MET   B C    1 
ATOM   3953 O O    A MET   B 1 2   ? 50.507 -14.061 -19.648 0.40 22.55 ?  2   MET   B O    1 
ATOM   3954 O O    B MET   B 1 2   ? 50.280 -14.121 -19.415 0.60 23.24 ?  2   MET   B O    1 
ATOM   3955 C CB   A MET   B 1 2   ? 50.473 -14.854 -22.508 0.40 29.06 ?  2   MET   B CB   1 
ATOM   3956 C CB   B MET   B 1 2   ? 50.402 -14.660 -22.237 0.60 28.20 ?  2   MET   B CB   1 
ATOM   3957 C CG   A MET   B 1 2   ? 49.593 -16.087 -22.626 0.40 31.63 ?  2   MET   B CG   1 
ATOM   3958 C CG   B MET   B 1 2   ? 49.554 -15.831 -22.705 0.60 30.83 ?  2   MET   B CG   1 
ATOM   3959 S SD   A MET   B 1 2   ? 50.386 -17.382 -23.595 0.40 34.29 ?  2   MET   B SD   1 
ATOM   3960 S SD   B MET   B 1 2   ? 50.519 -16.944 -23.740 0.60 33.59 ?  2   MET   B SD   1 
ATOM   3961 C CE   A MET   B 1 2   ? 50.993 -16.389 -24.958 0.40 34.47 ?  2   MET   B CE   1 
ATOM   3962 C CE   B MET   B 1 2   ? 51.520 -15.773 -24.633 0.60 33.74 ?  2   MET   B CE   1 
ATOM   3963 H H    A MET   B 1 2   ? 51.421 -12.574 -21.789 0.40 32.34 ?  2   MET   B H    1 
ATOM   3964 H H    B MET   B 1 2   ? 51.222 -12.360 -21.391 0.60 30.25 ?  2   MET   B H    1 
ATOM   3965 H HA   A MET   B 1 2   ? 48.935 -13.523 -22.342 0.40 31.44 ?  2   MET   B HA   1 
ATOM   3966 H HA   B MET   B 1 2   ? 48.809 -13.391 -22.124 0.60 30.07 ?  2   MET   B HA   1 
ATOM   3967 H HB2  A MET   B 1 2   ? 50.762 -14.581 -23.390 0.40 34.87 ?  2   MET   B HB2  1 
ATOM   3968 H HB2  B MET   B 1 2   ? 50.875 -14.282 -22.986 0.60 33.84 ?  2   MET   B HB2  1 
ATOM   3969 H HB3  A MET   B 1 2   ? 51.243 -15.100 -21.975 0.40 34.87 ?  2   MET   B HB3  1 
ATOM   3970 H HB3  B MET   B 1 2   ? 51.037 -15.017 -21.599 0.60 33.84 ?  2   MET   B HB3  1 
ATOM   3971 H HG2  A MET   B 1 2   ? 49.416 -16.433 -21.736 0.40 37.95 ?  2   MET   B HG2  1 
ATOM   3972 H HG2  B MET   B 1 2   ? 49.234 -16.331 -21.934 0.60 37.00 ?  2   MET   B HG2  1 
ATOM   3973 H HG3  A MET   B 1 2   ? 48.763 -15.851 -23.068 0.40 37.95 ?  2   MET   B HG3  1 
ATOM   3974 H HG3  B MET   B 1 2   ? 48.807 -15.517 -23.230 0.60 37.00 ?  2   MET   B HG3  1 
ATOM   3975 H HE1  A MET   B 1 2   ? 51.163 -16.966 -25.706 0.40 41.36 ?  2   MET   B HE1  1 
ATOM   3976 H HE1  B MET   B 1 2   ? 51.890 -16.220 -25.386 0.60 40.49 ?  2   MET   B HE1  1 
ATOM   3977 H HE2  A MET   B 1 2   ? 50.313 -15.731 -25.188 0.40 41.36 ?  2   MET   B HE2  1 
ATOM   3978 H HE2  B MET   B 1 2   ? 50.957 -15.034 -24.924 0.60 40.49 ?  2   MET   B HE2  1 
ATOM   3979 H HE3  A MET   B 1 2   ? 51.813 -15.932 -24.694 0.40 41.36 ?  2   MET   B HE3  1 
ATOM   3980 H HE3  B MET   B 1 2   ? 52.233 -15.447 -24.053 0.60 40.49 ?  2   MET   B HE3  1 
ATOM   3981 N N    A VAL   B 1 3   ? 48.292 -13.751 -19.986 0.40 20.83 ?  3   VAL   B N    1 
ATOM   3982 N N    B VAL   B 1 3   ? 48.166 -13.396 -19.717 0.60 20.87 ?  3   VAL   B N    1 
ATOM   3983 C CA   A VAL   B 1 3   ? 47.892 -13.983 -18.606 0.40 19.22 ?  3   VAL   B CA   1 
ATOM   3984 C CA   B VAL   B 1 3   ? 47.720 -13.683 -18.361 0.60 19.78 ?  3   VAL   B CA   1 
ATOM   3985 C C    A VAL   B 1 3   ? 46.651 -14.865 -18.615 0.40 17.43 ?  3   VAL   B C    1 
ATOM   3986 C C    B VAL   B 1 3   ? 46.480 -14.561 -18.434 0.60 18.09 ?  3   VAL   B C    1 
ATOM   3987 O O    A VAL   B 1 3   ? 45.975 -15.018 -19.636 0.40 16.85 ?  3   VAL   B O    1 
ATOM   3988 O O    B VAL   B 1 3   ? 45.676 -14.470 -19.366 0.60 18.49 ?  3   VAL   B O    1 
ATOM   3989 C CB   A VAL   B 1 3   ? 47.613 -12.665 -17.850 0.40 20.05 ?  3   VAL   B CB   1 
ATOM   3990 C CB   B VAL   B 1 3   ? 47.468 -12.408 -17.520 0.60 20.65 ?  3   VAL   B CB   1 
ATOM   3991 C CG1  A VAL   B 1 3   ? 48.871 -11.805 -17.779 0.40 20.37 ?  3   VAL   B CG1  1 
ATOM   3992 C CG1  B VAL   B 1 3   ? 48.753 -11.594 -17.384 0.60 21.06 ?  3   VAL   B CG1  1 
ATOM   3993 C CG2  A VAL   B 1 3   ? 46.474 -11.904 -18.514 0.40 20.39 ?  3   VAL   B CG2  1 
ATOM   3994 C CG2  B VAL   B 1 3   ? 46.353 -11.566 -18.121 0.60 20.91 ?  3   VAL   B CG2  1 
ATOM   3995 H H    A VAL   B 1 3   ? 47.637 -13.535 -20.500 0.40 24.99 ?  3   VAL   B H    1 
ATOM   3996 H H    B VAL   B 1 3   ? 47.568 -13.011 -20.204 0.60 25.04 ?  3   VAL   B H    1 
ATOM   3997 H HA   A VAL   B 1 3   ? 48.606 -14.455 -18.143 0.40 23.06 ?  3   VAL   B HA   1 
ATOM   3998 H HA   B VAL   B 1 3   ? 48.403 -14.192 -17.910 0.60 23.73 ?  3   VAL   B HA   1 
ATOM   3999 H HB   A VAL   B 1 3   ? 47.345 -12.877 -16.942 0.40 24.06 ?  3   VAL   B HB   1 
ATOM   4000 H HB   B VAL   B 1 3   ? 47.195 -12.668 -16.626 0.60 24.78 ?  3   VAL   B HB   1 
ATOM   4001 H HG11 A VAL   B 1 3   ? 48.669 -10.995 -17.285 0.40 24.44 ?  3   VAL   B HG11 1 
ATOM   4002 H HG11 B VAL   B 1 3   ? 48.576 -10.810 -16.841 0.60 25.27 ?  3   VAL   B HG11 1 
ATOM   4003 H HG12 A VAL   B 1 3   ? 49.569 -12.304 -17.326 0.40 24.44 ?  3   VAL   B HG12 1 
ATOM   4004 H HG12 B VAL   B 1 3   ? 49.430 -12.144 -16.961 0.60 25.27 ?  3   VAL   B HG12 1 
ATOM   4005 H HG13 A VAL   B 1 3   ? 49.152 -11.584 -18.679 0.40 24.44 ?  3   VAL   B HG13 1 
ATOM   4006 H HG13 B VAL   B 1 3   ? 49.049 -11.325 -18.268 0.60 25.27 ?  3   VAL   B HG13 1 
ATOM   4007 H HG21 A VAL   B 1 3   ? 46.413 -11.022 -18.116 0.40 24.46 ?  3   VAL   B HG21 1 
ATOM   4008 H HG21 B VAL   B 1 3   ? 46.318 -10.712 -17.662 0.60 25.09 ?  3   VAL   B HG21 1 
ATOM   4009 H HG22 A VAL   B 1 3   ? 46.657 -11.827 -19.463 0.40 24.46 ?  3   VAL   B HG22 1 
ATOM   4010 H HG22 B VAL   B 1 3   ? 46.535 -11.428 -19.063 0.60 25.09 ?  3   VAL   B HG22 1 
ATOM   4011 H HG23 A VAL   B 1 3   ? 45.645 -12.388 -18.375 0.40 24.46 ?  3   VAL   B HG23 1 
ATOM   4012 H HG23 B VAL   B 1 3   ? 45.511 -12.034 -18.011 0.60 25.09 ?  3   VAL   B HG23 1 
ATOM   4013 N N    . ASN   B 1 4   ? 46.352 -15.446 -17.450 1.00 16.75 ?  4   ASN   B N    1 
ATOM   4014 C CA   . ASN   B 1 4   ? 45.214 -16.358 -17.334 1.00 15.95 ?  4   ASN   B CA   1 
ATOM   4015 C C    . ASN   B 1 4   ? 45.167 -17.327 -18.511 1.00 16.03 ?  4   ASN   B C    1 
ATOM   4016 O O    . ASN   B 1 4   ? 44.103 -17.592 -19.070 1.00 16.83 ?  4   ASN   B O    1 
ATOM   4017 C CB   . ASN   B 1 4   ? 43.888 -15.605 -17.175 1.00 15.27 ?  4   ASN   B CB   1 
ATOM   4018 C CG   . ASN   B 1 4   ? 43.837 -14.792 -15.900 1.00 14.43 ?  4   ASN   B CG   1 
ATOM   4019 O OD1  . ASN   B 1 4   ? 44.120 -15.302 -14.820 1.00 14.25 ?  4   ASN   B OD1  1 
ATOM   4020 N ND2  . ASN   B 1 4   ? 43.509 -13.512 -16.022 1.00 15.55 ?  4   ASN   B ND2  1 
ATOM   4021 H H    A ASN   B 1 4   ? 46.787 -15.324 -16.723 0.40 20.10 ?  4   ASN   B H    1 
ATOM   4022 H H    B ASN   B 1 4   ? 46.942 -15.556 -16.839 0.60 20.10 ?  4   ASN   B H    1 
ATOM   4023 H HA   . ASN   B 1 4   ? 45.341 -16.884 -16.530 1.00 19.14 ?  4   ASN   B HA   1 
ATOM   4024 H HB2  . ASN   B 1 4   ? 43.765 -15.001 -17.921 1.00 18.33 ?  4   ASN   B HB2  1 
ATOM   4025 H HB3  . ASN   B 1 4   ? 43.160 -16.251 -17.149 1.00 18.33 ?  4   ASN   B HB3  1 
ATOM   4026 H HD21 . ASN   B 1 4   ? 43.468 -13.009 -15.323 1.00 18.66 ?  4   ASN   B HD21 1 
ATOM   4027 H HD22 . ASN   B 1 4   ? 43.324 -13.184 -16.795 1.00 18.66 ?  4   ASN   B HD22 1 
ATOM   4028 N N    . SER   B 1 5   ? 46.327 -17.849 -18.898 1.00 17.26 ?  5   SER   B N    1 
ATOM   4029 C CA   . SER   B 1 5   ? 46.423 -18.761 -20.034 1.00 19.39 ?  5   SER   B CA   1 
ATOM   4030 C C    . SER   B 1 5   ? 46.402 -20.197 -19.518 1.00 20.92 ?  5   SER   B C    1 
ATOM   4031 O O    . SER   B 1 5   ? 47.403 -20.907 -19.502 1.00 23.43 ?  5   SER   B O    1 
ATOM   4032 C CB   . SER   B 1 5   ? 47.678 -18.464 -20.850 1.00 20.75 ?  5   SER   B CB   1 
ATOM   4033 O OG   . SER   B 1 5   ? 48.842 -18.581 -20.051 1.00 23.15 ?  5   SER   B OG   1 
ATOM   4034 H H    . SER   B 1 5   ? 47.080 -17.693 -18.512 1.00 20.71 ?  5   SER   B H    1 
ATOM   4035 H HA   . SER   B 1 5   ? 45.655 -18.637 -20.610 1.00 23.26 ?  5   SER   B HA   1 
ATOM   4036 H HB2  . SER   B 1 5   ? 47.728 -19.091 -21.592 1.00 24.90 ?  5   SER   B HB2  1 
ATOM   4037 H HB3  . SER   B 1 5   ? 47.609 -17.559 -21.193 1.00 24.90 ?  5   SER   B HB3  1 
ATOM   4038 H HG   . SER   B 1 5   ? 48.920 -19.367 -19.769 1.00 27.78 ?  5   SER   B HG   1 
ATOM   4039 N N    . PHE   B 1 6   ? 45.221 -20.600 -19.068 1.00 21.09 ?  6   PHE   B N    1 
ATOM   4040 C CA   . PHE   B 1 6   ? 45.016 -21.948 -18.561 1.00 20.69 ?  6   PHE   B CA   1 
ATOM   4041 C C    . PHE   B 1 6   ? 44.921 -22.917 -19.730 1.00 23.67 ?  6   PHE   B C    1 
ATOM   4042 O O    . PHE   B 1 6   ? 44.248 -22.638 -20.725 1.00 26.15 ?  6   PHE   B O    1 
ATOM   4043 C CB   . PHE   B 1 6   ? 43.723 -21.999 -17.748 1.00 18.70 ?  6   PHE   B CB   1 
ATOM   4044 C CG   . PHE   B 1 6   ? 43.747 -21.148 -16.512 1.00 16.59 ?  6   PHE   B CG   1 
ATOM   4045 C CD1  . PHE   B 1 6   ? 44.257 -21.645 -15.329 1.00 15.47 ?  6   PHE   B CD1  1 
ATOM   4046 C CD2  . PHE   B 1 6   ? 43.266 -19.845 -16.536 1.00 16.12 ?  6   PHE   B CD2  1 
ATOM   4047 C CE1  . PHE   B 1 6   ? 44.274 -20.865 -14.182 1.00 15.19 ?  6   PHE   B CE1  1 
ATOM   4048 C CE2  . PHE   B 1 6   ? 43.288 -19.053 -15.398 1.00 16.81 ?  6   PHE   B CE2  1 
ATOM   4049 C CZ   . PHE   B 1 6   ? 43.794 -19.558 -14.222 1.00 15.75 ?  6   PHE   B CZ   1 
ATOM   4050 H H    . PHE   B 1 6   ? 44.514 -20.113 -19.052 1.00 25.30 ?  6   PHE   B H    1 
ATOM   4051 H HA   . PHE   B 1 6   ? 45.756 -22.209 -17.992 1.00 24.83 ?  6   PHE   B HA   1 
ATOM   4052 H HB2  . PHE   B 1 6   ? 42.991 -21.690 -18.303 1.00 22.43 ?  6   PHE   B HB2  1 
ATOM   4053 H HB3  . PHE   B 1 6   ? 43.560 -22.915 -17.469 1.00 22.43 ?  6   PHE   B HB3  1 
ATOM   4054 H HD1  . PHE   B 1 6   ? 44.589 -22.512 -15.295 1.00 18.56 ?  6   PHE   B HD1  1 
ATOM   4055 H HD2  . PHE   B 1 6   ? 42.919 -19.505 -17.326 1.00 19.35 ?  6   PHE   B HD2  1 
ATOM   4056 H HE1  . PHE   B 1 6   ? 44.630 -21.201 -13.387 1.00 18.22 ?  6   PHE   B HE1  1 
ATOM   4057 H HE2  . PHE   B 1 6   ? 42.954 -18.184 -15.428 1.00 20.17 ?  6   PHE   B HE2  1 
ATOM   4058 H HZ   . PHE   B 1 6   ? 43.810 -19.033 -13.453 1.00 18.89 ?  6   PHE   B HZ   1 
ATOM   4059 N N    . SER   B 1 7   ? 45.612 -24.052 -19.612 1.00 24.51 ?  7   SER   B N    1 
ATOM   4060 C CA   . SER   B 1 7   ? 45.662 -25.036 -20.682 1.00 26.92 ?  7   SER   B CA   1 
ATOM   4061 C C    . SER   B 1 7   ? 45.626 -26.441 -20.101 1.00 26.51 ?  7   SER   B C    1 
ATOM   4062 O O    . SER   B 1 7   ? 46.236 -26.711 -19.063 1.00 27.67 ?  7   SER   B O    1 
ATOM   4063 C CB   . SER   B 1 7   ? 46.930 -24.860 -21.532 1.00 29.65 ?  7   SER   B CB   1 
ATOM   4064 O OG   . SER   B 1 7   ? 46.878 -25.657 -22.700 1.00 31.52 ?  7   SER   B OG   1 
ATOM   4065 H H    . SER   B 1 7   ? 46.072 -24.276 -18.914 1.00 29.41 ?  7   SER   B H    1 
ATOM   4066 H HA   . SER   B 1 7   ? 44.894 -24.930 -21.257 1.00 32.30 ?  7   SER   B HA   1 
ATOM   4067 H HB2  . SER   B 1 7   ? 47.006 -23.929 -21.795 1.00 35.57 ?  7   SER   B HB2  1 
ATOM   4068 H HB3  . SER   B 1 7   ? 47.705 -25.118 -21.006 1.00 35.57 ?  7   SER   B HB3  1 
ATOM   4069 H HG   . SER   B 1 7   ? 47.580 -25.554 -23.153 1.00 37.82 ?  7   SER   B HG   1 
ATOM   4070 N N    . GLY   B 1 8   ? 44.913 -27.334 -20.785 1.00 26.60 ?  8   GLY   B N    1 
ATOM   4071 C CA   . GLY   B 1 8   ? 44.891 -28.727 -20.401 1.00 25.52 ?  8   GLY   B CA   1 
ATOM   4072 C C    . GLY   B 1 8   ? 43.952 -29.060 -19.272 1.00 24.00 ?  8   GLY   B C    1 
ATOM   4073 O O    . GLY   B 1 8   ? 44.093 -30.127 -18.664 1.00 25.29 ?  8   GLY   B O    1 
ATOM   4074 H H    . GLY   B 1 8   ? 44.438 -27.149 -21.475 1.00 31.92 ?  8   GLY   B H    1 
ATOM   4075 H HA2  . GLY   B 1 8   ? 44.634 -29.263 -21.167 1.00 30.62 ?  8   GLY   B HA2  1 
ATOM   4076 H HA3  . GLY   B 1 8   ? 45.779 -28.999 -20.127 1.00 30.62 ?  8   GLY   B HA3  1 
ATOM   4077 N N    . TYR   B 1 9   ? 42.979 -28.198 -18.981 1.00 22.05 ?  9   TYR   B N    1 
ATOM   4078 C CA   . TYR   B 1 9   ? 42.025 -28.481 -17.922 1.00 19.91 ?  9   TYR   B CA   1 
ATOM   4079 C C    . TYR   B 1 9   ? 40.849 -29.283 -18.445 1.00 19.37 ?  9   TYR   B C    1 
ATOM   4080 O O    . TYR   B 1 9   ? 40.432 -29.143 -19.598 1.00 21.46 ?  9   TYR   B O    1 
ATOM   4081 C CB   . TYR   B 1 9   ? 41.504 -27.202 -17.274 1.00 19.10 ?  9   TYR   B CB   1 
ATOM   4082 C CG   . TYR   B 1 9   ? 42.528 -26.572 -16.365 1.00 18.77 ?  9   TYR   B CG   1 
ATOM   4083 C CD1  . TYR   B 1 9   ? 43.605 -25.876 -16.888 1.00 19.54 ?  9   TYR   B CD1  1 
ATOM   4084 C CD2  . TYR   B 1 9   ? 42.436 -26.696 -14.987 1.00 18.10 ?  9   TYR   B CD2  1 
ATOM   4085 C CE1  . TYR   B 1 9   ? 44.563 -25.312 -16.066 1.00 19.86 ?  9   TYR   B CE1  1 
ATOM   4086 C CE2  . TYR   B 1 9   ? 43.389 -26.132 -14.154 1.00 18.57 ?  9   TYR   B CE2  1 
ATOM   4087 C CZ   . TYR   B 1 9   ? 44.451 -25.436 -14.700 1.00 19.45 ?  9   TYR   B CZ   1 
ATOM   4088 O OH   . TYR   B 1 9   ? 45.404 -24.886 -13.878 1.00 20.14 ?  9   TYR   B OH   1 
ATOM   4089 H H    . TYR   B 1 9   ? 42.835 -27.458 -19.395 1.00 26.46 ?  9   TYR   B H    1 
ATOM   4090 H HA   . TYR   B 1 9   ? 42.455 -29.007 -17.236 1.00 23.89 ?  9   TYR   B HA   1 
ATOM   4091 H HB2  . TYR   B 1 9   ? 41.264 -26.559 -17.963 1.00 22.92 ?  9   TYR   B HB2  1 
ATOM   4092 H HB3  . TYR   B 1 9   ? 40.727 -27.427 -16.743 1.00 22.92 ?  9   TYR   B HB3  1 
ATOM   4093 H HD1  . TYR   B 1 9   ? 43.682 -25.791 -17.812 1.00 23.44 ?  9   TYR   B HD1  1 
ATOM   4094 H HD2  . TYR   B 1 9   ? 41.718 -27.170 -14.618 1.00 21.71 ?  9   TYR   B HD2  1 
ATOM   4095 H HE1  . TYR   B 1 9   ? 45.272 -24.851 -16.436 1.00 23.83 ?  9   TYR   B HE1  1 
ATOM   4096 H HE2  . TYR   B 1 9   ? 43.305 -26.231 -13.231 1.00 22.28 ?  9   TYR   B HE2  1 
ATOM   4097 H HH   . TYR   B 1 9   ? 45.983 -24.500 -14.342 1.00 24.17 ?  9   TYR   B HH   1 
ATOM   4098 N N    . LEU   B 1 10  ? 40.323 -30.133 -17.570 1.00 17.68 ?  10  LEU   B N    1 
ATOM   4099 C CA   . LEU   B 1 10  ? 39.117 -30.895 -17.833 1.00 17.65 ?  10  LEU   B CA   1 
ATOM   4100 C C    . LEU   B 1 10  ? 37.926 -30.132 -17.267 1.00 16.85 ?  10  LEU   B C    1 
ATOM   4101 O O    . LEU   B 1 10  ? 37.943 -29.710 -16.106 1.00 16.40 ?  10  LEU   B O    1 
ATOM   4102 C CB   . LEU   B 1 10  ? 39.231 -32.264 -17.165 1.00 18.67 ?  10  LEU   B CB   1 
ATOM   4103 C CG   . LEU   B 1 10  ? 38.089 -33.228 -17.459 1.00 20.79 ?  10  LEU   B CG   1 
ATOM   4104 C CD1  . LEU   B 1 10  ? 38.154 -33.708 -18.903 1.00 22.28 ?  10  LEU   B CD1  1 
ATOM   4105 C CD2  . LEU   B 1 10  ? 38.121 -34.402 -16.498 1.00 21.98 ?  10  LEU   B CD2  1 
ATOM   4106 H H    . LEU   B 1 10  ? 40.654 -30.287 -16.786 1.00 21.21 ?  10  LEU   B H    1 
ATOM   4107 H HA   . LEU   B 1 10  ? 38.997 -31.018 -18.787 1.00 21.17 ?  10  LEU   B HA   1 
ATOM   4108 H HB2  . LEU   B 1 10  ? 40.053 -32.689 -17.464 1.00 22.40 ?  10  LEU   B HB2  1 
ATOM   4109 H HB3  . LEU   B 1 10  ? 39.266 -32.141 -16.203 1.00 22.40 ?  10  LEU   B HB3  1 
ATOM   4110 H HG   . LEU   B 1 10  ? 37.244 -32.770 -17.336 1.00 24.95 ?  10  LEU   B HG   1 
ATOM   4111 H HD11 . LEU   B 1 10  ? 37.463 -34.372 -19.046 1.00 26.73 ?  10  LEU   B HD11 1 
ATOM   4112 H HD12 . LEU   B 1 10  ? 38.011 -32.949 -19.491 1.00 26.73 ?  10  LEU   B HD12 1 
ATOM   4113 H HD13 . LEU   B 1 10  ? 39.027 -34.095 -19.067 1.00 26.73 ?  10  LEU   B HD13 1 
ATOM   4114 H HD21 . LEU   B 1 10  ? 37.388 -35.001 -16.709 1.00 26.38 ?  10  LEU   B HD21 1 
ATOM   4115 H HD22 . LEU   B 1 10  ? 38.967 -34.863 -16.594 1.00 26.38 ?  10  LEU   B HD22 1 
ATOM   4116 H HD23 . LEU   B 1 10  ? 38.025 -34.066 -15.593 1.00 26.38 ?  10  LEU   B HD23 1 
ATOM   4117 N N    . LYS   B 1 11  ? 36.899 -29.957 -18.088 1.00 18.14 ?  11  LYS   B N    1 
ATOM   4118 C CA   . LYS   B 1 11  ? 35.703 -29.243 -17.671 1.00 20.20 ?  11  LYS   B CA   1 
ATOM   4119 C C    . LYS   B 1 11  ? 34.830 -30.165 -16.824 1.00 19.44 ?  11  LYS   B C    1 
ATOM   4120 O O    . LYS   B 1 11  ? 34.450 -31.252 -17.273 1.00 21.10 ?  11  LYS   B O    1 
ATOM   4121 C CB   . LYS   B 1 11  ? 34.954 -28.775 -18.918 1.00 24.41 ?  11  LYS   B CB   1 
ATOM   4122 C CG   . LYS   B 1 11  ? 33.806 -27.816 -18.664 1.00 28.19 ?  11  LYS   B CG   1 
ATOM   4123 C CD   . LYS   B 1 11  ? 33.069 -27.510 -19.963 1.00 31.28 ?  11  LYS   B CD   1 
ATOM   4124 C CE   . LYS   B 1 11  ? 32.067 -26.382 -19.791 1.00 33.40 ?  11  LYS   B CE   1 
ATOM   4125 N NZ   . LYS   B 1 11  ? 32.736 -25.064 -19.617 1.00 34.64 ?  11  LYS   B NZ   1 
ATOM   4126 H H    . LYS   B 1 11  ? 36.868 -30.251 -18.899 1.00 21.76 ?  11  LYS   B H    1 
ATOM   4127 H HA   . LYS   B 1 11  ? 35.950 -28.469 -17.144 1.00 24.24 ?  11  LYS   B HA   1 
ATOM   4128 H HB2  . LYS   B 1 11  ? 35.583 -28.324 -19.506 1.00 29.29 ?  11  LYS   B HB2  1 
ATOM   4129 H HB3  . LYS   B 1 11  ? 34.589 -29.551 -19.371 1.00 29.29 ?  11  LYS   B HB3  1 
ATOM   4130 H HG2  . LYS   B 1 11  ? 33.179 -28.219 -18.045 1.00 33.83 ?  11  LYS   B HG2  1 
ATOM   4131 H HG3  . LYS   B 1 11  ? 34.152 -26.985 -18.306 1.00 33.83 ?  11  LYS   B HG3  1 
ATOM   4132 H HD2  . LYS   B 1 11  ? 33.712 -27.243 -20.640 1.00 37.53 ?  11  LYS   B HD2  1 
ATOM   4133 H HD3  . LYS   B 1 11  ? 32.590 -28.302 -20.253 1.00 37.53 ?  11  LYS   B HD3  1 
ATOM   4134 H HE2  . LYS   B 1 11  ? 31.502 -26.334 -20.579 1.00 40.08 ?  11  LYS   B HE2  1 
ATOM   4135 H HE3  . LYS   B 1 11  ? 31.528 -26.559 -19.005 1.00 40.08 ?  11  LYS   B HE3  1 
ATOM   4136 H HZ1  . LYS   B 1 11  ? 32.126 -24.423 -19.526 1.00 41.56 ?  11  LYS   B HZ1  1 
ATOM   4137 H HZ2  . LYS   B 1 11  ? 33.253 -25.078 -18.893 1.00 41.56 ?  11  LYS   B HZ2  1 
ATOM   4138 H HZ3  . LYS   B 1 11  ? 33.240 -24.883 -20.329 1.00 41.56 ?  11  LYS   B HZ3  1 
ATOM   4139 N N    . LEU   B 1 12  ? 34.517 -29.741 -15.599 1.00 17.68 ?  12  LEU   B N    1 
ATOM   4140 C CA   . LEU   B 1 12  ? 33.557 -30.445 -14.755 1.00 17.52 ?  12  LEU   B CA   1 
ATOM   4141 C C    . LEU   B 1 12  ? 32.167 -29.838 -14.844 1.00 17.57 ?  12  LEU   B C    1 
ATOM   4142 O O    . LEU   B 1 12  ? 31.183 -30.557 -15.006 1.00 18.03 ?  12  LEU   B O    1 
ATOM   4143 C CB   . LEU   B 1 12  ? 34.015 -30.466 -13.292 1.00 17.33 ?  12  LEU   B CB   1 
ATOM   4144 C CG   . LEU   B 1 12  ? 35.361 -31.142 -13.030 1.00 17.06 ?  12  LEU   B CG   1 
ATOM   4145 C CD1  . LEU   B 1 12  ? 35.723 -31.095 -11.553 1.00 17.40 ?  12  LEU   B CD1  1 
ATOM   4146 C CD2  . LEU   B 1 12  ? 35.350 -32.576 -13.537 1.00 17.70 ?  12  LEU   B CD2  1 
ATOM   4147 H H    . LEU   B 1 12  ? 34.853 -29.041 -15.233 1.00 21.21 ?  12  LEU   B H    1 
ATOM   4148 H HA   . LEU   B 1 12  ? 33.483 -31.359 -15.060 1.00 21.02 ?  12  LEU   B HA   1 
ATOM   4149 H HB2  . LEU   B 1 12  ? 34.080 -29.553 -12.977 1.00 20.80 ?  12  LEU   B HB2  1 
ATOM   4150 H HB3  . LEU   B 1 12  ? 33.345 -30.941 -12.771 1.00 20.80 ?  12  LEU   B HB3  1 
ATOM   4151 H HG   . LEU   B 1 12  ? 36.047 -30.663 -13.519 1.00 20.47 ?  12  LEU   B HG   1 
ATOM   4152 H HD11 . LEU   B 1 12  ? 36.583 -31.529 -11.425 1.00 20.88 ?  12  LEU   B HD11 1 
ATOM   4153 H HD12 . LEU   B 1 12  ? 35.775 -30.170 -11.269 1.00 20.88 ?  12  LEU   B HD12 1 
ATOM   4154 H HD13 . LEU   B 1 12  ? 35.041 -31.560 -11.044 1.00 20.88 ?  12  LEU   B HD13 1 
ATOM   4155 H HD21 . LEU   B 1 12  ? 36.144 -33.029 -13.222 1.00 21.24 ?  12  LEU   B HD21 1 
ATOM   4156 H HD22 . LEU   B 1 12  ? 34.556 -33.023 -13.201 1.00 21.24 ?  12  LEU   B HD22 1 
ATOM   4157 H HD23 . LEU   B 1 12  ? 35.334 -32.568 -14.509 1.00 21.24 ?  12  LEU   B HD23 1 
ATOM   4158 N N    . THR   B 1 13  ? 32.072 -28.520 -14.728 1.00 17.33 ?  13  THR   B N    1 
ATOM   4159 C CA   . THR   B 1 13  ? 30.845 -27.769 -14.934 1.00 17.03 ?  13  THR   B CA   1 
ATOM   4160 C C    . THR   B 1 13  ? 31.181 -26.574 -15.815 1.00 19.26 ?  13  THR   B C    1 
ATOM   4161 O O    . THR   B 1 13  ? 32.330 -26.381 -16.230 1.00 20.04 ?  13  THR   B O    1 
ATOM   4162 C CB   . THR   B 1 13  ? 30.250 -27.287 -13.606 1.00 16.35 ?  13  THR   B CB   1 
ATOM   4163 O OG1  . THR   B 1 13  ? 31.105 -26.274 -13.069 1.00 16.24 ?  13  THR   B OG1  1 
ATOM   4164 C CG2  . THR   B 1 13  ? 30.130 -28.438 -12.611 1.00 16.76 ?  13  THR   B CG2  1 
ATOM   4165 H H    . THR   B 1 13  ? 32.735 -28.013 -14.520 1.00 20.79 ?  13  THR   B H    1 
ATOM   4166 H HA   . THR   B 1 13  ? 30.186 -28.319 -15.384 1.00 20.43 ?  13  THR   B HA   1 
ATOM   4167 H HB   . THR   B 1 13  ? 29.364 -26.913 -13.757 1.00 19.61 ?  13  THR   B HB   1 
ATOM   4168 H HG1  . THR   B 1 13  ? 30.783 -25.506 -13.223 1.00 19.49 ?  13  THR   B HG1  1 
ATOM   4169 H HG21 . THR   B 1 13  ? 29.626 -28.157 -11.831 1.00 20.11 ?  13  THR   B HG21 1 
ATOM   4170 H HG22 . THR   B 1 13  ? 29.671 -29.187 -13.026 1.00 20.11 ?  13  THR   B HG22 1 
ATOM   4171 H HG23 . THR   B 1 13  ? 31.011 -28.729 -12.329 1.00 20.11 ?  13  THR   B HG23 1 
ATOM   4172 N N    A ASP   B 1 14  ? 30.170 -25.745 -16.082 0.40 20.30 ?  14  ASP   B N    1 
ATOM   4173 N N    B ASP   B 1 14  ? 30.172 -25.742 -16.085 0.60 20.42 ?  14  ASP   B N    1 
ATOM   4174 C CA   A ASP   B 1 14  ? 30.386 -24.585 -16.939 0.40 21.53 ?  14  ASP   B CA   1 
ATOM   4175 C CA   B ASP   B 1 14  ? 30.381 -24.584 -16.946 0.60 21.90 ?  14  ASP   B CA   1 
ATOM   4176 C C    A ASP   B 1 14  ? 31.484 -23.679 -16.400 0.40 19.85 ?  14  ASP   B C    1 
ATOM   4177 C C    B ASP   B 1 14  ? 31.393 -23.599 -16.380 0.60 20.27 ?  14  ASP   B C    1 
ATOM   4178 O O    A ASP   B 1 14  ? 32.157 -22.998 -17.182 0.40 20.31 ?  14  ASP   B O    1 
ATOM   4179 O O    B ASP   B 1 14  ? 31.879 -22.745 -17.128 0.60 21.18 ?  14  ASP   B O    1 
ATOM   4180 C CB   A ASP   B 1 14  ? 29.081 -23.808 -17.122 0.40 24.59 ?  14  ASP   B CB   1 
ATOM   4181 C CB   B ASP   B 1 14  ? 29.064 -23.850 -17.197 0.60 25.46 ?  14  ASP   B CB   1 
ATOM   4182 C CG   A ASP   B 1 14  ? 28.114 -24.499 -18.061 0.40 27.35 ?  14  ASP   B CG   1 
ATOM   4183 C CG   B ASP   B 1 14  ? 28.157 -24.597 -18.151 0.60 28.89 ?  14  ASP   B CG   1 
ATOM   4184 O OD1  A ASP   B 1 14  ? 28.477 -25.541 -18.651 0.40 28.33 ?  14  ASP   B OD1  1 
ATOM   4185 O OD1  B ASP   B 1 14  ? 28.680 -25.274 -19.062 0.60 29.93 ?  14  ASP   B OD1  1 
ATOM   4186 O OD2  A ASP   B 1 14  ? 26.983 -23.993 -18.207 0.40 28.25 -1 14  ASP   B OD2  1 
ATOM   4187 O OD2  B ASP   B 1 14  ? 26.923 -24.511 -17.991 0.60 30.22 -1 14  ASP   B OD2  1 
ATOM   4188 H H    A ASP   B 1 14  ? 29.372 -25.818 -15.775 0.40 24.36 ?  14  ASP   B H    1 
ATOM   4189 H H    B ASP   B 1 14  ? 29.373 -25.818 -15.781 0.60 24.51 ?  14  ASP   B H    1 
ATOM   4190 H HA   A ASP   B 1 14  ? 30.676 -24.881 -17.809 0.40 25.83 ?  14  ASP   B HA   1 
ATOM   4191 H HA   B ASP   B 1 14  ? 30.718 -24.884 -17.800 0.60 26.28 ?  14  ASP   B HA   1 
ATOM   4192 H HB2  A ASP   B 1 14  ? 28.633 -23.718 -16.268 0.40 29.50 ?  14  ASP   B HB2  1 
ATOM   4193 H HB2  B ASP   B 1 14  ? 28.593 -23.743 -16.357 0.60 30.55 ?  14  ASP   B HB2  1 
ATOM   4194 H HB3  A ASP   B 1 14  ? 29.273 -22.931 -17.492 0.40 29.50 ?  14  ASP   B HB3  1 
ATOM   4195 H HB3  B ASP   B 1 14  ? 29.256 -22.975 -17.581 0.60 30.55 ?  14  ASP   B HB3  1 
ATOM   4196 N N    . ASN   B 1 15  ? 31.703 -23.673 -15.082 1.00 17.82 ?  15  ASN   B N    1 
ATOM   4197 C CA   . ASN   B 1 15  ? 32.659 -22.752 -14.475 1.00 15.36 ?  15  ASN   B CA   1 
ATOM   4198 C C    . ASN   B 1 15  ? 33.750 -23.409 -13.638 1.00 13.96 ?  15  ASN   B C    1 
ATOM   4199 O O    . ASN   B 1 15  ? 34.598 -22.681 -13.110 1.00 14.13 ?  15  ASN   B O    1 
ATOM   4200 C CB   . ASN   B 1 15  ? 31.942 -21.698 -13.613 1.00 15.52 ?  15  ASN   B CB   1 
ATOM   4201 C CG   . ASN   B 1 15  ? 31.327 -22.297 -12.367 1.00 15.01 ?  15  ASN   B CG   1 
ATOM   4202 O OD1  . ASN   B 1 15  ? 30.384 -23.090 -12.447 1.00 17.02 ?  15  ASN   B OD1  1 
ATOM   4203 N ND2  . ASN   B 1 15  ? 31.864 -21.946 -11.211 1.00 14.08 ?  15  ASN   B ND2  1 
ATOM   4204 H H    A ASN   B 1 15  ? 31.314 -24.198 -14.520 0.40 21.38 ?  15  ASN   B H    1 
ATOM   4205 H H    B ASN   B 1 15  ? 31.356 -24.234 -14.529 0.60 21.38 ?  15  ASN   B H    1 
ATOM   4206 H HA   . ASN   B 1 15  ? 33.111 -22.269 -15.174 1.00 18.43 ?  15  ASN   B HA   1 
ATOM   4207 H HB2  . ASN   B 1 15  ? 32.587 -21.016 -13.338 1.00 18.63 ?  15  ASN   B HB2  1 
ATOM   4208 H HB3  . ASN   B 1 15  ? 31.234 -21.282 -14.131 1.00 18.63 ?  15  ASN   B HB3  1 
ATOM   4209 H HD21 . ASN   B 1 15  ? 31.549 -22.256 -10.473 1.00 16.89 ?  15  ASN   B HD21 1 
ATOM   4210 H HD22 . ASN   B 1 15  ? 32.532 -21.393 -11.186 1.00 16.89 ?  15  ASN   B HD22 1 
ATOM   4211 N N    . VAL   B 1 16  ? 33.768 -24.735 -13.499 1.00 13.75 ?  16  VAL   B N    1 
ATOM   4212 C CA   . VAL   B 1 16  ? 34.768 -25.425 -12.688 1.00 13.61 ?  16  VAL   B CA   1 
ATOM   4213 C C    . VAL   B 1 16  ? 35.565 -26.355 -13.586 1.00 13.76 ?  16  VAL   B C    1 
ATOM   4214 O O    . VAL   B 1 16  ? 34.989 -27.235 -14.248 1.00 14.75 ?  16  VAL   B O    1 
ATOM   4215 C CB   . VAL   B 1 16  ? 34.140 -26.197 -11.518 1.00 14.06 ?  16  VAL   B CB   1 
ATOM   4216 C CG1  . VAL   B 1 16  ? 35.222 -26.932 -10.725 1.00 13.78 ?  16  VAL   B CG1  1 
ATOM   4217 C CG2  . VAL   B 1 16  ? 33.336 -25.255 -10.623 1.00 14.88 ?  16  VAL   B CG2  1 
ATOM   4218 H H    . VAL   B 1 16  ? 33.197 -25.267 -13.867 1.00 16.49 ?  16  VAL   B H    1 
ATOM   4219 H HA   . VAL   B 1 16  ? 35.379 -24.771 -12.313 1.00 16.32 ?  16  VAL   B HA   1 
ATOM   4220 H HB   . VAL   B 1 16  ? 33.530 -26.865 -11.873 1.00 16.87 ?  16  VAL   B HB   1 
ATOM   4221 H HG11 . VAL   B 1 16  ? 34.844 -27.234 -9.883  1.00 16.53 ?  16  VAL   B HG11 1 
ATOM   4222 H HG12 . VAL   B 1 16  ? 35.535 -27.692 -11.237 1.00 16.53 ?  16  VAL   B HG12 1 
ATOM   4223 H HG13 . VAL   B 1 16  ? 35.956 -26.320 -10.553 1.00 16.53 ?  16  VAL   B HG13 1 
ATOM   4224 H HG21 . VAL   B 1 16  ? 32.993 -25.754 -9.865  1.00 17.86 ?  16  VAL   B HG21 1 
ATOM   4225 H HG22 . VAL   B 1 16  ? 33.909 -24.539 -10.320 1.00 17.86 ?  16  VAL   B HG22 1 
ATOM   4226 H HG23 . VAL   B 1 16  ? 32.594 -24.891 -11.137 1.00 17.86 ?  16  VAL   B HG23 1 
ATOM   4227 N N    . TYR   B 1 17  ? 36.888 -26.184 -13.567 1.00 14.00 ?  17  TYR   B N    1 
ATOM   4228 C CA   . TYR   B 1 17  ? 37.834 -26.933 -14.378 1.00 14.53 ?  17  TYR   B CA   1 
ATOM   4229 C C    . TYR   B 1 17  ? 38.883 -27.543 -13.462 1.00 13.48 ?  17  TYR   B C    1 
ATOM   4230 O O    . TYR   B 1 17  ? 39.170 -27.010 -12.387 1.00 13.78 ?  17  TYR   B O    1 
ATOM   4231 C CB   . TYR   B 1 17  ? 38.543 -26.001 -15.375 1.00 16.88 ?  17  TYR   B CB   1 
ATOM   4232 C CG   . TYR   B 1 17  ? 37.613 -25.231 -16.279 1.00 20.13 ?  17  TYR   B CG   1 
ATOM   4233 C CD1  . TYR   B 1 17  ? 37.005 -24.056 -15.851 1.00 21.59 ?  17  TYR   B CD1  1 
ATOM   4234 C CD2  . TYR   B 1 17  ? 37.342 -25.680 -17.564 1.00 22.17 ?  17  TYR   B CD2  1 
ATOM   4235 C CE1  . TYR   B 1 17  ? 36.149 -23.349 -16.680 1.00 22.99 ?  17  TYR   B CE1  1 
ATOM   4236 C CE2  . TYR   B 1 17  ? 36.493 -24.981 -18.401 1.00 23.57 ?  17  TYR   B CE2  1 
ATOM   4237 C CZ   . TYR   B 1 17  ? 35.896 -23.820 -17.953 1.00 24.25 ?  17  TYR   B CZ   1 
ATOM   4238 O OH   . TYR   B 1 17  ? 35.051 -23.121 -18.783 1.00 25.75 ?  17  TYR   B OH   1 
ATOM   4239 H H    . TYR   B 1 17  ? 37.281 -25.596 -13.069 1.00 16.80 ?  17  TYR   B H    1 
ATOM   4240 H HA   . TYR   B 1 17  ? 37.373 -27.635 -14.868 1.00 17.43 ?  17  TYR   B HA   1 
ATOM   4241 H HB2  . TYR   B 1 17  ? 39.083 -25.363 -14.884 1.00 20.25 ?  17  TYR   B HB2  1 
ATOM   4242 H HB3  . TYR   B 1 17  ? 39.110 -26.540 -15.945 1.00 20.25 ?  17  TYR   B HB3  1 
ATOM   4243 H HD1  . TYR   B 1 17  ? 37.175 -23.740 -14.995 1.00 25.91 ?  17  TYR   B HD1  1 
ATOM   4244 H HD2  . TYR   B 1 17  ? 37.739 -26.462 -17.871 1.00 26.60 ?  17  TYR   B HD2  1 
ATOM   4245 H HE1  . TYR   B 1 17  ? 35.748 -22.563 -16.384 1.00 27.59 ?  17  TYR   B HE1  1 
ATOM   4246 H HE2  . TYR   B 1 17  ? 36.317 -25.293 -19.261 1.00 28.28 ?  17  TYR   B HE2  1 
ATOM   4247 H HH   . TYR   B 1 17  ? 34.982 -23.510 -19.524 1.00 30.89 ?  17  TYR   B HH   1 
ATOM   4248 N N    . ILE   B 1 18  ? 39.491 -28.646 -13.893 1.00 13.73 ?  18  ILE   B N    1 
ATOM   4249 C CA   . ILE   B 1 18  ? 40.420 -29.366 -13.030 1.00 13.48 ?  18  ILE   B CA   1 
ATOM   4250 C C    . ILE   B 1 18  ? 41.579 -29.916 -13.855 1.00 13.89 ?  18  ILE   B C    1 
ATOM   4251 O O    . ILE   B 1 18  ? 41.416 -30.304 -15.017 1.00 15.25 ?  18  ILE   B O    1 
ATOM   4252 C CB   . ILE   B 1 18  ? 39.666 -30.463 -12.229 1.00 14.04 ?  18  ILE   B CB   1 
ATOM   4253 C CG1  . ILE   B 1 18  ? 40.535 -31.015 -11.098 1.00 14.62 ?  18  ILE   B CG1  1 
ATOM   4254 C CG2  . ILE   B 1 18  ? 39.152 -31.570 -13.150 1.00 14.32 ?  18  ILE   B CG2  1 
ATOM   4255 C CD1  . ILE   B 1 18  ? 39.742 -31.829 -10.090 1.00 16.28 ?  18  ILE   B CD1  1 
ATOM   4256 H H    . ILE   B 1 18  ? 39.387 -28.996 -14.671 1.00 16.47 ?  18  ILE   B H    1 
ATOM   4257 H HA   . ILE   B 1 18  ? 40.785 -28.745 -12.380 1.00 16.18 ?  18  ILE   B HA   1 
ATOM   4258 H HB   . ILE   B 1 18  ? 38.891 -30.049 -11.814 1.00 16.85 ?  18  ILE   B HB   1 
ATOM   4259 H HG12 . ILE   B 1 18  ? 41.218 -31.589 -11.472 1.00 17.54 ?  18  ILE   B HG12 1 
ATOM   4260 H HG13 . ILE   B 1 18  ? 40.944 -30.273 -10.623 1.00 17.54 ?  18  ILE   B HG13 1 
ATOM   4261 H HG21 . ILE   B 1 18  ? 38.565 -32.155 -12.643 1.00 17.19 ?  18  ILE   B HG21 1 
ATOM   4262 H HG22 . ILE   B 1 18  ? 38.655 -31.160 -13.878 1.00 17.19 ?  18  ILE   B HG22 1 
ATOM   4263 H HG23 . ILE   B 1 18  ? 39.902 -32.068 -13.497 1.00 17.19 ?  18  ILE   B HG23 1 
ATOM   4264 H HD11 . ILE   B 1 18  ? 40.334 -32.100 -9.370  1.00 19.54 ?  18  ILE   B HD11 1 
ATOM   4265 H HD12 . ILE   B 1 18  ? 39.024 -31.279 -9.737  1.00 19.54 ?  18  ILE   B HD12 1 
ATOM   4266 H HD13 . ILE   B 1 18  ? 39.377 -32.609 -10.532 1.00 19.54 ?  18  ILE   B HD13 1 
ATOM   4267 N N    . LYS   B 1 19  ? 42.761 -29.953 -13.239 1.00 14.22 ?  19  LYS   B N    1 
ATOM   4268 C CA   . LYS   B 1 19  ? 43.965 -30.422 -13.908 1.00 15.46 ?  19  LYS   B CA   1 
ATOM   4269 C C    . LYS   B 1 19  ? 44.871 -31.098 -12.892 1.00 15.24 ?  19  LYS   B C    1 
ATOM   4270 O O    . LYS   B 1 19  ? 44.956 -30.673 -11.738 1.00 14.50 ?  19  LYS   B O    1 
ATOM   4271 C CB   . LYS   B 1 19  ? 44.727 -29.254 -14.545 1.00 17.00 ?  19  LYS   B CB   1 
ATOM   4272 C CG   . LYS   B 1 19  ? 45.933 -29.657 -15.372 1.00 18.94 ?  19  LYS   B CG   1 
ATOM   4273 C CD   . LYS   B 1 19  ? 46.660 -28.420 -15.886 1.00 20.57 ?  19  LYS   B CD   1 
ATOM   4274 C CE   . LYS   B 1 19  ? 47.809 -28.783 -16.805 1.00 22.70 ?  19  LYS   B CE   1 
ATOM   4275 N NZ   . LYS   B 1 19  ? 48.510 -27.574 -17.309 1.00 23.68 ?  19  LYS   B NZ   1 
ATOM   4276 H H    . LYS   B 1 19  ? 42.881 -29.710 -12.420 1.00 17.06 ?  19  LYS   B H    1 
ATOM   4277 H HA   . LYS   B 1 19  ? 43.724 -31.061 -14.596 1.00 18.55 ?  19  LYS   B HA   1 
ATOM   4278 H HB2  . LYS   B 1 19  ? 44.115 -28.778 -15.126 1.00 20.39 ?  19  LYS   B HB2  1 
ATOM   4279 H HB3  . LYS   B 1 19  ? 45.028 -28.664 -13.834 1.00 20.39 ?  19  LYS   B HB3  1 
ATOM   4280 H HG2  . LYS   B 1 19  ? 46.540 -30.172 -14.821 1.00 22.72 ?  19  LYS   B HG2  1 
ATOM   4281 H HG3  . LYS   B 1 19  ? 45.632 -30.182 -16.131 1.00 22.72 ?  19  LYS   B HG3  1 
ATOM   4282 H HD2  . LYS   B 1 19  ? 46.034 -27.866 -16.379 1.00 24.69 ?  19  LYS   B HD2  1 
ATOM   4283 H HD3  . LYS   B 1 19  ? 47.016 -27.926 -15.129 1.00 24.69 ?  19  LYS   B HD3  1 
ATOM   4284 H HE2  . LYS   B 1 19  ? 48.447 -29.327 -16.315 1.00 27.23 ?  19  LYS   B HE2  1 
ATOM   4285 H HE3  . LYS   B 1 19  ? 47.463 -29.278 -17.565 1.00 27.23 ?  19  LYS   B HE3  1 
ATOM   4286 H HZ1  . LYS   B 1 19  ? 49.133 -27.809 -17.902 1.00 28.41 ?  19  LYS   B HZ1  1 
ATOM   4287 H HZ2  . LYS   B 1 19  ? 47.929 -27.027 -17.704 1.00 28.41 ?  19  LYS   B HZ2  1 
ATOM   4288 H HZ3  . LYS   B 1 19  ? 48.901 -27.144 -16.636 1.00 28.41 ?  19  LYS   B HZ3  1 
ATOM   4289 N N    . ASN   B 1 20  ? 45.548 -32.151 -13.331 1.00 16.36 ?  20  ASN   B N    1 
ATOM   4290 C CA   . ASN   B 1 20  ? 46.575 -32.789 -12.516 1.00 17.52 ?  20  ASN   B CA   1 
ATOM   4291 C C    . ASN   B 1 20  ? 47.846 -31.967 -12.695 1.00 18.00 ?  20  ASN   B C    1 
ATOM   4292 O O    . ASN   B 1 20  ? 48.495 -32.029 -13.744 1.00 19.80 ?  20  ASN   B O    1 
ATOM   4293 C CB   . ASN   B 1 20  ? 46.745 -34.239 -12.961 1.00 19.15 ?  20  ASN   B CB   1 
ATOM   4294 C CG   . ASN   B 1 20  ? 47.895 -34.953 -12.271 1.00 20.71 ?  20  ASN   B CG   1 
ATOM   4295 O OD1  . ASN   B 1 20  ? 48.542 -35.818 -12.871 1.00 23.10 ?  20  ASN   B OD1  1 
ATOM   4296 N ND2  . ASN   B 1 20  ? 48.148 -34.618 -11.015 1.00 20.16 ?  20  ASN   B ND2  1 
ATOM   4297 H H    . ASN   B 1 20  ? 45.435 -32.517 -14.103 1.00 19.63 ?  20  ASN   B H    1 
ATOM   4298 H HA   . ASN   B 1 20  ? 46.304 -32.774 -11.584 1.00 21.02 ?  20  ASN   B HA   1 
ATOM   4299 H HB2  . ASN   B 1 20  ? 45.931 -34.728 -12.760 1.00 22.97 ?  20  ASN   B HB2  1 
ATOM   4300 H HB3  . ASN   B 1 20  ? 46.913 -34.256 -13.915 1.00 22.97 ?  20  ASN   B HB3  1 
ATOM   4301 H HD21 . ASN   B 1 20  ? 48.794 -34.992 -10.590 1.00 24.19 ?  20  ASN   B HD21 1 
ATOM   4302 H HD22 . ASN   B 1 20  ? 47.675 -34.012 -10.620 1.00 24.19 ?  20  ASN   B HD22 1 
ATOM   4303 N N    . ALA   B 1 21  ? 48.199 -31.170 -11.684 1.00 17.22 ?  21  ALA   B N    1 
ATOM   4304 C CA   . ALA   B 1 21  ? 49.323 -30.260 -11.832 1.00 17.92 ?  21  ALA   B CA   1 
ATOM   4305 C C    . ALA   B 1 21  ? 49.777 -29.752 -10.471 1.00 16.67 ?  21  ALA   B C    1 
ATOM   4306 O O    . ALA   B 1 21  ? 49.033 -29.781 -9.489  1.00 16.82 ?  21  ALA   B O    1 
ATOM   4307 C CB   . ALA   B 1 21  ? 48.953 -29.096 -12.747 1.00 19.30 ?  21  ALA   B CB   1 
ATOM   4308 H H    . ALA   B 1 21  ? 47.805 -31.144 -10.913 1.00 20.67 ?  21  ALA   B H    1 
ATOM   4309 H HA   . ALA   B 1 21  ? 50.062 -30.746 -12.233 1.00 21.50 ?  21  ALA   B HA   1 
ATOM   4310 H HB1  . ALA   B 1 21  ? 49.745 -28.569 -12.901 1.00 23.16 ?  21  ALA   B HB1  1 
ATOM   4311 H HB2  . ALA   B 1 21  ? 48.623 -29.460 -13.584 1.00 23.16 ?  21  ALA   B HB2  1 
ATOM   4312 H HB3  . ALA   B 1 21  ? 48.264 -28.571 -12.318 1.00 23.16 ?  21  ALA   B HB3  1 
ATOM   4313 N N    . ASP   B 1 22  ? 51.037 -29.312 -10.445 1.00 16.15 ?  22  ASP   B N    1 
ATOM   4314 C CA   . ASP   B 1 22  ? 51.652 -28.611 -9.321  1.00 15.58 ?  22  ASP   B CA   1 
ATOM   4315 C C    . ASP   B 1 22  ? 51.239 -27.142 -9.403  1.00 13.92 ?  22  ASP   B C    1 
ATOM   4316 O O    . ASP   B 1 22  ? 51.550 -26.472 -10.391 1.00 14.38 ?  22  ASP   B O    1 
ATOM   4317 C CB   . ASP   B 1 22  ? 53.170 -28.782 -9.479  1.00 17.20 ?  22  ASP   B CB   1 
ATOM   4318 C CG   . ASP   B 1 22  ? 54.001 -28.020 -8.449  1.00 18.83 ?  22  ASP   B CG   1 
ATOM   4319 O OD1  . ASP   B 1 22  ? 53.628 -26.914 -8.034  1.00 18.87 ?  22  ASP   B OD1  1 
ATOM   4320 O OD2  . ASP   B 1 22  ? 55.087 -28.523 -8.079  1.00 21.31 -1 22  ASP   B OD2  1 
ATOM   4321 H H    . ASP   B 1 22  ? 51.583 -29.416 -11.109 1.00 19.38 ?  22  ASP   B H    1 
ATOM   4322 H HA   . ASP   B 1 22  ? 51.366 -28.997 -8.477  1.00 18.70 ?  22  ASP   B HA   1 
ATOM   4323 H HB2  . ASP   B 1 22  ? 53.396 -29.719 -9.404  1.00 20.64 ?  22  ASP   B HB2  1 
ATOM   4324 H HB3  . ASP   B 1 22  ? 53.433 -28.447 -10.351 1.00 20.64 ?  22  ASP   B HB3  1 
ATOM   4325 N N    . ILE   B 1 23  ? 50.521 -26.652 -8.383  1.00 13.13 ?  23  ILE   B N    1 
ATOM   4326 C CA   . ILE   B 1 23  ? 49.937 -25.310 -8.445  1.00 12.39 ?  23  ILE   B CA   1 
ATOM   4327 C C    . ILE   B 1 23  ? 50.995 -24.227 -8.587  1.00 12.28 ?  23  ILE   B C    1 
ATOM   4328 O O    . ILE   B 1 23  ? 50.731 -23.185 -9.193  1.00 12.14 ?  23  ILE   B O    1 
ATOM   4329 C CB   . ILE   B 1 23  ? 49.004 -25.068 -7.245  1.00 13.08 ?  23  ILE   B CB   1 
ATOM   4330 C CG1  . ILE   B 1 23  ? 48.175 -23.796 -7.445  1.00 13.73 ?  23  ILE   B CG1  1 
ATOM   4331 C CG2  . ILE   B 1 23  ? 49.776 -25.025 -5.944  1.00 13.91 ?  23  ILE   B CG2  1 
ATOM   4332 C CD1  . ILE   B 1 23  ? 47.044 -23.656 -6.449  1.00 14.44 ?  23  ILE   B CD1  1 
ATOM   4333 H H    . ILE   B 1 23  ? 50.360 -27.082 -7.656  1.00 15.75 ?  23  ILE   B H    1 
ATOM   4334 H HA   . ILE   B 1 23  ? 49.388 -25.268 -9.241  1.00 14.86 ?  23  ILE   B HA   1 
ATOM   4335 H HB   . ILE   B 1 23  ? 48.384 -25.817 -7.199  1.00 15.69 ?  23  ILE   B HB   1 
ATOM   4336 H HG12 . ILE   B 1 23  ? 48.760 -23.025 -7.344  1.00 16.47 ?  23  ILE   B HG12 1 
ATOM   4337 H HG13 . ILE   B 1 23  ? 47.794 -23.802 -8.338  1.00 16.47 ?  23  ILE   B HG13 1 
ATOM   4338 H HG21 . ILE   B 1 23  ? 49.150 -25.030 -5.206  1.00 16.69 ?  23  ILE   B HG21 1 
ATOM   4339 H HG22 . ILE   B 1 23  ? 50.352 -25.804 -5.896  1.00 16.69 ?  23  ILE   B HG22 1 
ATOM   4340 H HG23 . ILE   B 1 23  ? 50.311 -24.217 -5.925  1.00 16.69 ?  23  ILE   B HG23 1 
ATOM   4341 H HD11 . ILE   B 1 23  ? 46.518 -22.875 -6.679  1.00 17.32 ?  23  ILE   B HD11 1 
ATOM   4342 H HD12 . ILE   B 1 23  ? 46.490 -24.453 -6.495  1.00 17.32 ?  23  ILE   B HD12 1 
ATOM   4343 H HD13 . ILE   B 1 23  ? 47.415 -23.561 -5.561  1.00 17.32 ?  23  ILE   B HD13 1 
ATOM   4344 N N    . VAL   B 1 24  ? 52.190 -24.432 -8.026  1.00 12.59 ?  24  VAL   B N    1 
ATOM   4345 C CA   . VAL   B 1 24  ? 53.268 -23.456 -8.194  1.00 13.12 ?  24  VAL   B CA   1 
ATOM   4346 C C    . VAL   B 1 24  ? 53.717 -23.410 -9.647  1.00 13.19 ?  24  VAL   B C    1 
ATOM   4347 O O    . VAL   B 1 24  ? 53.860 -22.334 -10.238 1.00 13.72 ?  24  VAL   B O    1 
ATOM   4348 C CB   . VAL   B 1 24  ? 54.446 -23.785 -7.257  1.00 14.01 ?  24  VAL   B CB   1 
ATOM   4349 C CG1  . VAL   B 1 24  ? 55.652 -22.907 -7.585  1.00 15.64 ?  24  VAL   B CG1  1 
ATOM   4350 C CG2  . VAL   B 1 24  ? 54.043 -23.609 -5.811  1.00 15.43 ?  24  VAL   B CG2  1 
ATOM   4351 H H    . VAL   B 1 24  ? 52.399 -25.115 -7.548  1.00 15.11 ?  24  VAL   B H    1 
ATOM   4352 H HA   . VAL   B 1 24  ? 52.943 -22.579 -7.953  1.00 15.74 ?  24  VAL   B HA   1 
ATOM   4353 H HB   . VAL   B 1 24  ? 54.709 -24.715 -7.380  1.00 16.81 ?  24  VAL   B HB   1 
ATOM   4354 H HG11 . VAL   B 1 24  ? 56.247 -22.888 -6.818  1.00 18.76 ?  24  VAL   B HG11 1 
ATOM   4355 H HG12 . VAL   B 1 24  ? 56.115 -23.281 -8.350  1.00 18.76 ?  24  VAL   B HG12 1 
ATOM   4356 H HG13 . VAL   B 1 24  ? 55.342 -22.011 -7.784  1.00 18.76 ?  24  VAL   B HG13 1 
ATOM   4357 H HG21 . VAL   B 1 24  ? 54.781 -23.874 -5.240  1.00 18.52 ?  24  VAL   B HG21 1 
ATOM   4358 H HG22 . VAL   B 1 24  ? 53.825 -22.677 -5.659  1.00 18.52 ?  24  VAL   B HG22 1 
ATOM   4359 H HG23 . VAL   B 1 24  ? 53.269 -24.166 -5.629  1.00 18.52 ?  24  VAL   B HG23 1 
ATOM   4360 N N    . GLU   B 1 25  ? 53.975 -24.579 -10.238 1.00 14.26 ?  25  GLU   B N    1 
ATOM   4361 C CA   . GLU   B 1 25  ? 54.367 -24.610 -11.641 1.00 15.75 ?  25  GLU   B CA   1 
ATOM   4362 C C    . GLU   B 1 25  ? 53.258 -24.061 -12.525 1.00 14.34 ?  25  GLU   B C    1 
ATOM   4363 O O    . GLU   B 1 25  ? 53.524 -23.348 -13.501 1.00 15.48 ?  25  GLU   B O    1 
ATOM   4364 C CB   . GLU   B 1 25  ? 54.759 -26.030 -12.040 1.00 19.89 ?  25  GLU   B CB   1 
ATOM   4365 C CG   . GLU   B 1 25  ? 56.044 -26.490 -11.368 1.00 25.38 ?  25  GLU   B CG   1 
ATOM   4366 C CD   . GLU   B 1 25  ? 57.168 -25.463 -11.457 1.00 30.71 ?  25  GLU   B CD   1 
ATOM   4367 O OE1  . GLU   B 1 25  ? 57.537 -25.072 -12.586 1.00 32.69 ?  25  GLU   B OE1  1 
ATOM   4368 O OE2  . GLU   B 1 25  ? 57.672 -25.026 -10.396 1.00 32.60 -1 25  GLU   B OE2  1 
ATOM   4369 H H    . GLU   B 1 25  ? 53.929 -25.350 -9.854  1.00 17.11 ?  25  GLU   B H    1 
ATOM   4370 H HA   . GLU   B 1 25  ? 55.130 -24.029 -11.762 1.00 18.90 ?  25  GLU   B HA   1 
ATOM   4371 H HB2  . GLU   B 1 25  ? 54.051 -26.643 -11.779 1.00 23.86 ?  25  GLU   B HB2  1 
ATOM   4372 H HB3  . GLU   B 1 25  ? 54.890 -26.067 -13.000 1.00 23.86 ?  25  GLU   B HB3  1 
ATOM   4373 H HG2  . GLU   B 1 25  ? 55.874 -26.642 -10.430 1.00 30.45 ?  25  GLU   B HG2  1 
ATOM   4374 H HG3  . GLU   B 1 25  ? 56.346 -27.308 -11.795 1.00 30.45 ?  25  GLU   B HG3  1 
ATOM   4375 N N    A GLU   B 1 26  ? 52.005 -24.373 -12.193 0.40 13.65 ?  26  GLU   B N    1 
ATOM   4376 N N    B GLU   B 1 26  ? 52.004 -24.379 -12.194 0.60 14.06 ?  26  GLU   B N    1 
ATOM   4377 C CA   A GLU   B 1 26  ? 50.884 -23.842 -12.959 0.40 13.65 ?  26  GLU   B CA   1 
ATOM   4378 C CA   B GLU   B 1 26  ? 50.875 -23.850 -12.951 0.60 14.70 ?  26  GLU   B CA   1 
ATOM   4379 C C    A GLU   B 1 26  ? 50.838 -22.326 -12.876 0.40 13.14 ?  26  GLU   B C    1 
ATOM   4380 C C    B GLU   B 1 26  ? 50.834 -22.332 -12.874 0.60 13.50 ?  26  GLU   B C    1 
ATOM   4381 O O    A GLU   B 1 26  ? 50.652 -21.642 -13.887 0.40 14.15 ?  26  GLU   B O    1 
ATOM   4382 O O    B GLU   B 1 26  ? 50.641 -21.653 -13.887 0.60 14.73 ?  26  GLU   B O    1 
ATOM   4383 C CB   A GLU   B 1 26  ? 49.573 -24.428 -12.443 0.40 14.51 ?  26  GLU   B CB   1 
ATOM   4384 C CB   B GLU   B 1 26  ? 49.564 -24.425 -12.413 0.60 16.94 ?  26  GLU   B CB   1 
ATOM   4385 C CG   A GLU   B 1 26  ? 49.296 -25.818 -12.942 0.40 15.93 ?  26  GLU   B CG   1 
ATOM   4386 C CG   B GLU   B 1 26  ? 49.045 -25.647 -13.145 0.60 19.79 ?  26  GLU   B CG   1 
ATOM   4387 C CD   A GLU   B 1 26  ? 49.127 -25.876 -14.445 0.40 16.30 ?  26  GLU   B CD   1 
ATOM   4388 C CD   B GLU   B 1 26  ? 48.750 -25.368 -14.616 0.60 20.80 ?  26  GLU   B CD   1 
ATOM   4389 O OE1  A GLU   B 1 26  ? 48.318 -25.095 -14.985 0.40 15.83 ?  26  GLU   B OE1  1 
ATOM   4390 O OE1  B GLU   B 1 26  ? 47.732 -24.713 -14.940 0.60 21.71 ?  26  GLU   B OE1  1 
ATOM   4391 O OE2  A GLU   B 1 26  ? 49.810 -26.697 -15.086 0.40 17.23 -1 26  GLU   B OE2  1 
ATOM   4392 O OE2  B GLU   B 1 26  ? 49.549 -25.811 -15.453 0.60 20.75 -1 26  GLU   B OE2  1 
ATOM   4393 H H    A GLU   B 1 26  ? 51.780 -24.888 -11.538 0.40 16.37 ?  26  GLU   B H    1 
ATOM   4394 H H    B GLU   B 1 26  ? 51.783 -24.899 -11.540 0.60 16.86 ?  26  GLU   B H    1 
ATOM   4395 H HA   A GLU   B 1 26  ? 50.986 -24.091 -13.889 0.40 16.37 ?  26  GLU   B HA   1 
ATOM   4396 H HA   B GLU   B 1 26  ? 50.967 -24.106 -13.881 0.60 17.64 ?  26  GLU   B HA   1 
ATOM   4397 H HB2  A GLU   B 1 26  ? 49.605 -24.463 -11.472 0.40 17.41 ?  26  GLU   B HB2  1 
ATOM   4398 H HB2  B GLU   B 1 26  ? 49.691 -24.671 -11.484 0.60 20.33 ?  26  GLU   B HB2  1 
ATOM   4399 H HB3  A GLU   B 1 26  ? 48.840 -23.855 -12.724 0.40 17.41 ?  26  GLU   B HB3  1 
ATOM   4400 H HB3  B GLU   B 1 26  ? 48.879 -23.740 -12.476 0.60 20.33 ?  26  GLU   B HB3  1 
ATOM   4401 H HG2  A GLU   B 1 26  ? 50.044 -26.378 -12.715 0.40 19.12 ?  26  GLU   B HG2  1 
ATOM   4402 H HG2  B GLU   B 1 26  ? 49.712 -26.352 -13.075 0.60 23.74 ?  26  GLU   B HG2  1 
ATOM   4403 H HG3  A GLU   B 1 26  ? 48.483 -26.139 -12.526 0.40 19.12 ?  26  GLU   B HG3  1 
ATOM   4404 H HG3  B GLU   B 1 26  ? 48.218 -25.934 -12.732 0.60 23.74 ?  26  GLU   B HG3  1 
ATOM   4405 N N    . ALA   B 1 27  ? 50.988 -21.782 -11.669 1.00 12.74 ?  27  ALA   B N    1 
ATOM   4406 C CA   . ALA   B 1 27  ? 50.945 -20.334 -11.516 1.00 13.22 ?  27  ALA   B CA   1 
ATOM   4407 C C    . ALA   B 1 27  ? 52.021 -19.670 -12.366 1.00 14.28 ?  27  ALA   B C    1 
ATOM   4408 O O    . ALA   B 1 27  ? 51.767 -18.661 -13.042 1.00 15.03 ?  27  ALA   B O    1 
ATOM   4409 C CB   . ALA   B 1 27  ? 51.093 -19.959 -10.042 1.00 13.42 ?  27  ALA   B CB   1 
ATOM   4410 H H    A ALA   B 1 27  ? 51.113 -22.221 -10.940 0.40 15.29 ?  27  ALA   B H    1 
ATOM   4411 H H    B ALA   B 1 27  ? 51.114 -22.219 -10.939 0.60 15.29 ?  27  ALA   B H    1 
ATOM   4412 H HA   . ALA   B 1 27  ? 50.088 -20.008 -11.819 1.00 15.86 ?  27  ALA   B HA   1 
ATOM   4413 H HB1  . ALA   B 1 27  ? 51.055 -18.993 -9.956  1.00 16.11 ?  27  ALA   B HB1  1 
ATOM   4414 H HB2  . ALA   B 1 27  ? 50.364 -20.361 -9.541  1.00 16.11 ?  27  ALA   B HB2  1 
ATOM   4415 H HB3  . ALA   B 1 27  ? 51.942 -20.288 -9.712  1.00 16.11 ?  27  ALA   B HB3  1 
ATOM   4416 N N    . LYS   B 1 28  ? 53.234 -20.227 -12.356 1.00 15.26 ?  28  LYS   B N    1 
ATOM   4417 C CA   . LYS   B 1 28  ? 54.316 -19.615 -13.119 1.00 17.43 ?  28  LYS   B CA   1 
ATOM   4418 C C    . LYS   B 1 28  ? 54.061 -19.688 -14.618 1.00 18.18 ?  28  LYS   B C    1 
ATOM   4419 O O    . LYS   B 1 28  ? 54.483 -18.791 -15.359 1.00 19.70 ?  28  LYS   B O    1 
ATOM   4420 C CB   . LYS   B 1 28  ? 55.665 -20.231 -12.736 1.00 20.70 ?  28  LYS   B CB   1 
ATOM   4421 C CG   . LYS   B 1 28  ? 56.063 -19.912 -11.300 1.00 23.99 ?  28  LYS   B CG   1 
ATOM   4422 C CD   . LYS   B 1 28  ? 57.490 -20.317 -10.964 1.00 28.46 ?  28  LYS   B CD   1 
ATOM   4423 C CE   . LYS   B 1 28  ? 57.606 -21.795 -10.671 1.00 32.46 ?  28  LYS   B CE   1 
ATOM   4424 N NZ   . LYS   B 1 28  ? 58.967 -22.140 -10.167 1.00 34.31 ?  28  LYS   B NZ   1 
ATOM   4425 H H    . LYS   B 1 28  ? 53.456 -20.932 -11.919 1.00 18.31 ?  28  LYS   B H    1 
ATOM   4426 H HA   . LYS   B 1 28  ? 54.363 -18.676 -12.891 1.00 20.92 ?  28  LYS   B HA   1 
ATOM   4427 H HB2  . LYS   B 1 28  ? 55.612 -21.194 -12.825 1.00 24.84 ?  28  LYS   B HB2  1 
ATOM   4428 H HB3  . LYS   B 1 28  ? 56.354 -19.879 -13.322 1.00 24.84 ?  28  LYS   B HB3  1 
ATOM   4429 H HG2  . LYS   B 1 28  ? 55.980 -18.955 -11.160 1.00 28.79 ?  28  LYS   B HG2  1 
ATOM   4430 H HG3  . LYS   B 1 28  ? 55.467 -20.385 -10.700 1.00 28.79 ?  28  LYS   B HG3  1 
ATOM   4431 H HD2  . LYS   B 1 28  ? 58.064 -20.108 -11.717 1.00 34.15 ?  28  LYS   B HD2  1 
ATOM   4432 H HD3  . LYS   B 1 28  ? 57.779 -19.826 -10.178 1.00 34.15 ?  28  LYS   B HD3  1 
ATOM   4433 H HE2  . LYS   B 1 28  ? 56.957 -22.039 -9.992  1.00 38.95 ?  28  LYS   B HE2  1 
ATOM   4434 H HE3  . LYS   B 1 28  ? 57.445 -22.297 -11.485 1.00 38.95 ?  28  LYS   B HE3  1 
ATOM   4435 H HZ1  . LYS   B 1 28  ? 59.018 -23.012 -10.000 1.00 41.17 ?  28  LYS   B HZ1  1 
ATOM   4436 H HZ2  . LYS   B 1 28  ? 59.580 -21.925 -10.776 1.00 41.17 ?  28  LYS   B HZ2  1 
ATOM   4437 H HZ3  . LYS   B 1 28  ? 59.136 -21.691 -9.417  1.00 41.17 ?  28  LYS   B HZ3  1 
ATOM   4438 N N    . LYS   B 1 29  ? 53.347 -20.714 -15.081 1.00 19.20 ?  29  LYS   B N    1 
ATOM   4439 C CA   . LYS   B 1 29  ? 53.061 -20.843 -16.505 1.00 22.17 ?  29  LYS   B CA   1 
ATOM   4440 C C    . LYS   B 1 29  ? 51.822 -20.065 -16.937 1.00 21.10 ?  29  LYS   B C    1 
ATOM   4441 O O    . LYS   B 1 29  ? 51.828 -19.431 -17.999 1.00 22.33 ?  29  LYS   B O    1 
ATOM   4442 C CB   . LYS   B 1 29  ? 52.908 -22.320 -16.878 1.00 27.43 ?  29  LYS   B CB   1 
ATOM   4443 C CG   . LYS   B 1 29  ? 52.822 -22.576 -18.372 1.00 32.22 ?  29  LYS   B CG   1 
ATOM   4444 C CD   . LYS   B 1 29  ? 53.066 -24.046 -18.696 1.00 35.89 ?  29  LYS   B CD   1 
ATOM   4445 C CE   . LYS   B 1 29  ? 51.933 -24.933 -18.203 1.00 38.49 ?  29  LYS   B CE   1 
ATOM   4446 N NZ   . LYS   B 1 29  ? 52.178 -26.370 -18.524 1.00 39.96 ?  29  LYS   B NZ   1 
ATOM   4447 H H    . LYS   B 1 29  ? 53.015 -21.342 -14.588 1.00 23.03 ?  29  LYS   B H    1 
ATOM   4448 H HA   . LYS   B 1 29  ? 53.810 -20.490 -16.995 1.00 26.60 ?  29  LYS   B HA   1 
ATOM   4449 H HB2  . LYS   B 1 29  ? 53.679 -22.803 -16.542 1.00 32.91 ?  29  LYS   B HB2  1 
ATOM   4450 H HB3  . LYS   B 1 29  ? 52.101 -22.665 -16.472 1.00 32.91 ?  29  LYS   B HB3  1 
ATOM   4451 H HG2  . LYS   B 1 29  ? 51.936 -22.335 -18.687 1.00 38.66 ?  29  LYS   B HG2  1 
ATOM   4452 H HG3  . LYS   B 1 29  ? 53.495 -22.045 -18.828 1.00 38.66 ?  29  LYS   B HG3  1 
ATOM   4453 H HD2  . LYS   B 1 29  ? 53.139 -24.154 -19.656 1.00 43.06 ?  29  LYS   B HD2  1 
ATOM   4454 H HD3  . LYS   B 1 29  ? 53.886 -24.336 -18.264 1.00 43.06 ?  29  LYS   B HD3  1 
ATOM   4455 H HE2  . LYS   B 1 29  ? 51.854 -24.849 -17.240 1.00 46.18 ?  29  LYS   B HE2  1 
ATOM   4456 H HE3  . LYS   B 1 29  ? 51.106 -24.664 -18.633 1.00 46.18 ?  29  LYS   B HE3  1 
ATOM   4457 H HZ1  . LYS   B 1 29  ? 51.502 -26.868 -18.227 1.00 47.95 ?  29  LYS   B HZ1  1 
ATOM   4458 H HZ2  . LYS   B 1 29  ? 52.250 -26.478 -19.405 1.00 47.95 ?  29  LYS   B HZ2  1 
ATOM   4459 H HZ3  . LYS   B 1 29  ? 52.931 -26.645 -18.137 1.00 47.95 ?  29  LYS   B HZ3  1 
ATOM   4460 N N    . VAL   B 1 30  ? 50.758 -20.112 -16.130 1.00 19.43 ?  30  VAL   B N    1 
ATOM   4461 C CA   . VAL   B 1 30  ? 49.468 -19.515 -16.490 1.00 19.49 ?  30  VAL   B CA   1 
ATOM   4462 C C    . VAL   B 1 30  ? 49.471 -18.004 -16.318 1.00 19.02 ?  30  VAL   B C    1 
ATOM   4463 O O    . VAL   B 1 30  ? 48.732 -17.288 -17.013 1.00 20.12 ?  30  VAL   B O    1 
ATOM   4464 C CB   . VAL   B 1 30  ? 48.361 -20.140 -15.617 1.00 20.54 ?  30  VAL   B CB   1 
ATOM   4465 C CG1  . VAL   B 1 30  ? 47.070 -19.330 -15.694 1.00 20.88 ?  30  VAL   B CG1  1 
ATOM   4466 C CG2  . VAL   B 1 30  ? 48.122 -21.591 -16.003 1.00 21.53 ?  30  VAL   B CG2  1 
ATOM   4467 H H    . VAL   B 1 30  ? 50.742 -20.514 -15.357 1.00 23.31 ?  30  VAL   B H    1 
ATOM   4468 H HA   . VAL   B 1 30  ? 49.268 -19.726 -17.412 1.00 23.39 ?  30  VAL   B HA   1 
ATOM   4469 H HB   . VAL   B 1 30  ? 48.647 -20.136 -14.692 1.00 24.65 ?  30  VAL   B HB   1 
ATOM   4470 H HG11 . VAL   B 1 30  ? 46.326 -19.911 -15.466 1.00 25.05 ?  30  VAL   B HG11 1 
ATOM   4471 H HG12 . VAL   B 1 30  ? 47.115 -18.597 -15.063 1.00 25.05 ?  30  VAL   B HG12 1 
ATOM   4472 H HG13 . VAL   B 1 30  ? 46.955 -19.000 -16.594 1.00 25.05 ?  30  VAL   B HG13 1 
ATOM   4473 H HG21 . VAL   B 1 30  ? 47.429 -21.964 -15.431 1.00 25.84 ?  30  VAL   B HG21 1 
ATOM   4474 H HG22 . VAL   B 1 30  ? 47.834 -21.628 -16.930 1.00 25.84 ?  30  VAL   B HG22 1 
ATOM   4475 H HG23 . VAL   B 1 30  ? 48.945 -22.087 -15.890 1.00 25.84 ?  30  VAL   B HG23 1 
ATOM   4476 N N    . LYS   B 1 31  ? 50.243 -17.514 -15.366 1.00 18.79 ?  31  LYS   B N    1 
ATOM   4477 C CA   . LYS   B 1 31  ? 50.278 -16.111 -14.985 1.00 19.72 ?  31  LYS   B CA   1 
ATOM   4478 C C    . LYS   B 1 31  ? 48.874 -15.639 -14.617 1.00 17.22 ?  31  LYS   B C    1 
ATOM   4479 O O    . LYS   B 1 31  ? 48.338 -14.716 -15.245 1.00 18.28 ?  31  LYS   B O    1 
ATOM   4480 C CB   . LYS   B 1 31  ? 50.925 -15.286 -16.100 1.00 23.74 ?  31  LYS   B CB   1 
ATOM   4481 C CG   . LYS   B 1 31  ? 52.356 -15.733 -16.407 1.00 27.86 ?  31  LYS   B CG   1 
ATOM   4482 C CD   . LYS   B 1 31  ? 52.913 -15.041 -17.634 1.00 32.42 ?  31  LYS   B CD   1 
ATOM   4483 C CE   . LYS   B 1 31  ? 54.398 -15.286 -17.781 1.00 35.91 ?  31  LYS   B CE   1 
ATOM   4484 N NZ   . LYS   B 1 31  ? 55.126 -14.837 -16.564 1.00 38.02 ?  31  LYS   B NZ   1 
ATOM   4485 H H    . LYS   B 1 31  ? 50.773 -18.008 -14.910 1.00 22.54 ?  31  LYS   B H    1 
ATOM   4486 H HA   . LYS   B 1 31  ? 50.826 -16.035 -14.201 1.00 23.66 ?  31  LYS   B HA   1 
ATOM   4487 H HB2  . LYS   B 1 31  ? 50.401 -15.377 -16.911 1.00 28.48 ?  31  LYS   B HB2  1 
ATOM   4488 H HB3  . LYS   B 1 31  ? 50.951 -14.360 -15.820 1.00 28.48 ?  31  LYS   B HB3  1 
ATOM   4489 H HG2  . LYS   B 1 31  ? 52.915 -15.522 -15.644 1.00 33.43 ?  31  LYS   B HG2  1 
ATOM   4490 H HG3  . LYS   B 1 31  ? 52.362 -16.692 -16.568 1.00 33.43 ?  31  LYS   B HG3  1 
ATOM   4491 H HD2  . LYS   B 1 31  ? 52.466 -15.387 -18.420 1.00 38.91 ?  31  LYS   B HD2  1 
ATOM   4492 H HD3  . LYS   B 1 31  ? 52.767 -14.089 -17.550 1.00 38.91 ?  31  LYS   B HD3  1 
ATOM   4493 H HE2  . LYS   B 1 31  ? 54.561 -16.235 -17.905 1.00 43.09 ?  31  LYS   B HE2  1 
ATOM   4494 H HE3  . LYS   B 1 31  ? 54.731 -14.784 -18.542 1.00 43.09 ?  31  LYS   B HE3  1 
ATOM   4495 H HZ1  . LYS   B 1 31  ? 55.999 -14.816 -16.723 1.00 45.63 ?  31  LYS   B HZ1  1 
ATOM   4496 H HZ2  . LYS   B 1 31  ? 54.852 -14.023 -16.331 1.00 45.63 ?  31  LYS   B HZ2  1 
ATOM   4497 H HZ3  . LYS   B 1 31  ? 54.967 -15.398 -15.891 1.00 45.63 ?  31  LYS   B HZ3  1 
ATOM   4498 N N    . PRO   B 1 32  ? 48.252 -16.246 -13.600 1.00 14.28 ?  32  PRO   B N    1 
ATOM   4499 C CA   . PRO   B 1 32  ? 46.870 -15.892 -13.263 1.00 13.22 ?  32  PRO   B CA   1 
ATOM   4500 C C    . PRO   B 1 32  ? 46.788 -14.545 -12.566 1.00 13.35 ?  32  PRO   B C    1 
ATOM   4501 O O    . PRO   B 1 32  ? 47.706 -14.125 -11.857 1.00 14.67 ?  32  PRO   B O    1 
ATOM   4502 C CB   . PRO   B 1 32  ? 46.460 -17.012 -12.301 1.00 13.76 ?  32  PRO   B CB   1 
ATOM   4503 C CG   . PRO   B 1 32  ? 47.754 -17.359 -11.606 1.00 14.05 ?  32  PRO   B CG   1 
ATOM   4504 C CD   . PRO   B 1 32  ? 48.811 -17.242 -12.664 1.00 14.25 ?  32  PRO   B CD   1 
ATOM   4505 H HA   . PRO   B 1 32  ? 46.297 -15.903 -14.050 1.00 15.87 ?  32  PRO   B HA   1 
ATOM   4506 H HB2  . PRO   B 1 32  ? 45.800 -16.686 -11.667 1.00 16.51 ?  32  PRO   B HB2  1 
ATOM   4507 H HB3  . PRO   B 1 32  ? 46.118 -17.772 -12.797 1.00 16.51 ?  32  PRO   B HB3  1 
ATOM   4508 H HG2  . PRO   B 1 32  ? 47.916 -16.730 -10.883 1.00 16.86 ?  32  PRO   B HG2  1 
ATOM   4509 H HG3  . PRO   B 1 32  ? 47.711 -18.267 -11.264 1.00 16.86 ?  32  PRO   B HG3  1 
ATOM   4510 H HD2  . PRO   B 1 32  ? 49.632 -16.912 -12.281 1.00 17.10 ?  32  PRO   B HD2  1 
ATOM   4511 H HD3  . PRO   B 1 32  ? 48.928 -18.087 -13.113 1.00 17.10 ?  32  PRO   B HD3  1 
ATOM   4512 N N    . THR   B 1 33  ? 45.641 -13.887 -12.741 1.00 12.95 ?  33  THR   B N    1 
ATOM   4513 C CA   . THR   B 1 33  ? 45.348 -12.710 -11.933 1.00 13.04 ?  33  THR   B CA   1 
ATOM   4514 C C    . THR   B 1 33  ? 45.298 -13.062 -10.453 1.00 13.02 ?  33  THR   B C    1 
ATOM   4515 O O    . THR   B 1 33  ? 45.762 -12.282 -9.607  1.00 13.96 ?  33  THR   B O    1 
ATOM   4516 C CB   . THR   B 1 33  ? 44.029 -12.087 -12.391 1.00 13.81 ?  33  THR   B CB   1 
ATOM   4517 O OG1  . THR   B 1 33  ? 44.095 -11.821 -13.796 1.00 13.88 ?  33  THR   B OG1  1 
ATOM   4518 C CG2  . THR   B 1 33  ? 43.744 -10.802 -11.631 1.00 15.30 ?  33  THR   B CG2  1 
ATOM   4519 H H    . THR   B 1 33  ? 45.022 -14.096 -13.307 1.00 15.53 ?  33  THR   B H    1 
ATOM   4520 H HA   . THR   B 1 33  ? 46.043 -12.054 -12.059 1.00 15.64 ?  33  THR   B HA   1 
ATOM   4521 H HB   . THR   B 1 33  ? 43.298 -12.709 -12.223 1.00 16.57 ?  33  THR   B HB   1 
ATOM   4522 H HG1  . THR   B 1 33  ? 43.379 -11.457 -14.059 1.00 16.65 ?  33  THR   B HG1  1 
ATOM   4523 H HG21 . THR   B 1 33  ? 42.999 -10.335 -12.038 1.00 18.36 ?  33  THR   B HG21 1 
ATOM   4524 H HG22 . THR   B 1 33  ? 43.522 -11.006 -10.708 1.00 18.36 ?  33  THR   B HG22 1 
ATOM   4525 H HG23 . THR   B 1 33  ? 44.525 -10.231 -11.651 1.00 18.36 ?  33  THR   B HG23 1 
ATOM   4526 N N    . VAL   B 1 34  ? 44.750 -14.238 -10.120 1.00 12.11 ?  34  VAL   B N    1 
ATOM   4527 C CA   . VAL   B 1 34  ? 44.560 -14.636 -8.729  1.00 11.43 ?  34  VAL   B CA   1 
ATOM   4528 C C    . VAL   B 1 34  ? 44.994 -16.086 -8.566  1.00 10.59 ?  34  VAL   B C    1 
ATOM   4529 O O    . VAL   B 1 34  ? 44.465 -16.975 -9.244  1.00 11.52 ?  34  VAL   B O    1 
ATOM   4530 C CB   . VAL   B 1 34  ? 43.094 -14.497 -8.269  1.00 12.56 ?  34  VAL   B CB   1 
ATOM   4531 C CG1  . VAL   B 1 34  ? 42.944 -14.971 -6.829  1.00 12.95 ?  34  VAL   B CG1  1 
ATOM   4532 C CG2  . VAL   B 1 34  ? 42.586 -13.072 -8.432  1.00 13.76 ?  34  VAL   B CG2  1 
ATOM   4533 H H    . VAL   B 1 34  ? 44.478 -14.830 -10.686 1.00 14.54 ?  34  VAL   B H    1 
ATOM   4534 H HA   . VAL   B 1 34  ? 45.114 -14.085 -8.155  1.00 13.72 ?  34  VAL   B HA   1 
ATOM   4535 H HB   . VAL   B 1 34  ? 42.540 -15.073 -8.820  1.00 15.07 ?  34  VAL   B HB   1 
ATOM   4536 H HG11 . VAL   B 1 34  ? 42.099 -14.652 -6.475  1.00 15.54 ?  34  VAL   B HG11 1 
ATOM   4537 H HG12 . VAL   B 1 34  ? 42.960 -15.944 -6.806  1.00 15.54 ?  34  VAL   B HG12 1 
ATOM   4538 H HG13 . VAL   B 1 34  ? 43.676 -14.617 -6.300  1.00 15.54 ?  34  VAL   B HG13 1 
ATOM   4539 H HG21 . VAL   B 1 34  ? 41.668 -13.024 -8.118  1.00 16.52 ?  34  VAL   B HG21 1 
ATOM   4540 H HG22 . VAL   B 1 34  ? 43.144 -12.475 -7.913  1.00 16.52 ?  34  VAL   B HG22 1 
ATOM   4541 H HG23 . VAL   B 1 34  ? 42.625 -12.830 -9.371  1.00 16.52 ?  34  VAL   B HG23 1 
ATOM   4542 N N    . VAL   B 1 35  ? 45.910 -16.337 -7.634  1.00 10.29 ?  35  VAL   B N    1 
ATOM   4543 C CA   . VAL   B 1 35  ? 46.144 -17.681 -7.117  1.00 9.94  ?  35  VAL   B CA   1 
ATOM   4544 C C    . VAL   B 1 35  ? 45.606 -17.739 -5.696  1.00 9.65  ?  35  VAL   B C    1 
ATOM   4545 O O    . VAL   B 1 35  ? 45.826 -16.814 -4.907  1.00 10.27 ?  35  VAL   B O    1 
ATOM   4546 C CB   . VAL   B 1 35  ? 47.626 -18.105 -7.205  1.00 10.42 ?  35  VAL   B CB   1 
ATOM   4547 C CG1  . VAL   B 1 35  ? 48.534 -17.257 -6.304  1.00 11.14 ?  35  VAL   B CG1  1 
ATOM   4548 C CG2  . VAL   B 1 35  ? 47.767 -19.592 -6.872  1.00 10.99 ?  35  VAL   B CG2  1 
ATOM   4549 H H    . VAL   B 1 35  ? 46.424 -15.734 -7.291  1.00 12.34 ?  35  VAL   B H    1 
ATOM   4550 H HA   . VAL   B 1 35  ? 45.629 -18.307 -7.647  1.00 11.92 ?  35  VAL   B HA   1 
ATOM   4551 H HB   . VAL   B 1 35  ? 47.929 -17.995 -8.121  1.00 12.50 ?  35  VAL   B HB   1 
ATOM   4552 H HG11 . VAL   B 1 35  ? 49.455 -17.499 -6.478  1.00 13.36 ?  35  VAL   B HG11 1 
ATOM   4553 H HG12 . VAL   B 1 35  ? 48.381 -16.328 -6.506  1.00 13.36 ?  35  VAL   B HG12 1 
ATOM   4554 H HG13 . VAL   B 1 35  ? 48.310 -17.444 -5.378  1.00 13.36 ?  35  VAL   B HG13 1 
ATOM   4555 H HG21 . VAL   B 1 35  ? 48.686 -19.869 -6.991  1.00 13.19 ?  35  VAL   B HG21 1 
ATOM   4556 H HG22 . VAL   B 1 35  ? 47.494 -19.743 -5.948  1.00 13.19 ?  35  VAL   B HG22 1 
ATOM   4557 H HG23 . VAL   B 1 35  ? 47.189 -20.113 -7.464  1.00 13.19 ?  35  VAL   B HG23 1 
ATOM   4558 N N    . VAL   B 1 36  ? 44.879 -18.811 -5.378  1.00 9.72  ?  36  VAL   B N    1 
ATOM   4559 C CA   . VAL   B 1 36  ? 44.338 -19.013 -4.044  1.00 9.36  ?  36  VAL   B CA   1 
ATOM   4560 C C    . VAL   B 1 36  ? 45.351 -19.770 -3.198  1.00 9.22  ?  36  VAL   B C    1 
ATOM   4561 O O    . VAL   B 1 36  ? 45.890 -20.805 -3.620  1.00 10.28 ?  36  VAL   B O    1 
ATOM   4562 C CB   . VAL   B 1 36  ? 43.004 -19.775 -4.113  1.00 10.01 ?  36  VAL   B CB   1 
ATOM   4563 C CG1  . VAL   B 1 36  ? 42.510 -20.131 -2.724  1.00 10.30 ?  36  VAL   B CG1  1 
ATOM   4564 C CG2  . VAL   B 1 36  ? 41.971 -18.935 -4.856  1.00 10.60 ?  36  VAL   B CG2  1 
ATOM   4565 H H    . VAL   B 1 36  ? 44.692 -19.448 -5.929  1.00 11.67 ?  36  VAL   B H    1 
ATOM   4566 H HA   . VAL   B 1 36  ? 44.174 -18.154 -3.631  1.00 11.23 ?  36  VAL   B HA   1 
ATOM   4567 H HB   . VAL   B 1 36  ? 43.131 -20.599 -4.608  1.00 12.00 ?  36  VAL   B HB   1 
ATOM   4568 H HG11 . VAL   B 1 36  ? 41.568 -20.360 -2.776  1.00 12.35 ?  36  VAL   B HG11 1 
ATOM   4569 H HG12 . VAL   B 1 36  ? 43.016 -20.881 -2.388  1.00 12.35 ?  36  VAL   B HG12 1 
ATOM   4570 H HG13 . VAL   B 1 36  ? 42.625 -19.359 -2.144  1.00 12.35 ?  36  VAL   B HG13 1 
ATOM   4571 H HG21 . VAL   B 1 36  ? 41.126 -19.406 -4.873  1.00 12.71 ?  36  VAL   B HG21 1 
ATOM   4572 H HG22 . VAL   B 1 36  ? 41.868 -18.083 -4.400  1.00 12.71 ?  36  VAL   B HG22 1 
ATOM   4573 H HG23 . VAL   B 1 36  ? 42.282 -18.780 -5.766  1.00 12.71 ?  36  VAL   B HG23 1 
ATOM   4574 N N    . ASN   B 1 37  ? 45.569 -19.282 -1.981  1.00 9.63  ?  37  ASN   B N    1 
ATOM   4575 C CA   . ASN   B 1 37  ? 46.324 -20.003 -0.969  1.00 9.84  ?  37  ASN   B CA   1 
ATOM   4576 C C    . ASN   B 1 37  ? 45.382 -20.676 0.020   1.00 10.03 ?  37  ASN   B C    1 
ATOM   4577 O O    . ASN   B 1 37  ? 44.371 -20.100 0.433   1.00 10.55 ?  37  ASN   B O    1 
ATOM   4578 C CB   . ASN   B 1 37  ? 47.253 -19.052 -0.211  1.00 9.93  ?  37  ASN   B CB   1 
ATOM   4579 C CG   . ASN   B 1 37  ? 48.112 -19.768 0.793   1.00 10.19 ?  37  ASN   B CG   1 
ATOM   4580 O OD1  . ASN   B 1 37  ? 48.450 -20.945 0.616   1.00 10.97 ?  37  ASN   B OD1  1 
ATOM   4581 N ND2  . ASN   B 1 37  ? 48.462 -19.068 1.868   1.00 10.20 ?  37  ASN   B ND2  1 
ATOM   4582 H H    . ASN   B 1 37  ? 45.283 -18.511 -1.706  1.00 11.56 ?  37  ASN   B H    1 
ATOM   4583 H HA   . ASN   B 1 37  ? 46.861 -20.689 -1.391  1.00 11.81 ?  37  ASN   B HA   1 
ATOM   4584 H HB2  . ASN   B 1 37  ? 47.839 -18.615 -0.845  1.00 11.91 ?  37  ASN   B HB2  1 
ATOM   4585 H HB3  . ASN   B 1 37  ? 46.721 -18.396 0.264   1.00 11.91 ?  37  ASN   B HB3  1 
ATOM   4586 H HD21 . ASN   B 1 37  ? 48.957 -19.426 2.476   1.00 12.24 ?  37  ASN   B HD21 1 
ATOM   4587 H HD22 . ASN   B 1 37  ? 48.210 -18.255 1.958   1.00 12.24 ?  37  ASN   B HD22 1 
ATOM   4588 N N    . ALA   B 1 38  ? 45.733 -21.910 0.391   1.00 10.25 ?  38  ALA   B N    1 
ATOM   4589 C CA   . ALA   B 1 38  ? 45.078 -22.654 1.469   1.00 10.39 ?  38  ALA   B CA   1 
ATOM   4590 C C    . ALA   B 1 38  ? 45.665 -22.170 2.796   1.00 10.48 ?  38  ALA   B C    1 
ATOM   4591 O O    . ALA   B 1 38  ? 46.574 -22.773 3.379   1.00 11.27 ?  38  ALA   B O    1 
ATOM   4592 C CB   . ALA   B 1 38  ? 45.308 -24.145 1.279   1.00 11.51 ?  38  ALA   B CB   1 
ATOM   4593 H H    . ALA   B 1 38  ? 46.383 -22.345 0.033   1.00 12.30 ?  38  ALA   B H    1 
ATOM   4594 H HA   . ALA   B 1 38  ? 44.122 -22.477 1.459   1.00 12.47 ?  38  ALA   B HA   1 
ATOM   4595 H HB1  . ALA   B 1 38  ? 44.860 -24.629 2.000   1.00 13.81 ?  38  ALA   B HB1  1 
ATOM   4596 H HB2  . ALA   B 1 38  ? 44.932 -24.420 0.427   1.00 13.81 ?  38  ALA   B HB2  1 
ATOM   4597 H HB3  . ALA   B 1 38  ? 46.255 -24.329 1.302   1.00 13.81 ?  38  ALA   B HB3  1 
ATOM   4598 N N    . ALA   B 1 39  ? 45.160 -21.021 3.246   1.00 10.29 ?  39  ALA   B N    1 
ATOM   4599 C CA   . ALA   B 1 39  ? 45.708 -20.290 4.375   1.00 10.56 ?  39  ALA   B CA   1 
ATOM   4600 C C    . ALA   B 1 39  ? 45.088 -20.736 5.697   1.00 10.60 ?  39  ALA   B C    1 
ATOM   4601 O O    . ALA   B 1 39  ? 44.053 -21.402 5.745   1.00 11.53 ?  39  ALA   B O    1 
ATOM   4602 C CB   . ALA   B 1 39  ? 45.466 -18.787 4.184   1.00 11.38 ?  39  ALA   B CB   1 
ATOM   4603 H H    . ALA   B 1 39  ? 44.473 -20.633 2.889   1.00 12.35 ?  39  ALA   B H    1 
ATOM   4604 H HA   . ALA   B 1 39  ? 46.661 -20.440 4.417   1.00 12.67 ?  39  ALA   B HA   1 
ATOM   4605 H HB1  . ALA   B 1 39  ? 45.838 -18.310 4.945   1.00 13.65 ?  39  ALA   B HB1  1 
ATOM   4606 H HB2  . ALA   B 1 39  ? 45.906 -18.495 3.368   1.00 13.65 ?  39  ALA   B HB2  1 
ATOM   4607 H HB3  . ALA   B 1 39  ? 44.514 -18.620 4.124   1.00 13.65 ?  39  ALA   B HB3  1 
ATOM   4608 N N    . ASN   B 1 40  ? 45.729 -20.318 6.783   1.00 11.68 ?  40  ASN   B N    1 
ATOM   4609 C CA   . ASN   B 1 40  ? 45.165 -20.362 8.121   1.00 12.08 ?  40  ASN   B CA   1 
ATOM   4610 C C    . ASN   B 1 40  ? 44.987 -18.936 8.643   1.00 11.59 ?  40  ASN   B C    1 
ATOM   4611 O O    . ASN   B 1 40  ? 45.398 -17.957 8.009   1.00 11.63 ?  40  ASN   B O    1 
ATOM   4612 C CB   . ASN   B 1 40  ? 46.013 -21.243 9.053   1.00 12.79 ?  40  ASN   B CB   1 
ATOM   4613 C CG   . ASN   B 1 40  ? 47.461 -20.829 9.095   1.00 13.99 ?  40  ASN   B CG   1 
ATOM   4614 O OD1  . ASN   B 1 40  ? 47.772 -19.649 9.178   1.00 16.07 ?  40  ASN   B OD1  1 
ATOM   4615 N ND2  . ASN   B 1 40  ? 48.360 -21.800 9.047   1.00 13.90 ?  40  ASN   B ND2  1 
ATOM   4616 H H    . ASN   B 1 40  ? 46.529 -20.003 6.762   1.00 14.01 ?  40  ASN   B H    1 
ATOM   4617 H HA   . ASN   B 1 40  ? 44.281 -20.758 8.069   1.00 14.49 ?  40  ASN   B HA   1 
ATOM   4618 H HB2  . ASN   B 1 40  ? 45.653 -21.182 9.952   1.00 15.35 ?  40  ASN   B HB2  1 
ATOM   4619 H HB3  . ASN   B 1 40  ? 45.968 -22.161 8.741   1.00 15.35 ?  40  ASN   B HB3  1 
ATOM   4620 H HD21 . ASN   B 1 40  ? 49.200 -21.613 9.072   1.00 16.68 ?  40  ASN   B HD21 1 
ATOM   4621 H HD22 . ASN   B 1 40  ? 48.106 -22.620 8.991   1.00 16.68 ?  40  ASN   B HD22 1 
ATOM   4622 N N    . VAL   B 1 41  ? 44.344 -18.812 9.805   1.00 12.29 ?  41  VAL   B N    1 
ATOM   4623 C CA   . VAL   B 1 41  ? 43.885 -17.493 10.247  1.00 12.93 ?  41  VAL   B CA   1 
ATOM   4624 C C    . VAL   B 1 41  ? 45.036 -16.541 10.540  1.00 12.82 ?  41  VAL   B C    1 
ATOM   4625 O O    . VAL   B 1 41  ? 44.858 -15.322 10.459  1.00 12.99 ?  41  VAL   B O    1 
ATOM   4626 C CB   . VAL   B 1 41  ? 42.906 -17.558 11.438  1.00 14.58 ?  41  VAL   B CB   1 
ATOM   4627 C CG1  . VAL   B 1 41  ? 41.607 -18.237 11.037  1.00 15.18 ?  41  VAL   B CG1  1 
ATOM   4628 C CG2  . VAL   B 1 41  ? 43.550 -18.240 12.636  1.00 15.32 ?  41  VAL   B CG2  1 
ATOM   4629 H H    . VAL   B 1 41  ? 44.168 -19.454 10.340  1.00 14.75 ?  41  VAL   B H    1 
ATOM   4630 H HA   . VAL   B 1 41  ? 43.391 -17.095 9.516   1.00 15.51 ?  41  VAL   B HA   1 
ATOM   4631 H HB   . VAL   B 1 41  ? 42.684 -16.652 11.707  1.00 17.49 ?  41  VAL   B HB   1 
ATOM   4632 H HG11 . VAL   B 1 41  ? 41.003 -18.238 11.798  1.00 18.21 ?  41  VAL   B HG11 1 
ATOM   4633 H HG12 . VAL   B 1 41  ? 41.208 -17.743 10.302  1.00 18.21 ?  41  VAL   B HG12 1 
ATOM   4634 H HG13 . VAL   B 1 41  ? 41.796 -19.145 10.763  1.00 18.21 ?  41  VAL   B HG13 1 
ATOM   4635 H HG21 . VAL   B 1 41  ? 42.909 -18.275 13.363  1.00 18.38 ?  41  VAL   B HG21 1 
ATOM   4636 H HG22 . VAL   B 1 41  ? 43.812 -19.140 12.385  1.00 18.38 ?  41  VAL   B HG22 1 
ATOM   4637 H HG23 . VAL   B 1 41  ? 44.330 -17.732 12.908  1.00 18.38 ?  41  VAL   B HG23 1 
ATOM   4638 N N    . TYR   B 1 42  ? 46.205 -17.056 10.920  1.00 12.99 ?  42  TYR   B N    1 
ATOM   4639 C CA   . TYR   B 1 42  ? 47.360 -16.207 11.183  1.00 13.54 ?  42  TYR   B CA   1 
ATOM   4640 C C    . TYR   B 1 42  ? 48.320 -16.135 10.002  1.00 12.56 ?  42  TYR   B C    1 
ATOM   4641 O O    . TYR   B 1 42  ? 49.410 -15.569 10.134  1.00 13.81 ?  42  TYR   B O    1 
ATOM   4642 C CB   . TYR   B 1 42  ? 48.061 -16.610 12.485  1.00 15.60 ?  42  TYR   B CB   1 
ATOM   4643 C CG   . TYR   B 1 42  ? 47.441 -15.937 13.707  1.00 15.93 ?  42  TYR   B CG   1 
ATOM   4644 C CD1  . TYR   B 1 42  ? 47.644 -14.581 13.947  1.00 15.27 ?  42  TYR   B CD1  1 
ATOM   4645 C CD2  . TYR   B 1 42  ? 46.655 -16.642 14.604  1.00 18.09 ?  42  TYR   B CD2  1 
ATOM   4646 C CE1  . TYR   B 1 42  ? 47.088 -13.951 15.043  1.00 16.42 ?  42  TYR   B CE1  1 
ATOM   4647 C CE2  . TYR   B 1 42  ? 46.097 -16.022 15.709  1.00 18.44 ?  42  TYR   B CE2  1 
ATOM   4648 C CZ   . TYR   B 1 42  ? 46.314 -14.671 15.922  1.00 18.71 ?  42  TYR   B CZ   1 
ATOM   4649 O OH   . TYR   B 1 42  ? 45.764 -14.041 17.019  1.00 21.72 ?  42  TYR   B OH   1 
ATOM   4650 H H    . TYR   B 1 42  ? 46.355 -17.901 11.025  1.00 15.58 ?  42  TYR   B H    1 
ATOM   4651 H HA   . TYR   B 1 42  ? 47.034 -15.309 11.317  1.00 16.24 ?  42  TYR   B HA   1 
ATOM   4652 H HB2  . TYR   B 1 42  ? 47.991 -17.568 12.603  1.00 18.72 ?  42  TYR   B HB2  1 
ATOM   4653 H HB3  . TYR   B 1 42  ? 48.995 -16.346 12.436  1.00 18.72 ?  42  TYR   B HB3  1 
ATOM   4654 H HD1  . TYR   B 1 42  ? 48.169 -14.086 13.350  1.00 18.33 ?  42  TYR   B HD1  1 
ATOM   4655 H HD2  . TYR   B 1 42  ? 46.506 -17.550 14.460  1.00 21.70 ?  42  TYR   B HD2  1 
ATOM   4656 H HE1  . TYR   B 1 42  ? 47.236 -13.045 15.185  1.00 19.70 ?  42  TYR   B HE1  1 
ATOM   4657 H HE2  . TYR   B 1 42  ? 45.570 -16.512 16.297  1.00 22.13 ?  42  TYR   B HE2  1 
ATOM   4658 H HH   . TYR   B 1 42  ? 45.977 -13.233 17.016  1.00 26.06 ?  42  TYR   B HH   1 
ATOM   4659 N N    . LEU   B 1 43  ? 47.917 -16.649 8.844   1.00 11.78 ?  43  LEU   B N    1 
ATOM   4660 C CA   . LEU   B 1 43  ? 48.726 -16.578 7.633   1.00 11.51 ?  43  LEU   B CA   1 
ATOM   4661 C C    . LEU   B 1 43  ? 50.138 -17.088 7.888   1.00 11.85 ?  43  LEU   B C    1 
ATOM   4662 O O    . LEU   B 1 43  ? 51.118 -16.500 7.430   1.00 12.61 ?  43  LEU   B O    1 
ATOM   4663 C CB   . LEU   B 1 43  ? 48.748 -15.172 7.026   1.00 12.03 ?  43  LEU   B CB   1 
ATOM   4664 C CG   . LEU   B 1 43  ? 47.394 -14.558 6.661   1.00 12.20 ?  43  LEU   B CG   1 
ATOM   4665 C CD1  . LEU   B 1 43  ? 47.605 -13.160 6.080   1.00 13.45 ?  43  LEU   B CD1  1 
ATOM   4666 C CD2  . LEU   B 1 43  ? 46.615 -15.453 5.697   1.00 12.72 ?  43  LEU   B CD2  1 
ATOM   4667 H H    . LEU   B 1 43  ? 47.171 -17.057 8.730   1.00 14.13 ?  43  LEU   B H    1 
ATOM   4668 H HA   . LEU   B 1 43  ? 48.326 -17.168 6.966   1.00 13.81 ?  43  LEU   B HA   1 
ATOM   4669 H HB2  . LEU   B 1 43  ? 49.177 -14.579 7.660   1.00 14.43 ?  43  LEU   B HB2  1 
ATOM   4670 H HB3  . LEU   B 1 43  ? 49.276 -15.206 6.210   1.00 14.43 ?  43  LEU   B HB3  1 
ATOM   4671 H HG   . LEU   B 1 43  ? 46.871 -14.465 7.470   1.00 14.64 ?  43  LEU   B HG   1 
ATOM   4672 H HD11 . LEU   B 1 43  ? 46.740 -12.777 5.855   1.00 16.14 ?  43  LEU   B HD11 1 
ATOM   4673 H HD12 . LEU   B 1 43  ? 48.045 -12.603 6.744   1.00 16.14 ?  43  LEU   B HD12 1 
ATOM   4674 H HD13 . LEU   B 1 43  ? 48.155 -13.222 5.285   1.00 16.14 ?  43  LEU   B HD13 1 
ATOM   4675 H HD21 . LEU   B 1 43  ? 45.816 -14.983 5.409   1.00 15.27 ?  43  LEU   B HD21 1 
ATOM   4676 H HD22 . LEU   B 1 43  ? 47.173 -15.657 4.932   1.00 15.27 ?  43  LEU   B HD22 1 
ATOM   4677 H HD23 . LEU   B 1 43  ? 46.369 -16.272 6.157   1.00 15.27 ?  43  LEU   B HD23 1 
ATOM   4678 N N    . LYS   B 1 44  ? 50.238 -18.212 8.606   1.00 12.00 ?  44  LYS   B N    1 
ATOM   4679 C CA   . LYS   B 1 44  ? 51.505 -18.890 8.846   1.00 12.61 ?  44  LYS   B CA   1 
ATOM   4680 C C    . LYS   B 1 44  ? 51.623 -20.005 7.817   1.00 12.08 ?  44  LYS   B C    1 
ATOM   4681 O O    . LYS   B 1 44  ? 50.927 -21.021 7.902   1.00 13.25 ?  44  LYS   B O    1 
ATOM   4682 C CB   . LYS   B 1 44  ? 51.559 -19.407 10.282  1.00 14.46 ?  44  LYS   B CB   1 
ATOM   4683 C CG   . LYS   B 1 44  ? 51.738 -18.291 11.307  1.00 17.30 ?  44  LYS   B CG   1 
ATOM   4684 C CD   . LYS   B 1 44  ? 52.980 -17.460 10.949  1.00 20.04 ?  44  LYS   B CD   1 
ATOM   4685 C CE   . LYS   B 1 44  ? 53.388 -16.474 12.012  1.00 22.91 ?  44  LYS   B CE   1 
ATOM   4686 N NZ   . LYS   B 1 44  ? 54.626 -15.735 11.645  1.00 24.18 ?  44  LYS   B NZ   1 
ATOM   4687 H H    . LYS   B 1 44  ? 49.566 -18.600 8.974   1.00 14.40 ?  44  LYS   B H    1 
ATOM   4688 H HA   . LYS   B 1 44  ? 52.241 -18.281 8.685   1.00 15.12 ?  44  LYS   B HA   1 
ATOM   4689 H HB2  . LYS   B 1 44  ? 50.723 -19.862 10.484  1.00 17.35 ?  44  LYS   B HB2  1 
ATOM   4690 H HB3  . LYS   B 1 44  ? 52.300 -20.020 10.375  1.00 17.35 ?  44  LYS   B HB3  1 
ATOM   4691 H HG2  . LYS   B 1 44  ? 50.961 -17.713 11.304  1.00 20.75 ?  44  LYS   B HG2  1 
ATOM   4692 H HG3  . LYS   B 1 44  ? 51.869 -18.681 12.191  1.00 20.75 ?  44  LYS   B HG3  1 
ATOM   4693 H HD2  . LYS   B 1 44  ? 53.721 -18.071 10.783  1.00 24.05 ?  44  LYS   B HD2  1 
ATOM   4694 H HD3  . LYS   B 1 44  ? 52.789 -16.951 10.147  1.00 24.05 ?  44  LYS   B HD3  1 
ATOM   4695 H HE2  . LYS   B 1 44  ? 52.676 -15.827 12.120  1.00 27.50 ?  44  LYS   B HE2  1 
ATOM   4696 H HE3  . LYS   B 1 44  ? 53.552 -16.950 12.838  1.00 27.50 ?  44  LYS   B HE3  1 
ATOM   4697 H HZ1  . LYS   B 1 44  ? 54.838 -15.159 12.289  1.00 29.02 ?  44  LYS   B HZ1  1 
ATOM   4698 H HZ2  . LYS   B 1 44  ? 55.301 -16.304 11.532  1.00 29.02 ?  44  LYS   B HZ2  1 
ATOM   4699 H HZ3  . LYS   B 1 44  ? 54.500 -15.284 10.886  1.00 29.02 ?  44  LYS   B HZ3  1 
ATOM   4700 N N    . HIS   B 1 45  ? 52.470 -19.783 6.814   1.00 12.00 ?  45  HIS   B N    1 
ATOM   4701 C CA   . HIS   B 1 45  ? 52.493 -20.619 5.614   1.00 11.79 ?  45  HIS   B CA   1 
ATOM   4702 C C    . HIS   B 1 45  ? 53.517 -21.737 5.778   1.00 13.93 ?  45  HIS   B C    1 
ATOM   4703 O O    . HIS   B 1 45  ? 54.579 -21.754 5.160   1.00 16.11 ?  45  HIS   B O    1 
ATOM   4704 C CB   . HIS   B 1 45  ? 52.802 -19.770 4.394   1.00 11.98 ?  45  HIS   B CB   1 
ATOM   4705 C CG   . HIS   B 1 45  ? 51.932 -18.565 4.283   1.00 11.77 ?  45  HIS   B CG   1 
ATOM   4706 N ND1  . HIS   B 1 45  ? 50.555 -18.640 4.254   1.00 11.76 ?  45  HIS   B ND1  1 
ATOM   4707 C CD2  . HIS   B 1 45  ? 52.251 -17.252 4.208   1.00 12.51 ?  45  HIS   B CD2  1 
ATOM   4708 C CE1  . HIS   B 1 45  ? 50.069 -17.416 4.154   1.00 11.44 ?  45  HIS   B CE1  1 
ATOM   4709 N NE2  . HIS   B 1 45  ? 51.074 -16.557 4.121   1.00 11.98 ?  45  HIS   B NE2  1 
ATOM   4710 H H    . HIS   B 1 45  ? 53.034 -19.136 6.794   1.00 14.40 ?  45  HIS   B H    1 
ATOM   4711 H HA   . HIS   B 1 45  ? 51.611 -21.021 5.484   1.00 14.14 ?  45  HIS   B HA   1 
ATOM   4712 H HB2  . HIS   B 1 45  ? 53.721 -19.477 4.439   1.00 14.38 ?  45  HIS   B HB2  1 
ATOM   4713 H HB3  . HIS   B 1 45  ? 52.669 -20.313 3.591   1.00 14.38 ?  45  HIS   B HB3  1 
ATOM   4714 H HD2  . HIS   B 1 45  ? 53.109 -16.895 4.212   1.00 15.01 ?  45  HIS   B HD2  1 
ATOM   4715 H HE1  . HIS   B 1 45  ? 49.167 -17.195 4.102   1.00 13.72 ?  45  HIS   B HE1  1 
ATOM   4716 H HE2  . HIS   B 1 45  ? 51.001 -15.704 4.067   1.00 14.37 ?  45  HIS   B HE2  1 
ATOM   4717 N N    A GLY   B 1 46  ? 53.156 -22.704 6.618   0.40 15.05 ?  46  GLY   B N    1 
ATOM   4718 N N    B GLY   B 1 46  ? 53.164 -22.695 6.628   0.60 15.13 ?  46  GLY   B N    1 
ATOM   4719 C CA   A GLY   B 1 46  ? 54.083 -23.752 7.000   0.40 16.54 ?  46  GLY   B CA   1 
ATOM   4720 C CA   B GLY   B 1 46  ? 54.090 -23.755 6.975   0.60 16.74 ?  46  GLY   B CA   1 
ATOM   4721 C C    A GLY   B 1 46  ? 54.132 -24.971 6.098   0.40 17.86 ?  46  GLY   B C    1 
ATOM   4722 C C    B GLY   B 1 46  ? 54.126 -24.925 6.011   0.60 18.18 ?  46  GLY   B C    1 
ATOM   4723 O O    A GLY   B 1 46  ? 55.215 -25.402 5.690   0.40 19.92 ?  46  GLY   B O    1 
ATOM   4724 O O    B GLY   B 1 46  ? 55.179 -25.264 5.461   0.60 20.57 ?  46  GLY   B O    1 
ATOM   4725 H H    A GLY   B 1 46  ? 52.380 -22.758 6.995   0.40 18.06 ?  46  GLY   B H    1 
ATOM   4726 H H    B GLY   B 1 46  ? 52.398 -22.736 7.030   0.60 18.15 ?  46  GLY   B H    1 
ATOM   4727 H HA2  A GLY   B 1 46  ? 54.974 -23.373 7.037   0.40 19.85 ?  46  GLY   B HA2  1 
ATOM   4728 H HA2  B GLY   B 1 46  ? 54.981 -23.378 7.030   0.60 20.08 ?  46  GLY   B HA2  1 
ATOM   4729 H HA3  A GLY   B 1 46  ? 53.851 -24.058 7.889   0.40 19.85 ?  46  GLY   B HA3  1 
ATOM   4730 H HA3  B GLY   B 1 46  ? 53.853 -24.097 7.851   0.60 20.08 ?  46  GLY   B HA3  1 
ATOM   4731 N N    . GLY   B 1 47  ? 52.976 -25.555 5.788   1.00 17.72 ?  47  GLY   B N    1 
ATOM   4732 C CA   . GLY   B 1 47  ? 52.924 -26.827 5.094   1.00 15.87 ?  47  GLY   B CA   1 
ATOM   4733 C C    . GLY   B 1 47  ? 51.988 -26.813 3.901   1.00 13.41 ?  47  GLY   B C    1 
ATOM   4734 O O    . GLY   B 1 47  ? 51.329 -25.815 3.616   1.00 13.62 ?  47  GLY   B O    1 
ATOM   4735 H H    A GLY   B 1 47  ? 52.202 -25.236 5.990   0.40 21.26 ?  47  GLY   B H    1 
ATOM   4736 H H    B GLY   B 1 47  ? 52.207 -25.270 6.051   0.60 21.26 ?  47  GLY   B H    1 
ATOM   4737 H HA2  . GLY   B 1 47  ? 53.810 -27.065 4.782   1.00 19.04 ?  47  GLY   B HA2  1 
ATOM   4738 H HA3  . GLY   B 1 47  ? 52.625 -27.512 5.712   1.00 19.04 ?  47  GLY   B HA3  1 
ATOM   4739 N N    . GLY   B 1 48  ? 51.944 -27.952 3.216   1.00 12.75 ?  48  GLY   B N    1 
ATOM   4740 C CA   . GLY   B 1 48  ? 51.019 -28.103 2.110   1.00 12.24 ?  48  GLY   B CA   1 
ATOM   4741 C C    . GLY   B 1 48  ? 51.154 -26.996 1.090   1.00 11.66 ?  48  GLY   B C    1 
ATOM   4742 O O    . GLY   B 1 48  ? 52.250 -26.523 0.781   1.00 12.53 ?  48  GLY   B O    1 
ATOM   4743 H H    . GLY   B 1 48  ? 52.446 -28.631 3.363   1.00 15.30 ?  48  GLY   B H    1 
ATOM   4744 H HA2  . GLY   B 1 48  ? 51.182 -28.954 1.668   1.00 14.68 ?  48  GLY   B HA2  1 
ATOM   4745 H HA3  . GLY   B 1 48  ? 50.111 -28.100 2.445   1.00 14.68 ?  48  GLY   B HA3  1 
ATOM   4746 N N    . VAL   B 1 49  ? 50.009 -26.567 0.557   1.00 11.81 ?  49  VAL   B N    1 
ATOM   4747 C CA   . VAL   B 1 49  ? 49.986 -25.545 -0.486  1.00 11.77 ?  49  VAL   B CA   1 
ATOM   4748 C C    . VAL   B 1 49  ? 50.644 -24.257 -0.003  1.00 10.73 ?  49  VAL   B C    1 
ATOM   4749 O O    . VAL   B 1 49  ? 51.431 -23.638 -0.727  1.00 11.58 ?  49  VAL   B O    1 
ATOM   4750 C CB   . VAL   B 1 49  ? 48.538 -25.296 -0.951  1.00 13.18 ?  49  VAL   B CB   1 
ATOM   4751 C CG1  . VAL   B 1 49  ? 48.457 -24.050 -1.825  1.00 13.05 ?  49  VAL   B CG1  1 
ATOM   4752 C CG2  . VAL   B 1 49  ? 47.987 -26.506 -1.691  1.00 14.53 ?  49  VAL   B CG2  1 
ATOM   4753 H H    . VAL   B 1 49  ? 49.229 -26.850 0.786   1.00 14.17 ?  49  VAL   B H    1 
ATOM   4754 H HA   . VAL   B 1 49  ? 50.488 -25.867 -1.251  1.00 14.13 ?  49  VAL   B HA   1 
ATOM   4755 H HB   . VAL   B 1 49  ? 47.981 -25.146 -0.173  1.00 15.81 ?  49  VAL   B HB   1 
ATOM   4756 H HG11 . VAL   B 1 49  ? 47.623 -24.066 -2.320  1.00 15.66 ?  49  VAL   B HG11 1 
ATOM   4757 H HG12 . VAL   B 1 49  ? 48.484 -23.260 -1.258  1.00 15.66 ?  49  VAL   B HG12 1 
ATOM   4758 H HG13 . VAL   B 1 49  ? 49.206 -24.042 -2.440  1.00 15.66 ?  49  VAL   B HG13 1 
ATOM   4759 H HG21 . VAL   B 1 49  ? 47.075 -26.320 -1.965  1.00 17.43 ?  49  VAL   B HG21 1 
ATOM   4760 H HG22 . VAL   B 1 49  ? 48.538 -26.675 -2.473  1.00 17.43 ?  49  VAL   B HG22 1 
ATOM   4761 H HG23 . VAL   B 1 49  ? 48.006 -27.273 -1.100  1.00 17.43 ?  49  VAL   B HG23 1 
ATOM   4762 N N    . ALA   B 1 50  ? 50.301 -23.811 1.208   1.00 10.96 ?  50  ALA   B N    1 
ATOM   4763 C CA   . ALA   B 1 50  ? 50.825 -22.535 1.685   1.00 10.83 ?  50  ALA   B CA   1 
ATOM   4764 C C    . ALA   B 1 50  ? 52.345 -22.568 1.786   1.00 10.95 ?  50  ALA   B C    1 
ATOM   4765 O O    . ALA   B 1 50  ? 53.023 -21.603 1.416   1.00 11.10 ?  50  ALA   B O    1 
ATOM   4766 C CB   . ALA   B 1 50  ? 50.207 -22.177 3.033   1.00 11.44 ?  50  ALA   B CB   1 
ATOM   4767 H H    . ALA   B 1 50  ? 49.781 -24.217 1.756   1.00 13.15 ?  50  ALA   B H    1 
ATOM   4768 H HA   . ALA   B 1 50  ? 50.590 -21.840 1.055   1.00 12.99 ?  50  ALA   B HA   1 
ATOM   4769 H HB1  . ALA   B 1 50  ? 50.567 -21.325 3.329   1.00 13.72 ?  50  ALA   B HB1  1 
ATOM   4770 H HB2  . ALA   B 1 50  ? 49.245 -22.110 2.929   1.00 13.72 ?  50  ALA   B HB2  1 
ATOM   4771 H HB3  . ALA   B 1 50  ? 50.424 -22.869 3.675   1.00 13.72 ?  50  ALA   B HB3  1 
ATOM   4772 N N    . GLY   B 1 51  ? 52.898 -23.654 2.317   1.00 11.54 ?  51  GLY   B N    1 
ATOM   4773 C CA   . GLY   B 1 51  ? 54.340 -23.761 2.386   1.00 12.19 ?  51  GLY   B CA   1 
ATOM   4774 C C    . GLY   B 1 51  ? 54.980 -23.711 1.015   1.00 11.66 ?  51  GLY   B C    1 
ATOM   4775 O O    . GLY   B 1 51  ? 56.020 -23.074 0.831   1.00 12.66 ?  51  GLY   B O    1 
ATOM   4776 H H    . GLY   B 1 51  ? 52.469 -24.330 2.631   1.00 13.84 ?  51  GLY   B H    1 
ATOM   4777 H HA2  . GLY   B 1 51  ? 54.695 -23.031 2.917   1.00 14.62 ?  51  GLY   B HA2  1 
ATOM   4778 H HA3  . GLY   B 1 51  ? 54.584 -24.599 2.812   1.00 14.62 ?  51  GLY   B HA3  1 
ATOM   4779 N N    . ALA   B 1 52  ? 54.377 -24.380 0.036   1.00 11.37 ?  52  ALA   B N    1 
ATOM   4780 C CA   . ALA   B 1 52  ? 54.939 -24.388 -1.308  1.00 11.84 ?  52  ALA   B CA   1 
ATOM   4781 C C    . ALA   B 1 52  ? 54.851 -23.012 -1.963  1.00 11.38 ?  52  ALA   B C    1 
ATOM   4782 O O    . ALA   B 1 52  ? 55.816 -22.555 -2.595  1.00 12.37 ?  52  ALA   B O    1 
ATOM   4783 C CB   . ALA   B 1 52  ? 54.248 -25.447 -2.162  1.00 12.92 ?  52  ALA   B CB   1 
ATOM   4784 H H    . ALA   B 1 52  ? 53.644 -24.829 0.121   1.00 13.64 ?  52  ALA   B H    1 
ATOM   4785 H HA   . ALA   B 1 52  ? 55.876 -24.624 -1.247  1.00 14.20 ?  52  ALA   B HA   1 
ATOM   4786 H HB1  . ALA   B 1 52  ? 54.642 -25.439 -3.053  1.00 15.50 ?  52  ALA   B HB1  1 
ATOM   4787 H HB2  . ALA   B 1 52  ? 54.388 -26.320 -1.755  1.00 15.50 ?  52  ALA   B HB2  1 
ATOM   4788 H HB3  . ALA   B 1 52  ? 53.305 -25.253 -2.215  1.00 15.50 ?  52  ALA   B HB3  1 
ATOM   4789 N N    . LEU   B 1 53  ? 53.709 -22.336 -1.838  1.00 11.18 ?  53  LEU   B N    1 
ATOM   4790 C CA   . LEU   B 1 53  ? 53.599 -20.999 -2.411  1.00 11.23 ?  53  LEU   B CA   1 
ATOM   4791 C C    . LEU   B 1 53  ? 54.607 -20.058 -1.767  1.00 11.09 ?  53  LEU   B C    1 
ATOM   4792 O O    . LEU   B 1 53  ? 55.303 -19.305 -2.457  1.00 11.77 ?  53  LEU   B O    1 
ATOM   4793 C CB   . LEU   B 1 53  ? 52.177 -20.456 -2.239  1.00 11.74 ?  53  LEU   B CB   1 
ATOM   4794 C CG   . LEU   B 1 53  ? 51.043 -21.180 -2.979  1.00 12.01 ?  53  LEU   B CG   1 
ATOM   4795 C CD1  . LEU   B 1 53  ? 49.706 -20.578 -2.614  1.00 13.75 ?  53  LEU   B CD1  1 
ATOM   4796 C CD2  . LEU   B 1 53  ? 51.233 -21.157 -4.490  1.00 13.98 ?  53  LEU   B CD2  1 
ATOM   4797 H H    . LEU   B 1 53  ? 53.005 -22.620 -1.440  1.00 13.42 ?  53  LEU   B H    1 
ATOM   4798 H HA   . LEU   B 1 53  ? 53.794 -21.043 -3.364  1.00 13.47 ?  53  LEU   B HA   1 
ATOM   4799 H HB2  . LEU   B 1 53  ? 51.959 -20.484 -1.298  1.00 14.08 ?  53  LEU   B HB2  1 
ATOM   4800 H HB3  . LEU   B 1 53  ? 52.168 -19.537 -2.545  1.00 14.08 ?  53  LEU   B HB3  1 
ATOM   4801 H HG   . LEU   B 1 53  ? 51.028 -22.108 -2.700  1.00 14.41 ?  53  LEU   B HG   1 
ATOM   4802 H HD11 . LEU   B 1 53  ? 49.001 -21.054 -3.087  1.00 16.49 ?  53  LEU   B HD11 1 
ATOM   4803 H HD12 . LEU   B 1 53  ? 49.569 -20.668 -1.654  1.00 16.49 ?  53  LEU   B HD12 1 
ATOM   4804 H HD13 . LEU   B 1 53  ? 49.696 -19.643 -2.861  1.00 16.49 ?  53  LEU   B HD13 1 
ATOM   4805 H HD21 . LEU   B 1 53  ? 50.521 -21.667 -4.908  1.00 16.77 ?  53  LEU   B HD21 1 
ATOM   4806 H HD22 . LEU   B 1 53  ? 51.202 -20.237 -4.799  1.00 16.77 ?  53  LEU   B HD22 1 
ATOM   4807 H HD23 . LEU   B 1 53  ? 52.091 -21.551 -4.708  1.00 16.77 ?  53  LEU   B HD23 1 
ATOM   4808 N N    . ASN   B 1 54  ? 54.697 -20.083 -0.439  1.00 10.95 ?  54  ASN   B N    1 
ATOM   4809 C CA   . ASN   B 1 54  ? 55.612 -19.171 0.231   1.00 11.56 ?  54  ASN   B CA   1 
ATOM   4810 C C    . ASN   B 1 54  ? 57.054 -19.448 -0.172  1.00 11.93 ?  54  ASN   B C    1 
ATOM   4811 O O    . ASN   B 1 54  ? 57.830 -18.512 -0.409  1.00 12.37 ?  54  ASN   B O    1 
ATOM   4812 C CB   . ASN   B 1 54  ? 55.460 -19.256 1.740   1.00 12.31 ?  54  ASN   B CB   1 
ATOM   4813 C CG   . ASN   B 1 54  ? 56.432 -18.336 2.445   1.00 12.36 ?  54  ASN   B CG   1 
ATOM   4814 O OD1  . ASN   B 1 54  ? 56.445 -17.127 2.197   1.00 12.55 ?  54  ASN   B OD1  1 
ATOM   4815 N ND2  . ASN   B 1 54  ? 57.274 -18.899 3.298   1.00 14.32 ?  54  ASN   B ND2  1 
ATOM   4816 H H    . ASN   B 1 54  ? 54.255 -20.606 0.078   1.00 13.14 ?  54  ASN   B H    1 
ATOM   4817 H HA   . ASN   B 1 54  ? 55.398 -18.265 -0.041  1.00 13.86 ?  54  ASN   B HA   1 
ATOM   4818 H HB2  . ASN   B 1 54  ? 54.560 -18.992 1.985   1.00 14.77 ?  54  ASN   B HB2  1 
ATOM   4819 H HB3  . ASN   B 1 54  ? 55.638 -20.162 2.028   1.00 14.77 ?  54  ASN   B HB3  1 
ATOM   4820 H HD21 . ASN   B 1 54  ? 57.853 -18.417 3.721   1.00 17.18 ?  54  ASN   B HD21 1 
ATOM   4821 H HD22 . ASN   B 1 54  ? 57.246 -19.748 3.438   1.00 17.18 ?  54  ASN   B HD22 1 
ATOM   4822 N N    . LYS   B 1 55  ? 57.438 -20.724 -0.237  1.00 12.48 ?  55  LYS   B N    1 
ATOM   4823 C CA   . LYS   B 1 55  ? 58.792 -21.066 -0.656  1.00 13.27 ?  55  LYS   B CA   1 
ATOM   4824 C C    . LYS   B 1 55  ? 59.086 -20.528 -2.051  1.00 13.04 ?  55  LYS   B C    1 
ATOM   4825 O O    . LYS   B 1 55  ? 60.186 -20.027 -2.308  1.00 13.83 ?  55  LYS   B O    1 
ATOM   4826 C CB   . LYS   B 1 55  ? 58.981 -22.584 -0.605  1.00 14.94 ?  55  LYS   B CB   1 
ATOM   4827 C CG   . LYS   B 1 55  ? 60.344 -23.060 -1.055  1.00 19.31 ?  55  LYS   B CG   1 
ATOM   4828 C CD   . LYS   B 1 55  ? 60.495 -24.560 -0.876  1.00 22.87 ?  55  LYS   B CD   1 
ATOM   4829 C CE   . LYS   B 1 55  ? 60.577 -24.940 0.599   1.00 26.23 ?  55  LYS   B CE   1 
ATOM   4830 N NZ   . LYS   B 1 55  ? 61.017 -26.341 0.788   1.00 27.76 ?  55  LYS   B NZ   1 
ATOM   4831 H H    . LYS   B 1 55  ? 56.938 -21.396 -0.049  1.00 14.97 ?  55  LYS   B H    1 
ATOM   4832 H HA   . LYS   B 1 55  ? 59.423 -20.664 -0.041  1.00 15.92 ?  55  LYS   B HA   1 
ATOM   4833 H HB2  . LYS   B 1 55  ? 58.850 -22.878 0.311   1.00 17.93 ?  55  LYS   B HB2  1 
ATOM   4834 H HB3  . LYS   B 1 55  ? 58.320 -23.001 -1.178  1.00 17.93 ?  55  LYS   B HB3  1 
ATOM   4835 H HG2  . LYS   B 1 55  ? 60.465 -22.858 -1.996  1.00 23.17 ?  55  LYS   B HG2  1 
ATOM   4836 H HG3  . LYS   B 1 55  ? 61.030 -22.623 -0.526  1.00 23.17 ?  55  LYS   B HG3  1 
ATOM   4837 H HD2  . LYS   B 1 55  ? 59.724 -25.010 -1.261  1.00 27.44 ?  55  LYS   B HD2  1 
ATOM   4838 H HD3  . LYS   B 1 55  ? 61.309 -24.860 -1.311  1.00 27.44 ?  55  LYS   B HD3  1 
ATOM   4839 H HE2  . LYS   B 1 55  ? 61.215 -24.352 1.039   1.00 31.47 ?  55  LYS   B HE2  1 
ATOM   4840 H HE3  . LYS   B 1 55  ? 59.699 -24.835 1.002   1.00 31.47 ?  55  LYS   B HE3  1 
ATOM   4841 H HZ1  . LYS   B 1 55  ? 61.004 -26.546 1.653   1.00 33.31 ?  55  LYS   B HZ1  1 
ATOM   4842 H HZ2  . LYS   B 1 55  ? 60.469 -26.888 0.351   1.00 33.31 ?  55  LYS   B HZ2  1 
ATOM   4843 H HZ3  . LYS   B 1 55  ? 61.842 -26.443 0.475   1.00 33.31 ?  55  LYS   B HZ3  1 
ATOM   4844 N N    . ALA   B 1 56  ? 58.117 -20.620 -2.968  1.00 12.33 ?  56  ALA   B N    1 
ATOM   4845 C CA   . ALA   B 1 56  ? 58.335 -20.118 -4.321  1.00 13.11 ?  56  ALA   B CA   1 
ATOM   4846 C C    . ALA   B 1 56  ? 58.604 -18.619 -4.321  1.00 13.11 ?  56  ALA   B C    1 
ATOM   4847 O O    . ALA   B 1 56  ? 59.332 -18.119 -5.192  1.00 14.17 ?  56  ALA   B O    1 
ATOM   4848 C CB   . ALA   B 1 56  ? 57.133 -20.454 -5.204  1.00 14.48 ?  56  ALA   B CB   1 
ATOM   4849 H H    . ALA   B 1 56  ? 57.336 -20.954 -2.830  1.00 14.79 ?  56  ALA   B H    1 
ATOM   4850 H HA   . ALA   B 1 56  ? 59.114 -20.555 -4.692  1.00 15.74 ?  56  ALA   B HA   1 
ATOM   4851 H HB1  . ALA   B 1 56  ? 57.302 -20.122 -6.102  1.00 17.37 ?  56  ALA   B HB1  1 
ATOM   4852 H HB2  . ALA   B 1 56  ? 57.020 -21.417 -5.226  1.00 17.37 ?  56  ALA   B HB2  1 
ATOM   4853 H HB3  . ALA   B 1 56  ? 56.342 -20.034 -4.839  1.00 17.37 ?  56  ALA   B HB3  1 
ATOM   4854 N N    . THR   B 1 57  ? 58.038 -17.891 -3.355  1.00 12.99 ?  57  THR   B N    1 
ATOM   4855 C CA   . THR   B 1 57  ? 58.273 -16.457 -3.228  1.00 13.02 ?  57  THR   B CA   1 
ATOM   4856 C C    . THR   B 1 57  ? 59.524 -16.128 -2.420  1.00 13.84 ?  57  THR   B C    1 
ATOM   4857 O O    . THR   B 1 57  ? 59.761 -14.949 -2.119  1.00 14.42 ?  57  THR   B O    1 
ATOM   4858 C CB   . THR   B 1 57  ? 57.078 -15.728 -2.587  1.00 12.31 ?  57  THR   B CB   1 
ATOM   4859 O OG1  . THR   B 1 57  ? 57.063 -15.942 -1.169  1.00 12.95 ?  57  THR   B OG1  1 
ATOM   4860 C CG2  . THR   B 1 57  ? 55.762 -16.148 -3.212  1.00 12.43 ?  57  THR   B CG2  1 
ATOM   4861 H H    . THR   B 1 57  ? 57.499 -18.209 -2.758  1.00 15.59 ?  57  THR   B H    1 
ATOM   4862 H HA   . THR   B 1 57  ? 58.391 -16.089 -4.116  1.00 15.63 ?  57  THR   B HA   1 
ATOM   4863 H HB   . THR   B 1 57  ? 57.179 -14.779 -2.751  1.00 14.77 ?  57  THR   B HB   1 
ATOM   4864 H HG1  . THR   B 1 57  ? 56.996 -16.765 -1.004  1.00 15.53 ?  57  THR   B HG1  1 
ATOM   4865 H HG21 . THR   B 1 57  ? 55.039 -15.603 -2.871  1.00 14.91 ?  57  THR   B HG21 1 
ATOM   4866 H HG22 . THR   B 1 57  ? 55.803 -16.056 -4.176  1.00 14.91 ?  57  THR   B HG22 1 
ATOM   4867 H HG23 . THR   B 1 57  ? 55.575 -17.080 -2.999  1.00 14.91 ?  57  THR   B HG23 1 
ATOM   4868 N N    . ASN   B 1 58  ? 60.325 -17.128 -2.060  1.00 14.42 ?  58  ASN   B N    1 
ATOM   4869 C CA   . ASN   B 1 58  ? 61.527 -16.900 -1.262  1.00 17.29 ?  58  ASN   B CA   1 
ATOM   4870 C C    . ASN   B 1 58  ? 61.190 -16.192 0.051   1.00 15.31 ?  58  ASN   B C    1 
ATOM   4871 O O    . ASN   B 1 58  ? 61.928 -15.321 0.518   1.00 15.94 ?  58  ASN   B O    1 
ATOM   4872 C CB   . ASN   B 1 58  ? 62.600 -16.143 -2.052  1.00 26.01 ?  58  ASN   B CB   1 
ATOM   4873 C CG   . ASN   B 1 58  ? 63.973 -16.251 -1.418  1.00 36.23 ?  58  ASN   B CG   1 
ATOM   4874 O OD1  . ASN   B 1 58  ? 64.281 -17.233 -0.743  1.00 38.59 ?  58  ASN   B OD1  1 
ATOM   4875 N ND2  . ASN   B 1 58  ? 64.806 -15.239 -1.631  1.00 41.88 ?  58  ASN   B ND2  1 
ATOM   4876 H H    . ASN   B 1 58  ? 60.196 -17.956 -2.267  1.00 17.30 ?  58  ASN   B H    1 
ATOM   4877 H HA   . ASN   B 1 58  ? 61.903 -17.766 -1.037  1.00 20.74 ?  58  ASN   B HA   1 
ATOM   4878 H HB2  . ASN   B 1 58  ? 62.655 -16.510 -2.951  1.00 31.21 ?  58  ASN   B HB2  1 
ATOM   4879 H HB3  . ASN   B 1 58  ? 62.365 -15.204 -2.092  1.00 31.21 ?  58  ASN   B HB3  1 
ATOM   4880 H HD21 . ASN   B 1 58  ? 65.598 -15.254 -1.293  1.00 50.26 ?  58  ASN   B HD21 1 
ATOM   4881 H HD22 . ASN   B 1 58  ? 64.555 -14.568 -2.106  1.00 50.26 ?  58  ASN   B HD22 1 
ATOM   4882 N N    . ASN   B 1 59  ? 60.065 -16.576 0.655   1.00 14.24 ?  59  ASN   B N    1 
ATOM   4883 C CA   . ASN   B 1 59  ? 59.589 -16.101 1.958   1.00 14.42 ?  59  ASN   B CA   1 
ATOM   4884 C C    . ASN   B 1 59  ? 58.994 -14.694 1.900   1.00 13.76 ?  59  ASN   B C    1 
ATOM   4885 O O    . ASN   B 1 59  ? 58.565 -14.184 2.947   1.00 14.04 ?  59  ASN   B O    1 
ATOM   4886 C CB   . ASN   B 1 59  ? 60.660 -16.163 3.063   1.00 15.33 ?  59  ASN   B CB   1 
ATOM   4887 C CG   . ASN   B 1 59  ? 60.074 -16.336 4.443   1.00 16.52 ?  59  ASN   B CG   1 
ATOM   4888 O OD1  . ASN   B 1 59  ? 59.252 -17.227 4.670   1.00 16.51 ?  59  ASN   B OD1  1 
ATOM   4889 N ND2  . ASN   B 1 59  ? 60.485 -15.481 5.377   1.00 17.30 ?  59  ASN   B ND2  1 
ATOM   4890 H H    . ASN   B 1 59  ? 59.526 -17.155 0.308   1.00 17.09 ?  59  ASN   B H    1 
ATOM   4891 H HA   . ASN   B 1 59  ? 58.878 -16.695 2.234   1.00 17.31 ?  59  ASN   B HA   1 
ATOM   4892 H HB2  . ASN   B 1 59  ? 61.245 -16.919 2.903   1.00 18.39 ?  59  ASN   B HB2  1 
ATOM   4893 H HB3  . ASN   B 1 59  ? 61.169 -15.340 3.062   1.00 18.39 ?  59  ASN   B HB3  1 
ATOM   4894 H HD21 . ASN   B 1 59  ? 60.172 -15.534 6.179   1.00 20.76 ?  59  ASN   B HD21 1 
ATOM   4895 H HD22 . ASN   B 1 59  ? 61.053 -14.869 5.179   1.00 20.76 ?  59  ASN   B HD22 1 
ATOM   4896 N N    . ALA   B 1 60  ? 58.934 -14.053 0.729   1.00 13.58 ?  60  ALA   B N    1 
ATOM   4897 C CA   . ALA   B 1 60  ? 58.339 -12.722 0.658   1.00 13.45 ?  60  ALA   B CA   1 
ATOM   4898 C C    . ALA   B 1 60  ? 56.871 -12.751 1.065   1.00 12.48 ?  60  ALA   B C    1 
ATOM   4899 O O    . ALA   B 1 60  ? 56.361 -11.798 1.673   1.00 13.10 ?  60  ALA   B O    1 
ATOM   4900 C CB   . ALA   B 1 60  ? 58.497 -12.141 -0.746  1.00 14.33 ?  60  ALA   B CB   1 
ATOM   4901 H H    . ALA   B 1 60  ? 59.226 -14.366 -0.020  1.00 16.29 ?  60  ALA   B H    1 
ATOM   4902 H HA   . ALA   B 1 60  ? 58.802 -12.142 1.277   1.00 16.14 ?  60  ALA   B HA   1 
ATOM   4903 H HB1  . ALA   B 1 60  ? 58.095 -11.260 -0.767  1.00 17.19 ?  60  ALA   B HB1  1 
ATOM   4904 H HB2  . ALA   B 1 60  ? 59.443 -12.080 -0.956  1.00 17.19 ?  60  ALA   B HB2  1 
ATOM   4905 H HB3  . ALA   B 1 60  ? 58.055 -12.724 -1.383  1.00 17.19 ?  60  ALA   B HB3  1 
ATOM   4906 N N    . MET   B 1 61  ? 56.168 -13.832 0.724   1.00 12.05 ?  61  MET   B N    1 
ATOM   4907 C CA   . MET   B 1 61  ? 54.770 -13.951 1.115   1.00 11.36 ?  61  MET   B CA   1 
ATOM   4908 C C    . MET   B 1 61  ? 54.632 -13.960 2.636   1.00 11.67 ?  61  MET   B C    1 
ATOM   4909 O O    . MET   B 1 61  ? 53.735 -13.311 3.191   1.00 11.66 ?  61  MET   B O    1 
ATOM   4910 C CB   . MET   B 1 61  ? 54.189 -15.217 0.485   1.00 11.40 ?  61  MET   B CB   1 
ATOM   4911 C CG   . MET   B 1 61  ? 52.744 -15.503 0.891   1.00 11.35 ?  61  MET   B CG   1 
ATOM   4912 S SD   . MET   B 1 61  ? 52.105 -17.019 0.138   1.00 12.07 ?  61  MET   B SD   1 
ATOM   4913 C CE   . MET   B 1 61  ? 51.837 -16.434 -1.533  1.00 13.15 ?  61  MET   B CE   1 
ATOM   4914 H H    . MET   B 1 61  ? 56.473 -14.508 0.279   1.00 14.46 ?  61  MET   B H    1 
ATOM   4915 H HA   . MET   B 1 61  ? 54.278 -13.196 0.752   1.00 13.63 ?  61  MET   B HA   1 
ATOM   4916 H HB2  . MET   B 1 61  ? 54.208 -15.129 -0.483  1.00 13.68 ?  61  MET   B HB2  1 
ATOM   4917 H HB3  . MET   B 1 61  ? 54.726 -15.979 0.753   1.00 13.68 ?  61  MET   B HB3  1 
ATOM   4918 H HG2  . MET   B 1 61  ? 52.694 -15.613 1.855   1.00 13.62 ?  61  MET   B HG2  1 
ATOM   4919 H HG3  . MET   B 1 61  ? 52.179 -14.766 0.611   1.00 13.62 ?  61  MET   B HG3  1 
ATOM   4920 H HE1  . MET   B 1 61  ? 51.458 -17.153 -2.065  1.00 15.78 ?  61  MET   B HE1  1 
ATOM   4921 H HE2  . MET   B 1 61  ? 51.219 -15.683 -1.512  1.00 15.78 ?  61  MET   B HE2  1 
ATOM   4922 H HE3  . MET   B 1 61  ? 52.683 -16.153 -1.911  1.00 15.78 ?  61  MET   B HE3  1 
ATOM   4923 N N    . GLN   B 1 62  ? 55.516 -14.677 3.332   1.00 11.89 ?  62  GLN   B N    1 
ATOM   4924 C CA   . GLN   B 1 62  ? 55.414 -14.737 4.786   1.00 12.25 ?  62  GLN   B CA   1 
ATOM   4925 C C    . GLN   B 1 62  ? 55.699 -13.381 5.418   1.00 12.23 ?  62  GLN   B C    1 
ATOM   4926 O O    . GLN   B 1 62  ? 55.017 -12.981 6.366   1.00 12.72 ?  62  GLN   B O    1 
ATOM   4927 C CB   . GLN   B 1 62  ? 56.366 -15.794 5.345   1.00 12.33 ?  62  GLN   B CB   1 
ATOM   4928 C CG   . GLN   B 1 62  ? 56.154 -16.053 6.825   1.00 12.61 ?  62  GLN   B CG   1 
ATOM   4929 C CD   . GLN   B 1 62  ? 54.778 -16.645 7.080   1.00 12.24 ?  62  GLN   B CD   1 
ATOM   4930 O OE1  . GLN   B 1 62  ? 54.518 -17.792 6.718   1.00 13.08 ?  62  GLN   B OE1  1 
ATOM   4931 N NE2  . GLN   B 1 62  ? 53.871 -15.850 7.648   1.00 12.91 ?  62  GLN   B NE2  1 
ATOM   4932 H H    . GLN   B 1 62  ? 56.164 -15.125 2.988   1.00 14.27 ?  62  GLN   B H    1 
ATOM   4933 H HA   . GLN   B 1 62  ? 54.506 -14.994 5.019   1.00 14.70 ?  62  GLN   B HA   1 
ATOM   4934 H HB2  . GLN   B 1 62  ? 56.229 -16.629 4.868   1.00 14.79 ?  62  GLN   B HB2  1 
ATOM   4935 H HB3  . GLN   B 1 62  ? 57.280 -15.490 5.218   1.00 14.79 ?  62  GLN   B HB3  1 
ATOM   4936 H HG2  . GLN   B 1 62  ? 56.820 -16.686 7.134   1.00 15.13 ?  62  GLN   B HG2  1 
ATOM   4937 H HG3  . GLN   B 1 62  ? 56.227 -15.220 7.312   1.00 15.13 ?  62  GLN   B HG3  1 
ATOM   4938 H HE21 . GLN   B 1 62  ? 54.085 -15.049 7.874   1.00 15.49 ?  62  GLN   B HE21 1 
ATOM   4939 H HE22 . GLN   B 1 62  ? 53.080 -16.146 7.804   1.00 15.49 ?  62  GLN   B HE22 1 
ATOM   4940 N N    . VAL   B 1 63  ? 56.708 -12.664 4.921   1.00 13.00 ?  63  VAL   B N    1 
ATOM   4941 C CA   . VAL   B 1 63  ? 57.017 -11.350 5.480   1.00 13.74 ?  63  VAL   B CA   1 
ATOM   4942 C C    . VAL   B 1 63  ? 55.827 -10.414 5.305   1.00 12.79 ?  63  VAL   B C    1 
ATOM   4943 O O    . VAL   B 1 63  ? 55.415 -9.715  6.241   1.00 13.53 ?  63  VAL   B O    1 
ATOM   4944 C CB   . VAL   B 1 63  ? 58.305 -10.788 4.855   1.00 15.42 ?  63  VAL   B CB   1 
ATOM   4945 C CG1  . VAL   B 1 63  ? 58.531 -9.356  5.318   1.00 15.87 ?  63  VAL   B CG1  1 
ATOM   4946 C CG2  . VAL   B 1 63  ? 59.495 -11.663 5.233   1.00 15.95 ?  63  VAL   B CG2  1 
ATOM   4947 H H    . VAL   B 1 63  ? 57.208 -12.910 4.264   1.00 15.59 ?  63  VAL   B H    1 
ATOM   4948 H HA   . VAL   B 1 63  ? 57.174 -11.456 6.429   1.00 16.49 ?  63  VAL   B HA   1 
ATOM   4949 H HB   . VAL   B 1 63  ? 58.228 -10.794 3.889   1.00 18.50 ?  63  VAL   B HB   1 
ATOM   4950 H HG11 . VAL   B 1 63  ? 59.451 -9.108  5.139   1.00 19.05 ?  63  VAL   B HG11 1 
ATOM   4951 H HG12 . VAL   B 1 63  ? 57.929 -8.771  4.837   1.00 19.05 ?  63  VAL   B HG12 1 
ATOM   4952 H HG13 . VAL   B 1 63  ? 58.356 -9.304  6.273   1.00 19.05 ?  63  VAL   B HG13 1 
ATOM   4953 H HG21 . VAL   B 1 63  ? 60.301 -11.284 4.845   1.00 19.14 ?  63  VAL   B HG21 1 
ATOM   4954 H HG22 . VAL   B 1 63  ? 59.576 -11.681 6.203   1.00 19.14 ?  63  VAL   B HG22 1 
ATOM   4955 H HG23 . VAL   B 1 63  ? 59.354 -12.558 4.897   1.00 19.14 ?  63  VAL   B HG23 1 
ATOM   4956 N N    . GLU   B 1 64  ? 55.249 -10.402 4.102   1.00 12.58 ?  64  GLU   B N    1 
ATOM   4957 C CA   . GLU   B 1 64  ? 54.087 -9.564  3.832   1.00 12.16 ?  64  GLU   B CA   1 
ATOM   4958 C C    . GLU   B 1 64  ? 52.907 -9.967  4.709   1.00 12.12 ?  64  GLU   B C    1 
ATOM   4959 O O    . GLU   B 1 64  ? 52.165 -9.110  5.216   1.00 12.55 ?  64  GLU   B O    1 
ATOM   4960 C CB   . GLU   B 1 64  ? 53.727 -9.713  2.353   1.00 12.48 ?  64  GLU   B CB   1 
ATOM   4961 C CG   . GLU   B 1 64  ? 52.471 -8.970  1.916   1.00 12.93 ?  64  GLU   B CG   1 
ATOM   4962 C CD   . GLU   B 1 64  ? 51.927 -9.478  0.587   1.00 13.69 ?  64  GLU   B CD   1 
ATOM   4963 O OE1  . GLU   B 1 64  ? 52.101 -10.686 0.272   1.00 14.39 ?  64  GLU   B OE1  1 
ATOM   4964 O OE2  . GLU   B 1 64  ? 51.299 -8.667  -0.134  1.00 14.21 -1 64  GLU   B OE2  1 
ATOM   4965 H H    . GLU   B 1 64  ? 55.513 -10.873 3.428   1.00 15.09 ?  64  GLU   B H    1 
ATOM   4966 H HA   . GLU   B 1 64  ? 54.303 -8.638  4.006   1.00 14.60 ?  64  GLU   B HA   1 
ATOM   4967 H HB2  . GLU   B 1 64  ? 54.458 -9.369  1.816   1.00 14.98 ?  64  GLU   B HB2  1 
ATOM   4968 H HB3  . GLU   B 1 64  ? 53.588 -10.649 2.157   1.00 14.98 ?  64  GLU   B HB3  1 
ATOM   4969 H HG2  . GLU   B 1 64  ? 51.771 -9.080  2.584   1.00 15.52 ?  64  GLU   B HG2  1 
ATOM   4970 H HG3  . GLU   B 1 64  ? 52.678 -8.025  1.818   1.00 15.52 ?  64  GLU   B HG3  1 
ATOM   4971 N N    . SER   B 1 65  ? 52.718 -11.277 4.882   1.00 11.90 ?  65  SER   B N    1 
ATOM   4972 C CA   . SER   B 1 65  ? 51.614 -11.784 5.686   1.00 12.03 ?  65  SER   B CA   1 
ATOM   4973 C C    . SER   B 1 65  ? 51.755 -11.386 7.148   1.00 12.08 ?  65  SER   B C    1 
ATOM   4974 O O    . SER   B 1 65  ? 50.762 -11.017 7.791   1.00 12.38 ?  65  SER   B O    1 
ATOM   4975 C CB   . SER   B 1 65  ? 51.548 -13.302 5.556   1.00 12.04 ?  65  SER   B CB   1 
ATOM   4976 O OG   . SER   B 1 65  ? 51.191 -13.699 4.240   1.00 12.18 ?  65  SER   B OG   1 
ATOM   4977 H H    . SER   B 1 65  ? 53.216 -11.896 4.542   1.00 14.27 ?  65  SER   B H    1 
ATOM   4978 H HA   . SER   B 1 65  ? 50.779 -11.419 5.352   1.00 14.44 ?  65  SER   B HA   1 
ATOM   4979 H HB2  . SER   B 1 65  ? 52.413 -13.678 5.769   1.00 14.44 ?  65  SER   B HB2  1 
ATOM   4980 H HB3  . SER   B 1 65  ? 50.878 -13.643 6.175   1.00 14.44 ?  65  SER   B HB3  1 
ATOM   4981 H HG   . SER   B 1 65  ? 51.755 -13.405 3.687   1.00 14.62 ?  65  SER   B HG   1 
ATOM   4982 N N    . ASP   B 1 66  ? 52.967 -11.484 7.706   1.00 12.46 ?  66  ASP   B N    1 
ATOM   4983 C CA   . ASP   B 1 66  ? 53.162 -11.096 9.100   1.00 12.66 ?  66  ASP   B CA   1 
ATOM   4984 C C    . ASP   B 1 66  ? 52.847 -9.619  9.306   1.00 12.98 ?  66  ASP   B C    1 
ATOM   4985 O O    . ASP   B 1 66  ? 52.268 -9.232  10.330  1.00 13.73 ?  66  ASP   B O    1 
ATOM   4986 C CB   . ASP   B 1 66  ? 54.594 -11.399 9.543   1.00 13.84 ?  66  ASP   B CB   1 
ATOM   4987 C CG   . ASP   B 1 66  ? 54.869 -12.888 9.692   1.00 15.87 ?  66  ASP   B CG   1 
ATOM   4988 O OD1  . ASP   B 1 66  ? 53.918 -13.701 9.634   1.00 16.51 ?  66  ASP   B OD1  1 
ATOM   4989 O OD2  . ASP   B 1 66  ? 56.053 -13.248 9.886   1.00 18.70 -1 66  ASP   B OD2  1 
ATOM   4990 H H    . ASP   B 1 66  ? 53.669 -11.778 7.312   1.00 14.95 ?  66  ASP   B H    1 
ATOM   4991 H HA   . ASP   B 1 66  ? 52.561 -11.602 9.667   1.00 15.19 ?  66  ASP   B HA   1 
ATOM   4992 H HB2  . ASP   B 1 66  ? 55.212 -11.046 8.885   1.00 16.61 ?  66  ASP   B HB2  1 
ATOM   4993 H HB3  . ASP   B 1 66  ? 54.756 -10.975 10.406  1.00 16.61 ?  66  ASP   B HB3  1 
ATOM   4994 N N    . ASP   B 1 67  ? 53.224 -8.772  8.345   1.00 12.59 ?  67  ASP   B N    1 
ATOM   4995 C CA   . ASP   B 1 67  ? 52.875 -7.362  8.436   1.00 13.15 ?  67  ASP   B CA   1 
ATOM   4996 C C    . ASP   B 1 67  ? 51.362 -7.160  8.363   1.00 13.32 ?  67  ASP   B C    1 
ATOM   4997 O O    . ASP   B 1 67  ? 50.801 -6.357  9.117   1.00 13.65 ?  67  ASP   B O    1 
ATOM   4998 C CB   . ASP   B 1 67  ? 53.580 -6.588  7.329   1.00 14.36 ?  67  ASP   B CB   1 
ATOM   4999 C CG   . ASP   B 1 67  ? 53.146 -5.146  7.285   1.00 15.64 ?  67  ASP   B CG   1 
ATOM   5000 O OD1  . ASP   B 1 67  ? 53.645 -4.326  8.091   1.00 16.74 ?  67  ASP   B OD1  1 
ATOM   5001 O OD2  . ASP   B 1 67  ? 52.268 -4.854  6.457   1.00 16.97 -1 67  ASP   B OD2  1 
ATOM   5002 H H    . ASP   B 1 67  ? 53.684 -8.988  7.647   1.00 15.11 ?  67  ASP   B H    1 
ATOM   5003 H HA   . ASP   B 1 67  ? 53.187 -7.009  9.283   1.00 15.78 ?  67  ASP   B HA   1 
ATOM   5004 H HB2  . ASP   B 1 67  ? 54.540 -6.606  7.480   1.00 17.23 ?  67  ASP   B HB2  1 
ATOM   5005 H HB3  . ASP   B 1 67  ? 53.378 -7.002  6.469   1.00 17.23 ?  67  ASP   B HB3  1 
ATOM   5006 N N    . TYR   B 1 68  ? 50.684 -7.888  7.467   1.00 12.72 ?  68  TYR   B N    1 
ATOM   5007 C CA   . TYR   B 1 68  ? 49.227 -7.816  7.394   1.00 13.49 ?  68  TYR   B CA   1 
ATOM   5008 C C    . TYR   B 1 68  ? 48.598 -8.158  8.742   1.00 13.26 ?  68  TYR   B C    1 
ATOM   5009 O O    . TYR   B 1 68  ? 47.675 -7.473  9.200   1.00 13.82 ?  68  TYR   B O    1 
ATOM   5010 C CB   . TYR   B 1 68  ? 48.695 -8.741  6.289   1.00 14.05 ?  68  TYR   B CB   1 
ATOM   5011 C CG   . TYR   B 1 68  ? 47.190 -8.889  6.346   1.00 15.25 ?  68  TYR   B CG   1 
ATOM   5012 C CD1  . TYR   B 1 68  ? 46.599 -9.837  7.175   1.00 16.33 ?  68  TYR   B CD1  1 
ATOM   5013 C CD2  . TYR   B 1 68  ? 46.362 -8.053  5.616   1.00 16.47 ?  68  TYR   B CD2  1 
ATOM   5014 C CE1  . TYR   B 1 68  ? 45.236 -9.953  7.271   1.00 17.43 ?  68  TYR   B CE1  1 
ATOM   5015 C CE2  . TYR   B 1 68  ? 44.976 -8.175  5.697   1.00 16.76 ?  68  TYR   B CE2  1 
ATOM   5016 C CZ   . TYR   B 1 68  ? 44.434 -9.125  6.529   1.00 17.10 ?  68  TYR   B CZ   1 
ATOM   5017 O OH   . TYR   B 1 68  ? 43.067 -9.241  6.627   1.00 18.41 ?  68  TYR   B OH   1 
ATOM   5018 H H    . TYR   B 1 68  ? 51.047 -8.436  6.903   1.00 15.26 ?  68  TYR   B H    1 
ATOM   5019 H HA   . TYR   B 1 68  ? 48.980 -6.911  7.173   1.00 16.19 ?  68  TYR   B HA   1 
ATOM   5020 H HB2  . TYR   B 1 68  ? 48.929 -8.367  5.427   1.00 16.86 ?  68  TYR   B HB2  1 
ATOM   5021 H HB3  . TYR   B 1 68  ? 49.091 -9.621  6.392   1.00 16.86 ?  68  TYR   B HB3  1 
ATOM   5022 H HD1  . TYR   B 1 68  ? 47.140 -10.404 7.683   1.00 19.59 ?  68  TYR   B HD1  1 
ATOM   5023 H HD2  . TYR   B 1 68  ? 46.739 -7.403  5.069   1.00 19.76 ?  68  TYR   B HD2  1 
ATOM   5024 H HE1  . TYR   B 1 68  ? 44.856 -10.607 7.819   1.00 20.92 ?  68  TYR   B HE1  1 
ATOM   5025 H HE2  . TYR   B 1 68  ? 44.424 -7.610  5.206   1.00 20.11 ?  68  TYR   B HE2  1 
ATOM   5026 H HH   . TYR   B 1 68  ? 42.682 -8.689  6.117   1.00 22.09 ?  68  TYR   B HH   1 
ATOM   5027 N N    . ILE   B 1 69  ? 49.075 -9.233  9.382   1.00 13.12 ?  69  ILE   B N    1 
ATOM   5028 C CA   . ILE   B 1 69  ? 48.523 -9.660  10.668  1.00 13.65 ?  69  ILE   B CA   1 
ATOM   5029 C C    . ILE   B 1 69  ? 48.777 -8.613  11.744  1.00 13.36 ?  69  ILE   B C    1 
ATOM   5030 O O    . ILE   B 1 69  ? 47.909 -8.333  12.577  1.00 13.77 ?  69  ILE   B O    1 
ATOM   5031 C CB   . ILE   B 1 69  ? 49.100 -11.034 11.063  1.00 14.38 ?  69  ILE   B CB   1 
ATOM   5032 C CG1  . ILE   B 1 69  ? 48.572 -12.136 10.137  1.00 14.83 ?  69  ILE   B CG1  1 
ATOM   5033 C CG2  . ILE   B 1 69  ? 48.800 -11.355 12.520  1.00 15.40 ?  69  ILE   B CG2  1 
ATOM   5034 C CD1  . ILE   B 1 69  ? 47.097 -12.442 10.302  1.00 15.31 ?  69  ILE   B CD1  1 
ATOM   5035 H H    . ILE   B 1 69  ? 49.717 -9.727  9.098   1.00 15.74 ?  69  ILE   B H    1 
ATOM   5036 H HA   . ILE   B 1 69  ? 47.566 -9.757  10.578  1.00 16.38 ?  69  ILE   B HA   1 
ATOM   5037 H HB   . ILE   B 1 69  ? 50.065 -10.997 10.963  1.00 17.25 ?  69  ILE   B HB   1 
ATOM   5038 H HG12 . ILE   B 1 69  ? 48.716 -11.860 9.217   1.00 17.79 ?  69  ILE   B HG12 1 
ATOM   5039 H HG13 . ILE   B 1 69  ? 49.066 -12.953 10.312  1.00 17.79 ?  69  ILE   B HG13 1 
ATOM   5040 H HG21 . ILE   B 1 69  ? 48.945 -12.303 12.669  1.00 18.47 ?  69  ILE   B HG21 1 
ATOM   5041 H HG22 . ILE   B 1 69  ? 49.391 -10.840 13.091  1.00 18.47 ?  69  ILE   B HG22 1 
ATOM   5042 H HG23 . ILE   B 1 69  ? 47.874 -11.131 12.709  1.00 18.47 ?  69  ILE   B HG23 1 
ATOM   5043 H HD11 . ILE   B 1 69  ? 46.854 -13.145 9.678   1.00 18.37 ?  69  ILE   B HD11 1 
ATOM   5044 H HD12 . ILE   B 1 69  ? 46.933 -12.742 11.210  1.00 18.37 ?  69  ILE   B HD12 1 
ATOM   5045 H HD13 . ILE   B 1 69  ? 46.581 -11.645 10.116  1.00 18.37 ?  69  ILE   B HD13 1 
ATOM   5046 N N    . ALA   B 1 70  ? 49.969 -8.024  11.760  1.00 13.34 ?  70  ALA   B N    1 
ATOM   5047 C CA   . ALA   B 1 70  ? 50.253 -6.993  12.752  1.00 13.28 ?  70  ALA   B CA   1 
ATOM   5048 C C    . ALA   B 1 70  ? 49.265 -5.843  12.644  1.00 13.40 ?  70  ALA   B C    1 
ATOM   5049 O O    . ALA   B 1 70  ? 48.837 -5.287  13.661  1.00 14.07 ?  70  ALA   B O    1 
ATOM   5050 C CB   . ALA   B 1 70  ? 51.683 -6.484  12.584  1.00 13.85 ?  70  ALA   B CB   1 
ATOM   5051 H H    . ALA   B 1 70  ? 50.611 -8.197  11.224  1.00 16.00 ?  70  ALA   B H    1 
ATOM   5052 H HA   . ALA   B 1 70  ? 50.175 -7.373  13.643  1.00 15.93 ?  70  ALA   B HA   1 
ATOM   5053 H HB1  . ALA   B 1 70  ? 51.869 -5.819  13.268  1.00 16.62 ?  70  ALA   B HB1  1 
ATOM   5054 H HB2  . ALA   B 1 70  ? 52.299 -7.229  12.679  1.00 16.62 ?  70  ALA   B HB2  1 
ATOM   5055 H HB3  . ALA   B 1 70  ? 51.779 -6.088  11.704  1.00 16.62 ?  70  ALA   B HB3  1 
ATOM   5056 N N    . THR   B 1 71  ? 48.885 -5.479  11.420  1.00 14.05 ?  71  THR   B N    1 
ATOM   5057 C CA   . THR   B 1 71  ? 48.000 -4.340  11.205  1.00 14.63 ?  71  THR   B CA   1 
ATOM   5058 C C    . THR   B 1 71  ? 46.531 -4.699  11.412  1.00 15.63 ?  71  THR   B C    1 
ATOM   5059 O O    . THR   B 1 71  ? 45.755 -3.877  11.921  1.00 17.34 ?  71  THR   B O    1 
ATOM   5060 C CB   . THR   B 1 71  ? 48.231 -3.778  9.798   1.00 16.81 ?  71  THR   B CB   1 
ATOM   5061 O OG1  . THR   B 1 71  ? 49.561 -3.254  9.706   1.00 19.21 ?  71  THR   B OG1  1 
ATOM   5062 C CG2  . THR   B 1 71  ? 47.228 -2.682  9.466   1.00 18.04 ?  71  THR   B CG2  1 
ATOM   5063 H H    . THR   B 1 71  ? 49.132 -5.878  10.699  1.00 16.86 ?  71  THR   B H    1 
ATOM   5064 H HA   . THR   B 1 71  ? 48.225 -3.647  11.837  1.00 17.55 ?  71  THR   B HA   1 
ATOM   5065 H HB   . THR   B 1 71  ? 48.133 -4.486  9.142   1.00 20.16 ?  71  THR   B HB   1 
ATOM   5066 H HG1  . THR   B 1 71  ? 49.698 -2.927  8.941   1.00 23.05 ?  71  THR   B HG1  1 
ATOM   5067 H HG21 . THR   B 1 71  ? 47.533 -2.174  8.695   1.00 21.65 ?  71  THR   B HG21 1 
ATOM   5068 H HG22 . THR   B 1 71  ? 46.364 -3.068  9.263   1.00 21.65 ?  71  THR   B HG22 1 
ATOM   5069 H HG23 . THR   B 1 71  ? 47.137 -2.075  10.219  1.00 21.65 ?  71  THR   B HG23 1 
ATOM   5070 N N    . ASN   B 1 72  ? 46.128 -5.914  11.025  1.00 15.16 ?  72  ASN   B N    1 
ATOM   5071 C CA   . ASN   B 1 72  ? 44.721 -6.273  10.911  1.00 15.78 ?  72  ASN   B CA   1 
ATOM   5072 C C    . ASN   B 1 72  ? 44.259 -7.374  11.854  1.00 16.44 ?  72  ASN   B C    1 
ATOM   5073 O O    . ASN   B 1 72  ? 43.043 -7.541  12.021  1.00 17.84 ?  72  ASN   B O    1 
ATOM   5074 C CB   . ASN   B 1 72  ? 44.406 -6.702  9.471   1.00 16.59 ?  72  ASN   B CB   1 
ATOM   5075 C CG   . ASN   B 1 72  ? 44.681 -5.603  8.477   1.00 17.44 ?  72  ASN   B CG   1 
ATOM   5076 O OD1  . ASN   B 1 72  ? 45.692 -5.616  7.766   1.00 18.85 ?  72  ASN   B OD1  1 
ATOM   5077 N ND2  . ASN   B 1 72  ? 43.808 -4.615  8.453   1.00 19.30 ?  72  ASN   B ND2  1 
ATOM   5078 H H    . ASN   B 1 72  ? 46.663 -6.562  10.820  1.00 18.18 ?  72  ASN   B H    1 
ATOM   5079 H HA   . ASN   B 1 72  ? 44.188 -5.488  11.104  1.00 18.94 ?  72  ASN   B HA   1 
ATOM   5080 H HB2  . ASN   B 1 72  ? 44.958 -7.466  9.239   1.00 19.91 ?  72  ASN   B HB2  1 
ATOM   5081 H HB3  . ASN   B 1 72  ? 43.466 -6.941  9.410   1.00 19.91 ?  72  ASN   B HB3  1 
ATOM   5082 H HD21 . ASN   B 1 72  ? 43.913 -3.959  7.908   1.00 23.16 ?  72  ASN   B HD21 1 
ATOM   5083 H HD22 . ASN   B 1 72  ? 43.117 -4.633  8.971   1.00 23.16 ?  72  ASN   B HD22 1 
ATOM   5084 N N    . GLY   B 1 73  ? 45.167 -8.121  12.474  1.00 15.77 ?  73  GLY   B N    1 
ATOM   5085 C CA   . GLY   B 1 73  ? 44.779 -9.269  13.257  1.00 15.48 ?  73  GLY   B CA   1 
ATOM   5086 C C    . GLY   B 1 73  ? 44.397 -10.443 12.382  1.00 13.82 ?  73  GLY   B C    1 
ATOM   5087 O O    . GLY   B 1 73  ? 44.379 -10.353 11.152  1.00 13.77 ?  73  GLY   B O    1 
ATOM   5088 H H    . GLY   B 1 73  ? 46.018 -7.976  12.456  1.00 18.93 ?  73  GLY   B H    1 
ATOM   5089 H HA2  . GLY   B 1 73  ? 45.517 -9.531  13.833  1.00 18.57 ?  73  GLY   B HA2  1 
ATOM   5090 H HA3  . GLY   B 1 73  ? 44.021 -9.037  13.817  1.00 18.57 ?  73  GLY   B HA3  1 
ATOM   5091 N N    . PRO   B 1 74  ? 44.087 -11.569 13.017  1.00 14.26 ?  74  PRO   B N    1 
ATOM   5092 C CA   . PRO   B 1 74  ? 43.834 -12.798 12.268  1.00 13.65 ?  74  PRO   B CA   1 
ATOM   5093 C C    . PRO   B 1 74  ? 42.537 -12.733 11.477  1.00 13.20 ?  74  PRO   B C    1 
ATOM   5094 O O    . PRO   B 1 74  ? 41.595 -12.002 11.802  1.00 14.21 ?  74  PRO   B O    1 
ATOM   5095 C CB   . PRO   B 1 74  ? 43.753 -13.865 13.367  1.00 14.26 ?  74  PRO   B CB   1 
ATOM   5096 C CG   . PRO   B 1 74  ? 43.310 -13.121 14.577  1.00 15.94 ?  74  PRO   B CG   1 
ATOM   5097 C CD   . PRO   B 1 74  ? 43.980 -11.782 14.471  1.00 15.51 ?  74  PRO   B CD   1 
ATOM   5098 H HA   . PRO   B 1 74  ? 44.578 -12.994 11.672  1.00 16.38 ?  74  PRO   B HA   1 
ATOM   5099 H HB2  . PRO   B 1 74  ? 43.103 -14.541 13.116  1.00 17.11 ?  74  PRO   B HB2  1 
ATOM   5100 H HB3  . PRO   B 1 74  ? 44.628 -14.263 13.504  1.00 17.11 ?  74  PRO   B HB3  1 
ATOM   5101 H HG2  . PRO   B 1 74  ? 42.344 -13.023 14.565  1.00 19.12 ?  74  PRO   B HG2  1 
ATOM   5102 H HG3  . PRO   B 1 74  ? 43.598 -13.590 15.374  1.00 19.12 ?  74  PRO   B HG3  1 
ATOM   5103 H HD2  . PRO   B 1 74  ? 43.426 -11.094 14.881  1.00 18.61 ?  74  PRO   B HD2  1 
ATOM   5104 H HD3  . PRO   B 1 74  ? 44.861 -11.811 14.878  1.00 18.61 ?  74  PRO   B HD3  1 
ATOM   5105 N N    . LEU   B 1 75  ? 42.505 -13.542 10.424  1.00 12.49 ?  75  LEU   B N    1 
ATOM   5106 C CA   . LEU   B 1 75  ? 41.292 -13.763 9.659   1.00 12.37 ?  75  LEU   B CA   1 
ATOM   5107 C C    . LEU   B 1 75  ? 40.325 -14.627 10.462  1.00 12.60 ?  75  LEU   B C    1 
ATOM   5108 O O    . LEU   B 1 75  ? 40.670 -15.184 11.502  1.00 13.80 ?  75  LEU   B O    1 
ATOM   5109 C CB   . LEU   B 1 75  ? 41.617 -14.481 8.349   1.00 12.27 ?  75  LEU   B CB   1 
ATOM   5110 C CG   . LEU   B 1 75  ? 42.475 -13.742 7.318   1.00 14.16 ?  75  LEU   B CG   1 
ATOM   5111 C CD1  . LEU   B 1 75  ? 42.675 -14.580 6.062   1.00 15.48 ?  75  LEU   B CD1  1 
ATOM   5112 C CD2  . LEU   B 1 75  ? 41.887 -12.406 6.964   1.00 17.60 ?  75  LEU   B CD2  1 
ATOM   5113 H H    . LEU   B 1 75  ? 43.182 -13.984 10.129  1.00 14.98 ?  75  LEU   B H    1 
ATOM   5114 H HA   . LEU   B 1 75  ? 40.865 -12.917 9.458   1.00 14.84 ?  75  LEU   B HA   1 
ATOM   5115 H HB2  . LEU   B 1 75  ? 42.083 -15.304 8.565   1.00 14.72 ?  75  LEU   B HB2  1 
ATOM   5116 H HB3  . LEU   B 1 75  ? 40.780 -14.699 7.908   1.00 14.72 ?  75  LEU   B HB3  1 
ATOM   5117 H HG   . LEU   B 1 75  ? 43.354 -13.586 7.701   1.00 16.99 ?  75  LEU   B HG   1 
ATOM   5118 H HD11 . LEU   B 1 75  ? 43.229 -14.085 5.432   1.00 18.58 ?  75  LEU   B HD11 1 
ATOM   5119 H HD12 . LEU   B 1 75  ? 43.114 -15.413 6.297   1.00 18.58 ?  75  LEU   B HD12 1 
ATOM   5120 H HD13 . LEU   B 1 75  ? 41.811 -14.764 5.661   1.00 18.58 ?  75  LEU   B HD13 1 
ATOM   5121 H HD21 . LEU   B 1 75  ? 42.403 -12.013 6.244   1.00 21.12 ?  75  LEU   B HD21 1 
ATOM   5122 H HD22 . LEU   B 1 75  ? 40.968 -12.532 6.686   1.00 21.12 ?  75  LEU   B HD22 1 
ATOM   5123 H HD23 . LEU   B 1 75  ? 41.921 -11.832 7.747   1.00 21.12 ?  75  LEU   B HD23 1 
ATOM   5124 N N    . LYS   B 1 76  ? 39.094 -14.724 9.963   1.00 14.17 ?  76  LYS   B N    1 
ATOM   5125 C CA   . LYS   B 1 76  ? 38.114 -15.684 10.451  1.00 15.60 ?  76  LYS   B CA   1 
ATOM   5126 C C    . LYS   B 1 76  ? 38.202 -16.958 9.615   1.00 13.93 ?  76  LYS   B C    1 
ATOM   5127 O O    . LYS   B 1 76  ? 38.470 -16.900 8.416   1.00 13.62 ?  76  LYS   B O    1 
ATOM   5128 C CB   . LYS   B 1 76  ? 36.695 -15.117 10.279  1.00 17.92 ?  76  LYS   B CB   1 
ATOM   5129 C CG   . LYS   B 1 76  ? 36.420 -13.732 10.886  1.00 19.76 ?  76  LYS   B CG   1 
ATOM   5130 C CD   . LYS   B 1 76  ? 35.017 -13.210 10.512  1.00 20.70 ?  76  LYS   B CD   1 
ATOM   5131 C CE   . LYS   B 1 76  ? 34.754 -11.829 11.093  1.00 22.87 ?  76  LYS   B CE   1 
ATOM   5132 N NZ   . LYS   B 1 76  ? 33.463 -11.235 10.644  1.00 23.48 ?  76  LYS   B NZ   1 
ATOM   5133 H H    . LYS   B 1 76  ? 38.799 -14.238 9.320   1.00 17.00 ?  76  LYS   B H    1 
ATOM   5134 H HA   . LYS   B 1 76  ? 38.271 -15.900 11.385  1.00 18.72 ?  76  LYS   B HA   1 
ATOM   5135 H HB2  . LYS   B 1 76  ? 36.509 -15.055 9.328   1.00 21.50 ?  76  LYS   B HB2  1 
ATOM   5136 H HB3  . LYS   B 1 76  ? 36.069 -15.736 10.686  1.00 21.50 ?  76  LYS   B HB3  1 
ATOM   5137 H HG2  . LYS   B 1 76  ? 36.478 -13.792 11.852  1.00 23.71 ?  76  LYS   B HG2  1 
ATOM   5138 H HG3  . LYS   B 1 76  ? 37.081 -13.103 10.550  1.00 23.71 ?  76  LYS   B HG3  1 
ATOM   5139 H HD2  . LYS   B 1 76  ? 34.950 -13.154 9.544   1.00 24.84 ?  76  LYS   B HD2  1 
ATOM   5140 H HD3  . LYS   B 1 76  ? 34.351 -13.822 10.858  1.00 24.84 ?  76  LYS   B HD3  1 
ATOM   5141 H HE2  . LYS   B 1 76  ? 34.733 -11.897 12.059  1.00 27.44 ?  76  LYS   B HE2  1 
ATOM   5142 H HE3  . LYS   B 1 76  ? 35.470 -11.234 10.819  1.00 27.44 ?  76  LYS   B HE3  1 
ATOM   5143 H HZ1  . LYS   B 1 76  ? 33.355 -10.430 11.009  1.00 28.18 ?  76  LYS   B HZ1  1 
ATOM   5144 H HZ2  . LYS   B 1 76  ? 33.457 -11.151 9.757   1.00 28.18 ?  76  LYS   B HZ2  1 
ATOM   5145 H HZ3  . LYS   B 1 76  ? 32.785 -11.757 10.889  1.00 28.18 ?  76  LYS   B HZ3  1 
ATOM   5146 N N    . VAL   B 1 77  ? 37.952 -18.114 10.242  1.00 14.78 ?  77  VAL   B N    1 
ATOM   5147 C CA   . VAL   B 1 77  ? 37.747 -19.327 9.454   1.00 14.45 ?  77  VAL   B CA   1 
ATOM   5148 C C    . VAL   B 1 77  ? 36.554 -19.090 8.543   1.00 13.38 ?  77  VAL   B C    1 
ATOM   5149 O O    . VAL   B 1 77  ? 35.495 -18.637 8.994   1.00 13.54 ?  77  VAL   B O    1 
ATOM   5150 C CB   . VAL   B 1 77  ? 37.552 -20.554 10.359  1.00 15.71 ?  77  VAL   B CB   1 
ATOM   5151 C CG1  . VAL   B 1 77  ? 37.271 -21.786 9.510   1.00 16.61 ?  77  VAL   B CG1  1 
ATOM   5152 C CG2  . VAL   B 1 77  ? 38.777 -20.777 11.246  1.00 17.08 ?  77  VAL   B CG2  1 
ATOM   5153 H H    . VAL   B 1 77  ? 37.901 -18.218 11.090  1.00 17.73 ?  77  VAL   B H    1 
ATOM   5154 H HA   . VAL   B 1 77  ? 38.522 -19.480 8.895   1.00 17.34 ?  77  VAL   B HA   1 
ATOM   5155 H HB   . VAL   B 1 77  ? 36.783 -20.401 10.932  1.00 18.85 ?  77  VAL   B HB   1 
ATOM   5156 H HG11 . VAL   B 1 77  ? 37.324 -22.570 10.077  1.00 19.93 ?  77  VAL   B HG11 1 
ATOM   5157 H HG12 . VAL   B 1 77  ? 36.380 -21.714 9.130   1.00 19.93 ?  77  VAL   B HG12 1 
ATOM   5158 H HG13 . VAL   B 1 77  ? 37.931 -21.839 8.805   1.00 19.93 ?  77  VAL   B HG13 1 
ATOM   5159 H HG21 . VAL   B 1 77  ? 38.637 -21.575 11.775  1.00 20.49 ?  77  VAL   B HG21 1 
ATOM   5160 H HG22 . VAL   B 1 77  ? 39.556 -20.882 10.681  1.00 20.49 ?  77  VAL   B HG22 1 
ATOM   5161 H HG23 . VAL   B 1 77  ? 38.887 -20.007 11.826  1.00 20.49 ?  77  VAL   B HG23 1 
ATOM   5162 N N    . GLY   B 1 78  ? 36.726 -19.367 7.251   1.00 12.81 ?  78  GLY   B N    1 
ATOM   5163 C CA   . GLY   B 1 78  ? 35.747 -19.041 6.242   1.00 12.46 ?  78  GLY   B CA   1 
ATOM   5164 C C    . GLY   B 1 78  ? 35.991 -17.726 5.540   1.00 12.05 ?  78  GLY   B C    1 
ATOM   5165 O O    . GLY   B 1 78  ? 35.303 -17.439 4.555   1.00 12.46 ?  78  GLY   B O    1 
ATOM   5166 H H    . GLY   B 1 78  ? 37.424 -19.758 6.931   1.00 15.37 ?  78  GLY   B H    1 
ATOM   5167 H HA2  . GLY   B 1 78  ? 35.733 -19.737 5.572   1.00 14.95 ?  78  GLY   B HA2  1 
ATOM   5168 H HA3  . GLY   B 1 78  ? 34.870 -18.995 6.654   1.00 14.95 ?  78  GLY   B HA3  1 
ATOM   5169 N N    . GLY   B 1 79  ? 36.944 -16.923 6.023   1.00 11.97 ?  79  GLY   B N    1 
ATOM   5170 C CA   . GLY   B 1 79  ? 37.239 -15.627 5.450   1.00 11.83 ?  79  GLY   B CA   1 
ATOM   5171 C C    . GLY   B 1 79  ? 38.474 -15.645 4.560   1.00 11.27 ?  79  GLY   B C    1 
ATOM   5172 O O    . GLY   B 1 79  ? 39.086 -16.681 4.306   1.00 11.94 ?  79  GLY   B O    1 
ATOM   5173 H H    . GLY   B 1 79  ? 37.451 -17.119 6.687   1.00 14.36 ?  79  GLY   B H    1 
ATOM   5174 H HA2  . GLY   B 1 79  ? 36.485 -15.323 4.918   1.00 14.19 ?  79  GLY   B HA2  1 
ATOM   5175 H HA3  . GLY   B 1 79  ? 37.392 -14.983 6.159   1.00 14.19 ?  79  GLY   B HA3  1 
ATOM   5176 N N    . SER   B 1 80  ? 38.844 -14.452 4.090   1.00 11.43 ?  80  SER   B N    1 
ATOM   5177 C CA   . SER   B 1 80  ? 39.954 -14.322 3.157   1.00 10.93 ?  80  SER   B CA   1 
ATOM   5178 C C    . SER   B 1 80  ? 40.529 -12.914 3.212   1.00 11.02 ?  80  SER   B C    1 
ATOM   5179 O O    . SER   B 1 80  ? 39.911 -11.980 3.728   1.00 12.43 ?  80  SER   B O    1 
ATOM   5180 C CB   . SER   B 1 80  ? 39.509 -14.610 1.719   1.00 11.46 ?  80  SER   B CB   1 
ATOM   5181 O OG   . SER   B 1 80  ? 38.667 -13.578 1.223   1.00 12.55 ?  80  SER   B OG   1 
ATOM   5182 H H    . SER   B 1 80  ? 38.478 -13.704 4.301   1.00 13.71 ?  80  SER   B H    1 
ATOM   5183 H HA   . SER   B 1 80  ? 40.647 -14.957 3.402   1.00 13.12 ?  80  SER   B HA   1 
ATOM   5184 H HB2  . SER   B 1 80  ? 40.292 -14.674 1.149   1.00 13.74 ?  80  SER   B HB2  1 
ATOM   5185 H HB3  . SER   B 1 80  ? 39.022 -15.452 1.701   1.00 13.74 ?  80  SER   B HB3  1 
ATOM   5186 H HG   . SER   B 1 80  ? 37.979 -13.519 1.709   1.00 15.05 ?  80  SER   B HG   1 
ATOM   5187 N N    . CYS   B 1 81  ? 41.714 -12.770 2.624   1.00 10.94 ?  81  CYS   B N    1 
ATOM   5188 C CA   . CYS   B 1 81  ? 42.256 -11.457 2.308   1.00 11.07 ?  81  CYS   B CA   1 
ATOM   5189 C C    . CYS   B 1 81  ? 43.028 -11.542 1.003   1.00 10.41 ?  81  CYS   B C    1 
ATOM   5190 O O    . CYS   B 1 81  ? 43.543 -12.602 0.630   1.00 11.50 ?  81  CYS   B O    1 
ATOM   5191 C CB   . CYS   B 1 81  ? 43.151 -10.895 3.421   1.00 11.89 ?  81  CYS   B CB   1 
ATOM   5192 S SG   . CYS   B 1 81  ? 44.670 -11.841 3.678   1.00 12.35 ?  81  CYS   B SG   1 
ATOM   5193 H H    . CYS   B 1 81  ? 42.232 -13.426 2.394   1.00 13.13 ?  81  CYS   B H    1 
ATOM   5194 H HA   . CYS   B 1 81  ? 41.523 -10.841 2.180   1.00 13.28 ?  81  CYS   B HA   1 
ATOM   5195 H HB2  . CYS   B 1 81  ? 43.406 -9.985  3.193   1.00 14.27 ?  81  CYS   B HB2  1 
ATOM   5196 H HB3  . CYS   B 1 81  ? 42.651 -10.892 4.256   1.00 14.27 ?  81  CYS   B HB3  1 
ATOM   5197 H HG   . CYS   B 1 81  ? 45.298 -11.334 4.571   1.00 14.82 ?  81  CYS   B HG   1 
ATOM   5198 N N    . VAL   B 1 82  ? 43.126 -10.401 0.327   1.00 10.70 ?  82  VAL   B N    1 
ATOM   5199 C CA   . VAL   B 1 82  ? 43.889 -10.275 -0.910  1.00 10.77 ?  82  VAL   B CA   1 
ATOM   5200 C C    . VAL   B 1 82  ? 45.229 -9.634  -0.591  1.00 11.40 ?  82  VAL   B C    1 
ATOM   5201 O O    . VAL   B 1 82  ? 45.280 -8.519  -0.053  1.00 12.28 ?  82  VAL   B O    1 
ATOM   5202 C CB   . VAL   B 1 82  ? 43.141 -9.435  -1.957  1.00 12.24 ?  82  VAL   B CB   1 
ATOM   5203 C CG1  . VAL   B 1 82  ? 43.992 -9.288  -3.217  1.00 13.69 ?  82  VAL   B CG1  1 
ATOM   5204 C CG2  . VAL   B 1 82  ? 41.785 -10.034 -2.272  1.00 13.22 ?  82  VAL   B CG2  1 
ATOM   5205 H H    . VAL   B 1 82  ? 42.741 -9.665  0.566   1.00 12.84 ?  82  VAL   B H    1 
ATOM   5206 H HA   . VAL   B 1 82  ? 44.046 -11.154 -1.284  1.00 12.92 ?  82  VAL   B HA   1 
ATOM   5207 H HB   . VAL   B 1 82  ? 42.991 -8.548  -1.600  1.00 14.68 ?  82  VAL   B HB   1 
ATOM   5208 H HG11 . VAL   B 1 82  ? 43.435 -8.980  -3.948  1.00 16.43 ?  82  VAL   B HG11 1 
ATOM   5209 H HG12 . VAL   B 1 82  ? 44.700 -8.641  -3.051  1.00 16.43 ?  82  VAL   B HG12 1 
ATOM   5210 H HG13 . VAL   B 1 82  ? 44.383 -10.149 -3.441  1.00 16.43 ?  82  VAL   B HG13 1 
ATOM   5211 H HG21 . VAL   B 1 82  ? 41.353 -9.506  -2.965  1.00 15.87 ?  82  VAL   B HG21 1 
ATOM   5212 H HG22 . VAL   B 1 82  ? 41.902 -10.947 -2.584  1.00 15.87 ?  82  VAL   B HG22 1 
ATOM   5213 H HG23 . VAL   B 1 82  ? 41.239 -10.030 -1.469  1.00 15.87 ?  82  VAL   B HG23 1 
ATOM   5214 N N    . LEU   B 1 83  ? 46.308 -10.319 -0.954  1.00 10.91 ?  83  LEU   B N    1 
ATOM   5215 C CA   . LEU   B 1 83  ? 47.663 -9.798  -0.840  1.00 10.80 ?  83  LEU   B CA   1 
ATOM   5216 C C    . LEU   B 1 83  ? 48.360 -9.939  -2.194  1.00 10.78 ?  83  LEU   B C    1 
ATOM   5217 O O    . LEU   B 1 83  ? 47.757 -10.359 -3.187  1.00 11.03 ?  83  LEU   B O    1 
ATOM   5218 C CB   . LEU   B 1 83  ? 48.422 -10.470 0.312   1.00 11.49 ?  83  LEU   B CB   1 
ATOM   5219 C CG   . LEU   B 1 83  ? 47.911 -10.123 1.716   1.00 12.57 ?  83  LEU   B CG   1 
ATOM   5220 C CD1  . LEU   B 1 83  ? 48.552 -10.994 2.780   1.00 13.46 ?  83  LEU   B CD1  1 
ATOM   5221 C CD2  . LEU   B 1 83  ? 48.113 -8.644  2.048   1.00 13.52 ?  83  LEU   B CD2  1 
ATOM   5222 H H    . LEU   B 1 83  ? 46.273 -11.117 -1.284  1.00 13.09 ?  83  LEU   B H    1 
ATOM   5223 H HA   . LEU   B 1 83  ? 47.607 -8.853  -0.644  1.00 12.95 ?  83  LEU   B HA   1 
ATOM   5224 H HB2  . LEU   B 1 83  ? 48.364 -11.429 0.208   1.00 13.78 ?  83  LEU   B HB2  1 
ATOM   5225 H HB3  . LEU   B 1 83  ? 49.353 -10.194 0.266   1.00 13.78 ?  83  LEU   B HB3  1 
ATOM   5226 H HG   . LEU   B 1 83  ? 46.959 -10.293 1.740   1.00 15.09 ?  83  LEU   B HG   1 
ATOM   5227 H HD11 . LEU   B 1 83  ? 48.194 -10.751 3.649   1.00 16.15 ?  83  LEU   B HD11 1 
ATOM   5228 H HD12 . LEU   B 1 83  ? 48.342 -11.927 2.592   1.00 16.15 ?  83  LEU   B HD12 1 
ATOM   5229 H HD13 . LEU   B 1 83  ? 49.511 -10.865 2.768   1.00 16.15 ?  83  LEU   B HD13 1 
ATOM   5230 H HD21 . LEU   B 1 83  ? 47.892 -8.500  2.984   1.00 16.22 ?  83  LEU   B HD21 1 
ATOM   5231 H HD22 . LEU   B 1 83  ? 49.038 -8.408  1.887   1.00 16.22 ?  83  LEU   B HD22 1 
ATOM   5232 H HD23 . LEU   B 1 83  ? 47.530 -8.112  1.486   1.00 16.22 ?  83  LEU   B HD23 1 
ATOM   5233 N N    . SER   B 1 84  ? 49.639 -9.571  -2.245  1.00 11.81 ?  84  SER   B N    1 
ATOM   5234 C CA   . SER   B 1 84  ? 50.373 -9.686  -3.494  1.00 12.09 ?  84  SER   B CA   1 
ATOM   5235 C C    . SER   B 1 84  ? 50.528 -11.143 -3.914  1.00 11.40 ?  84  SER   B C    1 
ATOM   5236 O O    . SER   B 1 84  ? 50.639 -12.047 -3.085  1.00 11.28 ?  84  SER   B O    1 
ATOM   5237 C CB   . SER   B 1 84  ? 51.766 -9.079  -3.349  1.00 14.10 ?  84  SER   B CB   1 
ATOM   5238 O OG   . SER   B 1 84  ? 52.514 -9.300  -4.531  1.00 15.50 ?  84  SER   B OG   1 
ATOM   5239 H H    . SER   B 1 84  ? 50.090 -9.244  -1.584  1.00 14.17 ?  84  SER   B H    1 
ATOM   5240 H HA   . SER   B 1 84  ? 49.902 -9.210  -4.193  1.00 14.51 ?  84  SER   B HA   1 
ATOM   5241 H HB2  . SER   B 1 84  ? 51.684 -8.121  -3.194  1.00 16.92 ?  84  SER   B HB2  1 
ATOM   5242 H HB3  . SER   B 1 84  ? 52.224 -9.496  -2.604  1.00 16.92 ?  84  SER   B HB3  1 
ATOM   5243 H HG   . SER   B 1 84  ? 53.280 -8.955  -4.458  1.00 18.60 ?  84  SER   B HG   1 
ATOM   5244 N N    . GLY   B 1 85  ? 50.587 -11.359 -5.223  1.00 12.55 ?  85  GLY   B N    1 
ATOM   5245 C CA   . GLY   B 1 85  ? 50.934 -12.654 -5.762  1.00 12.99 ?  85  GLY   B CA   1 
ATOM   5246 C C    . GLY   B 1 85  ? 52.405 -12.847 -6.064  1.00 11.97 ?  85  GLY   B C    1 
ATOM   5247 O O    . GLY   B 1 85  ? 52.785 -13.928 -6.522  1.00 12.28 ?  85  GLY   B O    1 
ATOM   5248 H H    . GLY   B 1 85  ? 50.435 -10.763 -5.821  1.00 15.06 ?  85  GLY   B H    1 
ATOM   5249 H HA2  . GLY   B 1 85  ? 50.668 -13.340 -5.131  1.00 15.59 ?  85  GLY   B HA2  1 
ATOM   5250 H HA3  . GLY   B 1 85  ? 50.449 -12.794 -6.583  1.00 15.59 ?  85  GLY   B HA3  1 
ATOM   5251 N N    . HIS   B 1 86  ? 53.257 -11.851 -5.833  1.00 12.17 ?  86  HIS   B N    1 
ATOM   5252 C CA   . HIS   B 1 86  ? 54.719 -12.027 -5.920  1.00 12.25 ?  86  HIS   B CA   1 
ATOM   5253 C C    . HIS   B 1 86  ? 55.089 -12.537 -7.311  1.00 12.46 ?  86  HIS   B C    1 
ATOM   5254 O O    . HIS   B 1 86  ? 54.703 -11.916 -8.314  1.00 13.39 ?  86  HIS   B O    1 
ATOM   5255 C CB   . HIS   B 1 86  ? 55.202 -12.874 -4.747  1.00 12.71 ?  86  HIS   B CB   1 
ATOM   5256 C CG   . HIS   B 1 86  ? 54.896 -12.264 -3.423  1.00 12.81 ?  86  HIS   B CG   1 
ATOM   5257 N ND1  . HIS   B 1 86  ? 55.731 -11.357 -2.807  1.00 14.42 ?  86  HIS   B ND1  1 
ATOM   5258 C CD2  . HIS   B 1 86  ? 53.821 -12.402 -2.614  1.00 13.26 ?  86  HIS   B CD2  1 
ATOM   5259 C CE1  . HIS   B 1 86  ? 55.178 -10.965 -1.673  1.00 14.28 ?  86  HIS   B CE1  1 
ATOM   5260 N NE2  . HIS   B 1 86  ? 54.015 -11.577 -1.537  1.00 13.44 ?  86  HIS   B NE2  1 
ATOM   5261 H H    . HIS   B 1 86  ? 53.022 -11.055 -5.622  1.00 14.60 ?  86  HIS   B H    1 
ATOM   5262 H HA   . HIS   B 1 86  ? 55.134 -11.160 -5.823  1.00 14.69 ?  86  HIS   B HA   1 
ATOM   5263 H HB2  . HIS   B 1 86  ? 54.774 -13.745 -4.785  1.00 15.25 ?  86  HIS   B HB2  1 
ATOM   5264 H HB3  . HIS   B 1 86  ? 56.166 -12.980 -4.807  1.00 15.25 ?  86  HIS   B HB3  1 
ATOM   5265 H HD2  . HIS   B 1 86  ? 53.070 -12.937 -2.770  1.00 15.91 ?  86  HIS   B HD2  1 
ATOM   5266 H HE1  . HIS   B 1 86  ? 55.551 -10.367 -1.069  1.00 17.13 ?  86  HIS   B HE1  1 
ATOM   5267 H HE2  . HIS   B 1 86  ? 53.478 -11.489 -0.868  1.00 16.13 ?  86  HIS   B HE2  1 
ATOM   5268 N N    . ASN   B 1 87  ? 55.859 -13.618 -7.423  1.00 12.74 ?  87  ASN   B N    1 
ATOM   5269 C CA   . ASN   B 1 87  ? 56.242 -14.190 -8.705  1.00 13.33 ?  87  ASN   B CA   1 
ATOM   5270 C C    . ASN   B 1 87  ? 55.253 -15.230 -9.204  1.00 13.18 ?  87  ASN   B C    1 
ATOM   5271 O O    . ASN   B 1 87  ? 55.560 -15.941 -10.166 1.00 15.03 ?  87  ASN   B O    1 
ATOM   5272 C CB   . ASN   B 1 87  ? 57.638 -14.819 -8.598  1.00 15.34 ?  87  ASN   B CB   1 
ATOM   5273 C CG   . ASN   B 1 87  ? 57.696 -15.945 -7.567  1.00 16.39 ?  87  ASN   B CG   1 
ATOM   5274 O OD1  . ASN   B 1 87  ? 57.059 -15.869 -6.512  1.00 15.15 ?  87  ASN   B OD1  1 
ATOM   5275 N ND2  . ASN   B 1 87  ? 58.427 -17.012 -7.891  1.00 18.77 ?  87  ASN   B ND2  1 
ATOM   5276 H H    . ASN   B 1 87  ? 56.181 -14.053 -6.752  1.00 15.29 ?  87  ASN   B H    1 
ATOM   5277 H HA   . ASN   B 1 87  ? 56.287 -13.481 -9.365  1.00 15.99 ?  87  ASN   B HA   1 
ATOM   5278 H HB2  . ASN   B 1 87  ? 57.887 -15.188 -9.465  1.00 18.40 ?  87  ASN   B HB2  1 
ATOM   5279 H HB3  . ASN   B 1 87  ? 58.274 -14.136 -8.337  1.00 18.40 ?  87  ASN   B HB3  1 
ATOM   5280 H HD21 . ASN   B 1 87  ? 58.492 -17.668 -7.345  1.00 22.53 ?  87  ASN   B HD21 1 
ATOM   5281 H HD22 . ASN   B 1 87  ? 58.850 -17.033 -8.644  1.00 22.53 ?  87  ASN   B HD22 1 
ATOM   5282 N N    . LEU   B 1 88  ? 54.081 -15.333 -8.576  1.00 12.16 ?  88  LEU   B N    1 
ATOM   5283 C CA   . LEU   B 1 88  ? 53.103 -16.365 -8.901  1.00 12.34 ?  88  LEU   B CA   1 
ATOM   5284 C C    . LEU   B 1 88  ? 51.873 -15.851 -9.626  1.00 12.15 ?  88  LEU   B C    1 
ATOM   5285 O O    . LEU   B 1 88  ? 51.265 -16.605 -10.394 1.00 13.96 ?  88  LEU   B O    1 
ATOM   5286 C CB   . LEU   B 1 88  ? 52.629 -17.048 -7.615  1.00 13.11 ?  88  LEU   B CB   1 
ATOM   5287 C CG   . LEU   B 1 88  ? 53.730 -17.722 -6.809  1.00 15.72 ?  88  LEU   B CG   1 
ATOM   5288 C CD1  . LEU   B 1 88  ? 53.209 -18.069 -5.425  1.00 17.28 ?  88  LEU   B CD1  1 
ATOM   5289 C CD2  . LEU   B 1 88  ? 54.203 -18.958 -7.538  1.00 18.96 ?  88  LEU   B CD2  1 
ATOM   5290 H H    . LEU   B 1 88  ? 53.827 -14.809 -7.936  1.00 14.59 ?  88  LEU   B H    1 
ATOM   5291 H HA   . LEU   B 1 88  ? 53.519 -17.031 -9.458  1.00 14.81 ?  88  LEU   B HA   1 
ATOM   5292 H HB2  . LEU   B 1 88  ? 52.210 -16.386 -7.041  1.00 15.73 ?  88  LEU   B HB2  1 
ATOM   5293 H HB3  . LEU   B 1 88  ? 51.978 -17.731 -7.848  1.00 15.73 ?  88  LEU   B HB3  1 
ATOM   5294 H HG   . LEU   B 1 88  ? 54.479 -17.114 -6.711  1.00 18.86 ?  88  LEU   B HG   1 
ATOM   5295 H HD11 . LEU   B 1 88  ? 53.834 -18.671 -4.993  1.00 20.73 ?  88  LEU   B HD11 1 
ATOM   5296 H HD12 . LEU   B 1 88  ? 53.121 -17.254 -4.907  1.00 20.73 ?  88  LEU   B HD12 1 
ATOM   5297 H HD13 . LEU   B 1 88  ? 52.344 -18.498 -5.515  1.00 20.73 ?  88  LEU   B HD13 1 
ATOM   5298 H HD21 . LEU   B 1 88  ? 54.848 -19.424 -6.985  1.00 22.76 ?  88  LEU   B HD21 1 
ATOM   5299 H HD22 . LEU   B 1 88  ? 53.441 -19.533 -7.714  1.00 22.76 ?  88  LEU   B HD22 1 
ATOM   5300 H HD23 . LEU   B 1 88  ? 54.616 -18.693 -8.375  1.00 22.76 ?  88  LEU   B HD23 1 
ATOM   5301 N N    . ALA   B 1 89  ? 51.470 -14.613 -9.365  1.00 11.58 ?  89  ALA   B N    1 
ATOM   5302 C CA   . ALA   B 1 89  ? 50.173 -14.119 -9.799  1.00 11.11 ?  89  ALA   B CA   1 
ATOM   5303 C C    . ALA   B 1 89  ? 50.150 -12.626 -9.528  1.00 11.81 ?  89  ALA   B C    1 
ATOM   5304 O O    . ALA   B 1 89  ? 50.992 -12.108 -8.794  1.00 12.60 ?  89  ALA   B O    1 
ATOM   5305 C CB   . ALA   B 1 89  ? 49.047 -14.787 -9.015  1.00 11.39 ?  89  ALA   B CB   1 
ATOM   5306 H H    . ALA   B 1 89  ? 51.933 -14.023 -8.933  1.00 13.89 ?  89  ALA   B H    1 
ATOM   5307 H HA   . ALA   B 1 89  ? 50.044 -14.273 -10.748 1.00 13.32 ?  89  ALA   B HA   1 
ATOM   5308 H HB1  . ALA   B 1 89  ? 48.192 -14.450 -9.337  1.00 13.66 ?  89  ALA   B HB1  1 
ATOM   5309 H HB2  . ALA   B 1 89  ? 49.094 -15.746 -9.156  1.00 13.66 ?  89  ALA   B HB2  1 
ATOM   5310 H HB3  . ALA   B 1 89  ? 49.150 -14.583 -8.076  1.00 13.66 ?  89  ALA   B HB3  1 
ATOM   5311 N N    . LYS   B 1 90  ? 49.151 -11.935 -10.077 1.00 12.48 ?  90  LYS   B N    1 
ATOM   5312 C CA   . LYS   B 1 90  ? 48.967 -10.545 -9.674  1.00 12.72 ?  90  LYS   B CA   1 
ATOM   5313 C C    . LYS   B 1 90  ? 48.653 -10.466 -8.185  1.00 12.36 ?  90  LYS   B C    1 
ATOM   5314 O O    . LYS   B 1 90  ? 49.288 -9.707  -7.436  1.00 13.69 ?  90  LYS   B O    1 
ATOM   5315 C CB   . LYS   B 1 90  ? 47.886 -9.882  -10.526 1.00 14.24 ?  90  LYS   B CB   1 
ATOM   5316 C CG   . LYS   B 1 90  ? 47.607 -8.436  -10.153 1.00 14.45 ?  90  LYS   B CG   1 
ATOM   5317 C CD   . LYS   B 1 90  ? 48.823 -7.558  -10.257 1.00 17.58 ?  90  LYS   B CD   1 
ATOM   5318 C CE   . LYS   B 1 90  ? 48.405 -6.123  -10.068 1.00 20.12 ?  90  LYS   B CE   1 
ATOM   5319 N NZ   . LYS   B 1 90  ? 49.575 -5.233  -9.906  1.00 20.51 ?  90  LYS   B NZ   1 
ATOM   5320 H H    . LYS   B 1 90  ? 48.583 -12.238 -10.653 1.00 14.98 ?  90  LYS   B H    1 
ATOM   5321 H HA   . LYS   B 1 90  ? 49.794 -10.072 -9.825  1.00 15.26 ?  90  LYS   B HA   1 
ATOM   5322 H HB2  . LYS   B 1 90  ? 48.172 -9.891  -11.457 1.00 17.09 ?  90  LYS   B HB2  1 
ATOM   5323 H HB3  . LYS   B 1 90  ? 47.059 -10.376 -10.435 1.00 17.09 ?  90  LYS   B HB3  1 
ATOM   5324 H HG2  . LYS   B 1 90  ? 46.930 -8.081  -10.752 1.00 17.33 ?  90  LYS   B HG2  1 
ATOM   5325 H HG3  . LYS   B 1 90  ? 47.284 -8.400  -9.237  1.00 17.33 ?  90  LYS   B HG3  1 
ATOM   5326 H HD2  . LYS   B 1 90  ? 49.459 -7.792  -9.561  1.00 21.09 ?  90  LYS   B HD2  1 
ATOM   5327 H HD3  . LYS   B 1 90  ? 49.226 -7.657  -11.135 1.00 21.09 ?  90  LYS   B HD3  1 
ATOM   5328 H HE2  . LYS   B 1 90  ? 47.908 -5.821  -10.848 1.00 24.14 ?  90  LYS   B HE2  1 
ATOM   5329 H HE3  . LYS   B 1 90  ? 47.858 -6.040  -9.272  1.00 24.14 ?  90  LYS   B HE3  1 
ATOM   5330 H HZ1  . LYS   B 1 90  ? 49.315 -4.387  -9.799  1.00 24.61 ?  90  LYS   B HZ1  1 
ATOM   5331 H HZ2  . LYS   B 1 90  ? 50.053 -5.477  -9.196  1.00 24.61 ?  90  LYS   B HZ2  1 
ATOM   5332 H HZ3  . LYS   B 1 90  ? 50.099 -5.277  -10.630 1.00 24.61 ?  90  LYS   B HZ3  1 
ATOM   5333 N N    . HIS   B 1 91  ? 47.702 -11.288 -7.735  1.00 11.07 ?  91  HIS   B N    1 
ATOM   5334 C CA   . HIS   B 1 91  ? 47.238 -11.311 -6.362  1.00 11.07 ?  91  HIS   B CA   1 
ATOM   5335 C C    . HIS   B 1 91  ? 47.235 -12.738 -5.845  1.00 10.45 ?  91  HIS   B C    1 
ATOM   5336 O O    . HIS   B 1 91  ? 46.996 -13.693 -6.596  1.00 10.96 ?  91  HIS   B O    1 
ATOM   5337 C CB   . HIS   B 1 91  ? 45.788 -10.835 -6.250  1.00 12.54 ?  91  HIS   B CB   1 
ATOM   5338 C CG   . HIS   B 1 91  ? 45.574 -9.429  -6.686  1.00 15.59 ?  91  HIS   B CG   1 
ATOM   5339 N ND1  . HIS   B 1 91  ? 46.167 -8.352  -6.061  1.00 18.44 ?  91  HIS   B ND1  1 
ATOM   5340 C CD2  . HIS   B 1 91  ? 44.804 -8.917  -7.670  1.00 18.19 ?  91  HIS   B CD2  1 
ATOM   5341 C CE1  . HIS   B 1 91  ? 45.787 -7.236  -6.657  1.00 19.31 ?  91  HIS   B CE1  1 
ATOM   5342 N NE2  . HIS   B 1 91  ? 44.951 -7.551  -7.631  1.00 19.47 ?  91  HIS   B NE2  1 
ATOM   5343 H H    . HIS   B 1 91  ? 47.298 -11.868 -8.231  1.00 13.28 ?  91  HIS   B H    1 
ATOM   5344 H HA   . HIS   B 1 91  ? 47.811 -10.756 -5.797  1.00 13.29 ?  91  HIS   B HA   1 
ATOM   5345 H HB2  . HIS   B 1 91  ? 45.234 -11.406 -6.803  1.00 15.04 ?  91  HIS   B HB2  1 
ATOM   5346 H HB3  . HIS   B 1 91  ? 45.509 -10.906 -5.322  1.00 15.04 ?  91  HIS   B HB3  1 
ATOM   5347 H HD1  . HIS   B 1 91  ? 46.710 -8.405  -5.391  1.00 22.13 ?  91  HIS   B HD1  1 
ATOM   5348 H HD2  . HIS   B 1 91  ? 44.280 -9.391  -8.270  1.00 21.82 ?  91  HIS   B HD2  1 
ATOM   5349 H HE1  . HIS   B 1 91  ? 46.059 -6.379  -6.418  1.00 23.17 ?  91  HIS   B HE1  1 
ATOM   5350 N N    . CYS   B 1 92  ? 47.434 -12.872 -4.542  1.00 10.33 ?  92  CYS   B N    1 
ATOM   5351 C CA   . CYS   B 1 92  ? 47.126 -14.104 -3.831  1.00 9.91  ?  92  CYS   B CA   1 
ATOM   5352 C C    . CYS   B 1 92  ? 45.909 -13.868 -2.946  1.00 9.75  ?  92  CYS   B C    1 
ATOM   5353 O O    . CYS   B 1 92  ? 45.909 -12.963 -2.095  1.00 10.68 ?  92  CYS   B O    1 
ATOM   5354 C CB   . CYS   B 1 92  ? 48.304 -14.566 -2.980  1.00 10.24 ?  92  CYS   B CB   1 
ATOM   5355 S SG   . CYS   B 1 92  ? 47.953 -16.102 -2.088  1.00 10.59 ?  92  CYS   B SG   1 
ATOM   5356 H H    . CYS   B 1 92  ? 47.764 -12.256 -4.033  1.00 12.39 ?  92  CYS   B H    1 
ATOM   5357 H HA   . CYS   B 1 92  ? 46.922 -14.804 -4.472  1.00 11.88 ?  92  CYS   B HA   1 
ATOM   5358 H HB2  . CYS   B 1 92  ? 49.069 -14.716 -3.547  1.00 12.29 ?  92  CYS   B HB2  1 
ATOM   5359 H HB3  . CYS   B 1 92  ? 48.501 -13.878 -2.321  1.00 12.29 ?  92  CYS   B HB3  1 
ATOM   5360 H HG   . CYS   B 1 92  ? 48.925 -16.414 -1.460  1.00 12.71 ?  92  CYS   B HG   1 
ATOM   5361 N N    . LEU   B 1 93  ? 44.873 -14.676 -3.158  1.00 9.75  ?  93  LEU   B N    1 
ATOM   5362 C CA   . LEU   B 1 93  ? 43.701 -14.689 -2.298  1.00 9.91  ?  93  LEU   B CA   1 
ATOM   5363 C C    . LEU   B 1 93  ? 43.925 -15.755 -1.234  1.00 9.53  ?  93  LEU   B C    1 
ATOM   5364 O O    . LEU   B 1 93  ? 43.881 -16.956 -1.526  1.00 10.20 ?  93  LEU   B O    1 
ATOM   5365 C CB   . LEU   B 1 93  ? 42.440 -14.977 -3.107  1.00 10.41 ?  93  LEU   B CB   1 
ATOM   5366 C CG   . LEU   B 1 93  ? 41.148 -15.001 -2.287  1.00 10.95 ?  93  LEU   B CG   1 
ATOM   5367 C CD1  . LEU   B 1 93  ? 40.796 -13.613 -1.788  1.00 11.69 ?  93  LEU   B CD1  1 
ATOM   5368 C CD2  . LEU   B 1 93  ? 40.004 -15.591 -3.096  1.00 11.34 ?  93  LEU   B CD2  1 
ATOM   5369 H H    . LEU   B 1 93  ? 44.825 -15.238 -3.818  1.00 11.70 ?  93  LEU   B H    1 
ATOM   5370 H HA   . LEU   B 1 93  ? 43.606 -13.826 -1.868  1.00 11.88 ?  93  LEU   B HA   1 
ATOM   5371 H HB2  . LEU   B 1 93  ? 42.342 -14.287 -3.784  1.00 12.48 ?  93  LEU   B HB2  1 
ATOM   5372 H HB3  . LEU   B 1 93  ? 42.536 -15.840 -3.535  1.00 12.48 ?  93  LEU   B HB3  1 
ATOM   5373 H HG   . LEU   B 1 93  ? 41.278 -15.572 -1.517  1.00 13.13 ?  93  LEU   B HG   1 
ATOM   5374 H HD11 . LEU   B 1 93  ? 39.940 -13.646 -1.334  1.00 14.02 ?  93  LEU   B HD11 1 
ATOM   5375 H HD12 . LEU   B 1 93  ? 41.485 -13.310 -1.179  1.00 14.02 ?  93  LEU   B HD12 1 
ATOM   5376 H HD13 . LEU   B 1 93  ? 40.739 -13.007 -2.549  1.00 14.02 ?  93  LEU   B HD13 1 
ATOM   5377 H HD21 . LEU   B 1 93  ? 39.200 -15.590 -2.552  1.00 13.61 ?  93  LEU   B HD21 1 
ATOM   5378 H HD22 . LEU   B 1 93  ? 39.866 -15.053 -3.891  1.00 13.61 ?  93  LEU   B HD22 1 
ATOM   5379 H HD23 . LEU   B 1 93  ? 40.229 -16.502 -3.349  1.00 13.61 ?  93  LEU   B HD23 1 
ATOM   5380 N N    . HIS   B 1 94  ? 44.209 -15.319 -0.014  1.00 9.37  ?  94  HIS   B N    1 
ATOM   5381 C CA   . HIS   B 1 94  ? 44.431 -16.222 1.107   1.00 9.63  ?  94  HIS   B CA   1 
ATOM   5382 C C    . HIS   B 1 94  ? 43.072 -16.578 1.685   1.00 9.95  ?  94  HIS   B C    1 
ATOM   5383 O O    . HIS   B 1 94  ? 42.404 -15.709 2.246   1.00 11.42 ?  94  HIS   B O    1 
ATOM   5384 C CB   . HIS   B 1 94  ? 45.304 -15.542 2.160   1.00 10.38 ?  94  HIS   B CB   1 
ATOM   5385 C CG   . HIS   B 1 94  ? 46.688 -15.240 1.690   1.00 10.08 ?  94  HIS   B CG   1 
ATOM   5386 N ND1  . HIS   B 1 94  ? 47.710 -16.159 1.768   1.00 10.32 ?  94  HIS   B ND1  1 
ATOM   5387 C CD2  . HIS   B 1 94  ? 47.198 -14.135 1.093   1.00 10.27 ?  94  HIS   B CD2  1 
ATOM   5388 C CE1  . HIS   B 1 94  ? 48.799 -15.613 1.260   1.00 10.64 ?  94  HIS   B CE1  1 
ATOM   5389 N NE2  . HIS   B 1 94  ? 48.518 -14.389 0.845   1.00 10.85 ?  94  HIS   B NE2  1 
ATOM   5390 H H    . HIS   B 1 94  ? 44.290 -14.482 0.188   1.00 11.24 ?  94  HIS   B H    1 
ATOM   5391 H HA   . HIS   B 1 94  ? 44.867 -17.029 0.796   1.00 11.56 ?  94  HIS   B HA   1 
ATOM   5392 H HB2  . HIS   B 1 94  ? 44.891 -14.712 2.419   1.00 12.45 ?  94  HIS   B HB2  1 
ATOM   5393 H HB3  . HIS   B 1 94  ? 45.376 -16.137 2.924   1.00 12.45 ?  94  HIS   B HB3  1 
ATOM   5394 H HD2  . HIS   B 1 94  ? 46.747 -13.352 0.904   1.00 12.32 ?  94  HIS   B HD2  1 
ATOM   5395 H HE1  . HIS   B 1 94  ? 49.631 -16.036 1.201   1.00 12.76 ?  94  HIS   B HE1  1 
ATOM   5396 H HE2  . HIS   B 1 94  ? 49.080 -13.851 0.482   1.00 13.02 ?  94  HIS   B HE2  1 
ATOM   5397 N N    . VAL   B 1 95  ? 42.639 -17.830 1.526   1.00 9.92  ?  95  VAL   B N    1 
ATOM   5398 C CA   . VAL   B 1 95  ? 41.314 -18.268 1.961   1.00 10.24 ?  95  VAL   B CA   1 
ATOM   5399 C C    . VAL   B 1 95  ? 41.482 -19.302 3.059   1.00 10.23 ?  95  VAL   B C    1 
ATOM   5400 O O    . VAL   B 1 95  ? 42.250 -20.260 2.900   1.00 10.95 ?  95  VAL   B O    1 
ATOM   5401 C CB   . VAL   B 1 95  ? 40.494 -18.875 0.808   1.00 10.42 ?  95  VAL   B CB   1 
ATOM   5402 C CG1  . VAL   B 1 95  ? 39.115 -19.324 1.297   1.00 11.38 ?  95  VAL   B CG1  1 
ATOM   5403 C CG2  . VAL   B 1 95  ? 40.373 -17.895 -0.334  1.00 10.63 ?  95  VAL   B CG2  1 
ATOM   5404 H H    . VAL   B 1 95  ? 43.098 -18.458 1.160   1.00 11.90 ?  95  VAL   B H    1 
ATOM   5405 H HA   . VAL   B 1 95  ? 40.817 -17.514 2.324   1.00 12.28 ?  95  VAL   B HA   1 
ATOM   5406 H HB   . VAL   B 1 95  ? 40.953 -19.655 0.475   1.00 12.50 ?  95  VAL   B HB   1 
ATOM   5407 H HG11 . VAL   B 1 95  ? 38.554 -19.525 0.525   1.00 13.65 ?  95  VAL   B HG11 1 
ATOM   5408 H HG12 . VAL   B 1 95  ? 39.210 -20.122 1.841   1.00 13.65 ?  95  VAL   B HG12 1 
ATOM   5409 H HG13 . VAL   B 1 95  ? 38.708 -18.614 1.816   1.00 13.65 ?  95  VAL   B HG13 1 
ATOM   5410 H HG21 . VAL   B 1 95  ? 39.789 -18.273 -1.011  1.00 12.76 ?  95  VAL   B HG21 1 
ATOM   5411 H HG22 . VAL   B 1 95  ? 39.993 -17.066 0.002   1.00 12.76 ?  95  VAL   B HG22 1 
ATOM   5412 H HG23 . VAL   B 1 95  ? 41.251 -17.735 -0.701  1.00 12.76 ?  95  VAL   B HG23 1 
ATOM   5413 N N    . VAL   B 1 96  ? 40.749 -19.134 4.154   1.00 10.58 ?  96  VAL   B N    1 
ATOM   5414 C CA   . VAL   B 1 96  ? 40.831 -20.049 5.293   1.00 11.15 ?  96  VAL   B CA   1 
ATOM   5415 C C    . VAL   B 1 96  ? 39.644 -21.010 5.248   1.00 11.38 ?  96  VAL   B C    1 
ATOM   5416 O O    . VAL   B 1 96  ? 38.525 -20.659 5.634   1.00 12.34 ?  96  VAL   B O    1 
ATOM   5417 C CB   . VAL   B 1 96  ? 40.884 -19.299 6.627   1.00 11.88 ?  96  VAL   B CB   1 
ATOM   5418 C CG1  . VAL   B 1 96  ? 41.072 -20.295 7.767   1.00 12.83 ?  96  VAL   B CG1  1 
ATOM   5419 C CG2  . VAL   B 1 96  ? 41.992 -18.256 6.629   1.00 12.54 ?  96  VAL   B CG2  1 
ATOM   5420 H H    . VAL   B 1 96  ? 40.188 -18.493 4.268   1.00 12.69 ?  96  VAL   B H    1 
ATOM   5421 H HA   . VAL   B 1 96  ? 41.640 -20.577 5.218   1.00 13.38 ?  96  VAL   B HA   1 
ATOM   5422 H HB   . VAL   B 1 96  ? 40.040 -18.843 6.769   1.00 14.26 ?  96  VAL   B HB   1 
ATOM   5423 H HG11 . VAL   B 1 96  ? 41.257 -19.805 8.587   1.00 15.39 ?  96  VAL   B HG11 1 
ATOM   5424 H HG12 . VAL   B 1 96  ? 40.261 -20.816 7.876   1.00 15.39 ?  96  VAL   B HG12 1 
ATOM   5425 H HG13 . VAL   B 1 96  ? 41.817 -20.879 7.561   1.00 15.39 ?  96  VAL   B HG13 1 
ATOM   5426 H HG21 . VAL   B 1 96  ? 42.045 -17.849 7.511   1.00 15.04 ?  96  VAL   B HG21 1 
ATOM   5427 H HG22 . VAL   B 1 96  ? 42.832 -18.681 6.410   1.00 15.04 ?  96  VAL   B HG22 1 
ATOM   5428 H HG23 . VAL   B 1 96  ? 41.784 -17.572 5.969   1.00 15.04 ?  96  VAL   B HG23 1 
ATOM   5429 N N    . GLY   B 1 97  ? 39.879 -22.240 4.801   1.00 11.32 ?  97  GLY   B N    1 
ATOM   5430 C CA   . GLY   B 1 97  ? 38.904 -23.296 4.967   1.00 12.10 ?  97  GLY   B CA   1 
ATOM   5431 C C    . GLY   B 1 97  ? 39.033 -23.904 6.346   1.00 13.11 ?  97  GLY   B C    1 
ATOM   5432 O O    . GLY   B 1 97  ? 40.079 -23.781 6.997   1.00 13.62 ?  97  GLY   B O    1 
ATOM   5433 H H    . GLY   B 1 97  ? 40.599 -22.480 4.393   1.00 13.58 ?  97  GLY   B H    1 
ATOM   5434 H HA2  . GLY   B 1 97  ? 38.008 -22.929 4.855   1.00 14.52 ?  97  GLY   B HA2  1 
ATOM   5435 H HA3  . GLY   B 1 97  ? 39.042 -23.981 4.292   1.00 14.52 ?  97  GLY   B HA3  1 
ATOM   5436 N N    . PRO   B 1 98  ? 37.987 -24.587 6.814   1.00 14.06 ?  98  PRO   B N    1 
ATOM   5437 C CA   . PRO   B 1 98  ? 38.082 -25.288 8.098   1.00 15.10 ?  98  PRO   B CA   1 
ATOM   5438 C C    . PRO   B 1 98  ? 39.112 -26.405 8.054   1.00 14.66 ?  98  PRO   B C    1 
ATOM   5439 O O    . PRO   B 1 98  ? 39.224 -27.139 7.073   1.00 14.88 ?  98  PRO   B O    1 
ATOM   5440 C CB   . PRO   B 1 98  ? 36.666 -25.840 8.299   1.00 15.40 ?  98  PRO   B CB   1 
ATOM   5441 C CG   . PRO   B 1 98  ? 36.108 -25.966 6.923   1.00 14.94 ?  98  PRO   B CG   1 
ATOM   5442 C CD   . PRO   B 1 98  ? 36.666 -24.775 6.186   1.00 14.11 ?  98  PRO   B CD   1 
ATOM   5443 H HA   . PRO   B 1 98  ? 38.297 -24.660 8.804   1.00 18.12 ?  98  PRO   B HA   1 
ATOM   5444 H HB2  . PRO   B 1 98  ? 36.718 -26.709 8.731   1.00 18.48 ?  98  PRO   B HB2  1 
ATOM   5445 H HB3  . PRO   B 1 98  ? 36.144 -25.222 8.825   1.00 18.48 ?  98  PRO   B HB3  1 
ATOM   5446 H HG2  . PRO   B 1 98  ? 36.415 -26.801 6.522   1.00 17.93 ?  98  PRO   B HG2  1 
ATOM   5447 H HG3  . PRO   B 1 98  ? 35.142 -25.938 6.959   1.00 17.93 ?  98  PRO   B HG3  1 
ATOM   5448 H HD2  . PRO   B 1 98  ? 36.756 -24.975 5.236   1.00 16.93 ?  98  PRO   B HD2  1 
ATOM   5449 H HD3  . PRO   B 1 98  ? 36.112 -23.994 6.331   1.00 16.93 ?  98  PRO   B HD3  1 
ATOM   5450 N N    . ASN   B 1 99  ? 39.865 -26.527 9.138   1.00 15.61 ?  99  ASN   B N    1 
ATOM   5451 C CA   . ASN   B 1 99  ? 40.846 -27.595 9.298   1.00 16.63 ?  99  ASN   B CA   1 
ATOM   5452 C C    . ASN   B 1 99  ? 40.222 -28.673 10.181  1.00 19.09 ?  99  ASN   B C    1 
ATOM   5453 O O    . ASN   B 1 99  ? 40.156 -28.527 11.404  1.00 20.33 ?  99  ASN   B O    1 
ATOM   5454 C CB   . ASN   B 1 99  ? 42.123 -27.037 9.910   1.00 17.12 ?  99  ASN   B CB   1 
ATOM   5455 C CG   . ASN   B 1 99  ? 43.246 -28.047 9.928   1.00 17.96 ?  99  ASN   B CG   1 
ATOM   5456 O OD1  . ASN   B 1 99  ? 43.016 -29.234 10.115  1.00 18.97 ?  99  ASN   B OD1  1 
ATOM   5457 N ND2  . ASN   B 1 99  ? 44.463 -27.584 9.727   1.00 18.26 ?  99  ASN   B ND2  1 
ATOM   5458 H H    . ASN   B 1 99  ? 39.824 -25.986 9.806   1.00 18.73 ?  99  ASN   B H    1 
ATOM   5459 H HA   . ASN   B 1 99  ? 41.051 -27.983 8.434   1.00 19.96 ?  99  ASN   B HA   1 
ATOM   5460 H HB2  . ASN   B 1 99  ? 42.408 -26.272 9.398   1.00 20.54 ?  99  ASN   B HB2  1 
ATOM   5461 H HB3  . ASN   B 1 99  ? 41.933 -26.774 10.829  1.00 20.54 ?  99  ASN   B HB3  1 
ATOM   5462 H HD21 . ASN   B 1 99  ? 45.132 -28.123 9.728   1.00 21.91 ?  99  ASN   B HD21 1 
ATOM   5463 H HD22 . ASN   B 1 99  ? 44.580 -26.745 9.600   1.00 21.91 ?  99  ASN   B HD22 1 
ATOM   5464 N N    A VAL   B 1 100 ? 39.744 -29.750 9.552   0.40 21.26 ?  100 VAL   B N    1 
ATOM   5465 N N    B VAL   B 1 100 ? 39.749 -29.749 9.547   0.60 21.12 ?  100 VAL   B N    1 
ATOM   5466 C CA   A VAL   B 1 100 ? 39.128 -30.837 10.310  0.40 23.74 ?  100 VAL   B CA   1 
ATOM   5467 C CA   B VAL   B 1 100 ? 39.129 -30.849 10.284  0.60 23.70 ?  100 VAL   B CA   1 
ATOM   5468 C C    A VAL   B 1 100 ? 40.141 -31.488 11.241  0.40 24.59 ?  100 VAL   B C    1 
ATOM   5469 C C    B VAL   B 1 100 ? 40.132 -31.517 11.216  0.60 24.38 ?  100 VAL   B C    1 
ATOM   5470 O O    A VAL   B 1 100 ? 39.787 -31.944 12.335  0.40 25.31 ?  100 VAL   B O    1 
ATOM   5471 O O    B VAL   B 1 100 ? 39.761 -32.022 12.283  0.60 25.12 ?  100 VAL   B O    1 
ATOM   5472 C CB   A VAL   B 1 100 ? 38.476 -31.859 9.357   0.40 25.53 ?  100 VAL   B CB   1 
ATOM   5473 C CB   B VAL   B 1 100 ? 38.494 -31.852 9.300   0.60 25.88 ?  100 VAL   B CB   1 
ATOM   5474 C CG1  A VAL   B 1 100 ? 37.998 -33.082 10.128  0.40 26.32 ?  100 VAL   B CG1  1 
ATOM   5475 C CG1  B VAL   B 1 100 ? 38.031 -33.105 10.030  0.60 26.90 ?  100 VAL   B CG1  1 
ATOM   5476 C CG2  A VAL   B 1 100 ? 37.317 -31.218 8.609   0.40 26.07 ?  100 VAL   B CG2  1 
ATOM   5477 C CG2  B VAL   B 1 100 ? 37.330 -31.203 8.566   0.60 26.47 ?  100 VAL   B CG2  1 
ATOM   5478 H H    A VAL   B 1 100 ? 39.764 -29.873 8.700   0.40 25.51 ?  100 VAL   B H    1 
ATOM   5479 H H    B VAL   B 1 100 ? 39.772 -29.862 8.692   0.60 25.34 ?  100 VAL   B H    1 
ATOM   5480 H HA   A VAL   B 1 100 ? 38.417 -30.467 10.857  0.40 28.49 ?  100 VAL   B HA   1 
ATOM   5481 H HA   B VAL   B 1 100 ? 38.411 -30.490 10.828  0.60 28.44 ?  100 VAL   B HA   1 
ATOM   5482 H HB   A VAL   B 1 100 ? 39.131 -32.152 8.705   0.40 30.63 ?  100 VAL   B HB   1 
ATOM   5483 H HB   B VAL   B 1 100 ? 39.155 -32.117 8.641   0.60 31.06 ?  100 VAL   B HB   1 
ATOM   5484 H HG11 A VAL   B 1 100 ? 37.392 -33.592 9.566   0.40 31.58 ?  100 VAL   B HG11 1 
ATOM   5485 H HG11 B VAL   B 1 100 ? 37.433 -33.606 9.451   0.60 32.27 ?  100 VAL   B HG11 1 
ATOM   5486 H HG12 A VAL   B 1 100 ? 38.763 -33.630 10.366  0.40 31.58 ?  100 VAL   B HG12 1 
ATOM   5487 H HG12 B VAL   B 1 100 ? 38.802 -33.650 10.252  0.60 32.27 ?  100 VAL   B HG12 1 
ATOM   5488 H HG13 A VAL   B 1 100 ? 37.535 -32.791 10.929  0.40 31.58 ?  100 VAL   B HG13 1 
ATOM   5489 H HG13 B VAL   B 1 100 ? 37.562 -32.845 10.839  0.60 32.27 ?  100 VAL   B HG13 1 
ATOM   5490 H HG21 A VAL   B 1 100 ? 36.921 -31.876 8.016   0.40 31.29 ?  100 VAL   B HG21 1 
ATOM   5491 H HG21 B VAL   B 1 100 ? 36.940 -31.850 7.957   0.60 31.77 ?  100 VAL   B HG21 1 
ATOM   5492 H HG22 A VAL   B 1 100 ? 36.657 -30.914 9.253   0.40 31.29 ?  100 VAL   B HG22 1 
ATOM   5493 H HG22 B VAL   B 1 100 ? 36.668 -30.920 9.217   0.60 31.77 ?  100 VAL   B HG22 1 
ATOM   5494 H HG23 A VAL   B 1 100 ? 37.649 -30.467 8.096   0.40 31.29 ?  100 VAL   B HG23 1 
ATOM   5495 H HG23 B VAL   B 1 100 ? 37.658 -30.437 8.071   0.60 31.77 ?  100 VAL   B HG23 1 
ATOM   5496 N N    . ASN   B 1 101 ? 41.410 -31.549 10.828  1.00 25.16 ?  101 ASN   B N    1 
ATOM   5497 C CA   . ASN   B 1 101 ? 42.448 -32.099 11.700  1.00 26.87 ?  101 ASN   B CA   1 
ATOM   5498 C C    . ASN   B 1 101 ? 42.653 -31.263 12.957  1.00 29.30 ?  101 ASN   B C    1 
ATOM   5499 O O    . ASN   B 1 101 ? 43.286 -31.740 13.909  1.00 30.73 ?  101 ASN   B O    1 
ATOM   5500 C CB   . ASN   B 1 101 ? 43.767 -32.241 10.936  1.00 26.79 ?  101 ASN   B CB   1 
ATOM   5501 C CG   . ASN   B 1 101 ? 43.739 -33.379 9.935   1.00 26.37 ?  101 ASN   B CG   1 
ATOM   5502 O OD1  . ASN   B 1 101 ? 43.041 -34.366 10.129  1.00 27.01 ?  101 ASN   B OD1  1 
ATOM   5503 N ND2  . ASN   B 1 101 ? 44.486 -33.237 8.849   1.00 25.84 ?  101 ASN   B ND2  1 
ATOM   5504 H H    A ASN   B 1 101 ? 41.683 -31.293 10.053  0.40 30.19 ?  101 ASN   B H    1 
ATOM   5505 H H    B ASN   B 1 101 ? 41.692 -31.272 10.064  0.60 30.19 ?  101 ASN   B H    1 
ATOM   5506 H HA   . ASN   B 1 101 ? 42.173 -32.979 11.982  1.00 32.24 ?  101 ASN   B HA   1 
ATOM   5507 H HB2  . ASN   B 1 101 ? 43.950 -31.424 10.449  1.00 32.15 ?  101 ASN   B HB2  1 
ATOM   5508 H HB3  . ASN   B 1 101 ? 44.479 -32.418 11.570  1.00 32.15 ?  101 ASN   B HB3  1 
ATOM   5509 H HD21 . ASN   B 1 101 ? 44.500 -33.859 8.255   1.00 31.01 ?  101 ASN   B HD21 1 
ATOM   5510 H HD22 . ASN   B 1 101 ? 44.955 -32.527 8.743   1.00 31.01 ?  101 ASN   B HD22 1 
ATOM   5511 N N    . LYS   B 1 102 ? 42.147 -30.028 12.974  1.00 31.72 ?  102 LYS   B N    1 
ATOM   5512 C CA   . LYS   B 1 102 ? 42.115 -29.190 14.166  1.00 34.32 ?  102 LYS   B CA   1 
ATOM   5513 C C    . LYS   B 1 102 ? 40.732 -29.146 14.805  1.00 33.58 ?  102 LYS   B C    1 
ATOM   5514 O O    . LYS   B 1 102 ? 40.508 -28.341 15.713  1.00 34.59 ?  102 LYS   B O    1 
ATOM   5515 C CB   . LYS   B 1 102 ? 42.544 -27.761 13.828  1.00 38.13 ?  102 LYS   B CB   1 
ATOM   5516 C CG   . LYS   B 1 102 ? 44.000 -27.580 13.442  1.00 41.51 ?  102 LYS   B CG   1 
ATOM   5517 C CD   . LYS   B 1 102 ? 44.205 -26.167 12.914  1.00 45.08 ?  102 LYS   B CD   1 
ATOM   5518 C CE   . LYS   B 1 102 ? 45.669 -25.792 12.799  1.00 47.52 ?  102 LYS   B CE   1 
ATOM   5519 N NZ   . LYS   B 1 102 ? 45.818 -24.384 12.325  1.00 48.95 ?  102 LYS   B NZ   1 
ATOM   5520 H H    . LYS   B 1 102 ? 41.804 -29.640 12.283  1.00 38.06 ?  102 LYS   B H    1 
ATOM   5521 H HA   . LYS   B 1 102 ? 42.742 -29.543 14.815  1.00 41.18 ?  102 LYS   B HA   1 
ATOM   5522 H HB2  . LYS   B 1 102 ? 42.007 -27.446 13.086  1.00 45.75 ?  102 LYS   B HB2  1 
ATOM   5523 H HB3  . LYS   B 1 102 ? 42.381 -27.201 14.604  1.00 45.75 ?  102 LYS   B HB3  1 
ATOM   5524 H HG2  . LYS   B 1 102 ? 44.565 -27.706 14.221  1.00 49.81 ?  102 LYS   B HG2  1 
ATOM   5525 H HG3  . LYS   B 1 102 ? 44.235 -28.210 12.743  1.00 49.81 ?  102 LYS   B HG3  1 
ATOM   5526 H HD2  . LYS   B 1 102 ? 43.807 -26.098 12.032  1.00 54.09 ?  102 LYS   B HD2  1 
ATOM   5527 H HD3  . LYS   B 1 102 ? 43.780 -25.539 13.519  1.00 54.09 ?  102 LYS   B HD3  1 
ATOM   5528 H HE2  . LYS   B 1 102 ? 46.091 -25.869 13.669  1.00 57.02 ?  102 LYS   B HE2  1 
ATOM   5529 H HE3  . LYS   B 1 102 ? 46.103 -26.378 12.159  1.00 57.02 ?  102 LYS   B HE3  1 
ATOM   5530 H HZ1  . LYS   B 1 102 ? 46.679 -24.174 12.261  1.00 58.73 ?  102 LYS   B HZ1  1 
ATOM   5531 H HZ2  . LYS   B 1 102 ? 45.436 -24.291 11.526  1.00 58.73 ?  102 LYS   B HZ2  1 
ATOM   5532 H HZ3  . LYS   B 1 102 ? 45.426 -23.827 12.899  1.00 58.73 ?  102 LYS   B HZ3  1 
ATOM   5533 N N    . GLY   B 1 103 ? 39.795 -29.963 14.332  1.00 32.75 ?  103 GLY   B N    1 
ATOM   5534 C CA   . GLY   B 1 103 ? 38.467 -30.017 14.909  1.00 32.35 ?  103 GLY   B CA   1 
ATOM   5535 C C    . GLY   B 1 103 ? 37.518 -28.931 14.454  1.00 31.14 ?  103 GLY   B C    1 
ATOM   5536 O O    . GLY   B 1 103 ? 36.420 -28.819 15.013  1.00 32.07 ?  103 GLY   B O    1 
ATOM   5537 H H    . GLY   B 1 103 ? 39.907 -30.494 13.668  1.00 39.29 ?  103 GLY   B H    1 
ATOM   5538 H HA2  . GLY   B 1 103 ? 38.066 -30.872 14.690  1.00 38.81 ?  103 GLY   B HA2  1 
ATOM   5539 H HA3  . GLY   B 1 103 ? 38.541 -29.960 15.875  1.00 38.81 ?  103 GLY   B HA3  1 
ATOM   5540 N N    A GLU   B 1 104 ? 37.910 -28.119 13.477  0.40 30.28 ?  104 GLU   B N    1 
ATOM   5541 N N    B GLU   B 1 104 ? 37.884 -28.146 13.446  0.60 29.48 ?  104 GLU   B N    1 
ATOM   5542 C CA   A GLU   B 1 104 ? 37.071 -27.017 13.033  0.40 29.26 ?  104 GLU   B CA   1 
ATOM   5543 C CA   B GLU   B 1 104 ? 37.020 -27.070 12.985  0.60 27.85 ?  104 GLU   B CA   1 
ATOM   5544 C C    A GLU   B 1 104 ? 35.886 -27.534 12.222  0.40 29.55 ?  104 GLU   B C    1 
ATOM   5545 C C    B GLU   B 1 104 ? 35.856 -27.624 12.162  0.60 28.14 ?  104 GLU   B C    1 
ATOM   5546 O O    A GLU   B 1 104 ? 35.930 -28.615 11.627  0.40 29.95 ?  104 GLU   B O    1 
ATOM   5547 O O    B GLU   B 1 104 ? 35.926 -28.714 11.587  0.60 28.99 ?  104 GLU   B O    1 
ATOM   5548 C CB   A GLU   B 1 104 ? 37.902 -26.018 12.225  0.40 28.25 ?  104 GLU   B CB   1 
ATOM   5549 C CB   B GLU   B 1 104 ? 37.834 -26.045 12.195  0.60 26.48 ?  104 GLU   B CB   1 
ATOM   5550 C CG   A GLU   B 1 104 ? 39.022 -25.387 13.047  0.40 27.46 ?  104 GLU   B CG   1 
ATOM   5551 C CG   B GLU   B 1 104 ? 38.929 -25.417 13.045  0.60 25.20 ?  104 GLU   B CG   1 
ATOM   5552 C CD   A GLU   B 1 104 ? 39.936 -24.496 12.233  0.40 26.83 ?  104 GLU   B CD   1 
ATOM   5553 C CD   B GLU   B 1 104 ? 39.881 -24.533 12.269  0.60 23.88 ?  104 GLU   B CD   1 
ATOM   5554 O OE1  A GLU   B 1 104 ? 39.894 -24.560 10.986  0.40 25.86 ?  104 GLU   B OE1  1 
ATOM   5555 O OE1  B GLU   B 1 104 ? 39.880 -24.568 11.021  0.60 21.90 ?  104 GLU   B OE1  1 
ATOM   5556 O OE2  A GLU   B 1 104 ? 40.705 -23.730 12.849  0.40 27.09 -1 104 GLU   B OE2  1 
ATOM   5557 O OE2  B GLU   B 1 104 ? 40.647 -23.801 12.929  0.60 24.12 -1 104 GLU   B OE2  1 
ATOM   5558 H H    A GLU   B 1 104 ? 38.661 -28.180 13.063  0.40 36.33 ?  104 GLU   B H    1 
ATOM   5559 H H    B GLU   B 1 104 ? 38.628 -28.212 13.018  0.60 35.37 ?  104 GLU   B H    1 
ATOM   5560 H HA   A GLU   B 1 104 ? 36.726 -26.552 13.809  0.40 35.11 ?  104 GLU   B HA   1 
ATOM   5561 H HA   B GLU   B 1 104 ? 36.647 -26.617 13.758  0.60 33.42 ?  104 GLU   B HA   1 
ATOM   5562 H HB2  A GLU   B 1 104 ? 38.307 -26.472 11.471  0.40 33.90 ?  104 GLU   B HB2  1 
ATOM   5563 H HB2  B GLU   B 1 104 ? 38.251 -26.483 11.438  0.60 31.77 ?  104 GLU   B HB2  1 
ATOM   5564 H HB3  A GLU   B 1 104 ? 37.325 -25.302 11.913  0.40 33.90 ?  104 GLU   B HB3  1 
ATOM   5565 H HB3  B GLU   B 1 104 ? 37.244 -25.337 11.889  0.60 31.77 ?  104 GLU   B HB3  1 
ATOM   5566 H HG2  A GLU   B 1 104 ? 38.633 -24.845 13.752  0.40 32.95 ?  104 GLU   B HG2  1 
ATOM   5567 H HG2  B GLU   B 1 104 ? 38.518 -24.873 13.737  0.60 30.23 ?  104 GLU   B HG2  1 
ATOM   5568 H HG3  A GLU   B 1 104 ? 39.567 -26.089 13.434  0.40 32.95 ?  104 GLU   B HG3  1 
ATOM   5569 H HG3  B GLU   B 1 104 ? 39.455 -26.121 13.454  0.60 30.23 ?  104 GLU   B HG3  1 
ATOM   5570 N N    A ASP   B 1 105 ? 34.814 -26.745 12.211  0.40 29.13 ?  105 ASP   B N    1 
ATOM   5571 N N    B ASP   B 1 105 ? 34.770 -26.852 12.118  0.60 27.15 ?  105 ASP   B N    1 
ATOM   5572 C CA   A ASP   B 1 105 ? 33.540 -27.193 11.663  0.40 29.47 ?  105 ASP   B CA   1 
ATOM   5573 C CA   B ASP   B 1 105 ? 33.504 -27.329 11.574  0.60 27.38 ?  105 ASP   B CA   1 
ATOM   5574 C C    A ASP   B 1 105 ? 33.607 -27.253 10.141  0.40 28.03 ?  105 ASP   B C    1 
ATOM   5575 C C    B ASP   B 1 105 ? 33.554 -27.344 10.051  0.60 25.68 ?  105 ASP   B C    1 
ATOM   5576 O O    A ASP   B 1 105 ? 33.810 -26.231 9.478   0.40 27.46 ?  105 ASP   B O    1 
ATOM   5577 O O    B ASP   B 1 105 ? 33.695 -26.292 9.416   0.60 24.79 ?  105 ASP   B O    1 
ATOM   5578 C CB   A ASP   B 1 105 ? 32.429 -26.245 12.109  0.40 31.17 ?  105 ASP   B CB   1 
ATOM   5579 C CB   B ASP   B 1 105 ? 32.359 -26.441 12.059  0.60 29.76 ?  105 ASP   B CB   1 
ATOM   5580 C CG   A ASP   B 1 105 ? 31.056 -26.701 11.660  0.40 32.82 ?  105 ASP   B CG   1 
ATOM   5581 C CG   B ASP   B 1 105 ? 30.993 -27.005 11.710  0.60 31.69 ?  105 ASP   B CG   1 
ATOM   5582 O OD1  A ASP   B 1 105 ? 30.936 -27.833 11.146  0.40 33.09 ?  105 ASP   B OD1  1 
ATOM   5583 O OD1  B ASP   B 1 105 ? 30.930 -28.017 10.981  0.60 31.87 ?  105 ASP   B OD1  1 
ATOM   5584 O OD2  A ASP   B 1 105 ? 30.095 -25.917 11.812  0.40 33.74 -1 105 ASP   B OD2  1 
ATOM   5585 O OD2  B ASP   B 1 105 ? 29.979 -26.440 12.174  0.60 32.48 -1 105 ASP   B OD2  1 
ATOM   5586 H H    A ASP   B 1 105 ? 34.803 -25.942 12.517  0.40 34.95 ?  105 ASP   B H    1 
ATOM   5587 H H    B ASP   B 1 105 ? 34.744 -26.039 12.396  0.60 32.58 ?  105 ASP   B H    1 
ATOM   5588 H HA   A ASP   B 1 105 ? 33.339 -28.081 11.996  0.40 35.36 ?  105 ASP   B HA   1 
ATOM   5589 H HA   B ASP   B 1 105 ? 33.340 -28.233 11.880  0.60 32.85 ?  105 ASP   B HA   1 
ATOM   5590 H HB2  A ASP   B 1 105 ? 32.443 -26.177 13.079  0.40 37.40 ?  105 ASP   B HB2  1 
ATOM   5591 H HB2  B ASP   B 1 105 ? 32.414 -26.355 13.024  0.60 35.72 ?  105 ASP   B HB2  1 
ATOM   5592 H HB3  A ASP   B 1 105 ? 32.575 -25.375 11.714  0.40 37.40 ?  105 ASP   B HB3  1 
ATOM   5593 H HB3  B ASP   B 1 105 ? 32.438 -25.567 11.644  0.60 35.72 ?  105 ASP   B HB3  1 
ATOM   5594 N N    A ILE   B 1 106 ? 33.421 -28.456 9.590   0.40 27.33 ?  106 ILE   B N    1 
ATOM   5595 N N    B ILE   B 1 106 ? 33.411 -28.538 9.467   0.60 25.39 ?  106 ILE   B N    1 
ATOM   5596 C CA   A ILE   B 1 106 ? 33.425 -28.646 8.144   0.40 26.55 ?  106 ILE   B CA   1 
ATOM   5597 C CA   B ILE   B 1 106 ? 33.401 -28.690 8.017   0.60 24.71 ?  106 ILE   B CA   1 
ATOM   5598 C C    A ILE   B 1 106 ? 32.331 -27.831 7.461   0.40 25.71 ?  106 ILE   B C    1 
ATOM   5599 C C    B ILE   B 1 106 ? 32.298 -27.862 7.369   0.60 23.66 ?  106 ILE   B C    1 
ATOM   5600 O O    A ILE   B 1 106 ? 32.446 -27.515 6.273   0.40 25.23 ?  106 ILE   B O    1 
ATOM   5601 O O    B ILE   B 1 106 ? 32.382 -27.542 6.180   0.60 22.61 ?  106 ILE   B O    1 
ATOM   5602 C CB   A ILE   B 1 106 ? 33.320 -30.155 7.819   0.40 26.88 ?  106 ILE   B CB   1 
ATOM   5603 C CB   B ILE   B 1 106 ? 33.297 -30.190 7.655   0.60 25.81 ?  106 ILE   B CB   1 
ATOM   5604 C CG1  A ILE   B 1 106 ? 33.546 -30.411 6.327   0.40 26.76 ?  106 ILE   B CG1  1 
ATOM   5605 C CG1  B ILE   B 1 106 ? 33.592 -30.423 6.173   0.60 26.41 ?  106 ILE   B CG1  1 
ATOM   5606 C CG2  A ILE   B 1 106 ? 31.967 -30.704 8.249   0.40 27.38 ?  106 ILE   B CG2  1 
ATOM   5607 C CG2  B ILE   B 1 106 ? 31.920 -30.738 8.012   0.60 26.44 ?  106 ILE   B CG2  1 
ATOM   5608 C CD1  A ILE   B 1 106 ? 34.907 -29.974 5.837   0.40 26.54 ?  106 ILE   B CD1  1 
ATOM   5609 C CD1  B ILE   B 1 106 ? 34.965 -29.957 5.756   0.60 26.42 ?  106 ILE   B CD1  1 
ATOM   5610 H H    A ILE   B 1 106 ? 33.298 -29.177 10.038  0.40 32.79 ?  106 ILE   B H    1 
ATOM   5611 H H    B ILE   B 1 106 ? 33.324 -29.275 9.894   0.60 30.47 ?  106 ILE   B H    1 
ATOM   5612 H HA   A ILE   B 1 106 ? 34.272 -28.332 7.801   0.40 31.86 ?  106 ILE   B HA   1 
ATOM   5613 H HA   B ILE   B 1 106 ? 34.242 -28.361 7.674   0.60 29.65 ?  106 ILE   B HA   1 
ATOM   5614 H HB   A ILE   B 1 106 ? 34.010 -30.625 8.315   0.40 32.26 ?  106 ILE   B HB   1 
ATOM   5615 H HB   B ILE   B 1 106 ? 33.957 -30.674 8.175   0.60 30.97 ?  106 ILE   B HB   1 
ATOM   5616 H HG12 A ILE   B 1 106 ? 33.466 -31.364 6.158   0.40 32.11 ?  106 ILE   B HG12 1 
ATOM   5617 H HG12 B ILE   B 1 106 ? 33.536 -31.375 5.987   0.60 31.69 ?  106 ILE   B HG12 1 
ATOM   5618 H HG13 A ILE   B 1 106 ? 32.877 -29.931 5.817   0.40 32.11 ?  106 ILE   B HG13 1 
ATOM   5619 H HG13 B ILE   B 1 106 ? 32.940 -29.946 5.640   0.60 31.69 ?  106 ILE   B HG13 1 
ATOM   5620 H HG21 A ILE   B 1 106 ? 31.977 -31.670 8.163   0.40 32.86 ?  106 ILE   B HG21 1 
ATOM   5621 H HG21 B ILE   B 1 106 ? 31.937 -31.706 7.942   0.60 31.73 ?  106 ILE   B HG21 1 
ATOM   5622 H HG22 A ILE   B 1 106 ? 31.805 -30.456 9.173   0.40 32.86 ?  106 ILE   B HG22 1 
ATOM   5623 H HG22 B ILE   B 1 106 ? 31.704 -30.478 8.922   0.60 31.73 ?  106 ILE   B HG22 1 
ATOM   5624 H HG23 A ILE   B 1 106 ? 31.277 -30.329 7.680   0.40 32.86 ?  106 ILE   B HG23 1 
ATOM   5625 H HG23 B ILE   B 1 106 ? 31.263 -30.374 7.400   0.60 31.73 ?  106 ILE   B HG23 1 
ATOM   5626 H HD11 A ILE   B 1 106 ? 35.071 -30.370 4.968   0.40 31.84 ?  106 ILE   B HD11 1 
ATOM   5627 H HD11 B ILE   B 1 106 ? 35.197 -30.374 4.913   0.60 31.70 ?  106 ILE   B HD11 1 
ATOM   5628 H HD12 A ILE   B 1 106 ? 34.923 -29.006 5.767   0.40 31.84 ?  106 ILE   B HD12 1 
ATOM   5629 H HD12 B ILE   B 1 106 ? 34.954 -28.992 5.655   0.60 31.70 ?  106 ILE   B HD12 1 
ATOM   5630 H HD13 A ILE   B 1 106 ? 35.581 -30.272 6.469   0.40 31.84 ?  106 ILE   B HD13 1 
ATOM   5631 H HD13 B ILE   B 1 106 ? 35.606 -30.212 6.438   0.60 31.70 ?  106 ILE   B HD13 1 
ATOM   5632 N N    A GLN   B 1 107 ? 31.266 -27.482 8.188   0.40 25.71 ?  107 GLN   B N    1 
ATOM   5633 N N    B GLN   B 1 107 ? 31.268 -27.485 8.129   0.60 24.23 ?  107 GLN   B N    1 
ATOM   5634 C CA   A GLN   B 1 107 ? 30.189 -26.683 7.608   0.40 25.71 ?  107 GLN   B CA   1 
ATOM   5635 C CA   B GLN   B 1 107 ? 30.185 -26.681 7.574   0.60 24.78 ?  107 GLN   B CA   1 
ATOM   5636 C C    A GLN   B 1 107 ? 30.689 -25.344 7.073   0.40 23.26 ?  107 GLN   B C    1 
ATOM   5637 C C    B GLN   B 1 107 ? 30.664 -25.315 7.101   0.60 22.72 ?  107 GLN   B C    1 
ATOM   5638 O O    A GLN   B 1 107 ? 30.070 -24.774 6.167   0.40 23.48 ?  107 GLN   B O    1 
ATOM   5639 O O    B GLN   B 1 107 ? 30.001 -24.704 6.259   0.60 23.24 ?  107 GLN   B O    1 
ATOM   5640 C CB   A GLN   B 1 107 ? 29.087 -26.467 8.649   0.40 28.63 ?  107 GLN   B CB   1 
ATOM   5641 C CB   B GLN   B 1 107 ? 29.072 -26.523 8.612   0.60 28.42 ?  107 GLN   B CB   1 
ATOM   5642 C CG   A GLN   B 1 107 ? 27.767 -25.945 8.082   0.40 31.44 ?  107 GLN   B CG   1 
ATOM   5643 C CG   B GLN   B 1 107 ? 27.742 -26.019 8.056   0.60 32.15 ?  107 GLN   B CG   1 
ATOM   5644 C CD   A GLN   B 1 107 ? 27.722 -24.430 7.963   0.40 33.64 ?  107 GLN   B CD   1 
ATOM   5645 C CD   B GLN   B 1 107 ? 27.648 -24.503 8.026   0.60 35.05 ?  107 GLN   B CD   1 
ATOM   5646 O OE1  A GLN   B 1 107 ? 28.563 -23.725 8.523   0.40 34.39 ?  107 GLN   B OE1  1 
ATOM   5647 O OE1  B GLN   B 1 107 ? 28.471 -23.804 8.619   0.60 36.02 ?  107 GLN   B OE1  1 
ATOM   5648 N NE2  A GLN   B 1 107 ? 26.732 -23.923 7.230   0.40 34.31 ?  107 GLN   B NE2  1 
ATOM   5649 N NE2  B GLN   B 1 107 ? 26.635 -23.987 7.335   0.60 35.98 ?  107 GLN   B NE2  1 
ATOM   5650 H H    A GLN   B 1 107 ? 31.138 -27.712 9.003   0.40 30.85 ?  107 GLN   B H    1 
ATOM   5651 H H    B GLN   B 1 107 ? 31.180 -27.664 8.958   0.60 29.08 ?  107 GLN   B H    1 
ATOM   5652 H HA   A GLN   B 1 107 ? 29.800 -27.169 6.865   0.40 30.85 ?  107 GLN   B HA   1 
ATOM   5653 H HA   B GLN   B 1 107 ? 29.812 -27.142 6.806   0.60 29.73 ?  107 GLN   B HA   1 
ATOM   5654 H HB2  A GLN   B 1 107 ? 28.904 -27.314 9.083   0.40 34.36 ?  107 GLN   B HB2  1 
ATOM   5655 H HB2  B GLN   B 1 107 ? 28.908 -27.385 9.016   0.60 34.10 ?  107 GLN   B HB2  1 
ATOM   5656 H HB3  A GLN   B 1 107 ? 29.402 -25.827 9.306   0.40 34.36 ?  107 GLN   B HB3  1 
ATOM   5657 H HB3  B GLN   B 1 107 ? 29.365 -25.894 9.290   0.60 34.10 ?  107 GLN   B HB3  1 
ATOM   5658 H HG2  A GLN   B 1 107 ? 27.632 -26.316 7.197   0.40 37.72 ?  107 GLN   B HG2  1 
ATOM   5659 H HG2  B GLN   B 1 107 ? 27.633 -26.341 7.148   0.60 38.58 ?  107 GLN   B HG2  1 
ATOM   5660 H HG3  A GLN   B 1 107 ? 27.042 -26.221 8.668   0.40 37.72 ?  107 GLN   B HG3  1 
ATOM   5661 H HG3  B GLN   B 1 107 ? 27.020 -26.356 8.614   0.60 38.58 ?  107 GLN   B HG3  1 
ATOM   5662 H HE21 A GLN   B 1 107 ? 26.163 -24.447 6.852   0.40 41.18 ?  107 GLN   B HE21 1 
ATOM   5663 H HE21 B GLN   B 1 107 ? 26.078 -24.506 6.932   0.60 43.17 ?  107 GLN   B HE21 1 
ATOM   5664 H HE22 A GLN   B 1 107 ? 26.658 -23.070 7.134   0.40 41.18 ?  107 GLN   B HE22 1 
ATOM   5665 H HE22 B GLN   B 1 107 ? 26.534 -23.134 7.291   0.60 43.17 ?  107 GLN   B HE22 1 
ATOM   5666 N N    . LEU   B 1 108 ? 31.800 -24.828 7.606   1.00 20.93 ?  108 LEU   B N    1 
ATOM   5667 C CA   . LEU   B 1 108 ? 32.335 -23.530 7.192   1.00 18.27 ?  108 LEU   B CA   1 
ATOM   5668 C C    . LEU   B 1 108 ? 32.985 -23.552 5.818   1.00 16.01 ?  108 LEU   B C    1 
ATOM   5669 O O    . LEU   B 1 108 ? 33.412 -22.492 5.330   1.00 15.33 ?  108 LEU   B O    1 
ATOM   5670 C CB   . LEU   B 1 108 ? 33.340 -23.022 8.223   1.00 18.76 ?  108 LEU   B CB   1 
ATOM   5671 C CG   . LEU   B 1 108 ? 32.715 -22.554 9.534   1.00 20.47 ?  108 LEU   B CG   1 
ATOM   5672 C CD1  . LEU   B 1 108 ? 33.750 -22.505 10.638  1.00 20.57 ?  108 LEU   B CD1  1 
ATOM   5673 C CD2  . LEU   B 1 108 ? 32.090 -21.183 9.341   1.00 21.57 ?  108 LEU   B CD2  1 
ATOM   5674 H H    A LEU   B 1 108 ? 32.261 -25.211 8.216   0.40 25.12 ?  108 LEU   B H    1 
ATOM   5675 H H    B LEU   B 1 108 ? 32.267 -25.225 8.202   0.60 25.12 ?  108 LEU   B H    1 
ATOM   5676 H HA   . LEU   B 1 108 ? 31.605 -22.895 7.153   1.00 21.92 ?  108 LEU   B HA   1 
ATOM   5677 H HB2  . LEU   B 1 108 ? 33.954 -23.739 8.436   1.00 22.50 ?  108 LEU   B HB2  1 
ATOM   5678 H HB3  . LEU   B 1 108 ? 33.821 -22.273 7.846   1.00 22.50 ?  108 LEU   B HB3  1 
ATOM   5679 H HG   . LEU   B 1 108 ? 32.012 -23.170 9.802   1.00 24.57 ?  108 LEU   B HG   1 
ATOM   5680 H HD11 . LEU   B 1 108 ? 33.323 -22.222 11.463  1.00 24.68 ?  108 LEU   B HD11 1 
ATOM   5681 H HD12 . LEU   B 1 108 ? 34.133 -23.388 10.750  1.00 24.68 ?  108 LEU   B HD12 1 
ATOM   5682 H HD13 . LEU   B 1 108 ? 34.443 -21.872 10.392  1.00 24.68 ?  108 LEU   B HD13 1 
ATOM   5683 H HD21 . LEU   B 1 108 ? 31.736 -20.873 10.190  1.00 25.88 ?  108 LEU   B HD21 1 
ATOM   5684 H HD22 . LEU   B 1 108 ? 32.769 -20.570 9.022   1.00 25.88 ?  108 LEU   B HD22 1 
ATOM   5685 H HD23 . LEU   B 1 108 ? 31.373 -21.251 8.691   1.00 25.88 ?  108 LEU   B HD23 1 
ATOM   5686 N N    . LEU   B 1 109 ? 33.048 -24.721 5.185   1.00 14.86 ?  109 LEU   B N    1 
ATOM   5687 C CA   . LEU   B 1 109 ? 33.676 -24.831 3.877   1.00 14.20 ?  109 LEU   B CA   1 
ATOM   5688 C C    . LEU   B 1 109 ? 32.913 -24.044 2.820   1.00 13.30 ?  109 LEU   B C    1 
ATOM   5689 O O    . LEU   B 1 109 ? 33.530 -23.457 1.924   1.00 13.09 ?  109 LEU   B O    1 
ATOM   5690 C CB   . LEU   B 1 109 ? 33.780 -26.304 3.494   1.00 14.02 ?  109 LEU   B CB   1 
ATOM   5691 C CG   . LEU   B 1 109 ? 34.577 -26.635 2.234   1.00 13.91 ?  109 LEU   B CG   1 
ATOM   5692 C CD1  . LEU   B 1 109 ? 35.955 -25.981 2.255   1.00 13.40 ?  109 LEU   B CD1  1 
ATOM   5693 C CD2  . LEU   B 1 109 ? 34.714 -28.140 2.085   1.00 14.62 ?  109 LEU   B CD2  1 
ATOM   5694 H H    . LEU   B 1 109 ? 32.742 -25.462 5.487   1.00 17.83 ?  109 LEU   B H    1 
ATOM   5695 H HA   . LEU   B 1 109 ? 34.572 -24.468 3.922   1.00 17.03 ?  109 LEU   B HA   1 
ATOM   5696 H HB2  . LEU   B 1 109 ? 34.203 -26.780 4.225   1.00 16.82 ?  109 LEU   B HB2  1 
ATOM   5697 H HB3  . LEU   B 1 109 ? 32.885 -26.653 3.361   1.00 16.82 ?  109 LEU   B HB3  1 
ATOM   5698 H HG   . LEU   B 1 109 ? 34.099 -26.309 1.454   1.00 16.69 ?  109 LEU   B HG   1 
ATOM   5699 H HD11 . LEU   B 1 109 ? 36.493 -26.352 1.535   1.00 16.08 ?  109 LEU   B HD11 1 
ATOM   5700 H HD12 . LEU   B 1 109 ? 35.851 -25.028 2.132   1.00 16.08 ?  109 LEU   B HD12 1 
ATOM   5701 H HD13 . LEU   B 1 109 ? 36.376 -26.168 3.108   1.00 16.08 ?  109 LEU   B HD13 1 
ATOM   5702 H HD21 . LEU   B 1 109 ? 35.290 -28.335 1.326   1.00 17.54 ?  109 LEU   B HD21 1 
ATOM   5703 H HD22 . LEU   B 1 109 ? 35.103 -28.505 2.894   1.00 17.54 ?  109 LEU   B HD22 1 
ATOM   5704 H HD23 . LEU   B 1 109 ? 33.835 -28.527 1.937   1.00 17.54 ?  109 LEU   B HD23 1 
ATOM   5705 N N    . LYS   B 1 110 ? 31.580 -24.008 2.901   1.00 13.15 ?  110 LYS   B N    1 
ATOM   5706 C CA   . LYS   B 1 110 ? 30.827 -23.249 1.911   1.00 13.04 ?  110 LYS   B CA   1 
ATOM   5707 C C    . LYS   B 1 110 ? 31.168 -21.764 2.001   1.00 12.47 ?  110 LYS   B C    1 
ATOM   5708 O O    . LYS   B 1 110 ? 31.427 -21.118 0.983   1.00 12.43 ?  110 LYS   B O    1 
ATOM   5709 C CB   . LYS   B 1 110 ? 29.323 -23.499 2.059   1.00 13.74 ?  110 LYS   B CB   1 
ATOM   5710 C CG   . LYS   B 1 110 ? 28.510 -22.868 0.934   1.00 14.24 ?  110 LYS   B CG   1 
ATOM   5711 C CD   . LYS   B 1 110 ? 27.050 -23.298 0.957   1.00 14.46 ?  110 LYS   B CD   1 
ATOM   5712 C CE   . LYS   B 1 110 ? 26.293 -22.773 -0.262  1.00 15.53 ?  110 LYS   B CE   1 
ATOM   5713 N NZ   . LYS   B 1 110 ? 26.627 -23.508 -1.510  1.00 15.46 ?  110 LYS   B NZ   1 
ATOM   5714 H H    . LYS   B 1 110 ? 31.107 -24.411 3.490   1.00 15.77 ?  110 LYS   B H    1 
ATOM   5715 H HA   . LYS   B 1 110 ? 31.083 -23.550 1.022   1.00 15.65 ?  110 LYS   B HA   1 
ATOM   5716 H HB2  . LYS   B 1 110 ? 29.161 -24.461 2.043   1.00 16.49 ?  110 LYS   B HB2  1 
ATOM   5717 H HB3  . LYS   B 1 110 ? 29.019 -23.130 2.900   1.00 16.49 ?  110 LYS   B HB3  1 
ATOM   5718 H HG2  . LYS   B 1 110 ? 28.532 -21.904 1.030   1.00 17.09 ?  110 LYS   B HG2  1 
ATOM   5719 H HG3  . LYS   B 1 110 ? 28.882 -23.131 0.081   1.00 17.09 ?  110 LYS   B HG3  1 
ATOM   5720 H HD2  . LYS   B 1 110 ? 26.997 -24.273 0.951   1.00 17.35 ?  110 LYS   B HD2  1 
ATOM   5721 H HD3  . LYS   B 1 110 ? 26.617 -22.952 1.757   1.00 17.35 ?  110 LYS   B HD3  1 
ATOM   5722 H HE2  . LYS   B 1 110 ? 25.338 -22.862 -0.110  1.00 18.64 ?  110 LYS   B HE2  1 
ATOM   5723 H HE3  . LYS   B 1 110 ? 26.522 -21.841 -0.396  1.00 18.64 ?  110 LYS   B HE3  1 
ATOM   5724 H HZ1  . LYS   B 1 110 ? 26.173 -23.177 -2.196  1.00 18.55 ?  110 LYS   B HZ1  1 
ATOM   5725 H HZ2  . LYS   B 1 110 ? 27.500 -23.444 -1.679  1.00 18.55 ?  110 LYS   B HZ2  1 
ATOM   5726 H HZ3  . LYS   B 1 110 ? 26.420 -24.374 -1.419  1.00 18.55 ?  110 LYS   B HZ3  1 
ATOM   5727 N N    . SER   B 1 111 ? 31.184 -21.209 3.221   1.00 13.02 ?  111 SER   B N    1 
ATOM   5728 C CA   . SER   B 1 111 ? 31.581 -19.813 3.402   1.00 13.02 ?  111 SER   B CA   1 
ATOM   5729 C C    . SER   B 1 111 ? 32.959 -19.555 2.809   1.00 12.06 ?  111 SER   B C    1 
ATOM   5730 O O    . SER   B 1 111 ? 33.185 -18.526 2.155   1.00 12.61 ?  111 SER   B O    1 
ATOM   5731 C CB   . SER   B 1 111 ? 31.585 -19.454 4.888   1.00 14.15 ?  111 SER   B CB   1 
ATOM   5732 O OG   . SER   B 1 111 ? 30.279 -19.432 5.417   1.00 15.58 ?  111 SER   B OG   1 
ATOM   5733 H H    . SER   B 1 111 ? 30.987 -21.627 3.946   1.00 15.62 ?  111 SER   B H    1 
ATOM   5734 H HA   . SER   B 1 111 ? 30.949 -19.244 2.954   1.00 15.63 ?  111 SER   B HA   1 
ATOM   5735 H HB2  . SER   B 1 111 ? 32.106 -20.117 5.375   1.00 16.98 ?  111 SER   B HB2  1 
ATOM   5736 H HB3  . SER   B 1 111 ? 31.975 -18.580 5.003   1.00 16.98 ?  111 SER   B HB3  1 
ATOM   5737 H HG   . SER   B 1 111 ? 30.298 -19.241 6.242   1.00 18.70 ?  111 SER   B HG   1 
ATOM   5738 N N    . ALA   B 1 112 ? 33.898 -20.472 3.035   1.00 12.24 ?  112 ALA   B N    1 
ATOM   5739 C CA   . ALA   B 1 112 ? 35.239 -20.304 2.488   1.00 11.95 ?  112 ALA   B CA   1 
ATOM   5740 C C    . ALA   B 1 112 ? 35.199 -20.209 0.965   1.00 11.29 ?  112 ALA   B C    1 
ATOM   5741 O O    . ALA   B 1 112 ? 35.829 -19.321 0.373   1.00 11.62 ?  112 ALA   B O    1 
ATOM   5742 C CB   . ALA   B 1 112 ? 36.145 -21.443 2.966   1.00 12.89 ?  112 ALA   B CB   1 
ATOM   5743 H H    . ALA   B 1 112 ? 33.788 -21.193 3.495   1.00 14.69 ?  112 ALA   B H    1 
ATOM   5744 H HA   . ALA   B 1 112 ? 35.610 -19.475 2.824   1.00 14.34 ?  112 ALA   B HA   1 
ATOM   5745 H HB1  . ALA   B 1 112 ? 37.036 -21.311 2.601   1.00 15.47 ?  112 ALA   B HB1  1 
ATOM   5746 H HB2  . ALA   B 1 112 ? 36.187 -21.423 3.939   1.00 15.47 ?  112 ALA   B HB2  1 
ATOM   5747 H HB3  . ALA   B 1 112 ? 35.783 -22.286 2.668   1.00 15.47 ?  112 ALA   B HB3  1 
ATOM   5748 N N    . TYR   B 1 113 ? 34.465 -21.113 0.306   1.00 11.55 ?  113 TYR   B N    1 
ATOM   5749 C CA   . TYR   B 1 113 ? 34.391 -21.061 -1.148  1.00 11.13 ?  113 TYR   B CA   1 
ATOM   5750 C C    . TYR   B 1 113 ? 33.680 -19.811 -1.661  1.00 10.84 ?  113 TYR   B C    1 
ATOM   5751 O O    . TYR   B 1 113 ? 33.947 -19.379 -2.785  1.00 10.98 ?  113 TYR   B O    1 
ATOM   5752 C CB   . TYR   B 1 113 ? 33.718 -22.320 -1.695  1.00 11.76 ?  113 TYR   B CB   1 
ATOM   5753 C CG   . TYR   B 1 113 ? 34.680 -23.468 -1.958  1.00 12.00 ?  113 TYR   B CG   1 
ATOM   5754 C CD1  . TYR   B 1 113 ? 35.671 -23.364 -2.927  1.00 12.43 ?  113 TYR   B CD1  1 
ATOM   5755 C CD2  . TYR   B 1 113 ? 34.584 -24.656 -1.253  1.00 12.17 ?  113 TYR   B CD2  1 
ATOM   5756 C CE1  . TYR   B 1 113 ? 36.554 -24.401 -3.176  1.00 12.46 ?  113 TYR   B CE1  1 
ATOM   5757 C CE2  . TYR   B 1 113 ? 35.450 -25.710 -1.503  1.00 12.27 ?  113 TYR   B CE2  1 
ATOM   5758 C CZ   . TYR   B 1 113 ? 36.433 -25.575 -2.465  1.00 12.38 ?  113 TYR   B CZ   1 
ATOM   5759 O OH   . TYR   B 1 113 ? 37.313 -26.592 -2.746  1.00 13.08 ?  113 TYR   B OH   1 
ATOM   5760 H H    . TYR   B 1 113 ? 34.007 -21.746 0.677   1.00 13.85 ?  113 TYR   B H    1 
ATOM   5761 H HA   . TYR   B 1 113 ? 35.296 -21.045 -1.489  1.00 13.36 ?  113 TYR   B HA   1 
ATOM   5762 H HB2  . TYR   B 1 113 ? 33.061 -22.637 -1.052  1.00 14.12 ?  113 TYR   B HB2  1 
ATOM   5763 H HB3  . TYR   B 1 113 ? 33.279 -22.105 -2.531  1.00 14.12 ?  113 TYR   B HB3  1 
ATOM   5764 H HD1  . TYR   B 1 113 ? 35.758 -22.573 -3.415  1.00 14.91 ?  113 TYR   B HD1  1 
ATOM   5765 H HD2  . TYR   B 1 113 ? 33.918 -24.755 -0.616  1.00 14.60 ?  113 TYR   B HD2  1 
ATOM   5766 H HE1  . TYR   B 1 113 ? 37.213 -24.315 -3.837  1.00 14.95 ?  113 TYR   B HE1  1 
ATOM   5767 H HE2  . TYR   B 1 113 ? 35.368 -26.507 -1.031  1.00 14.73 ?  113 TYR   B HE2  1 
ATOM   5768 H HH   . TYR   B 1 113 ? 37.139 -27.262 -2.269  1.00 15.69 ?  113 TYR   B HH   1 
ATOM   5769 N N    . GLU   B 1 114 ? 32.760 -19.233 -0.882  1.00 11.59 ?  114 GLU   B N    1 
ATOM   5770 C CA   . GLU   B 1 114 ? 32.076 -18.025 -1.342  1.00 11.12 ?  114 GLU   B CA   1 
ATOM   5771 C C    . GLU   B 1 114 ? 33.061 -16.901 -1.641  1.00 11.06 ?  114 GLU   B C    1 
ATOM   5772 O O    . GLU   B 1 114 ? 32.788 -16.043 -2.484  1.00 11.27 ?  114 GLU   B O    1 
ATOM   5773 C CB   . GLU   B 1 114 ? 31.023 -17.596 -0.321  1.00 11.56 ?  114 GLU   B CB   1 
ATOM   5774 C CG   . GLU   B 1 114 ? 29.803 -18.514 -0.389  1.00 11.70 ?  114 GLU   B CG   1 
ATOM   5775 C CD   . GLU   B 1 114 ? 28.783 -18.328 0.720   1.00 12.15 ?  114 GLU   B CD   1 
ATOM   5776 O OE1  . GLU   B 1 114 ? 29.079 -17.708 1.762   1.00 12.19 ?  114 GLU   B OE1  1 
ATOM   5777 O OE2  . GLU   B 1 114 ? 27.660 -18.864 0.553   1.00 13.07 -1 114 GLU   B OE2  1 
ATOM   5778 H H    . GLU   B 1 114 ? 32.514 -19.521 -0.106  1.00 13.90 ?  114 GLU   B H    1 
ATOM   5779 H HA   . GLU   B 1 114 ? 31.615 -18.229 -2.163  1.00 13.34 ?  114 GLU   B HA   1 
ATOM   5780 H HB2  . GLU   B 1 114 ? 31.397 -17.649 0.576   1.00 13.87 ?  114 GLU   B HB2  1 
ATOM   5781 H HB3  . GLU   B 1 114 ? 30.736 -16.692 -0.513  1.00 13.87 ?  114 GLU   B HB3  1 
ATOM   5782 H HG2  . GLU   B 1 114 ? 29.359 -18.362 -1.233  1.00 14.03 ?  114 GLU   B HG2  1 
ATOM   5783 H HG3  . GLU   B 1 114 ? 30.118 -19.434 -0.348  1.00 14.03 ?  114 GLU   B HG3  1 
ATOM   5784 N N    . ASN   B 1 115 ? 34.226 -16.900 -0.988  1.00 10.87 ?  115 ASN   B N    1 
ATOM   5785 C CA   . ASN   B 1 115 ? 35.218 -15.868 -1.287  1.00 10.67 ?  115 ASN   B CA   1 
ATOM   5786 C C    . ASN   B 1 115 ? 35.628 -15.892 -2.750  1.00 10.54 ?  115 ASN   B C    1 
ATOM   5787 O O    . ASN   B 1 115 ? 36.008 -14.852 -3.309  1.00 11.26 ?  115 ASN   B O    1 
ATOM   5788 C CB   . ASN   B 1 115 ? 36.461 -16.044 -0.412  1.00 11.08 ?  115 ASN   B CB   1 
ATOM   5789 C CG   . ASN   B 1 115 ? 36.196 -15.782 1.049   1.00 11.63 ?  115 ASN   B CG   1 
ATOM   5790 O OD1  . ASN   B 1 115 ? 36.207 -14.635 1.494   1.00 13.55 ?  115 ASN   B OD1  1 
ATOM   5791 N ND2  . ASN   B 1 115 ? 36.033 -16.846 1.821   1.00 12.11 ?  115 ASN   B ND2  1 
ATOM   5792 H H    . ASN   B 1 115 ? 34.463 -17.465 -0.378  1.00 13.04 ?  115 ASN   B H    1 
ATOM   5793 H HA   . ASN   B 1 115 ? 34.841 -14.998 -1.095  1.00 12.80 ?  115 ASN   B HA   1 
ATOM   5794 H HB2  . ASN   B 1 115 ? 36.784 -16.955 -0.500  1.00 13.29 ?  115 ASN   B HB2  1 
ATOM   5795 H HB3  . ASN   B 1 115 ? 37.146 -15.422 -0.709  1.00 13.29 ?  115 ASN   B HB3  1 
ATOM   5796 H HD21 . ASN   B 1 115 ? 35.887 -16.747 2.665   1.00 14.52 ?  115 ASN   B HD21 1 
ATOM   5797 H HD22 . ASN   B 1 115 ? 36.047 -17.635 1.480   1.00 14.52 ?  115 ASN   B HD22 1 
ATOM   5798 N N    . PHE   B 1 116 ? 35.596 -17.073 -3.384  1.00 10.44 ?  116 PHE   B N    1 
ATOM   5799 C CA   . PHE   B 1 116 ? 36.026 -17.169 -4.775  1.00 10.84 ?  116 PHE   B CA   1 
ATOM   5800 C C    . PHE   B 1 116 ? 35.124 -16.343 -5.686  1.00 10.69 ?  116 PHE   B C    1 
ATOM   5801 O O    . PHE   B 1 116 ? 35.557 -15.916 -6.762  1.00 11.17 ?  116 PHE   B O    1 
ATOM   5802 C CB   . PHE   B 1 116 ? 35.997 -18.615 -5.293  1.00 10.84 ?  116 PHE   B CB   1 
ATOM   5803 C CG   . PHE   B 1 116 ? 37.070 -19.563 -4.746  1.00 10.40 ?  116 PHE   B CG   1 
ATOM   5804 C CD1  . PHE   B 1 116 ? 37.721 -19.379 -3.537  1.00 11.17 ?  116 PHE   B CD1  1 
ATOM   5805 C CD2  . PHE   B 1 116 ? 37.372 -20.698 -5.483  1.00 10.76 ?  116 PHE   B CD2  1 
ATOM   5806 C CE1  . PHE   B 1 116 ? 38.658 -20.309 -3.092  1.00 11.10 ?  116 PHE   B CE1  1 
ATOM   5807 C CE2  . PHE   B 1 116 ? 38.298 -21.628 -5.043  1.00 10.97 ?  116 PHE   B CE2  1 
ATOM   5808 C CZ   . PHE   B 1 116 ? 38.933 -21.443 -3.853  1.00 10.98 ?  116 PHE   B CZ   1 
ATOM   5809 H H    . PHE   B 1 116 ? 35.337 -17.821 -3.034  1.00 12.53 ?  116 PHE   B H    1 
ATOM   5810 H HA   . PHE   B 1 116 ? 36.932 -16.838 -4.857  1.00 13.01 ?  116 PHE   B HA   1 
ATOM   5811 H HB2  . PHE   B 1 116 ? 35.126 -18.996 -5.072  1.00 13.00 ?  116 PHE   B HB2  1 
ATOM   5812 H HB3  . PHE   B 1 116 ? 36.093 -18.593 -6.258  1.00 13.00 ?  116 PHE   B HB3  1 
ATOM   5813 H HD1  . PHE   B 1 116 ? 37.527 -18.626 -3.018  1.00 13.41 ?  116 PHE   B HD1  1 
ATOM   5814 H HD2  . PHE   B 1 116 ? 36.928 -20.847 -6.288  1.00 12.91 ?  116 PHE   B HD2  1 
ATOM   5815 H HE1  . PHE   B 1 116 ? 39.098 -20.173 -2.283  1.00 13.32 ?  116 PHE   B HE1  1 
ATOM   5816 H HE2  . PHE   B 1 116 ? 38.482 -22.375 -5.560  1.00 13.16 ?  116 PHE   B HE2  1 
ATOM   5817 H HZ   . PHE   B 1 116 ? 39.571 -22.051 -3.563  1.00 13.17 ?  116 PHE   B HZ   1 
ATOM   5818 N N    . ASN   B 1 117 ? 33.856 -16.141 -5.297  1.00 11.15 ?  117 ASN   B N    1 
ATOM   5819 C CA   . ASN   B 1 117 ? 32.909 -15.442 -6.162  1.00 11.09 ?  117 ASN   B CA   1 
ATOM   5820 C C    . ASN   B 1 117 ? 33.226 -13.963 -6.313  1.00 11.37 ?  117 ASN   B C    1 
ATOM   5821 O O    . ASN   B 1 117 ? 32.635 -13.310 -7.174  1.00 12.38 ?  117 ASN   B O    1 
ATOM   5822 C CB   . ASN   B 1 117 ? 31.486 -15.664 -5.671  1.00 11.48 ?  117 ASN   B CB   1 
ATOM   5823 C CG   . ASN   B 1 117 ? 31.039 -17.070 -5.922  1.00 11.62 ?  117 ASN   B CG   1 
ATOM   5824 O OD1  . ASN   B 1 117 ? 31.389 -17.658 -6.948  1.00 12.55 ?  117 ASN   B OD1  1 
ATOM   5825 N ND2  . ASN   B 1 117 ? 30.303 -17.638 -4.984  1.00 11.82 ?  117 ASN   B ND2  1 
ATOM   5826 H H    . ASN   B 1 117 ? 33.537 -16.389 -4.532  1.00 13.38 ?  117 ASN   B H    1 
ATOM   5827 H HA   . ASN   B 1 117 ? 32.974 -15.838 -7.037  1.00 13.31 ?  117 ASN   B HA   1 
ATOM   5828 H HB2  . ASN   B 1 117 ? 31.441 -15.493 -4.713  1.00 13.77 ?  117 ASN   B HB2  1 
ATOM   5829 H HB3  . ASN   B 1 117 ? 30.890 -15.054 -6.141  1.00 13.77 ?  117 ASN   B HB3  1 
ATOM   5830 H HD21 . ASN   B 1 117 ? 30.022 -18.445 -5.086  1.00 14.18 ?  117 ASN   B HD21 1 
ATOM   5831 H HD22 . ASN   B 1 117 ? 30.086 -17.196 -4.277  1.00 14.18 ?  117 ASN   B HD22 1 
ATOM   5832 N N    . GLN   B 1 118 ? 34.163 -13.435 -5.535  1.00 11.37 ?  118 GLN   B N    1 
ATOM   5833 C CA   . GLN   B 1 118 ? 34.589 -12.048 -5.669  1.00 11.73 ?  118 GLN   B CA   1 
ATOM   5834 C C    . GLN   B 1 118 ? 35.655 -11.856 -6.741  1.00 12.15 ?  118 GLN   B C    1 
ATOM   5835 O O    . GLN   B 1 118 ? 36.125 -10.729 -6.930  1.00 13.40 ?  118 GLN   B O    1 
ATOM   5836 C CB   . GLN   B 1 118 ? 35.063 -11.516 -4.315  1.00 12.32 ?  118 GLN   B CB   1 
ATOM   5837 C CG   . GLN   B 1 118 ? 33.978 -11.553 -3.255  1.00 12.23 ?  118 GLN   B CG   1 
ATOM   5838 C CD   . GLN   B 1 118 ? 32.803 -10.650 -3.600  1.00 12.40 ?  118 GLN   B CD   1 
ATOM   5839 O OE1  . GLN   B 1 118 ? 32.988 -9.516  -4.053  1.00 13.22 ?  118 GLN   B OE1  1 
ATOM   5840 N NE2  . GLN   B 1 118 ? 31.590 -11.143 -3.392  1.00 12.27 ?  118 GLN   B NE2  1 
ATOM   5841 H H    . GLN   B 1 118 ? 34.585 -13.861 -4.915  1.00 13.65 ?  118 GLN   B H    1 
ATOM   5842 H HA   . GLN   B 1 118 ? 33.826 -11.521 -5.940  1.00 14.07 ?  118 GLN   B HA   1 
ATOM   5843 H HB2  . GLN   B 1 118 ? 35.809 -12.046 -4.004  1.00 14.79 ?  118 GLN   B HB2  1 
ATOM   5844 H HB3  . GLN   B 1 118 ? 35.343 -10.586 -4.422  1.00 14.79 ?  118 GLN   B HB3  1 
ATOM   5845 H HG2  . GLN   B 1 118 ? 33.652 -12.460 -3.174  1.00 14.67 ?  118 GLN   B HG2  1 
ATOM   5846 H HG3  . GLN   B 1 118 ? 34.353 -11.254 -2.412  1.00 14.67 ?  118 GLN   B HG3  1 
ATOM   5847 H HE21 . GLN   B 1 118 ? 31.500 -11.935 -3.072  1.00 14.72 ?  118 GLN   B HE21 1 
ATOM   5848 H HE22 . GLN   B 1 118 ? 30.902 -10.667 -3.575  1.00 14.72 ?  118 GLN   B HE22 1 
ATOM   5849 N N    . HIS   B 1 119 ? 36.008 -12.914 -7.472  1.00 11.33 ?  119 HIS   B N    1 
ATOM   5850 C CA   . HIS   B 1 119 ? 37.046 -12.864 -8.495  1.00 11.56 ?  119 HIS   B CA   1 
ATOM   5851 C C    . HIS   B 1 119 ? 36.567 -13.596 -9.735  1.00 11.84 ?  119 HIS   B C    1 
ATOM   5852 O O    . HIS   B 1 119 ? 36.060 -14.714 -9.634  1.00 12.32 ?  119 HIS   B O    1 
ATOM   5853 C CB   . HIS   B 1 119 ? 38.331 -13.493 -7.954  1.00 12.33 ?  119 HIS   B CB   1 
ATOM   5854 C CG   . HIS   B 1 119 ? 38.814 -12.799 -6.729  1.00 13.42 ?  119 HIS   B CG   1 
ATOM   5855 N ND1  . HIS   B 1 119 ? 39.602 -11.669 -6.780  1.00 14.84 ?  119 HIS   B ND1  1 
ATOM   5856 C CD2  . HIS   B 1 119 ? 38.527 -13.005 -5.424  1.00 14.22 ?  119 HIS   B CD2  1 
ATOM   5857 C CE1  . HIS   B 1 119 ? 39.810 -11.234 -5.551  1.00 16.17 ?  119 HIS   B CE1  1 
ATOM   5858 N NE2  . HIS   B 1 119 ? 39.159 -12.017 -4.711  1.00 15.84 ?  119 HIS   B NE2  1 
ATOM   5859 H H    . HIS   B 1 119 ? 35.643 -13.696 -7.401  1.00 13.59 ?  119 HIS   B H    1 
ATOM   5860 H HA   . HIS   B 1 119 ? 37.225 -11.940 -8.732  1.00 13.87 ?  119 HIS   B HA   1 
ATOM   5861 H HB2  . HIS   B 1 119 ? 38.164 -14.421 -7.736  1.00 14.79 ?  119 HIS   B HB2  1 
ATOM   5862 H HB3  . HIS   B 1 119 ? 39.025 -13.428 -8.633  1.00 14.79 ?  119 HIS   B HB3  1 
ATOM   5863 H HD2  . HIS   B 1 119 ? 37.996 -13.688 -5.077  1.00 17.06 ?  119 HIS   B HD2  1 
ATOM   5864 H HE1  . HIS   B 1 119 ? 40.337 -10.508 -5.311  1.00 19.41 ?  119 HIS   B HE1  1 
ATOM   5865 H HE2  . HIS   B 1 119 ? 39.166 -11.952 -3.852  1.00 19.01 ?  119 HIS   B HE2  1 
ATOM   5866 N N    . GLU   B 1 120 ? 36.722 -12.978 -10.906 1.00 12.25 ?  120 GLU   B N    1 
ATOM   5867 C CA   . GLU   B 1 120 ? 36.126 -13.562 -12.103 1.00 13.73 ?  120 GLU   B CA   1 
ATOM   5868 C C    . GLU   B 1 120 ? 36.802 -14.863 -12.518 1.00 12.54 ?  120 GLU   B C    1 
ATOM   5869 O O    . GLU   B 1 120 ? 36.140 -15.739 -13.085 1.00 12.82 ?  120 GLU   B O    1 
ATOM   5870 C CB   . GLU   B 1 120 ? 36.136 -12.558 -13.252 1.00 18.76 ?  120 GLU   B CB   1 
ATOM   5871 C CG   . GLU   B 1 120 ? 35.189 -11.388 -13.034 1.00 25.30 ?  120 GLU   B CG   1 
ATOM   5872 C CD   . GLU   B 1 120 ? 35.054 -10.497 -14.254 1.00 32.25 ?  120 GLU   B CD   1 
ATOM   5873 O OE1  . GLU   B 1 120 ? 36.039 -10.362 -15.012 1.00 34.29 ?  120 GLU   B OE1  1 
ATOM   5874 O OE2  . GLU   B 1 120 ? 33.959 -9.932  -14.455 1.00 35.45 -1 120 GLU   B OE2  1 
ATOM   5875 H H    . GLU   B 1 120 ? 37.147 -12.238 -11.029 1.00 14.70 ?  120 GLU   B H    1 
ATOM   5876 H HA   . GLU   B 1 120 ? 35.201 -13.769 -11.909 1.00 16.47 ?  120 GLU   B HA   1 
ATOM   5877 H HB2  . GLU   B 1 120 ? 37.027 -12.198 -13.354 1.00 22.51 ?  120 GLU   B HB2  1 
ATOM   5878 H HB3  . GLU   B 1 120 ? 35.862 -13.008 -14.066 1.00 22.51 ?  120 GLU   B HB3  1 
ATOM   5879 H HG2  . GLU   B 1 120 ? 34.304 -11.730 -12.823 1.00 30.35 ?  120 GLU   B HG2  1 
ATOM   5880 H HG3  . GLU   B 1 120 ? 35.517 -10.845 -12.301 1.00 30.35 ?  120 GLU   B HG3  1 
ATOM   5881 N N    . VAL   B 1 121 ? 38.104 -14.999 -12.263 1.00 12.13 ?  121 VAL   B N    1 
ATOM   5882 C CA   . VAL   B 1 121 ? 38.849 -16.206 -12.613 1.00 12.04 ?  121 VAL   B CA   1 
ATOM   5883 C C    . VAL   B 1 121 ? 39.962 -16.417 -11.592 1.00 11.72 ?  121 VAL   B C    1 
ATOM   5884 O O    . VAL   B 1 121 ? 40.642 -15.464 -11.198 1.00 12.12 ?  121 VAL   B O    1 
ATOM   5885 C CB   . VAL   B 1 121 ? 39.369 -16.152 -14.069 1.00 13.84 ?  121 VAL   B CB   1 
ATOM   5886 C CG1  . VAL   B 1 121 ? 40.241 -14.926 -14.311 1.00 14.95 ?  121 VAL   B CG1  1 
ATOM   5887 C CG2  . VAL   B 1 121 ? 40.106 -17.440 -14.425 1.00 15.22 ?  121 VAL   B CG2  1 
ATOM   5888 H H    . VAL   B 1 121 ? 38.587 -14.393 -11.890 1.00 14.55 ?  121 VAL   B H    1 
ATOM   5889 H HA   . VAL   B 1 121 ? 38.241 -16.960 -12.555 1.00 14.44 ?  121 VAL   B HA   1 
ATOM   5890 H HB   . VAL   B 1 121 ? 38.604 -16.083 -14.667 1.00 16.60 ?  121 VAL   B HB   1 
ATOM   5891 H HG11 . VAL   B 1 121 ? 40.550 -14.930 -15.231 1.00 17.94 ?  121 VAL   B HG11 1 
ATOM   5892 H HG12 . VAL   B 1 121 ? 39.718 -14.124 -14.144 1.00 17.94 ?  121 VAL   B HG12 1 
ATOM   5893 H HG13 . VAL   B 1 121 ? 41.001 -14.953 -13.708 1.00 17.94 ?  121 VAL   B HG13 1 
ATOM   5894 H HG21 . VAL   B 1 121 ? 40.306 -17.432 -15.377 1.00 18.27 ?  121 VAL   B HG21 1 
ATOM   5895 H HG22 . VAL   B 1 121 ? 40.929 -17.482 -13.917 1.00 18.27 ?  121 VAL   B HG22 1 
ATOM   5896 H HG23 . VAL   B 1 121 ? 39.540 -18.196 -14.214 1.00 18.27 ?  121 VAL   B HG23 1 
ATOM   5897 N N    . LEU   B 1 122 ? 40.144 -17.672 -11.161 1.00 11.08 ?  122 LEU   B N    1 
ATOM   5898 C CA   . LEU   B 1 122 ? 41.124 -18.018 -10.136 1.00 10.89 ?  122 LEU   B CA   1 
ATOM   5899 C C    . LEU   B 1 122 ? 41.783 -19.346 -10.460 1.00 10.66 ?  122 LEU   B C    1 
ATOM   5900 O O    . LEU   B 1 122 ? 41.126 -20.266 -10.955 1.00 11.80 ?  122 LEU   B O    1 
ATOM   5901 C CB   . LEU   B 1 122 ? 40.472 -18.243 -8.759  1.00 12.60 ?  122 LEU   B CB   1 
ATOM   5902 C CG   . LEU   B 1 122 ? 39.442 -17.225 -8.266  1.00 12.52 ?  122 LEU   B CG   1 
ATOM   5903 C CD1  . LEU   B 1 122 ? 38.046 -17.581 -8.740  1.00 13.22 ?  122 LEU   B CD1  1 
ATOM   5904 C CD2  . LEU   B 1 122 ? 39.488 -17.114 -6.752  1.00 12.11 ?  122 LEU   B CD2  1 
ATOM   5905 H H    . LEU   B 1 122 ? 39.711 -18.353 -11.464 1.00 13.29 ?  122 LEU   B H    1 
ATOM   5906 H HA   . LEU   B 1 122 ? 41.802 -17.326 -10.065 1.00 13.06 ?  122 LEU   B HA   1 
ATOM   5907 H HB2  . LEU   B 1 122 ? 40.030 -19.103 -8.777  1.00 15.11 ?  122 LEU   B HB2  1 
ATOM   5908 H HB3  . LEU   B 1 122 ? 41.179 -18.262 -8.097  1.00 15.11 ?  122 LEU   B HB3  1 
ATOM   5909 H HG   . LEU   B 1 122 ? 39.658 -16.354 -8.630  1.00 15.03 ?  122 LEU   B HG   1 
ATOM   5910 H HD11 . LEU   B 1 122 ? 37.415 -16.935 -8.381  1.00 15.86 ?  122 LEU   B HD11 1 
ATOM   5911 H HD12 . LEU   B 1 122 ? 38.024 -17.552 -9.711  1.00 15.86 ?  122 LEU   B HD12 1 
ATOM   5912 H HD13 . LEU   B 1 122 ? 37.821 -18.470 -8.430  1.00 15.86 ?  122 LEU   B HD13 1 
ATOM   5913 H HD21 . LEU   B 1 122 ? 38.806 -16.490 -6.454  1.00 14.53 ?  122 LEU   B HD21 1 
ATOM   5914 H HD22 . LEU   B 1 122 ? 39.325 -17.989 -6.362  1.00 14.53 ?  122 LEU   B HD22 1 
ATOM   5915 H HD23 . LEU   B 1 122 ? 40.365 -16.794 -6.485  1.00 14.53 ?  122 LEU   B HD23 1 
ATOM   5916 N N    . LEU   B 1 123 ? 43.069 -19.453 -10.106 1.00 10.36 ?  123 LEU   B N    1 
ATOM   5917 C CA   . LEU   B 1 123 ? 43.780 -20.721 -9.987  1.00 10.45 ?  123 LEU   B CA   1 
ATOM   5918 C C    . LEU   B 1 123 ? 43.751 -21.116 -8.517  1.00 10.39 ?  123 LEU   B C    1 
ATOM   5919 O O    . LEU   B 1 123 ? 44.102 -20.294 -7.663  1.00 10.93 ?  123 LEU   B O    1 
ATOM   5920 C CB   . LEU   B 1 123 ? 45.231 -20.535 -10.433 1.00 11.20 ?  123 LEU   B CB   1 
ATOM   5921 C CG   . LEU   B 1 123 ? 46.169 -21.727 -10.199 1.00 11.38 ?  123 LEU   B CG   1 
ATOM   5922 C CD1  . LEU   B 1 123 ? 45.738 -22.966 -10.982 1.00 11.91 ?  123 LEU   B CD1  1 
ATOM   5923 C CD2  . LEU   B 1 123 ? 47.585 -21.340 -10.577 1.00 12.22 ?  123 LEU   B CD2  1 
ATOM   5924 H H    . LEU   B 1 123 ? 43.569 -18.776 -9.917  1.00 12.43 ?  123 LEU   B H    1 
ATOM   5925 H HA   . LEU   B 1 123 ? 43.349 -21.414 -10.519 1.00 12.53 ?  123 LEU   B HA   1 
ATOM   5926 H HB2  . LEU   B 1 123 ? 45.231 -20.350 -11.386 1.00 13.44 ?  123 LEU   B HB2  1 
ATOM   5927 H HB3  . LEU   B 1 123 ? 45.599 -19.777 -9.956  1.00 13.44 ?  123 LEU   B HB3  1 
ATOM   5928 H HG   . LEU   B 1 123 ? 46.166 -21.954 -9.256  1.00 13.65 ?  123 LEU   B HG   1 
ATOM   5929 H HD11 . LEU   B 1 123 ? 46.373 -23.676 -10.819 1.00 14.29 ?  123 LEU   B HD11 1 
ATOM   5930 H HD12 . LEU   B 1 123 ? 44.854 -23.234 -10.678 1.00 14.29 ?  123 LEU   B HD12 1 
ATOM   5931 H HD13 . LEU   B 1 123 ? 45.711 -22.747 -11.924 1.00 14.29 ?  123 LEU   B HD13 1 
ATOM   5932 H HD21 . LEU   B 1 123 ? 48.169 -22.099 -10.425 1.00 14.66 ?  123 LEU   B HD21 1 
ATOM   5933 H HD22 . LEU   B 1 123 ? 47.604 -21.088 -11.513 1.00 14.66 ?  123 LEU   B HD22 1 
ATOM   5934 H HD23 . LEU   B 1 123 ? 47.863 -20.591 -10.026 1.00 14.66 ?  123 LEU   B HD23 1 
ATOM   5935 N N    . ALA   B 1 124 ? 43.327 -22.345 -8.206  1.00 10.24 ?  124 ALA   B N    1 
ATOM   5936 C CA   . ALA   B 1 124 ? 43.067 -22.661 -6.809  1.00 10.54 ?  124 ALA   B CA   1 
ATOM   5937 C C    . ALA   B 1 124 ? 43.346 -24.119 -6.489  1.00 10.11 ?  124 ALA   B C    1 
ATOM   5938 O O    . ALA   B 1 124 ? 43.208 -24.995 -7.354  1.00 10.80 ?  124 ALA   B O    1 
ATOM   5939 C CB   . ALA   B 1 124 ? 41.612 -22.353 -6.432  1.00 10.97 ?  124 ALA   B CB   1 
ATOM   5940 H H    . ALA   B 1 124 ? 43.181 -22.993 -8.762  1.00 12.29 ?  124 ALA   B H    1 
ATOM   5941 H HA   . ALA   B 1 124 ? 43.642 -22.108 -6.260  1.00 12.65 ?  124 ALA   B HA   1 
ATOM   5942 H HB1  . ALA   B 1 124 ? 41.461 -22.564 -5.497  1.00 13.17 ?  124 ALA   B HB1  1 
ATOM   5943 H HB2  . ALA   B 1 124 ? 41.437 -21.402 -6.579  1.00 13.17 ?  124 ALA   B HB2  1 
ATOM   5944 H HB3  . ALA   B 1 124 ? 41.013 -22.877 -6.988  1.00 13.17 ?  124 ALA   B HB3  1 
ATOM   5945 N N    . PRO   B 1 125 ? 43.636 -24.414 -5.227  1.00 10.22 ?  125 PRO   B N    1 
ATOM   5946 C CA   . PRO   B 1 125 ? 43.578 -25.778 -4.706  1.00 11.04 ?  125 PRO   B CA   1 
ATOM   5947 C C    . PRO   B 1 125 ? 42.179 -26.053 -4.159  1.00 11.11 ?  125 PRO   B C    1 
ATOM   5948 O O    . PRO   B 1 125 ? 41.383 -25.139 -3.946  1.00 11.65 ?  125 PRO   B O    1 
ATOM   5949 C CB   . PRO   B 1 125 ? 44.564 -25.699 -3.535  1.00 12.28 ?  125 PRO   B CB   1 
ATOM   5950 C CG   . PRO   B 1 125 ? 44.305 -24.307 -2.969  1.00 11.99 ?  125 PRO   B CG   1 
ATOM   5951 C CD   . PRO   B 1 125 ? 43.956 -23.445 -4.163  1.00 11.05 ?  125 PRO   B CD   1 
ATOM   5952 H HA   . PRO   B 1 125 ? 43.853 -26.444 -5.356  1.00 13.24 ?  125 PRO   B HA   1 
ATOM   5953 H HB2  . PRO   B 1 125 ? 44.362 -26.384 -2.877  1.00 14.74 ?  125 PRO   B HB2  1 
ATOM   5954 H HB3  . PRO   B 1 125 ? 45.475 -25.778 -3.855  1.00 14.74 ?  125 PRO   B HB3  1 
ATOM   5955 H HG2  . PRO   B 1 125 ? 43.561 -24.339 -2.342  1.00 14.38 ?  125 PRO   B HG2  1 
ATOM   5956 H HG3  . PRO   B 1 125 ? 45.105 -23.978 -2.523  1.00 14.38 ?  125 PRO   B HG3  1 
ATOM   5957 H HD2  . PRO   B 1 125 ? 43.191 -22.884 -3.971  1.00 13.26 ?  125 PRO   B HD2  1 
ATOM   5958 H HD3  . PRO   B 1 125 ? 44.729 -22.905 -4.423  1.00 13.26 ?  125 PRO   B HD3  1 
ATOM   5959 N N    . LEU   B 1 126 ? 41.916 -27.330 -3.872  1.00 11.65 ?  126 LEU   B N    1 
ATOM   5960 C CA   . LEU   B 1 126 ? 40.695 -27.698 -3.161  1.00 12.35 ?  126 LEU   B CA   1 
ATOM   5961 C C    . LEU   B 1 126 ? 40.810 -27.297 -1.696  1.00 12.56 ?  126 LEU   B C    1 
ATOM   5962 O O    . LEU   B 1 126 ? 41.694 -27.767 -0.974  1.00 14.09 ?  126 LEU   B O    1 
ATOM   5963 C CB   . LEU   B 1 126 ? 40.444 -29.195 -3.274  1.00 13.88 ?  126 LEU   B CB   1 
ATOM   5964 C CG   . LEU   B 1 126 ? 39.921 -29.677 -4.628  1.00 14.72 ?  126 LEU   B CG   1 
ATOM   5965 C CD1  . LEU   B 1 126 ? 39.969 -31.188 -4.694  1.00 16.67 ?  126 LEU   B CD1  1 
ATOM   5966 C CD2  . LEU   B 1 126 ? 38.501 -29.188 -4.886  1.00 14.78 ?  126 LEU   B CD2  1 
ATOM   5967 H H    . LEU   B 1 126 ? 42.427 -27.999 -4.065  1.00 13.98 ?  126 LEU   B H    1 
ATOM   5968 H HA   . LEU   B 1 126 ? 39.943 -27.229 -3.553  1.00 14.81 ?  126 LEU   B HA   1 
ATOM   5969 H HB2  . LEU   B 1 126 ? 41.277 -29.661 -3.103  1.00 16.65 ?  126 LEU   B HB2  1 
ATOM   5970 H HB3  . LEU   B 1 126 ? 39.788 -29.449 -2.605  1.00 16.65 ?  126 LEU   B HB3  1 
ATOM   5971 H HG   . LEU   B 1 126 ? 40.493 -29.328 -5.331  1.00 17.66 ?  126 LEU   B HG   1 
ATOM   5972 H HD11 . LEU   B 1 126 ? 39.632 -31.478 -5.557  1.00 20.00 ?  126 LEU   B HD11 1 
ATOM   5973 H HD12 . LEU   B 1 126 ? 40.885 -31.482 -4.580  1.00 20.00 ?  126 LEU   B HD12 1 
ATOM   5974 H HD13 . LEU   B 1 126 ? 39.413 -31.552 -3.985  1.00 20.00 ?  126 LEU   B HD13 1 
ATOM   5975 H HD21 . LEU   B 1 126 ? 38.165 -29.599 -5.698  1.00 17.73 ?  126 LEU   B HD21 1 
ATOM   5976 H HD22 . LEU   B 1 126 ? 37.939 -29.432 -4.134  1.00 17.73 ?  126 LEU   B HD22 1 
ATOM   5977 H HD23 . LEU   B 1 126 ? 38.511 -28.221 -4.989  1.00 17.73 ?  126 LEU   B HD23 1 
ATOM   5978 N N    . LEU   B 1 127 ? 39.887 -26.457 -1.244  1.00 12.29 ?  127 LEU   B N    1 
ATOM   5979 C CA   . LEU   B 1 127 ? 39.938 -25.965 0.121   1.00 12.73 ?  127 LEU   B CA   1 
ATOM   5980 C C    . LEU   B 1 127 ? 39.663 -27.084 1.115   1.00 12.52 ?  127 LEU   B C    1 
ATOM   5981 O O    . LEU   B 1 127 ? 38.843 -27.980 0.885   1.00 12.79 ?  127 LEU   B O    1 
ATOM   5982 C CB   . LEU   B 1 127 ? 38.913 -24.850 0.327   1.00 13.11 ?  127 LEU   B CB   1 
ATOM   5983 C CG   . LEU   B 1 127 ? 39.092 -23.584 -0.511  1.00 13.49 ?  127 LEU   B CG   1 
ATOM   5984 C CD1  . LEU   B 1 127 ? 37.962 -22.626 -0.199  1.00 13.72 ?  127 LEU   B CD1  1 
ATOM   5985 C CD2  . LEU   B 1 127 ? 40.444 -22.931 -0.256  1.00 14.38 ?  127 LEU   B CD2  1 
ATOM   5986 H H    . LEU   B 1 127 ? 39.224 -26.148 -1.709  1.00 14.74 ?  127 LEU   B H    1 
ATOM   5987 H HA   . LEU   B 1 127 ? 40.821 -25.598 0.298   1.00 15.28 ?  127 LEU   B HA   1 
ATOM   5988 H HB2  . LEU   B 1 127 ? 38.031 -25.204 0.126   1.00 15.73 ?  127 LEU   B HB2  1 
ATOM   5989 H HB3  . LEU   B 1 127 ? 38.938 -24.577 1.260   1.00 15.73 ?  127 LEU   B HB3  1 
ATOM   5990 H HG   . LEU   B 1 127 ? 39.026 -23.808 -1.449  1.00 16.19 ?  127 LEU   B HG   1 
ATOM   5991 H HD11 . LEU   B 1 127 ? 38.076 -21.815 -0.727  1.00 16.46 ?  127 LEU   B HD11 1 
ATOM   5992 H HD12 . LEU   B 1 127 ? 37.114 -23.041 -0.418  1.00 16.46 ?  127 LEU   B HD12 1 
ATOM   5993 H HD13 . LEU   B 1 127 ? 37.984 -22.400 0.747   1.00 16.46 ?  127 LEU   B HD13 1 
ATOM   5994 H HD21 . LEU   B 1 127 ? 40.479 -22.075 -0.717  1.00 17.25 ?  127 LEU   B HD21 1 
ATOM   5995 H HD22 . LEU   B 1 127 ? 40.558 -22.793 0.698   1.00 17.25 ?  127 LEU   B HD22 1 
ATOM   5996 H HD23 . LEU   B 1 127 ? 41.141 -23.514 -0.592  1.00 17.25 ?  127 LEU   B HD23 1 
ATOM   5997 N N    . SER   B 1 128 ? 40.353 -27.004 2.243   1.00 12.51 ?  128 SER   B N    1 
ATOM   5998 C CA   . SER   B 1 128 ? 40.242 -27.913 3.366   1.00 12.94 ?  128 SER   B CA   1 
ATOM   5999 C C    . SER   B 1 128 ? 40.740 -29.318 3.047   1.00 14.12 ?  128 SER   B C    1 
ATOM   6000 O O    . SER   B 1 128 ? 40.651 -30.191 3.904   1.00 15.50 ?  128 SER   B O    1 
ATOM   6001 C CB   . SER   B 1 128 ? 38.843 -27.925 3.997   1.00 13.57 ?  128 SER   B CB   1 
ATOM   6002 O OG   . SER   B 1 128 ? 38.525 -26.648 4.538   1.00 14.13 ?  128 SER   B OG   1 
ATOM   6003 H H    . SER   B 1 128 ? 40.928 -26.379 2.388   1.00 15.01 ?  128 SER   B H    1 
ATOM   6004 H HA   . SER   B 1 128 ? 40.834 -27.578 4.049   1.00 15.53 ?  128 SER   B HA   1 
ATOM   6005 H HB2  . SER   B 1 128 ? 38.187 -28.166 3.325   1.00 16.29 ?  128 SER   B HB2  1 
ATOM   6006 H HB3  . SER   B 1 128 ? 38.830 -28.591 4.716   1.00 16.29 ?  128 SER   B HB3  1 
ATOM   6007 H HG   . SER   B 1 128 ? 39.095 -26.444 5.123   1.00 16.95 ?  128 SER   B HG   1 
ATOM   6008 N N    . ALA   B 1 129 ? 41.309 -29.547 1.861   1.00 15.12 ?  129 ALA   B N    1 
ATOM   6009 C CA   . ALA   B 1 129 ? 41.846 -30.851 1.514   1.00 15.82 ?  129 ALA   B CA   1 
ATOM   6010 C C    . ALA   B 1 129 ? 43.240 -31.021 2.102   1.00 14.93 ?  129 ALA   B C    1 
ATOM   6011 O O    . ALA   B 1 129 ? 43.801 -30.118 2.736   1.00 14.65 ?  129 ALA   B O    1 
ATOM   6012 C CB   . ALA   B 1 129 ? 41.884 -31.030 -0.002  1.00 18.37 ?  129 ALA   B CB   1 
ATOM   6013 H H    . ALA   B 1 129 ? 41.395 -28.958 1.237   1.00 18.14 ?  129 ALA   B H    1 
ATOM   6014 H HA   . ALA   B 1 129 ? 41.276 -31.539 1.885   1.00 18.98 ?  129 ALA   B HA   1 
ATOM   6015 H HB1  . ALA   B 1 129 ? 42.236 -31.913 -0.207  1.00 22.04 ?  129 ALA   B HB1  1 
ATOM   6016 H HB2  . ALA   B 1 129 ? 40.986 -30.944 -0.352  1.00 22.04 ?  129 ALA   B HB2  1 
ATOM   6017 H HB3  . ALA   B 1 129 ? 42.459 -30.350 -0.387  1.00 22.04 ?  129 ALA   B HB3  1 
ATOM   6018 N N    . GLY   B 1 130 ? 43.807 -32.201 1.869   1.00 15.13 ?  130 GLY   B N    1 
ATOM   6019 C CA   . GLY   B 1 130 ? 45.197 -32.429 2.215   1.00 15.69 ?  130 GLY   B CA   1 
ATOM   6020 C C    . GLY   B 1 130 ? 45.408 -32.334 3.706   1.00 15.62 ?  130 GLY   B C    1 
ATOM   6021 O O    . GLY   B 1 130 ? 44.710 -32.978 4.501   1.00 16.72 ?  130 GLY   B O    1 
ATOM   6022 H H    . GLY   B 1 130 ? 43.413 -32.876 1.511   1.00 18.15 ?  130 GLY   B H    1 
ATOM   6023 H HA2  . GLY   B 1 130 ? 45.469 -33.314 1.919   1.00 18.83 ?  130 GLY   B HA2  1 
ATOM   6024 H HA3  . GLY   B 1 130 ? 45.758 -31.771 1.778   1.00 18.83 ?  130 GLY   B HA3  1 
ATOM   6025 N N    . ILE   B 1 131 ? 46.387 -31.510 4.095   1.00 15.86 ?  131 ILE   B N    1 
ATOM   6026 C CA   . ILE   B 1 131 ? 46.740 -31.385 5.502   1.00 16.85 ?  131 ILE   B CA   1 
ATOM   6027 C C    . ILE   B 1 131 ? 45.622 -30.788 6.335   1.00 16.25 ?  131 ILE   B C    1 
ATOM   6028 O O    . ILE   B 1 131 ? 45.685 -30.867 7.564   1.00 17.73 ?  131 ILE   B O    1 
ATOM   6029 C CB   . ILE   B 1 131 ? 48.062 -30.617 5.715   1.00 18.84 ?  131 ILE   B CB   1 
ATOM   6030 C CG1  . ILE   B 1 131 ? 47.903 -29.132 5.366   1.00 20.10 ?  131 ILE   B CG1  1 
ATOM   6031 C CG2  . ILE   B 1 131 ? 49.178 -31.249 4.891   1.00 20.04 ?  131 ILE   B CG2  1 
ATOM   6032 C CD1  . ILE   B 1 131 ? 49.140 -28.298 5.649   1.00 20.94 ?  131 ILE   B CD1  1 
ATOM   6033 H H    . ILE   B 1 131 ? 46.858 -31.017 3.567   1.00 19.03 ?  131 ILE   B H    1 
ATOM   6034 H HA   . ILE   B 1 131 ? 46.882 -32.279 5.844   1.00 20.22 ?  131 ILE   B HA   1 
ATOM   6035 H HB   . ILE   B 1 131 ? 48.300 -30.685 6.653   1.00 22.60 ?  131 ILE   B HB   1 
ATOM   6036 H HG12 . ILE   B 1 131 ? 47.698 -29.054 4.423   1.00 24.12 ?  131 ILE   B HG12 1 
ATOM   6037 H HG13 . ILE   B 1 131 ? 47.176 -28.757 5.891   1.00 24.12 ?  131 ILE   B HG13 1 
ATOM   6038 H HG21 . ILE   B 1 131 ? 50.024 -30.867 5.164   1.00 24.04 ?  131 ILE   B HG21 1 
ATOM   6039 H HG22 . ILE   B 1 131 ? 49.176 -32.205 5.044   1.00 24.04 ?  131 ILE   B HG22 1 
ATOM   6040 H HG23 . ILE   B 1 131 ? 49.014 -31.063 3.952   1.00 24.04 ?  131 ILE   B HG23 1 
ATOM   6041 H HD11 . ILE   B 1 131 ? 48.925 -27.362 5.513   1.00 25.12 ?  131 ILE   B HD11 1 
ATOM   6042 H HD12 . ILE   B 1 131 ? 49.416 -28.445 6.567   1.00 25.12 ?  131 ILE   B HD12 1 
ATOM   6043 H HD13 . ILE   B 1 131 ? 49.847 -28.567 5.043   1.00 25.12 ?  131 ILE   B HD13 1 
ATOM   6044 N N    . PHE   B 1 132 ? 44.597 -30.206 5.703   1.00 15.23 ?  132 PHE   B N    1 
ATOM   6045 C CA   . PHE   B 1 132 ? 43.437 -29.703 6.433   1.00 15.22 ?  132 PHE   B CA   1 
ATOM   6046 C C    . PHE   B 1 132 ? 42.410 -30.792 6.753   1.00 16.63 ?  132 PHE   B C    1 
ATOM   6047 O O    . PHE   B 1 132 ? 41.494 -30.539 7.544   1.00 18.41 ?  132 PHE   B O    1 
ATOM   6048 C CB   . PHE   B 1 132 ? 42.761 -28.565 5.658   1.00 14.74 ?  132 PHE   B CB   1 
ATOM   6049 C CG   . PHE   B 1 132 ? 43.463 -27.226 5.760   1.00 14.36 ?  132 PHE   B CG   1 
ATOM   6050 C CD1  . PHE   B 1 132 ? 44.753 -27.049 5.281   1.00 15.45 ?  132 PHE   B CD1  1 
ATOM   6051 C CD2  . PHE   B 1 132 ? 42.795 -26.127 6.283   1.00 13.70 ?  132 PHE   B CD2  1 
ATOM   6052 C CE1  . PHE   B 1 132 ? 45.373 -25.804 5.366   1.00 16.02 ?  132 PHE   B CE1  1 
ATOM   6053 C CE2  . PHE   B 1 132 ? 43.401 -24.891 6.362   1.00 14.57 ?  132 PHE   B CE2  1 
ATOM   6054 C CZ   . PHE   B 1 132 ? 44.686 -24.728 5.906   1.00 15.52 ?  132 PHE   B CZ   1 
ATOM   6055 H H    . PHE   B 1 132 ? 44.548 -30.090 4.850   1.00 18.27 ?  132 PHE   B H    1 
ATOM   6056 H HA   . PHE   B 1 132 ? 43.741 -29.337 7.276   1.00 18.27 ?  132 PHE   B HA   1 
ATOM   6057 H HB2  . PHE   B 1 132 ? 42.735 -28.806 4.722   1.00 17.68 ?  132 PHE   B HB2  1 
ATOM   6058 H HB3  . PHE   B 1 132 ? 41.858 -28.451 5.996   1.00 17.68 ?  132 PHE   B HB3  1 
ATOM   6059 H HD1  . PHE   B 1 132 ? 45.218 -27.772 4.923   1.00 18.54 ?  132 PHE   B HD1  1 
ATOM   6060 H HD2  . PHE   B 1 132 ? 41.926 -26.229 6.598   1.00 16.44 ?  132 PHE   B HD2  1 
ATOM   6061 H HE1  . PHE   B 1 132 ? 46.244 -25.692 5.057   1.00 19.22 ?  132 PHE   B HE1  1 
ATOM   6062 H HE2  . PHE   B 1 132 ? 42.943 -24.165 6.732   1.00 17.49 ?  132 PHE   B HE2  1 
ATOM   6063 H HZ   . PHE   B 1 132 ? 45.097 -23.889 5.967   1.00 18.62 ?  132 PHE   B HZ   1 
ATOM   6064 N N    . GLY   B 1 133 ? 42.521 -31.986 6.155   1.00 16.64 ?  133 GLY   B N    1 
ATOM   6065 C CA   . GLY   B 1 133 ? 41.815 -33.161 6.638   1.00 17.60 ?  133 GLY   B CA   1 
ATOM   6066 C C    . GLY   B 1 133 ? 40.416 -33.419 6.108   1.00 17.85 ?  133 GLY   B C    1 
ATOM   6067 O O    . GLY   B 1 133 ? 39.827 -34.437 6.481   1.00 19.88 ?  133 GLY   B O    1 
ATOM   6068 H H    . GLY   B 1 133 ? 43.008 -32.133 5.458   1.00 19.96 ?  133 GLY   B H    1 
ATOM   6069 H HA2  . GLY   B 1 133 ? 42.351 -33.942 6.431   1.00 21.12 ?  133 GLY   B HA2  1 
ATOM   6070 H HA3  . GLY   B 1 133 ? 41.747 -33.098 7.601   1.00 21.12 ?  133 GLY   B HA3  1 
ATOM   6071 N N    . ALA   B 1 134 ? 39.854 -32.553 5.275   1.00 16.68 ?  134 ALA   B N    1 
ATOM   6072 C CA   . ALA   B 1 134 ? 38.531 -32.835 4.741   1.00 16.78 ?  134 ALA   B CA   1 
ATOM   6073 C C    . ALA   B 1 134 ? 38.619 -33.822 3.581   1.00 16.81 ?  134 ALA   B C    1 
ATOM   6074 O O    . ALA   B 1 134 ? 39.673 -34.012 2.966   1.00 17.95 ?  134 ALA   B O    1 
ATOM   6075 C CB   . ALA   B 1 134 ? 37.847 -31.548 4.279   1.00 17.31 ?  134 ALA   B CB   1 
ATOM   6076 H H    . ALA   B 1 134 ? 40.206 -31.810 5.013   1.00 20.01 ?  134 ALA   B H    1 
ATOM   6077 H HA   . ALA   B 1 134 ? 37.986 -33.230 5.440   1.00 20.13 ?  134 ALA   B HA   1 
ATOM   6078 H HB1  . ALA   B 1 134 ? 36.962 -31.767 3.945   1.00 20.77 ?  134 ALA   B HB1  1 
ATOM   6079 H HB2  . ALA   B 1 134 ? 37.775 -30.940 5.031   1.00 20.77 ?  134 ALA   B HB2  1 
ATOM   6080 H HB3  . ALA   B 1 134 ? 38.376 -31.145 3.574   1.00 20.77 ?  134 ALA   B HB3  1 
ATOM   6081 N N    . ASP   B 1 135 ? 37.489 -34.456 3.292   1.00 16.94 ?  135 ASP   B N    1 
ATOM   6082 C CA   . ASP   B 1 135 ? 37.392 -35.348 2.150   1.00 17.98 ?  135 ASP   B CA   1 
ATOM   6083 C C    . ASP   B 1 135 ? 37.484 -34.510 0.883   1.00 16.82 ?  135 ASP   B C    1 
ATOM   6084 O O    . ASP   B 1 135 ? 36.630 -33.636 0.667   1.00 16.87 ?  135 ASP   B O    1 
ATOM   6085 C CB   . ASP   B 1 135 ? 36.054 -36.080 2.208   1.00 19.73 ?  135 ASP   B CB   1 
ATOM   6086 C CG   . ASP   B 1 135 ? 35.875 -37.079 1.083   1.00 21.96 ?  135 ASP   B CG   1 
ATOM   6087 O OD1  . ASP   B 1 135 ? 36.739 -37.133 0.183   1.00 21.73 ?  135 ASP   B OD1  1 
ATOM   6088 O OD2  . ASP   B 1 135 ? 34.874 -37.833 1.114   1.00 24.94 -1 135 ASP   B OD2  1 
ATOM   6089 H H    . ASP   B 1 135 ? 36.763 -34.380 3.744   1.00 20.33 ?  135 ASP   B H    1 
ATOM   6090 H HA   . ASP   B 1 135 ? 38.113 -36.000 2.181   1.00 21.57 ?  135 ASP   B HA   1 
ATOM   6091 H HB2  . ASP   B 1 135 ? 35.998 -36.564 3.043   1.00 23.68 ?  135 ASP   B HB2  1 
ATOM   6092 H HB3  . ASP   B 1 135 ? 35.342 -35.430 2.145   1.00 23.68 ?  135 ASP   B HB3  1 
ATOM   6093 N N    . PRO   B 1 136 ? 38.493 -34.717 0.033   1.00 16.82 ?  136 PRO   B N    1 
ATOM   6094 C CA   . PRO   B 1 136 ? 38.595 -33.892 -1.180  1.00 16.12 ?  136 PRO   B CA   1 
ATOM   6095 C C    . PRO   B 1 136 ? 37.403 -34.044 -2.101  1.00 15.30 ?  136 PRO   B C    1 
ATOM   6096 O O    . PRO   B 1 136 ? 37.077 -33.097 -2.824  1.00 14.54 ?  136 PRO   B O    1 
ATOM   6097 C CB   . PRO   B 1 136 ? 39.906 -34.363 -1.828  1.00 17.47 ?  136 PRO   B CB   1 
ATOM   6098 C CG   . PRO   B 1 136 ? 40.131 -35.743 -1.275  1.00 18.71 ?  136 PRO   B CG   1 
ATOM   6099 C CD   . PRO   B 1 136 ? 39.580 -35.706 0.121   1.00 18.05 ?  136 PRO   B CD   1 
ATOM   6100 H HA   . PRO   B 1 136 ? 38.684 -32.957 -0.942  1.00 19.34 ?  136 PRO   B HA   1 
ATOM   6101 H HB2  . PRO   B 1 136 ? 39.805 -34.393 -2.795  1.00 20.97 ?  136 PRO   B HB2  1 
ATOM   6102 H HB3  . PRO   B 1 136 ? 40.628 -33.767 -1.578  1.00 20.97 ?  136 PRO   B HB3  1 
ATOM   6103 H HG2  . PRO   B 1 136 ? 39.654 -36.396 -1.811  1.00 22.45 ?  136 PRO   B HG2  1 
ATOM   6104 H HG3  . PRO   B 1 136 ? 41.081 -35.941 -1.261  1.00 22.45 ?  136 PRO   B HG3  1 
ATOM   6105 H HD2  . PRO   B 1 136 ? 39.228 -36.575 0.369   1.00 21.65 ?  136 PRO   B HD2  1 
ATOM   6106 H HD3  . PRO   B 1 136 ? 40.260 -35.406 0.748   1.00 21.65 ?  136 PRO   B HD3  1 
ATOM   6107 N N    . ILE   B 1 137 ? 36.742 -35.207 -2.098  1.00 15.65 ?  137 ILE   B N    1 
ATOM   6108 C CA   . ILE   B 1 137 ? 35.522 -35.374 -2.885  1.00 16.19 ?  137 ILE   B CA   1 
ATOM   6109 C C    . ILE   B 1 137 ? 34.448 -34.406 -2.407  1.00 15.72 ?  137 ILE   B C    1 
ATOM   6110 O O    . ILE   B 1 137 ? 33.728 -33.797 -3.209  1.00 15.35 ?  137 ILE   B O    1 
ATOM   6111 C CB   . ILE   B 1 137 ? 35.048 -36.842 -2.824  1.00 18.47 ?  137 ILE   B CB   1 
ATOM   6112 C CG1  . ILE   B 1 137 ? 36.057 -37.747 -3.533  1.00 21.06 ?  137 ILE   B CG1  1 
ATOM   6113 C CG2  . ILE   B 1 137 ? 33.647 -36.992 -3.432  1.00 19.00 ?  137 ILE   B CG2  1 
ATOM   6114 C CD1  . ILE   B 1 137 ? 35.722 -39.226 -3.466  1.00 23.73 ?  137 ILE   B CD1  1 
ATOM   6115 H H    . ILE   B 1 137 ? 36.982 -35.909 -1.661  1.00 18.78 ?  137 ILE   B H    1 
ATOM   6116 H HA   . ILE   B 1 137 ? 35.712 -35.172 -3.814  1.00 19.43 ?  137 ILE   B HA   1 
ATOM   6117 H HB   . ILE   B 1 137 ? 34.998 -37.112 -1.897  1.00 22.16 ?  137 ILE   B HB   1 
ATOM   6118 H HG12 . ILE   B 1 137 ? 36.101 -37.502 -4.469  1.00 25.27 ?  137 ILE   B HG12 1 
ATOM   6119 H HG13 . ILE   B 1 137 ? 36.926 -37.629 -3.120  1.00 25.27 ?  137 ILE   B HG13 1 
ATOM   6120 H HG21 . ILE   B 1 137 ? 33.386 -37.928 -3.427  1.00 22.79 ?  137 ILE   B HG21 1 
ATOM   6121 H HG22 . ILE   B 1 137 ? 33.009 -36.488 -2.905  1.00 22.79 ?  137 ILE   B HG22 1 
ATOM   6122 H HG23 . ILE   B 1 137 ? 33.659 -36.662 -4.344  1.00 22.79 ?  137 ILE   B HG23 1 
ATOM   6123 H HD11 . ILE   B 1 137 ? 36.395 -39.709 -3.966  1.00 28.47 ?  137 ILE   B HD11 1 
ATOM   6124 H HD12 . ILE   B 1 137 ? 35.723 -39.513 -2.539  1.00 28.47 ?  137 ILE   B HD12 1 
ATOM   6125 H HD13 . ILE   B 1 137 ? 34.853 -39.384 -3.864  1.00 28.47 ?  137 ILE   B HD13 1 
ATOM   6126 N N    . HIS   B 1 138 ? 34.321 -34.258 -1.090  1.00 15.64 ?  138 HIS   B N    1 
ATOM   6127 C CA   . HIS   B 1 138 ? 33.373 -33.295 -0.548  1.00 15.81 ?  138 HIS   B CA   1 
ATOM   6128 C C    . HIS   B 1 138 ? 33.791 -31.865 -0.862  1.00 15.15 ?  138 HIS   B C    1 
ATOM   6129 O O    . HIS   B 1 138 ? 32.941 -31.020 -1.163  1.00 15.70 ?  138 HIS   B O    1 
ATOM   6130 C CB   . HIS   B 1 138 ? 33.256 -33.481 0.955   1.00 17.53 ?  138 HIS   B CB   1 
ATOM   6131 C CG   . HIS   B 1 138 ? 32.328 -32.503 1.597   1.00 18.90 ?  138 HIS   B CG   1 
ATOM   6132 N ND1  . HIS   B 1 138 ? 30.985 -32.445 1.293   1.00 20.45 ?  138 HIS   B ND1  1 
ATOM   6133 C CD2  . HIS   B 1 138 ? 32.552 -31.524 2.504   1.00 19.51 ?  138 HIS   B CD2  1 
ATOM   6134 C CE1  . HIS   B 1 138 ? 30.418 -31.484 1.998   1.00 20.58 ?  138 HIS   B CE1  1 
ATOM   6135 N NE2  . HIS   B 1 138 ? 31.348 -30.908 2.740   1.00 19.86 ?  138 HIS   B NE2  1 
ATOM   6136 H H    . HIS   B 1 138 ? 34.769 -34.697 -0.503  1.00 18.76 ?  138 HIS   B H    1 
ATOM   6137 H HA   . HIS   B 1 138 ? 32.502 -33.456 -0.946  1.00 18.97 ?  138 HIS   B HA   1 
ATOM   6138 H HB2  . HIS   B 1 138 ? 32.918 -34.373 1.135   1.00 21.03 ?  138 HIS   B HB2  1 
ATOM   6139 H HB3  . HIS   B 1 138 ? 34.129 -33.369 1.355   1.00 21.03 ?  138 HIS   B HB3  1 
ATOM   6140 H HD1  . HIS   B 1 138 ? 30.575 -32.965 0.738   1.00 24.54 ?  138 HIS   B HD1  1 
ATOM   6141 H HD2  . HIS   B 1 138 ? 33.362 -31.314 2.900   1.00 23.42 ?  138 HIS   B HD2  1 
ATOM   6142 H HE1  . HIS   B 1 138 ? 29.512 -31.258 1.979   1.00 24.69 ?  138 HIS   B HE1  1 
ATOM   6143 N N    . SER   B 1 139 ? 35.086 -31.567 -0.784  1.00 14.78 ?  139 SER   B N    1 
ATOM   6144 C CA   . SER   B 1 139 ? 35.524 -30.218 -1.108  1.00 14.28 ?  139 SER   B CA   1 
ATOM   6145 C C    . SER   B 1 139 ? 35.179 -29.871 -2.548  1.00 13.33 ?  139 SER   B C    1 
ATOM   6146 O O    . SER   B 1 139 ? 34.731 -28.756 -2.826  1.00 13.28 ?  139 SER   B O    1 
ATOM   6147 C CB   . SER   B 1 139 ? 37.020 -30.075 -0.847  1.00 14.39 ?  139 SER   B CB   1 
ATOM   6148 O OG   . SER   B 1 139 ? 37.427 -28.750 -1.127  1.00 14.29 ?  139 SER   B OG   1 
ATOM   6149 H H    . SER   B 1 139 ? 35.706 -32.111 -0.553  1.00 17.74 ?  139 SER   B H    1 
ATOM   6150 H HA   . SER   B 1 139 ? 35.057 -29.594 -0.534  1.00 17.14 ?  139 SER   B HA   1 
ATOM   6151 H HB2  . SER   B 1 139 ? 37.202 -30.280 0.086   1.00 17.27 ?  139 SER   B HB2  1 
ATOM   6152 H HB3  . SER   B 1 139 ? 37.508 -30.683 -1.423  1.00 17.27 ?  139 SER   B HB3  1 
ATOM   6153 H HG   . SER   B 1 139 ? 38.252 -28.662 -0.972  1.00 17.14 ?  139 SER   B HG   1 
ATOM   6154 N N    . LEU   B 1 140 ? 35.369 -30.813 -3.476  1.00 13.30 ?  140 LEU   B N    1 
ATOM   6155 C CA   . LEU   B 1 140 ? 35.001 -30.562 -4.863  1.00 13.22 ?  140 LEU   B CA   1 
ATOM   6156 C C    . LEU   B 1 140 ? 33.495 -30.336 -4.991  1.00 13.23 ?  140 LEU   B C    1 
ATOM   6157 O O    . LEU   B 1 140 ? 33.054 -29.450 -5.727  1.00 13.62 ?  140 LEU   B O    1 
ATOM   6158 C CB   . LEU   B 1 140 ? 35.465 -31.724 -5.743  1.00 13.39 ?  140 LEU   B CB   1 
ATOM   6159 C CG   . LEU   B 1 140 ? 35.098 -31.624 -7.217  1.00 13.57 ?  140 LEU   B CG   1 
ATOM   6160 C CD1  . LEU   B 1 140 ? 35.669 -30.350 -7.816  1.00 14.22 ?  140 LEU   B CD1  1 
ATOM   6161 C CD2  . LEU   B 1 140 ? 35.580 -32.857 -7.964  1.00 14.53 ?  140 LEU   B CD2  1 
ATOM   6162 H H    . LEU   B 1 140 ? 35.703 -31.588 -3.327  1.00 15.96 ?  140 LEU   B H    1 
ATOM   6163 H HA   . LEU   B 1 140 ? 35.454 -29.757 -5.166  1.00 15.87 ?  140 LEU   B HA   1 
ATOM   6164 H HB2  . LEU   B 1 140 ? 36.430 -31.785 -5.689  1.00 16.06 ?  140 LEU   B HB2  1 
ATOM   6165 H HB3  . LEU   B 1 140 ? 35.067 -32.541 -5.405  1.00 16.06 ?  140 LEU   B HB3  1 
ATOM   6166 H HG   . LEU   B 1 140 ? 34.132 -31.575 -7.298  1.00 16.28 ?  140 LEU   B HG   1 
ATOM   6167 H HD11 . LEU   B 1 140 ? 35.547 -30.375 -8.776  1.00 17.06 ?  140 LEU   B HD11 1 
ATOM   6168 H HD12 . LEU   B 1 140 ? 35.199 -29.584 -7.444  1.00 17.06 ?  140 LEU   B HD12 1 
ATOM   6169 H HD13 . LEU   B 1 140 ? 36.612 -30.296 -7.600  1.00 17.06 ?  140 LEU   B HD13 1 
ATOM   6170 H HD21 . LEU   B 1 140 ? 35.332 -32.767 -8.899  1.00 17.44 ?  140 LEU   B HD21 1 
ATOM   6171 H HD22 . LEU   B 1 140 ? 36.538 -32.922 -7.877  1.00 17.44 ?  140 LEU   B HD22 1 
ATOM   6172 H HD23 . LEU   B 1 140 ? 35.149 -33.636 -7.581  1.00 17.44 ?  140 LEU   B HD23 1 
ATOM   6173 N N    . ARG   B 1 141 ? 32.697 -31.132 -4.276  1.00 13.56 ?  141 ARG   B N    1 
ATOM   6174 C CA   . ARG   B 1 141 ? 31.245 -30.956 -4.254  1.00 14.99 ?  141 ARG   B CA   1 
ATOM   6175 C C    . ARG   B 1 141 ? 30.865 -29.542 -3.827  1.00 14.38 ?  141 ARG   B C    1 
ATOM   6176 O O    . ARG   B 1 141 ? 30.058 -28.866 -4.483  1.00 14.64 ?  141 ARG   B O    1 
ATOM   6177 C CB   . ARG   B 1 141 ? 30.662 -31.988 -3.281  1.00 16.16 ?  141 ARG   B CB   1 
ATOM   6178 C CG   . ARG   B 1 141 ? 29.200 -31.866 -2.951  1.00 17.88 ?  141 ARG   B CG   1 
ATOM   6179 C CD   . ARG   B 1 141 ? 28.398 -32.501 -4.012  1.00 19.43 ?  141 ARG   B CD   1 
ATOM   6180 N NE   . ARG   B 1 141 ? 28.145 -31.597 -5.124  1.00 19.53 ?  141 ARG   B NE   1 
ATOM   6181 C CZ   . ARG   B 1 141 ? 28.143 -31.959 -6.399  1.00 18.89 ?  141 ARG   B CZ   1 
ATOM   6182 N NH1  . ARG   B 1 141 ? 28.593 -33.144 -6.786  1.00 18.59 ?  141 ARG   B NH1  1 
ATOM   6183 N NH2  . ARG   B 1 141 ? 27.680 -31.109 -7.312  1.00 20.05 ?  141 ARG   B NH2  1 
ATOM   6184 H H    . ARG   B 1 141 ? 32.976 -31.787 -3.794  1.00 16.27 ?  141 ARG   B H    1 
ATOM   6185 H HA   . ARG   B 1 141 ? 30.883 -31.118 -5.135  1.00 17.99 ?  141 ARG   B HA   1 
ATOM   6186 H HB2  . ARG   B 1 141 ? 30.808 -32.873 -3.657  1.00 19.38 ?  141 ARG   B HB2  1 
ATOM   6187 H HB3  . ARG   B 1 141 ? 31.146 -31.923 -2.445  1.00 19.38 ?  141 ARG   B HB3  1 
ATOM   6188 H HG2  . ARG   B 1 141 ? 29.025 -32.316 -2.113  1.00 21.45 ?  141 ARG   B HG2  1 
ATOM   6189 H HG3  . ARG   B 1 141 ? 28.948 -30.928 -2.886  1.00 21.45 ?  141 ARG   B HG3  1 
ATOM   6190 H HD2  . ARG   B 1 141 ? 28.870 -33.285 -4.343  1.00 23.32 ?  141 ARG   B HD2  1 
ATOM   6191 H HD3  . ARG   B 1 141 ? 27.550 -32.770 -3.640  1.00 23.32 ?  141 ARG   B HD3  1 
ATOM   6192 H HE   . ARG   B 1 141 ? 27.973 -30.775 -4.939  1.00 23.43 ?  141 ARG   B HE   1 
ATOM   6193 H HH11 . ARG   B 1 141 ? 28.887 -33.710 -6.211  1.00 22.30 ?  141 ARG   B HH11 1 
ATOM   6194 H HH12 . ARG   B 1 141 ? 28.593 -33.349 -7.620  1.00 22.30 ?  141 ARG   B HH12 1 
ATOM   6195 H HH21 . ARG   B 1 141 ? 27.394 -30.333 -7.074  1.00 24.06 ?  141 ARG   B HH21 1 
ATOM   6196 H HH22 . ARG   B 1 141 ? 27.695 -31.322 -8.147  1.00 24.06 ?  141 ARG   B HH22 1 
ATOM   6197 N N    . VAL   B 1 142 ? 31.418 -29.091 -2.707  1.00 13.97 ?  142 VAL   B N    1 
ATOM   6198 C CA   . VAL   B 1 142 ? 31.081 -27.759 -2.222  1.00 13.85 ?  142 VAL   B CA   1 
ATOM   6199 C C    . VAL   B 1 142 ? 31.557 -26.702 -3.209  1.00 13.43 ?  142 VAL   B C    1 
ATOM   6200 O O    . VAL   B 1 142 ? 30.855 -25.717 -3.468  1.00 13.75 ?  142 VAL   B O    1 
ATOM   6201 C CB   . VAL   B 1 142 ? 31.630 -27.539 -0.801  1.00 14.59 ?  142 VAL   B CB   1 
ATOM   6202 C CG1  . VAL   B 1 142 ? 31.327 -26.124 -0.321  1.00 14.57 ?  142 VAL   B CG1  1 
ATOM   6203 C CG2  . VAL   B 1 142 ? 31.045 -28.566 0.154   1.00 15.43 ?  142 VAL   B CG2  1 
ATOM   6204 H H    . VAL   B 1 142 ? 31.986 -29.521 -2.223  1.00 16.77 ?  142 VAL   B H    1 
ATOM   6205 H HA   . VAL   B 1 142 ? 30.122 -27.689 -2.168  1.00 16.62 ?  142 VAL   B HA   1 
ATOM   6206 H HB   . VAL   B 1 142 ? 32.597 -27.655 -0.808  1.00 17.51 ?  142 VAL   B HB   1 
ATOM   6207 H HG11 . VAL   B 1 142 ? 31.518 -26.066 0.628   1.00 17.48 ?  142 VAL   B HG11 1 
ATOM   6208 H HG12 . VAL   B 1 142 ? 31.886 -25.498 -0.808  1.00 17.48 ?  142 VAL   B HG12 1 
ATOM   6209 H HG13 . VAL   B 1 142 ? 30.392 -25.933 -0.484  1.00 17.48 ?  142 VAL   B HG13 1 
ATOM   6210 H HG21 . VAL   B 1 142 ? 31.362 -28.385 1.050   1.00 18.52 ?  142 VAL   B HG21 1 
ATOM   6211 H HG22 . VAL   B 1 142 ? 30.077 -28.507 0.123   1.00 18.52 ?  142 VAL   B HG22 1 
ATOM   6212 H HG23 . VAL   B 1 142 ? 31.328 -29.455 -0.124  1.00 18.52 ?  142 VAL   B HG23 1 
ATOM   6213 N N    . CYS   B 1 143 ? 32.738 -26.897 -3.793  1.00 13.21 ?  143 CYS   B N    1 
ATOM   6214 C CA   . CYS   B 1 143 ? 33.227 -25.960 -4.799  1.00 12.84 ?  143 CYS   B CA   1 
ATOM   6215 C C    . CYS   B 1 143 ? 32.225 -25.819 -5.939  1.00 12.90 ?  143 CYS   B C    1 
ATOM   6216 O O    . CYS   B 1 143 ? 31.822 -24.710 -6.302  1.00 13.07 ?  143 CYS   B O    1 
ATOM   6217 C CB   . CYS   B 1 143 ? 34.578 -26.448 -5.328  1.00 13.45 ?  143 CYS   B CB   1 
ATOM   6218 S SG   . CYS   B 1 143 ? 35.328 -25.350 -6.541  1.00 13.45 ?  143 CYS   B SG   1 
ATOM   6219 H H    . CYS   B 1 143 ? 33.276 -27.544 -3.619  1.00 15.85 ?  143 CYS   B H    1 
ATOM   6220 H HA   . CYS   B 1 143 ? 33.366 -25.086 -4.401  1.00 15.41 ?  143 CYS   B HA   1 
ATOM   6221 H HB2  . CYS   B 1 143 ? 35.202 -26.542 -4.590  1.00 16.14 ?  143 CYS   B HB2  1 
ATOM   6222 H HB3  . CYS   B 1 143 ? 34.456 -27.313 -5.754  1.00 16.14 ?  143 CYS   B HB3  1 
ATOM   6223 H HG   . CYS   B 1 143 ? 36.403 -25.791 -6.865  1.00 16.14 ?  143 CYS   B HG   1 
ATOM   6224 N N    . VAL   B 1 144 ? 31.821 -26.943 -6.525  1.00 13.35 ?  144 VAL   B N    1 
ATOM   6225 C CA   . VAL   B 1 144 ? 30.913 -26.891 -7.666  1.00 14.36 ?  144 VAL   B CA   1 
ATOM   6226 C C    . VAL   B 1 144 ? 29.576 -26.267 -7.285  1.00 14.32 ?  144 VAL   B C    1 
ATOM   6227 O O    . VAL   B 1 144 ? 28.956 -25.554 -8.086  1.00 15.80 ?  144 VAL   B O    1 
ATOM   6228 C CB   . VAL   B 1 144 ? 30.746 -28.306 -8.232  1.00 16.64 ?  144 VAL   B CB   1 
ATOM   6229 C CG1  . VAL   B 1 144 ? 29.480 -28.429 -9.071  1.00 19.14 ?  144 VAL   B CG1  1 
ATOM   6230 C CG2  . VAL   B 1 144 ? 31.995 -28.715 -9.011  1.00 16.73 ?  144 VAL   B CG2  1 
ATOM   6231 H H    . VAL   B 1 144 ? 32.056 -27.736 -6.289  1.00 16.02 ?  144 VAL   B H    1 
ATOM   6232 H HA   . VAL   B 1 144 ? 31.305 -26.345 -8.363  1.00 17.23 ?  144 VAL   B HA   1 
ATOM   6233 H HB   . VAL   B 1 144 ? 30.655 -28.929 -7.491  1.00 19.96 ?  144 VAL   B HB   1 
ATOM   6234 H HG11 . VAL   B 1 144 ? 29.553 -29.216 -9.637  1.00 22.96 ?  144 VAL   B HG11 1 
ATOM   6235 H HG12 . VAL   B 1 144 ? 28.717 -28.523 -8.480  1.00 22.96 ?  144 VAL   B HG12 1 
ATOM   6236 H HG13 . VAL   B 1 144 ? 29.386 -27.638 -9.620  1.00 22.96 ?  144 VAL   B HG13 1 
ATOM   6237 H HG21 . VAL   B 1 144 ? 31.874 -29.615 -9.358  1.00 20.07 ?  144 VAL   B HG21 1 
ATOM   6238 H HG22 . VAL   B 1 144 ? 32.124 -28.095 -9.746  1.00 20.07 ?  144 VAL   B HG22 1 
ATOM   6239 H HG23 . VAL   B 1 144 ? 32.758 -28.691 -8.416  1.00 20.07 ?  144 VAL   B HG23 1 
ATOM   6240 N N    . ASP   B 1 145 ? 29.103 -26.524 -6.069  1.00 14.52 ?  145 ASP   B N    1 
ATOM   6241 C CA   . ASP   B 1 145 ? 27.795 -26.046 -5.638  1.00 15.24 ?  145 ASP   B CA   1 
ATOM   6242 C C    . ASP   B 1 145 ? 27.827 -24.623 -5.093  1.00 14.90 ?  145 ASP   B C    1 
ATOM   6243 O O    . ASP   B 1 145 ? 26.768 -24.076 -4.762  1.00 16.61 ?  145 ASP   B O    1 
ATOM   6244 C CB   . ASP   B 1 145 ? 27.203 -26.961 -4.559  1.00 17.05 ?  145 ASP   B CB   1 
ATOM   6245 C CG   . ASP   B 1 145 ? 26.857 -28.342 -5.066  1.00 18.70 ?  145 ASP   B CG   1 
ATOM   6246 O OD1  . ASP   B 1 145 ? 26.754 -28.534 -6.293  1.00 19.01 ?  145 ASP   B OD1  1 
ATOM   6247 O OD2  . ASP   B 1 145 ? 26.686 -29.230 -4.210  1.00 20.78 -1 145 ASP   B OD2  1 
ATOM   6248 H H    . ASP   B 1 145 ? 29.532 -26.963 -5.470  1.00 17.42 ?  145 ASP   B H    1 
ATOM   6249 H HA   . ASP   B 1 145 ? 27.201 -26.041 -6.402  1.00 18.29 ?  145 ASP   B HA   1 
ATOM   6250 H HB2  . ASP   B 1 145 ? 27.839 -27.069 -3.848  1.00 20.45 ?  145 ASP   B HB2  1 
ATOM   6251 H HB3  . ASP   B 1 145 ? 26.383 -26.559 -4.226  1.00 20.45 ?  145 ASP   B HB3  1 
ATOM   6252 N N    . THR   B 1 146 ? 29.005 -24.012 -4.978  1.00 13.18 ?  146 THR   B N    1 
ATOM   6253 C CA   . THR   B 1 146 ? 29.136 -22.687 -4.372  1.00 12.87 ?  146 THR   B CA   1 
ATOM   6254 C C    . THR   B 1 146 ? 29.764 -21.652 -5.289  1.00 12.42 ?  146 THR   B C    1 
ATOM   6255 O O    . THR   B 1 146 ? 29.308 -20.495 -5.330  1.00 13.02 ?  146 THR   B O    1 
ATOM   6256 C CB   . THR   B 1 146 ? 29.976 -22.792 -3.090  1.00 13.05 ?  146 THR   B CB   1 
ATOM   6257 O OG1  . THR   B 1 146 ? 29.402 -23.775 -2.222  1.00 13.45 ?  146 THR   B OG1  1 
ATOM   6258 C CG2  . THR   B 1 146 ? 30.051 -21.453 -2.369  1.00 13.55 ?  146 THR   B CG2  1 
ATOM   6259 H H    . THR   B 1 146 ? 29.758 -24.340 -5.242  1.00 15.82 ?  146 THR   B H    1 
ATOM   6260 H HA   . THR   B 1 146 ? 28.263 -22.360 -4.125  1.00 15.44 ?  146 THR   B HA   1 
ATOM   6261 H HB   . THR   B 1 146 ? 30.884 -23.048 -3.314  1.00 15.66 ?  146 THR   B HB   1 
ATOM   6262 H HG1  . THR   B 1 146 ? 29.432 -24.531 -2.593  1.00 16.14 ?  146 THR   B HG1  1 
ATOM   6263 H HG21 . THR   B 1 146 ? 30.404 -21.575 -1.475  1.00 16.26 ?  146 THR   B HG21 1 
ATOM   6264 H HG22 . THR   B 1 146 ? 30.635 -20.846 -2.855  1.00 16.26 ?  146 THR   B HG22 1 
ATOM   6265 H HG23 . THR   B 1 146 ? 29.168 -21.060 -2.310  1.00 16.26 ?  146 THR   B HG23 1 
ATOM   6266 N N    . VAL   B 1 147 ? 30.824 -22.025 -5.995  1.00 12.47 ?  147 VAL   B N    1 
ATOM   6267 C CA   . VAL   B 1 147 ? 31.553 -21.086 -6.832  1.00 12.05 ?  147 VAL   B CA   1 
ATOM   6268 C C    . VAL   B 1 147 ? 30.818 -20.959 -8.154  1.00 12.19 ?  147 VAL   B C    1 
ATOM   6269 O O    . VAL   B 1 147 ? 30.446 -21.963 -8.775  1.00 13.23 ?  147 VAL   B O    1 
ATOM   6270 C CB   . VAL   B 1 147 ? 33.003 -21.552 -7.038  1.00 12.25 ?  147 VAL   B CB   1 
ATOM   6271 C CG1  . VAL   B 1 147 ? 33.770 -20.532 -7.860  1.00 12.43 ?  147 VAL   B CG1  1 
ATOM   6272 C CG2  . VAL   B 1 147 ? 33.686 -21.764 -5.702  1.00 12.38 ?  147 VAL   B CG2  1 
ATOM   6273 H H    . VAL   B 1 147 ? 31.147 -22.830 -6.014  1.00 14.96 ?  147 VAL   B H    1 
ATOM   6274 H HA   . VAL   B 1 147 ? 31.573 -20.220 -6.400  1.00 14.46 ?  147 VAL   B HA   1 
ATOM   6275 H HB   . VAL   B 1 147 ? 33.008 -22.398 -7.522  1.00 14.70 ?  147 VAL   B HB   1 
ATOM   6276 H HG11 . VAL   B 1 147 ? 34.710 -20.762 -7.856  1.00 14.91 ?  147 VAL   B HG11 1 
ATOM   6277 H HG12 . VAL   B 1 147 ? 33.432 -20.535 -8.770  1.00 14.91 ?  147 VAL   B HG12 1 
ATOM   6278 H HG13 . VAL   B 1 147 ? 33.642 -19.654 -7.464  1.00 14.91 ?  147 VAL   B HG13 1 
ATOM   6279 H HG21 . VAL   B 1 147 ? 34.624 -21.966 -5.853  1.00 14.85 ?  147 VAL   B HG21 1 
ATOM   6280 H HG22 . VAL   B 1 147 ? 33.604 -20.953 -5.177  1.00 14.85 ?  147 VAL   B HG22 1 
ATOM   6281 H HG23 . VAL   B 1 147 ? 33.260 -22.502 -5.240  1.00 14.85 ?  147 VAL   B HG23 1 
ATOM   6282 N N    . ARG   B 1 148 ? 30.605 -19.714 -8.575  1.00 12.13 ?  148 ARG   B N    1 
ATOM   6283 C CA   . ARG   B 1 148 ? 29.983 -19.399 -9.850  1.00 12.42 ?  148 ARG   B CA   1 
ATOM   6284 C C    . ARG   B 1 148 ? 30.939 -18.726 -10.822 1.00 12.60 ?  148 ARG   B C    1 
ATOM   6285 O O    . ARG   B 1 148 ? 30.652 -18.699 -12.020 1.00 14.07 ?  148 ARG   B O    1 
ATOM   6286 C CB   . ARG   B 1 148 ? 28.748 -18.509 -9.636  1.00 12.83 ?  148 ARG   B CB   1 
ATOM   6287 C CG   . ARG   B 1 148 ? 27.668 -19.214 -8.829  1.00 13.84 ?  148 ARG   B CG   1 
ATOM   6288 C CD   . ARG   B 1 148 ? 26.467 -18.323 -8.525  1.00 14.50 ?  148 ARG   B CD   1 
ATOM   6289 N NE   . ARG   B 1 148 ? 26.864 -17.127 -7.790  1.00 14.54 ?  148 ARG   B NE   1 
ATOM   6290 C CZ   . ARG   B 1 148 ? 27.169 -17.095 -6.499  1.00 13.61 ?  148 ARG   B CZ   1 
ATOM   6291 N NH1  . ARG   B 1 148 ? 27.094 -18.178 -5.740  1.00 13.72 ?  148 ARG   B NH1  1 
ATOM   6292 N NH2  . ARG   B 1 148 ? 27.567 -15.948 -5.954  1.00 13.69 ?  148 ARG   B NH2  1 
ATOM   6293 H H    . ARG   B 1 148 ? 30.829 -19.012 -8.120  1.00 14.56 ?  148 ARG   B H    1 
ATOM   6294 H HA   . ARG   B 1 148 ? 29.686 -20.222 -10.257 1.00 14.91 ?  148 ARG   B HA   1 
ATOM   6295 H HB2  . ARG   B 1 148 ? 29.012 -17.709 -9.152  1.00 15.39 ?  148 ARG   B HB2  1 
ATOM   6296 H HB3  . ARG   B 1 148 ? 28.377 -18.270 -10.499 1.00 15.39 ?  148 ARG   B HB3  1 
ATOM   6297 H HG2  . ARG   B 1 148 ? 27.345 -19.981 -9.336  1.00 16.61 ?  148 ARG   B HG2  1 
ATOM   6298 H HG3  . ARG   B 1 148 ? 28.039 -19.512 -7.986  1.00 16.61 ?  148 ARG   B HG3  1 
ATOM   6299 H HD2  . ARG   B 1 148 ? 26.055 -18.041 -9.357  1.00 17.39 ?  148 ARG   B HD2  1 
ATOM   6300 H HD3  . ARG   B 1 148 ? 25.828 -18.812 -7.983  1.00 17.39 ?  148 ARG   B HD3  1 
ATOM   6301 H HE   . ARG   B 1 148 ? 26.917 -16.389 -8.226  1.00 17.44 ?  148 ARG   B HE   1 
ATOM   6302 H HH11 . ARG   B 1 148 ? 26.829 -18.928 -6.076  1.00 16.46 ?  148 ARG   B HH11 1 
ATOM   6303 H HH12 . ARG   B 1 148 ? 27.287 -18.136 -4.902  1.00 16.46 ?  148 ARG   B HH12 1 
ATOM   6304 H HH21 . ARG   B 1 148 ? 27.631 -15.243 -6.438  1.00 16.42 ?  148 ARG   B HH21 1 
ATOM   6305 H HH22 . ARG   B 1 148 ? 27.771 -15.916 -5.118  1.00 16.42 ?  148 ARG   B HH22 1 
ATOM   6306 N N    . THR   B 1 149 ? 32.049 -18.174 -10.335 1.00 12.60 ?  149 THR   B N    1 
ATOM   6307 C CA   . THR   B 1 149 ? 33.085 -17.609 -11.183 1.00 12.73 ?  149 THR   B CA   1 
ATOM   6308 C C    . THR   B 1 149 ? 33.971 -18.745 -11.693 1.00 11.94 ?  149 THR   B C    1 
ATOM   6309 O O    . THR   B 1 149 ? 33.782 -19.914 -11.351 1.00 12.64 ?  149 THR   B O    1 
ATOM   6310 C CB   . THR   B 1 149 ? 33.861 -16.559 -10.401 1.00 12.85 ?  149 THR   B CB   1 
ATOM   6311 O OG1  . THR   B 1 149 ? 34.322 -17.160 -9.187  1.00 12.80 ?  149 THR   B OG1  1 
ATOM   6312 C CG2  . THR   B 1 149 ? 32.976 -15.348 -10.097 1.00 13.72 ?  149 THR   B CG2  1 
ATOM   6313 H H    . THR   B 1 149 ? 32.222 -18.117 -9.493  1.00 15.11 ?  149 THR   B H    1 
ATOM   6314 H HA   . THR   B 1 149 ? 32.671 -17.176 -11.944 1.00 15.27 ?  149 THR   B HA   1 
ATOM   6315 H HB   . THR   B 1 149 ? 34.624 -16.271 -10.918 1.00 15.42 ?  149 THR   B HB   1 
ATOM   6316 H HG1  . THR   B 1 149 ? 34.740 -16.583 -8.724  1.00 15.36 ?  149 THR   B HG1  1 
ATOM   6317 H HG21 . THR   B 1 149 ? 33.484 -14.680 -9.608  1.00 16.46 ?  149 THR   B HG21 1 
ATOM   6318 H HG22 . THR   B 1 149 ? 32.661 -14.952 -10.927 1.00 16.46 ?  149 THR   B HG22 1 
ATOM   6319 H HG23 . THR   B 1 149 ? 32.211 -15.613 -9.565  1.00 16.46 ?  149 THR   B HG23 1 
ATOM   6320 N N    . ASN   B 1 150 ? 34.930 -18.423 -12.548 1.00 12.05 ?  150 ASN   B N    1 
ATOM   6321 C CA   . ASN   B 1 150 ? 35.697 -19.451 -13.243 1.00 12.75 ?  150 ASN   B CA   1 
ATOM   6322 C C    . ASN   B 1 150 ? 36.865 -19.900 -12.372 1.00 12.03 ?  150 ASN   B C    1 
ATOM   6323 O O    . ASN   B 1 150 ? 37.796 -19.126 -12.119 1.00 12.76 ?  150 ASN   B O    1 
ATOM   6324 C CB   . ASN   B 1 150 ? 36.169 -18.923 -14.589 1.00 14.44 ?  150 ASN   B CB   1 
ATOM   6325 C CG   . ASN   B 1 150 ? 35.024 -18.684 -15.525 1.00 17.31 ?  150 ASN   B CG   1 
ATOM   6326 O OD1  . ASN   B 1 150 ? 34.125 -19.509 -15.620 1.00 18.46 ?  150 ASN   B OD1  1 
ATOM   6327 N ND2  . ASN   B 1 150 ? 35.019 -17.537 -16.191 1.00 19.01 ?  150 ASN   B ND2  1 
ATOM   6328 H H    . ASN   B 1 150 ? 35.164 -17.615 -12.742 1.00 14.45 ?  150 ASN   B H    1 
ATOM   6329 H HA   . ASN   B 1 150 ? 35.117 -20.216 -13.409 1.00 15.29 ?  150 ASN   B HA   1 
ATOM   6330 H HB2  . ASN   B 1 150 ? 36.629 -18.079 -14.460 1.00 17.32 ?  150 ASN   B HB2  1 
ATOM   6331 H HB3  . ASN   B 1 150 ? 36.760 -19.569 -15.000 1.00 17.32 ?  150 ASN   B HB3  1 
ATOM   6332 H HD21 . ASN   B 1 150 ? 34.381 -17.354 -16.742 1.00 22.81 ?  150 ASN   B HD21 1 
ATOM   6333 H HD22 . ASN   B 1 150 ? 35.666 -16.976 -16.089 1.00 22.81 ?  150 ASN   B HD22 1 
ATOM   6334 N N    . VAL   B 1 151 ? 36.819 -21.147 -11.915 1.00 11.85 ?  151 VAL   B N    1 
ATOM   6335 C CA   . VAL   B 1 151 ? 37.837 -21.675 -11.024 1.00 12.10 ?  151 VAL   B CA   1 
ATOM   6336 C C    . VAL   B 1 151 ? 38.541 -22.844 -11.699 1.00 12.08 ?  151 VAL   B C    1 
ATOM   6337 O O    . VAL   B 1 151 ? 37.901 -23.780 -12.203 1.00 13.00 ?  151 VAL   B O    1 
ATOM   6338 C CB   . VAL   B 1 151 ? 37.276 -22.007 -9.628  1.00 13.33 ?  151 VAL   B CB   1 
ATOM   6339 C CG1  . VAL   B 1 151 ? 36.121 -23.004 -9.707  1.00 14.24 ?  151 VAL   B CG1  1 
ATOM   6340 C CG2  . VAL   B 1 151 ? 38.379 -22.496 -8.710  1.00 13.99 ?  151 VAL   B CG2  1 
ATOM   6341 H H    . VAL   B 1 151 ? 36.190 -21.709 -12.111 1.00 14.22 ?  151 VAL   B H    1 
ATOM   6342 H HA   . VAL   B 1 151 ? 38.502 -20.978 -10.898 1.00 14.51 ?  151 VAL   B HA   1 
ATOM   6343 H HB   . VAL   B 1 151 ? 36.923 -21.188 -9.242  1.00 15.99 ?  151 VAL   B HB   1 
ATOM   6344 H HG11 . VAL   B 1 151 ? 35.803 -23.191 -8.810  1.00 17.09 ?  151 VAL   B HG11 1 
ATOM   6345 H HG12 . VAL   B 1 151 ? 35.403 -22.620 -10.237 1.00 17.09 ?  151 VAL   B HG12 1 
ATOM   6346 H HG13 . VAL   B 1 151 ? 36.435 -23.822 -10.124 1.00 17.09 ?  151 VAL   B HG13 1 
ATOM   6347 H HG21 . VAL   B 1 151 ? 38.026 -22.572 -7.809  1.00 16.79 ?  151 VAL   B HG21 1 
ATOM   6348 H HG22 . VAL   B 1 151 ? 38.690 -23.360 -9.018  1.00 16.79 ?  151 VAL   B HG22 1 
ATOM   6349 H HG23 . VAL   B 1 151 ? 39.110 -21.855 -8.723  1.00 16.79 ?  151 VAL   B HG23 1 
ATOM   6350 N N    . TYR   B 1 152 ? 39.867 -22.756 -11.719 1.00 11.44 ?  152 TYR   B N    1 
ATOM   6351 C CA   . TYR   B 1 152 ? 40.773 -23.730 -12.304 1.00 11.78 ?  152 TYR   B CA   1 
ATOM   6352 C C    . TYR   B 1 152 ? 41.493 -24.410 -11.145 1.00 11.26 ?  152 TYR   B C    1 
ATOM   6353 O O    . TYR   B 1 152 ? 42.345 -23.794 -10.494 1.00 11.78 ?  152 TYR   B O    1 
ATOM   6354 C CB   . TYR   B 1 152 ? 41.742 -23.013 -13.245 1.00 12.56 ?  152 TYR   B CB   1 
ATOM   6355 C CG   . TYR   B 1 152 ? 41.063 -22.551 -14.510 1.00 12.99 ?  152 TYR   B CG   1 
ATOM   6356 C CD1  . TYR   B 1 152 ? 40.395 -21.330 -14.577 1.00 13.59 ?  152 TYR   B CD1  1 
ATOM   6357 C CD2  . TYR   B 1 152 ? 41.064 -23.358 -15.632 1.00 14.09 ?  152 TYR   B CD2  1 
ATOM   6358 C CE1  . TYR   B 1 152 ? 39.756 -20.931 -15.739 1.00 15.11 ?  152 TYR   B CE1  1 
ATOM   6359 C CE2  . TYR   B 1 152 ? 40.434 -22.972 -16.794 1.00 15.42 ?  152 TYR   B CE2  1 
ATOM   6360 C CZ   . TYR   B 1 152 ? 39.780 -21.758 -16.847 1.00 15.81 ?  152 TYR   B CZ   1 
ATOM   6361 O OH   . TYR   B 1 152 ? 39.155 -21.387 -18.013 1.00 18.18 ?  152 TYR   B OH   1 
ATOM   6362 H H    . TYR   B 1 152 ? 40.299 -22.095 -11.358 1.00 13.73 ?  152 TYR   B H    1 
ATOM   6363 H HA   . TYR   B 1 152 ? 40.271 -24.393 -12.805 1.00 14.14 ?  152 TYR   B HA   1 
ATOM   6364 H HB2  . TYR   B 1 152 ? 42.102 -22.232 -12.790 1.00 15.07 ?  152 TYR   B HB2  1 
ATOM   6365 H HB3  . TYR   B 1 152 ? 42.460 -23.616 -13.486 1.00 15.07 ?  152 TYR   B HB3  1 
ATOM   6366 H HD1  . TYR   B 1 152 ? 40.373 -20.774 -13.829 1.00 16.30 ?  152 TYR   B HD1  1 
ATOM   6367 H HD2  . TYR   B 1 152 ? 41.501 -24.181 -15.600 1.00 16.91 ?  152 TYR   B HD2  1 
ATOM   6368 H HE1  . TYR   B 1 152 ? 39.314 -20.112 -15.776 1.00 18.13 ?  152 TYR   B HE1  1 
ATOM   6369 H HE2  . TYR   B 1 152 ? 40.451 -23.528 -17.537 1.00 18.50 ?  152 TYR   B HE2  1 
ATOM   6370 H HH   . TYR   B 1 152 ? 38.798 -20.634 -17.917 1.00 21.81 ?  152 TYR   B HH   1 
ATOM   6371 N N    . LEU   B 1 153 ? 41.130 -25.665 -10.874 1.00 11.46 ?  153 LEU   B N    1 
ATOM   6372 C CA   . LEU   B 1 153 ? 41.646 -26.412 -9.737  1.00 11.06 ?  153 LEU   B CA   1 
ATOM   6373 C C    . LEU   B 1 153 ? 42.876 -27.213 -10.139 1.00 11.53 ?  153 LEU   B C    1 
ATOM   6374 O O    . LEU   B 1 153 ? 42.852 -27.944 -11.131 1.00 12.70 ?  153 LEU   B O    1 
ATOM   6375 C CB   . LEU   B 1 153 ? 40.573 -27.369 -9.214  1.00 11.64 ?  153 LEU   B CB   1 
ATOM   6376 C CG   . LEU   B 1 153 ? 39.310 -26.719 -8.648  1.00 12.58 ?  153 LEU   B CG   1 
ATOM   6377 C CD1  . LEU   B 1 153 ? 38.204 -27.760 -8.494  1.00 13.32 ?  153 LEU   B CD1  1 
ATOM   6378 C CD2  . LEU   B 1 153 ? 39.606 -26.060 -7.309  1.00 13.15 ?  153 LEU   B CD2  1 
ATOM   6379 H H    . LEU   B 1 153 ? 40.559 -26.111 -11.347 1.00 13.74 ?  153 LEU   B H    1 
ATOM   6380 H HA   . LEU   B 1 153 ? 41.880 -25.790 -9.030  1.00 13.27 ?  153 LEU   B HA   1 
ATOM   6381 H HB2  . LEU   B 1 153 ? 40.296 -27.943 -9.938  1.00 13.97 ?  153 LEU   B HB2  1 
ATOM   6382 H HB3  . LEU   B 1 153 ? 40.962 -27.900 -8.503  1.00 13.97 ?  153 LEU   B HB3  1 
ATOM   6383 H HG   . LEU   B 1 153 ? 38.992 -26.028 -9.254  1.00 15.09 ?  153 LEU   B HG   1 
ATOM   6384 H HD11 . LEU   B 1 153 ? 37.394 -27.317 -8.185  1.00 15.98 ?  153 LEU   B HD11 1 
ATOM   6385 H HD12 . LEU   B 1 153 ? 38.046 -28.173 -9.353  1.00 15.98 ?  153 LEU   B HD12 1 
ATOM   6386 H HD13 . LEU   B 1 153 ? 38.485 -28.420 -7.846  1.00 15.98 ?  153 LEU   B HD13 1 
ATOM   6387 H HD21 . LEU   B 1 153 ? 38.789 -25.681 -6.946  1.00 15.78 ?  153 LEU   B HD21 1 
ATOM   6388 H HD22 . LEU   B 1 153 ? 39.958 -26.728 -6.698  1.00 15.78 ?  153 LEU   B HD22 1 
ATOM   6389 H HD23 . LEU   B 1 153 ? 40.263 -25.357 -7.439  1.00 15.78 ?  153 LEU   B HD23 1 
ATOM   6390 N N    . ALA   B 1 154 ? 43.933 -27.099 -9.344  1.00 12.07 ?  154 ALA   B N    1 
ATOM   6391 C CA   . ALA   B 1 154 ? 45.160 -27.859 -9.530  1.00 13.18 ?  154 ALA   B CA   1 
ATOM   6392 C C    . ALA   B 1 154 ? 45.223 -28.937 -8.456  1.00 13.69 ?  154 ALA   B C    1 
ATOM   6393 O O    . ALA   B 1 154 ? 45.155 -28.635 -7.255  1.00 14.96 ?  154 ALA   B O    1 
ATOM   6394 C CB   . ALA   B 1 154 ? 46.378 -26.940 -9.451  1.00 13.78 ?  154 ALA   B CB   1 
ATOM   6395 H H    . ALA   B 1 154 ? 43.964 -26.557 -8.670  1.00 14.48 ?  154 ALA   B H    1 
ATOM   6396 H HA   . ALA   B 1 154 ? 45.152 -28.280 -10.401 1.00 15.82 ?  154 ALA   B HA   1 
ATOM   6397 H HB1  . ALA   B 1 154 ? 47.183 -27.466 -9.577  1.00 16.54 ?  154 ALA   B HB1  1 
ATOM   6398 H HB2  . ALA   B 1 154 ? 46.316 -26.263 -10.147 1.00 16.54 ?  154 ALA   B HB2  1 
ATOM   6399 H HB3  . ALA   B 1 154 ? 46.399 -26.509 -8.580  1.00 16.54 ?  154 ALA   B HB3  1 
ATOM   6400 N N    . VAL   B 1 155 ? 45.342 -30.187 -8.888  1.00 12.82 ?  155 VAL   B N    1 
ATOM   6401 C CA   . VAL   B 1 155 ? 45.451 -31.330 -7.993  1.00 13.06 ?  155 VAL   B CA   1 
ATOM   6402 C C    . VAL   B 1 155 ? 46.790 -31.999 -8.276  1.00 13.15 ?  155 VAL   B C    1 
ATOM   6403 O O    . VAL   B 1 155 ? 47.018 -32.497 -9.385  1.00 14.90 ?  155 VAL   B O    1 
ATOM   6404 C CB   . VAL   B 1 155 ? 44.295 -32.322 -8.184  1.00 14.44 ?  155 VAL   B CB   1 
ATOM   6405 C CG1  . VAL   B 1 155 ? 44.482 -33.521 -7.276  1.00 14.41 ?  155 VAL   B CG1  1 
ATOM   6406 C CG2  . VAL   B 1 155 ? 42.958 -31.640 -7.912  1.00 15.55 ?  155 VAL   B CG2  1 
ATOM   6407 H H    . VAL   B 1 155 ? 45.372 -30.401 -9.722  1.00 15.38 ?  155 VAL   B H    1 
ATOM   6408 H HA   . VAL   B 1 155 ? 45.444 -31.029 -7.074  1.00 15.67 ?  155 VAL   B HA   1 
ATOM   6409 H HB   . VAL   B 1 155 ? 44.288 -32.632 -9.104  1.00 17.33 ?  155 VAL   B HB   1 
ATOM   6410 H HG11 . VAL   B 1 155 ? 43.652 -34.021 -7.232  1.00 17.30 ?  155 VAL   B HG11 1 
ATOM   6411 H HG12 . VAL   B 1 155 ? 45.185 -34.089 -7.638  1.00 17.30 ?  155 VAL   B HG12 1 
ATOM   6412 H HG13 . VAL   B 1 155 ? 44.729 -33.215 -6.390  1.00 17.30 ?  155 VAL   B HG13 1 
ATOM   6413 H HG21 . VAL   B 1 155 ? 42.247 -32.296 -8.003  1.00 18.65 ?  155 VAL   B HG21 1 
ATOM   6414 H HG22 . VAL   B 1 155 ? 42.966 -31.285 -7.010  1.00 18.65 ?  155 VAL   B HG22 1 
ATOM   6415 H HG23 . VAL   B 1 155 ? 42.831 -30.924 -8.552  1.00 18.65 ?  155 VAL   B HG23 1 
ATOM   6416 N N    . PHE   B 1 156 ? 47.661 -32.035 -7.265  1.00 13.33 ?  156 PHE   B N    1 
ATOM   6417 C CA   . PHE   B 1 156 ? 49.036 -32.499 -7.466  1.00 14.87 ?  156 PHE   B CA   1 
ATOM   6418 C C    . PHE   B 1 156 ? 49.125 -34.001 -7.742  1.00 15.82 ?  156 PHE   B C    1 
ATOM   6419 O O    . PHE   B 1 156 ? 49.837 -34.434 -8.658  1.00 17.88 ?  156 PHE   B O    1 
ATOM   6420 C CB   . PHE   B 1 156 ? 49.873 -32.125 -6.245  1.00 14.66 ?  156 PHE   B CB   1 
ATOM   6421 C CG   . PHE   B 1 156 ? 51.294 -32.591 -6.312  1.00 15.50 ?  156 PHE   B CG   1 
ATOM   6422 C CD1  . PHE   B 1 156 ? 52.163 -32.076 -7.255  1.00 16.99 ?  156 PHE   B CD1  1 
ATOM   6423 C CD2  . PHE   B 1 156 ? 51.762 -33.525 -5.417  1.00 15.97 ?  156 PHE   B CD2  1 
ATOM   6424 C CE1  . PHE   B 1 156 ? 53.482 -32.488 -7.307  1.00 17.99 ?  156 PHE   B CE1  1 
ATOM   6425 C CE2  . PHE   B 1 156 ? 53.076 -33.942 -5.463  1.00 16.94 ?  156 PHE   B CE2  1 
ATOM   6426 C CZ   . PHE   B 1 156 ? 53.932 -33.429 -6.416  1.00 17.50 ?  156 PHE   B CZ   1 
ATOM   6427 H H    . PHE   B 1 156 ? 47.478 -31.803 -6.457  1.00 16.00 ?  156 PHE   B H    1 
ATOM   6428 H HA   . PHE   B 1 156 ? 49.403 -32.036 -8.232  1.00 17.85 ?  156 PHE   B HA   1 
ATOM   6429 H HB2  . PHE   B 1 156 ? 49.881 -31.157 -6.163  1.00 17.59 ?  156 PHE   B HB2  1 
ATOM   6430 H HB3  . PHE   B 1 156 ? 49.468 -32.516 -5.456  1.00 17.59 ?  156 PHE   B HB3  1 
ATOM   6431 H HD1  . PHE   B 1 156 ? 51.860 -31.437 -7.862  1.00 20.38 ?  156 PHE   B HD1  1 
ATOM   6432 H HD2  . PHE   B 1 156 ? 51.184 -33.880 -4.777  1.00 19.16 ?  156 PHE   B HD2  1 
ATOM   6433 H HE1  . PHE   B 1 156 ? 54.056 -32.140 -7.951  1.00 21.58 ?  156 PHE   B HE1  1 
ATOM   6434 H HE2  . PHE   B 1 156 ? 53.383 -34.588 -4.861  1.00 20.33 ?  156 PHE   B HE2  1 
ATOM   6435 H HZ   . PHE   B 1 156 ? 54.818 -33.718 -6.449  1.00 21.00 ?  156 PHE   B HZ   1 
ATOM   6436 N N    . ASP   B 1 157 ? 48.461 -34.816 -6.936  1.00 16.03 ?  157 ASP   B N    1 
ATOM   6437 C CA   . ASP   B 1 157 ? 48.613 -36.262 -7.030  1.00 17.44 ?  157 ASP   B CA   1 
ATOM   6438 C C    . ASP   B 1 157 ? 47.697 -36.809 -8.118  1.00 17.64 ?  157 ASP   B C    1 
ATOM   6439 O O    . ASP   B 1 157 ? 46.471 -36.690 -8.014  1.00 17.15 ?  157 ASP   B O    1 
ATOM   6440 C CB   . ASP   B 1 157 ? 48.252 -36.876 -5.685  1.00 19.38 ?  157 ASP   B CB   1 
ATOM   6441 C CG   . ASP   B 1 157 ? 48.400 -38.381 -5.669  1.00 20.84 ?  157 ASP   B CG   1 
ATOM   6442 O OD1  . ASP   B 1 157 ? 48.721 -38.985 -6.723  1.00 21.22 ?  157 ASP   B OD1  1 
ATOM   6443 O OD2  . ASP   B 1 157 ? 48.215 -38.958 -4.581  1.00 22.62 -1 157 ASP   B OD2  1 
ATOM   6444 H H    . ASP   B 1 157 ? 47.925 -34.561 -6.325  1.00 19.24 ?  157 ASP   B H    1 
ATOM   6445 H HA   . ASP   B 1 157 ? 49.533 -36.494 -7.248  1.00 20.92 ?  157 ASP   B HA   1 
ATOM   6446 H HB2  . ASP   B 1 157 ? 48.825 -36.500 -5.006  1.00 23.26 ?  157 ASP   B HB2  1 
ATOM   6447 H HB3  . ASP   B 1 157 ? 47.322 -36.666 -5.488  1.00 23.26 ?  157 ASP   B HB3  1 
ATOM   6448 N N    . LYS   B 1 158 ? 48.290 -37.438 -9.141  1.00 18.78 ?  158 LYS   B N    1 
ATOM   6449 C CA   . LYS   B 1 158 ? 47.511 -38.034 -10.228 1.00 19.93 ?  158 LYS   B CA   1 
ATOM   6450 C C    . LYS   B 1 158 ? 46.450 -39.002 -9.703  1.00 19.68 ?  158 LYS   B C    1 
ATOM   6451 O O    . LYS   B 1 158 ? 45.342 -39.088 -10.250 1.00 19.86 ?  158 LYS   B O    1 
ATOM   6452 C CB   . LYS   B 1 158 ? 48.458 -38.740 -11.209 1.00 21.81 ?  158 LYS   B CB   1 
ATOM   6453 C CG   . LYS   B 1 158 ? 47.785 -39.654 -12.225 1.00 24.08 ?  158 LYS   B CG   1 
ATOM   6454 C CD   . LYS   B 1 158 ? 46.914 -38.891 -13.201 1.00 26.85 ?  158 LYS   B CD   1 
ATOM   6455 C CE   . LYS   B 1 158 ? 46.340 -39.827 -14.251 1.00 28.73 ?  158 LYS   B CE   1 
ATOM   6456 N NZ   . LYS   B 1 158 ? 45.258 -39.185 -15.047 1.00 29.14 ?  158 LYS   B NZ   1 
ATOM   6457 H H    . LYS   B 1 158 ? 49.146 -37.535 -9.229  1.00 22.53 ?  158 LYS   B H    1 
ATOM   6458 H HA   . LYS   B 1 158 ? 47.064 -37.328 -10.721 1.00 23.92 ?  158 LYS   B HA   1 
ATOM   6459 H HB2  . LYS   B 1 158 ? 48.950 -38.066 -11.714 1.00 26.17 ?  158 LYS   B HB2  1 
ATOM   6460 H HB3  . LYS   B 1 158 ? 49.087 -39.281 -10.705 1.00 26.17 ?  158 LYS   B HB3  1 
ATOM   6461 H HG2  . LYS   B 1 158 ? 48.471 -40.111 -12.739 1.00 28.89 ?  158 LYS   B HG2  1 
ATOM   6462 H HG3  . LYS   B 1 158 ? 47.234 -40.311 -11.769 1.00 28.89 ?  158 LYS   B HG3  1 
ATOM   6463 H HD2  . LYS   B 1 158 ? 46.179 -38.477 -12.724 1.00 32.22 ?  158 LYS   B HD2  1 
ATOM   6464 H HD3  . LYS   B 1 158 ? 47.448 -38.217 -13.652 1.00 32.22 ?  158 LYS   B HD3  1 
ATOM   6465 H HE2  . LYS   B 1 158 ? 47.045 -40.092 -14.861 1.00 34.48 ?  158 LYS   B HE2  1 
ATOM   6466 H HE3  . LYS   B 1 158 ? 45.969 -40.609 -13.813 1.00 34.48 ?  158 LYS   B HE3  1 
ATOM   6467 H HZ1  . LYS   B 1 158 ? 44.943 -39.758 -15.651 1.00 34.96 ?  158 LYS   B HZ1  1 
ATOM   6468 H HZ2  . LYS   B 1 158 ? 44.593 -38.935 -14.511 1.00 34.96 ?  158 LYS   B HZ2  1 
ATOM   6469 H HZ3  . LYS   B 1 158 ? 45.576 -38.468 -15.467 1.00 34.96 ?  158 LYS   B HZ3  1 
ATOM   6470 N N    . ASN   B 1 159 ? 46.776 -39.762 -8.657  1.00 19.83 ?  159 ASN   B N    1 
ATOM   6471 C CA   . ASN   B 1 159 ? 45.821 -40.740 -8.147  1.00 20.31 ?  159 ASN   B CA   1 
ATOM   6472 C C    . ASN   B 1 159 ? 44.632 -40.067 -7.457  1.00 19.45 ?  159 ASN   B C    1 
ATOM   6473 O O    . ASN   B 1 159 ? 43.502 -40.566 -7.544  1.00 19.95 ?  159 ASN   B O    1 
ATOM   6474 C CB   . ASN   B 1 159 ? 46.534 -41.723 -7.225  1.00 22.06 ?  159 ASN   B CB   1 
ATOM   6475 C CG   . ASN   B 1 159 ? 47.573 -42.549 -7.955  1.00 24.20 ?  159 ASN   B CG   1 
ATOM   6476 O OD1  . ASN   B 1 159 ? 47.329 -43.036 -9.066  1.00 24.63 ?  159 ASN   B OD1  1 
ATOM   6477 N ND2  . ASN   B 1 159 ? 48.741 -42.721 -7.334  1.00 24.87 ?  159 ASN   B ND2  1 
ATOM   6478 H H    . ASN   B 1 159 ? 47.526 -39.725 -8.244  1.00 23.79 ?  159 ASN   B H    1 
ATOM   6479 H HA   . ASN   B 1 159 ? 45.477 -41.245 -8.904  1.00 24.37 ?  159 ASN   B HA   1 
ATOM   6480 H HB2  . ASN   B 1 159 ? 46.983 -41.234 -6.522  1.00 26.47 ?  159 ASN   B HB2  1 
ATOM   6481 H HB3  . ASN   B 1 159 ? 45.885 -42.335 -6.855  1.00 26.47 ?  159 ASN   B HB3  1 
ATOM   6482 H HD21 . ASN   B 1 159 ? 49.369 -43.181 -7.708  1.00 29.84 ?  159 ASN   B HD21 1 
ATOM   6483 H HD22 . ASN   B 1 159 ? 48.869 -42.384 -6.553  1.00 29.84 ?  159 ASN   B HD22 1 
ATOM   6484 N N    . LEU   B 1 160 ? 44.849 -38.928 -6.792  1.00 18.40 ?  160 LEU   B N    1 
ATOM   6485 C CA   . LEU   B 1 160 ? 43.718 -38.192 -6.246  1.00 17.08 ?  160 LEU   B CA   1 
ATOM   6486 C C    . LEU   B 1 160 ? 42.924 -37.532 -7.358  1.00 16.15 ?  160 LEU   B C    1 
ATOM   6487 O O    . LEU   B 1 160 ? 41.688 -37.540 -7.334  1.00 16.21 ?  160 LEU   B O    1 
ATOM   6488 C CB   . LEU   B 1 160 ? 44.183 -37.156 -5.227  1.00 17.10 ?  160 LEU   B CB   1 
ATOM   6489 C CG   . LEU   B 1 160 ? 43.056 -36.261 -4.697  1.00 16.87 ?  160 LEU   B CG   1 
ATOM   6490 C CD1  . LEU   B 1 160 ? 41.933 -37.083 -4.084  1.00 17.69 ?  160 LEU   B CD1  1 
ATOM   6491 C CD2  . LEU   B 1 160 ? 43.611 -35.283 -3.683  1.00 16.84 ?  160 LEU   B CD2  1 
ATOM   6492 H H    . LEU   B 1 160 ? 45.629 -38.574 -6.658  1.00 22.08 ?  160 LEU   B H    1 
ATOM   6493 H HA   . LEU   B 1 160 ? 43.136 -38.820 -5.800  1.00 20.50 ?  160 LEU   B HA   1 
ATOM   6494 H HB2  . LEU   B 1 160 ? 44.579 -37.623 -4.473  1.00 20.51 ?  160 LEU   B HB2  1 
ATOM   6495 H HB3  . LEU   B 1 160 ? 44.852 -36.588 -5.645  1.00 20.51 ?  160 LEU   B HB3  1 
ATOM   6496 H HG   . LEU   B 1 160 ? 42.691 -35.748 -5.433  1.00 20.25 ?  160 LEU   B HG   1 
ATOM   6497 H HD11 . LEU   B 1 160 ? 41.306 -36.483 -3.658  1.00 21.22 ?  160 LEU   B HD11 1 
ATOM   6498 H HD12 . LEU   B 1 160 ? 41.488 -37.588 -4.783  1.00 21.22 ?  160 LEU   B HD12 1 
ATOM   6499 H HD13 . LEU   B 1 160 ? 42.310 -37.691 -3.426  1.00 21.22 ?  160 LEU   B HD13 1 
ATOM   6500 H HD21 . LEU   B 1 160 ? 42.892 -34.707 -3.381  1.00 20.21 ?  160 LEU   B HD21 1 
ATOM   6501 H HD22 . LEU   B 1 160 ? 43.977 -35.778 -2.934  1.00 20.21 ?  160 LEU   B HD22 1 
ATOM   6502 H HD23 . LEU   B 1 160 ? 44.307 -34.752 -4.102  1.00 20.21 ?  160 LEU   B HD23 1 
ATOM   6503 N N    . TYR   B 1 161 ? 43.620 -36.957 -8.343  1.00 16.64 ?  161 TYR   B N    1 
ATOM   6504 C CA   . TYR   B 1 161 ? 42.945 -36.390 -9.505  1.00 16.60 ?  161 TYR   B CA   1 
ATOM   6505 C C    . TYR   B 1 161 ? 42.003 -37.415 -10.123 1.00 16.54 ?  161 TYR   B C    1 
ATOM   6506 O O    . TYR   B 1 161 ? 40.831 -37.125 -10.375 1.00 16.12 ?  161 TYR   B O    1 
ATOM   6507 C CB   . TYR   B 1 161 ? 43.981 -35.906 -10.529 1.00 17.09 ?  161 TYR   B CB   1 
ATOM   6508 C CG   . TYR   B 1 161 ? 43.399 -35.446 -11.847 1.00 17.62 ?  161 TYR   B CG   1 
ATOM   6509 C CD1  . TYR   B 1 161 ? 42.992 -34.128 -12.021 1.00 17.61 ?  161 TYR   B CD1  1 
ATOM   6510 C CD2  . TYR   B 1 161 ? 43.247 -36.326 -12.915 1.00 18.25 ?  161 TYR   B CD2  1 
ATOM   6511 C CE1  . TYR   B 1 161 ? 42.458 -33.697 -13.214 1.00 18.87 ?  161 TYR   B CE1  1 
ATOM   6512 C CE2  . TYR   B 1 161 ? 42.708 -35.903 -14.114 1.00 19.65 ?  161 TYR   B CE2  1 
ATOM   6513 C CZ   . TYR   B 1 161 ? 42.319 -34.585 -14.258 1.00 19.40 ?  161 TYR   B CZ   1 
ATOM   6514 O OH   . TYR   B 1 161 ? 41.777 -34.153 -15.446 1.00 21.21 ?  161 TYR   B OH   1 
ATOM   6515 H H    . TYR   B 1 161 ? 44.476 -36.895 -8.373  1.00 19.97 ?  161 TYR   B H    1 
ATOM   6516 H HA   . TYR   B 1 161 ? 42.416 -35.627 -9.229  1.00 19.91 ?  161 TYR   B HA   1 
ATOM   6517 H HB2  . TYR   B 1 161 ? 44.463 -35.153 -10.152 1.00 20.50 ?  161 TYR   B HB2  1 
ATOM   6518 H HB3  . TYR   B 1 161 ? 44.595 -36.626 -10.723 1.00 20.50 ?  161 TYR   B HB3  1 
ATOM   6519 H HD1  . TYR   B 1 161 ? 43.081 -33.521 -11.324 1.00 21.13 ?  161 TYR   B HD1  1 
ATOM   6520 H HD2  . TYR   B 1 161 ? 43.508 -37.213 -12.825 1.00 21.90 ?  161 TYR   B HD2  1 
ATOM   6521 H HE1  . TYR   B 1 161 ? 42.189 -32.808 -13.315 1.00 22.64 ?  161 TYR   B HE1  1 
ATOM   6522 H HE2  . TYR   B 1 161 ? 42.612 -36.499 -14.823 1.00 23.58 ?  161 TYR   B HE2  1 
ATOM   6523 H HH   . TYR   B 1 161 ? 41.757 -34.785 -16.002 1.00 25.45 ?  161 TYR   B HH   1 
ATOM   6524 N N    . ASP   B 1 162 ? 42.500 -38.634 -10.351 1.00 17.15 ?  162 ASP   B N    1 
ATOM   6525 C CA   . ASP   B 1 162 ? 41.675 -39.671 -10.963 1.00 17.54 ?  162 ASP   B CA   1 
ATOM   6526 C C    . ASP   B 1 162 ? 40.468 -40.010 -10.094 1.00 16.78 ?  162 ASP   B C    1 
ATOM   6527 O O    . ASP   B 1 162 ? 39.365 -40.224 -10.611 1.00 17.18 ?  162 ASP   B O    1 
ATOM   6528 C CB   . ASP   B 1 162 ? 42.508 -40.931 -11.215 1.00 19.16 ?  162 ASP   B CB   1 
ATOM   6529 C CG   . ASP   B 1 162 ? 43.516 -40.766 -12.339 1.00 20.79 ?  162 ASP   B CG   1 
ATOM   6530 O OD1  . ASP   B 1 162 ? 43.394 -39.818 -13.137 1.00 20.98 ?  162 ASP   B OD1  1 
ATOM   6531 O OD2  . ASP   B 1 162 ? 44.423 -41.620 -12.440 1.00 22.53 -1 162 ASP   B OD2  1 
ATOM   6532 H H    . ASP   B 1 162 ? 43.296 -38.878 -10.161 1.00 20.58 ?  162 ASP   B H    1 
ATOM   6533 H HA   . ASP   B 1 162 ? 41.346 -39.354 -11.817 1.00 21.04 ?  162 ASP   B HA   1 
ATOM   6534 H HB2  . ASP   B 1 162 ? 43.003 -41.149 -10.411 1.00 22.98 ?  162 ASP   B HB2  1 
ATOM   6535 H HB3  . ASP   B 1 162 ? 41.915 -41.660 -11.450 1.00 22.98 ?  162 ASP   B HB3  1 
ATOM   6536 N N    A LYS   B 1 163 ? 40.654 -40.070 -8.773  0.40 16.77 ?  163 LYS   B N    1 
ATOM   6537 N N    B LYS   B 1 163 ? 40.661 -40.085 -8.776  0.60 16.20 ?  163 LYS   B N    1 
ATOM   6538 C CA   A LYS   B 1 163 ? 39.529 -40.368 -7.889  0.40 17.39 ?  163 LYS   B CA   1 
ATOM   6539 C CA   B LYS   B 1 163 ? 39.538 -40.362 -7.886  0.60 16.56 ?  163 LYS   B CA   1 
ATOM   6540 C C    A LYS   B 1 163 ? 38.492 -39.252 -7.916  0.40 15.96 ?  163 LYS   B C    1 
ATOM   6541 C C    B LYS   B 1 163 ? 38.495 -39.256 -7.961  0.60 15.55 ?  163 LYS   B C    1 
ATOM   6542 O O    A LYS   B 1 163 ? 37.284 -39.516 -7.857  0.40 16.56 ?  163 LYS   B O    1 
ATOM   6543 O O    B LYS   B 1 163 ? 37.287 -39.529 -7.999  0.60 16.30 ?  163 LYS   B O    1 
ATOM   6544 C CB   A LYS   B 1 163 ? 40.019 -40.594 -6.460  0.40 19.79 ?  163 LYS   B CB   1 
ATOM   6545 C CB   B LYS   B 1 163 ? 40.034 -40.524 -6.451  0.60 18.67 ?  163 LYS   B CB   1 
ATOM   6546 C CG   A LYS   B 1 163 ? 38.938 -41.140 -5.543  0.40 22.86 ?  163 LYS   B CG   1 
ATOM   6547 C CG   B LYS   B 1 163 ? 38.971 -41.034 -5.500  0.60 22.35 ?  163 LYS   B CG   1 
ATOM   6548 C CD   A LYS   B 1 163 ? 39.344 -41.106 -4.082  0.40 25.55 ?  163 LYS   B CD   1 
ATOM   6549 C CD   B LYS   B 1 163 ? 39.489 -41.177 -4.081  0.60 25.99 ?  163 LYS   B CD   1 
ATOM   6550 C CE   A LYS   B 1 163 ? 38.279 -41.764 -3.220  0.40 27.76 ?  163 LYS   B CE   1 
ATOM   6551 C CE   B LYS   B 1 163 ? 38.459 -41.881 -3.213  0.60 28.71 ?  163 LYS   B CE   1 
ATOM   6552 N NZ   A LYS   B 1 163 ? 38.414 -41.410 -1.782  0.40 28.76 ?  163 LYS   B NZ   1 
ATOM   6553 N NZ   B LYS   B 1 163 ? 38.655 -41.618 -1.761  0.60 30.30 ?  163 LYS   B NZ   1 
ATOM   6554 H H    A LYS   B 1 163 ? 41.408 -39.951 -8.374  0.40 20.12 ?  163 LYS   B H    1 
ATOM   6555 H H    B LYS   B 1 163 ? 41.420 -39.984 -8.381  0.60 19.43 ?  163 LYS   B H    1 
ATOM   6556 H HA   A LYS   B 1 163 ? 39.101 -41.185 -8.191  0.40 20.86 ?  163 LYS   B HA   1 
ATOM   6557 H HA   B LYS   B 1 163 ? 39.119 -41.194 -8.158  0.60 19.87 ?  163 LYS   B HA   1 
ATOM   6558 H HB2  A LYS   B 1 163 ? 40.749 -41.234 -6.473  0.40 23.75 ?  163 LYS   B HB2  1 
ATOM   6559 H HB2  B LYS   B 1 163 ? 40.767 -41.159 -6.443  0.60 22.40 ?  163 LYS   B HB2  1 
ATOM   6560 H HB3  A LYS   B 1 163 ? 40.324 -39.751 -6.094  0.40 23.75 ?  163 LYS   B HB3  1 
ATOM   6561 H HB3  B LYS   B 1 163 ? 40.335 -39.664 -6.125  0.60 22.40 ?  163 LYS   B HB3  1 
ATOM   6562 H HG2  A LYS   B 1 163 ? 38.133 -40.607 -5.641  0.40 27.43 ?  163 LYS   B HG2  1 
ATOM   6563 H HG2  B LYS   B 1 163 ? 38.227 -40.412 -5.486  0.60 26.82 ?  163 LYS   B HG2  1 
ATOM   6564 H HG3  A LYS   B 1 163 ? 38.755 -42.063 -5.782  0.40 27.43 ?  163 LYS   B HG3  1 
ATOM   6565 H HG3  B LYS   B 1 163 ? 38.667 -41.908 -5.797  0.60 26.82 ?  163 LYS   B HG3  1 
ATOM   6566 H HD2  A LYS   B 1 163 ? 40.176 -41.592 -3.966  0.40 30.65 ?  163 LYS   B HD2  1 
ATOM   6567 H HD2  B LYS   B 1 163 ? 40.303 -41.706 -4.085  0.60 31.18 ?  163 LYS   B HD2  1 
ATOM   6568 H HD3  A LYS   B 1 163 ? 39.447 -40.185 -3.796  0.40 30.65 ?  163 LYS   B HD3  1 
ATOM   6569 H HD3  B LYS   B 1 163 ? 39.658 -40.298 -3.708  0.60 31.18 ?  163 LYS   B HD3  1 
ATOM   6570 H HE2  A LYS   B 1 163 ? 37.401 -41.489 -3.524  0.40 33.31 ?  163 LYS   B HE2  1 
ATOM   6571 H HE2  B LYS   B 1 163 ? 37.573 -41.572 -3.459  0.60 34.45 ?  163 LYS   B HE2  1 
ATOM   6572 H HE3  A LYS   B 1 163 ? 38.365 -42.726 -3.299  0.40 33.31 ?  163 LYS   B HE3  1 
ATOM   6573 H HE3  B LYS   B 1 163 ? 38.527 -42.838 -3.357  0.60 34.45 ?  163 LYS   B HE3  1 
ATOM   6574 H HZ1  A LYS   B 1 163 ? 37.775 -41.811 -1.310  0.40 34.51 ?  163 LYS   B HZ1  1 
ATOM   6575 H HZ1  B LYS   B 1 163 ? 38.033 -42.046 -1.290  0.60 36.36 ?  163 LYS   B HZ1  1 
ATOM   6576 H HZ2  A LYS   B 1 163 ? 39.208 -41.674 -1.479  0.40 34.51 ?  163 LYS   B HZ2  1 
ATOM   6577 H HZ2  B LYS   B 1 163 ? 39.458 -41.902 -1.507  0.60 36.36 ?  163 LYS   B HZ2  1 
ATOM   6578 H HZ3  A LYS   B 1 163 ? 38.342 -40.529 -1.678  0.40 34.51 ?  163 LYS   B HZ3  1 
ATOM   6579 H HZ3  B LYS   B 1 163 ? 38.590 -40.745 -1.600  0.60 36.36 ?  163 LYS   B HZ3  1 
ATOM   6580 N N    . LEU   B 1 164 ? 38.948 -38.000 -7.992  1.00 14.71 ?  164 LEU   B N    1 
ATOM   6581 C CA   . LEU   B 1 164 ? 38.035 -36.862 -8.046  1.00 14.10 ?  164 LEU   B CA   1 
ATOM   6582 C C    . LEU   B 1 164 ? 37.254 -36.844 -9.354  1.00 14.36 ?  164 LEU   B C    1 
ATOM   6583 O O    . LEU   B 1 164 ? 36.029 -36.656 -9.357  1.00 15.79 ?  164 LEU   B O    1 
ATOM   6584 C CB   . LEU   B 1 164 ? 38.839 -35.569 -7.888  1.00 13.77 ?  164 LEU   B CB   1 
ATOM   6585 C CG   . LEU   B 1 164 ? 39.361 -35.282 -6.485  1.00 14.62 ?  164 LEU   B CG   1 
ATOM   6586 C CD1  . LEU   B 1 164 ? 40.455 -34.225 -6.544  1.00 14.70 ?  164 LEU   B CD1  1 
ATOM   6587 C CD2  . LEU   B 1 164 ? 38.239 -34.833 -5.569  1.00 16.40 ?  164 LEU   B CD2  1 
ATOM   6588 H H    A LEU   B 1 164 ? 39.786 -37.787 -8.019  0.40 17.65 ?  164 LEU   B H    1 
ATOM   6589 H H    B LEU   B 1 164 ? 39.785 -37.784 -7.982  0.60 17.65 ?  164 LEU   B H    1 
ATOM   6590 H HA   . LEU   B 1 164 ? 37.408 -36.925 -7.316  1.00 16.92 ?  164 LEU   B HA   1 
ATOM   6591 H HB2  . LEU   B 1 164 ? 39.612 -35.617 -8.479  1.00 16.52 ?  164 LEU   B HB2  1 
ATOM   6592 H HB3  . LEU   B 1 164 ? 38.279 -34.829 -8.149  1.00 16.52 ?  164 LEU   B HB3  1 
ATOM   6593 H HG   . LEU   B 1 164 ? 39.751 -36.086 -6.116  1.00 17.54 ?  164 LEU   B HG   1 
ATOM   6594 H HD11 . LEU   B 1 164 ? 40.771 -34.039 -5.643  1.00 17.64 ?  164 LEU   B HD11 1 
ATOM   6595 H HD12 . LEU   B 1 164 ? 41.192 -34.553 -7.087  1.00 17.64 ?  164 LEU   B HD12 1 
ATOM   6596 H HD13 . LEU   B 1 164 ? 40.097 -33.411 -6.938  1.00 17.64 ?  164 LEU   B HD13 1 
ATOM   6597 H HD21 . LEU   B 1 164 ? 38.606 -34.601 -4.701  1.00 19.68 ?  164 LEU   B HD21 1 
ATOM   6598 H HD22 . LEU   B 1 164 ? 37.799 -34.059 -5.957  1.00 19.68 ?  164 LEU   B HD22 1 
ATOM   6599 H HD23 . LEU   B 1 164 ? 37.601 -35.559 -5.473  1.00 19.68 ?  164 LEU   B HD23 1 
ATOM   6600 N N    . VAL   B 1 165 ? 37.948 -37.020 -10.479 1.00 15.85 ?  165 VAL   B N    1 
ATOM   6601 C CA   . VAL   B 1 165 ? 37.297 -36.963 -11.784 1.00 17.41 ?  165 VAL   B CA   1 
ATOM   6602 C C    . VAL   B 1 165 ? 36.370 -38.157 -11.962 1.00 19.12 ?  165 VAL   B C    1 
ATOM   6603 O O    . VAL   B 1 165 ? 35.204 -38.016 -12.355 1.00 20.16 ?  165 VAL   B O    1 
ATOM   6604 C CB   . VAL   B 1 165 ? 38.352 -36.889 -12.904 1.00 18.67 ?  165 VAL   B CB   1 
ATOM   6605 C CG1  . VAL   B 1 165 ? 37.701 -36.994 -14.263 1.00 19.73 ?  165 VAL   B CG1  1 
ATOM   6606 C CG2  . VAL   B 1 165 ? 39.155 -35.603 -12.797 1.00 18.23 ?  165 VAL   B CG2  1 
ATOM   6607 H H    . VAL   B 1 165 ? 38.801 -37.167 -10.513 1.00 19.01 ?  165 VAL   B H    1 
ATOM   6608 H HA   . VAL   B 1 165 ? 36.763 -36.158 -11.833 1.00 20.89 ?  165 VAL   B HA   1 
ATOM   6609 H HB   . VAL   B 1 165 ? 38.975 -37.628 -12.807 1.00 22.40 ?  165 VAL   B HB   1 
ATOM   6610 H HG11 . VAL   B 1 165 ? 38.332 -36.707 -14.939 1.00 23.68 ?  165 VAL   B HG11 1 
ATOM   6611 H HG12 . VAL   B 1 165 ? 37.456 -37.922 -14.419 1.00 23.68 ?  165 VAL   B HG12 1 
ATOM   6612 H HG13 . VAL   B 1 165 ? 36.914 -36.435 -14.279 1.00 23.68 ?  165 VAL   B HG13 1 
ATOM   6613 H HG21 . VAL   B 1 165 ? 39.796 -35.565 -13.527 1.00 21.87 ?  165 VAL   B HG21 1 
ATOM   6614 H HG22 . VAL   B 1 165 ? 38.549 -34.846 -12.854 1.00 21.87 ?  165 VAL   B HG22 1 
ATOM   6615 H HG23 . VAL   B 1 165 ? 39.624 -35.586 -11.948 1.00 21.87 ?  165 VAL   B HG23 1 
ATOM   6616 N N    . SER   B 1 166 ? 36.880 -39.356 -11.667 1.00 19.85 ?  166 SER   B N    1 
ATOM   6617 C CA   . SER   B 1 166 ? 36.123 -40.568 -11.948 1.00 21.33 ?  166 SER   B CA   1 
ATOM   6618 C C    . SER   B 1 166 ? 34.862 -40.652 -11.102 1.00 21.75 ?  166 SER   B C    1 
ATOM   6619 O O    . SER   B 1 166 ? 33.887 -41.271 -11.528 1.00 23.47 ?  166 SER   B O    1 
ATOM   6620 C CB   . SER   B 1 166 ? 36.991 -41.820 -11.762 1.00 22.33 ?  166 SER   B CB   1 
ATOM   6621 O OG   . SER   B 1 166 ? 37.349 -42.022 -10.405 1.00 22.18 ?  166 SER   B OG   1 
ATOM   6622 H H    . SER   B 1 166 ? 37.660 -39.490 -11.318 1.00 23.81 ?  166 SER   B H    1 
ATOM   6623 H HA   . SER   B 1 166 ? 35.853 -40.551 -12.877 1.00 25.60 ?  166 SER   B HA   1 
ATOM   6624 H HB2  . SER   B 1 166 ? 36.493 -42.595 -12.069 1.00 26.79 ?  166 SER   B HB2  1 
ATOM   6625 H HB3  . SER   B 1 166 ? 37.800 -41.725 -12.295 1.00 26.79 ?  166 SER   B HB3  1 
ATOM   6626 H HG   . SER   B 1 166 ? 37.801 -41.366 -10.133 1.00 26.62 ?  166 SER   B HG   1 
ATOM   6627 N N    . SER   B 1 167 ? 34.846 -40.041 -9.920  1.00 20.19 ?  167 SER   B N    1 
ATOM   6628 C CA   . SER   B 1 167 ? 33.691 -40.101 -9.033  1.00 19.74 ?  167 SER   B CA   1 
ATOM   6629 C C    . SER   B 1 167 ? 32.772 -38.884 -9.127  1.00 19.10 ?  167 SER   B C    1 
ATOM   6630 O O    . SER   B 1 167 ? 31.692 -38.896 -8.523  1.00 19.12 ?  167 SER   B O    1 
ATOM   6631 C CB   . SER   B 1 167 ? 34.140 -40.281 -7.578  1.00 19.75 ?  167 SER   B CB   1 
ATOM   6632 O OG   . SER   B 1 167 ? 34.798 -39.114 -7.106  1.00 19.00 ?  167 SER   B OG   1 
ATOM   6633 H H    . SER   B 1 167 ? 35.497 -39.583 -9.610  1.00 24.22 ?  167 SER   B H    1 
ATOM   6634 H HA   . SER   B 1 167 ? 33.163 -40.884 -9.273  1.00 23.69 ?  167 SER   B HA   1 
ATOM   6635 H HB2  . SER   B 1 167 ? 33.357 -40.454 -7.029  1.00 23.70 ?  167 SER   B HB2  1 
ATOM   6636 H HB3  . SER   B 1 167 ? 34.745 -41.042 -7.530  1.00 23.70 ?  167 SER   B HB3  1 
ATOM   6637 H HG   . SER   B 1 167 ? 35.479 -38.969 -7.576  1.00 22.79 ?  167 SER   B HG   1 
ATOM   6638 N N    . PHE   B 1 168 ? 33.147 -37.846 -9.875  1.00 18.94 ?  168 PHE   B N    1 
ATOM   6639 C CA   . PHE   B 1 168 ? 32.305 -36.650 -9.939  1.00 17.92 ?  168 PHE   B CA   1 
ATOM   6640 C C    . PHE   B 1 168 ? 30.997 -36.913 -10.681 1.00 15.75 ?  168 PHE   B C    1 
ATOM   6641 O O    . PHE   B 1 168 ? 29.945 -36.328 -10.344 1.00 16.14 ?  168 PHE   B O    1 
ATOM   6642 C CB   . PHE   B 1 168 ? 33.070 -35.519 -10.615 1.00 18.63 ?  168 PHE   B CB   1 
ATOM   6643 C CG   . PHE   B 1 168 ? 32.274 -34.267 -10.738 1.00 18.55 ?  168 PHE   B CG   1 
ATOM   6644 C CD1  . PHE   B 1 168 ? 31.944 -33.539 -9.606  1.00 19.71 ?  168 PHE   B CD1  1 
ATOM   6645 C CD2  . PHE   B 1 168 ? 31.832 -33.826 -11.968 1.00 18.01 ?  168 PHE   B CD2  1 
ATOM   6646 C CE1  . PHE   B 1 168 ? 31.190 -32.390 -9.699  1.00 20.08 ?  168 PHE   B CE1  1 
ATOM   6647 C CE2  . PHE   B 1 168 ? 31.091 -32.659 -12.072 1.00 19.10 ?  168 PHE   B CE2  1 
ATOM   6648 C CZ   . PHE   B 1 168 ? 30.766 -31.943 -10.933 1.00 19.29 ?  168 PHE   B CZ   1 
ATOM   6649 H H    . PHE   B 1 168 ? 33.868 -37.808 -10.337 1.00 22.73 ?  168 PHE   B H    1 
ATOM   6650 H HA   . PHE   B 1 168 ? 32.082 -36.372 -9.039  1.00 21.50 ?  168 PHE   B HA   1 
ATOM   6651 H HB2  . PHE   B 1 168 ? 33.859 -35.319 -10.091 1.00 22.35 ?  168 PHE   B HB2  1 
ATOM   6652 H HB3  . PHE   B 1 168 ? 33.322 -35.797 -11.507 1.00 22.35 ?  168 PHE   B HB3  1 
ATOM   6653 H HD1  . PHE   B 1 168 ? 32.222 -33.839 -8.772  1.00 23.65 ?  168 PHE   B HD1  1 
ATOM   6654 H HD2  . PHE   B 1 168 ? 32.052 -34.297 -12.735 1.00 21.61 ?  168 PHE   B HD2  1 
ATOM   6655 H HE1  . PHE   B 1 168 ? 30.977 -31.910 -8.931  1.00 24.10 ?  168 PHE   B HE1  1 
ATOM   6656 H HE2  . PHE   B 1 168 ? 30.802 -32.359 -12.907 1.00 22.92 ?  168 PHE   B HE2  1 
ATOM   6657 H HZ   . PHE   B 1 168 ? 30.263 -31.162 -11.001 1.00 23.15 ?  168 PHE   B HZ   1 
ATOM   6658 N N    . LEU   B 1 169 ? 31.048 -37.787 -11.685 1.00 16.22 ?  169 LEU   B N    1 
ATOM   6659 C CA   . LEU   B 1 169 ? 29.882 -38.117 -12.496 1.00 18.30 ?  169 LEU   B CA   1 
ATOM   6660 C C    . LEU   B 1 169 ? 29.886 -39.561 -12.985 1.00 21.31 ?  169 LEU   B C    1 
ATOM   6661 O O    . LEU   B 1 169 ? 28.992 -39.984 -13.723 1.00 23.74 ?  169 LEU   B O    1 
ATOM   6662 C CB   . LEU   B 1 169 ? 29.803 -37.189 -13.707 1.00 20.15 ?  169 LEU   B CB   1 
ATOM   6663 C CG   . LEU   B 1 169 ? 28.572 -36.287 -13.773 1.00 23.34 ?  169 LEU   B CG   1 
ATOM   6664 C CD1  . LEU   B 1 169 ? 28.554 -35.543 -15.091 1.00 24.66 ?  169 LEU   B CD1  1 
ATOM   6665 C CD2  . LEU   B 1 169 ? 27.293 -37.086 -13.587 1.00 23.21 ?  169 LEU   B CD2  1 
ATOM   6666 O OXT  . LEU   B 1 169 ? 30.789 -40.326 -12.663 1.00 22.40 -1 169 LEU   B OXT  1 
ATOM   6667 H H    . LEU   B 1 169 ? 31.764 -38.198 -11.935 1.00 19.46 ?  169 LEU   B H    1 
ATOM   6668 H HA   . LEU   B 1 169 ? 29.090 -37.982 -11.960 1.00 21.96 ?  169 LEU   B HA   1 
ATOM   6669 H HB2  . LEU   B 1 169 ? 30.583 -36.615 -13.712 1.00 24.17 ?  169 LEU   B HB2  1 
ATOM   6670 H HB3  . LEU   B 1 169 ? 29.801 -37.732 -14.515 1.00 24.17 ?  169 LEU   B HB3  1 
ATOM   6671 H HG   . LEU   B 1 169 ? 28.623 -35.629 -13.062 1.00 28.01 ?  169 LEU   B HG   1 
ATOM   6672 H HD11 . LEU   B 1 169 ? 27.782 -34.958 -15.112 1.00 29.59 ?  169 LEU   B HD11 1 
ATOM   6673 H HD12 . LEU   B 1 169 ? 29.368 -35.024 -15.170 1.00 29.59 ?  169 LEU   B HD12 1 
ATOM   6674 H HD13 . LEU   B 1 169 ? 28.501 -36.189 -15.813 1.00 29.59 ?  169 LEU   B HD13 1 
ATOM   6675 H HD21 . LEU   B 1 169 ? 26.557 -36.609 -13.997 1.00 27.85 ?  169 LEU   B HD21 1 
ATOM   6676 H HD22 . LEU   B 1 169 ? 27.403 -37.954 -14.009 1.00 27.85 ?  169 LEU   B HD22 1 
ATOM   6677 H HD23 . LEU   B 1 169 ? 27.130 -37.200 -12.639 1.00 27.85 ?  169 LEU   B HD23 1 
HETATM 6678 N N2   B A1BAB C 2 .   ? 15.651 3.409   5.889   0.36 13.02 ?  201 A1BAB A N2   1 
HETATM 6679 C C3   B A1BAB C 2 .   ? 14.866 -0.573  0.097   0.36 14.50 ?  201 A1BAB A C3   1 
HETATM 6680 C C6   B A1BAB C 2 .   ? 17.170 0.305   -0.552  0.36 14.11 ?  201 A1BAB A C6   1 
HETATM 6681 C C9   B A1BAB C 2 .   ? 16.111 2.719   -1.062  0.36 11.46 ?  201 A1BAB A C9   1 
HETATM 6682 C C12  B A1BAB C 2 .   ? 14.757 1.024   3.364   0.36 13.15 ?  201 A1BAB A C12  1 
HETATM 6683 C C14  B A1BAB C 2 .   ? 15.355 3.621   3.663   0.36 13.64 ?  201 A1BAB A C14  1 
HETATM 6684 C C17  B A1BAB C 2 .   ? 14.852 -0.063  5.423   0.36 12.11 ?  201 A1BAB A C17  1 
HETATM 6685 C C1   B A1BAB C 2 .   ? 12.497 0.199   0.796   0.36 14.94 ?  201 A1BAB A C1   1 
HETATM 6686 C C10  B A1BAB C 2 .   ? 17.411 2.551   -1.244  0.36 13.18 ?  201 A1BAB A C10  1 
HETATM 6687 C C11  B A1BAB C 2 .   ? 18.027 1.330   -0.996  0.36 14.04 ?  201 A1BAB A C11  1 
HETATM 6688 C C13  B A1BAB C 2 .   ? 15.119 2.241   4.009   0.36 12.82 ?  201 A1BAB A C13  1 
HETATM 6689 C C15  B A1BAB C 2 .   ? 15.680 4.314   4.821   0.36 13.69 ?  201 A1BAB A C15  1 
HETATM 6690 C C16  B A1BAB C 2 .   ? 15.315 2.156   5.399   0.36 12.22 ?  201 A1BAB A C16  1 
HETATM 6691 C C2   B A1BAB C 2 .   ? 13.959 -0.185  1.315   0.36 14.71 ?  201 A1BAB A C2   1 
HETATM 6692 C C4   B A1BAB C 2 .   ? 15.978 -1.555  0.503   0.36 14.97 ?  201 A1BAB A C4   1 
HETATM 6693 C C5   B A1BAB C 2 .   ? 17.340 -1.121  -0.164  0.36 13.93 ?  201 A1BAB A C5   1 
HETATM 6694 C C7   B A1BAB C 2 .   ? 15.758 0.519   -0.378  0.36 14.10 ?  201 A1BAB A C7   1 
HETATM 6695 C C8   B A1BAB C 2 .   ? 15.277 1.768   -0.657  0.36 13.77 ?  201 A1BAB A C8   1 
HETATM 6696 N N1   B A1BAB C 2 .   ? 14.528 0.975   2.032   0.36 14.33 ?  201 A1BAB A N1   1 
HETATM 6697 N N3   B A1BAB C 2 .   ? 15.185 1.014   6.131   0.36 11.47 ?  201 A1BAB A N3   1 
HETATM 6698 N N4   B A1BAB C 2 .   ? 14.626 -0.123  4.085   0.36 12.79 ?  201 A1BAB A N4   1 
HETATM 6699 O O1   B A1BAB C 2 .   ? 11.647 0.328   1.898   0.36 15.97 ?  201 A1BAB A O1   1 
HETATM 6700 H H17  B A1BAB C 2 .   ? 15.849 3.662   6.872   0.36 15.62 ?  201 A1BAB A H17  1 
HETATM 6701 H H2   B A1BAB C 2 .   ? 14.152 -1.008  -0.685  0.36 17.39 ?  201 A1BAB A H2   1 
HETATM 6702 H H11  B A1BAB C 2 .   ? 15.705 3.731   -1.295  0.36 13.75 ?  201 A1BAB A H11  1 
HETATM 6703 H H15  B A1BAB C 2 .   ? 15.306 4.057   2.682   0.36 16.37 ?  201 A1BAB A H15  1 
HETATM 6704 H H18  B A1BAB C 2 .   ? 14.730 -1.025  6.006   0.36 14.53 ?  201 A1BAB A H18  1 
HETATM 6705 H H5   B A1BAB C 2 .   ? 12.116 -0.560  0.085   0.36 17.92 ?  201 A1BAB A H5   1 
HETATM 6706 H H4   B A1BAB C 2 .   ? 12.492 1.167   0.243   0.36 17.92 ?  201 A1BAB A H4   1 
HETATM 6707 H H12  B A1BAB C 2 .   ? 17.777 3.529   -1.586  0.36 15.82 ?  201 A1BAB A H12  1 
HETATM 6708 H H13  B A1BAB C 2 .   ? 19.059 1.666   -1.265  0.36 16.85 ?  201 A1BAB A H13  1 
HETATM 6709 H H16  B A1BAB C 2 .   ? 15.929 5.367   5.006   0.36 16.43 ?  201 A1BAB A H16  1 
HETATM 6710 H H1   B A1BAB C 2 .   ? 13.935 -1.105  1.948   0.36 17.66 ?  201 A1BAB A H1   1 
HETATM 6711 H H7   B A1BAB C 2 .   ? 16.107 -1.560  1.588   0.36 17.96 ?  201 A1BAB A H7   1 
HETATM 6712 H H6   B A1BAB C 2 .   ? 15.729 -2.600  0.210   0.36 17.96 ?  201 A1BAB A H6   1 
HETATM 6713 H H8   B A1BAB C 2 .   ? 18.133 -1.301  0.589   0.36 16.72 ?  201 A1BAB A H8   1 
HETATM 6714 H H9   B A1BAB C 2 .   ? 17.546 -1.840  -0.991  0.36 16.72 ?  201 A1BAB A H9   1 
HETATM 6715 H H10  B A1BAB C 2 .   ? 14.326 2.265   -0.640  0.36 16.52 ?  201 A1BAB A H10  1 
HETATM 6716 H H14  B A1BAB C 2 .   ? 14.743 1.789   1.509   0.36 17.19 ?  201 A1BAB A H14  1 
HETATM 6717 H H3   B A1BAB C 2 .   ? 10.825 0.782   1.650   0.36 19.16 ?  201 A1BAB A H3   1 
HETATM 6718 O O1   C A1BAC D 3 .   ? 16.638 -1.232  0.152   0.24 18.10 ?  202 A1BAC A O1   1 
HETATM 6719 C C1   C A1BAC D 3 .   ? 15.384 -0.682  -0.117  0.24 16.79 ?  202 A1BAC A C1   1 
HETATM 6720 C C2   C A1BAC D 3 .   ? 14.633 -0.538  1.276   0.24 14.74 ?  202 A1BAC A C2   1 
HETATM 6721 C C3   C A1BAC D 3 .   ? 13.047 -0.817  1.095   0.24 14.70 ?  202 A1BAC A C3   1 
HETATM 6722 C C4   C A1BAC D 3 .   ? 12.702 -2.153  0.337   0.24 14.75 ?  202 A1BAC A C4   1 
HETATM 6723 C C5   C A1BAC D 3 .   ? 11.704 -1.885  -0.887  0.24 14.80 ?  202 A1BAC A C5   1 
HETATM 6724 C C6   C A1BAC D 3 .   ? 11.374 -0.384  -0.915  0.24 14.77 ?  202 A1BAC A C6   1 
HETATM 6725 C C7   C A1BAC D 3 .   ? 12.163 0.098   0.201   0.24 14.87 ?  202 A1BAC A C7   1 
HETATM 6726 C C8   C A1BAC D 3 .   ? 12.082 1.418   0.455   0.24 14.59 ?  202 A1BAC A C8   1 
HETATM 6727 C C10  C A1BAC D 3 .   ? 10.581 1.841   -1.325  0.24 14.78 ?  202 A1BAC A C10  1 
HETATM 6728 C C11  C A1BAC D 3 .   ? 10.575 0.507   -1.688  0.24 14.78 ?  202 A1BAC A C11  1 
HETATM 6729 C C12  C A1BAC D 3 .   ? 15.005 0.932   3.359   0.24 13.19 ?  202 A1BAC A C12  1 
HETATM 6730 C C13  C A1BAC D 3 .   ? 15.257 2.195   4.030   0.24 12.89 ?  202 A1BAC A C13  1 
HETATM 6731 C C14  C A1BAC D 3 .   ? 15.517 3.578   3.648   0.24 13.25 ?  202 A1BAC A C14  1 
HETATM 6732 C C15  C A1BAC D 3 .   ? 15.673 4.330   4.812   0.24 13.35 ?  202 A1BAC A C15  1 
HETATM 6733 C C16  C A1BAC D 3 .   ? 15.273 2.177   5.467   0.24 12.86 ?  202 A1BAC A C16  1 
HETATM 6734 C C17  C A1BAC D 3 .   ? 14.852 -0.051  5.544   0.24 12.93 ?  202 A1BAC A C17  1 
HETATM 6735 C C9   C A1BAC D 3 .   ? 11.314 2.286   -0.286  0.24 14.42 ?  202 A1BAC A C9   1 
HETATM 6736 N N1   C A1BAC D 3 .   ? 14.958 0.774   1.953   0.24 13.90 ?  202 A1BAC A N1   1 
HETATM 6737 N N2   C A1BAC D 3 .   ? 15.523 3.472   5.929   0.24 13.02 ?  202 A1BAC A N2   1 
HETATM 6738 N N3   C A1BAC D 3 .   ? 15.070 1.061   6.272   0.24 13.02 ?  202 A1BAC A N3   1 
HETATM 6739 N N4   C A1BAC D 3 .   ? 14.807 -0.175  4.167   0.24 12.77 ?  202 A1BAC A N4   1 
HETATM 6740 H H3   C A1BAC D 3 .   ? 17.031 -1.649  -0.626  0.24 21.72 ?  202 A1BAC A H3   1 
HETATM 6741 H H5   C A1BAC D 3 .   ? 14.794 -1.308  -0.866  0.24 20.15 ?  202 A1BAC A H5   1 
HETATM 6742 H H4   C A1BAC D 3 .   ? 15.488 0.308   -0.555  0.24 20.15 ?  202 A1BAC A H4   1 
HETATM 6743 H H1   C A1BAC D 3 .   ? 14.967 -1.370  1.962   0.24 17.68 ?  202 A1BAC A H1   1 
HETATM 6744 H H2   C A1BAC D 3 .   ? 12.646 -0.897  2.181   0.24 17.64 ?  202 A1BAC A H2   1 
HETATM 6745 H H7   C A1BAC D 3 .   ? 13.609 -2.666  -0.060  0.24 17.70 ?  202 A1BAC A H7   1 
HETATM 6746 H H6   C A1BAC D 3 .   ? 12.188 -2.848  1.015   0.24 17.70 ?  202 A1BAC A H6   1 
HETATM 6747 H H9   C A1BAC D 3 .   ? 12.257 -2.170  -1.816  0.24 17.76 ?  202 A1BAC A H9   1 
HETATM 6748 H H8   C A1BAC D 3 .   ? 10.841 -2.589  -0.753  0.24 17.76 ?  202 A1BAC A H8   1 
HETATM 6749 H H10  C A1BAC D 3 .   ? 12.419 2.179   1.089   0.24 17.51 ?  202 A1BAC A H10  1 
HETATM 6750 H H12  C A1BAC D 3 .   ? 10.172 2.769   -1.604  0.24 17.73 ?  202 A1BAC A H12  1 
HETATM 6751 H H13  C A1BAC D 3 .   ? 9.864  0.703   -2.534  0.24 17.73 ?  202 A1BAC A H13  1 
HETATM 6752 H H15  C A1BAC D 3 .   ? 15.572 3.984   2.626   0.24 15.90 ?  202 A1BAC A H15  1 
HETATM 6753 H H16  C A1BAC D 3 .   ? 15.883 5.413   4.995   0.24 16.01 ?  202 A1BAC A H16  1 
HETATM 6754 H H18  C A1BAC D 3 .   ? 14.667 -1.015  6.115   0.24 15.51 ?  202 A1BAC A H18  1 
HETATM 6755 H H11  C A1BAC D 3 .   ? 11.220 3.302   -0.137  0.24 17.31 ?  202 A1BAC A H11  1 
HETATM 6756 H H14  C A1BAC D 3 .   ? 15.140 1.592   1.326   0.24 16.68 ?  202 A1BAC A H14  1 
HETATM 6757 H H17  C A1BAC D 3 .   ? 15.600 3.782   6.893   0.24 15.63 ?  202 A1BAC A H17  1 
HETATM 6758 O O    . HOH   E 4 .   ? 7.592  -6.333  -6.673  1.00 49.14 ?  301 HOH   A O    1 
HETATM 6759 O O    A HOH   E 4 .   ? 14.742 -4.539  20.437  0.40 31.05 ?  302 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? -0.830 -8.338  2.288   1.00 49.39 ?  303 HOH   A O    1 
HETATM 6761 O O    C HOH   E 4 .   ? 18.526 -1.729  -1.266  0.24 18.73 ?  304 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 34.361 -1.847  12.440  1.00 38.37 ?  305 HOH   A O    1 
HETATM 6763 O O    B HOH   E 4 .   ? 8.391  4.032   0.974   0.60 27.21 ?  306 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 28.865 0.491   -9.685  1.00 20.60 ?  307 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 18.549 -2.413  -16.437 1.00 44.57 ?  308 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 14.972 -12.118 18.579  1.00 43.07 ?  309 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 0.889  -4.165  -0.049  1.00 32.38 ?  310 HOH   A O    1 
HETATM 6768 O O    A HOH   E 4 .   ? 4.625  3.974   0.642   0.40 17.35 ?  311 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 14.159 -4.555  -11.933 1.00 42.22 ?  312 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 11.835 0.541   14.680  1.00 37.76 ?  313 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 17.004 -17.931 14.980  1.00 30.93 ?  314 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 14.916 3.896   17.669  1.00 42.69 ?  315 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 28.176 -6.230  19.611  1.00 41.26 ?  316 HOH   A O    1 
HETATM 6774 O O    B HOH   E 4 .   ? 4.864  3.443   0.392   0.60 19.25 ?  317 HOH   A O    1 
HETATM 6775 O O    A HOH   E 4 .   ? -0.546 -3.031  3.136   0.40 26.51 ?  318 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 42.442 10.513  5.157   1.00 21.08 ?  319 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 14.652 -13.880 16.692  1.00 27.62 ?  320 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 30.981 6.143   -12.334 1.00 29.51 ?  321 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 30.143 -13.315 -8.507  1.00 21.26 ?  322 HOH   A O    1 
HETATM 6780 O O    B HOH   E 4 .   ? 15.031 7.093   7.133   0.60 23.91 ?  323 HOH   A O    1 
HETATM 6781 O O    A HOH   E 4 .   ? 6.889  -8.101  11.877  0.40 16.23 ?  324 HOH   A O    1 
HETATM 6782 O O    A HOH   E 4 .   ? 17.424 -1.664  0.454   0.40 28.91 ?  325 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 16.935 -19.175 4.930   1.00 16.06 ?  326 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 26.400 -19.299 -1.773  1.00 13.93 ?  327 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 9.078  -10.039 19.239  1.00 46.79 ?  328 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 27.255 13.789  2.876   1.00 28.43 ?  329 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 19.854 -12.478 -8.901  1.00 25.75 ?  330 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 13.193 -1.499  -6.743  1.00 20.28 ?  331 HOH   A O    1 
HETATM 6789 O O    A HOH   E 4 .   ? 15.480 11.970  8.060   0.40 22.00 ?  332 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 15.167 -8.080  -9.915  1.00 28.34 ?  333 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 7.898  -12.496 -0.962  1.00 21.72 ?  334 HOH   A O    1 
HETATM 6792 O O    B HOH   E 4 .   ? 21.199 -2.368  -2.575  0.60 14.01 ?  335 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 36.186 -5.062  -0.548  1.00 32.27 ?  336 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 33.906 -1.112  -8.985  1.00 27.40 ?  337 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 30.960 -18.082 7.823   1.00 19.38 ?  338 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 22.185 -19.235 11.374  1.00 35.39 ?  339 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 18.878 -21.915 7.004   1.00 34.97 ?  340 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 39.625 -1.051  -5.230  1.00 19.46 ?  341 HOH   A O    1 
HETATM 6799 O O    A HOH   E 4 .   ? 14.566 -3.602  3.114   0.40 19.12 ?  342 HOH   A O    1 
HETATM 6800 O O    A HOH   E 4 .   ? 8.112  -21.341 4.025   0.40 33.78 ?  343 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 14.445 -0.517  -12.162 1.00 26.73 ?  344 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 38.237 10.124  7.108   1.00 32.51 ?  345 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 28.198 -0.098  -13.398 1.00 36.42 ?  346 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 44.280 7.115   6.347   1.00 26.36 ?  347 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 38.511 4.965   6.911   1.00 15.24 ?  348 HOH   A O    1 
HETATM 6806 O O    B HOH   E 4 .   ? 15.138 -2.672  3.320   0.60 22.02 ?  349 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 20.546 -19.741 -5.036  1.00 27.74 ?  350 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 38.066 -1.382  -1.966  1.00 17.56 ?  351 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 9.869  -21.240 5.637   1.00 21.16 ?  352 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 37.292 11.930  4.917   1.00 31.57 ?  353 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 24.269 3.610   -1.770  1.00 14.01 ?  354 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 31.699 8.225   14.797  1.00 24.91 ?  355 HOH   A O    1 
HETATM 6813 O O    A HOH   E 4 .   ? 14.213 0.628   6.815   0.40 25.10 ?  356 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 14.296 -21.184 -4.213  1.00 30.19 ?  357 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 37.527 2.774   10.156  1.00 28.87 ?  358 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 37.134 -2.805  9.660   1.00 40.65 ?  359 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 42.477 4.237   5.289   1.00 31.36 ?  360 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 31.677 -9.341  -6.686  1.00 21.95 ?  361 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 27.316 -6.059  -13.950 1.00 38.61 ?  362 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 14.002 -22.949 7.432   1.00 18.85 ?  363 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 18.631 -19.336 13.594  1.00 38.04 ?  364 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 26.778 11.435  1.665   1.00 16.22 ?  365 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 13.538 -15.301 -7.513  1.00 26.67 ?  366 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 13.842 -4.703  17.269  1.00 28.71 ?  367 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 17.097 -17.812 -5.022  1.00 28.21 ?  368 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 18.533 9.418   9.033   1.00 22.75 ?  369 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 23.953 -2.096  -2.107  1.00 10.67 ?  370 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 6.610  -3.139  12.709  1.00 27.51 ?  371 HOH   A O    1 
HETATM 6829 O O    B HOH   E 4 .   ? 11.927 6.634   10.295  0.60 30.85 ?  372 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 43.873 8.393   -3.119  1.00 27.43 ?  373 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 22.684 12.516  1.646   1.00 14.97 ?  374 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 35.713 -12.617 6.842   1.00 15.57 ?  375 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 23.445 11.407  4.095   1.00 12.27 ?  376 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 22.223 5.364   18.935  1.00 40.86 ?  377 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 19.970 4.529   -7.524  1.00 20.85 ?  378 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 24.210 -7.726  14.403  1.00 16.77 ?  379 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 30.996 -13.912 -2.451  1.00 13.07 ?  380 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 30.763 3.108   8.224   1.00 11.75 ?  381 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 21.823 -21.856 8.529   1.00 27.68 ?  382 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 21.247 10.265  15.013  1.00 33.89 ?  383 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 16.468 -21.999 1.013   1.00 29.47 ?  384 HOH   A O    1 
HETATM 6842 O O    A HOH   E 4 .   ? 3.536  -9.402  9.764   0.40 26.79 ?  385 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 43.302 7.800   2.670   1.00 23.69 ?  386 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 27.797 0.824   -7.158  1.00 13.77 ?  387 HOH   A O    1 
HETATM 6845 O O    A HOH   E 4 .   ? 21.171 -2.350  -2.044  0.40 10.21 ?  388 HOH   A O    1 
HETATM 6846 O O    B HOH   E 4 .   ? 2.973  -3.025  8.269   0.60 27.30 ?  389 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 33.594 -7.137  4.262   1.00 16.11 ?  390 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 14.438 -24.599 11.572  1.00 39.83 ?  391 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 27.444 -10.564 14.061  1.00 17.07 ?  392 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 31.660 -7.293  -9.884  1.00 21.56 ?  393 HOH   A O    1 
HETATM 6851 O O    B HOH   E 4 .   ? 24.056 1.897   -6.622  0.60 28.48 ?  394 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 10.343 -22.136 -1.193  1.00 46.45 ?  395 HOH   A O    1 
HETATM 6853 O O    B HOH   E 4 .   ? 3.661  0.319   9.479   0.60 38.82 ?  396 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 32.712 -9.232  5.946   1.00 19.52 ?  397 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 16.141 16.539  8.589   1.00 39.59 ?  398 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 25.524 -0.755  -7.290  1.00 16.05 ?  399 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 24.616 -17.487 12.700  1.00 24.49 ?  400 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 8.955  -11.848 17.229  1.00 42.37 ?  401 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 37.479 -1.987  5.731   1.00 24.76 ?  402 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 15.119 -21.415 14.227  1.00 18.41 ?  403 HOH   A O    1 
HETATM 6861 O O    A HOH   E 4 .   ? 18.885 -0.621  -1.617  0.40 14.13 ?  404 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 27.416 2.307   18.688  1.00 27.98 ?  405 HOH   A O    1 
HETATM 6863 O O    A HOH   E 4 .   ? 10.982 1.611   12.770  0.40 17.72 ?  406 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 22.652 -11.901 21.800  1.00 50.89 ?  407 HOH   A O    1 
HETATM 6865 O O    B HOH   E 4 .   ? 21.004 2.794   0.090   0.60 12.27 ?  408 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 30.695 1.875   16.644  1.00 20.14 ?  409 HOH   A O    1 
HETATM 6867 O O    A HOH   E 4 .   ? 10.998 -0.326  1.953   0.40 23.88 ?  410 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 30.018 -10.048 12.983  1.00 21.36 ?  411 HOH   A O    1 
HETATM 6869 O O    A HOH   E 4 .   ? 15.735 -0.892  5.284   0.40 31.45 ?  412 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 26.840 4.170   -0.678  1.00 12.22 ?  413 HOH   A O    1 
HETATM 6871 O O    A HOH   E 4 .   ? 24.503 2.083   -6.987  0.40 14.05 ?  414 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 21.697 -13.740 -8.192  1.00 42.20 ?  415 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 44.807 -0.664  2.959   1.00 37.81 ?  416 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 20.537 -19.996 2.772   1.00 18.59 ?  417 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 32.568 -4.307  -9.890  1.00 28.52 ?  418 HOH   A O    1 
HETATM 6876 O O    A HOH   E 4 .   ? 21.278 3.203   -0.345  0.40 9.74  ?  419 HOH   A O    1 
HETATM 6877 O O    . HOH   E 4 .   ? 30.266 -12.853 13.514  1.00 20.32 ?  420 HOH   A O    1 
HETATM 6878 O O    B HOH   E 4 .   ? 10.839 2.237   11.990  0.60 23.43 ?  421 HOH   A O    1 
HETATM 6879 O O    A HOH   E 4 .   ? 5.240  2.695   5.298   0.40 23.67 ?  422 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 23.846 -20.244 -1.325  1.00 17.08 ?  423 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 16.190 -14.108 20.217  1.00 56.45 ?  424 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 34.897 -5.223  -3.088  1.00 17.26 ?  425 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 10.319 -13.690 -1.729  1.00 17.54 ?  426 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? -1.348 -4.204  7.405   1.00 66.73 ?  427 HOH   A O    1 
HETATM 6885 O O    A HOH   E 4 .   ? 6.407  -5.544  11.206  0.40 15.71 ?  428 HOH   A O    1 
HETATM 6886 O O    . HOH   E 4 .   ? 11.690 -10.581 16.956  1.00 29.44 ?  429 HOH   A O    1 
HETATM 6887 O O    . HOH   E 4 .   ? 15.894 2.226   24.706  1.00 47.34 ?  430 HOH   A O    1 
HETATM 6888 O O    . HOH   E 4 .   ? 36.688 -4.949  5.347   1.00 23.94 ?  431 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 19.039 -10.810 24.070  1.00 72.20 ?  432 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 41.538 1.549   4.966   1.00 35.79 ?  433 HOH   A O    1 
HETATM 6891 O O    . HOH   E 4 .   ? 15.946 6.973   2.931   1.00 22.92 ?  434 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 22.663 8.114   18.360  1.00 47.75 ?  435 HOH   A O    1 
HETATM 6893 O O    B HOH   E 4 .   ? 20.632 4.430   -2.286  0.60 22.37 ?  436 HOH   A O    1 
HETATM 6894 O O    . HOH   E 4 .   ? 32.457 -10.625 3.209   1.00 30.99 ?  437 HOH   A O    1 
HETATM 6895 O O    . HOH   E 4 .   ? 40.851 -8.201  -6.810  1.00 37.05 ?  438 HOH   A O    1 
HETATM 6896 O O    . HOH   E 4 .   ? 23.743 -15.751 -9.213  1.00 33.52 ?  439 HOH   A O    1 
HETATM 6897 O O    A HOH   E 4 .   ? 18.791 2.082   -0.743  0.64 17.28 ?  440 HOH   A O    1 
HETATM 6898 O O    . HOH   E 4 .   ? 18.513 4.970   -15.127 1.00 47.52 ?  441 HOH   A O    1 
HETATM 6899 O O    . HOH   E 4 .   ? 18.318 -15.827 16.335  1.00 42.27 ?  442 HOH   A O    1 
HETATM 6900 O O    B HOH   E 4 .   ? 5.500  3.181   4.358   0.60 29.71 ?  443 HOH   A O    1 
HETATM 6901 O O    A HOH   E 4 .   ? 28.456 -10.609 -13.918 0.40 27.51 ?  444 HOH   A O    1 
HETATM 6902 O O    A HOH   E 4 .   ? 23.128 7.557   -3.236  0.40 18.89 ?  445 HOH   A O    1 
HETATM 6903 O O    A HOH   E 4 .   ? 24.015 4.003   -4.916  0.40 15.05 ?  446 HOH   A O    1 
HETATM 6904 O O    . HOH   E 4 .   ? 27.093 -3.078  19.346  1.00 36.67 ?  447 HOH   A O    1 
HETATM 6905 O O    . HOH   E 4 .   ? 23.282 -20.893 1.329   1.00 18.90 ?  448 HOH   A O    1 
HETATM 6906 O O    . HOH   E 4 .   ? 23.510 -7.993  17.059  1.00 22.04 ?  449 HOH   A O    1 
HETATM 6907 O O    . HOH   E 4 .   ? 20.493 -17.730 24.777  1.00 53.67 ?  450 HOH   A O    1 
HETATM 6908 O O    . HOH   E 4 .   ? 31.239 -12.780 0.027   1.00 19.10 ?  451 HOH   A O    1 
HETATM 6909 O O    . HOH   E 4 .   ? 21.430 -14.668 17.915  1.00 57.55 ?  452 HOH   A O    1 
HETATM 6910 O O    B HOH   E 4 .   ? 23.051 6.384   -1.988  0.60 21.68 ?  453 HOH   A O    1 
HETATM 6911 O O    . HOH   E 4 .   ? 9.397  -16.288 -2.044  1.00 40.05 ?  454 HOH   A O    1 
HETATM 6912 O O    A HOH   E 4 .   ? 16.186 2.997   -1.430  0.64 23.60 ?  455 HOH   A O    1 
HETATM 6913 O O    . HOH   E 4 .   ? 34.344 -8.083  -0.548  1.00 30.63 ?  456 HOH   A O    1 
HETATM 6914 O O    B HOH   E 4 .   ? 23.666 3.638   -4.443  0.60 23.53 ?  457 HOH   A O    1 
HETATM 6915 O O    A HOH   E 4 .   ? 11.642 -10.735 -10.041 0.40 30.80 ?  458 HOH   A O    1 
HETATM 6916 O O    . HOH   E 4 .   ? 30.565 14.737  2.744   1.00 18.77 ?  459 HOH   A O    1 
HETATM 6917 O O    . HOH   E 4 .   ? 21.312 -9.058  21.366  1.00 53.98 ?  460 HOH   A O    1 
HETATM 6918 O O    . HOH   E 4 .   ? 37.594 -8.717  -3.273  1.00 23.54 ?  461 HOH   A O    1 
HETATM 6919 O O    A HOH   E 4 .   ? 13.960 -0.285  3.477   0.40 23.79 ?  462 HOH   A O    1 
HETATM 6920 O O    B HOH   E 4 .   ? 3.882  2.322   2.370   0.60 17.89 ?  463 HOH   A O    1 
HETATM 6921 O O    . HOH   E 4 .   ? 29.752 -16.010 10.693  1.00 33.71 ?  464 HOH   A O    1 
HETATM 6922 O O    . HOH   E 4 .   ? 29.633 -1.905  -12.753 1.00 43.60 ?  465 HOH   A O    1 
HETATM 6923 O O    . HOH   E 4 .   ? 27.721 7.043   -6.591  1.00 37.55 ?  466 HOH   A O    1 
HETATM 6924 O O    . HOH   E 4 .   ? 25.326 8.236   -4.819  1.00 36.35 ?  467 HOH   A O    1 
HETATM 6925 O O    . HOH   E 4 .   ? 32.428 -15.874 10.886  1.00 33.55 ?  468 HOH   A O    1 
HETATM 6926 O O    . HOH   E 4 .   ? 19.811 -17.341 -5.030  1.00 25.00 ?  469 HOH   A O    1 
HETATM 6927 O O    . HOH   E 4 .   ? 24.869 5.663   20.738  1.00 48.80 ?  470 HOH   A O    1 
HETATM 6928 O O    B HOH   E 4 .   ? 7.935  1.921   -3.310  0.60 26.17 ?  471 HOH   A O    1 
HETATM 6929 O O    . HOH   E 4 .   ? 39.518 -7.045  -3.576  1.00 45.38 ?  472 HOH   A O    1 
HETATM 6930 O O    . HOH   E 4 .   ? 23.108 -22.352 -3.209  1.00 34.85 ?  473 HOH   A O    1 
HETATM 6931 O O    . HOH   E 4 .   ? 24.546 14.693  7.831   1.00 35.17 ?  474 HOH   A O    1 
HETATM 6932 O O    . HOH   E 4 .   ? 15.701 -21.451 3.698   1.00 26.39 ?  475 HOH   A O    1 
HETATM 6933 O O    . HOH   E 4 .   ? 26.834 11.711  -1.390  1.00 33.92 ?  476 HOH   A O    1 
HETATM 6934 O O    . HOH   E 4 .   ? 18.773 10.878  11.322  1.00 31.99 ?  477 HOH   A O    1 
HETATM 6935 O O    . HOH   E 4 .   ? 11.906 -13.363 16.403  1.00 51.33 ?  478 HOH   A O    1 
HETATM 6936 O O    . HOH   E 4 .   ? 27.460 -11.252 16.590  1.00 35.76 ?  479 HOH   A O    1 
HETATM 6937 O O    . HOH   E 4 .   ? 11.049 -15.077 -6.130  1.00 34.92 ?  480 HOH   A O    1 
HETATM 6938 O O    . HOH   E 4 .   ? 23.440 13.736  5.516   1.00 18.42 ?  481 HOH   A O    1 
HETATM 6939 O O    . HOH   E 4 .   ? 25.756 10.781  -3.757  1.00 32.64 ?  482 HOH   A O    1 
HETATM 6940 O O    . HOH   E 4 .   ? 12.280 1.714   17.375  1.00 37.87 ?  483 HOH   A O    1 
HETATM 6941 O O    . HOH   E 4 .   ? 17.895 -16.272 -8.797  1.00 42.85 ?  484 HOH   A O    1 
HETATM 6942 O O    A HOH   E 4 .   ? 21.888 5.311   -5.833  0.40 22.44 ?  485 HOH   A O    1 
HETATM 6943 O O    . HOH   E 4 .   ? 23.042 11.809  -4.058  1.00 19.49 ?  486 HOH   A O    1 
HETATM 6944 O O    . HOH   E 4 .   ? 13.945 -10.373 -10.926 1.00 34.57 ?  487 HOH   A O    1 
HETATM 6945 O O    . HOH   E 4 .   ? 28.912 8.964   17.502  1.00 38.31 ?  488 HOH   A O    1 
HETATM 6946 O O    . HOH   E 4 .   ? 35.163 7.478   12.224  1.00 44.56 ?  489 HOH   A O    1 
HETATM 6947 O O    . HOH   E 4 .   ? 15.715 -17.201 -7.004  1.00 32.61 ?  490 HOH   A O    1 
HETATM 6948 O O    . HOH   E 4 .   ? 16.747 -20.437 16.138  1.00 31.90 ?  491 HOH   A O    1 
HETATM 6949 O O    . HOH   E 4 .   ? 40.925 -3.954  -0.426  1.00 41.67 ?  492 HOH   A O    1 
HETATM 6950 O O    . HOH   E 4 .   ? 15.935 -6.803  -11.946 1.00 43.69 ?  493 HOH   A O    1 
HETATM 6951 O O    . HOH   E 4 .   ? 17.359 -18.718 19.857  1.00 54.23 ?  494 HOH   A O    1 
HETATM 6952 O O    . HOH   E 4 .   ? 8.256  -3.067  -6.019  1.00 53.78 ?  495 HOH   A O    1 
HETATM 6953 O O    . HOH   E 4 .   ? 30.831 0.762   19.154  1.00 38.66 ?  496 HOH   A O    1 
HETATM 6954 O O    . HOH   E 4 .   ? 28.627 -7.902  -15.245 1.00 50.12 ?  497 HOH   A O    1 
HETATM 6955 O O    . HOH   E 4 .   ? 31.386 -0.562  -10.587 1.00 29.61 ?  498 HOH   A O    1 
HETATM 6956 O O    B HOH   E 4 .   ? 21.184 4.764   -4.957  0.60 26.72 ?  499 HOH   A O    1 
HETATM 6957 O O    . HOH   E 4 .   ? 28.433 -4.628  -12.335 1.00 36.14 ?  500 HOH   A O    1 
HETATM 6958 O O    . HOH   E 4 .   ? 41.686 9.342   -4.025  1.00 30.96 ?  501 HOH   A O    1 
HETATM 6959 O O    . HOH   E 4 .   ? 44.438 10.406  -1.666  1.00 29.09 ?  502 HOH   A O    1 
HETATM 6960 O O    . HOH   E 4 .   ? 39.128 2.408   7.430   1.00 33.50 ?  503 HOH   A O    1 
HETATM 6961 O O    . HOH   E 4 .   ? 13.886 -25.109 8.907   1.00 30.24 ?  504 HOH   A O    1 
HETATM 6962 O O    . HOH   E 4 .   ? 23.248 -12.829 19.309  1.00 52.07 ?  505 HOH   A O    1 
HETATM 6963 O O    . HOH   E 4 .   ? 18.338 -23.140 1.934   1.00 43.74 ?  506 HOH   A O    1 
HETATM 6964 O O    . HOH   E 4 .   ? 40.471 -0.232  -7.807  1.00 33.29 ?  507 HOH   A O    1 
HETATM 6965 O O    . HOH   E 4 .   ? 16.178 -23.378 5.793   1.00 29.66 ?  508 HOH   A O    1 
HETATM 6966 O O    B HOH   E 4 .   ? 5.275  6.109   1.192   0.60 20.13 ?  509 HOH   A O    1 
HETATM 6967 O O    . HOH   E 4 .   ? 30.717 5.759   -14.722 1.00 33.46 ?  510 HOH   A O    1 
HETATM 6968 O O    . HOH   E 4 .   ? 20.024 -22.301 4.234   1.00 29.34 ?  511 HOH   A O    1 
HETATM 6969 O O    . HOH   E 4 .   ? 37.320 -6.646  7.474   1.00 23.89 ?  512 HOH   A O    1 
HETATM 6970 O O    . HOH   E 4 .   ? 23.103 -23.731 1.719   1.00 30.60 ?  513 HOH   A O    1 
HETATM 6971 O O    B HOH   E 4 .   ? 14.386 7.736   4.661   0.60 25.96 ?  514 HOH   A O    1 
HETATM 6972 O O    . HOH   E 4 .   ? 30.670 -5.796  -11.922 1.00 44.77 ?  515 HOH   A O    1 
HETATM 6973 O O    . HOH   E 4 .   ? 38.033 13.817  6.706   1.00 53.92 ?  516 HOH   A O    1 
HETATM 6974 O O    . HOH   E 4 .   ? 39.485 -0.008  6.508   1.00 30.91 ?  517 HOH   A O    1 
HETATM 6975 O O    . HOH   E 4 .   ? 28.953 14.482  0.825   1.00 51.95 ?  518 HOH   A O    1 
HETATM 6976 O O    . HOH   E 4 .   ? 20.449 -16.027 -7.395  1.00 31.13 ?  519 HOH   A O    1 
HETATM 6977 O O    B HOH   E 4 .   ? 21.366 7.470   -5.582  0.60 41.91 ?  520 HOH   A O    1 
HETATM 6978 O O    . HOH   E 4 .   ? 21.943 -23.977 4.502   1.00 26.52 ?  521 HOH   A O    1 
HETATM 6979 O O    . HOH   E 4 .   ? 36.328 -6.540  10.141  1.00 45.10 ?  522 HOH   A O    1 
HETATM 6980 O O    B HOH   E 4 .   ? 9.360  0.600   -5.358  0.60 29.65 ?  523 HOH   A O    1 
HETATM 6981 O O    B HOH   E 4 .   ? 7.825  6.864   2.068   0.60 24.97 ?  524 HOH   A O    1 
HETATM 6982 O O    . HOH   E 4 .   ? 17.265 -6.544  -14.165 1.00 43.92 ?  525 HOH   A O    1 
HETATM 6983 O O    A HOH   E 4 .   ? 14.789 8.704   4.899   0.40 25.05 ?  526 HOH   A O    1 
HETATM 6984 O O    . HOH   E 4 .   ? 23.938 9.063   -7.151  1.00 41.53 ?  527 HOH   A O    1 
HETATM 6985 O O    . HOH   E 4 .   ? 15.791 -12.316 27.328  1.00 48.31 ?  528 HOH   A O    1 
HETATM 6986 O O    . HOH   E 4 .   ? 16.278 -21.107 18.787  1.00 38.52 ?  529 HOH   A O    1 
HETATM 6987 O O    . HOH   E 4 .   ? 14.722 -22.771 19.783  1.00 38.09 ?  530 HOH   A O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 29.782 -22.369 5.496   1.00 20.12 ?  201 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 52.827 -13.409 -20.236 1.00 32.64 ?  202 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 41.601 -36.017 -17.115 1.00 32.99 ?  203 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 27.652 -29.114 -1.845  1.00 36.76 ?  204 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 48.039 -6.887  15.495  1.00 37.76 ?  205 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 37.952 -39.360 -0.181  1.00 38.71 ?  206 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 29.846 -26.239 4.071   1.00 27.49 ?  207 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 27.818 -41.902 -15.038 1.00 34.91 ?  208 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 55.414 -16.576 -14.351 1.00 35.52 ?  209 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 54.412 -9.366  -8.772  1.00 19.08 ?  210 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 59.053 -18.798 6.749   1.00 35.57 ?  211 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 58.143 -12.875 8.358   1.00 32.15 ?  212 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 41.301 -7.727  5.388   1.00 37.05 ?  213 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 30.163 -40.995 -8.071  1.00 16.28 ?  214 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 47.293 -7.340  -3.895  1.00 39.35 ?  215 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 57.657 -24.431 5.070   1.00 35.94 ?  216 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 50.149 -3.299  7.129   1.00 38.12 ?  217 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 56.289 -19.677 7.304   1.00 32.68 ?  218 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 41.460 -39.162 -14.829 1.00 22.49 ?  219 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 49.333 -22.717 -19.741 1.00 52.19 ?  220 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 57.139 -26.857 -7.746  1.00 42.87 ?  221 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 44.344 -7.082  1.988   1.00 34.08 ?  222 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 50.677 -6.081  0.128   1.00 25.47 ?  223 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 35.925 -43.224 -8.483  1.00 33.52 ?  224 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 37.039 -19.742 -18.068 1.00 37.79 ?  225 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 30.820 -28.704 4.332   1.00 27.74 ?  226 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 34.824 -24.598 13.827  1.00 31.06 ?  227 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 34.467 -36.325 -7.187  1.00 17.74 ?  228 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 42.855 -20.321 -20.750 1.00 37.51 ?  229 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 57.349 -16.257 -12.169 1.00 18.06 ?  230 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 40.512 -16.042 14.078  1.00 25.02 ?  231 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 25.344 -25.896 -1.288  1.00 31.82 ?  232 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 39.251 -10.850 6.114   1.00 25.51 ?  233 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 56.625 -30.744 -7.748  1.00 28.44 ?  234 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 51.584 -6.460  4.362   1.00 19.68 ?  235 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 50.648 -12.930 -0.501  1.00 11.75 ?  236 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 46.385 -1.521  13.152  1.00 28.69 ?  237 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 32.778 -43.758 -11.306 1.00 19.42 ?  238 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 45.172 -34.918 6.806   1.00 38.86 ?  239 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 44.414 -27.721 -0.684  1.00 22.20 ?  240 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 28.314 -19.651 -13.075 1.00 23.80 ?  241 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 41.300 -9.585  13.054  1.00 21.65 ?  242 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 38.402 -11.010 -2.275  1.00 18.58 ?  243 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 29.738 -34.169 -0.438  1.00 34.75 ?  244 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 39.423 -11.092 0.336   1.00 16.47 ?  245 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 43.062 -32.341 -17.060 1.00 23.93 ?  246 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 42.495 -25.321 2.618   1.00 14.88 ?  247 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 41.788 -23.476 9.311   1.00 17.34 ?  248 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 35.013 -7.981  -2.995  1.00 19.02 ?  249 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 42.561 -22.830 3.841   1.00 11.55 ?  250 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 44.896 -43.472 -10.454 1.00 27.28 ?  251 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 43.000 -43.199 -8.220  1.00 28.05 ?  252 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 57.517 -24.355 -3.829  1.00 21.08 ?  253 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 48.492 -36.534 -15.545 1.00 47.75 ?  254 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 31.692 -17.839 -14.438 1.00 30.17 ?  255 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 34.158 -18.450 11.414  1.00 24.52 ?  256 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 50.911 -39.863 -8.180  1.00 33.47 ?  257 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 58.080 -10.625 -4.090  1.00 21.18 ?  258 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 30.782 -15.705 2.665   1.00 13.45 ?  259 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 51.488 -13.836 10.979  1.00 25.99 ?  260 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 28.431 -30.861 -14.731 1.00 28.32 ?  261 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 27.088 -31.796 -9.944  1.00 19.41 ?  262 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 56.039 -23.499 -14.697 1.00 27.12 ?  263 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 38.864 -11.950 12.366  1.00 33.28 ?  264 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 29.647 -25.200 -10.778 1.00 16.33 ?  265 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 33.469 -16.953 8.071   1.00 18.83 ?  266 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 43.256 -15.755 -12.148 1.00 14.20 ?  267 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 47.902 -24.430 -17.720 1.00 30.49 ?  268 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 40.208 -12.713 -11.485 1.00 14.99 ?  269 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 57.382 -9.201  1.383   1.00 20.11 ?  270 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 34.888 -33.272 -19.174 1.00 31.88 ?  271 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 30.538 -42.190 -10.577 1.00 27.23 ?  272 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 42.254 -9.845  9.383   1.00 20.86 ?  273 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 47.936 -22.731 5.843   1.00 17.11 ?  274 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 28.221 -34.319 -9.383  1.00 18.29 ?  275 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 56.864 -8.611  8.393   1.00 19.34 ?  276 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 49.248 -28.668 -6.878  1.00 15.18 ?  277 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 42.314 -34.650 3.757   1.00 26.21 ?  278 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 42.295 -9.927  -14.892 1.00 39.51 ?  279 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 27.887 -22.875 -7.958  1.00 17.26 ?  280 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 52.509 -10.375 12.922  1.00 22.66 ?  281 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 46.545 -31.193 -4.788  1.00 21.77 ?  282 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 59.735 -15.332 8.117   1.00 31.41 ?  283 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 48.327 -25.008 3.102   1.00 13.26 ?  284 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 33.452 -15.268 -13.928 1.00 20.88 ?  285 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 43.481 -15.358 18.121  1.00 30.18 ?  286 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 46.812 -29.482 9.800   1.00 31.20 ?  287 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 41.107 -5.502  11.466  1.00 44.25 ?  288 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 47.010 -33.924 -4.630  1.00 17.63 ?  289 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 34.373 -12.749 2.638   1.00 24.56 ?  290 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 49.710 -0.433  10.212  1.00 31.86 ?  291 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 49.821 -24.714 5.806   1.00 33.40 ?  292 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 27.495 -26.698 -15.614 1.00 32.38 ?  293 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 48.623 -19.993 5.911   1.00 13.64 ?  294 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 45.242 -33.310 -15.954 1.00 23.03 ?  295 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 36.714 -12.729 -1.480  1.00 26.23 ?  296 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 51.151 -37.571 -9.578  1.00 26.48 ?  297 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 37.272 -35.605 7.200   1.00 32.27 ?  298 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 44.544 -27.407 2.010   1.00 14.54 ?  299 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 37.411 -18.092 13.098  1.00 28.58 ?  300 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 53.414 -30.130 4.475   1.00 17.96 ?  301 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 43.933 -29.300 -4.692  1.00 24.35 ?  302 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 40.147 -10.803 -9.522  1.00 17.34 ?  303 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 42.610 -12.286 -18.525 1.00 29.40 ?  304 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 57.064 -12.009 12.350  1.00 37.74 ?  305 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 62.604 -13.536 4.777   1.00 29.12 ?  306 HOH   B O    1 
HETATM 7094 O O    . HOH   F 4 .   ? 52.518 -35.636 -8.595  1.00 29.43 ?  307 HOH   B O    1 
HETATM 7095 O O    . HOH   F 4 .   ? 25.875 -21.451 -3.471  1.00 16.28 ?  308 HOH   B O    1 
HETATM 7096 O O    . HOH   F 4 .   ? 53.174 -16.100 -12.693 1.00 28.46 ?  309 HOH   B O    1 
HETATM 7097 O O    . HOH   F 4 .   ? 51.640 -5.953  -7.935  1.00 46.71 ?  310 HOH   B O    1 
HETATM 7098 O O    . HOH   F 4 .   ? 41.667 -8.061  1.359   1.00 24.74 ?  311 HOH   B O    1 
HETATM 7099 O O    . HOH   F 4 .   ? 34.985 -33.529 4.543   1.00 30.10 ?  312 HOH   B O    1 
HETATM 7100 O O    . HOH   F 4 .   ? 32.743 -34.550 -5.887  1.00 16.73 ?  313 HOH   B O    1 
HETATM 7101 O O    . HOH   F 4 .   ? 52.419 -29.172 -13.049 1.00 24.55 ?  314 HOH   B O    1 
HETATM 7102 O O    . HOH   F 4 .   ? 45.822 -40.338 -3.540  1.00 29.40 ?  315 HOH   B O    1 
HETATM 7103 O O    . HOH   F 4 .   ? 43.149 -21.364 10.689  1.00 15.66 ?  316 HOH   B O    1 
HETATM 7104 O O    . HOH   F 4 .   ? 37.762 -10.213 -10.728 1.00 16.91 ?  317 HOH   B O    1 
HETATM 7105 O O    . HOH   F 4 .   ? 59.819 -17.221 -10.502 1.00 32.24 ?  318 HOH   B O    1 
HETATM 7106 O O    . HOH   F 4 .   ? 26.269 -20.989 -6.226  1.00 16.52 ?  319 HOH   B O    1 
HETATM 7107 O O    . HOH   F 4 .   ? 38.277 -12.708 7.940   1.00 18.63 ?  320 HOH   B O    1 
HETATM 7108 O O    . HOH   F 4 .   ? 53.588 -12.561 -22.190 1.00 34.33 ?  321 HOH   B O    1 
HETATM 7109 O O    . HOH   F 4 .   ? 37.063 -30.503 -21.016 1.00 32.23 ?  322 HOH   B O    1 
HETATM 7110 O O    . HOH   F 4 .   ? 51.310 -32.902 -10.760 1.00 37.70 ?  323 HOH   B O    1 
HETATM 7111 O O    . HOH   F 4 .   ? 57.509 -22.017 3.208   1.00 29.08 ?  324 HOH   B O    1 
HETATM 7112 O O    . HOH   F 4 .   ? 43.076 -34.518 0.091   1.00 21.33 ?  325 HOH   B O    1 
HETATM 7113 O O    . HOH   F 4 .   ? 48.009 -32.566 -16.674 1.00 40.32 ?  326 HOH   B O    1 
HETATM 7114 O O    . HOH   F 4 .   ? 36.643 -12.390 4.276   1.00 17.81 ?  327 HOH   B O    1 
HETATM 7115 O O    . HOH   F 4 .   ? 41.165 -24.443 15.838  1.00 45.40 ?  328 HOH   B O    1 
HETATM 7116 O O    . HOH   F 4 .   ? 44.549 -24.564 9.561   1.00 19.69 ?  329 HOH   B O    1 
HETATM 7117 O O    . HOH   F 4 .   ? 62.792 -20.104 -0.769  1.00 36.25 ?  330 HOH   B O    1 
HETATM 7118 O O    . HOH   F 4 .   ? 38.291 -9.308  -13.265 1.00 26.33 ?  331 HOH   B O    1 
HETATM 7119 O O    . HOH   F 4 .   ? 27.776 -14.753 -9.454  1.00 35.28 ?  332 HOH   B O    1 
HETATM 7120 O O    . HOH   F 4 .   ? 44.120 -1.693  7.662   1.00 44.17 ?  333 HOH   B O    1 
HETATM 7121 O O    . HOH   F 4 .   ? 47.133 -24.442 8.164   1.00 25.66 ?  334 HOH   B O    1 
HETATM 7122 O O    . HOH   F 4 .   ? 33.531 -31.152 11.095  1.00 35.62 ?  335 HOH   B O    1 
HETATM 7123 O O    . HOH   F 4 .   ? 47.397 -27.388 2.008   1.00 14.36 ?  336 HOH   B O    1 
HETATM 7124 O O    . HOH   F 4 .   ? 48.490 -11.902 -13.870 1.00 26.67 ?  337 HOH   B O    1 
HETATM 7125 O O    . HOH   F 4 .   ? 36.934 -15.122 -16.538 1.00 41.08 ?  338 HOH   B O    1 
HETATM 7126 O O    . HOH   F 4 .   ? 42.773 -43.444 -14.349 1.00 37.27 ?  339 HOH   B O    1 
HETATM 7127 O O    . HOH   F 4 .   ? 45.608 -36.262 -16.080 1.00 36.21 ?  340 HOH   B O    1 
HETATM 7128 O O    . HOH   F 4 .   ? 38.316 -12.165 -16.197 1.00 42.61 ?  341 HOH   B O    1 
HETATM 7129 O O    . HOH   F 4 .   ? 39.470 -23.572 -20.285 1.00 38.54 ?  342 HOH   B O    1 
HETATM 7130 O O    . HOH   F 4 .   ? 46.707 -19.877 12.274  1.00 30.93 ?  343 HOH   B O    1 
HETATM 7131 O O    . HOH   F 4 .   ? 28.841 -42.922 -12.340 1.00 40.99 ?  344 HOH   B O    1 
HETATM 7132 O O    . HOH   F 4 .   ? 32.944 -14.640 1.072   1.00 19.28 ?  345 HOH   B O    1 
HETATM 7133 O O    . HOH   F 4 .   ? 37.016 -45.242 -9.673  1.00 37.26 ?  346 HOH   B O    1 
HETATM 7134 O O    . HOH   F 4 .   ? 38.542 -22.302 15.066  1.00 41.49 ?  347 HOH   B O    1 
HETATM 7135 O O    . HOH   F 4 .   ? 39.712 -44.281 -11.195 1.00 38.80 ?  348 HOH   B O    1 
HETATM 7136 O O    . HOH   F 4 .   ? 34.515 -10.277 7.577   1.00 23.54 ?  349 HOH   B O    1 
HETATM 7137 O O    . HOH   F 4 .   ? 27.692 -26.575 -0.542  1.00 29.14 ?  350 HOH   B O    1 
HETATM 7138 O O    . HOH   F 4 .   ? 40.345 -43.444 -9.093  1.00 26.21 ?  351 HOH   B O    1 
HETATM 7139 O O    . HOH   F 4 .   ? 62.419 -20.130 -4.878  1.00 43.83 ?  352 HOH   B O    1 
HETATM 7140 O O    . HOH   F 4 .   ? 33.679 -9.328  -8.859  1.00 33.22 ?  353 HOH   B O    1 
HETATM 7141 O O    . HOH   F 4 .   ? 55.586 -8.252  10.809  1.00 25.39 ?  354 HOH   B O    1 
HETATM 7142 O O    . HOH   F 4 .   ? 23.198 -23.621 6.822   1.00 36.66 ?  355 HOH   B O    1 
HETATM 7143 O O    . HOH   F 4 .   ? 44.100 -37.324 -17.793 1.00 33.57 ?  356 HOH   B O    1 
HETATM 7144 O O    . HOH   F 4 .   ? 35.979 -8.535  -9.699  1.00 36.35 ?  357 HOH   B O    1 
HETATM 7145 O O    . HOH   F 4 .   ? 56.442 -7.212  3.033   1.00 27.34 ?  358 HOH   B O    1 
HETATM 7146 O O    . HOH   F 4 .   ? 43.070 -12.692 -21.130 1.00 42.26 ?  359 HOH   B O    1 
HETATM 7147 O O    . HOH   F 4 .   ? 34.018 -7.747  11.426  1.00 39.13 ?  360 HOH   B O    1 
HETATM 7148 O O    . HOH   F 4 .   ? 61.424 -19.840 1.659   1.00 34.03 ?  361 HOH   B O    1 
HETATM 7149 O O    . HOH   F 4 .   ? 56.835 -21.512 -16.437 1.00 39.53 ?  362 HOH   B O    1 
HETATM 7150 O O    . HOH   F 4 .   ? 40.181 -8.751  9.866   1.00 39.35 ?  363 HOH   B O    1 
HETATM 7151 O O    . HOH   F 4 .   ? 27.057 -25.922 -11.378 1.00 32.83 ?  364 HOH   B O    1 
HETATM 7152 O O    . HOH   F 4 .   ? 58.838 -10.509 9.188   1.00 36.86 ?  365 HOH   B O    1 
HETATM 7153 O O    . HOH   F 4 .   ? 32.505 -23.574 14.080  1.00 39.61 ?  366 HOH   B O    1 
HETATM 7154 O O    . HOH   F 4 .   ? 48.264 -26.455 8.807   1.00 42.77 ?  367 HOH   B O    1 
HETATM 7155 O O    . HOH   F 4 .   ? 36.105 -8.615  8.989   1.00 37.43 ?  368 HOH   B O    1 
HETATM 7156 O O    . HOH   F 4 .   ? 41.716 -10.117 -17.423 1.00 55.58 ?  369 HOH   B O    1 
HETATM 7157 O O    . HOH   F 4 .   ? 54.133 -5.749  2.930   1.00 34.64 ?  370 HOH   B O    1 
HETATM 7158 O O    . HOH   F 4 .   ? 40.032 -11.331 -13.972 1.00 31.29 ?  371 HOH   B O    1 
HETATM 7159 O O    . HOH   F 4 .   ? 52.024 -12.899 13.297  1.00 32.16 ?  372 HOH   B O    1 
HETATM 7160 O O    . HOH   F 4 .   ? 39.730 -7.002  7.856   1.00 40.55 ?  373 HOH   B O    1 
HETATM 7161 O O    . HOH   F 4 .   ? 62.923 -12.355 6.921   1.00 36.82 ?  374 HOH   B O    1 
HETATM 7162 O O    . HOH   F 4 .   ? 55.933 -7.719  -0.610  1.00 33.86 ?  375 HOH   B O    1 
HETATM 7163 O O    . HOH   F 4 .   ? 37.988 -10.515 9.999   1.00 28.44 ?  376 HOH   B O    1 
HETATM 7164 O O    . HOH   F 4 .   ? 44.055 -5.597  -3.459  1.00 45.89 ?  377 HOH   B O    1 
HETATM 7165 O O    . HOH   F 4 .   ? 41.768 -6.725  -4.799  1.00 49.67 ?  378 HOH   B O    1 
HETATM 7166 O O    . HOH   F 4 .   ? 36.439 -22.752 13.309  1.00 26.64 ?  379 HOH   B O    1 
HETATM 7167 O O    . HOH   F 4 .   ? 42.595 -17.070 -23.165 1.00 43.35 ?  380 HOH   B O    1 
HETATM 7168 O O    . HOH   F 4 .   ? 52.790 -29.858 7.149   1.00 22.61 ?  381 HOH   B O    1 
HETATM 7169 O O    . HOH   F 4 .   ? 40.070 -7.544  3.226   1.00 34.85 ?  382 HOH   B O    1 
HETATM 7170 O O    . HOH   F 4 .   ? 39.623 -13.953 15.670  1.00 47.09 ?  383 HOH   B O    1 
HETATM 7171 O O    . HOH   F 4 .   ? 46.687 -5.399  2.911   1.00 40.72 ?  384 HOH   B O    1 
HETATM 7172 O O    . HOH   F 4 .   ? 60.428 -22.273 2.820   1.00 47.66 ?  385 HOH   B O    1 
HETATM 7173 O O    . HOH   F 4 .   ? 23.841 -20.807 -7.609  1.00 27.34 ?  386 HOH   B O    1 
HETATM 7174 O O    . HOH   F 4 .   ? 40.893 -9.786  15.777  1.00 49.90 ?  387 HOH   B O    1 
HETATM 7175 O O    . HOH   F 4 .   ? 35.334 -33.671 7.305   1.00 39.58 ?  388 HOH   B O    1 
HETATM 7176 O O    . HOH   F 4 .   ? 35.214 -20.297 13.310  1.00 30.89 ?  389 HOH   B O    1 
HETATM 7177 O O    . HOH   F 4 .   ? 25.701 -18.833 -11.966 1.00 39.86 ?  390 HOH   B O    1 
HETATM 7178 O O    . HOH   F 4 .   ? 44.082 -31.642 -3.813  1.00 34.03 ?  391 HOH   B O    1 
HETATM 7179 O O    . HOH   F 4 .   ? 40.654 -6.580  -0.896  1.00 25.91 ?  392 HOH   B O    1 
HETATM 7180 O O    . HOH   F 4 .   ? 27.841 -27.039 2.245   1.00 30.31 ?  393 HOH   B O    1 
HETATM 7181 O O    . HOH   F 4 .   ? 26.551 -27.922 -13.503 1.00 34.83 ?  394 HOH   B O    1 
HETATM 7182 O O    . HOH   F 4 .   ? 34.278 -33.377 9.617   1.00 33.71 ?  395 HOH   B O    1 
HETATM 7183 O O    . HOH   F 4 .   ? 24.533 -20.617 -10.493 1.00 35.87 ?  396 HOH   B O    1 
HETATM 7184 O O    . HOH   F 4 .   ? 26.803 -30.637 -12.583 1.00 25.97 ?  397 HOH   B O    1 
HETATM 7185 O O    . HOH   F 4 .   ? 50.593 -30.798 8.754   1.00 28.22 ?  398 HOH   B O    1 
HETATM 7186 O O    . HOH   F 4 .   ? 45.653 -20.208 15.173  1.00 50.75 ?  399 HOH   B O    1 
HETATM 7187 O O    . HOH   F 4 .   ? 57.604 -6.542  -2.362  1.00 34.77 ?  400 HOH   B O    1 
HETATM 7188 O O    . HOH   F 4 .   ? 40.802 -11.804 -22.331 1.00 40.19 ?  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   ? 0.6598 0.6636 0.7511 -0.0038 -0.0141 0.0428  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6763 0.6747 0.7678 -0.0089 -0.0210 0.0647  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6571 0.6599 0.7411 -0.0056 -0.0130 0.0428  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6736 0.6706 0.7550 -0.0110 -0.0191 0.0653  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6406 0.6450 0.7044 -0.0116 -0.0137 0.0449  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6564 0.6552 0.7144 -0.0185 -0.0193 0.0676  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6423 0.6465 0.7150 -0.0109 -0.0158 0.0464  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6584 0.6570 0.7269 -0.0179 -0.0227 0.0693  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6680 0.6685 0.7602 -0.0028 -0.0115 0.0408  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6848 0.6789 0.7740 -0.0073 -0.0178 0.0629  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6712 0.6708 0.7622 -0.0013 -0.0112 0.0402  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6878 0.6806 0.7754 -0.0052 -0.0177 0.0625  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6721 0.6720 0.7623 -0.0021 -0.0111 0.0401  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6894 0.6830 0.7759 -0.0067 -0.0176 0.0619  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6190 0.6255 0.6517 -0.0188 -0.0121 0.0446  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6335 0.6346 0.6531 -0.0272 -0.0159 0.0673  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5936 0.6029 0.5943 -0.0265 -0.0104 0.0428  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6062 0.6106 0.5865 -0.0367 -0.0124 0.0659  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5556 0.5730 0.5571 -0.0354 -0.0043 0.0310  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5640 0.5803 0.5446 -0.0491 -0.0016 0.0524  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5557 0.5736 0.5547 -0.0361 -0.0052 0.0322  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5642 0.5816 0.5390 -0.0493 -0.0027 0.0543  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6023 0.6074 0.5710 -0.0251 -0.0139 0.0524  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6164 0.6139 0.5590 -0.0345 -0.0183 0.0781  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6075 0.6093 0.5488 -0.0240 -0.0166 0.0609  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6224 0.6142 0.5322 -0.0329 -0.0237 0.0889  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6099 0.6104 0.5426 -0.0236 -0.0179 0.0640  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6251 0.6144 0.5234 -0.0324 -0.0267 0.0935  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6084 0.6089 0.5439 -0.0233 -0.0171 0.0643  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6234 0.6134 0.5275 -0.0319 -0.0248 0.0930  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5154 0.5404 0.5158 -0.0442 0.0029  0.0181  5   SER   A N   
60   N N   B SER   A 5   ? 0.5191 0.5463 0.5020 -0.0626 0.0118  0.0382  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4731 0.5070 0.4721 -0.0534 0.0120  0.0054  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4716 0.5114 0.4574 -0.0775 0.0302  0.0259  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4271 0.4674 0.4178 -0.0596 0.0196  -0.0012 5   SER   A C   
64   C C   B SER   A 5   ? 0.4189 0.4671 0.3977 -0.0924 0.0529  0.0272  5   SER   A C   
65   O O   A SER   A 5   ? 0.4270 0.4672 0.4109 -0.0599 0.0214  -0.0050 5   SER   A O   
66   O O   B SER   A 5   ? 0.4204 0.4682 0.3879 -0.0911 0.0571  0.0205  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4760 0.5120 0.4942 -0.0564 0.0139  0.0010  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4766 0.5194 0.4869 -0.0782 0.0278  0.0167  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4773 0.5148 0.5021 -0.0586 0.0145  -0.0013 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4792 0.5237 0.4973 -0.0796 0.0256  0.0124  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3805 0.4273 0.3649 -0.0643 0.0260  -0.0004 6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3643 0.4219 0.3391 -0.1078 0.0727  0.0412  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3358 0.3863 0.3126 -0.0675 0.0298  0.0060  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3145 0.3756 0.2788 -0.1175 0.0833  0.0621  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3173 0.3705 0.3084 -0.0732 0.0399  0.0057  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3067 0.3662 0.2802 -0.1133 0.0955  0.0591  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3202 0.3731 0.3230 -0.0744 0.0364  0.0036  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3098 0.3688 0.3025 -0.1115 0.0927  0.0698  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.3131 0.3611 0.2761 -0.0624 0.0238  0.0134  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2842 0.3421 0.2406 -0.1174 0.0647  0.0785  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2940 0.3378 0.2483 -0.0571 0.0169  0.0181  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2631 0.3159 0.2166 -0.1048 0.0413  0.0731  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2847 0.3281 0.2344 -0.0551 0.0117  0.0203  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2506 0.3035 0.2015 -0.1017 0.0320  0.0742  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2906 0.3284 0.2462 -0.0514 0.0187  0.0209  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2664 0.3099 0.2306 -0.0885 0.0323  0.0656  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2821 0.3221 0.2361 -0.0534 0.0143  0.0244  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2489 0.2986 0.2079 -0.0954 0.0333  0.0732  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2869 0.3228 0.2434 -0.0497 0.0184  0.0228  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2618 0.3046 0.2355 -0.0829 0.0304  0.0594  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2834 0.3204 0.2399 -0.0509 0.0146  0.0229  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2554 0.2999 0.2263 -0.0858 0.0273  0.0603  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2962 0.3525 0.2906 -0.0758 0.0520  0.0085  7   SER   A N   
122  N N   B SER   A 7   ? 0.2967 0.3531 0.2682 -0.1089 0.1039  0.0431  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2794 0.3363 0.2836 -0.0716 0.0597  0.0075  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2940 0.3452 0.2825 -0.0923 0.0973  0.0207  7   SER   A CA  
125  C C   A SER   A 7   ? 0.2562 0.3124 0.2691 -0.0703 0.0653  0.0057  7   SER   A C   
126  C C   B SER   A 7   ? 0.2673 0.3237 0.2685 -0.0849 0.1073  0.0162  7   SER   A C   
127  O O   A SER   A 7   ? 0.2597 0.3110 0.2722 -0.0719 0.0647  0.0007  7   SER   A O   
128  O O   B SER   A 7   ? 0.2669 0.3175 0.2660 -0.0918 0.1037  0.0162  7   SER   A O   
129  C CB  A SER   A 7   ? 0.2852 0.3417 0.2883 -0.0666 0.0615  0.0093  7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3128 0.3557 0.3019 -0.0867 0.0867  0.0107  7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2907 0.3455 0.2980 -0.0633 0.0597  0.0112  7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3305 0.3642 0.3333 -0.0805 0.0679  0.0036  7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2345 0.2908 0.2615 -0.0653 0.0645  0.0037  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2490 0.3085 0.2751 -0.0692 0.1051  0.0088  8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2136 0.2658 0.2552 -0.0562 0.0674  0.0087  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2364 0.2854 0.2830 -0.0545 0.0939  0.0080  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1902 0.2451 0.2463 -0.0411 0.0578  0.0075  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2134 0.2639 0.2759 -0.0375 0.0843  0.0054  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1923 0.2450 0.2593 -0.0325 0.0571  -0.0104 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2146 0.2618 0.2908 -0.0279 0.0818  -0.0171 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1695 0.2281 0.2269 -0.0309 0.0495  0.0237  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1949 0.2470 0.2593 -0.0250 0.0733  0.0288  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1507 0.2085 0.2046 -0.0271 0.0338  0.0337  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1827 0.2257 0.2386 -0.0198 0.0556  0.0480  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1391 0.1928 0.1961 -0.0221 0.0342  0.0500  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1698 0.2041 0.2333 -0.0106 0.0540  0.0603  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1426 0.2049 0.2042 -0.0164 0.0164  0.0562  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1672 0.2149 0.2584 -0.0101 0.0488  0.0683  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1465 0.2082 0.1992 -0.0221 0.0256  0.0276  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1771 0.2284 0.2243 -0.0163 0.0479  0.0484  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1471 0.2020 0.1951 -0.0146 0.0317  0.0173  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1748 0.2249 0.2127 -0.0111 0.0525  0.0398  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1487 0.1976 0.1994 -0.0120 0.0343  0.0075  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1852 0.2303 0.2123 -0.0143 0.0537  0.0355  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1503 0.1959 0.1948 -0.0163 0.0267  0.0198  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1739 0.2170 0.1981 -0.0047 0.0454  0.0379  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1512 0.1987 0.2074 -0.0088 0.0339  -0.0069 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1826 0.2204 0.2090 -0.0135 0.0591  0.0322  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1527 0.1984 0.2015 -0.0165 0.0274  0.0076  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1716 0.2126 0.1934 0.0030  0.0485  0.0333  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1529 0.1999 0.2196 -0.0201 0.0328  -0.0041 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1678 0.2098 0.2078 -0.0061 0.0610  0.0282  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1620 0.2033 0.2396 -0.0284 0.0315  -0.0129 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1606 0.2043 0.2282 -0.0145 0.0588  0.0236  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1366 0.1786 0.2101 -0.0196 0.0287  0.0433  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1628 0.1859 0.2393 -0.0075 0.0426  0.0482  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1350 0.1712 0.2086 -0.0202 0.0283  0.0535  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1512 0.1729 0.2383 -0.0120 0.0401  0.0520  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1349 0.1662 0.1961 -0.0236 0.0211  0.0474  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1491 0.1647 0.2173 -0.0164 0.0258  0.0537  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1298 0.1581 0.1784 -0.0238 0.0160  0.0435  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1512 0.1562 0.2052 -0.0182 0.0248  0.0513  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1411 0.1730 0.2350 -0.0103 0.0201  0.0616  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1489 0.1657 0.2652 -0.0132 0.0244  0.0575  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1633 0.1840 0.2675 -0.0021 0.0048  0.0573  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1615 0.1726 0.2941 -0.0128 -0.0044 0.0544  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1717 0.1914 0.2853 -0.0072 0.0056  0.0569  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1693 0.1857 0.3246 -0.0247 -0.0015 0.0602  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1800 0.1898 0.2733 0.0062  0.0071  0.0537  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1761 0.1834 0.3015 0.0023  -0.0106 0.0397  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1418 0.1684 0.2018 -0.0272 0.0152  0.0432  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1473 0.1626 0.2127 -0.0198 0.0096  0.0552  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1432 0.1674 0.2084 -0.0419 0.0142  0.0374  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1519 0.1553 0.2184 -0.0333 0.0047  0.0561  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1429 0.1775 0.2283 -0.0417 0.0164  0.0343  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1440 0.1442 0.2170 -0.0355 0.0086  0.0461  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1467 0.1764 0.2648 -0.0535 0.0205  0.0290  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1367 0.1370 0.2394 -0.0328 0.0065  0.0281  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1548 0.1607 0.1937 -0.0427 0.0125  0.0231  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1697 0.1532 0.2252 -0.0351 -0.0036 0.0467  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1684 0.1575 0.1760 -0.0359 0.0173  0.0238  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1855 0.1533 0.2202 -0.0293 -0.0084 0.0533  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1800 0.1531 0.1553 -0.0348 0.0223  0.0223  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.2021 0.1534 0.2174 -0.0235 -0.0052 0.0490  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1911 0.1544 0.1409 -0.0267 0.0235  0.0223  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.2118 0.1554 0.2164 -0.0194 -0.0064 0.0464  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1921 0.1575 0.1426 -0.0203 0.0165  0.0240  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.2125 0.1573 0.2292 -0.0151 -0.0166 0.0427  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1356 0.1758 0.2017 -0.0432 0.0084  0.0384  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1391 0.1541 0.2090 -0.0279 -0.0042 0.0452  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1403 0.1823 0.1823 -0.0401 0.0047  0.0442  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1406 0.1785 0.2085 -0.0198 0.0002  0.0448  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1373 0.1774 0.1796 -0.0495 0.0094  0.0482  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1475 0.1830 0.2150 -0.0221 0.0119  0.0493  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1478 0.1845 0.1897 -0.0528 0.0005  0.0372  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1547 0.1888 0.2178 -0.0198 0.0111  0.0439  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1469 0.1793 0.1697 -0.0384 0.0034  0.0447  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1501 0.1855 0.2096 -0.0129 -0.0048 0.0409  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1606 0.1858 0.1684 -0.0262 0.0099  0.0451  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1560 0.1889 0.2103 -0.0078 -0.0011 0.0332  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1697 0.1867 0.1723 -0.0115 0.0164  0.0444  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1650 0.1989 0.2268 -0.0043 0.0059  0.0279  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1618 0.1883 0.1768 -0.0283 0.0074  0.0380  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1557 0.1915 0.2172 -0.0056 -0.0004 0.0196  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1273 0.1686 0.1846 -0.0402 0.0095  0.0419  13  THR   A N   
320  N N   B THR   A 13  ? 0.1476 0.1746 0.2287 -0.0134 0.0096  0.0393  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1284 0.1636 0.1720 -0.0374 0.0150  0.0352  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1546 0.1694 0.2177 -0.0196 0.0172  0.0281  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1324 0.1566 0.1664 -0.0327 0.0167  0.0404  13  THR   A C   
324  C C   B THR   A 13  ? 0.1588 0.1630 0.2110 -0.0219 0.0198  0.0299  13  THR   A C   
325  O O   A THR   A 13  ? 0.1383 0.1606 0.1841 -0.0292 0.0075  0.0289  13  THR   A O   
326  O O   B THR   A 13  ? 0.1569 0.1606 0.2200 -0.0103 0.0164  0.0239  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1283 0.1706 0.1736 -0.0333 0.0211  0.0318  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1570 0.1702 0.2242 -0.0224 0.0057  0.0254  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1209 0.1646 0.1768 -0.0290 0.0317  0.0329  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1606 0.1521 0.2430 -0.0227 0.0088  0.0228  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1382 0.1815 0.1858 -0.0278 0.0145  0.0340  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1615 0.1820 0.2286 -0.0111 0.0107  0.0309  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1327 0.1488 0.1621 -0.0349 0.0128  0.0423  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1665 0.1650 0.2093 -0.0309 0.0207  0.0260  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1361 0.1526 0.1836 -0.0217 0.0025  0.0519  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1743 0.1771 0.2220 -0.0278 0.0164  0.0390  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1340 0.1503 0.1720 -0.0178 -0.0067 0.0501  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1636 0.1664 0.1869 -0.0253 0.0083  0.0413  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1528 0.1524 0.1828 -0.0254 -0.0052 0.0366  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1812 0.1674 0.1853 -0.0241 0.0153  0.0448  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1552 0.1641 0.2286 -0.0235 0.0027  0.0544  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.2026 0.2067 0.2859 -0.0278 0.0241  0.0490  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1682 0.2028 0.2688 -0.0212 0.0031  0.0488  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2356 0.2573 0.3510 -0.0195 0.0193  0.0425  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.1635 0.2027 0.2687 -0.0335 0.0025  0.0669  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2483 0.2703 0.3741 -0.0189 0.0051  0.0610  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.1759 0.2257 0.2975 -0.0105 -0.0062 0.0256  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2453 0.2802 0.3833 -0.0050 0.0180  0.0177  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1311 0.1478 0.1799 -0.0105 0.0076  0.0496  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1485 0.1566 0.1784 -0.0289 0.0106  0.0469  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1365 0.1449 0.1856 -0.0054 0.0031  0.0437  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1409 0.1524 0.2081 -0.0220 0.0105  0.0366  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1308 0.1443 0.2032 -0.0150 0.0136  0.0380  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1318 0.1460 0.2330 -0.0153 0.0176  0.0387  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1233 0.1461 0.2004 -0.0146 0.0180  0.0252  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1228 0.1428 0.2605 -0.0031 0.0174  0.0361  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1428 0.1497 0.1750 0.0028  -0.0008 0.0506  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1308 0.1462 0.1978 -0.0217 0.0179  0.0328  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1486 0.1608 0.1746 0.0029  0.0071  0.0342  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1380 0.1544 0.2163 -0.0237 0.0169  0.0153  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1649 0.1724 0.1947 -0.0129 0.0006  0.0380  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1539 0.1607 0.2386 -0.0420 0.0001  0.0164  15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1442 0.1650 0.1727 0.0084  0.0214  0.0280  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1389 0.1654 0.2162 -0.0229 0.0254  0.0161  15  ASN   A ND2 
399  N N   . VAL   A 16  ? 0.1357 0.1468 0.2241 -0.0193 0.0065  0.0455  16  VAL   A N   
400  C CA  . VAL   A 16  ? 0.1351 0.1590 0.2266 -0.0195 0.0076  0.0498  16  VAL   A CA  
401  C C   . VAL   A 16  ? 0.1312 0.1580 0.2156 -0.0246 -0.0033 0.0491  16  VAL   A C   
402  O O   . VAL   A 16  ? 0.1286 0.1560 0.2276 -0.0210 0.0122  0.0476  16  VAL   A O   
403  C CB  . VAL   A 16  ? 0.1458 0.1722 0.2205 -0.0037 0.0205  0.0525  16  VAL   A CB  
404  C CG1 . VAL   A 16  ? 0.1632 0.1764 0.2269 0.0121  0.0290  0.0503  16  VAL   A CG1 
405  C CG2 . VAL   A 16  ? 0.1601 0.1861 0.2405 0.0003  0.0331  0.0557  16  VAL   A CG2 
416  N N   A TYR   A 17  ? 0.1342 0.1511 0.2048 -0.0246 0.0063  0.0522  17  TYR   A N   
417  N N   B TYR   A 17  ? 0.1261 0.1548 0.2189 -0.0216 0.0091  0.0534  17  TYR   A N   
418  C CA  A TYR   A 17  ? 0.1445 0.1498 0.2000 -0.0266 0.0092  0.0497  17  TYR   A CA  
419  C CA  B TYR   A 17  ? 0.1310 0.1580 0.2162 -0.0235 0.0102  0.0564  17  TYR   A CA  
420  C C   A TYR   A 17  ? 0.1375 0.1469 0.2001 -0.0232 0.0143  0.0396  17  TYR   A C   
421  C C   B TYR   A 17  ? 0.1345 0.1546 0.2143 -0.0174 0.0056  0.0526  17  TYR   A C   
422  O O   A TYR   A 17  ? 0.1304 0.1424 0.2014 -0.0225 0.0215  0.0348  17  TYR   A O   
423  O O   B TYR   A 17  ? 0.1271 0.1538 0.2110 -0.0259 -0.0061 0.0556  17  TYR   A O   
424  C CB  A TYR   A 17  ? 0.1708 0.1459 0.2023 -0.0280 -0.0020 0.0516  17  TYR   A CB  
425  C CB  B TYR   A 17  ? 0.1477 0.1584 0.2230 -0.0227 0.0022  0.0533  17  TYR   A CB  
426  C CG  A TYR   A 17  ? 0.1963 0.1507 0.1944 -0.0232 -0.0146 0.0442  17  TYR   A CG  
427  C CG  B TYR   A 17  ? 0.1712 0.1688 0.2201 -0.0200 -0.0034 0.0378  17  TYR   A CG  
428  C CD1 A TYR   A 17  ? 0.2105 0.1593 0.2090 -0.0152 -0.0192 0.0393  17  TYR   A CD1 
429  C CD1 B TYR   A 17  ? 0.1845 0.1714 0.2275 -0.0058 -0.0102 0.0350  17  TYR   A CD1 
430  C CD2 A TYR   A 17  ? 0.2067 0.1557 0.1865 -0.0267 -0.0126 0.0460  17  TYR   A CD2 
431  C CD2 B TYR   A 17  ? 0.1842 0.1788 0.2209 -0.0269 0.0013  0.0350  17  TYR   A CD2 
432  C CE1 A TYR   A 17  ? 0.2191 0.1611 0.2204 -0.0151 -0.0170 0.0414  17  TYR   A CE1 
433  C CE1 B TYR   A 17  ? 0.1936 0.1693 0.2378 -0.0085 -0.0147 0.0387  17  TYR   A CE1 
434  C CE2 A TYR   A 17  ? 0.2199 0.1597 0.2018 -0.0263 -0.0146 0.0417  17  TYR   A CE2 
435  C CE2 B TYR   A 17  ? 0.1988 0.1727 0.2301 -0.0265 -0.0071 0.0230  17  TYR   A CE2 
436  C CZ  A TYR   A 17  ? 0.2279 0.1574 0.2045 -0.0180 -0.0106 0.0371  17  TYR   A CZ  
437  C CZ  B TYR   A 17  ? 0.2074 0.1640 0.2282 -0.0226 -0.0125 0.0329  17  TYR   A CZ  
438  O OH  A TYR   A 17  ? 0.2450 0.1546 0.2154 -0.0072 -0.0013 0.0268  17  TYR   A OH  
439  O OH  B TYR   A 17  ? 0.2260 0.1571 0.2361 -0.0201 -0.0148 0.0269  17  TYR   A OH  
458  N N   . ILE   A 18  ? 0.1396 0.1519 0.2085 -0.0231 0.0152  0.0555  18  ILE   A N   
459  C CA  . ILE   A 18  ? 0.1397 0.1547 0.2118 -0.0108 0.0215  0.0533  18  ILE   A CA  
460  C C   . ILE   A 18  ? 0.1417 0.1634 0.2263 -0.0149 0.0275  0.0473  18  ILE   A C   
461  O O   . ILE   A 18  ? 0.1422 0.1766 0.2291 -0.0201 0.0280  0.0549  18  ILE   A O   
462  C CB  . ILE   A 18  ? 0.1475 0.1638 0.2014 -0.0059 0.0233  0.0546  18  ILE   A CB  
463  C CG1 . ILE   A 18  ? 0.1642 0.1811 0.1969 -0.0036 0.0112  0.0663  18  ILE   A CG1 
464  C CG2 . ILE   A 18  ? 0.1522 0.1688 0.2350 -0.0129 0.0178  0.0487  18  ILE   A CG2 
465  C CD1 . ILE   A 18  ? 0.1962 0.2029 0.2095 -0.0037 0.0017  0.0554  18  ILE   A CD1 
478  N N   A LYS   A 19  ? 0.1520 0.1645 0.2158 -0.0121 0.0409  0.0425  19  LYS   A N   
479  N N   B LYS   A 19  ? 0.1427 0.1599 0.2241 -0.0025 0.0417  0.0562  19  LYS   A N   
480  C CA  A LYS   A 19  ? 0.1666 0.1726 0.2185 -0.0104 0.0459  0.0347  19  LYS   A CA  
481  C CA  B LYS   A 19  ? 0.1527 0.1692 0.2374 0.0035  0.0507  0.0567  19  LYS   A CA  
482  C C   A LYS   A 19  ? 0.1651 0.1620 0.2143 -0.0067 0.0392  0.0327  19  LYS   A C   
483  C C   B LYS   A 19  ? 0.1442 0.1638 0.2415 0.0021  0.0428  0.0560  19  LYS   A C   
484  O O   A LYS   A 19  ? 0.1587 0.1604 0.2083 -0.0072 0.0303  0.0328  19  LYS   A O   
485  O O   B LYS   A 19  ? 0.1340 0.1626 0.2289 0.0036  0.0290  0.0562  19  LYS   A O   
486  C CB  A LYS   A 19  ? 0.1758 0.1930 0.2250 -0.0125 0.0456  0.0290  19  LYS   A CB  
487  C CB  B LYS   A 19  ? 0.1664 0.1875 0.2301 0.0114  0.0488  0.0625  19  LYS   A CB  
488  C CG  A LYS   A 19  ? 0.1880 0.2022 0.2162 -0.0100 0.0382  0.0224  19  LYS   A CG  
489  C CG  B LYS   A 19  ? 0.1838 0.2001 0.2397 0.0115  0.0446  0.0502  19  LYS   A CG  
490  C CD  A LYS   A 19  ? 0.1980 0.2103 0.2130 -0.0095 0.0391  0.0213  19  LYS   A CD  
491  C CD  B LYS   A 19  ? 0.2010 0.2183 0.2449 0.0059  0.0406  0.0415  19  LYS   A CD  
492  C CE  A LYS   A 19  ? 0.2028 0.2099 0.2098 -0.0082 0.0410  0.0241  19  LYS   A CE  
493  C CE  B LYS   A 19  ? 0.2139 0.2316 0.2459 -0.0006 0.0414  0.0335  19  LYS   A CE  
494  N NZ  A LYS   A 19  ? 0.2066 0.2088 0.2040 -0.0083 0.0439  0.0151  19  LYS   A NZ  
495  N NZ  B LYS   A 19  ? 0.2215 0.2362 0.2339 -0.0031 0.0395  0.0271  19  LYS   A NZ  
522  N N   A ASN   A 20  ? 0.1711 0.1613 0.2179 -0.0054 0.0405  0.0352  20  ASN   A N   
523  N N   B ASN   A 20  ? 0.1466 0.1717 0.2620 -0.0019 0.0401  0.0578  20  ASN   A N   
524  C CA  A ASN   A 20  ? 0.1771 0.1661 0.2111 0.0011  0.0310  0.0213  20  ASN   A CA  
525  C CA  B ASN   A 20  ? 0.1501 0.1833 0.2606 0.0051  0.0388  0.0449  20  ASN   A CA  
526  C C   A ASN   A 20  ? 0.1831 0.1652 0.2011 0.0010  0.0303  0.0199  20  ASN   A C   
527  C C   B ASN   A 20  ? 0.1629 0.1883 0.2638 0.0036  0.0434  0.0424  20  ASN   A C   
528  O O   A ASN   A 20  ? 0.1866 0.1625 0.1861 -0.0154 0.0339  0.0241  20  ASN   A O   
529  O O   B ASN   A 20  ? 0.1807 0.1990 0.2628 0.0022  0.0377  0.0363  20  ASN   A O   
530  C CB  A ASN   A 20  ? 0.1879 0.1698 0.2143 0.0080  0.0260  0.0163  20  ASN   A CB  
531  C CB  B ASN   A 20  ? 0.1496 0.1847 0.2558 0.0110  0.0355  0.0435  20  ASN   A CB  
532  C CG  A ASN   A 20  ? 0.2025 0.1753 0.2272 0.0160  0.0227  0.0100  20  ASN   A CG  
533  C CG  B ASN   A 20  ? 0.1492 0.1815 0.2455 0.0181  0.0312  0.0388  20  ASN   A CG  
534  O OD1 A ASN   A 20  ? 0.2177 0.1906 0.2541 0.0225  0.0241  0.0144  20  ASN   A OD1 
535  O OD1 B ASN   A 20  ? 0.1502 0.1812 0.2508 0.0262  0.0298  0.0269  20  ASN   A OD1 
536  N ND2 A ASN   A 20  ? 0.2026 0.1680 0.2294 0.0228  0.0223  -0.0020 20  ASN   A ND2 
537  N ND2 B ASN   A 20  ? 0.1568 0.1839 0.2625 0.0149  0.0194  0.0502  20  ASN   A ND2 
550  N N   A ALA   A 21  ? 0.1924 0.1731 0.2108 0.0032  0.0204  0.0120  21  ALA   A N   
551  N N   B ALA   A 21  ? 0.1669 0.1876 0.2635 -0.0035 0.0449  0.0359  21  ALA   A N   
552  C CA  A ALA   A 21  ? 0.2017 0.1792 0.2113 0.0052  0.0159  0.0151  21  ALA   A CA  
553  C CA  B ALA   A 21  ? 0.1728 0.1825 0.2562 -0.0087 0.0450  0.0417  21  ALA   A CA  
554  C C   A ALA   A 21  ? 0.2013 0.1822 0.2089 0.0013  0.0290  0.0038  21  ALA   A C   
555  C C   B ALA   A 21  ? 0.1540 0.1656 0.2434 -0.0077 0.0483  0.0317  21  ALA   A C   
556  O O   A ALA   A 21  ? 0.2049 0.1917 0.2097 -0.0033 0.0307  -0.0068 21  ALA   A O   
557  O O   B ALA   A 21  ? 0.1441 0.1678 0.2412 -0.0115 0.0330  0.0247  21  ALA   A O   
558  C CB  A ALA   A 21  ? 0.2128 0.1864 0.2334 0.0096  0.0001  0.0202  21  ALA   A CB  
559  C CB  B ALA   A 21  ? 0.1913 0.1920 0.2732 -0.0149 0.0357  0.0493  21  ALA   A CB  
570  N N   A ASP   A 22  ? 0.2038 0.1777 0.2158 -0.0031 0.0341  0.0038  22  ASP   A N   
571  N N   B ASP   A 22  ? 0.1624 0.1560 0.2492 -0.0063 0.0562  0.0254  22  ASP   A N   
572  C CA  A ASP   A 22  ? 0.2070 0.1759 0.2150 -0.0047 0.0314  0.0041  22  ASP   A CA  
573  C CA  B ASP   A 22  ? 0.1713 0.1511 0.2405 0.0007  0.0512  0.0198  22  ASP   A CA  
574  C C   A ASP   A 22  ? 0.1971 0.1714 0.1984 -0.0084 0.0255  0.0078  22  ASP   A C   
575  C C   B ASP   A 22  ? 0.1525 0.1516 0.2088 -0.0116 0.0553  0.0096  22  ASP   A C   
576  O O   A ASP   A 22  ? 0.1998 0.1754 0.2104 -0.0143 0.0269  0.0054  22  ASP   A O   
577  O O   B ASP   A 22  ? 0.1514 0.1722 0.2171 -0.0238 0.0562  -0.0012 22  ASP   A O   
578  C CB  A ASP   A 22  ? 0.2214 0.1808 0.2386 -0.0053 0.0316  -0.0057 22  ASP   A CB  
579  C CB  B ASP   A 22  ? 0.1997 0.1510 0.2639 0.0086  0.0559  0.0139  22  ASP   A CB  
580  C CG  A ASP   A 22  ? 0.2288 0.1836 0.2628 -0.0130 0.0219  -0.0102 22  ASP   A CG  
581  C CG  B ASP   A 22  ? 0.2139 0.1522 0.2714 0.0120  0.0614  0.0157  22  ASP   A CG  
582  O OD1 A ASP   A 22  ? 0.2195 0.1773 0.2759 -0.0315 0.0034  -0.0124 22  ASP   A OD1 
583  O OD1 B ASP   A 22  ? 0.2096 0.1478 0.2430 -0.0016 0.0588  0.0170  22  ASP   A OD1 
584  O OD2 A ASP   A 22  ? 0.2385 0.1905 0.2757 -0.0051 0.0287  -0.0175 22  ASP   A OD2 
585  O OD2 B ASP   A 22  ? 0.2297 0.1662 0.3115 0.0086  0.0747  0.0173  22  ASP   A OD2 
594  N N   A ILE   A 23  ? 0.1927 0.1692 0.1747 -0.0080 0.0201  0.0044  23  ILE   A N   
595  N N   B ILE   A 23  ? 0.1479 0.1423 0.1987 -0.0086 0.0463  0.0132  23  ILE   A N   
596  C CA  A ILE   A 23  ? 0.1851 0.1606 0.1622 -0.0068 0.0257  0.0057  23  ILE   A CA  
597  C CA  B ILE   A 23  ? 0.1441 0.1539 0.1816 -0.0136 0.0324  0.0165  23  ILE   A CA  
598  C C   A ILE   A 23  ? 0.1834 0.1600 0.1618 -0.0100 0.0432  0.0055  23  ILE   A C   
599  C C   B ILE   A 23  ? 0.1490 0.1696 0.1870 -0.0219 0.0415  0.0071  23  ILE   A C   
600  O O   A ILE   A 23  ? 0.1896 0.1684 0.1626 -0.0179 0.0426  0.0115  23  ILE   A O   
601  O O   B ILE   A 23  ? 0.1556 0.1762 0.1957 -0.0185 0.0346  0.0012  23  ILE   A O   
602  C CB  A ILE   A 23  ? 0.1832 0.1561 0.1443 0.0021  0.0208  0.0010  23  ILE   A CB  
603  C CB  B ILE   A 23  ? 0.1390 0.1493 0.1603 -0.0072 0.0191  0.0255  23  ILE   A CB  
604  C CG1 A ILE   A 23  ? 0.1874 0.1491 0.1364 0.0035  0.0188  -0.0006 23  ILE   A CG1 
605  C CG1 B ILE   A 23  ? 0.1525 0.1527 0.1546 -0.0049 0.0094  0.0140  23  ILE   A CG1 
606  C CG2 A ILE   A 23  ? 0.1783 0.1618 0.1477 0.0072  0.0165  0.0023  23  ILE   A CG2 
607  C CG2 B ILE   A 23  ? 0.1411 0.1522 0.1554 0.0002  0.0144  0.0206  23  ILE   A CG2 
608  C CD1 A ILE   A 23  ? 0.1889 0.1446 0.1294 0.0027  0.0108  -0.0057 23  ILE   A CD1 
609  C CD1 B ILE   A 23  ? 0.1483 0.1519 0.1707 0.0032  0.0004  0.0085  23  ILE   A CD1 
632  N N   A VAL   A 24  ? 0.1897 0.1634 0.1775 -0.0115 0.0418  -0.0027 24  VAL   A N   
633  N N   B VAL   A 24  ? 0.1649 0.1735 0.2044 -0.0343 0.0419  0.0013  24  VAL   A N   
634  C CA  A VAL   A 24  ? 0.1960 0.1804 0.1971 -0.0181 0.0395  -0.0159 24  VAL   A CA  
635  C CA  B VAL   A 24  ? 0.1859 0.1825 0.2254 -0.0377 0.0473  -0.0036 24  VAL   A CA  
636  C C   A VAL   A 24  ? 0.2047 0.1996 0.2064 -0.0279 0.0327  -0.0152 24  VAL   A C   
637  C C   B VAL   A 24  ? 0.1975 0.2020 0.2265 -0.0391 0.0587  -0.0266 24  VAL   A C   
638  O O   A VAL   A 24  ? 0.2094 0.2023 0.2047 -0.0302 0.0330  -0.0117 24  VAL   A O   
639  O O   B VAL   A 24  ? 0.2051 0.2079 0.2291 -0.0296 0.0567  -0.0215 24  VAL   A O   
640  C CB  A VAL   A 24  ? 0.1979 0.1829 0.2090 -0.0129 0.0437  -0.0167 24  VAL   A CB  
641  C CB  B VAL   A 24  ? 0.1998 0.1840 0.2482 -0.0385 0.0436  0.0150  24  VAL   A CB  
642  C CG1 A VAL   A 24  ? 0.1972 0.1864 0.2130 -0.0052 0.0474  -0.0305 24  VAL   A CG1 
643  C CG1 B VAL   A 24  ? 0.2178 0.1911 0.2800 -0.0385 0.0299  0.0150  24  VAL   A CG1 
644  C CG2 A VAL   A 24  ? 0.2031 0.1840 0.2139 -0.0095 0.0548  -0.0055 24  VAL   A CG2 
645  C CG2 B VAL   A 24  ? 0.2121 0.1835 0.2476 -0.0344 0.0521  0.0280  24  VAL   A CG2 
664  N N   A GLU   A 25  ? 0.2125 0.2191 0.2145 -0.0288 0.0321  -0.0215 25  GLU   A N   
665  N N   B GLU   A 25  ? 0.2011 0.2114 0.2204 -0.0425 0.0806  -0.0455 25  GLU   A N   
666  C CA  A GLU   A 25  ? 0.2236 0.2391 0.2234 -0.0242 0.0296  -0.0257 25  GLU   A CA  
667  C CA  B GLU   A 25  ? 0.2190 0.2420 0.2243 -0.0431 0.0928  -0.0499 25  GLU   A CA  
668  C C   A GLU   A 25  ? 0.2122 0.2421 0.1979 -0.0313 0.0354  -0.0260 25  GLU   A C   
669  C C   B GLU   A 25  ? 0.2085 0.2550 0.1962 -0.0476 0.1013  -0.0448 25  GLU   A C   
670  O O   A GLU   A 25  ? 0.2131 0.2487 0.2067 -0.0265 0.0357  -0.0341 25  GLU   A O   
671  O O   B GLU   A 25  ? 0.2126 0.2651 0.2132 -0.0487 0.0991  -0.0535 25  GLU   A O   
672  C CB  A GLU   A 25  ? 0.2454 0.2591 0.2582 -0.0162 0.0255  -0.0270 25  GLU   A CB  
673  C CB  B GLU   A 25  ? 0.2460 0.2599 0.2608 -0.0393 0.0972  -0.0463 25  GLU   A CB  
674  C CG  A GLU   A 25  ? 0.2676 0.2766 0.3003 -0.0126 0.0128  -0.0279 25  GLU   A CG  
675  C CG  B GLU   A 25  ? 0.2765 0.2806 0.3177 -0.0370 0.0889  -0.0404 25  GLU   A CG  
676  C CD  A GLU   A 25  ? 0.2853 0.2928 0.3415 -0.0084 0.0023  -0.0270 25  GLU   A CD  
677  C CD  B GLU   A 25  ? 0.3022 0.3017 0.3712 -0.0343 0.0707  -0.0357 25  GLU   A CD  
678  O OE1 A GLU   A 25  ? 0.2919 0.3002 0.3480 -0.0027 -0.0045 -0.0321 25  GLU   A OE1 
679  O OE1 B GLU   A 25  ? 0.3126 0.3094 0.3960 -0.0301 0.0609  -0.0359 25  GLU   A OE1 
680  O OE2 A GLU   A 25  ? 0.2926 0.3017 0.3674 -0.0095 -0.0038 -0.0287 25  GLU   A OE2 
681  O OE2 B GLU   A 25  ? 0.3142 0.3105 0.3969 -0.0340 0.0624  -0.0358 25  GLU   A OE2 
694  N N   A GLU   A 26  ? 0.2047 0.2402 0.1889 -0.0415 0.0423  -0.0274 26  GLU   A N   
695  N N   B GLU   A 26  ? 0.2042 0.2558 0.1959 -0.0486 0.0919  -0.0370 26  GLU   A N   
696  C CA  A GLU   A 26  ? 0.2092 0.2431 0.1702 -0.0524 0.0443  -0.0240 26  GLU   A CA  
697  C CA  B GLU   A 26  ? 0.2102 0.2641 0.1849 -0.0516 0.0834  -0.0174 26  GLU   A CA  
698  C C   A GLU   A 26  ? 0.2106 0.2403 0.1471 -0.0533 0.0484  -0.0228 26  GLU   A C   
699  C C   B GLU   A 26  ? 0.2074 0.2607 0.1678 -0.0559 0.0766  -0.0166 26  GLU   A C   
700  O O   A GLU   A 26  ? 0.2187 0.2408 0.1369 -0.0538 0.0568  -0.0191 26  GLU   A O   
701  O O   B GLU   A 26  ? 0.2196 0.2637 0.1723 -0.0587 0.0778  -0.0265 26  GLU   A O   
702  C CB  A GLU   A 26  ? 0.2174 0.2451 0.1830 -0.0598 0.0438  -0.0193 26  GLU   A CB  
703  C CB  B GLU   A 26  ? 0.2226 0.2697 0.1996 -0.0556 0.0716  -0.0019 26  GLU   A CB  
704  C CG  A GLU   A 26  ? 0.2287 0.2526 0.2196 -0.0587 0.0457  -0.0244 26  GLU   A CG  
705  C CG  B GLU   A 26  ? 0.2352 0.2832 0.2304 -0.0538 0.0681  -0.0032 26  GLU   A CG  
706  C CD  A GLU   A 26  ? 0.2366 0.2575 0.2357 -0.0606 0.0573  -0.0259 26  GLU   A CD  
707  C CD  B GLU   A 26  ? 0.2444 0.2936 0.2350 -0.0594 0.0688  -0.0038 26  GLU   A CD  
708  O OE1 A GLU   A 26  ? 0.2321 0.2652 0.2386 -0.0551 0.0823  -0.0415 26  GLU   A OE1 
709  O OE1 B GLU   A 26  ? 0.2493 0.3083 0.2260 -0.0546 0.0847  -0.0072 26  GLU   A OE1 
710  O OE2 A GLU   A 26  ? 0.2453 0.2594 0.2312 -0.0642 0.0515  -0.0165 26  GLU   A OE2 
711  O OE2 B GLU   A 26  ? 0.2461 0.2934 0.2204 -0.0641 0.0737  -0.0032 26  GLU   A OE2 
724  N N   A ALA   A 27  ? 0.2037 0.2325 0.1465 -0.0595 0.0435  -0.0208 27  ALA   A N   
725  N N   B ALA   A 27  ? 0.1938 0.2555 0.1559 -0.0546 0.0672  -0.0024 27  ALA   A N   
726  C CA  A ALA   A 27  ? 0.2103 0.2390 0.1546 -0.0581 0.0397  -0.0209 27  ALA   A CA  
727  C CA  B ALA   A 27  ? 0.1985 0.2678 0.1524 -0.0424 0.0527  0.0022  27  ALA   A CA  
728  C C   A ALA   A 27  ? 0.2278 0.2498 0.1691 -0.0630 0.0436  -0.0306 27  ALA   A C   
729  C C   B ALA   A 27  ? 0.2192 0.2851 0.1680 -0.0360 0.0528  -0.0044 27  ALA   A C   
730  O O   A ALA   A 27  ? 0.2320 0.2456 0.1748 -0.0674 0.0451  -0.0283 27  ALA   A O   
731  O O   B ALA   A 27  ? 0.2227 0.2828 0.1720 -0.0339 0.0447  0.0036  27  ALA   A O   
732  C CB  A ALA   A 27  ? 0.2034 0.2353 0.1571 -0.0563 0.0353  -0.0138 27  ALA   A CB  
733  C CB  B ALA   A 27  ? 0.1874 0.2637 0.1473 -0.0437 0.0444  0.0091  27  ALA   A CB  
744  N N   A LYS   A 28  ? 0.2510 0.2675 0.1797 -0.0581 0.0357  -0.0483 28  LYS   A N   
745  N N   B LYS   A 28  ? 0.2463 0.3020 0.1804 -0.0278 0.0501  -0.0270 28  LYS   A N   
746  C CA  A LYS   A 28  ? 0.2774 0.2943 0.2054 -0.0489 0.0395  -0.0512 28  LYS   A CA  
747  C CA  B LYS   A 28  ? 0.2770 0.3286 0.2019 -0.0168 0.0509  -0.0451 28  LYS   A CA  
748  C C   A LYS   A 28  ? 0.2986 0.3249 0.2158 -0.0496 0.0562  -0.0399 28  LYS   A C   
749  C C   B LYS   A 28  ? 0.3053 0.3579 0.1960 -0.0210 0.0675  -0.0370 28  LYS   A C   
750  O O   A LYS   A 28  ? 0.3018 0.3284 0.2308 -0.0467 0.0452  -0.0399 28  LYS   A O   
751  O O   B LYS   A 28  ? 0.3154 0.3655 0.2211 -0.0163 0.0445  -0.0362 28  LYS   A O   
752  C CB  A LYS   A 28  ? 0.2835 0.2956 0.2321 -0.0364 0.0334  -0.0555 28  LYS   A CB  
753  C CB  B LYS   A 28  ? 0.2846 0.3317 0.2341 -0.0026 0.0477  -0.0631 28  LYS   A CB  
754  C CG  A LYS   A 28  ? 0.2893 0.2953 0.2523 -0.0291 0.0344  -0.0557 28  LYS   A CG  
755  C CG  B LYS   A 28  ? 0.2933 0.3371 0.2657 0.0053  0.0487  -0.0708 28  LYS   A CG  
756  C CD  A LYS   A 28  ? 0.2959 0.3007 0.2867 -0.0266 0.0318  -0.0459 28  LYS   A CD  
757  C CD  B LYS   A 28  ? 0.3068 0.3495 0.3191 0.0151  0.0501  -0.0661 28  LYS   A CD  
758  C CE  A LYS   A 28  ? 0.3026 0.3073 0.3121 -0.0250 0.0328  -0.0381 28  LYS   A CE  
759  C CE  B LYS   A 28  ? 0.3201 0.3609 0.3545 0.0227  0.0508  -0.0662 28  LYS   A CE  
760  N NZ  A LYS   A 28  ? 0.3070 0.3106 0.3232 -0.0229 0.0376  -0.0367 28  LYS   A NZ  
761  N NZ  B LYS   A 28  ? 0.3300 0.3671 0.3775 0.0281  0.0485  -0.0705 28  LYS   A NZ  
788  N N   A LYS   A 29  ? 0.3166 0.3525 0.2302 -0.0545 0.0793  -0.0228 29  LYS   A N   
789  N N   B LYS   A 29  ? 0.3206 0.3804 0.1910 -0.0345 0.1062  -0.0183 29  LYS   A N   
790  C CA  A LYS   A 29  ? 0.3394 0.3812 0.2606 -0.0572 0.0900  -0.0085 29  LYS   A CA  
791  C CA  B LYS   A 29  ? 0.3437 0.4035 0.2243 -0.0458 0.1174  -0.0042 29  LYS   A CA  
792  C C   A LYS   A 29  ? 0.3457 0.3893 0.2315 -0.0660 0.0940  0.0016  29  LYS   A C   
793  C C   B LYS   A 29  ? 0.3499 0.4025 0.2062 -0.0617 0.1096  0.0062  29  LYS   A C   
794  O O   A LYS   A 29  ? 0.3542 0.3991 0.2436 -0.0619 0.0879  0.0010  29  LYS   A O   
795  O O   B LYS   A 29  ? 0.3619 0.4161 0.2170 -0.0592 0.1032  0.0090  29  LYS   A O   
796  C CB  A LYS   A 29  ? 0.3554 0.4020 0.3211 -0.0497 0.0924  -0.0050 29  LYS   A CB  
797  C CB  B LYS   A 29  ? 0.3600 0.4272 0.2875 -0.0365 0.1279  -0.0024 29  LYS   A CB  
798  C CG  A LYS   A 29  ? 0.3726 0.4210 0.3855 -0.0421 0.0880  -0.0028 29  LYS   A CG  
799  C CG  B LYS   A 29  ? 0.3793 0.4487 0.3643 -0.0256 0.1222  -0.0022 29  LYS   A CG  
800  C CD  A LYS   A 29  ? 0.3885 0.4375 0.4433 -0.0356 0.0816  -0.0037 29  LYS   A CD  
801  C CD  B LYS   A 29  ? 0.3981 0.4676 0.4358 -0.0155 0.1111  -0.0052 29  LYS   A CD  
802  C CE  A LYS   A 29  ? 0.3998 0.4493 0.4808 -0.0314 0.0782  -0.0055 29  LYS   A CE  
803  C CE  B LYS   A 29  ? 0.4111 0.4815 0.4840 -0.0089 0.1048  -0.0105 29  LYS   A CE  
804  N NZ  A LYS   A 29  ? 0.4052 0.4555 0.5039 -0.0285 0.0745  -0.0062 29  LYS   A NZ  
805  N NZ  B LYS   A 29  ? 0.4180 0.4886 0.5137 -0.0053 0.0978  -0.0115 29  LYS   A NZ  
832  N N   . VAL   A 30  ? 0.3413 0.3866 0.1940 -0.0772 0.0980  0.0078  30  VAL   A N   
833  C CA  . VAL   A 30  ? 0.3332 0.3677 0.1864 -0.0991 0.0693  0.0257  30  VAL   A CA  
834  C C   . VAL   A 30  ? 0.3354 0.3481 0.1414 -0.1015 0.0485  0.0364  30  VAL   A C   
835  O O   . VAL   A 30  ? 0.3484 0.3538 0.1521 -0.1032 0.0409  0.0405  30  VAL   A O   
836  C CB  . VAL   A 30  ? 0.3307 0.3631 0.2306 -0.1140 0.0542  0.0327  30  VAL   A CB  
837  C CG1 . VAL   A 30  ? 0.3314 0.3610 0.2524 -0.1159 0.0406  0.0344  30  VAL   A CG1 
838  C CG2 . VAL   A 30  ? 0.3316 0.3679 0.2624 -0.1214 0.0547  0.0328  30  VAL   A CG2 
849  N N   A LYS   A 31  ? 0.3322 0.3396 0.1505 -0.0977 0.0343  0.0317  31  LYS   A N   
850  N N   B LYS   A 31  ? 0.3300 0.3370 0.1247 -0.1000 0.0317  0.0312  31  LYS   A N   
851  C CA  A LYS   A 31  ? 0.3361 0.3360 0.1785 -0.0875 0.0137  0.0319  31  LYS   A CA  
852  C CA  B LYS   A 31  ? 0.3335 0.3314 0.1386 -0.0862 0.0085  0.0349  31  LYS   A CA  
853  C C   A LYS   A 31  ? 0.3126 0.3169 0.1354 -0.0807 0.0059  0.0508  31  LYS   A C   
854  C C   B LYS   A 31  ? 0.3114 0.3153 0.1187 -0.0781 -0.0004 0.0597  31  LYS   A C   
855  O O   A LYS   A 31  ? 0.3187 0.3277 0.1509 -0.0811 -0.0035 0.0536  31  LYS   A O   
856  O O   B LYS   A 31  ? 0.3159 0.3270 0.1336 -0.0731 -0.0187 0.0672  31  LYS   A O   
857  C CB  A LYS   A 31  ? 0.3654 0.3529 0.2769 -0.0775 -0.0032 0.0125  31  LYS   A CB  
858  C CB  B LYS   A 31  ? 0.3701 0.3535 0.2475 -0.0786 -0.0111 0.0109  31  LYS   A CB  
859  C CG  A LYS   A 31  ? 0.3938 0.3706 0.3799 -0.0638 -0.0197 -0.0024 31  LYS   A CG  
860  C CG  B LYS   A 31  ? 0.4062 0.3765 0.3723 -0.0639 -0.0314 -0.0091 31  LYS   A CG  
861  C CD  A LYS   A 31  ? 0.4153 0.3856 0.4548 -0.0518 -0.0314 -0.0135 31  LYS   A CD  
862  C CD  B LYS   A 31  ? 0.4331 0.3955 0.4608 -0.0499 -0.0453 -0.0244 31  LYS   A CD  
863  C CE  A LYS   A 31  ? 0.4281 0.3962 0.5001 -0.0431 -0.0391 -0.0200 31  LYS   A CE  
864  C CE  B LYS   A 31  ? 0.4494 0.4089 0.5131 -0.0394 -0.0541 -0.0336 31  LYS   A CE  
865  N NZ  A LYS   A 31  ? 0.4339 0.4013 0.5291 -0.0380 -0.0439 -0.0235 31  LYS   A NZ  
866  N NZ  B LYS   A 31  ? 0.4576 0.4156 0.5458 -0.0331 -0.0599 -0.0391 31  LYS   A NZ  
893  N N   . PRO   A 32  ? 0.2818 0.2871 0.1057 -0.0750 0.0034  0.0480  32  PRO   A N   
894  C CA  . PRO   A 32  ? 0.2698 0.2657 0.1266 -0.0665 -0.0081 0.0636  32  PRO   A CA  
895  C C   . PRO   A 32  ? 0.2619 0.2565 0.1326 -0.0560 -0.0208 0.0664  32  PRO   A C   
896  O O   . PRO   A 32  ? 0.2492 0.2396 0.1584 -0.0537 -0.0381 0.0635  32  PRO   A O   
897  C CB  . PRO   A 32  ? 0.2607 0.2667 0.1359 -0.0658 -0.0058 0.0552  32  PRO   A CB  
898  C CG  . PRO   A 32  ? 0.2499 0.2708 0.0964 -0.0627 -0.0172 0.0373  32  PRO   A CG  
899  C CD  . PRO   A 32  ? 0.2568 0.2739 0.0925 -0.0677 -0.0031 0.0374  32  PRO   A CD  
907  N N   . THR   A 33  ? 0.2656 0.2525 0.1333 -0.0491 -0.0210 0.0646  33  THR   A N   
908  C CA  . THR   A 33  ? 0.2621 0.2486 0.1411 -0.0329 -0.0337 0.0650  33  THR   A CA  
909  C C   . THR   A 33  ? 0.2307 0.2195 0.1345 -0.0326 -0.0289 0.0541  33  THR   A C   
910  O O   . THR   A 33  ? 0.2256 0.2156 0.1486 -0.0360 -0.0443 0.0550  33  THR   A O   
911  C CB  . THR   A 33  ? 0.2887 0.2709 0.1615 -0.0218 -0.0416 0.0863  33  THR   A CB  
912  O OG1 . THR   A 33  ? 0.3115 0.2868 0.1889 -0.0100 -0.0278 0.0952  33  THR   A OG1 
913  C CG2 . THR   A 33  ? 0.2936 0.2807 0.1920 -0.0180 -0.0570 0.0814  33  THR   A CG2 
921  N N   . VAL   A 34  ? 0.2026 0.2005 0.1236 -0.0348 -0.0191 0.0481  34  VAL   A N   
922  C CA  . VAL   A 34  ? 0.1838 0.1779 0.1161 -0.0319 -0.0107 0.0439  34  VAL   A CA  
923  C C   . VAL   A 34  ? 0.1669 0.1709 0.1107 -0.0324 -0.0053 0.0292  34  VAL   A C   
924  O O   . VAL   A 34  ? 0.1711 0.1751 0.1407 -0.0354 -0.0061 0.0388  34  VAL   A O   
925  C CB  . VAL   A 34  ? 0.1924 0.1739 0.1362 -0.0266 -0.0075 0.0351  34  VAL   A CB  
926  C CG1 . VAL   A 34  ? 0.1969 0.1705 0.1410 -0.0261 0.0015  0.0204  34  VAL   A CG1 
927  C CG2 . VAL   A 34  ? 0.1960 0.1859 0.1712 -0.0209 -0.0156 0.0373  34  VAL   A CG2 
937  N N   . VAL   A 35  ? 0.1538 0.1614 0.1094 -0.0282 -0.0073 0.0289  35  VAL   A N   
938  C CA  . VAL   A 35  ? 0.1477 0.1573 0.1040 -0.0252 -0.0041 0.0257  35  VAL   A CA  
939  C C   . VAL   A 35  ? 0.1457 0.1374 0.0989 -0.0215 -0.0003 0.0170  35  VAL   A C   
940  O O   . VAL   A 35  ? 0.1340 0.1529 0.1291 -0.0285 0.0128  0.0142  35  VAL   A O   
941  C CB  . VAL   A 35  ? 0.1576 0.1652 0.1207 -0.0143 0.0117  0.0140  35  VAL   A CB  
942  C CG1 . VAL   A 35  ? 0.1658 0.1667 0.1345 -0.0064 0.0136  0.0062  35  VAL   A CG1 
943  C CG2 . VAL   A 35  ? 0.1588 0.1667 0.1365 -0.0082 0.0176  0.0034  35  VAL   A CG2 
953  N N   . VAL   A 36  ? 0.1282 0.1392 0.1041 -0.0148 0.0073  0.0181  36  VAL   A N   
954  C CA  . VAL   A 36  ? 0.1225 0.1304 0.1085 -0.0102 0.0059  0.0111  36  VAL   A CA  
955  C C   . VAL   A 36  ? 0.1209 0.1307 0.1101 -0.0156 0.0044  0.0133  36  VAL   A C   
956  O O   . VAL   A 36  ? 0.1236 0.1336 0.1383 -0.0078 0.0169  0.0160  36  VAL   A O   
957  C CB  . VAL   A 36  ? 0.1240 0.1241 0.1193 -0.0109 0.0044  0.0158  36  VAL   A CB  
958  C CG1 . VAL   A 36  ? 0.1359 0.1241 0.1295 -0.0134 0.0056  0.0048  36  VAL   A CG1 
959  C CG2 . VAL   A 36  ? 0.1311 0.1295 0.1507 -0.0087 0.0022  0.0278  36  VAL   A CG2 
969  N N   A ASN   A 37  ? 0.1226 0.1304 0.1110 -0.0094 0.0047  0.0157  37  ASN   A N   
970  N N   B ASN   A 37  ? 0.1148 0.1192 0.1083 -0.0077 0.0022  0.0141  37  ASN   A N   
971  C CA  A ASN   A 37  ? 0.1253 0.1331 0.1110 -0.0030 0.0078  0.0176  37  ASN   A CA  
972  C CA  B ASN   A 37  ? 0.1101 0.1138 0.1017 0.0015  0.0027  0.0170  37  ASN   A CA  
973  C C   A ASN   A 37  ? 0.1232 0.1398 0.1094 -0.0054 0.0155  0.0238  37  ASN   A C   
974  C C   B ASN   A 37  ? 0.1123 0.1116 0.1006 0.0044  0.0128  0.0259  37  ASN   A C   
975  O O   A ASN   A 37  ? 0.1276 0.1465 0.1131 0.0023  0.0069  0.0144  37  ASN   A O   
976  O O   B ASN   A 37  ? 0.1223 0.1187 0.1117 0.0084  0.0055  0.0092  37  ASN   A O   
977  C CB  A ASN   A 37  ? 0.1322 0.1317 0.1137 -0.0006 0.0064  0.0154  37  ASN   A CB  
978  C CB  B ASN   A 37  ? 0.1116 0.1143 0.1208 -0.0041 0.0003  0.0148  37  ASN   A CB  
979  C CG  A ASN   A 37  ? 0.1355 0.1269 0.0964 0.0062  -0.0046 0.0029  37  ASN   A CG  
980  C CG  B ASN   A 37  ? 0.1113 0.1101 0.1194 -0.0055 0.0029  0.0004  37  ASN   A CG  
981  O OD1 A ASN   A 37  ? 0.1371 0.1236 0.0961 0.0103  -0.0082 -0.0069 37  ASN   A OD1 
982  O OD1 B ASN   A 37  ? 0.1121 0.1163 0.1117 -0.0058 0.0031  0.0122  37  ASN   A OD1 
983  N ND2 A ASN   A 37  ? 0.1388 0.1265 0.1026 0.0084  -0.0163 0.0143  37  ASN   A ND2 
984  N ND2 B ASN   A 37  ? 0.1191 0.1067 0.1204 -0.0085 0.0052  0.0168  37  ASN   A ND2 
997  N N   A ALA   A 38  ? 0.1250 0.1370 0.1200 -0.0106 0.0142  0.0137  38  ALA   A N   
998  N N   B ALA   A 38  ? 0.1187 0.1085 0.1170 0.0074  0.0071  0.0155  38  ALA   A N   
999  C CA  A ALA   A 38  ? 0.1318 0.1268 0.1088 -0.0068 0.0066  -0.0023 38  ALA   A CA  
1000 C CA  B ALA   A 38  ? 0.1284 0.1208 0.1194 0.0055  -0.0074 0.0151  38  ALA   A CA  
1001 C C   A ALA   A 38  ? 0.1319 0.1291 0.1008 -0.0066 -0.0033 -0.0074 38  ALA   A C   
1002 C C   B ALA   A 38  ? 0.1259 0.1294 0.1242 0.0038  -0.0152 0.0067  38  ALA   A C   
1003 O O   A ALA   A 38  ? 0.1340 0.1220 0.0974 -0.0096 -0.0071 -0.0085 38  ALA   A O   
1004 O O   B ALA   A 38  ? 0.1211 0.1256 0.1413 -0.0002 -0.0147 0.0161  38  ALA   A O   
1005 C CB  A ALA   A 38  ? 0.1353 0.1354 0.1120 -0.0129 0.0061  -0.0086 38  ALA   A CB  
1006 C CB  B ALA   A 38  ? 0.1342 0.1316 0.1384 0.0021  -0.0222 0.0038  38  ALA   A CB  
1017 N N   A ALA   A 39  ? 0.1286 0.1241 0.1061 -0.0026 -0.0026 -0.0015 39  ALA   A N   
1018 N N   B ALA   A 39  ? 0.1313 0.1264 0.1290 0.0023  -0.0032 0.0150  39  ALA   A N   
1019 C CA  A ALA   A 39  ? 0.1253 0.1249 0.1132 0.0063  0.0013  0.0037  39  ALA   A CA  
1020 C CA  B ALA   A 39  ? 0.1308 0.1268 0.1113 -0.0034 -0.0025 0.0078  39  ALA   A CA  
1021 C C   A ALA   A 39  ? 0.1267 0.1306 0.1024 0.0015  -0.0066 0.0030  39  ALA   A C   
1022 C C   B ALA   A 39  ? 0.1206 0.1170 0.1205 -0.0032 -0.0138 0.0052  39  ALA   A C   
1023 O O   A ALA   A 39  ? 0.1292 0.1344 0.1014 0.0006  -0.0014 0.0070  39  ALA   A O   
1024 O O   B ALA   A 39  ? 0.1373 0.1224 0.1348 -0.0061 -0.0059 0.0063  39  ALA   A O   
1025 C CB  A ALA   A 39  ? 0.1270 0.1307 0.1366 0.0113  0.0003  0.0054  39  ALA   A CB  
1026 C CB  B ALA   A 39  ? 0.1444 0.1504 0.1138 -0.0060 -0.0106 0.0141  39  ALA   A CB  
1037 N N   A ASN   A 40  ? 0.1196 0.1343 0.1007 -0.0053 0.0010  0.0041  40  ASN   A N   
1038 N N   B ASN   A 40  ? 0.1247 0.1157 0.1233 -0.0033 0.0065  0.0060  40  ASN   A N   
1039 C CA  A ASN   A 40  ? 0.1235 0.1342 0.1076 -0.0026 -0.0029 0.0075  40  ASN   A CA  
1040 C CA  B ASN   A 40  ? 0.1323 0.1163 0.1185 0.0012  -0.0083 0.0060  40  ASN   A CA  
1041 C C   A ASN   A 40  ? 0.1253 0.1254 0.1045 -0.0037 0.0008  0.0152  40  ASN   A C   
1042 C C   B ASN   A 40  ? 0.1277 0.1107 0.0942 -0.0002 0.0133  0.0100  40  ASN   A C   
1043 O O   A ASN   A 40  ? 0.1254 0.1274 0.1195 -0.0117 -0.0006 0.0179  40  ASN   A O   
1044 O O   B ASN   A 40  ? 0.1229 0.1148 0.1042 -0.0021 0.0097  0.0127  40  ASN   A O   
1045 C CB  A ASN   A 40  ? 0.1305 0.1451 0.1254 0.0004  -0.0069 0.0038  40  ASN   A CB  
1046 C CB  B ASN   A 40  ? 0.1456 0.1209 0.1362 0.0069  -0.0151 0.0085  40  ASN   A CB  
1047 C CG  A ASN   A 40  ? 0.1336 0.1430 0.1470 0.0046  -0.0042 0.0143  40  ASN   A CG  
1048 C CG  B ASN   A 40  ? 0.1525 0.1224 0.1577 0.0065  -0.0273 0.0079  40  ASN   A CG  
1049 O OD1 A ASN   A 40  ? 0.1336 0.1424 0.1410 0.0001  0.0018  0.0191  40  ASN   A OD1 
1050 O OD1 B ASN   A 40  ? 0.1657 0.1323 0.1926 0.0050  -0.0267 -0.0007 40  ASN   A OD1 
1051 N ND2 A ASN   A 40  ? 0.1408 0.1524 0.1711 0.0079  0.0033  0.0103  40  ASN   A ND2 
1052 N ND2 B ASN   A 40  ? 0.1510 0.1308 0.1701 -0.0004 -0.0137 -0.0057 40  ASN   A ND2 
1065 N N   A VAL   A 41  ? 0.1297 0.1276 0.1098 0.0025  0.0014  0.0131  41  VAL   A N   
1066 N N   B VAL   A 41  ? 0.1407 0.1191 0.1048 -0.0031 0.0140  0.0160  41  VAL   A N   
1067 C CA  A VAL   A 41  ? 0.1393 0.1356 0.1194 0.0046  0.0108  0.0105  41  VAL   A CA  
1068 C CA  B VAL   A 41  ? 0.1467 0.1245 0.1205 -0.0017 0.0278  0.0138  41  VAL   A CA  
1069 C C   A VAL   A 41  ? 0.1352 0.1279 0.1171 0.0107  0.0080  0.0103  41  VAL   A C   
1070 C C   B VAL   A 41  ? 0.1425 0.1245 0.1331 -0.0065 0.0283  0.0104  41  VAL   A C   
1071 O O   A VAL   A 41  ? 0.1368 0.1236 0.1295 0.0145  0.0068  0.0037  41  VAL   A O   
1072 O O   B VAL   A 41  ? 0.1471 0.1178 0.1378 -0.0125 0.0167  0.0035  41  VAL   A O   
1073 C CB  A VAL   A 41  ? 0.1563 0.1471 0.1219 -0.0054 0.0171  0.0036  41  VAL   A CB  
1074 C CB  B VAL   A 41  ? 0.1709 0.1406 0.1476 -0.0111 0.0420  0.0045  41  VAL   A CB  
1075 C CG1 A VAL   A 41  ? 0.1669 0.1501 0.1348 -0.0035 0.0153  -0.0031 41  VAL   A CG1 
1076 C CG1 B VAL   A 41  ? 0.1876 0.1452 0.1640 -0.0105 0.0484  -0.0064 41  VAL   A CG1 
1077 C CG2 A VAL   A 41  ? 0.1686 0.1548 0.1089 -0.0097 0.0303  0.0115  41  VAL   A CG2 
1078 C CG2 B VAL   A 41  ? 0.1907 0.1505 0.1422 -0.0198 0.0360  -0.0005 41  VAL   A CG2 
1097 N N   A TYR   A 42  ? 0.1336 0.1236 0.1263 -0.0003 0.0134  0.0128  42  TYR   A N   
1098 N N   B TYR   A 42  ? 0.1349 0.1217 0.1434 -0.0016 0.0333  0.0156  42  TYR   A N   
1099 C CA  A TYR   A 42  ? 0.1445 0.1226 0.1397 -0.0044 0.0150  0.0173  42  TYR   A CA  
1100 C CA  B TYR   A 42  ? 0.1402 0.1211 0.1431 -0.0070 0.0362  0.0236  42  TYR   A CA  
1101 C C   A TYR   A 42  ? 0.1298 0.1192 0.1367 0.0028  0.0099  0.0213  42  TYR   A C   
1102 C C   B TYR   A 42  ? 0.1367 0.1218 0.1344 -0.0054 0.0277  0.0295  42  TYR   A C   
1103 O O   A TYR   A 42  ? 0.1235 0.1203 0.1539 0.0009  0.0031  0.0125  42  TYR   A O   
1104 O O   B TYR   A 42  ? 0.1337 0.1195 0.1581 -0.0160 0.0264  0.0115  42  TYR   A O   
1105 C CB  A TYR   A 42  ? 0.1623 0.1333 0.1343 0.0007  0.0175  0.0242  42  TYR   A CB  
1106 C CB  B TYR   A 42  ? 0.1597 0.1329 0.1355 -0.0066 0.0364  0.0338  42  TYR   A CB  
1107 C CG  A TYR   A 42  ? 0.1729 0.1465 0.1335 0.0053  0.0157  0.0318  42  TYR   A CG  
1108 C CG  B TYR   A 42  ? 0.1683 0.1511 0.1452 -0.0064 0.0324  0.0339  42  TYR   A CG  
1109 C CD1 A TYR   A 42  ? 0.1725 0.1528 0.1327 0.0027  0.0154  0.0407  42  TYR   A CD1 
1110 C CD1 B TYR   A 42  ? 0.1718 0.1620 0.1549 -0.0132 0.0272  0.0286  42  TYR   A CD1 
1111 C CD2 A TYR   A 42  ? 0.1847 0.1658 0.1524 0.0092  0.0138  0.0243  42  TYR   A CD2 
1112 C CD2 B TYR   A 42  ? 0.1697 0.1720 0.1624 0.0053  0.0330  0.0140  42  TYR   A CD2 
1113 C CE1 A TYR   A 42  ? 0.1648 0.1604 0.1236 0.0046  0.0176  0.0440  42  TYR   A CE1 
1114 C CE1 B TYR   A 42  ? 0.1699 0.1734 0.1509 -0.0129 0.0311  0.0196  42  TYR   A CE1 
1115 C CE2 A TYR   A 42  ? 0.1814 0.1746 0.1471 0.0167  0.0192  0.0259  42  TYR   A CE2 
1116 C CE2 B TYR   A 42  ? 0.1714 0.1826 0.1678 -0.0031 0.0318  0.0127  42  TYR   A CE2 
1117 C CZ  A TYR   A 42  ? 0.1684 0.1719 0.1386 0.0104  0.0198  0.0280  42  TYR   A CZ  
1118 C CZ  B TYR   A 42  ? 0.1743 0.1807 0.1488 -0.0072 0.0369  0.0147  42  TYR   A CZ  
1119 O OH  A TYR   A 42  ? 0.1551 0.1855 0.1520 0.0047  0.0304  0.0180  42  TYR   A OH  
1120 O OH  B TYR   A 42  ? 0.1803 0.1902 0.1710 -0.0020 0.0228  0.0027  42  TYR   A OH  
1139 N N   . LEU   A 43  ? 0.1379 0.1198 0.1309 -0.0048 0.0163  0.0094  43  LEU   A N   
1140 C CA  . LEU   A 43  ? 0.1262 0.1201 0.1315 -0.0062 0.0090  0.0099  43  LEU   A CA  
1141 C C   . LEU   A 43  ? 0.1294 0.1223 0.1220 -0.0046 0.0094  0.0065  43  LEU   A C   
1142 O O   . LEU   A 43  ? 0.1462 0.1248 0.1435 0.0044  -0.0020 0.0048  43  LEU   A O   
1143 C CB  . LEU   A 43  ? 0.1328 0.1157 0.1455 -0.0048 0.0049  0.0148  43  LEU   A CB  
1144 C CG  . LEU   A 43  ? 0.1428 0.1217 0.1536 0.0006  0.0105  0.0123  43  LEU   A CG  
1145 C CD1 . LEU   A 43  ? 0.1479 0.1336 0.1668 0.0008  0.0023  0.0184  43  LEU   A CD1 
1146 C CD2 . LEU   A 43  ? 0.1556 0.1203 0.1630 -0.0099 0.0053  0.0226  43  LEU   A CD2 
1159 N N   A LYS   A 44  ? 0.1425 0.1287 0.1355 -0.0062 0.0092  0.0104  44  LYS   A N   
1160 N N   B LYS   A 44  ? 0.1415 0.1256 0.1282 -0.0016 0.0102  0.0125  44  LYS   A N   
1161 C CA  A LYS   A 44  ? 0.1528 0.1329 0.1448 -0.0088 0.0114  0.0166  44  LYS   A CA  
1162 C CA  B LYS   A 44  ? 0.1506 0.1255 0.1248 0.0011  0.0148  0.0228  44  LYS   A CA  
1163 C C   A LYS   A 44  ? 0.1404 0.1290 0.1239 -0.0042 0.0028  0.0092  44  LYS   A C   
1164 C C   B LYS   A 44  ? 0.1391 0.1253 0.1063 0.0024  0.0031  0.0112  44  LYS   A C   
1165 O O   A LYS   A 44  ? 0.1468 0.1408 0.1344 -0.0053 0.0001  0.0023  44  LYS   A O   
1166 O O   B LYS   A 44  ? 0.1496 0.1425 0.1254 -0.0004 0.0001  0.0006  44  LYS   A O   
1167 C CB  A LYS   A 44  ? 0.1792 0.1480 0.1824 -0.0107 0.0193  0.0202  44  LYS   A CB  
1168 C CB  B LYS   A 44  ? 0.1772 0.1362 0.1563 0.0073  0.0259  0.0258  44  LYS   A CB  
1169 C CG  A LYS   A 44  ? 0.2053 0.1728 0.2322 -0.0162 0.0334  0.0297  44  LYS   A CG  
1170 C CG  B LYS   A 44  ? 0.2051 0.1666 0.2161 0.0054  0.0420  0.0334  44  LYS   A CG  
1171 C CD  A LYS   A 44  ? 0.2348 0.2064 0.3094 -0.0215 0.0348  0.0275  44  LYS   A CD  
1172 C CD  B LYS   A 44  ? 0.2410 0.2150 0.3247 0.0019  0.0371  0.0230  44  LYS   A CD  
1173 C CE  A LYS   A 44  ? 0.2542 0.2303 0.3581 -0.0260 0.0347  0.0309  44  LYS   A CE  
1174 C CE  B LYS   A 44  ? 0.2624 0.2456 0.3892 -0.0002 0.0332  0.0214  44  LYS   A CE  
1175 N NZ  A LYS   A 44  ? 0.2643 0.2458 0.3820 -0.0322 0.0343  0.0330  44  LYS   A NZ  
1176 N NZ  B LYS   A 44  ? 0.2711 0.2608 0.4131 -0.0039 0.0251  0.0236  44  LYS   A NZ  
1203 N N   . HIS   A 45  ? 0.1298 0.1203 0.1233 -0.0019 -0.0029 0.0081  45  HIS   A N   
1204 C CA  . HIS   A 45  ? 0.1267 0.1213 0.1349 -0.0007 -0.0033 0.0079  45  HIS   A CA  
1205 C C   . HIS   A 45  ? 0.1384 0.1307 0.1403 0.0057  -0.0001 0.0135  45  HIS   A C   
1206 O O   . HIS   A 45  ? 0.1549 0.1452 0.1789 0.0223  -0.0046 -0.0040 45  HIS   A O   
1207 C CB  . HIS   A 45  ? 0.1273 0.1216 0.1269 -0.0038 -0.0001 0.0055  45  HIS   A CB  
1208 C CG  . HIS   A 45  ? 0.1242 0.1212 0.1201 -0.0056 0.0048  0.0094  45  HIS   A CG  
1209 N ND1 . HIS   A 45  ? 0.1201 0.1284 0.1298 -0.0051 -0.0011 0.0150  45  HIS   A ND1 
1210 C CD2 . HIS   A 45  ? 0.1226 0.1306 0.1273 -0.0126 -0.0044 0.0148  45  HIS   A CD2 
1211 C CE1 . HIS   A 45  ? 0.1211 0.1317 0.1238 -0.0094 0.0001  0.0233  45  HIS   A CE1 
1212 N NE2 . HIS   A 45  ? 0.1226 0.1375 0.1214 -0.0050 0.0023  0.0198  45  HIS   A NE2 
1221 N N   A GLY   A 46  ? 0.1408 0.1453 0.1552 0.0214  -0.0001 0.0202  46  GLY   A N   
1222 N N   B GLY   A 46  ? 0.1524 0.1351 0.1530 0.0055  -0.0092 0.0198  46  GLY   A N   
1223 C CA  A GLY   A 46  ? 0.1405 0.1455 0.1637 0.0172  -0.0027 0.0308  46  GLY   A CA  
1224 C CA  B GLY   A 46  ? 0.1490 0.1400 0.1531 0.0028  -0.0100 0.0214  46  GLY   A CA  
1225 C C   A GLY   A 46  ? 0.1417 0.1407 0.1614 0.0198  -0.0062 0.0428  46  GLY   A C   
1226 C C   B GLY   A 46  ? 0.1454 0.1381 0.1438 0.0099  -0.0087 0.0325  46  GLY   A C   
1227 O O   A GLY   A 46  ? 0.1516 0.1413 0.1738 0.0221  -0.0028 0.0556  46  GLY   A O   
1228 O O   B GLY   A 46  ? 0.1555 0.1383 0.1637 0.0054  -0.0090 0.0214  46  GLY   A O   
1235 N N   A GLY   A 47  ? 0.1308 0.1368 0.1417 0.0214  -0.0080 0.0272  47  GLY   A N   
1236 N N   B GLY   A 47  ? 0.1492 0.1404 0.1512 0.0155  -0.0059 0.0207  47  GLY   A N   
1237 C CA  A GLY   A 47  ? 0.1346 0.1412 0.1442 0.0228  -0.0140 0.0174  47  GLY   A CA  
1238 C CA  B GLY   A 47  ? 0.1414 0.1480 0.1651 0.0105  -0.0150 0.0208  47  GLY   A CA  
1239 C C   A GLY   A 47  ? 0.1241 0.1433 0.1430 0.0224  -0.0091 0.0143  47  GLY   A C   
1240 C C   B GLY   A 47  ? 0.1331 0.1419 0.1326 0.0081  -0.0096 0.0114  47  GLY   A C   
1241 O O   A GLY   A 47  ? 0.1211 0.1408 0.1674 0.0225  -0.0079 0.0219  47  GLY   A O   
1242 O O   B GLY   A 47  ? 0.1313 0.1386 0.1408 0.0097  -0.0088 0.0184  47  GLY   A O   
1249 N N   A GLY   A 48  ? 0.1243 0.1502 0.1417 0.0214  -0.0062 0.0049  48  GLY   A N   
1250 N N   B GLY   A 48  ? 0.1322 0.1452 0.1413 0.0109  -0.0016 0.0101  48  GLY   A N   
1251 C CA  A GLY   A 48  ? 0.1263 0.1452 0.1408 0.0163  -0.0016 0.0002  48  GLY   A CA  
1252 C CA  B GLY   A 48  ? 0.1312 0.1347 0.1414 0.0034  0.0010  0.0099  48  GLY   A CA  
1253 C C   A GLY   A 48  ? 0.1311 0.1433 0.1360 0.0051  0.0059  0.0026  48  GLY   A C   
1254 C C   B GLY   A 48  ? 0.1294 0.1369 0.1414 0.0019  0.0040  0.0120  48  GLY   A C   
1255 O O   A GLY   A 48  ? 0.1435 0.1426 0.1294 -0.0002 0.0034  0.0119  48  GLY   A O   
1256 O O   B GLY   A 48  ? 0.1446 0.1443 0.1382 0.0061  0.0026  0.0025  48  GLY   A O   
1263 N N   A VAL   A 49  ? 0.1317 0.1407 0.1372 -0.0001 0.0004  0.0010  49  VAL   A N   
1264 N N   B VAL   A 49  ? 0.1218 0.1311 0.1310 0.0003  -0.0088 0.0042  49  VAL   A N   
1265 C CA  A VAL   A 49  ? 0.1371 0.1330 0.1402 -0.0046 0.0039  0.0065  49  VAL   A CA  
1266 C CA  B VAL   A 49  ? 0.1228 0.1364 0.1367 -0.0035 0.0001  0.0056  49  VAL   A CA  
1267 C C   A VAL   A 49  ? 0.1331 0.1235 0.1392 -0.0105 0.0002  0.0254  49  VAL   A C   
1268 C C   B VAL   A 49  ? 0.1227 0.1298 0.1189 0.0034  0.0009  -0.0070 49  VAL   A C   
1269 O O   A VAL   A 49  ? 0.1326 0.1279 0.1571 -0.0169 -0.0051 0.0146  49  VAL   A O   
1270 O O   B VAL   A 49  ? 0.1303 0.1368 0.1002 0.0035  0.0134  -0.0031 49  VAL   A O   
1271 C CB  A VAL   A 49  ? 0.1447 0.1353 0.1545 -0.0048 -0.0002 -0.0112 49  VAL   A CB  
1272 C CB  B VAL   A 49  ? 0.1180 0.1338 0.1488 -0.0048 -0.0081 0.0062  49  VAL   A CB  
1273 C CG1 A VAL   A 49  ? 0.1402 0.1294 0.1629 -0.0042 -0.0008 -0.0195 49  VAL   A CG1 
1274 C CG1 B VAL   A 49  ? 0.1159 0.1304 0.1433 0.0031  -0.0001 0.0070  49  VAL   A CG1 
1275 C CG2 A VAL   A 49  ? 0.1547 0.1390 0.1826 -0.0152 -0.0025 -0.0114 49  VAL   A CG2 
1276 C CG2 B VAL   A 49  ? 0.1239 0.1373 0.1815 -0.0107 -0.0154 0.0123  49  VAL   A CG2 
1295 N N   A ALA   A 50  ? 0.1302 0.1227 0.1267 -0.0152 -0.0117 0.0250  50  ALA   A N   
1296 N N   B ALA   A 50  ? 0.1253 0.1244 0.1158 0.0065  -0.0043 -0.0110 50  ALA   A N   
1297 C CA  A ALA   A 50  ? 0.1236 0.1186 0.1228 -0.0185 -0.0164 0.0248  50  ALA   A CA  
1298 C CA  B ALA   A 50  ? 0.1191 0.1181 0.1153 0.0064  -0.0027 -0.0025 50  ALA   A CA  
1299 C C   A ALA   A 50  ? 0.1217 0.1240 0.1315 -0.0159 -0.0099 0.0150  50  ALA   A C   
1300 C C   B ALA   A 50  ? 0.1202 0.1228 0.1042 0.0054  0.0049  -0.0083 50  ALA   A C   
1301 O O   A ALA   A 50  ? 0.1212 0.1234 0.1403 -0.0136 -0.0084 0.0151  50  ALA   A O   
1302 O O   B ALA   A 50  ? 0.1237 0.1299 0.1053 0.0055  0.0042  -0.0023 50  ALA   A O   
1303 C CB  A ALA   A 50  ? 0.1246 0.1205 0.1276 -0.0157 -0.0182 0.0214  50  ALA   A CB  
1304 C CB  B ALA   A 50  ? 0.1219 0.1135 0.1145 0.0096  0.0083  -0.0093 50  ALA   A CB  
1315 N N   A GLY   A 51  ? 0.1271 0.1241 0.1283 -0.0059 -0.0110 0.0133  51  GLY   A N   
1316 N N   B GLY   A 51  ? 0.1286 0.1175 0.1272 0.0114  -0.0048 -0.0037 51  GLY   A N   
1317 C CA  A GLY   A 51  ? 0.1330 0.1257 0.1275 -0.0057 -0.0124 0.0113  51  GLY   A CA  
1318 C CA  B GLY   A 51  ? 0.1445 0.1175 0.1180 0.0110  -0.0164 -0.0001 51  GLY   A CA  
1319 C C   A GLY   A 51  ? 0.1237 0.1259 0.1190 -0.0053 -0.0048 0.0059  51  GLY   A C   
1320 C C   B GLY   A 51  ? 0.1318 0.1223 0.1187 0.0134  -0.0067 -0.0018 51  GLY   A C   
1321 O O   A GLY   A 51  ? 0.1281 0.1326 0.1129 -0.0079 -0.0009 -0.0012 51  GLY   A O   
1322 O O   B GLY   A 51  ? 0.1350 0.1304 0.1237 0.0112  -0.0004 -0.0022 51  GLY   A O   
1329 N N   A ALA   A 52  ? 0.1208 0.1305 0.1324 -0.0058 -0.0035 0.0019  52  ALA   A N   
1330 N N   B ALA   A 52  ? 0.1327 0.1334 0.1212 0.0064  0.0009  -0.0078 52  ALA   A N   
1331 C CA  A ALA   A 52  ? 0.1211 0.1287 0.1295 -0.0055 -0.0053 0.0102  52  ALA   A CA  
1332 C CA  B ALA   A 52  ? 0.1270 0.1335 0.1423 0.0047  0.0029  -0.0012 52  ALA   A CA  
1333 C C   A ALA   A 52  ? 0.1225 0.1260 0.1201 -0.0153 -0.0045 0.0036  52  ALA   A C   
1334 C C   B ALA   A 52  ? 0.1179 0.1333 0.1277 -0.0074 0.0088  -0.0009 52  ALA   A C   
1335 O O   A ALA   A 52  ? 0.1324 0.1355 0.1351 -0.0169 -0.0070 -0.0060 52  ALA   A O   
1336 O O   B ALA   A 52  ? 0.1279 0.1457 0.1373 -0.0007 0.0159  0.0013  52  ALA   A O   
1337 C CB  A ALA   A 52  ? 0.1224 0.1351 0.1297 -0.0023 -0.0079 0.0180  52  ALA   A CB  
1338 C CB  B ALA   A 52  ? 0.1272 0.1493 0.1761 0.0030  -0.0054 0.0041  52  ALA   A CB  
1349 N N   A LEU   A 53  ? 0.1225 0.1274 0.1159 -0.0145 -0.0092 0.0119  53  LEU   A N   
1350 N N   B LEU   A 53  ? 0.1142 0.1354 0.1242 0.0005  0.0086  0.0006  53  LEU   A N   
1351 C CA  A LEU   A 53  ? 0.1254 0.1351 0.1276 -0.0178 -0.0041 0.0080  53  LEU   A CA  
1352 C CA  B LEU   A 53  ? 0.1157 0.1396 0.1123 0.0012  0.0080  -0.0057 53  LEU   A CA  
1353 C C   A LEU   A 53  ? 0.1320 0.1381 0.1270 -0.0176 -0.0017 0.0089  53  LEU   A C   
1354 C C   B LEU   A 53  ? 0.1280 0.1444 0.1031 0.0136  0.0043  -0.0096 53  LEU   A C   
1355 O O   A LEU   A 53  ? 0.1396 0.1431 0.1304 -0.0305 -0.0030 0.0050  53  LEU   A O   
1356 O O   B LEU   A 53  ? 0.1404 0.1519 0.1137 0.0026  0.0007  -0.0026 53  LEU   A O   
1357 C CB  A LEU   A 53  ? 0.1303 0.1426 0.1495 -0.0117 -0.0046 0.0171  53  LEU   A CB  
1358 C CB  B LEU   A 53  ? 0.1130 0.1403 0.0968 -0.0059 -0.0055 -0.0056 53  LEU   A CB  
1359 C CG  A LEU   A 53  ? 0.1304 0.1450 0.1532 -0.0070 0.0006  0.0218  53  LEU   A CG  
1360 C CG  B LEU   A 53  ? 0.1210 0.1415 0.1110 -0.0041 -0.0064 0.0003  53  LEU   A CG  
1361 C CD1 A LEU   A 53  ? 0.1255 0.1516 0.1443 -0.0022 0.0102  0.0192  53  LEU   A CD1 
1362 C CD1 B LEU   A 53  ? 0.1279 0.1514 0.1176 -0.0082 0.0039  -0.0059 53  LEU   A CD1 
1363 C CD2 A LEU   A 53  ? 0.1406 0.1537 0.1606 -0.0025 0.0006  0.0319  53  LEU   A CD2 
1364 C CD2 B LEU   A 53  ? 0.1293 0.1488 0.1272 -0.0038 -0.0013 0.0063  53  LEU   A CD2 
1387 N N   A ASN   A 54  ? 0.1261 0.1307 0.1267 -0.0228 -0.0028 0.0152  54  ASN   A N   
1388 N N   B ASN   A 54  ? 0.1249 0.1361 0.1084 0.0103  -0.0002 -0.0044 54  ASN   A N   
1389 C CA  A ASN   A 54  ? 0.1230 0.1270 0.1386 -0.0245 -0.0061 0.0097  54  ASN   A CA  
1390 C CA  B ASN   A 54  ? 0.1202 0.1351 0.1117 0.0055  -0.0081 -0.0060 54  ASN   A CA  
1391 C C   A ASN   A 54  ? 0.1261 0.1312 0.1438 -0.0245 -0.0035 0.0116  54  ASN   A C   
1392 C C   B ASN   A 54  ? 0.1321 0.1367 0.1041 -0.0001 0.0050  -0.0039 54  ASN   A C   
1393 O O   A ASN   A 54  ? 0.1297 0.1347 0.1464 -0.0257 -0.0122 0.0097  54  ASN   A O   
1394 O O   B ASN   A 54  ? 0.1354 0.1345 0.0959 0.0062  0.0093  -0.0123 54  ASN   A O   
1395 C CB  A ASN   A 54  ? 0.1238 0.1223 0.1413 -0.0248 -0.0054 0.0059  54  ASN   A CB  
1396 C CB  B ASN   A 54  ? 0.1138 0.1350 0.1104 0.0118  -0.0152 -0.0023 54  ASN   A CB  
1397 C CG  A ASN   A 54  ? 0.1292 0.1220 0.1511 -0.0213 -0.0005 0.0092  54  ASN   A CG  
1398 C CG  B ASN   A 54  ? 0.1134 0.1350 0.1081 0.0103  -0.0003 -0.0095 54  ASN   A CG  
1399 O OD1 A ASN   A 54  ? 0.1325 0.1248 0.1627 -0.0197 -0.0038 0.0269  54  ASN   A OD1 
1400 O OD1 B ASN   A 54  ? 0.1136 0.1348 0.1132 0.0085  -0.0058 -0.0193 54  ASN   A OD1 
1401 N ND2 A ASN   A 54  ? 0.1312 0.1232 0.1656 -0.0193 -0.0083 0.0074  54  ASN   A ND2 
1402 N ND2 B ASN   A 54  ? 0.1238 0.1374 0.1293 0.0067  -0.0090 0.0005  54  ASN   A ND2 
1415 N N   A LYS   A 55  ? 0.1232 0.1327 0.1497 -0.0135 -0.0036 0.0034  55  LYS   A N   
1416 N N   B LYS   A 55  ? 0.1321 0.1365 0.1334 0.0063  0.0011  -0.0114 55  LYS   A N   
1417 C CA  A LYS   A 55  ? 0.1256 0.1369 0.1429 -0.0026 -0.0050 -0.0125 55  LYS   A CA  
1418 C CA  B LYS   A 55  ? 0.1427 0.1480 0.1412 0.0197  -0.0028 -0.0155 55  LYS   A CA  
1419 C C   A LYS   A 55  ? 0.1297 0.1431 0.1507 -0.0035 0.0007  -0.0219 55  LYS   A C   
1420 C C   B LYS   A 55  ? 0.1367 0.1495 0.1454 0.0073  0.0016  -0.0241 55  LYS   A C   
1421 O O   A LYS   A 55  ? 0.1372 0.1502 0.1647 -0.0015 0.0005  -0.0238 55  LYS   A O   
1422 O O   B LYS   A 55  ? 0.1454 0.1614 0.1492 0.0070  0.0039  -0.0258 55  LYS   A O   
1423 C CB  A LYS   A 55  ? 0.1211 0.1444 0.1405 0.0087  -0.0107 -0.0215 55  LYS   A CB  
1424 C CB  B LYS   A 55  ? 0.1523 0.1669 0.1720 0.0254  -0.0021 -0.0093 55  LYS   A CB  
1425 C CG  A LYS   A 55  ? 0.1312 0.1643 0.1458 0.0188  -0.0120 -0.0250 55  LYS   A CG  
1426 C CG  B LYS   A 55  ? 0.1812 0.2054 0.2202 0.0272  -0.0131 -0.0122 55  LYS   A CG  
1427 C CD  A LYS   A 55  ? 0.1285 0.1723 0.1486 0.0280  -0.0091 -0.0227 55  LYS   A CD  
1428 C CD  B LYS   A 55  ? 0.2077 0.2350 0.2710 0.0254  -0.0099 -0.0045 55  LYS   A CD  
1429 C CE  A LYS   A 55  ? 0.1380 0.1839 0.1500 0.0470  -0.0246 -0.0207 55  LYS   A CE  
1430 C CE  B LYS   A 55  ? 0.2328 0.2676 0.3131 0.0136  -0.0266 0.0027  55  LYS   A CE  
1431 N NZ  A LYS   A 55  ? 0.1460 0.1860 0.1507 0.0588  -0.0306 -0.0194 55  LYS   A NZ  
1432 N NZ  B LYS   A 55  ? 0.2440 0.2820 0.3341 0.0062  -0.0407 0.0010  55  LYS   A NZ  
1459 N N   . ALA   A 56  ? 0.1373 0.1552 0.1538 -0.0069 0.0055  -0.0233 56  ALA   A N   
1460 C CA  . ALA   A 56  ? 0.1467 0.1716 0.1382 -0.0072 0.0144  -0.0191 56  ALA   A CA  
1461 C C   . ALA   A 56  ? 0.1550 0.1823 0.1221 -0.0099 0.0066  -0.0252 56  ALA   A C   
1462 O O   . ALA   A 56  ? 0.1607 0.2178 0.1362 0.0013  0.0213  -0.0221 56  ALA   A O   
1463 C CB  . ALA   A 56  ? 0.1571 0.1893 0.1542 -0.0164 0.0163  -0.0080 56  ALA   A CB  
1470 N N   . THR   A 57  ? 0.1425 0.1666 0.1211 -0.0112 0.0154  -0.0190 57  THR   A N   
1471 C CA  . THR   A 57  ? 0.1474 0.1680 0.1110 -0.0157 0.0042  -0.0125 57  THR   A CA  
1472 C C   . THR   A 57  ? 0.1467 0.1722 0.1214 -0.0069 0.0010  -0.0184 57  THR   A C   
1473 O O   . THR   A 57  ? 0.1454 0.1737 0.1454 -0.0139 -0.0071 -0.0257 57  THR   A O   
1474 C CB  . THR   A 57  ? 0.1436 0.1627 0.1260 -0.0090 -0.0012 -0.0134 57  THR   A CB  
1475 O OG1 . THR   A 57  ? 0.1327 0.1565 0.1222 -0.0086 0.0048  -0.0116 57  THR   A OG1 
1476 C CG2 . THR   A 57  ? 0.1477 0.1696 0.1195 -0.0078 0.0015  -0.0028 57  THR   A CG2 
1484 N N   . ASN   A 58  ? 0.1482 0.1655 0.1498 -0.0071 0.0030  -0.0281 58  ASN   A N   
1485 C CA  . ASN   A 58  ? 0.1662 0.1572 0.1685 -0.0131 0.0110  -0.0410 58  ASN   A CA  
1486 C C   . ASN   A 58  ? 0.1398 0.1459 0.1580 -0.0024 -0.0049 -0.0213 58  ASN   A C   
1487 O O   . ASN   A 58  ? 0.1473 0.1603 0.1709 -0.0179 -0.0041 -0.0288 58  ASN   A O   
1488 C CB  . ASN   A 58  ? 0.2077 0.1765 0.2006 -0.0168 0.0337  -0.0501 58  ASN   A CB  
1489 C CG  . ASN   A 58  ? 0.2500 0.1996 0.2644 -0.0170 0.0265  -0.0375 58  ASN   A CG  
1490 O OD1 . ASN   A 58  ? 0.2766 0.2003 0.3038 0.0138  0.0558  -0.0296 58  ASN   A OD1 
1491 N ND2 . ASN   A 58  ? 0.2601 0.2138 0.2863 -0.0182 0.0075  -0.0452 58  ASN   A ND2 
1498 N N   . ASN   A 59  ? 0.1258 0.1395 0.1518 -0.0082 -0.0076 -0.0156 59  ASN   A N   
1499 C CA  . ASN   A 59  ? 0.1301 0.1287 0.1463 -0.0045 -0.0078 -0.0072 59  ASN   A CA  
1500 C C   . ASN   A 59  ? 0.1318 0.1339 0.1358 -0.0053 -0.0107 -0.0075 59  ASN   A C   
1501 O O   . ASN   A 59  ? 0.1311 0.1354 0.1436 -0.0079 -0.0011 0.0032  59  ASN   A O   
1502 C CB  . ASN   A 59  ? 0.1392 0.1304 0.1467 -0.0033 -0.0206 -0.0149 59  ASN   A CB  
1503 C CG  . ASN   A 59  ? 0.1418 0.1301 0.1576 -0.0034 -0.0256 0.0055  59  ASN   A CG  
1504 O OD1 . ASN   A 59  ? 0.1496 0.1394 0.1447 -0.0117 -0.0207 0.0052  59  ASN   A OD1 
1505 N ND2 . ASN   A 59  ? 0.1503 0.1357 0.1632 -0.0149 -0.0168 0.0068  59  ASN   A ND2 
1512 N N   . ALA   A 60  ? 0.1261 0.1389 0.1425 -0.0072 -0.0029 -0.0080 60  ALA   A N   
1513 C CA  . ALA   A 60  ? 0.1250 0.1394 0.1408 -0.0008 -0.0078 -0.0099 60  ALA   A CA  
1514 C C   . ALA   A 60  ? 0.1288 0.1331 0.1330 -0.0036 -0.0022 -0.0007 60  ALA   A C   
1515 O O   . ALA   A 60  ? 0.1260 0.1347 0.1597 -0.0019 -0.0100 -0.0082 60  ALA   A O   
1516 C CB  . ALA   A 60  ? 0.1408 0.1551 0.1457 -0.0056 -0.0124 -0.0290 60  ALA   A CB  
1522 N N   . MET   A 61  ? 0.1213 0.1309 0.1402 -0.0082 -0.0010 -0.0069 61  MET   A N   
1523 C CA  . MET   A 61  ? 0.1255 0.1267 0.1376 -0.0072 0.0065  -0.0024 61  MET   A CA  
1524 C C   . MET   A 61  ? 0.1186 0.1257 0.1375 -0.0065 -0.0051 -0.0018 61  MET   A C   
1525 O O   . MET   A 61  ? 0.1220 0.1245 0.1443 -0.0046 0.0019  0.0042  61  MET   A O   
1526 C CB  . MET   A 61  ? 0.1273 0.1294 0.1251 -0.0073 -0.0003 -0.0066 61  MET   A CB  
1527 C CG  . MET   A 61  ? 0.1314 0.1384 0.1343 -0.0060 0.0041  -0.0037 61  MET   A CG  
1528 S SD  . MET   A 61  ? 0.1317 0.1389 0.1758 -0.0111 0.0008  -0.0178 61  MET   A SD  
1529 C CE  . MET   A 61  ? 0.1508 0.1518 0.1942 -0.0222 0.0219  -0.0076 61  MET   A CE  
1539 N N   . GLN   A 62  ? 0.1229 0.1260 0.1327 -0.0069 -0.0013 -0.0022 62  GLN   A N   
1540 C CA  . GLN   A 62  ? 0.1237 0.1225 0.1374 -0.0088 0.0028  -0.0002 62  GLN   A CA  
1541 C C   . GLN   A 62  ? 0.1277 0.1130 0.1414 -0.0033 0.0021  0.0007  62  GLN   A C   
1542 O O   . GLN   A 62  ? 0.1297 0.1290 0.1379 -0.0037 0.0046  -0.0028 62  GLN   A O   
1543 C CB  . GLN   A 62  ? 0.1253 0.1186 0.1435 -0.0015 -0.0023 -0.0010 62  GLN   A CB  
1544 C CG  . GLN   A 62  ? 0.1333 0.1178 0.1356 -0.0020 -0.0022 0.0136  62  GLN   A CG  
1545 C CD  . GLN   A 62  ? 0.1368 0.1217 0.1310 -0.0019 0.0077  0.0133  62  GLN   A CD  
1546 O OE1 . GLN   A 62  ? 0.1408 0.1319 0.1463 -0.0027 -0.0019 0.0044  62  GLN   A OE1 
1547 N NE2 . GLN   A 62  ? 0.1464 0.1320 0.1469 -0.0011 0.0015  0.0007  62  GLN   A NE2 
1556 N N   . VAL   A 63  ? 0.1226 0.1238 0.1596 -0.0065 0.0129  -0.0130 63  VAL   A N   
1557 C CA  . VAL   A 63  ? 0.1281 0.1359 0.1782 -0.0174 0.0024  -0.0173 63  VAL   A CA  
1558 C C   . VAL   A 63  ? 0.1177 0.1337 0.1671 -0.0144 -0.0037 -0.0105 63  VAL   A C   
1559 O O   . VAL   A 63  ? 0.1189 0.1332 0.1784 -0.0140 0.0040  -0.0046 63  VAL   A O   
1560 C CB  . VAL   A 63  ? 0.1378 0.1545 0.2146 -0.0131 -0.0032 -0.0387 63  VAL   A CB  
1561 C CG1 . VAL   A 63  ? 0.1513 0.1728 0.2550 -0.0139 -0.0092 -0.0641 63  VAL   A CG1 
1562 C CG2 . VAL   A 63  ? 0.1446 0.1444 0.2283 -0.0086 0.0112  -0.0285 63  VAL   A CG2 
1572 N N   . GLU   A 64  ? 0.1179 0.1430 0.1531 -0.0043 -0.0021 -0.0061 64  GLU   A N   
1573 C CA  . GLU   A 64  ? 0.1203 0.1407 0.1506 -0.0048 -0.0003 0.0035  64  GLU   A CA  
1574 C C   . GLU   A 64  ? 0.1170 0.1346 0.1538 -0.0075 -0.0020 0.0095  64  GLU   A C   
1575 O O   . GLU   A 64  ? 0.1209 0.1409 0.1650 0.0005  0.0037  -0.0025 64  GLU   A O   
1576 C CB  . GLU   A 64  ? 0.1286 0.1452 0.1580 -0.0094 0.0027  -0.0058 64  GLU   A CB  
1577 C CG  . GLU   A 64  ? 0.1426 0.1558 0.1631 -0.0161 0.0065  0.0010  64  GLU   A CG  
1578 C CD  . GLU   A 64  ? 0.1600 0.1587 0.1596 -0.0199 0.0136  -0.0005 64  GLU   A CD  
1579 O OE1 . GLU   A 64  ? 0.1523 0.1709 0.1892 -0.0213 0.0160  0.0031  64  GLU   A OE1 
1580 O OE2 . GLU   A 64  ? 0.1755 0.1565 0.1620 -0.0269 -0.0006 0.0126  64  GLU   A OE2 
1587 N N   . SER   A 65  ? 0.1154 0.1346 0.1408 -0.0016 0.0030  0.0032  65  SER   A N   
1588 C CA  . SER   A 65  ? 0.1241 0.1251 0.1360 -0.0046 -0.0037 -0.0002 65  SER   A CA  
1589 C C   . SER   A 65  ? 0.1263 0.1330 0.1325 -0.0053 0.0010  -0.0004 65  SER   A C   
1590 O O   . SER   A 65  ? 0.1365 0.1361 0.1571 -0.0019 0.0161  -0.0004 65  SER   A O   
1591 C CB  . SER   A 65  ? 0.1270 0.1207 0.1462 -0.0050 0.0108  0.0061  65  SER   A CB  
1592 O OG  . SER   A 65  ? 0.1222 0.1377 0.1551 -0.0107 -0.0002 0.0145  65  SER   A OG  
1598 N N   . ASP   A 66  ? 0.1281 0.1313 0.1437 -0.0039 0.0134  0.0064  66  ASP   A N   
1599 C CA  . ASP   A 66  ? 0.1375 0.1398 0.1543 -0.0050 0.0108  0.0146  66  ASP   A CA  
1600 C C   . ASP   A 66  ? 0.1287 0.1319 0.1632 -0.0075 0.0121  0.0154  66  ASP   A C   
1601 O O   . ASP   A 66  ? 0.1352 0.1461 0.1865 -0.0072 0.0260  0.0181  66  ASP   A O   
1602 C CB  . ASP   A 66  ? 0.1446 0.1488 0.1830 0.0044  0.0142  0.0323  66  ASP   A CB  
1603 C CG  . ASP   A 66  ? 0.1623 0.1625 0.2158 -0.0000 0.0021  0.0481  66  ASP   A CG  
1604 O OD1 . ASP   A 66  ? 0.1638 0.1922 0.1953 -0.0094 -0.0094 0.0519  66  ASP   A OD1 
1605 O OD2 . ASP   A 66  ? 0.1730 0.1689 0.2906 0.0151  -0.0076 0.0310  66  ASP   A OD2 
1610 N N   . ASP   A 67  ? 0.1230 0.1384 0.1781 -0.0059 0.0163  0.0170  67  ASP   A N   
1611 C CA  . ASP   A 67  ? 0.1315 0.1530 0.1921 -0.0020 0.0082  0.0279  67  ASP   A CA  
1612 C C   . ASP   A 67  ? 0.1305 0.1536 0.1798 0.0030  0.0120  0.0283  67  ASP   A C   
1613 O O   . ASP   A 67  ? 0.1250 0.1645 0.2037 0.0034  0.0257  0.0304  67  ASP   A O   
1614 C CB  . ASP   A 67  ? 0.1422 0.1561 0.2188 -0.0046 -0.0069 0.0306  67  ASP   A CB  
1615 C CG  . ASP   A 67  ? 0.1369 0.1725 0.2565 -0.0132 -0.0219 0.0277  67  ASP   A CG  
1616 O OD1 . ASP   A 67  ? 0.1398 0.1897 0.3377 -0.0165 -0.0290 0.0385  67  ASP   A OD1 
1617 O OD2 . ASP   A 67  ? 0.1404 0.1792 0.2303 0.0005  -0.0108 0.0191  67  ASP   A OD2 
1622 N N   A TYR   A 68  ? 0.1291 0.1424 0.1781 0.0025  0.0238  0.0271  68  TYR   A N   
1623 N N   B TYR   A 68  ? 0.1308 0.1432 0.1828 0.0052  0.0203  0.0376  68  TYR   A N   
1624 C CA  A TYR   A 68  ? 0.1370 0.1367 0.1648 0.0033  0.0283  0.0204  68  TYR   A CA  
1625 C CA  B TYR   A 68  ? 0.1455 0.1419 0.1718 0.0080  0.0150  0.0384  68  TYR   A CA  
1626 C C   A TYR   A 68  ? 0.1297 0.1372 0.1619 -0.0015 0.0239  0.0194  68  TYR   A C   
1627 C C   B TYR   A 68  ? 0.1330 0.1404 0.1683 0.0027  0.0196  0.0234  68  TYR   A C   
1628 O O   A TYR   A 68  ? 0.1342 0.1420 0.1684 0.0028  0.0296  0.0219  68  TYR   A O   
1629 O O   B TYR   A 68  ? 0.1400 0.1467 0.1826 0.0133  0.0304  0.0218  68  TYR   A O   
1630 C CB  A TYR   A 68  ? 0.1374 0.1284 0.1665 0.0067  0.0513  0.0034  68  TYR   A CB  
1631 C CB  B TYR   A 68  ? 0.1533 0.1425 0.1836 0.0114  0.0209  0.0394  68  TYR   A CB  
1632 C CG  A TYR   A 68  ? 0.1374 0.1354 0.1915 -0.0011 0.0731  0.0033  68  TYR   A CG  
1633 C CG  B TYR   A 68  ? 0.1612 0.1566 0.2066 0.0078  0.0240  0.0487  68  TYR   A CG  
1634 C CD1 A TYR   A 68  ? 0.1384 0.1410 0.2200 -0.0243 0.0618  -0.0142 68  TYR   A CD1 
1635 C CD1 B TYR   A 68  ? 0.1693 0.1642 0.2171 -0.0016 0.0110  0.0366  68  TYR   A CD1 
1636 C CD2 A TYR   A 68  ? 0.1514 0.1378 0.2243 0.0022  0.0751  0.0007  68  TYR   A CD2 
1637 C CD2 B TYR   A 68  ? 0.1748 0.1608 0.2237 0.0080  0.0141  0.0553  68  TYR   A CD2 
1638 C CE1 A TYR   A 68  ? 0.1469 0.1535 0.2623 -0.0267 0.0613  -0.0320 68  TYR   A CE1 
1639 C CE1 B TYR   A 68  ? 0.1787 0.1635 0.2085 0.0020  0.0099  0.0590  68  TYR   A CE1 
1640 C CE2 A TYR   A 68  ? 0.1483 0.1457 0.2538 -0.0028 0.0782  -0.0155 68  TYR   A CE2 
1641 C CE2 B TYR   A 68  ? 0.1718 0.1677 0.1979 0.0039  0.0075  0.0453  68  TYR   A CE2 
1642 C CZ  A TYR   A 68  ? 0.1455 0.1509 0.2829 -0.0186 0.0625  -0.0460 68  TYR   A CZ  
1643 C CZ  B TYR   A 68  ? 0.1790 0.1617 0.1873 0.0020  0.0099  0.0545  68  TYR   A CZ  
1644 O OH  A TYR   A 68  ? 0.1582 0.1558 0.3284 -0.0123 0.0368  -0.0707 68  TYR   A OH  
1645 O OH  B TYR   A 68  ? 0.2026 0.1575 0.1905 0.0048  -0.0071 0.0514  68  TYR   A OH  
1664 N N   . ILE   A 69  ? 0.1287 0.1335 0.1679 -0.0029 0.0187  0.0218  69  ILE   A N   
1665 C CA  . ILE   A 69  ? 0.1344 0.1347 0.1637 0.0057  0.0158  0.0120  69  ILE   A CA  
1666 C C   . ILE   A 69  ? 0.1405 0.1404 0.1581 0.0071  0.0231  0.0205  69  ILE   A C   
1667 O O   . ILE   A 69  ? 0.1453 0.1486 0.1566 0.0018  0.0259  0.0164  69  ILE   A O   
1668 C CB  . ILE   A 69  ? 0.1435 0.1566 0.1651 0.0033  0.0126  0.0016  69  ILE   A CB  
1669 C CG1 . ILE   A 69  ? 0.1474 0.1631 0.1741 0.0064  0.0139  -0.0120 69  ILE   A CG1 
1670 C CG2 . ILE   A 69  ? 0.1641 0.1797 0.1784 0.0100  0.0068  -0.0037 69  ILE   A CG2 
1671 C CD1 . ILE   A 69  ? 0.1485 0.1740 0.1797 -0.0042 0.0126  -0.0193 69  ILE   A CD1 
1684 N N   . ALA   A 70  ? 0.1435 0.1409 0.1585 -0.0039 0.0244  0.0221  70  ALA   A N   
1685 C CA  . ALA   A 70  ? 0.1459 0.1531 0.1841 -0.0125 0.0352  0.0227  70  ALA   A CA  
1686 C C   . ALA   A 70  ? 0.1447 0.1677 0.1867 -0.0105 0.0365  0.0207  70  ALA   A C   
1687 O O   . ALA   A 70  ? 0.1642 0.1993 0.2064 0.0045  0.0556  0.0428  70  ALA   A O   
1688 C CB  . ALA   A 70  ? 0.1499 0.1498 0.2126 -0.0111 0.0281  0.0207  70  ALA   A CB  
1694 N N   . THR   A 71  ? 0.1352 0.1653 0.1706 -0.0040 0.0220  0.0251  71  THR   A N   
1695 C CA  . THR   A 71  ? 0.1433 0.1836 0.1957 0.0079  0.0253  0.0269  71  THR   A CA  
1696 C C   . THR   A 71  ? 0.1371 0.1731 0.2234 0.0150  0.0354  0.0236  71  THR   A C   
1697 O O   . THR   A 71  ? 0.1425 0.1999 0.2784 0.0119  0.0438  0.0025  71  THR   A O   
1698 C CB  . THR   A 71  ? 0.1697 0.2075 0.2217 0.0187  -0.0089 0.0360  71  THR   A CB  
1699 O OG1 . THR   A 71  ? 0.2017 0.2263 0.2229 0.0056  -0.0284 0.0320  71  THR   A OG1 
1700 C CG2 . THR   A 71  ? 0.1850 0.2216 0.2561 0.0287  -0.0134 0.0509  71  THR   A CG2 
1708 N N   . ASN   A 72  ? 0.1438 0.1564 0.1976 0.0147  0.0302  0.0219  72  ASN   A N   
1709 C CA  . ASN   A 72  ? 0.1503 0.1570 0.1982 0.0126  0.0350  0.0219  72  ASN   A CA  
1710 C C   . ASN   A 72  ? 0.1602 0.1523 0.1910 0.0115  0.0524  0.0141  72  ASN   A C   
1711 O O   . ASN   A 72  ? 0.1782 0.1546 0.2250 0.0159  0.0409  0.0022  72  ASN   A O   
1712 C CB  . ASN   A 72  ? 0.1644 0.1635 0.2008 0.0125  0.0403  0.0260  72  ASN   A CB  
1713 C CG  . ASN   A 72  ? 0.1937 0.1795 0.2028 0.0182  0.0361  0.0320  72  ASN   A CG  
1714 O OD1 . ASN   A 72  ? 0.2035 0.2105 0.2230 0.0190  0.0409  0.0251  72  ASN   A OD1 
1715 N ND2 . ASN   A 72  ? 0.2121 0.1766 0.2083 0.0494  0.0160  0.0218  72  ASN   A ND2 
1722 N N   . GLY   A 73  ? 0.1610 0.1507 0.1805 0.0088  0.0440  0.0119  73  GLY   A N   
1723 C CA  . GLY   A 73  ? 0.1641 0.1490 0.1703 0.0014  0.0429  0.0146  73  GLY   A CA  
1724 C C   . GLY   A 73  ? 0.1632 0.1382 0.1640 0.0040  0.0511  0.0247  73  GLY   A C   
1725 O O   . GLY   A 73  ? 0.1676 0.1455 0.1804 0.0117  0.0452  0.0321  73  GLY   A O   
1729 N N   . PRO   A 74  ? 0.1717 0.1457 0.1628 -0.0068 0.0453  0.0154  74  PRO   A N   
1730 C CA  . PRO   A 74  ? 0.1646 0.1425 0.1709 -0.0024 0.0408  0.0167  74  PRO   A CA  
1731 C C   . PRO   A 74  ? 0.1568 0.1301 0.1643 -0.0028 0.0307  -0.0005 74  PRO   A C   
1732 O O   . PRO   A 74  ? 0.1702 0.1340 0.1884 0.0042  0.0340  0.0012  74  PRO   A O   
1733 C CB  . PRO   A 74  ? 0.1833 0.1672 0.1876 0.0033  0.0449  0.0259  74  PRO   A CB  
1734 C CG  . PRO   A 74  ? 0.2085 0.1997 0.2321 -0.0176 0.0362  0.0181  74  PRO   A CG  
1735 C CD  . PRO   A 74  ? 0.1932 0.1841 0.1727 -0.0207 0.0395  0.0096  74  PRO   A CD  
1743 N N   . LEU   A 75  ? 0.1597 0.1220 0.1522 0.0010  0.0201  0.0043  75  LEU   A N   
1744 C CA  . LEU   A 75  ? 0.1650 0.1211 0.1402 0.0012  0.0081  0.0068  75  LEU   A CA  
1745 C C   . LEU   A 75  ? 0.1785 0.1358 0.1404 0.0064  0.0146  0.0127  75  LEU   A C   
1746 O O   . LEU   A 75  ? 0.2189 0.1488 0.1452 0.0113  0.0102  0.0038  75  LEU   A O   
1747 C CB  . LEU   A 75  ? 0.1709 0.1305 0.1328 -0.0074 0.0130  0.0199  75  LEU   A CB  
1748 C CG  . LEU   A 75  ? 0.1817 0.1598 0.1418 -0.0316 0.0080  0.0182  75  LEU   A CG  
1749 C CD1 . LEU   A 75  ? 0.1914 0.2100 0.1622 -0.0282 0.0016  -0.0000 75  LEU   A CD1 
1750 C CD2 . LEU   A 75  ? 0.2050 0.1976 0.2062 -0.0127 0.0058  0.0100  75  LEU   A CD2 
1762 N N   . LYS   A 76  ? 0.1816 0.1359 0.1480 -0.0065 0.0151  0.0009  76  LYS   A N   
1763 C CA  . LYS   A 76  ? 0.1803 0.1556 0.1560 -0.0061 0.0144  -0.0094 76  LYS   A CA  
1764 C C   . LYS   A 76  ? 0.1759 0.1354 0.1198 -0.0034 0.0106  0.0111  76  LYS   A C   
1765 O O   . LYS   A 76  ? 0.1729 0.1328 0.1273 -0.0038 0.0190  0.0127  76  LYS   A O   
1766 C CB  . LYS   A 76  ? 0.1746 0.1804 0.2025 0.0034  0.0217  -0.0315 76  LYS   A CB  
1767 C CG  . LYS   A 76  ? 0.1818 0.1760 0.2652 0.0093  0.0147  -0.0323 76  LYS   A CG  
1768 C CD  . LYS   A 76  ? 0.1896 0.1769 0.3105 0.0109  0.0005  -0.0466 76  LYS   A CD  
1769 C CE  . LYS   A 76  ? 0.2088 0.1962 0.3796 0.0026  0.0001  -0.0495 76  LYS   A CE  
1770 N NZ  . LYS   A 76  ? 0.2069 0.1910 0.4212 -0.0194 -0.0137 -0.0541 76  LYS   A NZ  
1784 N N   . VAL   A 77  ? 0.1843 0.1406 0.1274 -0.0052 0.0262  0.0126  77  VAL   A N   
1785 C CA  . VAL   A 77  ? 0.1807 0.1425 0.1306 0.0039  0.0156  0.0119  77  VAL   A CA  
1786 C C   . VAL   A 77  ? 0.1698 0.1379 0.1236 0.0080  0.0035  0.0061  77  VAL   A C   
1787 O O   . VAL   A 77  ? 0.1762 0.1414 0.1284 0.0118  0.0241  -0.0055 77  VAL   A O   
1788 C CB  . VAL   A 77  ? 0.1950 0.1650 0.1418 0.0032  0.0126  0.0194  77  VAL   A CB  
1789 C CG1 . VAL   A 77  ? 0.1901 0.1834 0.1594 0.0117  0.0004  0.0094  77  VAL   A CG1 
1790 C CG2 . VAL   A 77  ? 0.2191 0.1735 0.1604 -0.0031 0.0035  0.0278  77  VAL   A CG2 
1800 N N   . GLY   A 78  ? 0.1662 0.1325 0.1256 0.0039  0.0204  0.0091  78  GLY   A N   
1801 C CA  . GLY   A 78  ? 0.1624 0.1323 0.1324 0.0041  0.0176  0.0123  78  GLY   A CA  
1802 C C   . GLY   A 78  ? 0.1482 0.1227 0.1362 0.0051  0.0191  0.0111  78  GLY   A C   
1803 O O   . GLY   A 78  ? 0.1469 0.1361 0.1559 0.0058  0.0204  0.0175  78  GLY   A O   
1807 N N   . GLY   A 79  ? 0.1572 0.1218 0.1309 -0.0022 0.0131  0.0080  79  GLY   A N   
1808 C CA  . GLY   A 79  ? 0.1531 0.1244 0.1453 -0.0031 0.0211  0.0081  79  GLY   A CA  
1809 C C   . GLY   A 79  ? 0.1384 0.1191 0.1393 -0.0027 0.0162  0.0057  79  GLY   A C   
1810 O O   . GLY   A 79  ? 0.1381 0.1348 0.1469 0.0195  0.0125  0.0065  79  GLY   A O   
1814 N N   . SER   A 80  ? 0.1310 0.1391 0.1563 0.0003  0.0147  -0.0078 80  SER   A N   
1815 C CA  . SER   A 80  ? 0.1269 0.1323 0.1420 0.0020  0.0077  0.0058  80  SER   A CA  
1816 C C   . SER   A 80  ? 0.1252 0.1349 0.1470 -0.0026 0.0066  0.0116  80  SER   A C   
1817 O O   . SER   A 80  ? 0.1308 0.1555 0.1732 0.0085  0.0137  -0.0043 80  SER   A O   
1818 C CB  . SER   A 80  ? 0.1399 0.1360 0.1721 -0.0009 0.0088  0.0063  80  SER   A CB  
1819 O OG  . SER   A 80  ? 0.1641 0.1347 0.2192 0.0018  -0.0032 0.0222  80  SER   A OG  
1825 N N   . CYS   A 81  ? 0.1224 0.1271 0.1455 0.0011  -0.0041 0.0084  81  CYS   A N   
1826 C CA  . CYS   A 81  ? 0.1197 0.1369 0.1399 -0.0037 -0.0033 0.0200  81  CYS   A CA  
1827 C C   . CYS   A 81  ? 0.1217 0.1311 0.1360 -0.0129 -0.0033 0.0229  81  CYS   A C   
1828 O O   . CYS   A 81  ? 0.1212 0.1615 0.1572 0.0014  0.0042  0.0331  81  CYS   A O   
1829 C CB  . CYS   A 81  ? 0.1277 0.1479 0.1490 -0.0095 0.0034  0.0239  81  CYS   A CB  
1830 S SG  . CYS   A 81  ? 0.1412 0.1357 0.1463 -0.0128 0.0028  0.0148  81  CYS   A SG  
1836 N N   . VAL   A 82  ? 0.1265 0.1408 0.1403 -0.0003 -0.0146 0.0168  82  VAL   A N   
1837 C CA  . VAL   A 82  ? 0.1366 0.1462 0.1390 0.0003  -0.0134 0.0245  82  VAL   A CA  
1838 C C   . VAL   A 82  ? 0.1343 0.1561 0.1440 -0.0000 -0.0091 0.0238  82  VAL   A C   
1839 O O   . VAL   A 82  ? 0.1251 0.1615 0.1764 0.0025  -0.0071 0.0023  82  VAL   A O   
1840 C CB  . VAL   A 82  ? 0.1627 0.1585 0.1531 0.0005  0.0002  0.0304  82  VAL   A CB  
1841 C CG1 . VAL   A 82  ? 0.1903 0.1734 0.1721 0.0060  -0.0003 0.0266  82  VAL   A CG1 
1842 C CG2 . VAL   A 82  ? 0.1729 0.1626 0.1755 -0.0088 -0.0065 0.0339  82  VAL   A CG2 
1852 N N   . LEU   A 83  ? 0.1284 0.1463 0.1369 -0.0082 -0.0070 0.0129  83  LEU   A N   
1853 C CA  . LEU   A 83  ? 0.1360 0.1484 0.1324 -0.0122 -0.0080 0.0153  83  LEU   A CA  
1854 C C   . LEU   A 83  ? 0.1364 0.1529 0.1219 -0.0135 -0.0116 0.0162  83  LEU   A C   
1855 O O   . LEU   A 83  ? 0.1406 0.1546 0.1392 -0.0143 -0.0036 0.0209  83  LEU   A O   
1856 C CB  . LEU   A 83  ? 0.1460 0.1517 0.1371 -0.0134 -0.0048 0.0113  83  LEU   A CB  
1857 C CG  . LEU   A 83  ? 0.1539 0.1611 0.1345 -0.0119 0.0033  0.0065  83  LEU   A CG  
1858 C CD1 . LEU   A 83  ? 0.1700 0.1639 0.1421 -0.0238 -0.0021 0.0201  83  LEU   A CD1 
1859 C CD2 . LEU   A 83  ? 0.1519 0.1774 0.1523 -0.0090 0.0114  0.0139  83  LEU   A CD2 
1871 N N   . SER   A 84  ? 0.1519 0.1611 0.1263 -0.0184 -0.0129 0.0162  84  SER   A N   
1872 C CA  . SER   A 84  ? 0.1627 0.1659 0.1145 -0.0149 -0.0094 0.0193  84  SER   A CA  
1873 C C   . SER   A 84  ? 0.1627 0.1628 0.1105 -0.0192 0.0002  0.0099  84  SER   A C   
1874 O O   . SER   A 84  ? 0.1578 0.1737 0.1217 -0.0114 -0.0086 0.0079  84  SER   A O   
1875 C CB  . SER   A 84  ? 0.1720 0.1848 0.1301 -0.0198 -0.0101 0.0077  84  SER   A CB  
1876 O OG  . SER   A 84  ? 0.1731 0.2080 0.1446 -0.0159 -0.0141 -0.0058 84  SER   A OG  
1882 N N   . GLY   A 85  ? 0.1793 0.1782 0.1187 -0.0219 0.0024  0.0065  85  GLY   A N   
1883 C CA  . GLY   A 85  ? 0.1858 0.1854 0.1329 -0.0243 0.0158  0.0053  85  GLY   A CA  
1884 C C   . GLY   A 85  ? 0.1759 0.1892 0.1134 -0.0247 0.0019  0.0024  85  GLY   A C   
1885 O O   . GLY   A 85  ? 0.1794 0.1951 0.1277 -0.0269 0.0171  -0.0109 85  GLY   A O   
1889 N N   . HIS   A 86  ? 0.1741 0.1869 0.1171 -0.0232 -0.0060 0.0096  86  HIS   A N   
1890 C CA  . HIS   A 86  ? 0.1958 0.1934 0.1105 -0.0252 -0.0036 0.0064  86  HIS   A CA  
1891 C C   . HIS   A 86  ? 0.2196 0.2063 0.1013 -0.0252 -0.0051 0.0046  86  HIS   A C   
1892 O O   . HIS   A 86  ? 0.2275 0.2298 0.1171 -0.0255 0.0109  0.0022  86  HIS   A O   
1893 C CB  . HIS   A 86  ? 0.1952 0.1817 0.1264 -0.0142 0.0020  0.0044  86  HIS   A CB  
1894 C CG  . HIS   A 86  ? 0.1891 0.1789 0.1309 -0.0073 -0.0020 0.0164  86  HIS   A CG  
1895 N ND1 . HIS   A 86  ? 0.1950 0.1795 0.1735 -0.0181 -0.0005 0.0134  86  HIS   A ND1 
1896 C CD2 . HIS   A 86  ? 0.1865 0.1717 0.1244 0.0073  0.0085  0.0192  86  HIS   A CD2 
1897 C CE1 . HIS   A 86  ? 0.1924 0.1727 0.1653 -0.0098 0.0210  0.0198  86  HIS   A CE1 
1898 N NE2 . HIS   A 86  ? 0.1846 0.1686 0.1458 0.0033  0.0226  0.0251  86  HIS   A NE2 
1906 N N   . ASN   A 87  ? 0.2326 0.2103 0.1273 -0.0169 0.0188  -0.0019 87  ASN   A N   
1907 C CA  . ASN   A 87  ? 0.2486 0.2208 0.1328 -0.0128 0.0397  -0.0130 87  ASN   A CA  
1908 C C   . ASN   A 87  ? 0.2416 0.2322 0.1573 -0.0206 0.0596  -0.0072 87  ASN   A C   
1909 O O   . ASN   A 87  ? 0.2710 0.2539 0.1904 -0.0312 0.0908  -0.0162 87  ASN   A O   
1910 C CB  . ASN   A 87  ? 0.2655 0.2275 0.1366 -0.0043 0.0465  -0.0175 87  ASN   A CB  
1911 C CG  . ASN   A 87  ? 0.2767 0.2387 0.1522 0.0032  0.0585  -0.0109 87  ASN   A CG  
1912 O OD1 . ASN   A 87  ? 0.2915 0.2351 0.1574 0.0203  0.0523  0.0003  87  ASN   A OD1 
1913 N ND2 . ASN   A 87  ? 0.2805 0.2645 0.1668 0.0022  0.0614  -0.0009 87  ASN   A ND2 
1920 N N   A LEU   A 88  ? 0.2218 0.2222 0.1540 -0.0264 0.0413  0.0061  88  LEU   A N   
1921 N N   B LEU   A 88  ? 0.2180 0.2202 0.1504 -0.0275 0.0408  0.0051  88  LEU   A N   
1922 C CA  A LEU   A 88  ? 0.2072 0.2208 0.1668 -0.0291 0.0330  0.0211  88  LEU   A CA  
1923 C CA  B LEU   A 88  ? 0.2020 0.2214 0.1691 -0.0284 0.0365  0.0194  88  LEU   A CA  
1924 C C   A LEU   A 88  ? 0.2026 0.2218 0.1564 -0.0297 0.0369  0.0232  88  LEU   A C   
1925 C C   B LEU   A 88  ? 0.2008 0.2220 0.1615 -0.0291 0.0380  0.0287  88  LEU   A C   
1926 O O   A LEU   A 88  ? 0.2050 0.2249 0.1751 -0.0298 0.0401  0.0264  88  LEU   A O   
1927 O O   B LEU   A 88  ? 0.2057 0.2240 0.1882 -0.0275 0.0376  0.0393  88  LEU   A O   
1928 C CB  A LEU   A 88  ? 0.2056 0.2230 0.1811 -0.0318 0.0086  0.0311  88  LEU   A CB  
1929 C CB  B LEU   A 88  ? 0.1997 0.2283 0.1771 -0.0298 0.0114  0.0178  88  LEU   A CB  
1930 C CG  A LEU   A 88  ? 0.2114 0.2301 0.2067 -0.0312 0.0010  0.0385  88  LEU   A CG  
1931 C CG  B LEU   A 88  ? 0.2078 0.2406 0.1962 -0.0239 0.0076  0.0139  88  LEU   A CG  
1932 C CD1 A LEU   A 88  ? 0.2147 0.2318 0.2137 -0.0295 -0.0019 0.0366  88  LEU   A CD1 
1933 C CD1 B LEU   A 88  ? 0.2141 0.2453 0.1995 -0.0214 0.0070  0.0049  88  LEU   A CD1 
1934 C CD2 A LEU   A 88  ? 0.2193 0.2376 0.2392 -0.0288 0.0014  0.0322  88  LEU   A CD2 
1935 C CD2 B LEU   A 88  ? 0.2165 0.2510 0.2348 -0.0175 0.0101  0.0063  88  LEU   A CD2 
1958 N N   . ALA   A 89  ? 0.1970 0.2171 0.1431 -0.0270 0.0298  0.0116  89  ALA   A N   
1959 C CA  . ALA   A 89  ? 0.1977 0.2131 0.1229 -0.0220 0.0105  0.0200  89  ALA   A CA  
1960 C C   . ALA   A 89  ? 0.2045 0.2149 0.1271 -0.0182 -0.0036 0.0145  89  ALA   A C   
1961 O O   . ALA   A 89  ? 0.2019 0.2121 0.1648 -0.0233 -0.0087 -0.0080 89  ALA   A O   
1962 C CB  . ALA   A 89  ? 0.1918 0.2073 0.1071 -0.0223 0.0095  0.0213  89  ALA   A CB  
1969 N N   . LYS   A 90  ? 0.2130 0.2276 0.1233 -0.0249 -0.0183 0.0139  90  LYS   A N   
1970 C CA  . LYS   A 90  ? 0.2228 0.2445 0.1284 -0.0204 -0.0270 0.0275  90  LYS   A CA  
1971 C C   . LYS   A 90  ? 0.1958 0.2247 0.1323 -0.0243 -0.0304 0.0147  90  LYS   A C   
1972 O O   . LYS   A 90  ? 0.1965 0.2351 0.1608 -0.0287 -0.0311 0.0075  90  LYS   A O   
1973 C CB  . LYS   A 90  ? 0.2527 0.2803 0.1461 -0.0160 -0.0382 0.0527  90  LYS   A CB  
1974 C CG  . LYS   A 90  ? 0.2872 0.3143 0.2557 -0.0124 -0.0402 0.0608  90  LYS   A CG  
1975 C CD  . LYS   A 90  ? 0.3312 0.3466 0.3610 -0.0142 -0.0248 0.0614  90  LYS   A CD  
1976 C CE  . LYS   A 90  ? 0.3724 0.3840 0.4353 -0.0155 -0.0095 0.0579  90  LYS   A CE  
1977 N NZ  . LYS   A 90  ? 0.3915 0.3972 0.4923 -0.0171 -0.0025 0.0543  90  LYS   A NZ  
1991 N N   . HIS   A 91  ? 0.1817 0.2005 0.1127 -0.0190 -0.0273 0.0211  91  HIS   A N   
1992 C CA  . HIS   A 91  ? 0.1760 0.1841 0.1170 -0.0121 -0.0196 0.0189  91  HIS   A CA  
1993 C C   . HIS   A 91  ? 0.1512 0.1690 0.1055 -0.0154 -0.0129 0.0192  91  HIS   A C   
1994 O O   . HIS   A 91  ? 0.1473 0.1834 0.1178 -0.0194 -0.0030 0.0245  91  HIS   A O   
1995 C CB  . HIS   A 91  ? 0.1972 0.2090 0.1691 0.0087  -0.0361 0.0183  91  HIS   A CB  
1996 C CG  . HIS   A 91  ? 0.2395 0.2615 0.2322 0.0220  -0.0728 0.0068  91  HIS   A CG  
1997 N ND1 . HIS   A 91  ? 0.2504 0.2894 0.2841 0.0287  -0.0829 -0.0087 91  HIS   A ND1 
1998 C CD2 . HIS   A 91  ? 0.2698 0.2827 0.2576 0.0290  -0.0942 0.0150  91  HIS   A CD2 
1999 C CE1 . HIS   A 91  ? 0.2658 0.2998 0.2972 0.0317  -0.0877 0.0005  91  HIS   A CE1 
2000 N NE2 . HIS   A 91  ? 0.2821 0.3014 0.2883 0.0360  -0.0948 0.0110  91  HIS   A NE2 
2008 N N   . CYS   A 92  ? 0.1408 0.1616 0.1151 -0.0198 -0.0113 0.0189  92  CYS   A N   
2009 C CA  . CYS   A 92  ? 0.1329 0.1589 0.1231 -0.0099 -0.0025 0.0174  92  CYS   A CA  
2010 C C   . CYS   A 92  ? 0.1330 0.1516 0.1097 -0.0125 0.0008  0.0246  92  CYS   A C   
2011 O O   . CYS   A 92  ? 0.1335 0.1521 0.1361 -0.0147 0.0013  0.0127  92  CYS   A O   
2012 C CB  . CYS   A 92  ? 0.1389 0.1511 0.1343 -0.0038 -0.0059 0.0131  92  CYS   A CB  
2013 S SG  . CYS   A 92  ? 0.1385 0.1400 0.1245 -0.0118 -0.0031 0.0124  92  CYS   A SG  
2019 N N   . LEU   A 93  ? 0.1324 0.1400 0.1147 -0.0135 0.0052  0.0215  93  LEU   A N   
2020 C CA  . LEU   A 93  ? 0.1231 0.1314 0.1162 -0.0067 -0.0001 0.0157  93  LEU   A CA  
2021 C C   . LEU   A 93  ? 0.1201 0.1242 0.1161 -0.0004 0.0041  0.0099  93  LEU   A C   
2022 O O   . LEU   A 93  ? 0.1140 0.1347 0.1207 -0.0018 -0.0012 0.0139  93  LEU   A O   
2023 C CB  . LEU   A 93  ? 0.1285 0.1328 0.1417 -0.0033 -0.0003 0.0265  93  LEU   A CB  
2024 C CG  . LEU   A 93  ? 0.1367 0.1309 0.1403 -0.0026 0.0045  0.0243  93  LEU   A CG  
2025 C CD1 . LEU   A 93  ? 0.1362 0.1378 0.1709 0.0014  0.0080  0.0171  93  LEU   A CD1 
2026 C CD2 . LEU   A 93  ? 0.1485 0.1280 0.1674 -0.0094 0.0035  0.0158  93  LEU   A CD2 
2038 N N   . HIS   A 94  ? 0.1155 0.1189 0.1157 -0.0056 0.0009  0.0205  94  HIS   A N   
2039 C CA  . HIS   A 94  ? 0.1169 0.1187 0.1113 -0.0053 0.0011  0.0136  94  HIS   A CA  
2040 C C   . HIS   A 94  ? 0.1144 0.1190 0.1227 -0.0036 -0.0006 0.0101  94  HIS   A C   
2041 O O   . HIS   A 94  ? 0.1172 0.1386 0.1606 0.0037  0.0038  -0.0111 94  HIS   A O   
2042 C CB  . HIS   A 94  ? 0.1161 0.1182 0.1290 0.0012  0.0006  0.0127  94  HIS   A CB  
2043 C CG  . HIS   A 94  ? 0.1224 0.1220 0.1146 -0.0049 -0.0003 0.0180  94  HIS   A CG  
2044 N ND1 . HIS   A 94  ? 0.1200 0.1196 0.1248 -0.0028 -0.0002 0.0145  94  HIS   A ND1 
2045 C CD2 . HIS   A 94  ? 0.1318 0.1322 0.1217 -0.0069 -0.0056 0.0075  94  HIS   A CD2 
2046 C CE1 . HIS   A 94  ? 0.1250 0.1240 0.1250 -0.0107 -0.0069 0.0104  94  HIS   A CE1 
2047 N NE2 . HIS   A 94  ? 0.1292 0.1289 0.1319 -0.0102 -0.0045 0.0099  94  HIS   A NE2 
2055 N N   . VAL   A 95  ? 0.1133 0.1153 0.1133 -0.0018 0.0052  0.0081  95  VAL   A N   
2056 C CA  . VAL   A 95  ? 0.1218 0.1173 0.1153 -0.0035 0.0052  0.0086  95  VAL   A CA  
2057 C C   . VAL   A 95  ? 0.1266 0.1161 0.0969 -0.0089 0.0055  0.0059  95  VAL   A C   
2058 O O   . VAL   A 95  ? 0.1282 0.1269 0.1199 0.0078  0.0049  0.0093  95  VAL   A O   
2059 C CB  . VAL   A 95  ? 0.1268 0.1227 0.1314 -0.0106 0.0029  0.0102  95  VAL   A CB  
2060 C CG1 . VAL   A 95  ? 0.1434 0.1290 0.1435 -0.0155 0.0022  0.0064  95  VAL   A CG1 
2061 C CG2 . VAL   A 95  ? 0.1331 0.1256 0.1334 -0.0163 0.0014  0.0228  95  VAL   A CG2 
2071 N N   . VAL   A 96  ? 0.1311 0.1189 0.0964 -0.0012 0.0061  0.0118  96  VAL   A N   
2072 C CA  . VAL   A 96  ? 0.1414 0.1189 0.1104 -0.0011 0.0092  0.0116  96  VAL   A CA  
2073 C C   . VAL   A 96  ? 0.1431 0.1263 0.1233 -0.0043 0.0082  0.0133  96  VAL   A C   
2074 O O   . VAL   A 96  ? 0.1522 0.1314 0.1426 -0.0075 0.0168  -0.0026 96  VAL   A O   
2075 C CB  . VAL   A 96  ? 0.1421 0.1251 0.1195 -0.0016 0.0182  0.0105  96  VAL   A CB  
2076 C CG1 . VAL   A 96  ? 0.1535 0.1336 0.1147 -0.0027 0.0103  0.0128  96  VAL   A CG1 
2077 C CG2 . VAL   A 96  ? 0.1458 0.1353 0.1305 -0.0080 0.0247  0.0103  96  VAL   A CG2 
2087 N N   A GLY   A 97  ? 0.1401 0.1307 0.1267 -0.0043 0.0031  0.0126  97  GLY   A N   
2088 N N   B GLY   A 97  ? 0.1436 0.1280 0.1222 -0.0070 0.0055  0.0114  97  GLY   A N   
2089 C CA  A GLY   A 97  ? 0.1454 0.1431 0.1273 -0.0048 -0.0049 0.0155  97  GLY   A CA  
2090 C CA  B GLY   A 97  ? 0.1559 0.1410 0.1200 -0.0080 -0.0031 0.0153  97  GLY   A CA  
2091 C C   A GLY   A 97  ? 0.1463 0.1560 0.1229 -0.0092 -0.0082 0.0162  97  GLY   A C   
2092 C C   B GLY   A 97  ? 0.1617 0.1529 0.1149 -0.0123 -0.0073 0.0192  97  GLY   A C   
2093 O O   A GLY   A 97  ? 0.1525 0.1563 0.1427 -0.0081 -0.0061 0.0226  97  GLY   A O   
2094 O O   B GLY   A 97  ? 0.1689 0.1485 0.1340 -0.0118 -0.0091 0.0256  97  GLY   A O   
2101 N N   A PRO   A 98  ? 0.1529 0.1624 0.1128 -0.0115 -0.0130 0.0099  98  PRO   A N   
2102 N N   B PRO   A 98  ? 0.1704 0.1579 0.1111 -0.0113 -0.0080 0.0219  98  PRO   A N   
2103 C CA  A PRO   A 98  ? 0.1623 0.1804 0.1135 -0.0137 -0.0135 0.0034  98  PRO   A CA  
2104 C CA  B PRO   A 98  ? 0.1924 0.1824 0.1227 -0.0122 -0.0098 0.0197  98  PRO   A CA  
2105 C C   A PRO   A 98  ? 0.1618 0.1904 0.1195 -0.0166 -0.0175 0.0161  98  PRO   A C   
2106 C C   B PRO   A 98  ? 0.2085 0.1886 0.1366 -0.0184 -0.0137 0.0522  98  PRO   A C   
2107 O O   A PRO   A 98  ? 0.1543 0.1787 0.1334 -0.0110 -0.0167 0.0180  98  PRO   A O   
2108 O O   B PRO   A 98  ? 0.2039 0.1757 0.1667 -0.0120 -0.0162 0.0349  98  PRO   A O   
2109 C CB  A PRO   A 98  ? 0.1777 0.1878 0.1154 -0.0089 -0.0128 -0.0075 98  PRO   A CB  
2110 C CB  B PRO   A 98  ? 0.2040 0.1867 0.1157 -0.0030 -0.0078 0.0079  98  PRO   A CB  
2111 C CG  A PRO   A 98  ? 0.1749 0.1818 0.1244 -0.0043 -0.0089 -0.0088 98  PRO   A CG  
2112 C CG  B PRO   A 98  ? 0.1986 0.1794 0.1236 -0.0012 0.0007  0.0039  98  PRO   A CG  
2113 C CD  A PRO   A 98  ? 0.1631 0.1669 0.1245 -0.0085 -0.0105 0.0037  98  PRO   A CD  
2114 C CD  B PRO   A 98  ? 0.1793 0.1583 0.1130 -0.0043 -0.0010 0.0192  98  PRO   A CD  
2129 N N   A ASN   A 99  ? 0.1675 0.2090 0.1358 -0.0191 -0.0111 0.0243  99  ASN   A N   
2130 N N   B ASN   A 99  ? 0.2264 0.2136 0.1558 -0.0193 -0.0155 0.0860  99  ASN   A N   
2131 C CA  A ASN   A 99  ? 0.1795 0.2170 0.1378 -0.0223 -0.0112 0.0287  99  ASN   A CA  
2132 C CA  B ASN   A 99  ? 0.2488 0.2448 0.1698 -0.0190 -0.0242 0.1069  99  ASN   A CA  
2133 C C   A ASN   A 99  ? 0.1895 0.2389 0.1055 -0.0221 -0.0058 0.0259  99  ASN   A C   
2134 C C   B ASN   A 99  ? 0.2766 0.2950 0.1841 -0.0283 -0.0186 0.1080  99  ASN   A C   
2135 O O   A ASN   A 99  ? 0.1941 0.2675 0.1128 -0.0165 -0.0039 0.0366  99  ASN   A O   
2136 O O   B ASN   A 99  ? 0.2825 0.3188 0.1863 -0.0261 -0.0182 0.1013  99  ASN   A O   
2137 C CB  A ASN   A 99  ? 0.1797 0.2065 0.1841 -0.0297 -0.0271 0.0318  99  ASN   A CB  
2138 C CB  B ASN   A 99  ? 0.2423 0.2398 0.2125 -0.0153 -0.0375 0.1056  99  ASN   A CB  
2139 C CG  A ASN   A 99  ? 0.1832 0.1970 0.2163 -0.0327 -0.0306 0.0300  99  ASN   A CG  
2140 C CG  B ASN   A 99  ? 0.2372 0.2452 0.2641 -0.0118 -0.0529 0.0914  99  ASN   A CG  
2141 O OD1 A ASN   A 99  ? 0.1934 0.2032 0.2224 -0.0259 -0.0246 0.0332  99  ASN   A OD1 
2142 O OD1 B ASN   A 99  ? 0.2476 0.2505 0.2754 -0.0107 -0.0705 0.0916  99  ASN   A OD1 
2143 N ND2 A ASN   A 99  ? 0.1827 0.1849 0.2383 -0.0327 -0.0411 0.0314  99  ASN   A ND2 
2144 N ND2 B ASN   A 99  ? 0.2254 0.2444 0.2783 -0.0062 -0.0492 0.0948  99  ASN   A ND2 
2157 N N   A VAL   A 100 ? 0.1969 0.2317 0.0721 -0.0224 -0.0195 0.0107  100 VAL   A N   
2158 N N   B VAL   A 100 ? 0.2978 0.3211 0.2005 -0.0323 -0.0260 0.1097  100 VAL   A N   
2159 C CA  A VAL   A 100 ? 0.2066 0.2366 0.0768 -0.0258 -0.0314 0.0146  100 VAL   A CA  
2160 C CA  B VAL   A 100 ? 0.3205 0.3529 0.2543 -0.0329 -0.0311 0.0950  100 VAL   A CA  
2161 C C   A VAL   A 100 ? 0.2146 0.2450 0.0763 -0.0287 -0.0307 0.0259  100 VAL   A C   
2162 C C   B VAL   A 100 ? 0.3324 0.3726 0.2687 -0.0337 -0.0426 0.1061  100 VAL   A C   
2163 O O   A VAL   A 100 ? 0.2236 0.2509 0.0841 -0.0278 -0.0079 0.0298  100 VAL   A O   
2164 O O   B VAL   A 100 ? 0.3393 0.3879 0.2846 -0.0311 -0.0355 0.0968  100 VAL   A O   
2165 C CB  A VAL   A 100 ? 0.2147 0.2373 0.1346 -0.0321 -0.0309 0.0098  100 VAL   A CB  
2166 C CB  B VAL   A 100 ? 0.3286 0.3611 0.2998 -0.0327 -0.0192 0.0719  100 VAL   A CB  
2167 C CG1 A VAL   A 100 ? 0.2171 0.2443 0.1562 -0.0370 -0.0249 0.0125  100 VAL   A CG1 
2168 C CG1 B VAL   A 100 ? 0.3296 0.3624 0.3054 -0.0339 -0.0185 0.0607  100 VAL   A CG1 
2169 C CG2 A VAL   A 100 ? 0.2210 0.2378 0.1605 -0.0333 -0.0283 -0.0000 100 VAL   A CG2 
2170 C CG2 B VAL   A 100 ? 0.3317 0.3637 0.3253 -0.0318 -0.0102 0.0649  100 VAL   A CG2 
2189 N N   A ASN   A 101 ? 0.2156 0.2475 0.0995 -0.0309 -0.0271 0.0508  101 ASN   A N   
2190 N N   B ASN   A 101 ? 0.3395 0.3738 0.2829 -0.0395 -0.0541 0.1245  101 ASN   A N   
2191 C CA  A ASN   A 101 ? 0.2340 0.2640 0.1397 -0.0284 -0.0270 0.0687  101 ASN   A CA  
2192 C CA  B ASN   A 101 ? 0.3511 0.3772 0.2935 -0.0436 -0.0585 0.1387  101 ASN   A CA  
2193 C C   A ASN   A 101 ? 0.2619 0.2915 0.1892 -0.0379 -0.0072 0.0985  101 ASN   A C   
2194 C C   B ASN   A 101 ? 0.3649 0.4013 0.3082 -0.0482 -0.0346 0.1541  101 ASN   A C   
2195 O O   A ASN   A 101 ? 0.2781 0.2952 0.2277 -0.0390 -0.0059 0.0789  101 ASN   A O   
2196 O O   B ASN   A 101 ? 0.3758 0.4067 0.3245 -0.0452 -0.0278 0.1604  101 ASN   A O   
2197 C CB  A ASN   A 101 ? 0.2310 0.2557 0.1505 -0.0182 -0.0425 0.0515  101 ASN   A CB  
2198 C CB  B ASN   A 101 ? 0.3474 0.3539 0.2803 -0.0448 -0.0798 0.1355  101 ASN   A CB  
2199 C CG  A ASN   A 101 ? 0.2303 0.2504 0.1563 -0.0082 -0.0529 0.0193  101 ASN   A CG  
2200 C CG  B ASN   A 101 ? 0.3450 0.3399 0.2804 -0.0487 -0.0907 0.1090  101 ASN   A CG  
2201 O OD1 A ASN   A 101 ? 0.2280 0.2523 0.1772 0.0051  -0.0544 -0.0071 101 ASN   A OD1 
2202 O OD1 B ASN   A 101 ? 0.3454 0.3405 0.2965 -0.0517 -0.0856 0.0887  101 ASN   A OD1 
2203 N ND2 A ASN   A 101 ? 0.2353 0.2502 0.1607 -0.0104 -0.0432 0.0137  101 ASN   A ND2 
2204 N ND2 B ASN   A 101 ? 0.3456 0.3281 0.2865 -0.0539 -0.0895 0.0983  101 ASN   A ND2 
2217 N N   A LYS   A 102 ? 0.2704 0.3193 0.2227 -0.0441 0.0013  0.1178  102 LYS   A N   
2218 N N   B LYS   A 102 ? 0.3649 0.4201 0.3270 -0.0566 -0.0202 0.1374  102 LYS   A N   
2219 C CA  A LYS   A 102 ? 0.2864 0.3489 0.2505 -0.0435 -0.0011 0.1106  102 LYS   A CA  
2220 C CA  B LYS   A 102 ? 0.3693 0.4396 0.3270 -0.0611 -0.0153 0.1092  102 LYS   A CA  
2221 C C   A LYS   A 102 ? 0.2926 0.3695 0.2417 -0.0356 -0.0108 0.1037  102 LYS   A C   
2222 C C   B LYS   A 102 ? 0.3745 0.4507 0.3153 -0.0571 -0.0087 0.1029  102 LYS   A C   
2223 O O   A LYS   A 102 ? 0.2945 0.3816 0.2475 -0.0346 -0.0103 0.0934  102 LYS   A O   
2224 O O   B LYS   A 102 ? 0.3785 0.4603 0.3116 -0.0579 -0.0060 0.0995  102 LYS   A O   
2225 C CB  A LYS   A 102 ? 0.2996 0.3574 0.2926 -0.0501 -0.0018 0.0975  102 LYS   A CB  
2226 C CB  B LYS   A 102 ? 0.3731 0.4482 0.3462 -0.0677 -0.0258 0.0834  102 LYS   A CB  
2227 C CG  A LYS   A 102 ? 0.3121 0.3651 0.3252 -0.0547 -0.0039 0.0845  102 LYS   A CG  
2228 C CG  B LYS   A 102 ? 0.3788 0.4567 0.3574 -0.0722 -0.0364 0.0602  102 LYS   A CG  
2229 C CD  A LYS   A 102 ? 0.3248 0.3719 0.3535 -0.0585 -0.0043 0.0687  102 LYS   A CD  
2230 C CD  B LYS   A 102 ? 0.3856 0.4648 0.3617 -0.0732 -0.0417 0.0366  102 LYS   A CD  
2231 C CE  A LYS   A 102 ? 0.3349 0.3772 0.3745 -0.0605 -0.0023 0.0573  102 LYS   A CE  
2232 C CE  B LYS   A 102 ? 0.3914 0.4706 0.3678 -0.0714 -0.0445 0.0197  102 LYS   A CE  
2233 N NZ  A LYS   A 102 ? 0.3401 0.3793 0.3881 -0.0635 -0.0009 0.0498  102 LYS   A NZ  
2234 N NZ  B LYS   A 102 ? 0.3941 0.4735 0.3635 -0.0698 -0.0473 0.0131  102 LYS   A NZ  
2261 N N   A GLY   A 103 ? 0.2945 0.3778 0.2440 -0.0282 -0.0210 0.0897  103 GLY   A N   
2262 N N   B GLY   A 103 ? 0.3745 0.4522 0.3131 -0.0479 -0.0103 0.0911  103 GLY   A N   
2263 C CA  A GLY   A 103 ? 0.2965 0.3823 0.2445 -0.0239 -0.0160 0.0725  103 GLY   A CA  
2264 C CA  B GLY   A 103 ? 0.3709 0.4505 0.2902 -0.0380 -0.0104 0.0823  103 GLY   A CA  
2265 C C   A GLY   A 103 ? 0.2952 0.3849 0.2513 -0.0247 -0.0079 0.0561  103 GLY   A C   
2266 C C   B GLY   A 103 ? 0.3630 0.4473 0.2797 -0.0279 -0.0058 0.0725  103 GLY   A C   
2267 O O   A GLY   A 103 ? 0.2991 0.3888 0.2613 -0.0243 -0.0051 0.0475  103 GLY   A O   
2268 O O   B GLY   A 103 ? 0.3674 0.4574 0.2918 -0.0273 -0.0081 0.0640  103 GLY   A O   
2275 N N   A GLU   A 104 ? 0.2862 0.3809 0.2325 -0.0292 -0.0035 0.0471  104 GLU   A N   
2276 N N   B GLU   A 104 ? 0.3471 0.4282 0.2317 -0.0206 0.0015  0.0746  104 GLU   A N   
2277 C CA  A GLU   A 104 ? 0.2696 0.3731 0.2159 -0.0381 -0.0020 0.0370  104 GLU   A CA  
2278 C CA  B GLU   A 104 ? 0.3300 0.4079 0.1953 -0.0174 0.0045  0.0706  104 GLU   A CA  
2279 C C   A GLU   A 104 ? 0.2799 0.3815 0.2116 -0.0333 0.0003  0.0101  104 GLU   A C   
2280 C C   B GLU   A 104 ? 0.3215 0.4047 0.1798 -0.0123 0.0043  0.0429  104 GLU   A C   
2281 O O   A GLU   A 104 ? 0.2833 0.3861 0.2121 -0.0336 -0.0001 -0.0014 104 GLU   A O   
2282 O O   B GLU   A 104 ? 0.3231 0.4070 0.1847 -0.0122 -0.0050 0.0388  104 GLU   A O   
2283 C CB  A GLU   A 104 ? 0.2410 0.3560 0.1977 -0.0518 -0.0046 0.0608  104 GLU   A CB  
2284 C CB  B GLU   A 104 ? 0.3222 0.3938 0.1987 -0.0176 0.0123  0.0923  104 GLU   A CB  
2285 C CG  A GLU   A 104 ? 0.2178 0.3389 0.1938 -0.0625 -0.0121 0.0779  104 GLU   A CG  
2286 C CG  B GLU   A 104 ? 0.3196 0.3850 0.2217 -0.0133 0.0120  0.1037  104 GLU   A CG  
2287 C CD  A GLU   A 104 ? 0.1962 0.3194 0.1780 -0.0706 -0.0175 0.0975  104 GLU   A CD  
2288 C CD  B GLU   A 104 ? 0.3164 0.3822 0.2384 -0.0048 0.0116  0.1027  104 GLU   A CD  
2289 O OE1 A GLU   A 104 ? 0.1812 0.3045 0.1424 -0.0722 -0.0314 0.0987  104 GLU   A OE1 
2290 O OE1 B GLU   A 104 ? 0.3130 0.3755 0.2314 0.0006  0.0106  0.1036  104 GLU   A OE1 
2291 O OE2 A GLU   A 104 ? 0.1962 0.3179 0.1873 -0.0807 -0.0071 0.1145  104 GLU   A OE2 
2292 O OE2 B GLU   A 104 ? 0.3175 0.3867 0.2581 -0.0023 0.0112  0.0967  104 GLU   A OE2 
2305 N N   A ASP   A 105 ? 0.2849 0.3834 0.2101 -0.0271 0.0026  -0.0098 105 ASP   A N   
2306 N N   B ASP   A 105 ? 0.3146 0.3979 0.1958 -0.0073 0.0122  0.0170  105 ASP   A N   
2307 C CA  A ASP   A 105 ? 0.2851 0.3851 0.2328 -0.0199 0.0051  -0.0314 105 ASP   A CA  
2308 C CA  B ASP   A 105 ? 0.3004 0.3903 0.2198 0.0012  0.0201  -0.0159 105 ASP   A CA  
2309 C C   A ASP   A 105 ? 0.2578 0.3717 0.1986 -0.0300 -0.0102 -0.0510 105 ASP   A C   
2310 C C   B ASP   A 105 ? 0.2832 0.3684 0.1845 -0.0100 0.0231  -0.0304 105 ASP   A C   
2311 O O   A ASP   A 105 ? 0.2485 0.3742 0.1692 -0.0340 -0.0205 -0.0630 105 ASP   A O   
2312 O O   B ASP   A 105 ? 0.2642 0.3591 0.1246 -0.0061 0.0286  -0.0438 105 ASP   A O   
2313 C CB  A ASP   A 105 ? 0.3081 0.3985 0.2897 -0.0047 0.0158  -0.0365 105 ASP   A CB  
2314 C CB  B ASP   A 105 ? 0.3013 0.4041 0.2776 0.0187  0.0242  -0.0332 105 ASP   A CB  
2315 C CG  A ASP   A 105 ? 0.3268 0.4107 0.3385 0.0071  0.0192  -0.0433 105 ASP   A CG  
2316 C CG  B ASP   A 105 ? 0.3002 0.4151 0.3288 0.0333  0.0252  -0.0555 105 ASP   A CG  
2317 O OD1 A ASP   A 105 ? 0.3290 0.4140 0.3490 0.0124  0.0226  -0.0542 105 ASP   A OD1 
2318 O OD1 B ASP   A 105 ? 0.2967 0.4182 0.3309 0.0363  0.0205  -0.0669 105 ASP   A OD1 
2319 O OD2 A ASP   A 105 ? 0.3370 0.4167 0.3740 0.0092  0.0169  -0.0388 105 ASP   A OD2 
2320 O OD2 B ASP   A 105 ? 0.3036 0.4205 0.3563 0.0373  0.0318  -0.0613 105 ASP   A OD2 
2329 N N   A ILE   A 106 ? 0.2383 0.3541 0.2041 -0.0378 -0.0250 -0.0588 106 ILE   A N   
2330 N N   B ILE   A 106 ? 0.2860 0.3560 0.2143 -0.0216 0.0024  -0.0323 106 ILE   A N   
2331 C CA  A ILE   A 106 ? 0.2127 0.3301 0.2057 -0.0454 -0.0364 -0.0760 106 ILE   A CA  
2332 C CA  B ILE   A 106 ? 0.2871 0.3409 0.2359 -0.0381 -0.0111 -0.0375 106 ILE   A CA  
2333 C C   A ILE   A 106 ? 0.1906 0.3082 0.2044 -0.0600 -0.0357 -0.1014 106 ILE   A C   
2334 C C   B ILE   A 106 ? 0.2903 0.3227 0.2265 -0.0447 -0.0014 -0.0271 106 ILE   A C   
2335 O O   A ILE   A 106 ? 0.1706 0.2929 0.2122 -0.0632 -0.0250 -0.1069 106 ILE   A O   
2336 O O   B ILE   A 106 ? 0.2838 0.3185 0.2243 -0.0486 0.0081  -0.0191 106 ILE   A O   
2337 C CB  A ILE   A 106 ? 0.2107 0.3270 0.2210 -0.0331 -0.0477 -0.0590 106 ILE   A CB  
2338 C CB  B ILE   A 106 ? 0.2866 0.3453 0.2748 -0.0462 -0.0296 -0.0447 106 ILE   A CB  
2339 C CG1 A ILE   A 106 ? 0.2080 0.3170 0.2415 -0.0226 -0.0462 -0.0505 106 ILE   A CG1 
2340 C CG1 B ILE   A 106 ? 0.2803 0.3468 0.2927 -0.0431 -0.0386 -0.0482 106 ILE   A CG1 
2341 C CG2 A ILE   A 106 ? 0.2115 0.3304 0.2251 -0.0309 -0.0590 -0.0528 106 ILE   A CG2 
2342 C CG2 B ILE   A 106 ? 0.2913 0.3486 0.2811 -0.0506 -0.0344 -0.0467 106 ILE   A CG2 
2343 C CD1 A ILE   A 106 ? 0.2077 0.3096 0.2461 -0.0151 -0.0410 -0.0432 106 ILE   A CD1 
2344 C CD1 B ILE   A 106 ? 0.2748 0.3465 0.3071 -0.0429 -0.0430 -0.0455 106 ILE   A CD1 
2367 N N   A GLN   A 107 ? 0.2016 0.2998 0.2283 -0.0606 -0.0230 -0.1134 107 GLN   A N   
2368 N N   B GLN   A 107 ? 0.3022 0.3095 0.2445 -0.0407 0.0042  -0.0261 107 GLN   A N   
2369 C CA  A GLN   A 107 ? 0.2158 0.2864 0.2709 -0.0488 0.0017  -0.1075 107 GLN   A CA  
2370 C CA  B GLN   A 107 ? 0.3209 0.3005 0.2968 -0.0370 0.0110  -0.0157 107 GLN   A CA  
2371 C C   A GLN   A 107 ? 0.1913 0.2475 0.2523 -0.0374 0.0252  -0.0900 107 GLN   A C   
2372 C C   B GLN   A 107 ? 0.2906 0.2509 0.2566 -0.0305 0.0206  0.0031  107 GLN   A C   
2373 O O   A GLN   A 107 ? 0.1966 0.2450 0.3007 -0.0277 0.0451  -0.0860 107 GLN   A O   
2374 O O   B GLN   A 107 ? 0.2955 0.2385 0.2653 -0.0392 0.0179  -0.0010 107 GLN   A O   
2375 C CB  A GLN   A 107 ? 0.2549 0.3103 0.3511 -0.0483 -0.0087 -0.1050 107 GLN   A CB  
2376 C CB  B GLN   A 107 ? 0.3639 0.3425 0.3929 -0.0417 -0.0005 -0.0181 107 GLN   A CB  
2377 C CG  A GLN   A 107 ? 0.2925 0.3363 0.4418 -0.0389 -0.0144 -0.0881 107 GLN   A CG  
2378 C CG  B GLN   A 107 ? 0.4038 0.3820 0.4920 -0.0436 -0.0140 -0.0110 107 GLN   A CG  
2379 C CD  A GLN   A 107 ? 0.3287 0.3567 0.5191 -0.0288 -0.0149 -0.0682 107 GLN   A CD  
2380 C CD  B GLN   A 107 ? 0.4408 0.4139 0.5782 -0.0470 -0.0234 -0.0006 107 GLN   A CD  
2381 O OE1 A GLN   A 107 ? 0.3376 0.3647 0.5506 -0.0265 -0.0138 -0.0595 107 GLN   A OE1 
2382 O OE1 B GLN   A 107 ? 0.4485 0.4234 0.6114 -0.0507 -0.0271 0.0031  107 GLN   A OE1 
2383 N NE2 A GLN   A 107 ? 0.3334 0.3623 0.5444 -0.0244 -0.0139 -0.0649 107 GLN   A NE2 
2384 N NE2 B GLN   A 107 ? 0.4461 0.4240 0.6075 -0.0470 -0.0283 0.0012  107 GLN   A NE2 
2401 N N   A LEU   A 108 ? 0.1627 0.2035 0.1906 -0.0327 0.0223  -0.0818 108 LEU   A N   
2402 N N   B LEU   A 108 ? 0.2543 0.2144 0.2045 -0.0171 0.0240  0.0103  108 LEU   A N   
2403 C CA  A LEU   A 108 ? 0.1474 0.1722 0.1730 -0.0184 0.0189  -0.0453 108 LEU   A CA  
2404 C CA  B LEU   A 108 ? 0.2246 0.1847 0.1890 -0.0009 0.0275  0.0135  108 LEU   A CA  
2405 C C   A LEU   A 108 ? 0.1304 0.1456 0.1650 -0.0073 0.0186  -0.0237 108 LEU   A C   
2406 C C   B LEU   A 108 ? 0.1967 0.1609 0.1768 0.0005  0.0211  0.0157  108 LEU   A C   
2407 O O   A LEU   A 108 ? 0.1302 0.1415 0.1689 -0.0046 0.0236  -0.0108 108 LEU   A O   
2408 O O   B LEU   A 108 ? 0.1993 0.1656 0.1865 0.0012  0.0299  0.0220  108 LEU   A O   
2409 C CB  A LEU   A 108 ? 0.1539 0.1794 0.1593 -0.0272 0.0232  -0.0304 108 LEU   A CB  
2410 C CB  B LEU   A 108 ? 0.2244 0.1915 0.1704 0.0065  0.0349  0.0130  108 LEU   A CB  
2411 C CG  A LEU   A 108 ? 0.1647 0.1927 0.1749 -0.0277 0.0241  -0.0205 108 LEU   A CG  
2412 C CG  B LEU   A 108 ? 0.2319 0.2043 0.1943 0.0194  0.0410  0.0111  108 LEU   A CG  
2413 C CD1 A LEU   A 108 ? 0.1728 0.1970 0.1740 -0.0266 0.0229  -0.0142 108 LEU   A CD1 
2414 C CD1 B LEU   A 108 ? 0.2337 0.2114 0.1941 0.0187  0.0465  0.0141  108 LEU   A CD1 
2415 C CD2 A LEU   A 108 ? 0.1698 0.1979 0.1959 -0.0251 0.0303  -0.0091 108 LEU   A CD2 
2416 C CD2 B LEU   A 108 ? 0.2393 0.2097 0.2303 0.0298  0.0397  0.0135  108 LEU   A CD2 
2439 N N   A LEU   A 109 ? 0.1233 0.1454 0.1691 -0.0020 0.0126  -0.0088 109 LEU   A N   
2440 N N   B LEU   A 109 ? 0.1760 0.1543 0.1721 -0.0007 0.0088  0.0181  109 LEU   A N   
2441 C CA  A LEU   A 109 ? 0.1339 0.1427 0.1662 -0.0040 0.0077  -0.0013 109 LEU   A CA  
2442 C CA  B LEU   A 109 ? 0.1636 0.1438 0.1681 -0.0022 0.0047  0.0260  109 LEU   A CA  
2443 C C   A LEU   A 109 ? 0.1347 0.1359 0.1680 -0.0067 0.0058  -0.0032 109 LEU   A C   
2444 C C   B LEU   A 109 ? 0.1483 0.1359 0.1609 -0.0094 0.0027  0.0162  109 LEU   A C   
2445 O O   A LEU   A 109 ? 0.1357 0.1296 0.1846 -0.0023 0.0042  -0.0153 109 LEU   A O   
2446 O O   B LEU   A 109 ? 0.1492 0.1283 0.1722 -0.0095 -0.0026 0.0134  109 LEU   A O   
2447 C CB  A LEU   A 109 ? 0.1391 0.1527 0.1774 0.0032  0.0026  0.0085  109 LEU   A CB  
2448 C CB  B LEU   A 109 ? 0.1615 0.1453 0.1846 0.0018  0.0048  0.0290  109 LEU   A CB  
2449 C CG  A LEU   A 109 ? 0.1380 0.1556 0.1821 0.0014  -0.0023 0.0060  109 LEU   A CG  
2450 C CG  B LEU   A 109 ? 0.1548 0.1440 0.1918 -0.0020 0.0052  0.0296  109 LEU   A CG  
2451 C CD1 A LEU   A 109 ? 0.1389 0.1537 0.1831 0.0042  0.0076  0.0023  109 LEU   A CD1 
2452 C CD1 B LEU   A 109 ? 0.1529 0.1390 0.1899 0.0003  0.0016  0.0212  109 LEU   A CD1 
2453 C CD2 A LEU   A 109 ? 0.1391 0.1654 0.1896 -0.0046 -0.0083 0.0083  109 LEU   A CD2 
2454 C CD2 B LEU   A 109 ? 0.1525 0.1487 0.2044 -0.0058 0.0141  0.0216  109 LEU   A CD2 
2477 N N   . LYS   A 110 ? 0.1404 0.1349 0.1632 -0.0066 -0.0040 0.0020  110 LYS   A N   
2478 C CA  . LYS   A 110 ? 0.1397 0.1312 0.1763 -0.0091 -0.0047 0.0036  110 LYS   A CA  
2479 C C   . LYS   A 110 ? 0.1434 0.1275 0.1515 -0.0089 0.0081  -0.0062 110 LYS   A C   
2480 O O   . LYS   A 110 ? 0.1365 0.1266 0.1652 -0.0041 0.0060  -0.0069 110 LYS   A O   
2481 C CB  . LYS   A 110 ? 0.1457 0.1351 0.1942 -0.0045 -0.0105 -0.0101 110 LYS   A CB  
2482 C CG  . LYS   A 110 ? 0.1439 0.1384 0.2040 -0.0025 -0.0124 -0.0052 110 LYS   A CG  
2483 C CD  . LYS   A 110 ? 0.1493 0.1429 0.2203 -0.0070 -0.0133 -0.0149 110 LYS   A CD  
2484 C CE  . LYS   A 110 ? 0.1602 0.1452 0.2375 -0.0049 0.0062  -0.0131 110 LYS   A CE  
2485 N NZ  . LYS   A 110 ? 0.1625 0.1491 0.2513 -0.0177 0.0099  -0.0115 110 LYS   A NZ  
2500 N N   . SER   A 111 ? 0.1417 0.1294 0.1557 -0.0004 0.0030  0.0021  111 SER   A N   
2501 C CA  . SER   A 111 ? 0.1327 0.1323 0.1617 -0.0042 0.0082  -0.0006 111 SER   A CA  
2502 C C   . SER   A 111 ? 0.1306 0.1256 0.1461 -0.0058 0.0047  0.0097  111 SER   A C   
2503 O O   . SER   A 111 ? 0.1466 0.1176 0.1648 -0.0036 0.0108  0.0094  111 SER   A O   
2504 C CB  . SER   A 111 ? 0.1534 0.1529 0.1804 -0.0027 0.0150  -0.0064 111 SER   A CB  
2505 O OG  . SER   A 111 ? 0.1972 0.1694 0.1997 0.0049  0.0275  -0.0226 111 SER   A OG  
2511 N N   . ALA   A 112 ? 0.1333 0.1239 0.1566 -0.0049 0.0095  0.0079  112 ALA   A N   
2512 C CA  . ALA   A 112 ? 0.1439 0.1174 0.1513 -0.0059 0.0122  0.0020  112 ALA   A CA  
2513 C C   . ALA   A 112 ? 0.1370 0.1124 0.1523 -0.0035 0.0093  0.0033  112 ALA   A C   
2514 O O   . ALA   A 112 ? 0.1360 0.1165 0.1634 -0.0132 0.0134  0.0092  112 ALA   A O   
2515 C CB  . ALA   A 112 ? 0.1480 0.1222 0.1628 -0.0064 0.0122  0.0034  112 ALA   A CB  
2521 N N   . TYR   A 113 ? 0.1233 0.1187 0.1687 -0.0018 0.0109  0.0081  113 TYR   A N   
2522 C CA  . TYR   A 113 ? 0.1198 0.1171 0.1635 -0.0006 0.0151  0.0136  113 TYR   A CA  
2523 C C   . TYR   A 113 ? 0.1176 0.1203 0.1553 -0.0064 0.0101  0.0126  113 TYR   A C   
2524 O O   . TYR   A 113 ? 0.1261 0.1234 0.1682 -0.0053 0.0169  0.0108  113 TYR   A O   
2525 C CB  . TYR   A 113 ? 0.1253 0.1220 0.1668 -0.0040 0.0112  0.0182  113 TYR   A CB  
2526 C CG  . TYR   A 113 ? 0.1280 0.1270 0.1587 -0.0078 0.0140  0.0183  113 TYR   A CG  
2527 C CD1 . TYR   A 113 ? 0.1328 0.1331 0.1544 -0.0027 0.0066  0.0223  113 TYR   A CD1 
2528 C CD2 . TYR   A 113 ? 0.1327 0.1370 0.1608 -0.0091 0.0066  0.0188  113 TYR   A CD2 
2529 C CE1 . TYR   A 113 ? 0.1336 0.1367 0.1650 -0.0049 0.0087  0.0207  113 TYR   A CE1 
2530 C CE2 . TYR   A 113 ? 0.1273 0.1425 0.1618 -0.0097 -0.0012 0.0234  113 TYR   A CE2 
2531 C CZ  . TYR   A 113 ? 0.1342 0.1415 0.1613 -0.0025 0.0082  0.0299  113 TYR   A CZ  
2532 O OH  . TYR   A 113 ? 0.1288 0.1443 0.1843 0.0114  0.0110  0.0151  113 TYR   A OH  
2542 N N   . GLU   A 114 ? 0.1196 0.1190 0.1624 -0.0019 0.0117  0.0137  114 GLU   A N   
2543 C CA  . GLU   A 114 ? 0.1274 0.1139 0.1743 0.0022  0.0096  0.0139  114 GLU   A CA  
2544 C C   . GLU   A 114 ? 0.1203 0.1216 0.1714 0.0027  0.0141  0.0122  114 GLU   A C   
2545 O O   . GLU   A 114 ? 0.1263 0.1213 0.1691 -0.0004 0.0036  0.0125  114 GLU   A O   
2546 C CB  . GLU   A 114 ? 0.1266 0.1198 0.1777 0.0013  0.0063  0.0164  114 GLU   A CB  
2547 C CG  . GLU   A 114 ? 0.1380 0.1192 0.1899 0.0024  0.0101  0.0083  114 GLU   A CG  
2548 C CD  . GLU   A 114 ? 0.1417 0.1193 0.1852 -0.0019 0.0102  0.0108  114 GLU   A CD  
2549 O OE1 . GLU   A 114 ? 0.1468 0.1244 0.1906 -0.0052 0.0148  -0.0062 114 GLU   A OE1 
2550 O OE2 . GLU   A 114 ? 0.1628 0.1273 0.2099 -0.0128 0.0112  -0.0105 114 GLU   A OE2 
2557 N N   . ASN   A 115 ? 0.1211 0.1201 0.1607 -0.0045 0.0115  0.0065  115 ASN   A N   
2558 C CA  . ASN   A 115 ? 0.1284 0.1220 0.1628 -0.0092 0.0131  0.0109  115 ASN   A CA  
2559 C C   . ASN   A 115 ? 0.1267 0.1177 0.1619 -0.0070 0.0027  0.0089  115 ASN   A C   
2560 O O   . ASN   A 115 ? 0.1288 0.1350 0.1581 -0.0111 0.0105  0.0223  115 ASN   A O   
2561 C CB  . ASN   A 115 ? 0.1370 0.1293 0.1569 -0.0168 0.0091  0.0084  115 ASN   A CB  
2562 C CG  . ASN   A 115 ? 0.1372 0.1502 0.1634 -0.0133 0.0220  0.0110  115 ASN   A CG  
2563 O OD1 . ASN   A 115 ? 0.1391 0.2541 0.1929 -0.0140 0.0234  0.0265  115 ASN   A OD1 
2564 N ND2 . ASN   A 115 ? 0.1398 0.1349 0.1611 -0.0113 0.0251  0.0163  115 ASN   A ND2 
2571 N N   . PHE   A 116 ? 0.1207 0.1224 0.1657 -0.0025 0.0129  0.0182  116 PHE   A N   
2572 C CA  . PHE   A 116 ? 0.1256 0.1269 0.1467 -0.0045 0.0139  0.0139  116 PHE   A CA  
2573 C C   . PHE   A 116 ? 0.1252 0.1338 0.1540 -0.0080 0.0083  0.0213  116 PHE   A C   
2574 O O   . PHE   A 116 ? 0.1301 0.1415 0.1684 0.0030  0.0143  0.0337  116 PHE   A O   
2575 C CB  . PHE   A 116 ? 0.1286 0.1227 0.1582 -0.0055 0.0167  0.0075  116 PHE   A CB  
2576 C CG  . PHE   A 116 ? 0.1262 0.1224 0.1517 -0.0032 0.0162  0.0109  116 PHE   A CG  
2577 C CD1 . PHE   A 116 ? 0.1319 0.1198 0.1572 -0.0066 0.0195  0.0137  116 PHE   A CD1 
2578 C CD2 . PHE   A 116 ? 0.1296 0.1328 0.1628 -0.0059 0.0221  0.0207  116 PHE   A CD2 
2579 C CE1 . PHE   A 116 ? 0.1362 0.1159 0.1655 -0.0126 0.0133  0.0119  116 PHE   A CE1 
2580 C CE2 . PHE   A 116 ? 0.1299 0.1308 0.1719 -0.0021 0.0161  0.0162  116 PHE   A CE2 
2581 C CZ  . PHE   A 116 ? 0.1370 0.1163 0.1589 -0.0014 0.0038  0.0122  116 PHE   A CZ  
2591 N N   . ASN   A 117 ? 0.1271 0.1301 0.1672 -0.0027 0.0095  0.0274  117 ASN   A N   
2592 C CA  . ASN   A 117 ? 0.1257 0.1308 0.1854 -0.0037 0.0131  0.0264  117 ASN   A CA  
2593 C C   . ASN   A 117 ? 0.1291 0.1366 0.1899 0.0021  0.0146  0.0281  117 ASN   A C   
2594 O O   . ASN   A 117 ? 0.1365 0.1445 0.2109 -0.0041 -0.0061 0.0421  117 ASN   A O   
2595 C CB  . ASN   A 117 ? 0.1220 0.1346 0.1921 0.0005  0.0144  0.0328  117 ASN   A CB  
2596 C CG  . ASN   A 117 ? 0.1271 0.1326 0.1881 -0.0015 0.0179  0.0327  117 ASN   A CG  
2597 O OD1 . ASN   A 117 ? 0.1296 0.1518 0.2013 -0.0152 0.0152  0.0186  117 ASN   A OD1 
2598 N ND2 . ASN   A 117 ? 0.1240 0.1262 0.1922 -0.0053 0.0131  0.0213  117 ASN   A ND2 
2605 N N   . GLN   A 118 ? 0.1247 0.1344 0.1882 -0.0077 0.0017  0.0272  118 GLN   A N   
2606 C CA  . GLN   A 118 ? 0.1329 0.1449 0.1901 -0.0027 0.0003  0.0278  118 GLN   A CA  
2607 C C   . GLN   A 118 ? 0.1363 0.1551 0.1785 -0.0067 0.0007  0.0322  118 GLN   A C   
2608 O O   . GLN   A 118 ? 0.1377 0.1849 0.2081 -0.0022 -0.0101 0.0091  118 GLN   A O   
2609 C CB  . GLN   A 118 ? 0.1284 0.1455 0.2025 -0.0013 0.0102  0.0225  118 GLN   A CB  
2610 C CG  . GLN   A 118 ? 0.1276 0.1479 0.2011 -0.0056 0.0149  0.0296  118 GLN   A CG  
2611 C CD  . GLN   A 118 ? 0.1254 0.1528 0.2220 0.0004  0.0111  0.0220  118 GLN   A CD  
2612 O OE1 . GLN   A 118 ? 0.1358 0.1644 0.2282 0.0110  0.0062  0.0140  118 GLN   A OE1 
2613 N NE2 . GLN   A 118 ? 0.1350 0.1498 0.2250 0.0053  0.0091  0.0314  118 GLN   A NE2 
2622 N N   . HIS   A 119 ? 0.1388 0.1553 0.1683 -0.0054 0.0059  0.0357  119 HIS   A N   
2623 C CA  . HIS   A 119 ? 0.1470 0.1661 0.1642 -0.0057 0.0020  0.0413  119 HIS   A CA  
2624 C C   . HIS   A 119 ? 0.1471 0.1702 0.1704 -0.0027 0.0119  0.0404  119 HIS   A C   
2625 O O   . HIS   A 119 ? 0.1540 0.1769 0.1751 -0.0203 0.0030  0.0440  119 HIS   A O   
2626 C CB  . HIS   A 119 ? 0.1491 0.1600 0.1806 -0.0070 0.0159  0.0396  119 HIS   A CB  
2627 C CG  . HIS   A 119 ? 0.1526 0.1646 0.2222 0.0019  0.0139  0.0446  119 HIS   A CG  
2628 N ND1 . HIS   A 119 ? 0.1654 0.1801 0.2820 -0.0063 0.0112  0.0285  119 HIS   A ND1 
2629 C CD2 . HIS   A 119 ? 0.1624 0.1688 0.2465 0.0139  0.0364  0.0636  119 HIS   A CD2 
2630 C CE1 . HIS   A 119 ? 0.1651 0.1699 0.3007 -0.0142 0.0238  0.0441  119 HIS   A CE1 
2631 N NE2 . HIS   A 119 ? 0.1723 0.1666 0.2843 0.0044  0.0388  0.0677  119 HIS   A NE2 
2639 N N   . GLU   A 120 ? 0.1563 0.1905 0.1717 -0.0028 0.0042  0.0671  120 GLU   A N   
2640 C CA  . GLU   A 120 ? 0.1952 0.2338 0.2012 0.0050  0.0017  0.1074  120 GLU   A CA  
2641 C C   . GLU   A 120 ? 0.1697 0.2148 0.1757 -0.0069 0.0022  0.0987  120 GLU   A C   
2642 O O   . GLU   A 120 ? 0.1651 0.2054 0.2002 -0.0162 0.0052  0.0890  120 GLU   A O   
2643 C CB  . GLU   A 120 ? 0.2897 0.3250 0.2567 0.0219  -0.0038 0.1644  120 GLU   A CB  
2644 C CG  . GLU   A 120 ? 0.3948 0.4142 0.3990 0.0272  -0.0065 0.1689  120 GLU   A CG  
2645 C CD  . GLU   A 120 ? 0.5080 0.5166 0.5448 0.0283  0.0017  0.1533  120 GLU   A CD  
2646 O OE1 . GLU   A 120 ? 0.5268 0.5288 0.5705 0.0287  0.0058  0.1472  120 GLU   A OE1 
2647 O OE2 . GLU   A 120 ? 0.5602 0.5602 0.6126 0.0280  0.0054  0.1455  120 GLU   A OE2 
2654 N N   . VAL   A 121 ? 0.1623 0.2123 0.1493 -0.0125 0.0080  0.0722  121 VAL   A N   
2655 C CA  . VAL   A 121 ? 0.1706 0.2183 0.1441 -0.0167 0.0162  0.0623  121 VAL   A CA  
2656 C C   . VAL   A 121 ? 0.1572 0.1956 0.1292 -0.0252 0.0089  0.0531  121 VAL   A C   
2657 O O   . VAL   A 121 ? 0.1610 0.1968 0.1464 -0.0279 -0.0062 0.0441  121 VAL   A O   
2658 C CB  . VAL   A 121 ? 0.2068 0.2587 0.1809 -0.0038 0.0280  0.0678  121 VAL   A CB  
2659 C CG1 . VAL   A 121 ? 0.2079 0.2749 0.1755 0.0066  0.0353  0.0778  121 VAL   A CG1 
2660 C CG2 . VAL   A 121 ? 0.2296 0.2755 0.2207 -0.0120 0.0216  0.0516  121 VAL   A CG2 
2670 N N   . LEU   A 122 ? 0.1488 0.1684 0.1473 -0.0247 0.0103  0.0420  122 LEU   A N   
2671 C CA  . LEU   A 122 ? 0.1551 0.1556 0.1462 -0.0195 0.0197  0.0363  122 LEU   A CA  
2672 C C   . LEU   A 122 ? 0.1495 0.1543 0.1359 -0.0200 0.0093  0.0351  122 LEU   A C   
2673 O O   . LEU   A 122 ? 0.1521 0.1588 0.1707 -0.0254 0.0061  0.0340  122 LEU   A O   
2674 C CB  . LEU   A 122 ? 0.1694 0.1579 0.1754 -0.0065 0.0114  0.0493  122 LEU   A CB  
2675 C CG  . LEU   A 122 ? 0.1694 0.1628 0.1810 -0.0074 0.0182  0.0346  122 LEU   A CG  
2676 C CD1 . LEU   A 122 ? 0.1862 0.1661 0.1945 -0.0153 0.0235  0.0329  122 LEU   A CD1 
2677 C CD2 . LEU   A 122 ? 0.1623 0.1517 0.1594 -0.0032 0.0340  0.0288  122 LEU   A CD2 
2689 N N   A LEU   A 123 ? 0.1415 0.1533 0.1362 -0.0226 0.0107  0.0371  123 LEU   A N   
2690 N N   B LEU   A 123 ? 0.1413 0.1526 0.1469 -0.0225 0.0024  0.0323  123 LEU   A N   
2691 C CA  A LEU   A 123 ? 0.1423 0.1516 0.1306 -0.0211 0.0163  0.0367  123 LEU   A CA  
2692 C CA  B LEU   A 123 ? 0.1464 0.1532 0.1440 -0.0213 0.0028  0.0276  123 LEU   A CA  
2693 C C   A LEU   A 123 ? 0.1350 0.1399 0.1219 -0.0187 0.0171  0.0336  123 LEU   A C   
2694 C C   B LEU   A 123 ? 0.1460 0.1424 0.1306 -0.0199 0.0037  0.0241  123 LEU   A C   
2695 O O   A LEU   A 123 ? 0.1249 0.1350 0.1217 -0.0243 0.0224  0.0268  123 LEU   A O   
2696 O O   B LEU   A 123 ? 0.1385 0.1423 0.1299 -0.0172 0.0056  0.0195  123 LEU   A O   
2697 C CB  A LEU   A 123 ? 0.1528 0.1637 0.1260 -0.0228 0.0237  0.0350  123 LEU   A CB  
2698 C CB  B LEU   A 123 ? 0.1519 0.1637 0.1327 -0.0234 0.0044  0.0200  123 LEU   A CB  
2699 C CG  A LEU   A 123 ? 0.1630 0.1767 0.1404 -0.0162 0.0234  0.0210  123 LEU   A CG  
2700 C CG  B LEU   A 123 ? 0.1564 0.1722 0.1387 -0.0210 0.0105  0.0152  123 LEU   A CG  
2701 C CD1 A LEU   A 123 ? 0.1664 0.1843 0.1586 -0.0108 0.0203  0.0149  123 LEU   A CD1 
2702 C CD1 B LEU   A 123 ? 0.1623 0.1773 0.1675 -0.0170 0.0125  0.0088  123 LEU   A CD1 
2703 C CD2 A LEU   A 123 ? 0.1706 0.1819 0.1439 -0.0156 0.0161  0.0158  123 LEU   A CD2 
2704 C CD2 B LEU   A 123 ? 0.1630 0.1778 0.1476 -0.0208 0.0081  0.0144  123 LEU   A CD2 
2727 N N   A ALA   A 124 ? 0.1315 0.1344 0.1211 -0.0127 0.0177  0.0324  124 ALA   A N   
2728 N N   B ALA   A 124 ? 0.1469 0.1294 0.1310 -0.0195 0.0078  0.0189  124 ALA   A N   
2729 C CA  A ALA   A 124 ? 0.1193 0.1257 0.1189 -0.0049 0.0112  0.0264  124 ALA   A CA  
2730 C CA  B ALA   A 124 ? 0.1401 0.1287 0.1450 -0.0183 0.0013  0.0234  124 ALA   A CA  
2731 C C   A ALA   A 124 ? 0.1167 0.1292 0.1211 -0.0068 0.0146  0.0178  124 ALA   A C   
2732 C C   B ALA   A 124 ? 0.1335 0.1277 0.1406 -0.0142 0.0049  0.0258  124 ALA   A C   
2733 O O   A ALA   A 124 ? 0.1185 0.1336 0.1394 -0.0113 0.0255  0.0261  124 ALA   A O   
2734 O O   B ALA   A 124 ? 0.1298 0.1309 0.1622 -0.0100 0.0131  0.0302  124 ALA   A O   
2735 C CB  A ALA   A 124 ? 0.1171 0.1228 0.1310 0.0058  0.0086  0.0240  124 ALA   A CB  
2736 C CB  B ALA   A 124 ? 0.1448 0.1328 0.1627 -0.0165 0.0078  0.0198  124 ALA   A CB  
2747 N N   A PRO   A 125 ? 0.1162 0.1345 0.1374 -0.0054 0.0108  0.0169  125 PRO   A N   
2748 N N   B PRO   A 125 ? 0.1240 0.1273 0.1285 -0.0134 0.0076  0.0326  125 PRO   A N   
2749 C CA  A PRO   A 125 ? 0.1239 0.1365 0.1419 -0.0062 -0.0036 0.0151  125 PRO   A CA  
2750 C CA  B PRO   A 125 ? 0.1264 0.1301 0.1324 -0.0110 0.0009  0.0223  125 PRO   A CA  
2751 C C   A PRO   A 125 ? 0.1131 0.1324 0.1378 -0.0118 -0.0025 0.0325  125 PRO   A C   
2752 C C   B PRO   A 125 ? 0.1322 0.1396 0.1405 -0.0068 0.0056  0.0217  125 PRO   A C   
2753 O O   A PRO   A 125 ? 0.1196 0.1319 0.1439 -0.0058 -0.0054 0.0258  125 PRO   A O   
2754 O O   B PRO   A 125 ? 0.1402 0.1395 0.1548 -0.0031 0.0048  0.0103  125 PRO   A O   
2755 C CB  A PRO   A 125 ? 0.1350 0.1412 0.1452 -0.0054 0.0077  0.0082  125 PRO   A CB  
2756 C CB  B PRO   A 125 ? 0.1194 0.1303 0.1268 -0.0149 0.0076  0.0290  125 PRO   A CB  
2757 C CG  A PRO   A 125 ? 0.1394 0.1385 0.1424 -0.0033 0.0072  0.0125  125 PRO   A CG  
2758 C CG  B PRO   A 125 ? 0.1182 0.1195 0.1168 -0.0055 0.0158  0.0263  125 PRO   A CG  
2759 C CD  A PRO   A 125 ? 0.1237 0.1371 0.1384 -0.0018 0.0116  0.0023  125 PRO   A CD  
2760 C CD  B PRO   A 125 ? 0.1159 0.1173 0.1249 -0.0081 0.0146  0.0296  125 PRO   A CD  
2775 N N   A LEU   A 126 ? 0.1093 0.1364 0.1382 -0.0120 -0.0008 0.0337  126 LEU   A N   
2776 N N   B LEU   A 126 ? 0.1428 0.1485 0.1525 0.0014  0.0048  0.0109  126 LEU   A N   
2777 C CA  A LEU   A 126 ? 0.1170 0.1390 0.1364 -0.0143 -0.0024 0.0285  126 LEU   A CA  
2778 C CA  B LEU   A 126 ? 0.1442 0.1468 0.1611 0.0024  0.0016  0.0095  126 LEU   A CA  
2779 C C   A LEU   A 126 ? 0.1313 0.1336 0.1275 -0.0081 -0.0064 0.0239  126 LEU   A C   
2780 C C   B LEU   A 126 ? 0.1415 0.1372 0.1535 0.0082  -0.0102 -0.0039 126 LEU   A C   
2781 O O   A LEU   A 126 ? 0.1340 0.1260 0.1408 0.0012  0.0066  0.0342  126 LEU   A O   
2782 O O   B LEU   A 126 ? 0.1509 0.1433 0.1793 0.0069  -0.0189 0.0011  126 LEU   A O   
2783 C CB  A LEU   A 126 ? 0.1185 0.1437 0.1330 -0.0183 -0.0069 0.0219  126 LEU   A CB  
2784 C CB  B LEU   A 126 ? 0.1593 0.1701 0.2119 -0.0075 -0.0131 0.0136  126 LEU   A CB  
2785 C CG  A LEU   A 126 ? 0.1145 0.1575 0.1394 -0.0281 -0.0046 0.0200  126 LEU   A CG  
2786 C CG  B LEU   A 126 ? 0.1734 0.1874 0.2438 -0.0152 -0.0196 0.0206  126 LEU   A CG  
2787 C CD1 A LEU   A 126 ? 0.1175 0.1688 0.1585 -0.0270 -0.0123 0.0245  126 LEU   A CD1 
2788 C CD1 B LEU   A 126 ? 0.1743 0.1924 0.2441 -0.0196 -0.0134 0.0153  126 LEU   A CD1 
2789 C CD2 A LEU   A 126 ? 0.1279 0.1603 0.1406 -0.0368 -0.0071 0.0260  126 LEU   A CD2 
2790 C CD2 B LEU   A 126 ? 0.1775 0.1904 0.2475 -0.0223 -0.0241 0.0284  126 LEU   A CD2 
2813 N N   A LEU   A 127 ? 0.1422 0.1434 0.1374 -0.0058 0.0088  0.0217  127 LEU   A N   
2814 N N   B LEU   A 127 ? 0.1469 0.1378 0.1635 0.0215  -0.0012 0.0076  127 LEU   A N   
2815 C CA  A LEU   A 127 ? 0.1438 0.1398 0.1365 -0.0066 0.0088  0.0114  127 LEU   A CA  
2816 C CA  B LEU   A 127 ? 0.1491 0.1395 0.1546 0.0137  -0.0062 0.0150  127 LEU   A CA  
2817 C C   A LEU   A 127 ? 0.1454 0.1365 0.1430 -0.0070 0.0083  0.0133  127 LEU   A C   
2818 C C   B LEU   A 127 ? 0.1475 0.1325 0.1395 -0.0001 -0.0140 0.0074  127 LEU   A C   
2819 O O   A LEU   A 127 ? 0.1496 0.1381 0.1424 -0.0103 0.0147  0.0194  127 LEU   A O   
2820 O O   B LEU   A 127 ? 0.1568 0.1355 0.1502 -0.0031 -0.0179 -0.0055 127 LEU   A O   
2821 C CB  A LEU   A 127 ? 0.1484 0.1367 0.1439 0.0043  0.0078  0.0027  127 LEU   A CB  
2822 C CB  B LEU   A 127 ? 0.1541 0.1571 0.1545 0.0239  0.0010  0.0189  127 LEU   A CB  
2823 C CG  A LEU   A 127 ? 0.1528 0.1253 0.1463 0.0039  0.0054  0.0047  127 LEU   A CG  
2824 C CG  B LEU   A 127 ? 0.1619 0.1718 0.1507 0.0199  -0.0071 0.0226  127 LEU   A CG  
2825 C CD1 A LEU   A 127 ? 0.1475 0.1096 0.1635 -0.0034 0.0054  -0.0141 127 LEU   A CD1 
2826 C CD1 B LEU   A 127 ? 0.1649 0.1802 0.1577 0.0231  0.0090  0.0293  127 LEU   A CD1 
2827 C CD2 A LEU   A 127 ? 0.1631 0.1162 0.1532 0.0180  0.0023  0.0122  127 LEU   A CD2 
2828 C CD2 B LEU   A 127 ? 0.1768 0.1863 0.1522 0.0144  -0.0212 0.0106  127 LEU   A CD2 
2851 N N   A SER   A 128 ? 0.1531 0.1409 0.1464 -0.0072 0.0002  0.0140  128 SER   A N   
2852 N N   B SER   A 128 ? 0.1517 0.1332 0.1400 -0.0051 -0.0159 0.0112  128 SER   A N   
2853 C CA  A SER   A 128 ? 0.1604 0.1454 0.1407 -0.0052 -0.0053 0.0097  128 SER   A CA  
2854 C CA  B SER   A 128 ? 0.1652 0.1379 0.1452 -0.0034 -0.0184 0.0171  128 SER   A CA  
2855 C C   A SER   A 128 ? 0.1732 0.1483 0.1448 0.0017  -0.0108 0.0065  128 SER   A C   
2856 C C   B SER   A 128 ? 0.1739 0.1402 0.1348 0.0046  -0.0364 0.0229  128 SER   A C   
2857 O O   A SER   A 128 ? 0.1794 0.1512 0.1512 -0.0024 -0.0164 -0.0000 128 SER   A O   
2858 O O   B SER   A 128 ? 0.1902 0.1578 0.1647 0.0130  -0.0259 0.0110  128 SER   A O   
2859 C CB  A SER   A 128 ? 0.1529 0.1472 0.1280 -0.0144 -0.0052 0.0263  128 SER   A CB  
2860 C CB  B SER   A 128 ? 0.1686 0.1565 0.1519 -0.0069 -0.0183 0.0187  128 SER   A CB  
2861 O OG  A SER   A 128 ? 0.1461 0.1602 0.1320 -0.0137 -0.0080 0.0199  128 SER   A OG  
2862 O OG  B SER   A 128 ? 0.1704 0.1732 0.1613 -0.0072 -0.0124 0.0187  128 SER   A OG  
2873 N N   A ALA   A 129 ? 0.1773 0.1571 0.1722 -0.0002 -0.0064 0.0115  129 ALA   A N   
2874 N N   B ALA   A 129 ? 0.1679 0.1485 0.1683 -0.0039 -0.0355 0.0355  129 ALA   A N   
2875 C CA  A ALA   A 129 ? 0.1770 0.1633 0.1892 0.0023  -0.0090 0.0040  129 ALA   A CA  
2876 C CA  B ALA   A 129 ? 0.1646 0.1592 0.1867 -0.0045 -0.0259 0.0388  129 ALA   A CA  
2877 C C   A ALA   A 129 ? 0.1730 0.1598 0.1952 0.0057  -0.0186 -0.0193 129 ALA   A C   
2878 C C   B ALA   A 129 ? 0.1696 0.1599 0.2049 -0.0062 -0.0140 0.0102  129 ALA   A C   
2879 O O   A ALA   A 129 ? 0.1778 0.1671 0.2113 0.0017  -0.0133 -0.0170 129 ALA   A O   
2880 O O   B ALA   A 129 ? 0.1784 0.1697 0.2046 -0.0129 -0.0086 0.0166  129 ALA   A O   
2881 C CB  A ALA   A 129 ? 0.1801 0.1783 0.2132 0.0001  0.0006  0.0027  129 ALA   A CB  
2882 C CB  B ALA   A 129 ? 0.1593 0.1870 0.1953 -0.0104 -0.0191 0.0421  129 ALA   A CB  
2893 N N   A GLY   A 130 ? 0.1711 0.1591 0.2161 0.0059  -0.0251 -0.0214 130 GLY   A N   
2894 N N   B GLY   A 130 ? 0.1700 0.1627 0.2257 -0.0143 -0.0123 0.0009  130 GLY   A N   
2895 C CA  A GLY   A 130 ? 0.1787 0.1576 0.2408 0.0092  -0.0240 -0.0234 130 GLY   A CA  
2896 C CA  B GLY   A 130 ? 0.1793 0.1703 0.2424 -0.0059 -0.0147 -0.0120 130 GLY   A CA  
2897 C C   A GLY   A 130 ? 0.1812 0.1527 0.2462 0.0127  -0.0382 -0.0128 130 GLY   A C   
2898 C C   B GLY   A 130 ? 0.1799 0.1617 0.2505 -0.0077 -0.0217 -0.0115 130 GLY   A C   
2899 O O   A GLY   A 130 ? 0.1808 0.1464 0.2388 0.0191  -0.0503 -0.0006 130 GLY   A O   
2900 O O   B GLY   A 130 ? 0.1857 0.1627 0.2482 -0.0114 -0.0307 0.0002  130 GLY   A O   
2907 N N   A ILE   A 131 ? 0.1855 0.1571 0.2486 0.0052  -0.0454 -0.0058 131 ILE   A N   
2908 N N   B ILE   A 131 ? 0.1878 0.1586 0.2723 -0.0056 -0.0141 -0.0123 131 ILE   A N   
2909 C CA  A ILE   A 131 ? 0.1909 0.1541 0.2281 -0.0003 -0.0593 0.0006  131 ILE   A CA  
2910 C CA  B ILE   A 131 ? 0.1984 0.1634 0.2723 -0.0046 -0.0234 -0.0081 131 ILE   A CA  
2911 C C   A ILE   A 131 ? 0.1960 0.1537 0.1892 -0.0036 -0.0425 0.0251  131 ILE   A C   
2912 C C   B ILE   A 131 ? 0.1991 0.1672 0.2331 -0.0020 -0.0230 0.0055  131 ILE   A C   
2913 O O   A ILE   A 131 ? 0.2124 0.1623 0.1947 -0.0055 -0.0364 0.0390  131 ILE   A O   
2914 O O   B ILE   A 131 ? 0.2099 0.1735 0.2344 0.0023  -0.0404 0.0275  131 ILE   A O   
2915 C CB  A ILE   A 131 ? 0.1932 0.1654 0.2493 -0.0006 -0.0832 -0.0198 131 ILE   A CB  
2916 C CB  B ILE   A 131 ? 0.2077 0.1704 0.3093 -0.0049 -0.0232 -0.0316 131 ILE   A CB  
2917 C CG1 A ILE   A 131 ? 0.1958 0.1870 0.2681 0.0030  -0.0936 -0.0303 131 ILE   A CG1 
2918 C CG1 B ILE   A 131 ? 0.2194 0.1973 0.3357 -0.0086 -0.0347 -0.0405 131 ILE   A CG1 
2919 C CG2 A ILE   A 131 ? 0.1915 0.1545 0.2485 -0.0053 -0.0911 -0.0327 131 ILE   A CG2 
2920 C CG2 B ILE   A 131 ? 0.2108 0.1561 0.3206 0.0030  -0.0137 -0.0318 131 ILE   A CG2 
2921 C CD1 A ILE   A 131 ? 0.2026 0.1960 0.2840 0.0053  -0.0947 -0.0322 131 ILE   A CD1 
2922 C CD1 B ILE   A 131 ? 0.2230 0.2101 0.3475 -0.0122 -0.0379 -0.0457 131 ILE   A CD1 
2945 N N   A PHE   A 132 ? 0.1867 0.1495 0.1701 0.0016  -0.0369 0.0298  132 PHE   A N   
2946 N N   B PHE   A 132 ? 0.1920 0.1655 0.2043 -0.0014 -0.0065 -0.0031 132 PHE   A N   
2947 C CA  A PHE   A 132 ? 0.1856 0.1554 0.1633 -0.0074 -0.0262 0.0267  132 PHE   A CA  
2948 C CA  B PHE   A 132 ? 0.1920 0.1798 0.1659 -0.0030 -0.0075 -0.0024 132 PHE   A CA  
2949 C C   A PHE   A 132 ? 0.1978 0.1692 0.1756 -0.0053 -0.0273 0.0280  132 PHE   A C   
2950 C C   B PHE   A 132 ? 0.1957 0.1961 0.1637 -0.0004 -0.0160 0.0145  132 PHE   A C   
2951 O O   A PHE   A 132 ? 0.2131 0.1848 0.1945 -0.0059 -0.0167 0.0245  132 PHE   A O   
2952 O O   B PHE   A 132 ? 0.2006 0.2078 0.1564 0.0006  -0.0100 0.0117  132 PHE   A O   
2953 C CB  A PHE   A 132 ? 0.1663 0.1463 0.1374 -0.0073 -0.0231 0.0327  132 PHE   A CB  
2954 C CB  B PHE   A 132 ? 0.1908 0.1778 0.1506 0.0042  -0.0100 0.0013  132 PHE   A CB  
2955 C CG  A PHE   A 132 ? 0.1607 0.1442 0.1267 0.0013  -0.0222 0.0165  132 PHE   A CG  
2956 C CG  B PHE   A 132 ? 0.1880 0.1774 0.1402 0.0157  -0.0082 0.0051  132 PHE   A CG  
2957 C CD1 A PHE   A 132 ? 0.1611 0.1569 0.1542 0.0053  -0.0169 -0.0038 132 PHE   A CD1 
2958 C CD1 B PHE   A 132 ? 0.1958 0.1851 0.1509 0.0167  -0.0002 0.0041  132 PHE   A CD1 
2959 C CD2 A PHE   A 132 ? 0.1613 0.1514 0.1357 0.0011  -0.0219 0.0083  132 PHE   A CD2 
2960 C CD2 B PHE   A 132 ? 0.1820 0.1787 0.1549 0.0105  0.0051  -0.0007 132 PHE   A CD2 
2961 C CE1 A PHE   A 132 ? 0.1578 0.1605 0.1456 0.0038  -0.0177 -0.0081 132 PHE   A CE1 
2962 C CE1 B PHE   A 132 ? 0.1989 0.1895 0.1503 0.0153  -0.0037 -0.0010 132 PHE   A CE1 
2963 C CE2 A PHE   A 132 ? 0.1583 0.1583 0.1497 0.0070  -0.0292 0.0058  132 PHE   A CE2 
2964 C CE2 B PHE   A 132 ? 0.1854 0.1803 0.1504 0.0147  0.0077  0.0094  132 PHE   A CE2 
2965 C CZ  A PHE   A 132 ? 0.1571 0.1593 0.1406 0.0018  -0.0294 0.0002  132 PHE   A CZ  
2966 C CZ  B PHE   A 132 ? 0.1931 0.1835 0.1331 0.0145  -0.0007 0.0118  132 PHE   A CZ  
2985 N N   A GLY   A 133 ? 0.1957 0.1683 0.1749 -0.0065 -0.0386 0.0226  133 GLY   A N   
2986 N N   B GLY   A 133 ? 0.2002 0.2048 0.1696 -0.0040 -0.0383 0.0169  133 GLY   A N   
2987 C CA  A GLY   A 133 ? 0.1972 0.1738 0.1757 -0.0056 -0.0432 0.0102  133 GLY   A CA  
2988 C CA  B GLY   A 133 ? 0.2128 0.2201 0.1844 -0.0058 -0.0562 0.0099  133 GLY   A CA  
2989 C C   A GLY   A 133 ? 0.1973 0.1788 0.1737 -0.0072 -0.0468 -0.0015 133 GLY   A C   
2990 C C   B GLY   A 133 ? 0.2210 0.2337 0.1944 -0.0124 -0.0686 0.0036  133 GLY   A C   
2991 O O   A GLY   A 133 ? 0.2056 0.1927 0.1882 -0.0160 -0.0557 -0.0199 133 GLY   A O   
2992 O O   B GLY   A 133 ? 0.2336 0.2509 0.2188 -0.0093 -0.0731 0.0007  133 GLY   A O   
2999 N N   A ALA   A 134 ? 0.1937 0.1677 0.1571 -0.0035 -0.0271 0.0006  134 ALA   A N   
3000 N N   B ALA   A 134 ? 0.2184 0.2263 0.1828 -0.0215 -0.0587 -0.0040 134 ALA   A N   
3001 C CA  A ALA   A 134 ? 0.1912 0.1595 0.1683 0.0011  -0.0179 0.0001  134 ALA   A CA  
3002 C CA  B ALA   A 134 ? 0.2205 0.2247 0.1900 -0.0216 -0.0453 -0.0136 134 ALA   A CA  
3003 C C   A ALA   A 134 ? 0.1916 0.1575 0.1664 0.0010  -0.0182 0.0099  134 ALA   A C   
3004 C C   B ALA   A 134 ? 0.2181 0.2323 0.1948 -0.0217 -0.0329 -0.0014 134 ALA   A C   
3005 O O   A ALA   A 134 ? 0.1937 0.1546 0.1866 0.0003  -0.0037 -0.0025 134 ALA   A O   
3006 O O   B ALA   A 134 ? 0.2306 0.2399 0.2020 -0.0190 -0.0380 -0.0028 134 ALA   A O   
3007 C CB  A ALA   A 134 ? 0.1925 0.1527 0.1822 0.0013  -0.0092 -0.0056 134 ALA   A CB  
3008 C CB  B ALA   A 134 ? 0.2254 0.2143 0.2100 -0.0224 -0.0416 -0.0275 134 ALA   A CB  
3019 N N   A ASP   A 135 ? 0.1921 0.1698 0.1655 -0.0088 -0.0266 0.0197  135 ASP   A N   
3020 N N   B ASP   A 135 ? 0.2066 0.2325 0.2124 -0.0243 -0.0209 0.0037  135 ASP   A N   
3021 C CA  A ASP   A 135 ? 0.1885 0.1850 0.1817 -0.0119 -0.0399 0.0262  135 ASP   A CA  
3022 C CA  B ASP   A 135 ? 0.1984 0.2357 0.2258 -0.0278 -0.0245 0.0101  135 ASP   A CA  
3023 C C   A ASP   A 135 ? 0.1741 0.1753 0.1840 -0.0057 -0.0349 0.0323  135 ASP   A C   
3024 C C   B ASP   A 135 ? 0.1867 0.2144 0.2147 -0.0182 -0.0129 0.0185  135 ASP   A C   
3025 O O   A ASP   A 135 ? 0.1689 0.1727 0.1865 -0.0075 -0.0351 0.0422  135 ASP   A O   
3026 O O   B ASP   A 135 ? 0.1839 0.2109 0.2113 -0.0148 -0.0089 0.0289  135 ASP   A O   
3027 C CB  A ASP   A 135 ? 0.2044 0.2079 0.2052 -0.0207 -0.0454 0.0188  135 ASP   A CB  
3028 C CB  B ASP   A 135 ? 0.2163 0.2644 0.2729 -0.0404 -0.0314 -0.0003 135 ASP   A CB  
3029 C CG  A ASP   A 135 ? 0.2155 0.2316 0.2349 -0.0274 -0.0500 0.0131  135 ASP   A CG  
3030 C CG  B ASP   A 135 ? 0.2322 0.2866 0.3202 -0.0550 -0.0271 -0.0173 135 ASP   A CG  
3031 O OD1 A ASP   A 135 ? 0.2134 0.2365 0.2319 -0.0246 -0.0558 0.0219  135 ASP   A OD1 
3032 O OD1 B ASP   A 135 ? 0.2351 0.2956 0.3287 -0.0619 -0.0276 -0.0154 135 ASP   A OD1 
3033 O OD2 A ASP   A 135 ? 0.2249 0.2502 0.2731 -0.0342 -0.0436 -0.0042 135 ASP   A OD2 
3034 O OD2 B ASP   A 135 ? 0.2462 0.2949 0.3587 -0.0608 -0.0211 -0.0279 135 ASP   A OD2 
3043 N N   A PRO   A 136 ? 0.1669 0.1647 0.1839 0.0054  -0.0291 0.0303  136 PRO   A N   
3044 N N   B PRO   A 136 ? 0.1811 0.2041 0.2078 -0.0040 -0.0161 0.0183  136 PRO   A N   
3045 C CA  A PRO   A 136 ? 0.1595 0.1691 0.1886 0.0039  -0.0180 0.0162  136 PRO   A CA  
3046 C CA  B PRO   A 136 ? 0.1719 0.1965 0.2134 -0.0027 -0.0162 0.0104  136 PRO   A CA  
3047 C C   A PRO   A 136 ? 0.1384 0.1689 0.1739 0.0041  -0.0091 0.0105  136 PRO   A C   
3048 C C   B PRO   A 136 ? 0.1533 0.1882 0.2148 -0.0057 -0.0092 0.0099  136 PRO   A C   
3049 O O   A PRO   A 136 ? 0.1344 0.1553 0.1470 0.0048  0.0055  0.0083  136 PRO   A O   
3050 O O   B PRO   A 136 ? 0.1493 0.1904 0.2055 -0.0097 -0.0044 0.0125  136 PRO   A O   
3051 C CB  A PRO   A 136 ? 0.1725 0.1646 0.2047 0.0032  -0.0256 0.0203  136 PRO   A CB  
3052 C CB  B PRO   A 136 ? 0.1878 0.1955 0.2161 0.0015  -0.0181 0.0142  136 PRO   A CB  
3053 C CG  A PRO   A 136 ? 0.1787 0.1656 0.2207 0.0113  -0.0354 0.0225  136 PRO   A CG  
3054 C CG  B PRO   A 136 ? 0.1936 0.2026 0.2186 0.0050  -0.0229 0.0052  136 PRO   A CG  
3055 C CD  A PRO   A 136 ? 0.1716 0.1600 0.2071 0.0085  -0.0310 0.0338  136 PRO   A CD  
3056 C CD  B PRO   A 136 ? 0.1891 0.2057 0.2079 0.0046  -0.0192 0.0142  136 PRO   A CD  
3071 N N   A ILE   A 137 ? 0.1330 0.1757 0.1935 0.0032  -0.0180 0.0054  137 ILE   A N   
3072 N N   B ILE   A 137 ? 0.1437 0.1888 0.2198 -0.0084 -0.0212 0.0134  137 ILE   A N   
3073 C CA  A ILE   A 137 ? 0.1388 0.1855 0.2010 -0.0008 -0.0175 -0.0022 137 ILE   A CA  
3074 C CA  B ILE   A 137 ? 0.1526 0.1978 0.2345 -0.0117 -0.0208 0.0197  137 ILE   A CA  
3075 C C   A ILE   A 137 ? 0.1400 0.1972 0.1946 -0.0077 -0.0039 0.0038  137 ILE   A C   
3076 C C   B ILE   A 137 ? 0.1598 0.1998 0.2191 -0.0103 -0.0199 0.0307  137 ILE   A C   
3077 O O   A ILE   A 137 ? 0.1355 0.2001 0.1927 -0.0144 0.0022  0.0032  137 ILE   A O   
3078 O O   B ILE   A 137 ? 0.1658 0.1901 0.2185 -0.0156 -0.0127 0.0245  137 ILE   A O   
3079 C CB  A ILE   A 137 ? 0.1509 0.1854 0.2125 0.0006  -0.0290 -0.0110 137 ILE   A CB  
3080 C CB  B ILE   A 137 ? 0.1608 0.2111 0.2533 -0.0145 -0.0260 0.0015  137 ILE   A CB  
3081 C CG1 A ILE   A 137 ? 0.1592 0.1930 0.2203 0.0023  -0.0421 -0.0145 137 ILE   A CG1 
3082 C CG1 B ILE   A 137 ? 0.1637 0.2235 0.2726 -0.0116 -0.0215 -0.0052 137 ILE   A CG1 
3083 C CG2 A ILE   A 137 ? 0.1590 0.1825 0.2328 0.0023  -0.0334 -0.0108 137 ILE   A CG2 
3084 C CG2 B ILE   A 137 ? 0.1738 0.2119 0.2596 -0.0201 -0.0227 -0.0021 137 ILE   A CG2 
3085 C CD1 A ILE   A 137 ? 0.1694 0.2029 0.2365 0.0057  -0.0409 -0.0195 137 ILE   A CD1 
3086 C CD1 B ILE   A 137 ? 0.1710 0.2337 0.2943 -0.0077 -0.0125 -0.0088 137 ILE   A CD1 
3109 N N   A HIS   A 138 ? 0.1420 0.2135 0.1904 -0.0043 0.0070  0.0079  138 HIS   A N   
3110 N N   B HIS   A 138 ? 0.1589 0.2172 0.2084 -0.0021 -0.0186 0.0408  138 HIS   A N   
3111 C CA  A HIS   A 138 ? 0.1461 0.2153 0.1848 -0.0045 0.0072  0.0132  138 HIS   A CA  
3112 C CA  B HIS   A 138 ? 0.1593 0.2286 0.2006 -0.0020 -0.0159 0.0312  138 HIS   A CA  
3113 C C   A HIS   A 138 ? 0.1398 0.2031 0.1848 -0.0044 0.0077  0.0263  138 HIS   A C   
3114 C C   B HIS   A 138 ? 0.1444 0.2119 0.1922 -0.0030 -0.0067 0.0354  138 HIS   A C   
3115 O O   A HIS   A 138 ? 0.1479 0.1993 0.1929 -0.0094 0.0064  0.0149  138 HIS   A O   
3116 O O   B HIS   A 138 ? 0.1493 0.2078 0.1917 -0.0110 -0.0070 0.0272  138 HIS   A O   
3117 C CB  A HIS   A 138 ? 0.1521 0.2253 0.1814 -0.0067 0.0033  -0.0021 138 HIS   A CB  
3118 C CB  B HIS   A 138 ? 0.1804 0.2509 0.2003 -0.0046 -0.0286 0.0164  138 HIS   A CB  
3119 C CG  A HIS   A 138 ? 0.1579 0.2280 0.1923 -0.0118 -0.0005 -0.0133 138 HIS   A CG  
3120 C CG  B HIS   A 138 ? 0.1940 0.2630 0.2184 -0.0086 -0.0252 0.0066  138 HIS   A CG  
3121 N ND1 A HIS   A 138 ? 0.1664 0.2316 0.2139 -0.0165 -0.0009 -0.0221 138 HIS   A ND1 
3122 N ND1 B HIS   A 138 ? 0.2057 0.2712 0.2427 -0.0151 -0.0155 -0.0035 138 HIS   A ND1 
3123 C CD2 A HIS   A 138 ? 0.1600 0.2246 0.1931 -0.0108 0.0063  -0.0166 138 HIS   A CD2 
3124 C CD2 B HIS   A 138 ? 0.1960 0.2697 0.2250 -0.0076 -0.0212 0.0063  138 HIS   A CD2 
3125 C CE1 A HIS   A 138 ? 0.1673 0.2270 0.2114 -0.0101 0.0027  -0.0293 138 HIS   A CE1 
3126 C CE1 B HIS   A 138 ? 0.2097 0.2746 0.2490 -0.0123 -0.0110 -0.0028 138 HIS   A CE1 
3127 N NE2 A HIS   A 138 ? 0.1641 0.2242 0.1965 -0.0094 0.0092  -0.0251 138 HIS   A NE2 
3128 N NE2 B HIS   A 138 ? 0.2024 0.2733 0.2294 -0.0096 -0.0080 0.0007  138 HIS   A NE2 
3143 N N   . SER   A 139 ? 0.1352 0.1985 0.1911 -0.0024 -0.0024 0.0416  139 SER   A N   
3144 C CA  . SER   A 139 ? 0.1271 0.1849 0.2031 -0.0079 -0.0031 0.0382  139 SER   A CA  
3145 C C   . SER   A 139 ? 0.1229 0.1653 0.1979 -0.0066 0.0041  0.0289  139 SER   A C   
3146 O O   . SER   A 139 ? 0.1226 0.1540 0.2007 -0.0075 0.0052  0.0249  139 SER   A O   
3147 C CB  . SER   A 139 ? 0.1316 0.1874 0.2027 -0.0127 -0.0020 0.0425  139 SER   A CB  
3148 O OG  . SER   A 139 ? 0.1349 0.1838 0.2073 -0.0091 -0.0081 0.0576  139 SER   A OG  
3155 N N   . LEU   A 140 ? 0.1240 0.1692 0.1872 -0.0036 -0.0027 0.0399  140 LEU   A N   
3156 C CA  . LEU   A 140 ? 0.1254 0.1587 0.1840 -0.0092 -0.0026 0.0297  140 LEU   A CA  
3157 C C   . LEU   A 140 ? 0.1208 0.1635 0.1832 -0.0107 -0.0031 0.0254  140 LEU   A C   
3158 O O   . LEU   A 140 ? 0.1281 0.1609 0.1948 -0.0034 0.0007  0.0264  140 LEU   A O   
3159 C CB  . LEU   A 140 ? 0.1255 0.1663 0.1908 -0.0118 0.0035  0.0184  140 LEU   A CB  
3160 C CG  . LEU   A 140 ? 0.1314 0.1803 0.1971 -0.0186 0.0082  0.0278  140 LEU   A CG  
3161 C CD1 . LEU   A 140 ? 0.1349 0.1827 0.2053 -0.0102 0.0086  0.0277  140 LEU   A CD1 
3162 C CD2 . LEU   A 140 ? 0.1393 0.1950 0.1969 -0.0172 0.0177  0.0345  140 LEU   A CD2 
3174 N N   . ARG   A 141 ? 0.1302 0.1714 0.1917 -0.0061 -0.0032 0.0182  141 ARG   A N   
3175 C CA  . ARG   A 141 ? 0.1431 0.1839 0.2075 -0.0186 -0.0081 -0.0013 141 ARG   A CA  
3176 C C   . ARG   A 141 ? 0.1454 0.1681 0.1989 -0.0163 -0.0090 0.0055  141 ARG   A C   
3177 O O   . ARG   A 141 ? 0.1412 0.1623 0.2179 -0.0178 0.0007  -0.0000 141 ARG   A O   
3178 C CB  . ARG   A 141 ? 0.1587 0.2131 0.2368 -0.0300 -0.0078 -0.0184 141 ARG   A CB  
3179 C CG  . ARG   A 141 ? 0.1978 0.2478 0.2781 -0.0398 0.0066  -0.0266 141 ARG   A CG  
3180 C CD  . ARG   A 141 ? 0.2313 0.2770 0.3163 -0.0509 0.0084  -0.0369 141 ARG   A CD  
3181 N NE  . ARG   A 141 ? 0.2350 0.3054 0.3257 -0.0573 0.0015  -0.0333 141 ARG   A NE  
3182 C CZ  . ARG   A 141 ? 0.2313 0.3265 0.3310 -0.0731 0.0129  -0.0169 141 ARG   A CZ  
3183 N NH1 . ARG   A 141 ? 0.2248 0.3311 0.3212 -0.0822 0.0419  -0.0270 141 ARG   A NH1 
3184 N NH2 . ARG   A 141 ? 0.2435 0.3352 0.3483 -0.0698 -0.0004 0.0025  141 ARG   A NH2 
3198 N N   . VAL   A 142 ? 0.1382 0.1664 0.1855 -0.0130 0.0002  0.0044  142 VAL   A N   
3199 C CA  . VAL   A 142 ? 0.1416 0.1585 0.1933 -0.0091 0.0118  0.0063  142 VAL   A CA  
3200 C C   . VAL   A 142 ? 0.1230 0.1505 0.1893 -0.0129 0.0086  0.0065  142 VAL   A C   
3201 O O   . VAL   A 142 ? 0.1316 0.1514 0.1927 -0.0027 0.0112  0.0088  142 VAL   A O   
3202 C CB  . VAL   A 142 ? 0.1523 0.1677 0.1803 -0.0069 0.0130  0.0052  142 VAL   A CB  
3203 C CG1 . VAL   A 142 ? 0.1522 0.1628 0.1842 -0.0148 0.0160  0.0064  142 VAL   A CG1 
3204 C CG2 . VAL   A 142 ? 0.1623 0.1841 0.2102 0.0004  0.0095  0.0073  142 VAL   A CG2 
3214 N N   . CYS   A 143 ? 0.1329 0.1374 0.1848 -0.0175 0.0063  0.0075  143 CYS   A N   
3215 C CA  . CYS   A 143 ? 0.1311 0.1398 0.1862 -0.0117 0.0121  0.0121  143 CYS   A CA  
3216 C C   . CYS   A 143 ? 0.1266 0.1406 0.1948 -0.0121 0.0082  0.0169  143 CYS   A C   
3217 O O   . CYS   A 143 ? 0.1252 0.1449 0.2020 -0.0032 0.0074  0.0266  143 CYS   A O   
3218 C CB  . CYS   A 143 ? 0.1372 0.1473 0.1919 -0.0109 0.0143  0.0197  143 CYS   A CB  
3219 S SG  . CYS   A 143 ? 0.1558 0.1556 0.1858 -0.0002 0.0135  0.0169  143 CYS   A SG  
3225 N N   . VAL   A 144 ? 0.1268 0.1465 0.2132 -0.0120 0.0093  0.0352  144 VAL   A N   
3226 C CA  . VAL   A 144 ? 0.1337 0.1578 0.2541 -0.0150 0.0175  0.0447  144 VAL   A CA  
3227 C C   . VAL   A 144 ? 0.1415 0.1446 0.2659 -0.0211 -0.0076 0.0309  144 VAL   A C   
3228 O O   . VAL   A 144 ? 0.1555 0.1447 0.2699 -0.0082 -0.0092 0.0333  144 VAL   A O   
3229 C CB  . VAL   A 144 ? 0.1641 0.1877 0.3215 -0.0030 0.0347  0.0503  144 VAL   A CB  
3230 C CG1 . VAL   A 144 ? 0.1843 0.2108 0.3579 -0.0154 0.0243  0.0494  144 VAL   A CG1 
3231 C CG2 . VAL   A 144 ? 0.1470 0.1931 0.3183 -0.0007 0.0482  0.0542  144 VAL   A CG2 
3241 N N   . ASP   A 145 ? 0.1436 0.1396 0.2785 -0.0200 -0.0033 0.0224  145 ASP   A N   
3242 C CA  . ASP   A 145 ? 0.1580 0.1471 0.2765 -0.0235 -0.0046 0.0086  145 ASP   A CA  
3243 C C   . ASP   A 145 ? 0.1534 0.1402 0.2623 -0.0081 -0.0014 -0.0044 145 ASP   A C   
3244 O O   . ASP   A 145 ? 0.1626 0.1543 0.3142 -0.0122 0.0003  -0.0352 145 ASP   A O   
3245 C CB  . ASP   A 145 ? 0.1741 0.1755 0.3119 -0.0338 -0.0213 0.0013  145 ASP   A CB  
3246 C CG  . ASP   A 145 ? 0.2000 0.2159 0.3407 -0.0537 -0.0374 0.0051  145 ASP   A CG  
3247 O OD1 . ASP   A 145 ? 0.1937 0.2355 0.3478 -0.0667 -0.0219 0.0089  145 ASP   A OD1 
3248 O OD2 . ASP   A 145 ? 0.2224 0.2426 0.3563 -0.0570 -0.0608 0.0082  145 ASP   A OD2 
3253 N N   . THR   A 146 ? 0.1388 0.1377 0.2113 -0.0108 0.0127  0.0065  146 THR   A N   
3254 C CA  . THR   A 146 ? 0.1358 0.1329 0.2027 -0.0050 0.0070  0.0017  146 THR   A CA  
3255 C C   . THR   A 146 ? 0.1320 0.1337 0.2037 -0.0052 0.0135  0.0173  146 THR   A C   
3256 O O   . THR   A 146 ? 0.1426 0.1460 0.2246 0.0021  0.0005  0.0175  146 THR   A O   
3257 C CB  . THR   A 146 ? 0.1358 0.1377 0.1981 -0.0044 0.0069  0.0076  146 THR   A CB  
3258 O OG1 . THR   A 146 ? 0.1382 0.1524 0.1987 -0.0003 -0.0006 -0.0014 146 THR   A OG1 
3259 C CG2 . THR   A 146 ? 0.1307 0.1419 0.2250 -0.0074 0.0072  0.0063  146 THR   A CG2 
3267 N N   . VAL   A 147 ? 0.1286 0.1362 0.2002 -0.0068 0.0155  0.0152  147 VAL   A N   
3268 C CA  . VAL   A 147 ? 0.1294 0.1366 0.2088 -0.0130 0.0241  0.0189  147 VAL   A CA  
3269 C C   . VAL   A 147 ? 0.1310 0.1339 0.2064 -0.0147 0.0174  0.0253  147 VAL   A C   
3270 O O   . VAL   A 147 ? 0.1355 0.1404 0.2304 -0.0164 0.0123  0.0298  147 VAL   A O   
3271 C CB  . VAL   A 147 ? 0.1389 0.1360 0.1896 -0.0118 0.0201  0.0259  147 VAL   A CB  
3272 C CG1 . VAL   A 147 ? 0.1736 0.1453 0.1932 -0.0108 0.0200  0.0321  147 VAL   A CG1 
3273 C CG2 . VAL   A 147 ? 0.1391 0.1412 0.1800 -0.0139 0.0057  0.0189  147 VAL   A CG2 
3283 N N   . ARG   A 148 ? 0.1301 0.1388 0.2094 -0.0109 0.0150  0.0384  148 ARG   A N   
3284 C CA  . ARG   A 148 ? 0.1352 0.1384 0.2144 -0.0150 0.0149  0.0528  148 ARG   A CA  
3285 C C   . ARG   A 148 ? 0.1459 0.1465 0.2191 -0.0171 0.0138  0.0673  148 ARG   A C   
3286 O O   . ARG   A 148 ? 0.1754 0.1628 0.2349 -0.0207 0.0271  0.0558  148 ARG   A O   
3287 C CB  . ARG   A 148 ? 0.1449 0.1396 0.2401 -0.0133 0.0230  0.0407  148 ARG   A CB  
3288 C CG  . ARG   A 148 ? 0.1643 0.1421 0.2861 -0.0158 0.0379  0.0359  148 ARG   A CG  
3289 C CD  . ARG   A 148 ? 0.1788 0.1417 0.2986 -0.0063 0.0500  0.0510  148 ARG   A CD  
3290 N NE  . ARG   A 148 ? 0.1713 0.1509 0.2847 0.0109  0.0531  0.0520  148 ARG   A NE  
3291 C CZ  . ARG   A 148 ? 0.1653 0.1383 0.2710 0.0091  0.0552  0.0377  148 ARG   A CZ  
3292 N NH1 . ARG   A 148 ? 0.1708 0.1387 0.2802 -0.0019 0.0513  0.0155  148 ARG   A NH1 
3293 N NH2 . ARG   A 148 ? 0.1637 0.1578 0.2685 0.0214  0.0527  0.0483  148 ARG   A NH2 
3307 N N   . THR   A 149 ? 0.1459 0.1533 0.2064 -0.0158 0.0019  0.0600  149 THR   A N   
3308 C CA  . THR   A 149 ? 0.1488 0.1594 0.2086 -0.0086 0.0031  0.0513  149 THR   A CA  
3309 C C   . THR   A 149 ? 0.1396 0.1553 0.1967 -0.0198 0.0083  0.0534  149 THR   A C   
3310 O O   . THR   A 149 ? 0.1445 0.1674 0.2096 -0.0231 0.0021  0.0519  149 THR   A O   
3311 C CB  . THR   A 149 ? 0.1457 0.1680 0.2092 -0.0174 0.0061  0.0492  149 THR   A CB  
3312 O OG1 . THR   A 149 ? 0.1535 0.1598 0.2108 -0.0233 0.0068  0.0415  149 THR   A OG1 
3313 C CG2 . THR   A 149 ? 0.1475 0.1847 0.2161 -0.0105 -0.0031 0.0374  149 THR   A CG2 
3321 N N   . ASN   A 150 ? 0.1519 0.1661 0.1955 -0.0094 0.0035  0.0582  150 ASN   A N   
3322 C CA  . ASN   A 150 ? 0.1628 0.1727 0.1929 -0.0129 0.0051  0.0526  150 ASN   A CA  
3323 C C   . ASN   A 150 ? 0.1462 0.1636 0.1978 -0.0179 0.0070  0.0555  150 ASN   A C   
3324 O O   . ASN   A 150 ? 0.1562 0.1761 0.2197 -0.0144 -0.0075 0.0541  150 ASN   A O   
3325 C CB  . ASN   A 150 ? 0.2055 0.1974 0.2255 -0.0212 0.0195  0.0752  150 ASN   A CB  
3326 C CG  . ASN   A 150 ? 0.2621 0.2317 0.2963 -0.0183 0.0097  0.0790  150 ASN   A CG  
3327 O OD1 . ASN   A 150 ? 0.2856 0.2368 0.3096 -0.0245 0.0209  0.0941  150 ASN   A OD1 
3328 N ND2 . ASN   A 150 ? 0.2896 0.2500 0.3435 -0.0118 -0.0110 0.0761  150 ASN   A ND2 
3335 N N   . VAL   A 151 ? 0.1426 0.1488 0.1998 -0.0202 0.0040  0.0461  151 VAL   A N   
3336 C CA  . VAL   A 151 ? 0.1536 0.1486 0.1853 -0.0209 0.0096  0.0422  151 VAL   A CA  
3337 C C   . VAL   A 151 ? 0.1401 0.1457 0.1857 -0.0239 0.0105  0.0470  151 VAL   A C   
3338 O O   . VAL   A 151 ? 0.1495 0.1535 0.2322 -0.0221 0.0069  0.0407  151 VAL   A O   
3339 C CB  . VAL   A 151 ? 0.1871 0.1680 0.1929 -0.0036 0.0039  0.0455  151 VAL   A CB  
3340 C CG1 . VAL   A 151 ? 0.1856 0.1887 0.2220 -0.0122 0.0001  0.0444  151 VAL   A CG1 
3341 C CG2 . VAL   A 151 ? 0.1975 0.1661 0.1833 0.0030  0.0130  0.0377  151 VAL   A CG2 
3351 N N   . TYR   A 152 ? 0.1341 0.1505 0.1911 -0.0249 0.0079  0.0436  152 TYR   A N   
3352 C CA  . TYR   A 152 ? 0.1379 0.1574 0.1711 -0.0226 0.0079  0.0424  152 TYR   A CA  
3353 C C   . TYR   A 152 ? 0.1368 0.1490 0.1570 -0.0194 0.0144  0.0418  152 TYR   A C   
3354 O O   . TYR   A 152 ? 0.1464 0.1483 0.1665 -0.0259 0.0181  0.0350  152 TYR   A O   
3355 C CB  . TYR   A 152 ? 0.1570 0.1776 0.1737 -0.0187 0.0163  0.0549  152 TYR   A CB  
3356 C CG  . TYR   A 152 ? 0.1650 0.2028 0.1706 -0.0250 0.0255  0.0572  152 TYR   A CG  
3357 C CD1 . TYR   A 152 ? 0.1797 0.2229 0.1882 -0.0131 0.0227  0.0706  152 TYR   A CD1 
3358 C CD2 . TYR   A 152 ? 0.1740 0.2198 0.1699 -0.0349 0.0152  0.0573  152 TYR   A CD2 
3359 C CE1 . TYR   A 152 ? 0.2168 0.2431 0.2065 -0.0057 0.0200  0.0819  152 TYR   A CE1 
3360 C CE2 . TYR   A 152 ? 0.2050 0.2423 0.1952 -0.0351 0.0201  0.0664  152 TYR   A CE2 
3361 C CZ  . TYR   A 152 ? 0.2317 0.2502 0.1928 -0.0203 0.0169  0.0982  152 TYR   A CZ  
3362 O OH  . TYR   A 152 ? 0.2627 0.2733 0.2371 -0.0140 0.0261  0.1157  152 TYR   A OH  
3372 N N   . LEU   A 153 ? 0.1334 0.1476 0.1676 -0.0220 0.0177  0.0432  153 LEU   A N   
3373 C CA  . LEU   A 153 ? 0.1280 0.1449 0.1742 -0.0118 0.0182  0.0378  153 LEU   A CA  
3374 C C   . LEU   A 153 ? 0.1347 0.1472 0.1897 -0.0087 0.0237  0.0398  153 LEU   A C   
3375 O O   . LEU   A 153 ? 0.1390 0.1545 0.2231 -0.0102 0.0413  0.0400  153 LEU   A O   
3376 C CB  . LEU   A 153 ? 0.1266 0.1496 0.1861 -0.0130 0.0128  0.0348  153 LEU   A CB  
3377 C CG  . LEU   A 153 ? 0.1352 0.1528 0.1871 -0.0159 0.0172  0.0267  153 LEU   A CG  
3378 C CD1 . LEU   A 153 ? 0.1438 0.1573 0.1937 -0.0155 0.0032  0.0257  153 LEU   A CD1 
3379 C CD2 . LEU   A 153 ? 0.1458 0.1577 0.1891 -0.0107 0.0241  0.0078  153 LEU   A CD2 
3391 N N   A ALA   A 154 ? 0.1439 0.1473 0.1950 -0.0070 0.0266  0.0367  154 ALA   A N   
3392 N N   B ALA   A 154 ? 0.1290 0.1418 0.2025 -0.0090 0.0322  0.0385  154 ALA   A N   
3393 C CA  A ALA   A 154 ? 0.1577 0.1499 0.2070 -0.0037 0.0279  0.0332  154 ALA   A CA  
3394 C CA  B ALA   A 154 ? 0.1336 0.1398 0.2242 -0.0052 0.0360  0.0436  154 ALA   A CA  
3395 C C   A ALA   A 154 ? 0.1649 0.1539 0.2141 0.0045  0.0240  0.0334  154 ALA   A C   
3396 C C   B ALA   A 154 ? 0.1349 0.1436 0.2294 0.0026  0.0370  0.0488  154 ALA   A C   
3397 O O   A ALA   A 154 ? 0.1686 0.1582 0.2222 0.0011  0.0282  0.0320  154 ALA   A O   
3398 O O   B ALA   A 154 ? 0.1387 0.1462 0.2340 -0.0008 0.0406  0.0525  154 ALA   A O   
3399 C CB  A ALA   A 154 ? 0.1664 0.1532 0.2150 -0.0031 0.0276  0.0234  154 ALA   A CB  
3400 C CB  B ALA   A 154 ? 0.1430 0.1448 0.2375 -0.0011 0.0260  0.0308  154 ALA   A CB  
3411 N N   A VAL   A 155 ? 0.1721 0.1578 0.2194 0.0121  0.0204  0.0365  155 VAL   A N   
3412 N N   B VAL   A 155 ? 0.1421 0.1458 0.2291 0.0004  0.0433  0.0551  155 VAL   A N   
3413 C CA  A VAL   A 155 ? 0.1766 0.1641 0.2229 0.0199  0.0189  0.0463  155 VAL   A CA  
3414 C CA  B VAL   A 155 ? 0.1557 0.1589 0.2457 0.0065  0.0253  0.0567  155 VAL   A CA  
3415 C C   A VAL   A 155 ? 0.1765 0.1620 0.2369 0.0258  0.0101  0.0471  155 VAL   A C   
3416 C C   B VAL   A 155 ? 0.1520 0.1580 0.2556 0.0029  0.0283  0.0586  155 VAL   A C   
3417 O O   A VAL   A 155 ? 0.1745 0.1655 0.2405 0.0286  0.0063  0.0305  155 VAL   A O   
3418 O O   B VAL   A 155 ? 0.1441 0.1533 0.2544 0.0070  0.0436  0.0423  155 VAL   A O   
3419 C CB  A VAL   A 155 ? 0.1759 0.1729 0.2092 0.0312  0.0200  0.0401  155 VAL   A CB  
3420 C CB  B VAL   A 155 ? 0.1641 0.1738 0.2329 0.0199  0.0171  0.0448  155 VAL   A CB  
3421 C CG1 A VAL   A 155 ? 0.1819 0.1823 0.2169 0.0337  0.0176  0.0390  155 VAL   A CG1 
3422 C CG1 B VAL   A 155 ? 0.1746 0.1827 0.2415 0.0221  0.0170  0.0326  155 VAL   A CG1 
3423 C CG2 A VAL   A 155 ? 0.1742 0.1751 0.1984 0.0319  0.0223  0.0418  155 VAL   A CG2 
3424 C CG2 B VAL   A 155 ? 0.1711 0.1862 0.2323 0.0215  0.0161  0.0389  155 VAL   A CG2 
3443 N N   A PHE   A 156 ? 0.1736 0.1603 0.2494 0.0303  0.0134  0.0611  156 PHE   A N   
3444 N N   B PHE   A 156 ? 0.1567 0.1675 0.2883 -0.0002 0.0193  0.0651  156 PHE   A N   
3445 C CA  A PHE   A 156 ? 0.1809 0.1610 0.2734 0.0321  0.0212  0.0671  156 PHE   A CA  
3446 C CA  B PHE   A 156 ? 0.1741 0.1757 0.3214 0.0062  0.0083  0.0621  156 PHE   A CA  
3447 C C   A PHE   A 156 ? 0.1816 0.1730 0.2712 0.0353  0.0261  0.0656  156 PHE   A C   
3448 C C   B PHE   A 156 ? 0.1649 0.1778 0.3026 0.0120  0.0295  0.0589  156 PHE   A C   
3449 O O   A PHE   A 156 ? 0.1821 0.1741 0.2823 0.0289  0.0224  0.0394  156 PHE   A O   
3450 O O   B PHE   A 156 ? 0.1784 0.1769 0.3109 0.0100  0.0276  0.0269  156 PHE   A O   
3451 C CB  A PHE   A 156 ? 0.2008 0.1685 0.3043 0.0232  0.0206  0.0749  156 PHE   A CB  
3452 C CB  B PHE   A 156 ? 0.1942 0.1900 0.3595 -0.0015 -0.0085 0.0676  156 PHE   A CB  
3453 C CG  A PHE   A 156 ? 0.2271 0.1702 0.3203 0.0282  0.0122  0.0806  156 PHE   A CG  
3454 C CG  B PHE   A 156 ? 0.2148 0.1954 0.3658 0.0032  -0.0244 0.0685  156 PHE   A CG  
3455 C CD1 A PHE   A 156 ? 0.2369 0.1787 0.3180 0.0255  0.0049  0.0789  156 PHE   A CD1 
3456 C CD1 B PHE   A 156 ? 0.2278 0.2032 0.3751 0.0036  -0.0338 0.0600  156 PHE   A CD1 
3457 C CD2 A PHE   A 156 ? 0.2457 0.1799 0.3244 0.0406  0.0036  0.0816  156 PHE   A CD2 
3458 C CD2 B PHE   A 156 ? 0.2232 0.2022 0.3684 -0.0013 -0.0301 0.0598  156 PHE   A CD2 
3459 C CE1 A PHE   A 156 ? 0.2522 0.1869 0.3247 0.0304  0.0086  0.0695  156 PHE   A CE1 
3460 C CE1 B PHE   A 156 ? 0.2375 0.2054 0.3774 -0.0043 -0.0406 0.0525  156 PHE   A CE1 
3461 C CE2 A PHE   A 156 ? 0.2597 0.1879 0.3244 0.0468  -0.0023 0.0716  156 PHE   A CE2 
3462 C CE2 B PHE   A 156 ? 0.2289 0.2048 0.3708 -0.0093 -0.0365 0.0539  156 PHE   A CE2 
3463 C CZ  A PHE   A 156 ? 0.2630 0.1910 0.3271 0.0409  0.0078  0.0664  156 PHE   A CZ  
3464 C CZ  B PHE   A 156 ? 0.2329 0.1977 0.3764 -0.0086 -0.0362 0.0563  156 PHE   A CZ  
3483 N N   A ASP   A 157 ? 0.1964 0.1933 0.2516 0.0430  0.0306  0.0788  157 ASP   A N   
3484 N N   B ASP   A 157 ? 0.1549 0.1998 0.2870 0.0197  0.0370  0.0800  157 ASP   A N   
3485 C CA  A ASP   A 157 ? 0.2230 0.2231 0.2587 0.0358  0.0303  0.0841  157 ASP   A CA  
3486 C CA  B ASP   A 157 ? 0.1626 0.2108 0.2593 0.0276  0.0370  0.0925  157 ASP   A CA  
3487 C C   A ASP   A 157 ? 0.2279 0.2339 0.2592 0.0397  0.0292  0.0943  157 ASP   A C   
3488 C C   B ASP   A 157 ? 0.1642 0.2132 0.2373 0.0398  0.0339  0.0981  157 ASP   A C   
3489 O O   A ASP   A 157 ? 0.2300 0.2316 0.2521 0.0417  0.0257  0.0986  157 ASP   A O   
3490 O O   B ASP   A 157 ? 0.1675 0.2092 0.2454 0.0441  0.0468  0.0822  157 ASP   A O   
3491 C CB  A ASP   A 157 ? 0.2432 0.2398 0.2816 0.0322  0.0204  0.0776  157 ASP   A CB  
3492 C CB  B ASP   A 157 ? 0.1694 0.2136 0.2633 0.0288  0.0354  0.0998  157 ASP   A CB  
3493 C CG  A ASP   A 157 ? 0.2610 0.2517 0.3082 0.0310  0.0117  0.0757  157 ASP   A CG  
3494 C CG  B ASP   A 157 ? 0.1707 0.2119 0.2921 0.0310  0.0259  0.0977  157 ASP   A CG  
3495 O OD1 A ASP   A 157 ? 0.2706 0.2583 0.3205 0.0308  0.0079  0.0747  157 ASP   A OD1 
3496 O OD1 B ASP   A 157 ? 0.1799 0.1992 0.3207 0.0224  0.0176  0.0849  157 ASP   A OD1 
3497 O OD2 A ASP   A 157 ? 0.2676 0.2540 0.3269 0.0271  0.0089  0.0710  157 ASP   A OD2 
3498 O OD2 B ASP   A 157 ? 0.1760 0.2221 0.2910 0.0376  0.0173  0.1087  157 ASP   A OD2 
3507 N N   A LYS   A 158 ? 0.2325 0.2483 0.2773 0.0350  0.0346  0.0905  158 LYS   A N   
3508 N N   B LYS   A 158 ? 0.1697 0.2257 0.2367 0.0331  0.0362  0.0865  158 LYS   A N   
3509 C CA  A LYS   A 158 ? 0.2354 0.2618 0.3032 0.0333  0.0342  0.0853  158 LYS   A CA  
3510 C CA  B LYS   A 158 ? 0.1725 0.2414 0.2398 0.0288  0.0374  0.0769  158 LYS   A CA  
3511 C C   A LYS   A 158 ? 0.2267 0.2605 0.2976 0.0383  0.0232  0.0860  158 LYS   A C   
3512 C C   B LYS   A 158 ? 0.1770 0.2385 0.2390 0.0302  0.0292  0.0772  158 LYS   A C   
3513 O O   A LYS   A 158 ? 0.2246 0.2593 0.2907 0.0342  0.0251  0.0933  158 LYS   A O   
3514 O O   B LYS   A 158 ? 0.1694 0.2285 0.2472 0.0266  0.0306  0.0579  158 LYS   A O   
3515 C CB  A LYS   A 158 ? 0.2476 0.2737 0.3286 0.0270  0.0468  0.0788  158 LYS   A CB  
3516 C CB  B LYS   A 158 ? 0.1815 0.2565 0.2641 0.0197  0.0530  0.0554  158 LYS   A CB  
3517 C CG  A LYS   A 158 ? 0.2619 0.2859 0.3474 0.0223  0.0532  0.0772  158 LYS   A CG  
3518 C CG  B LYS   A 158 ? 0.1899 0.2732 0.2839 0.0126  0.0640  0.0404  158 LYS   A CG  
3519 C CD  A LYS   A 158 ? 0.2728 0.2952 0.3602 0.0189  0.0640  0.0785  158 LYS   A CD  
3520 C CD  B LYS   A 158 ? 0.2051 0.2932 0.3167 0.0108  0.0604  0.0249  158 LYS   A CD  
3521 C CE  A LYS   A 158 ? 0.2804 0.3019 0.3642 0.0139  0.0769  0.0829  158 LYS   A CE  
3522 C CE  B LYS   A 158 ? 0.2135 0.3032 0.3296 0.0108  0.0585  0.0180  158 LYS   A CE  
3523 N NZ  A LYS   A 158 ? 0.2851 0.3041 0.3653 0.0083  0.0851  0.0894  158 LYS   A NZ  
3524 N NZ  B LYS   A 158 ? 0.2186 0.3052 0.3340 0.0112  0.0585  0.0204  158 LYS   A NZ  
3551 N N   A ASN   A 159 ? 0.2205 0.2573 0.2989 0.0420  0.0109  0.0777  159 ASN   A N   
3552 N N   B ASN   A 159 ? 0.1927 0.2533 0.2445 0.0336  0.0209  0.0786  159 ASN   A N   
3553 C CA  A ASN   A 159 ? 0.2209 0.2537 0.2971 0.0443  -0.0018 0.0715  159 ASN   A CA  
3554 C CA  B ASN   A 159 ? 0.2192 0.2682 0.2692 0.0423  0.0138  0.0741  159 ASN   A CA  
3555 C C   A ASN   A 159 ? 0.2126 0.2453 0.2791 0.0542  -0.0066 0.0610  159 ASN   A C   
3556 C C   B ASN   A 159 ? 0.2273 0.2795 0.2737 0.0394  0.0291  0.0592  159 ASN   A C   
3557 O O   A ASN   A 159 ? 0.2041 0.2425 0.2808 0.0632  -0.0253 0.0571  159 ASN   A O   
3558 O O   B ASN   A 159 ? 0.2279 0.2791 0.2773 0.0359  0.0235  0.0530  159 ASN   A O   
3559 C CB  A ASN   A 159 ? 0.2285 0.2597 0.3156 0.0371  -0.0047 0.0741  159 ASN   A CB  
3560 C CB  B ASN   A 159 ? 0.2424 0.2737 0.3043 0.0512  -0.0130 0.0838  159 ASN   A CB  
3561 C CG  A ASN   A 159 ? 0.2339 0.2667 0.3309 0.0296  -0.0034 0.0612  159 ASN   A CG  
3562 C CG  B ASN   A 159 ? 0.2619 0.2786 0.3395 0.0600  -0.0305 0.0748  159 ASN   A CG  
3563 O OD1 A ASN   A 159 ? 0.2381 0.2711 0.3487 0.0324  0.0024  0.0566  159 ASN   A OD1 
3564 O OD1 B ASN   A 159 ? 0.2701 0.2839 0.3632 0.0610  -0.0454 0.0644  159 ASN   A OD1 
3565 N ND2 A ASN   A 159 ? 0.2345 0.2715 0.3474 0.0258  -0.0029 0.0530  159 ASN   A ND2 
3566 N ND2 B ASN   A 159 ? 0.2610 0.2849 0.3583 0.0680  -0.0169 0.0660  159 ASN   A ND2 
3579 N N   A LEU   A 160 ? 0.2106 0.2318 0.2452 0.0584  0.0035  0.0590  160 LEU   A N   
3580 N N   B LEU   A 160 ? 0.2302 0.2859 0.2695 0.0347  0.0464  0.0581  160 LEU   A N   
3581 C CA  A LEU   A 160 ? 0.2137 0.2243 0.2212 0.0543  0.0168  0.0604  160 LEU   A CA  
3582 C CA  B LEU   A 160 ? 0.2412 0.2949 0.2922 0.0211  0.0561  0.0504  160 LEU   A CA  
3583 C C   A LEU   A 160 ? 0.1933 0.2205 0.2128 0.0464  0.0308  0.0566  160 LEU   A C   
3584 C C   B LEU   A 160 ? 0.2125 0.2786 0.2641 0.0131  0.0512  0.0600  160 LEU   A C   
3585 O O   A LEU   A 160 ? 0.1879 0.2214 0.2272 0.0427  0.0279  0.0516  160 LEU   A O   
3586 O O   B LEU   A 160 ? 0.2062 0.2806 0.2598 0.0051  0.0407  0.0652  160 LEU   A O   
3587 C CB  A LEU   A 160 ? 0.2288 0.2213 0.1985 0.0571  0.0175  0.0601  160 LEU   A CB  
3588 C CB  B LEU   A 160 ? 0.2712 0.3175 0.3459 0.0120  0.0658  0.0298  160 LEU   A CB  
3589 C CG  A LEU   A 160 ? 0.2359 0.2181 0.2067 0.0571  0.0201  0.0442  160 LEU   A CG  
3590 C CG  B LEU   A 160 ? 0.2941 0.3358 0.4041 0.0017  0.0684  0.0008  160 LEU   A CG  
3591 C CD1 A LEU   A 160 ? 0.2378 0.2183 0.2057 0.0579  0.0232  0.0338  160 LEU   A CD1 
3592 C CD1 B LEU   A 160 ? 0.3021 0.3421 0.4248 0.0016  0.0683  -0.0135 160 LEU   A CD1 
3593 C CD2 A LEU   A 160 ? 0.2383 0.2173 0.1977 0.0584  0.0286  0.0363  160 LEU   A CD2 
3594 C CD2 B LEU   A 160 ? 0.2985 0.3411 0.4228 -0.0045 0.0739  -0.0104 160 LEU   A CD2 
3617 N N   A TYR   A 161 ? 0.1807 0.2093 0.1999 0.0430  0.0381  0.0631  161 TYR   A N   
3618 N N   B TYR   A 161 ? 0.1909 0.2518 0.2407 0.0106  0.0630  0.0617  161 TYR   A N   
3619 C CA  A TYR   A 161 ? 0.1689 0.2070 0.2024 0.0378  0.0413  0.0582  161 TYR   A CA  
3620 C CA  B TYR   A 161 ? 0.1820 0.2393 0.2405 0.0097  0.0451  0.0631  161 TYR   A CA  
3621 C C   A TYR   A 161 ? 0.1642 0.2205 0.2207 0.0359  0.0256  0.0636  161 TYR   A C   
3622 C C   B TYR   A 161 ? 0.1763 0.2321 0.2446 0.0087  0.0297  0.0738  161 TYR   A C   
3623 O O   A TYR   A 161 ? 0.1581 0.2194 0.2116 0.0308  0.0281  0.0593  161 TYR   A O   
3624 O O   B TYR   A 161 ? 0.1684 0.2169 0.2374 0.0094  0.0265  0.0693  161 TYR   A O   
3625 C CB  A TYR   A 161 ? 0.1683 0.2026 0.1965 0.0333  0.0539  0.0519  161 TYR   A CB  
3626 C CB  B TYR   A 161 ? 0.1804 0.2385 0.2319 0.0073  0.0427  0.0657  161 TYR   A CB  
3627 C CG  A TYR   A 161 ? 0.1657 0.1977 0.1970 0.0359  0.0479  0.0490  161 TYR   A CG  
3628 C CG  B TYR   A 161 ? 0.1709 0.2291 0.2327 0.0079  0.0259  0.0664  161 TYR   A CG  
3629 C CD1 A TYR   A 161 ? 0.1663 0.1933 0.2039 0.0311  0.0519  0.0473  161 TYR   A CD1 
3630 C CD1 B TYR   A 161 ? 0.1699 0.2277 0.2382 0.0088  0.0195  0.0663  161 TYR   A CD1 
3631 C CD2 A TYR   A 161 ? 0.1643 0.1941 0.1961 0.0412  0.0376  0.0525  161 TYR   A CD2 
3632 C CD2 B TYR   A 161 ? 0.1653 0.2213 0.2360 0.0066  0.0251  0.0641  161 TYR   A CD2 
3633 C CE1 A TYR   A 161 ? 0.1725 0.1898 0.2129 0.0271  0.0441  0.0603  161 TYR   A CE1 
3634 C CE1 B TYR   A 161 ? 0.1676 0.2268 0.2377 0.0084  0.0145  0.0711  161 TYR   A CE1 
3635 C CE2 A TYR   A 161 ? 0.1734 0.1914 0.2156 0.0333  0.0323  0.0618  161 TYR   A CE2 
3636 C CE2 B TYR   A 161 ? 0.1646 0.2201 0.2286 -0.0016 0.0173  0.0725  161 TYR   A CE2 
3637 C CZ  A TYR   A 161 ? 0.1835 0.1905 0.2260 0.0267  0.0320  0.0697  161 TYR   A CZ  
3638 C CZ  B TYR   A 161 ? 0.1770 0.2258 0.2309 -0.0006 0.0090  0.0750  161 TYR   A CZ  
3639 O OH  A TYR   A 161 ? 0.2013 0.1908 0.2534 0.0247  0.0174  0.0786  161 TYR   A OH  
3640 O OH  B TYR   A 161 ? 0.1950 0.2316 0.2369 -0.0069 0.0099  0.0764  161 TYR   A OH  
3659 N N   A ASP   A 162 ? 0.1660 0.2320 0.2378 0.0339  0.0207  0.0837  162 ASP   A N   
3660 N N   B ASP   A 162 ? 0.1772 0.2457 0.2617 0.0090  0.0358  0.0804  162 ASP   A N   
3661 C CA  A ASP   A 162 ? 0.1656 0.2489 0.2437 0.0300  0.0187  0.0914  162 ASP   A CA  
3662 C CA  B ASP   A 162 ? 0.1775 0.2602 0.2705 0.0222  0.0295  0.0859  162 ASP   A CA  
3663 C C   A ASP   A 162 ? 0.1560 0.2602 0.2470 0.0193  0.0182  0.0915  162 ASP   A C   
3664 C C   B ASP   A 162 ? 0.1848 0.2747 0.2837 0.0226  0.0179  0.0807  162 ASP   A C   
3665 O O   A ASP   A 162 ? 0.1498 0.2610 0.2540 0.0109  0.0146  0.0980  162 ASP   A O   
3666 O O   B ASP   A 162 ? 0.1761 0.2761 0.2902 0.0265  0.0045  0.0755  162 ASP   A O   
3667 C CB  A ASP   A 162 ? 0.1816 0.2570 0.2526 0.0342  0.0282  0.0905  162 ASP   A CB  
3668 C CB  B ASP   A 162 ? 0.1815 0.2633 0.2918 0.0318  0.0305  0.0879  162 ASP   A CB  
3669 C CG  A ASP   A 162 ? 0.1996 0.2717 0.2736 0.0280  0.0351  0.0836  162 ASP   A CG  
3670 C CG  B ASP   A 162 ? 0.1877 0.2674 0.3004 0.0367  0.0290  0.1019  162 ASP   A CG  
3671 O OD1 A ASP   A 162 ? 0.2081 0.2767 0.2720 0.0283  0.0311  0.0897  162 ASP   A OD1 
3672 O OD1 B ASP   A 162 ? 0.1891 0.2741 0.3055 0.0390  0.0228  0.1158  162 ASP   A OD1 
3673 O OD2 A ASP   A 162 ? 0.2084 0.2761 0.2906 0.0240  0.0443  0.0768  162 ASP   A OD2 
3674 O OD2 B ASP   A 162 ? 0.1955 0.2707 0.2993 0.0492  0.0294  0.0998  162 ASP   A OD2 
3683 N N   A LYS   A 163 ? 0.1629 0.2710 0.2548 0.0155  0.0105  0.0745  163 LYS   A N   
3684 N N   B LYS   A 163 ? 0.2084 0.2894 0.2877 0.0261  0.0223  0.0760  163 LYS   A N   
3685 C CA  A LYS   A 163 ? 0.1696 0.2830 0.2708 0.0100  0.0039  0.0612  163 LYS   A CA  
3686 C CA  B LYS   A 163 ? 0.2293 0.3052 0.3082 0.0268  0.0215  0.0662  163 LYS   A CA  
3687 C C   A LYS   A 163 ? 0.1575 0.2768 0.2755 0.0061  0.0101  0.0496  163 LYS   A C   
3688 C C   B LYS   A 163 ? 0.2162 0.2862 0.2931 0.0200  0.0230  0.0591  163 LYS   A C   
3689 O O   A LYS   A 163 ? 0.1534 0.2849 0.2880 0.0010  0.0093  0.0386  163 LYS   A O   
3690 O O   B LYS   A 163 ? 0.2084 0.2836 0.2985 0.0079  0.0239  0.0460  163 LYS   A O   
3691 C CB  A LYS   A 163 ? 0.1975 0.2982 0.3004 0.0099  0.0028  0.0541  163 LYS   A CB  
3692 C CB  B LYS   A 163 ? 0.2692 0.3361 0.3498 0.0333  0.0287  0.0631  163 LYS   A CB  
3693 C CG  A LYS   A 163 ? 0.2252 0.3124 0.3378 0.0077  0.0039  0.0430  163 LYS   A CG  
3694 C CG  B LYS   A 163 ? 0.3075 0.3635 0.3968 0.0332  0.0343  0.0595  163 LYS   A CG  
3695 C CD  A LYS   A 163 ? 0.2500 0.3265 0.3819 0.0037  0.0017  0.0343  163 LYS   A CD  
3696 C CD  B LYS   A 163 ? 0.3410 0.3857 0.4497 0.0305  0.0398  0.0555  163 LYS   A CD  
3697 C CE  A LYS   A 163 ? 0.2735 0.3369 0.4119 -0.0021 0.0024  0.0317  163 LYS   A CE  
3698 C CE  B LYS   A 163 ? 0.3672 0.3993 0.4880 0.0290  0.0451  0.0575  163 LYS   A CE  
3699 N NZ  A LYS   A 163 ? 0.2804 0.3426 0.4288 -0.0065 0.0036  0.0341  163 LYS   A NZ  
3700 N NZ  B LYS   A 163 ? 0.3781 0.4060 0.5164 0.0286  0.0493  0.0560  163 LYS   A NZ  
3727 N N   A LEU   A 164 ? 0.1425 0.2531 0.2600 -0.0007 0.0112  0.0509  164 LEU   A N   
3728 N N   B LEU   A 164 ? 0.2031 0.2657 0.2689 0.0160  0.0251  0.0568  164 LEU   A N   
3729 C CA  A LEU   A 164 ? 0.1373 0.2374 0.2544 -0.0120 0.0274  0.0465  164 LEU   A CA  
3730 C CA  B LEU   A 164 ? 0.1967 0.2533 0.2643 0.0055  0.0384  0.0439  164 LEU   A CA  
3731 C C   A LEU   A 164 ? 0.1462 0.2406 0.2583 -0.0015 0.0349  0.0369  164 LEU   A C   
3732 C C   B LEU   A 164 ? 0.1884 0.2398 0.2704 -0.0053 0.0348  0.0355  164 LEU   A C   
3733 O O   A LEU   A 164 ? 0.1459 0.2397 0.2577 0.0051  0.0500  0.0301  164 LEU   A O   
3734 O O   B LEU   A 164 ? 0.1883 0.2354 0.2721 -0.0086 0.0407  0.0307  164 LEU   A O   
3735 C CB  A LEU   A 164 ? 0.1336 0.2224 0.2515 -0.0252 0.0292  0.0482  164 LEU   A CB  
3736 C CB  B LEU   A 164 ? 0.1997 0.2538 0.2654 0.0113  0.0477  0.0365  164 LEU   A CB  
3737 C CG  A LEU   A 164 ? 0.1393 0.2121 0.2578 -0.0304 0.0163  0.0474  164 LEU   A CG  
3738 C CG  B LEU   A 164 ? 0.2085 0.2551 0.2706 0.0164  0.0443  0.0372  164 LEU   A CG  
3739 C CD1 A LEU   A 164 ? 0.1393 0.2107 0.2691 -0.0339 0.0079  0.0439  164 LEU   A CD1 
3740 C CD1 B LEU   A 164 ? 0.2080 0.2539 0.2757 0.0157  0.0449  0.0404  164 LEU   A CD1 
3741 C CD2 A LEU   A 164 ? 0.1505 0.2114 0.2595 -0.0269 0.0134  0.0403  164 LEU   A CD2 
3742 C CD2 B LEU   A 164 ? 0.2170 0.2583 0.2740 0.0167  0.0415  0.0338  164 LEU   A CD2 
3765 N N   A VAL   A 165 ? 0.1434 0.2443 0.2568 -0.0020 0.0278  0.0422  165 VAL   A N   
3766 N N   B VAL   A 165 ? 0.1689 0.2335 0.2601 -0.0190 0.0336  0.0407  165 VAL   A N   
3767 C CA  A VAL   A 165 ? 0.1566 0.2529 0.2619 -0.0017 0.0294  0.0500  165 VAL   A CA  
3768 C CA  B VAL   A 165 ? 0.1780 0.2424 0.2585 -0.0135 0.0297  0.0392  165 VAL   A CA  
3769 C C   A VAL   A 165 ? 0.1544 0.2559 0.2622 -0.0000 0.0277  0.0575  165 VAL   A C   
3770 C C   B VAL   A 165 ? 0.1717 0.2419 0.2634 -0.0168 0.0318  0.0347  165 VAL   A C   
3771 O O   A VAL   A 165 ? 0.1517 0.2577 0.2626 -0.0042 0.0312  0.0590  165 VAL   A O   
3772 O O   B VAL   A 165 ? 0.1698 0.2333 0.2570 -0.0214 0.0302  0.0345  165 VAL   A O   
3773 C CB  A VAL   A 165 ? 0.1690 0.2576 0.2640 -0.0029 0.0282  0.0550  165 VAL   A CB  
3774 C CB  B VAL   A 165 ? 0.1958 0.2562 0.2636 -0.0094 0.0236  0.0406  165 VAL   A CB  
3775 C CG1 A VAL   A 165 ? 0.1754 0.2602 0.2622 -0.0063 0.0305  0.0545  165 VAL   A CG1 
3776 C CG1 B VAL   A 165 ? 0.2047 0.2625 0.2572 -0.0127 0.0290  0.0354  165 VAL   A CG1 
3777 C CG2 A VAL   A 165 ? 0.1758 0.2591 0.2715 -0.0003 0.0265  0.0561  165 VAL   A CG2 
3778 C CG2 B VAL   A 165 ? 0.2016 0.2594 0.2674 0.0002  0.0097  0.0462  165 VAL   A CG2 
3797 N N   A SER   A 166 ? 0.1501 0.2565 0.2712 -0.0023 0.0293  0.0573  166 SER   A N   
3798 N N   B SER   A 166 ? 0.1556 0.2545 0.2660 -0.0147 0.0382  0.0240  166 SER   A N   
3799 C CA  A SER   A 166 ? 0.1551 0.2633 0.2849 -0.0105 0.0309  0.0588  166 SER   A CA  
3800 C CA  B SER   A 166 ? 0.1612 0.2726 0.2819 -0.0063 0.0255  0.0162  166 SER   A CA  
3801 C C   A SER   A 166 ? 0.1578 0.2735 0.2896 -0.0102 0.0133  0.0440  166 SER   A C   
3802 C C   B SER   A 166 ? 0.1579 0.2774 0.2745 -0.0002 -0.0006 0.0194  166 SER   A C   
3803 O O   A SER   A 166 ? 0.1583 0.2779 0.3039 -0.0071 0.0059  0.0392  166 SER   A O   
3804 O O   B SER   A 166 ? 0.1694 0.2793 0.2753 0.0009  -0.0177 0.0214  166 SER   A O   
3805 C CB  A SER   A 166 ? 0.1748 0.2637 0.3082 -0.0112 0.0304  0.0688  166 SER   A CB  
3806 C CB  B SER   A 166 ? 0.1818 0.2897 0.3135 0.0020  0.0132  0.0056  166 SER   A CB  
3807 O OG  A SER   A 166 ? 0.2043 0.2676 0.3396 -0.0104 0.0244  0.0788  166 SER   A OG  
3808 O OG  B SER   A 166 ? 0.2184 0.3077 0.3527 -0.0064 0.0149  0.0103  166 SER   A OG  
3819 N N   A SER   A 167 ? 0.1700 0.2797 0.2814 -0.0051 0.0100  0.0318  167 SER   A N   
3820 N N   B SER   A 167 ? 0.1619 0.2882 0.2661 0.0081  0.0041  0.0216  167 SER   A N   
3821 C CA  A SER   A 167 ? 0.1909 0.2873 0.2851 0.0021  0.0047  0.0154  167 SER   A CA  
3822 C CA  B SER   A 167 ? 0.1810 0.2959 0.2730 0.0127  0.0007  0.0190  167 SER   A CA  
3823 C C   A SER   A 167 ? 0.2015 0.2893 0.2828 0.0068  0.0088  0.0086  167 SER   A C   
3824 C C   B SER   A 167 ? 0.1881 0.2951 0.2763 0.0210  0.0126  0.0166  167 SER   A C   
3825 O O   A SER   A 167 ? 0.2095 0.2890 0.2851 0.0136  0.0035  0.0066  167 SER   A O   
3826 O O   B SER   A 167 ? 0.2063 0.2972 0.2815 0.0259  0.0053  0.0159  167 SER   A O   
3827 C CB  A SER   A 167 ? 0.2019 0.2947 0.2941 0.0082  0.0064  0.0131  167 SER   A CB  
3828 C CB  B SER   A 167 ? 0.1910 0.3049 0.2745 0.0116  0.0070  0.0261  167 SER   A CB  
3829 O OG  A SER   A 167 ? 0.2099 0.2997 0.3041 0.0102  0.0101  0.0131  167 SER   A OG  
3830 O OG  B SER   A 167 ? 0.1996 0.3113 0.2807 0.0084  0.0232  0.0300  167 SER   A OG  
3841 N N   A PHE   A 168 ? 0.2066 0.2954 0.2825 0.0056  0.0074  0.0079  168 PHE   A N   
3842 N N   B PHE   A 168 ? 0.1798 0.2949 0.2778 0.0244  0.0179  0.0233  168 PHE   A N   
3843 C CA  A PHE   A 168 ? 0.2199 0.3065 0.2948 -0.0009 0.0070  0.0096  168 PHE   A CA  
3844 C CA  B PHE   A 168 ? 0.1832 0.3059 0.3060 0.0119  0.0303  0.0302  168 PHE   A CA  
3845 C C   A PHE   A 168 ? 0.2494 0.3310 0.3274 -0.0065 0.0211  0.0039  168 PHE   A C   
3846 C C   B PHE   A 168 ? 0.2083 0.3316 0.3390 -0.0010 0.0657  0.0214  168 PHE   A C   
3847 O O   A PHE   A 168 ? 0.2455 0.3338 0.3312 -0.0121 0.0302  0.0110  168 PHE   A O   
3848 O O   B PHE   A 168 ? 0.1999 0.3327 0.3513 -0.0162 0.0928  0.0366  168 PHE   A O   
3849 C CB  A PHE   A 168 ? 0.2145 0.2967 0.2826 -0.0037 -0.0044 0.0158  168 PHE   A CB  
3850 C CB  B PHE   A 168 ? 0.1773 0.2980 0.3064 0.0069  0.0146  0.0425  168 PHE   A CB  
3851 C CG  A PHE   A 168 ? 0.2082 0.2889 0.2709 -0.0081 -0.0107 0.0213  168 PHE   A CG  
3852 C CG  B PHE   A 168 ? 0.1669 0.2923 0.2978 -0.0047 0.0096  0.0544  168 PHE   A CG  
3853 C CD1 A PHE   A 168 ? 0.2059 0.2882 0.2725 -0.0110 -0.0123 0.0263  168 PHE   A CD1 
3854 C CD1 B PHE   A 168 ? 0.1607 0.2942 0.2999 -0.0073 0.0021  0.0633  168 PHE   A CD1 
3855 C CD2 A PHE   A 168 ? 0.2056 0.2856 0.2718 -0.0091 -0.0070 0.0243  168 PHE   A CD2 
3856 C CD2 B PHE   A 168 ? 0.1596 0.2901 0.2991 -0.0145 0.0272  0.0604  168 PHE   A CD2 
3857 C CE1 A PHE   A 168 ? 0.2022 0.2862 0.2680 -0.0127 -0.0121 0.0300  168 PHE   A CE1 
3858 C CE1 B PHE   A 168 ? 0.1544 0.2941 0.2989 -0.0095 0.0017  0.0706  168 PHE   A CE1 
3859 C CE2 A PHE   A 168 ? 0.2077 0.2832 0.2720 -0.0081 -0.0053 0.0289  168 PHE   A CE2 
3860 C CE2 B PHE   A 168 ? 0.1636 0.2876 0.3060 -0.0127 0.0264  0.0673  168 PHE   A CE2 
3861 C CZ  A PHE   A 168 ? 0.2043 0.2837 0.2670 -0.0114 -0.0112 0.0304  168 PHE   A CZ  
3862 C CZ  B PHE   A 168 ? 0.1565 0.2902 0.2985 -0.0117 0.0091  0.0693  168 PHE   A CZ  
3881 N N   A LEU   A 169 ? 0.2932 0.3547 0.3671 -0.0096 0.0157  -0.0090 169 LEU   A N   
3882 N N   B LEU   A 169 ? 0.2688 0.3599 0.3782 -0.0073 0.0477  -0.0010 169 LEU   A N   
3883 C CA  A LEU   A 169 ? 0.3427 0.3829 0.4188 -0.0102 0.0009  -0.0171 169 LEU   A CA  
3884 C CA  B LEU   A 169 ? 0.3385 0.3954 0.4284 -0.0102 0.0162  -0.0151 169 LEU   A CA  
3885 C C   A LEU   A 169 ? 0.3572 0.3925 0.4368 -0.0119 -0.0055 -0.0118 169 LEU   A C   
3886 C C   B LEU   A 169 ? 0.3589 0.4061 0.4415 -0.0130 0.0025  -0.0072 169 LEU   A C   
3887 O O   A LEU   A 169 ? 0.3634 0.3972 0.4344 -0.0116 -0.0060 -0.0128 169 LEU   A O   
3888 O O   B LEU   A 169 ? 0.3628 0.4108 0.4375 -0.0099 0.0002  -0.0056 169 LEU   A O   
3889 C CB  A LEU   A 169 ? 0.3717 0.4002 0.4382 -0.0099 -0.0032 -0.0306 169 LEU   A CB  
3890 C CB  B LEU   A 169 ? 0.3786 0.4181 0.4440 -0.0122 0.0079  -0.0357 169 LEU   A CB  
3891 C CG  A LEU   A 169 ? 0.3932 0.4148 0.4615 -0.0114 -0.0060 -0.0438 169 LEU   A CG  
3892 C CG  B LEU   A 169 ? 0.4101 0.4374 0.4648 -0.0163 0.0028  -0.0558 169 LEU   A CG  
3893 C CD1 A LEU   A 169 ? 0.3975 0.4184 0.4691 -0.0125 -0.0076 -0.0479 169 LEU   A CD1 
3894 C CD1 B LEU   A 169 ? 0.4165 0.4425 0.4721 -0.0185 -0.0003 -0.0619 169 LEU   A CD1 
3895 C CD2 A LEU   A 169 ? 0.4029 0.4220 0.4644 -0.0118 -0.0053 -0.0488 169 LEU   A CD2 
3896 C CD2 B LEU   A 169 ? 0.4213 0.4465 0.4657 -0.0173 0.0039  -0.0632 169 LEU   A CD2 
3897 O OXT A LEU   A 169 ? 0.3533 0.3947 0.4397 -0.0141 -0.0056 -0.0080 169 LEU   A OXT 
3898 O OXT B LEU   A 169 ? 0.3564 0.4084 0.4388 -0.0193 0.0011  -0.0030 169 LEU   A OXT 
3921 N N   A SER   B 1   ? 0.3710 0.3555 0.3765 -0.0893 -0.0724 0.0381  1   SER   B N   
3922 N N   B SER   B 1   ? 0.3620 0.3520 0.3500 -0.1039 -0.0639 0.0546  1   SER   B N   
3923 C CA  A SER   B 1   ? 0.3664 0.3564 0.3841 -0.0909 -0.0718 0.0375  1   SER   B CA  
3924 C CA  B SER   B 1   ? 0.3550 0.3529 0.3584 -0.1075 -0.0631 0.0522  1   SER   B CA  
3925 C C   A SER   B 1   ? 0.3490 0.3541 0.3651 -0.0908 -0.0731 0.0500  1   SER   B C   
3926 C C   B SER   B 1   ? 0.3297 0.3524 0.3195 -0.1083 -0.0673 0.0722  1   SER   B C   
3927 O O   A SER   B 1   ? 0.3552 0.3570 0.3545 -0.0885 -0.0726 0.0470  1   SER   B O   
3928 O O   B SER   B 1   ? 0.3363 0.3540 0.2902 -0.1020 -0.0649 0.0719  1   SER   B O   
3929 C CB  A SER   B 1   ? 0.3763 0.3567 0.3831 -0.0911 -0.0683 0.0283  1   SER   B CB  
3930 C CB  B SER   B 1   ? 0.3694 0.3506 0.3725 -0.1074 -0.0565 0.0349  1   SER   B CB  
3931 O OG  A SER   B 1   ? 0.3859 0.3631 0.4178 -0.0892 -0.0657 0.0256  1   SER   B OG  
3932 O OG  B SER   B 1   ? 0.3834 0.3576 0.4260 -0.1036 -0.0556 0.0254  1   SER   B OG  
3947 N N   A MET   B 2   ? 0.3253 0.3457 0.3531 -0.0915 -0.0706 0.0730  2   MET   B N   
3948 N N   B MET   B 2   ? 0.3014 0.3475 0.3091 -0.1100 -0.0647 0.1084  2   MET   B N   
3949 C CA  A MET   B 2   ? 0.3042 0.3392 0.3522 -0.0822 -0.0687 0.0877  2   MET   B CA  
3950 C CA  B MET   B 2   ? 0.2836 0.3500 0.3188 -0.0898 -0.0694 0.1204  2   MET   B CA  
3951 C C   A MET   B 2   ? 0.2638 0.3123 0.3043 -0.0778 -0.0807 0.1117  2   MET   B C   
3952 C C   B MET   B 2   ? 0.2492 0.3350 0.2831 -0.0676 -0.0802 0.1292  2   MET   B C   
3953 O O   A MET   B 2   ? 0.2578 0.3161 0.2827 -0.0767 -0.0918 0.1269  2   MET   B O   
3954 O O   B MET   B 2   ? 0.2457 0.3514 0.2859 -0.0567 -0.0875 0.1211  2   MET   B O   
3955 C CB  A MET   B 2   ? 0.3274 0.3629 0.4140 -0.0680 -0.0514 0.0702  2   MET   B CB  
3956 C CB  B MET   B 2   ? 0.3094 0.3758 0.3863 -0.0743 -0.0615 0.1077  2   MET   B CB  
3957 C CG  A MET   B 2   ? 0.3497 0.3836 0.4683 -0.0538 -0.0347 0.0587  2   MET   B CG  
3958 C CG  B MET   B 2   ? 0.3337 0.3987 0.4391 -0.0588 -0.0481 0.1072  2   MET   B CG  
3959 S SD  A MET   B 2   ? 0.3699 0.4016 0.5314 -0.0425 -0.0253 0.0507  2   MET   B SD  
3960 S SD  B MET   B 2   ? 0.3572 0.4223 0.4968 -0.0440 -0.0469 0.1050  2   MET   B SD  
3961 C CE  A MET   B 2   ? 0.3753 0.4074 0.5270 -0.0405 -0.0204 0.0508  2   MET   B CE  
3962 C CE  B MET   B 2   ? 0.3608 0.4268 0.4945 -0.0440 -0.0489 0.0991  2   MET   B CE  
3981 N N   A VAL   B 3   ? 0.2312 0.2767 0.2834 -0.0808 -0.0725 0.1149  3   VAL   B N   
3982 N N   B VAL   B 3   ? 0.2223 0.3004 0.2701 -0.0639 -0.0670 0.1353  3   VAL   B N   
3983 C CA  A VAL   B 3   ? 0.2127 0.2481 0.2693 -0.0766 -0.0610 0.1049  3   VAL   B CA  
3984 C CA  B VAL   B 3   ? 0.2152 0.2724 0.2638 -0.0529 -0.0489 0.1086  3   VAL   B CA  
3985 C C   A VAL   B 3   ? 0.1898 0.2324 0.2399 -0.0675 -0.0546 0.1002  3   VAL   B C   
3986 C C   B VAL   B 3   ? 0.1955 0.2553 0.2366 -0.0460 -0.0426 0.1009  3   VAL   B C   
3987 O O   A VAL   B 3   ? 0.1840 0.2211 0.2353 -0.0667 -0.0556 0.1078  3   VAL   B O   
3988 O O   B VAL   B 3   ? 0.1956 0.2648 0.2420 -0.0238 -0.0483 0.0995  3   VAL   B O   
3989 C CB  A VAL   B 3   ? 0.2258 0.2437 0.2924 -0.0769 -0.0530 0.0890  3   VAL   B CB  
3990 C CB  B VAL   B 3   ? 0.2367 0.2627 0.2852 -0.0485 -0.0376 0.0908  3   VAL   B CB  
3991 C CG1 A VAL   B 3   ? 0.2324 0.2422 0.2993 -0.0756 -0.0520 0.0824  3   VAL   B CG1 
3992 C CG1 B VAL   B 3   ? 0.2444 0.2574 0.2984 -0.0482 -0.0333 0.0847  3   VAL   B CG1 
3993 C CG2 A VAL   B 3   ? 0.2295 0.2430 0.3020 -0.0789 -0.0389 0.0914  3   VAL   B CG2 
3994 C CG2 B VAL   B 3   ? 0.2452 0.2648 0.2846 -0.0472 -0.0288 0.0906  3   VAL   B CG2 
4013 N N   . ASN   B 4   ? 0.1856 0.2282 0.2228 -0.0580 -0.0472 0.0890  4   ASN   B N   
4014 C CA  . ASN   B 4   ? 0.1862 0.2284 0.1914 -0.0592 -0.0428 0.0503  4   ASN   B CA  
4015 C C   . ASN   B 4   ? 0.1932 0.2424 0.1735 -0.0625 -0.0338 0.0334  4   ASN   B C   
4016 O O   . ASN   B 4   ? 0.1939 0.2507 0.1950 -0.0519 -0.0282 0.0106  4   ASN   B O   
4017 C CB  . ASN   B 4   ? 0.1896 0.2246 0.1661 -0.0543 -0.0532 0.0434  4   ASN   B CB  
4018 C CG  . ASN   B 4   ? 0.1900 0.2071 0.1512 -0.0558 -0.0481 0.0347  4   ASN   B CG  
4019 O OD1 . ASN   B 4   ? 0.1954 0.1868 0.1594 -0.0515 -0.0483 0.0296  4   ASN   B OD1 
4020 N ND2 . ASN   B 4   ? 0.2081 0.2185 0.1642 -0.0314 -0.0388 0.0302  4   ASN   B ND2 
4028 N N   . SER   B 5   ? 0.2076 0.2622 0.1860 -0.0643 -0.0276 0.0357  5   SER   B N   
4029 C CA  . SER   B 5   ? 0.2355 0.2946 0.2065 -0.0510 -0.0082 0.0351  5   SER   B CA  
4030 C C   . SER   B 5   ? 0.2524 0.2985 0.2439 -0.0664 0.0215  0.0310  5   SER   B C   
4031 O O   . SER   B 5   ? 0.2697 0.2932 0.3273 -0.0603 0.0607  0.0321  5   SER   B O   
4032 C CB  . SER   B 5   ? 0.2535 0.3146 0.2202 -0.0340 -0.0085 0.0471  5   SER   B CB  
4033 O OG  . SER   B 5   ? 0.2736 0.3353 0.2707 -0.0219 -0.0022 0.0548  5   SER   B OG  
4039 N N   . PHE   B 6   ? 0.2685 0.3131 0.2197 -0.0723 0.0279  0.0333  6   PHE   B N   
4040 C CA  . PHE   B 6   ? 0.2782 0.3169 0.1911 -0.0912 0.0371  0.0108  6   PHE   B CA  
4041 C C   . PHE   B 6   ? 0.3301 0.3509 0.2182 -0.1012 0.0584  -0.0202 6   PHE   B C   
4042 O O   . PHE   B 6   ? 0.3471 0.3850 0.2614 -0.0942 0.0430  -0.0371 6   PHE   B O   
4043 C CB  . PHE   B 6   ? 0.2518 0.2934 0.1652 -0.0810 0.0161  0.0078  6   PHE   B CB  
4044 C CG  . PHE   B 6   ? 0.2199 0.2613 0.1493 -0.0784 0.0006  0.0085  6   PHE   B CG  
4045 C CD1 . PHE   B 6   ? 0.2183 0.2333 0.1361 -0.0726 -0.0124 0.0101  6   PHE   B CD1 
4046 C CD2 . PHE   B 6   ? 0.1997 0.2611 0.1519 -0.0665 -0.0054 0.0402  6   PHE   B CD2 
4047 C CE1 . PHE   B 6   ? 0.2169 0.2130 0.1471 -0.0645 -0.0238 0.0160  6   PHE   B CE1 
4048 C CE2 . PHE   B 6   ? 0.2030 0.2492 0.1867 -0.0570 -0.0038 0.0387  6   PHE   B CE2 
4049 C CZ  . PHE   B 6   ? 0.2077 0.2227 0.1679 -0.0574 -0.0116 0.0228  6   PHE   B CZ  
4059 N N   . SER   B 7   ? 0.3656 0.3315 0.2343 -0.1242 0.0862  -0.0505 7   SER   B N   
4060 C CA  . SER   B 7   ? 0.3967 0.3369 0.2891 -0.1196 0.1098  -0.0614 7   SER   B CA  
4061 C C   . SER   B 7   ? 0.3916 0.3263 0.2892 -0.1197 0.1288  -0.0691 7   SER   B C   
4062 O O   . SER   B 7   ? 0.3970 0.3319 0.3225 -0.1171 0.1278  -0.0654 7   SER   B O   
4063 C CB  . SER   B 7   ? 0.4216 0.3551 0.3498 -0.1138 0.1209  -0.0598 7   SER   B CB  
4064 O OG  . SER   B 7   ? 0.4358 0.3617 0.4001 -0.1143 0.1205  -0.0470 7   SER   B OG  
4070 N N   . GLY   B 8   ? 0.3880 0.3186 0.3041 -0.1078 0.1376  -0.0759 8   GLY   B N   
4071 C CA  . GLY   B 8   ? 0.3728 0.2995 0.2973 -0.0983 0.1374  -0.0772 8   GLY   B CA  
4072 C C   . GLY   B 8   ? 0.3480 0.2718 0.2922 -0.0951 0.1346  -0.0639 8   GLY   B C   
4073 O O   . GLY   B 8   ? 0.3565 0.2731 0.3314 -0.0920 0.1362  -0.0733 8   GLY   B O   
4077 N N   . TYR   B 9   ? 0.3250 0.2492 0.2634 -0.0836 0.1061  -0.0710 9   TYR   B N   
4078 C CA  . TYR   B 9   ? 0.3020 0.2244 0.2300 -0.0711 0.0825  -0.0571 9   TYR   B CA  
4079 C C   . TYR   B 9   ? 0.2970 0.2234 0.2158 -0.0688 0.0552  -0.0448 9   TYR   B C   
4080 O O   . TYR   B 9   ? 0.3133 0.2426 0.2594 -0.0741 0.0561  -0.0386 9   TYR   B O   
4081 C CB  . TYR   B 9   ? 0.2897 0.1995 0.2366 -0.0642 0.0774  -0.0617 9   TYR   B CB  
4082 C CG  . TYR   B 9   ? 0.2853 0.1841 0.2438 -0.0643 0.0673  -0.0658 9   TYR   B CG  
4083 C CD1 . TYR   B 9   ? 0.2930 0.1869 0.2624 -0.0774 0.0687  -0.0520 9   TYR   B CD1 
4084 C CD2 . TYR   B 9   ? 0.2712 0.1844 0.2320 -0.0583 0.0604  -0.0699 9   TYR   B CD2 
4085 C CE1 . TYR   B 9   ? 0.2898 0.1985 0.2664 -0.0802 0.0728  -0.0626 9   TYR   B CE1 
4086 C CE2 . TYR   B 9   ? 0.2747 0.1880 0.2430 -0.0603 0.0601  -0.0652 9   TYR   B CE2 
4087 C CZ  . TYR   B 9   ? 0.2798 0.2038 0.2554 -0.0750 0.0682  -0.0772 9   TYR   B CZ  
4088 O OH  . TYR   B 9   ? 0.2768 0.2143 0.2741 -0.0902 0.0702  -0.0843 9   TYR   B OH  
4098 N N   . LEU   B 10  ? 0.2747 0.1997 0.1973 -0.0641 0.0305  -0.0469 10  LEU   B N   
4099 C CA  . LEU   B 10  ? 0.2730 0.1982 0.1993 -0.0695 -0.0067 -0.0421 10  LEU   B CA  
4100 C C   . LEU   B 10  ? 0.2497 0.1946 0.1958 -0.0630 -0.0223 -0.0381 10  LEU   B C   
4101 O O   . LEU   B 10  ? 0.2313 0.1899 0.2020 -0.0400 -0.0105 -0.0312 10  LEU   B O   
4102 C CB  . LEU   B 10  ? 0.2960 0.1974 0.2160 -0.0750 -0.0233 -0.0232 10  LEU   B CB  
4103 C CG  . LEU   B 10  ? 0.3268 0.2034 0.2598 -0.0719 -0.0498 -0.0139 10  LEU   B CG  
4104 C CD1 . LEU   B 10  ? 0.3489 0.2109 0.2866 -0.0708 -0.0428 -0.0141 10  LEU   B CD1 
4105 C CD2 . LEU   B 10  ? 0.3330 0.2112 0.2911 -0.0738 -0.0509 0.0094  10  LEU   B CD2 
4117 N N   . LYS   B 11  ? 0.2658 0.2256 0.1977 -0.0570 -0.0363 -0.0305 11  LYS   B N   
4118 C CA  . LYS   B 11  ? 0.2875 0.2488 0.2313 -0.0505 -0.0455 -0.0332 11  LYS   B CA  
4119 C C   . LYS   B 11  ? 0.2771 0.2254 0.2362 -0.0699 -0.0337 -0.0408 11  LYS   B C   
4120 O O   . LYS   B 11  ? 0.2950 0.2416 0.2652 -0.0860 -0.0243 -0.0695 11  LYS   B O   
4121 C CB  . LYS   B 11  ? 0.3207 0.2991 0.3077 -0.0229 -0.0535 -0.0283 11  LYS   B CB  
4122 C CG  . LYS   B 11  ? 0.3525 0.3325 0.3861 -0.0069 -0.0515 -0.0286 11  LYS   B CG  
4123 C CD  . LYS   B 11  ? 0.3769 0.3555 0.4561 -0.0002 -0.0478 -0.0301 11  LYS   B CD  
4124 C CE  . LYS   B 11  ? 0.3957 0.3713 0.5022 0.0004  -0.0518 -0.0338 11  LYS   B CE  
4125 N NZ  . LYS   B 11  ? 0.4060 0.3811 0.5290 -0.0006 -0.0566 -0.0346 11  LYS   B NZ  
4139 N N   . LEU   B 12  ? 0.2434 0.1946 0.2337 -0.0601 -0.0316 -0.0404 12  LEU   B N   
4140 C CA  . LEU   B 12  ? 0.2301 0.1784 0.2571 -0.0526 -0.0229 -0.0378 12  LEU   B CA  
4141 C C   . LEU   B 12  ? 0.2164 0.1832 0.2682 -0.0566 -0.0302 -0.0379 12  LEU   B C   
4142 O O   . LEU   B 12  ? 0.2137 0.1848 0.2864 -0.0652 -0.0460 -0.0259 12  LEU   B O   
4143 C CB  . LEU   B 12  ? 0.2300 0.1625 0.2660 -0.0381 -0.0207 -0.0413 12  LEU   B CB  
4144 C CG  . LEU   B 12  ? 0.2233 0.1592 0.2657 -0.0440 -0.0147 -0.0348 12  LEU   B CG  
4145 C CD1 . LEU   B 12  ? 0.2368 0.1656 0.2587 -0.0277 -0.0133 -0.0093 12  LEU   B CD1 
4146 C CD2 . LEU   B 12  ? 0.2256 0.1654 0.2813 -0.0423 -0.0086 -0.0349 12  LEU   B CD2 
4158 N N   . THR   B 13  ? 0.2029 0.1842 0.2713 -0.0548 -0.0323 -0.0498 13  THR   B N   
4159 C CA  . THR   B 13  ? 0.2043 0.1919 0.2508 -0.0578 -0.0451 -0.0306 13  THR   B CA  
4160 C C   . THR   B 13  ? 0.2454 0.2117 0.2748 -0.0703 -0.0692 -0.0235 13  THR   B C   
4161 O O   . THR   B 13  ? 0.2629 0.2132 0.2853 -0.0692 -0.0359 -0.0253 13  THR   B O   
4162 C CB  . THR   B 13  ? 0.1857 0.1899 0.2454 -0.0484 -0.0399 -0.0197 13  THR   B CB  
4163 O OG1 . THR   B 13  ? 0.1802 0.1826 0.2543 -0.0399 -0.0319 -0.0218 13  THR   B OG1 
4164 C CG2 . THR   B 13  ? 0.1887 0.1968 0.2512 -0.0419 -0.0288 -0.0100 13  THR   B CG2 
4172 N N   A ASP   B 14  ? 0.2552 0.2234 0.2927 -0.0752 -0.0928 -0.0139 14  ASP   B N   
4173 N N   B ASP   B 14  ? 0.2606 0.2282 0.2872 -0.0746 -0.1001 -0.0094 14  ASP   B N   
4174 C CA  A ASP   B 14  ? 0.2665 0.2349 0.3166 -0.0752 -0.0971 0.0021  14  ASP   B CA  
4175 C CA  B ASP   B 14  ? 0.2766 0.2442 0.3113 -0.0709 -0.1029 0.0140  14  ASP   B CA  
4176 C C   A ASP   B 14  ? 0.2568 0.2190 0.2785 -0.0717 -0.0905 0.0074  14  ASP   B C   
4177 C C   B ASP   B 14  ? 0.2643 0.2264 0.2795 -0.0702 -0.0889 0.0145  14  ASP   B C   
4178 O O   A ASP   B 14  ? 0.2723 0.2264 0.2730 -0.0731 -0.0963 0.0102  14  ASP   B O   
4179 O O   B ASP   B 14  ? 0.2840 0.2380 0.2830 -0.0718 -0.0869 0.0170  14  ASP   B O   
4180 C CB  A ASP   B 14  ? 0.2853 0.2635 0.3854 -0.0769 -0.1036 0.0033  14  ASP   B CB  
4181 C CB  B ASP   B 14  ? 0.3022 0.2813 0.3838 -0.0646 -0.1107 0.0210  14  ASP   B CB  
4182 C CG  A ASP   B 14  ? 0.3057 0.2875 0.4461 -0.0749 -0.1013 -0.0039 14  ASP   B CG  
4183 C CG  B ASP   B 14  ? 0.3312 0.3159 0.4507 -0.0540 -0.1048 0.0157  14  ASP   B CG  
4184 O OD1 A ASP   B 14  ? 0.3192 0.2971 0.4603 -0.0757 -0.1024 -0.0114 14  ASP   B OD1 
4185 O OD1 B ASP   B 14  ? 0.3422 0.3285 0.4663 -0.0499 -0.1001 0.0112  14  ASP   B OD1 
4186 O OD2 A ASP   B 14  ? 0.3068 0.2954 0.4711 -0.0756 -0.0976 -0.0008 14  ASP   B OD2 
4187 O OD2 B ASP   B 14  ? 0.3399 0.3278 0.4805 -0.0534 -0.0999 0.0175  14  ASP   B OD2 
4196 N N   . ASN   B 15  ? 0.2286 0.1965 0.2520 -0.0612 -0.0814 0.0111  15  ASN   B N   
4197 C CA  . ASN   B 15  ? 0.1867 0.1666 0.2303 -0.0388 -0.0553 0.0009  15  ASN   B CA  
4198 C C   . ASN   B 15  ? 0.1636 0.1547 0.2122 -0.0232 -0.0385 -0.0042 15  ASN   B C   
4199 O O   . ASN   B 15  ? 0.1625 0.1495 0.2250 -0.0233 -0.0416 -0.0177 15  ASN   B O   
4200 C CB  . ASN   B 15  ? 0.1817 0.1632 0.2449 -0.0245 -0.0518 -0.0014 15  ASN   B CB  
4201 C CG  . ASN   B 15  ? 0.1683 0.1602 0.2418 -0.0248 -0.0299 0.0062  15  ASN   B CG  
4202 O OD1 . ASN   B 15  ? 0.1722 0.1889 0.2855 -0.0406 -0.0349 0.0122  15  ASN   B OD1 
4203 N ND2 . ASN   B 15  ? 0.1699 0.1419 0.2231 -0.0214 -0.0039 -0.0023 15  ASN   B ND2 
4211 N N   . VAL   B 16  ? 0.1657 0.1476 0.2091 -0.0286 -0.0484 -0.0020 16  VAL   B N   
4212 C CA  . VAL   B 16  ? 0.1646 0.1551 0.1973 -0.0278 -0.0299 -0.0216 16  VAL   B CA  
4213 C C   . VAL   B 16  ? 0.1639 0.1668 0.1922 -0.0352 -0.0288 -0.0213 16  VAL   B C   
4214 O O   . VAL   B 16  ? 0.1687 0.1811 0.2106 -0.0357 -0.0260 -0.0274 16  VAL   B O   
4215 C CB  . VAL   B 16  ? 0.1716 0.1527 0.2100 -0.0189 -0.0162 -0.0224 16  VAL   B CB  
4216 C CG1 . VAL   B 16  ? 0.1744 0.1449 0.2043 -0.0071 -0.0133 -0.0158 16  VAL   B CG1 
4217 C CG2 . VAL   B 16  ? 0.1725 0.1632 0.2298 -0.0079 -0.0180 -0.0220 16  VAL   B CG2 
4227 N N   . TYR   B 17  ? 0.1688 0.1720 0.1914 -0.0324 -0.0279 -0.0261 17  TYR   B N   
4228 C CA  . TYR   B 17  ? 0.1772 0.1821 0.1928 -0.0390 -0.0280 -0.0052 17  TYR   B CA  
4229 C C   . TYR   B 17  ? 0.1672 0.1559 0.1890 -0.0424 -0.0180 -0.0083 17  TYR   B C   
4230 O O   . TYR   B 17  ? 0.1729 0.1616 0.1892 -0.0311 -0.0295 -0.0300 17  TYR   B O   
4231 C CB  . TYR   B 17  ? 0.2084 0.2219 0.2111 -0.0272 -0.0294 0.0265  17  TYR   B CB  
4232 C CG  . TYR   B 17  ? 0.2390 0.2751 0.2506 -0.0188 -0.0394 0.0325  17  TYR   B CG  
4233 C CD1 . TYR   B 17  ? 0.2548 0.2933 0.2724 -0.0143 -0.0503 0.0426  17  TYR   B CD1 
4234 C CD2 . TYR   B 17  ? 0.2607 0.3032 0.2783 -0.0144 -0.0493 0.0291  17  TYR   B CD2 
4235 C CE1 . TYR   B 17  ? 0.2742 0.3171 0.2823 -0.0064 -0.0632 0.0347  17  TYR   B CE1 
4236 C CE2 . TYR   B 17  ? 0.2782 0.3229 0.2944 -0.0052 -0.0699 0.0328  17  TYR   B CE2 
4237 C CZ  . TYR   B 17  ? 0.2873 0.3345 0.2997 0.0006  -0.0769 0.0385  17  TYR   B CZ  
4238 O OH  . TYR   B 17  ? 0.3060 0.3518 0.3204 0.0078  -0.0818 0.0440  17  TYR   B OH  
4248 N N   . ILE   B 18  ? 0.1789 0.1540 0.1887 -0.0319 -0.0116 -0.0197 18  ILE   B N   
4249 C CA  . ILE   B 18  ? 0.1815 0.1470 0.1838 -0.0324 -0.0075 -0.0238 18  ILE   B CA  
4250 C C   . ILE   B 18  ? 0.1932 0.1567 0.1777 -0.0446 -0.0043 -0.0368 18  ILE   B C   
4251 O O   . ILE   B 18  ? 0.2169 0.1770 0.1856 -0.0449 0.0001  -0.0414 18  ILE   B O   
4252 C CB  . ILE   B 18  ? 0.1929 0.1498 0.1907 -0.0414 -0.0113 -0.0188 18  ILE   B CB  
4253 C CG1 . ILE   B 18  ? 0.1973 0.1547 0.2035 -0.0437 -0.0081 -0.0041 18  ILE   B CG1 
4254 C CG2 . ILE   B 18  ? 0.1933 0.1554 0.1955 -0.0454 -0.0115 -0.0136 18  ILE   B CG2 
4255 C CD1 . ILE   B 18  ? 0.2056 0.1842 0.2289 -0.0343 -0.0307 0.0177  18  ILE   B CD1 
4267 N N   . LYS   B 19  ? 0.1914 0.1545 0.1943 -0.0242 0.0269  -0.0399 19  LYS   B N   
4268 C CA  . LYS   B 19  ? 0.2008 0.1610 0.2255 -0.0296 0.0246  -0.0474 19  LYS   B CA  
4269 C C   . LYS   B 19  ? 0.1822 0.1569 0.2399 -0.0236 0.0324  -0.0535 19  LYS   B C   
4270 O O   . LYS   B 19  ? 0.1772 0.1613 0.2124 -0.0155 0.0239  -0.0433 19  LYS   B O   
4271 C CB  . LYS   B 19  ? 0.2228 0.1828 0.2402 -0.0387 0.0410  -0.0319 19  LYS   B CB  
4272 C CG  . LYS   B 19  ? 0.2502 0.2068 0.2624 -0.0479 0.0474  -0.0364 19  LYS   B CG  
4273 C CD  . LYS   B 19  ? 0.2788 0.2385 0.2644 -0.0548 0.0573  -0.0392 19  LYS   B CD  
4274 C CE  . LYS   B 19  ? 0.3048 0.2657 0.2918 -0.0570 0.0612  -0.0390 19  LYS   B CE  
4275 N NZ  . LYS   B 19  ? 0.3182 0.2821 0.2994 -0.0645 0.0682  -0.0326 19  LYS   B NZ  
4289 N N   . ASN   B 20  ? 0.1819 0.1687 0.2711 -0.0214 0.0404  -0.0642 20  ASN   B N   
4290 C CA  . ASN   B 20  ? 0.1876 0.1841 0.2939 -0.0167 0.0384  -0.0835 20  ASN   B CA  
4291 C C   . ASN   B 20  ? 0.1855 0.2014 0.2971 -0.0232 0.0515  -0.0891 20  ASN   B C   
4292 O O   . ASN   B 20  ? 0.2017 0.2357 0.3149 -0.0361 0.0625  -0.0904 20  ASN   B O   
4293 C CB  . ASN   B 20  ? 0.2161 0.1917 0.3197 0.0086  0.0290  -0.0827 20  ASN   B CB  
4294 C CG  . ASN   B 20  ? 0.2436 0.1980 0.3452 0.0374  0.0333  -0.0935 20  ASN   B CG  
4295 O OD1 . ASN   B 20  ? 0.2791 0.2274 0.3713 0.0502  0.0304  -0.1020 20  ASN   B OD1 
4296 N ND2 . ASN   B 20  ? 0.2296 0.1955 0.3410 0.0382  0.0208  -0.0842 20  ASN   B ND2 
4303 N N   . ALA   B 21  ? 0.1848 0.1850 0.2846 -0.0297 0.0554  -0.0675 21  ALA   B N   
4304 C CA  . ALA   B 21  ? 0.1999 0.1911 0.2898 -0.0370 0.0420  -0.0552 21  ALA   B CA  
4305 C C   . ALA   B 21  ? 0.2002 0.1655 0.2678 -0.0227 0.0382  -0.0392 21  ALA   B C   
4306 O O   . ALA   B 21  ? 0.2071 0.1597 0.2721 -0.0337 0.0298  -0.0259 21  ALA   B O   
4307 C CB  . ALA   B 21  ? 0.2180 0.2190 0.2963 -0.0480 0.0450  -0.0419 21  ALA   B CB  
4313 N N   . ASP   B 22  ? 0.1910 0.1608 0.2619 -0.0204 0.0296  -0.0348 22  ASP   B N   
4314 C CA  . ASP   B 22  ? 0.1883 0.1548 0.2490 -0.0114 0.0201  -0.0271 22  ASP   B CA  
4315 C C   . ASP   B 22  ? 0.1801 0.1468 0.2021 -0.0118 0.0182  -0.0161 22  ASP   B C   
4316 O O   . ASP   B 22  ? 0.1810 0.1544 0.2110 -0.0142 0.0125  -0.0082 22  ASP   B O   
4317 C CB  . ASP   B 22  ? 0.1954 0.1651 0.2930 -0.0106 0.0212  -0.0064 22  ASP   B CB  
4318 C CG  . ASP   B 22  ? 0.1933 0.1852 0.3369 -0.0027 0.0072  -0.0000 22  ASP   B CG  
4319 O OD1 . ASP   B 22  ? 0.2024 0.1763 0.3384 -0.0026 -0.0134 -0.0058 22  ASP   B OD1 
4320 O OD2 . ASP   B 22  ? 0.2048 0.2129 0.3918 0.0122  -0.0081 -0.0140 22  ASP   B OD2 
4325 N N   . ILE   B 23  ? 0.1790 0.1404 0.1793 -0.0085 0.0043  0.0138  23  ILE   B N   
4326 C CA  . ILE   B 23  ? 0.1686 0.1380 0.1640 -0.0116 -0.0008 0.0004  23  ILE   B CA  
4327 C C   . ILE   B 23  ? 0.1616 0.1406 0.1644 -0.0062 -0.0118 0.0010  23  ILE   B C   
4328 O O   . ILE   B 23  ? 0.1561 0.1431 0.1620 -0.0089 -0.0051 0.0027  23  ILE   B O   
4329 C CB  . ILE   B 23  ? 0.1672 0.1488 0.1810 -0.0171 0.0019  0.0080  23  ILE   B CB  
4330 C CG1 . ILE   B 23  ? 0.1749 0.1593 0.1874 -0.0127 0.0083  0.0241  23  ILE   B CG1 
4331 C CG2 . ILE   B 23  ? 0.1714 0.1724 0.1848 -0.0181 0.0097  0.0118  23  ILE   B CG2 
4332 C CD1 . ILE   B 23  ? 0.1757 0.1751 0.1977 -0.0005 0.0070  0.0206  23  ILE   B CD1 
4344 N N   . VAL   B 24  ? 0.1679 0.1410 0.1694 -0.0085 -0.0097 0.0013  24  VAL   B N   
4345 C CA  . VAL   B 24  ? 0.1628 0.1471 0.1885 -0.0099 -0.0195 -0.0030 24  VAL   B CA  
4346 C C   . VAL   B 24  ? 0.1613 0.1551 0.1846 -0.0139 -0.0152 -0.0000 24  VAL   B C   
4347 O O   . VAL   B 24  ? 0.1573 0.1607 0.2031 -0.0185 -0.0095 0.0066  24  VAL   B O   
4348 C CB  . VAL   B 24  ? 0.1709 0.1638 0.1975 -0.0008 -0.0213 0.0029  24  VAL   B CB  
4349 C CG1 . VAL   B 24  ? 0.1776 0.1751 0.2414 -0.0063 -0.0323 0.0107  24  VAL   B CG1 
4350 C CG2 . VAL   B 24  ? 0.1791 0.1935 0.2137 0.0031  -0.0284 -0.0093 24  VAL   B CG2 
4360 N N   . GLU   B 25  ? 0.1834 0.1663 0.1921 -0.0132 0.0036  0.0002  25  GLU   B N   
4361 C CA  . GLU   B 25  ? 0.1927 0.1888 0.2169 -0.0017 0.0110  -0.0133 25  GLU   B CA  
4362 C C   . GLU   B 25  ? 0.1823 0.1808 0.1818 -0.0142 0.0158  -0.0068 25  GLU   B C   
4363 O O   . GLU   B 25  ? 0.1862 0.1998 0.2023 -0.0121 0.0164  0.0067  25  GLU   B O   
4364 C CB  . GLU   B 25  ? 0.2397 0.2371 0.2789 0.0275  0.0186  -0.0193 25  GLU   B CB  
4365 C CG  . GLU   B 25  ? 0.2778 0.2996 0.3869 0.0401  0.0214  -0.0219 25  GLU   B CG  
4366 C CD  . GLU   B 25  ? 0.3157 0.3656 0.4855 0.0389  0.0118  -0.0228 25  GLU   B CD  
4367 O OE1 . GLU   B 25  ? 0.3435 0.3881 0.5105 0.0430  0.0137  -0.0199 25  GLU   B OE1 
4368 O OE2 . GLU   B 25  ? 0.3403 0.3851 0.5132 0.0382  -0.0011 -0.0279 25  GLU   B OE2 
4375 N N   A GLU   B 26  ? 0.1829 0.1729 0.1627 -0.0279 0.0071  -0.0062 26  GLU   B N   
4376 N N   B GLU   B 26  ? 0.1812 0.1785 0.1744 -0.0296 0.0120  0.0023  26  GLU   B N   
4377 C CA  A GLU   B 26  ? 0.1827 0.1776 0.1583 -0.0342 -0.0034 -0.0062 26  GLU   B CA  
4378 C CA  B GLU   B 26  ? 0.1783 0.1934 0.1868 -0.0342 0.0041  0.0078  26  GLU   B CA  
4379 C C   A GLU   B 26  ? 0.1658 0.1809 0.1527 -0.0282 0.0001  0.0101  26  GLU   B C   
4380 C C   B GLU   B 26  ? 0.1607 0.1906 0.1617 -0.0263 0.0060  0.0197  26  GLU   B C   
4381 O O   A GLU   B 26  ? 0.1790 0.1981 0.1607 -0.0269 -0.0046 0.0129  26  GLU   B O   
4382 O O   B GLU   B 26  ? 0.1793 0.2128 0.1677 -0.0227 0.0020  0.0231  26  GLU   B O   
4383 C CB  A GLU   B 26  ? 0.2070 0.1826 0.1616 -0.0363 -0.0029 0.0037  26  GLU   B CB  
4384 C CB  B GLU   B 26  ? 0.2035 0.2137 0.2265 -0.0343 0.0116  0.0296  26  GLU   B CB  
4385 C CG  A GLU   B 26  ? 0.2345 0.1875 0.1834 -0.0366 -0.0028 -0.0040 26  GLU   B CG  
4386 C CG  B GLU   B 26  ? 0.2305 0.2373 0.2839 -0.0296 0.0218  0.0276  26  GLU   B CG  
4387 C CD  A GLU   B 26  ? 0.2501 0.1873 0.1818 -0.0408 -0.0010 -0.0165 26  GLU   B CD  
4388 C CD  B GLU   B 26  ? 0.2376 0.2477 0.3049 -0.0336 0.0388  0.0218  26  GLU   B CD  
4389 O OE1 A GLU   B 26  ? 0.2556 0.1773 0.1686 -0.0303 0.0130  -0.0265 26  GLU   B OE1 
4390 O OE1 B GLU   B 26  ? 0.2337 0.2459 0.3451 -0.0391 0.0861  0.0122  26  GLU   B OE1 
4391 O OE2 A GLU   B 26  ? 0.2583 0.2002 0.1963 -0.0482 0.0054  0.0048  26  GLU   B OE2 
4392 O OE2 B GLU   B 26  ? 0.2370 0.2542 0.2971 -0.0317 0.0287  0.0159  26  GLU   B OE2 
4405 N N   . ALA   B 27  ? 0.1551 0.1713 0.1578 -0.0246 0.0056  0.0195  27  ALA   B N   
4406 C CA  . ALA   B 27  ? 0.1549 0.1644 0.1831 -0.0180 0.0037  0.0307  27  ALA   B CA  
4407 C C   . ALA   B 27  ? 0.1628 0.1738 0.2061 -0.0157 0.0058  0.0334  27  ALA   B C   
4408 O O   . ALA   B 27  ? 0.1709 0.1811 0.2191 -0.0070 0.0072  0.0443  27  ALA   B O   
4409 C CB  . ALA   B 27  ? 0.1730 0.1488 0.1882 -0.0205 -0.0011 0.0282  27  ALA   B CB  
4416 N N   . LYS   B 28  ? 0.1544 0.1885 0.2369 -0.0236 0.0160  0.0514  28  LYS   B N   
4417 C CA  . LYS   B 28  ? 0.1689 0.2277 0.2659 -0.0105 0.0462  0.0784  28  LYS   B CA  
4418 C C   . LYS   B 28  ? 0.1853 0.2520 0.2533 -0.0081 0.0600  0.0679  28  LYS   B C   
4419 O O   . LYS   B 28  ? 0.2130 0.2621 0.2734 -0.0104 0.0567  0.0681  28  LYS   B O   
4420 C CB  . LYS   B 28  ? 0.1927 0.2638 0.3302 -0.0004 0.0786  0.0986  28  LYS   B CB  
4421 C CG  . LYS   B 28  ? 0.2273 0.3118 0.3726 0.0069  0.0812  0.1088  28  LYS   B CG  
4422 C CD  . LYS   B 28  ? 0.2838 0.3722 0.4254 0.0133  0.0951  0.1138  28  LYS   B CD  
4423 C CE  . LYS   B 28  ? 0.3354 0.4233 0.4747 0.0188  0.0995  0.1201  28  LYS   B CE  
4424 N NZ  . LYS   B 28  ? 0.3672 0.4443 0.4923 0.0228  0.0974  0.1249  28  LYS   B NZ  
4438 N N   . LYS   B 29  ? 0.1980 0.2781 0.2532 0.0104  0.0598  0.0639  29  LYS   B N   
4439 C CA  . LYS   B 29  ? 0.2509 0.3190 0.2723 0.0102  0.0624  0.0640  29  LYS   B CA  
4440 C C   . LYS   B 29  ? 0.2457 0.3270 0.2290 0.0080  0.0494  0.0776  29  LYS   B C   
4441 O O   . LYS   B 29  ? 0.2591 0.3530 0.2363 0.0145  0.0528  0.0813  29  LYS   B O   
4442 C CB  . LYS   B 29  ? 0.3126 0.3575 0.3719 0.0094  0.0531  0.0496  29  LYS   B CB  
4443 C CG  . LYS   B 29  ? 0.3643 0.3903 0.4694 0.0065  0.0547  0.0431  29  LYS   B CG  
4444 C CD  . LYS   B 29  ? 0.4075 0.4095 0.5465 -0.0015 0.0619  0.0376  29  LYS   B CD  
4445 C CE  . LYS   B 29  ? 0.4410 0.4290 0.5923 -0.0076 0.0683  0.0328  29  LYS   B CE  
4446 N NZ  . LYS   B 29  ? 0.4581 0.4329 0.6274 -0.0115 0.0682  0.0296  29  LYS   B NZ  
4460 N N   . VAL   B 30  ? 0.2192 0.3038 0.2152 -0.0025 0.0325  0.0788  30  VAL   B N   
4461 C CA  . VAL   B 30  ? 0.2042 0.2905 0.2458 -0.0132 0.0020  0.0853  30  VAL   B CA  
4462 C C   . VAL   B 30  ? 0.1852 0.2873 0.2500 -0.0127 0.0115  0.1100  30  VAL   B C   
4463 O O   . VAL   B 30  ? 0.2011 0.3081 0.2552 -0.0003 0.0147  0.1246  30  VAL   B O   
4464 C CB  . VAL   B 30  ? 0.2069 0.2797 0.2940 -0.0276 -0.0235 0.0718  30  VAL   B CB  
4465 C CG1 . VAL   B 30  ? 0.2127 0.2793 0.3012 -0.0298 -0.0123 0.0645  30  VAL   B CG1 
4466 C CG2 . VAL   B 30  ? 0.2169 0.2824 0.3189 -0.0323 -0.0340 0.0572  30  VAL   B CG2 
4476 N N   . LYS   B 31  ? 0.1708 0.2492 0.2939 -0.0385 0.0031  0.1149  31  LYS   B N   
4477 C CA  . LYS   B 31  ? 0.1623 0.2444 0.3425 -0.0490 -0.0004 0.1224  31  LYS   B CA  
4478 C C   . LYS   B 31  ? 0.1556 0.2047 0.2938 -0.0422 -0.0256 0.1021  31  LYS   B C   
4479 O O   . LYS   B 31  ? 0.1643 0.2231 0.3070 -0.0291 -0.0220 0.1173  31  LYS   B O   
4480 C CB  . LYS   B 31  ? 0.1864 0.3018 0.4138 -0.0451 0.0245  0.1365  31  LYS   B CB  
4481 C CG  . LYS   B 31  ? 0.2367 0.3571 0.4648 -0.0414 0.0399  0.1417  31  LYS   B CG  
4482 C CD  . LYS   B 31  ? 0.3007 0.4206 0.5106 -0.0373 0.0440  0.1276  31  LYS   B CD  
4483 C CE  . LYS   B 31  ? 0.3447 0.4649 0.5550 -0.0359 0.0428  0.1148  31  LYS   B CE  
4484 N NZ  . LYS   B 31  ? 0.3868 0.4917 0.5662 -0.0310 0.0360  0.1091  31  LYS   B NZ  
4498 N N   . PRO   B 32  ? 0.1682 0.1615 0.2130 -0.0372 -0.0410 0.0526  32  PRO   B N   
4499 C CA  . PRO   B 32  ? 0.1777 0.1595 0.1653 -0.0367 -0.0447 0.0305  32  PRO   B CA  
4500 C C   . PRO   B 32  ? 0.1875 0.1513 0.1686 -0.0360 -0.0560 0.0306  32  PRO   B C   
4501 O O   . PRO   B 32  ? 0.2028 0.1471 0.2076 -0.0400 -0.0763 0.0291  32  PRO   B O   
4502 C CB  . PRO   B 32  ? 0.1936 0.1522 0.1770 -0.0445 -0.0355 0.0187  32  PRO   B CB  
4503 C CG  . PRO   B 32  ? 0.2118 0.1393 0.1828 -0.0326 -0.0542 0.0164  32  PRO   B CG  
4504 C CD  . PRO   B 32  ? 0.1962 0.1459 0.1994 -0.0227 -0.0630 0.0239  32  PRO   B CD  
4512 N N   . THR   B 33  ? 0.1852 0.1395 0.1672 -0.0331 -0.0491 0.0256  33  THR   B N   
4513 C CA  . THR   B 33  ? 0.1937 0.1455 0.1560 -0.0340 -0.0468 0.0325  33  THR   B CA  
4514 C C   . THR   B 33  ? 0.1967 0.1363 0.1619 -0.0350 -0.0515 0.0214  33  THR   B C   
4515 O O   . THR   B 33  ? 0.2238 0.1378 0.1687 -0.0400 -0.0603 0.0156  33  THR   B O   
4516 C CB  . THR   B 33  ? 0.2045 0.1539 0.1662 -0.0190 -0.0584 0.0279  33  THR   B CB  
4517 O OG1 . THR   B 33  ? 0.1969 0.1594 0.1711 -0.0239 -0.0531 0.0371  33  THR   B OG1 
4518 C CG2 . THR   B 33  ? 0.2224 0.1611 0.1979 -0.0095 -0.0574 0.0232  33  THR   B CG2 
4526 N N   . VAL   B 34  ? 0.1870 0.1316 0.1417 -0.0357 -0.0425 0.0212  34  VAL   B N   
4527 C CA  . VAL   B 34  ? 0.1706 0.1312 0.1326 -0.0276 -0.0355 0.0112  34  VAL   B CA  
4528 C C   . VAL   B 34  ? 0.1576 0.1233 0.1214 -0.0311 -0.0240 0.0079  34  VAL   B C   
4529 O O   . VAL   B 34  ? 0.1758 0.1296 0.1322 -0.0278 -0.0317 0.0059  34  VAL   B O   
4530 C CB  . VAL   B 34  ? 0.1759 0.1394 0.1619 -0.0128 -0.0319 0.0016  34  VAL   B CB  
4531 C CG1 . VAL   B 34  ? 0.1696 0.1535 0.1690 -0.0076 -0.0182 -0.0017 34  VAL   B CG1 
4532 C CG2 . VAL   B 34  ? 0.1832 0.1467 0.1931 -0.0145 -0.0338 0.0011  34  VAL   B CG2 
4542 N N   . VAL   B 35  ? 0.1497 0.1237 0.1175 -0.0269 -0.0169 0.0087  35  VAL   B N   
4543 C CA  . VAL   B 35  ? 0.1403 0.1245 0.1128 -0.0236 -0.0140 0.0067  35  VAL   B CA  
4544 C C   . VAL   B 35  ? 0.1336 0.1162 0.1169 -0.0181 -0.0160 0.0022  35  VAL   B C   
4545 O O   . VAL   B 35  ? 0.1363 0.1213 0.1327 -0.0217 -0.0045 0.0020  35  VAL   B O   
4546 C CB  . VAL   B 35  ? 0.1395 0.1385 0.1180 -0.0174 0.0033  0.0057  35  VAL   B CB  
4547 C CG1 . VAL   B 35  ? 0.1348 0.1559 0.1324 -0.0238 0.0067  0.0028  35  VAL   B CG1 
4548 C CG2 . VAL   B 35  ? 0.1403 0.1368 0.1406 -0.0075 -0.0050 0.0055  35  VAL   B CG2 
4558 N N   . VAL   B 36  ? 0.1349 0.1158 0.1189 -0.0202 -0.0148 0.0076  36  VAL   B N   
4559 C CA  . VAL   B 36  ? 0.1314 0.1110 0.1133 -0.0107 -0.0064 0.0021  36  VAL   B CA  
4560 C C   . VAL   B 36  ? 0.1246 0.1189 0.1067 -0.0092 -0.0043 0.0038  36  VAL   B C   
4561 O O   . VAL   B 36  ? 0.1329 0.1253 0.1323 -0.0100 0.0005  -0.0033 36  VAL   B O   
4562 C CB  . VAL   B 36  ? 0.1315 0.1233 0.1254 -0.0147 -0.0078 0.0005  36  VAL   B CB  
4563 C CG1 . VAL   B 36  ? 0.1272 0.1338 0.1302 -0.0227 -0.0013 0.0015  36  VAL   B CG1 
4564 C CG2 . VAL   B 36  ? 0.1405 0.1290 0.1331 -0.0082 -0.0095 0.0044  36  VAL   B CG2 
4574 N N   . ASN   B 37  ? 0.1268 0.1249 0.1144 -0.0002 -0.0054 0.0024  37  ASN   B N   
4575 C CA  . ASN   B 37  ? 0.1276 0.1258 0.1205 0.0024  -0.0063 0.0043  37  ASN   B CA  
4576 C C   . ASN   B 37  ? 0.1328 0.1268 0.1215 0.0024  -0.0070 -0.0032 37  ASN   B C   
4577 O O   . ASN   B 37  ? 0.1376 0.1343 0.1290 0.0027  -0.0012 0.0095  37  ASN   B O   
4578 C CB  . ASN   B 37  ? 0.1332 0.1266 0.1174 0.0005  -0.0106 0.0043  37  ASN   B CB  
4579 C CG  . ASN   B 37  ? 0.1329 0.1271 0.1271 -0.0022 -0.0085 0.0038  37  ASN   B CG  
4580 O OD1 . ASN   B 37  ? 0.1406 0.1355 0.1407 0.0076  -0.0140 0.0029  37  ASN   B OD1 
4581 N ND2 . ASN   B 37  ? 0.1374 0.1227 0.1275 0.0002  -0.0125 0.0046  37  ASN   B ND2 
4588 N N   . ALA   B 38  ? 0.1403 0.1246 0.1246 0.0114  0.0009  0.0058  38  ALA   B N   
4589 C CA  . ALA   B 38  ? 0.1512 0.1291 0.1145 0.0026  0.0049  0.0049  38  ALA   B CA  
4590 C C   . ALA   B 38  ? 0.1462 0.1275 0.1246 0.0016  0.0080  0.0145  38  ALA   B C   
4591 O O   . ALA   B 38  ? 0.1574 0.1307 0.1401 0.0100  0.0021  0.0116  38  ALA   B O   
4592 C CB  . ALA   B 38  ? 0.1687 0.1335 0.1351 -0.0064 0.0137  0.0027  38  ALA   B CB  
4598 N N   . ALA   B 39  ? 0.1444 0.1282 0.1185 0.0081  -0.0026 0.0076  39  ALA   B N   
4599 C CA  . ALA   B 39  ? 0.1489 0.1318 0.1207 0.0075  -0.0095 0.0077  39  ALA   B CA  
4600 C C   . ALA   B 39  ? 0.1544 0.1409 0.1075 0.0108  -0.0040 0.0037  39  ALA   B C   
4601 O O   . ALA   B 39  ? 0.1564 0.1438 0.1381 -0.0021 0.0012  0.0076  39  ALA   B O   
4602 C CB  . ALA   B 39  ? 0.1560 0.1367 0.1396 -0.0028 -0.0045 0.0007  39  ALA   B CB  
4608 N N   . ASN   B 40  ? 0.1573 0.1661 0.1203 -0.0014 0.0013  -0.0052 40  ASN   B N   
4609 C CA  . ASN   B 40  ? 0.1640 0.1698 0.1250 0.0035  0.0005  -0.0039 40  ASN   B CA  
4610 C C   . ASN   B 40  ? 0.1666 0.1656 0.1084 0.0065  -0.0071 0.0020  40  ASN   B C   
4611 O O   . ASN   B 40  ? 0.1651 0.1585 0.1184 0.0091  -0.0102 0.0002  40  ASN   B O   
4612 C CB  . ASN   B 40  ? 0.1758 0.1656 0.1448 0.0094  -0.0048 0.0096  40  ASN   B CB  
4613 C CG  . ASN   B 40  ? 0.1818 0.1732 0.1764 0.0043  -0.0168 0.0139  40  ASN   B CG  
4614 O OD1 . ASN   B 40  ? 0.1752 0.1738 0.2615 0.0055  -0.0313 0.0168  40  ASN   B OD1 
4615 N ND2 . ASN   B 40  ? 0.1852 0.1748 0.1683 0.0021  -0.0100 0.0154  40  ASN   B ND2 
4622 N N   . VAL   B 41  ? 0.1760 0.1737 0.1174 0.0130  0.0043  0.0002  41  VAL   B N   
4623 C CA  . VAL   B 41  ? 0.1833 0.1897 0.1182 0.0100  0.0021  -0.0091 41  VAL   B CA  
4624 C C   . VAL   B 41  ? 0.1815 0.1856 0.1201 0.0161  -0.0076 -0.0141 41  VAL   B C   
4625 O O   . VAL   B 41  ? 0.1830 0.1798 0.1306 0.0117  -0.0141 -0.0142 41  VAL   B O   
4626 C CB  . VAL   B 41  ? 0.1978 0.2013 0.1548 -0.0031 0.0201  -0.0188 41  VAL   B CB  
4627 C CG1 . VAL   B 41  ? 0.1971 0.1986 0.1810 -0.0068 0.0374  -0.0217 41  VAL   B CG1 
4628 C CG2 . VAL   B 41  ? 0.2130 0.2206 0.1484 -0.0167 0.0203  -0.0185 41  VAL   B CG2 
4638 N N   . TYR   B 42  ? 0.1862 0.1859 0.1215 0.0187  -0.0182 -0.0018 42  TYR   B N   
4639 C CA  . TYR   B 42  ? 0.1924 0.1946 0.1273 0.0152  -0.0265 -0.0151 42  TYR   B CA  
4640 C C   . TYR   B 42  ? 0.1762 0.1709 0.1303 0.0212  -0.0171 -0.0106 42  TYR   B C   
4641 O O   . TYR   B 42  ? 0.1764 0.1783 0.1700 0.0129  -0.0290 -0.0170 42  TYR   B O   
4642 C CB  . TYR   B 42  ? 0.2209 0.2273 0.1446 0.0079  -0.0319 -0.0015 42  TYR   B CB  
4643 C CG  . TYR   B 42  ? 0.2205 0.2442 0.1404 -0.0038 -0.0298 0.0127  42  TYR   B CG  
4644 C CD1 . TYR   B 42  ? 0.2226 0.2450 0.1128 -0.0087 -0.0142 0.0079  42  TYR   B CD1 
4645 C CD2 . TYR   B 42  ? 0.2376 0.2594 0.1903 -0.0057 -0.0087 0.0228  42  TYR   B CD2 
4646 C CE1 . TYR   B 42  ? 0.2398 0.2635 0.1205 0.0009  -0.0071 0.0158  42  TYR   B CE1 
4647 C CE2 . TYR   B 42  ? 0.2425 0.2714 0.1869 -0.0051 0.0171  0.0409  42  TYR   B CE2 
4648 C CZ  . TYR   B 42  ? 0.2577 0.2890 0.1641 0.0102  0.0197  0.0291  42  TYR   B CZ  
4649 O OH  . TYR   B 42  ? 0.2928 0.3162 0.2162 0.0286  0.0284  0.0393  42  TYR   B OH  
4659 N N   . LEU   B 43  ? 0.1652 0.1560 0.1262 0.0082  -0.0088 -0.0124 43  LEU   B N   
4660 C CA  . LEU   B 43  ? 0.1661 0.1537 0.1175 0.0029  -0.0171 -0.0039 43  LEU   B CA  
4661 C C   . LEU   B 43  ? 0.1706 0.1568 0.1229 0.0036  -0.0194 -0.0008 43  LEU   B C   
4662 O O   . LEU   B 43  ? 0.1654 0.1635 0.1501 0.0066  -0.0232 0.0054  43  LEU   B O   
4663 C CB  . LEU   B 43  ? 0.1631 0.1488 0.1451 -0.0048 -0.0254 -0.0074 43  LEU   B CB  
4664 C CG  . LEU   B 43  ? 0.1701 0.1461 0.1474 0.0008  -0.0262 -0.0057 43  LEU   B CG  
4665 C CD1 . LEU   B 43  ? 0.1766 0.1501 0.1843 0.0049  -0.0443 -0.0106 43  LEU   B CD1 
4666 C CD2 . LEU   B 43  ? 0.1697 0.1516 0.1622 -0.0061 -0.0329 -0.0058 43  LEU   B CD2 
4678 N N   . LYS   B 44  ? 0.1670 0.1586 0.1304 0.0078  -0.0154 -0.0040 44  LYS   B N   
4679 C CA  . LYS   B 44  ? 0.1810 0.1634 0.1346 0.0093  -0.0134 0.0044  44  LYS   B CA  
4680 C C   . LYS   B 44  ? 0.1691 0.1589 0.1309 0.0115  -0.0162 0.0020  44  LYS   B C   
4681 O O   . LYS   B 44  ? 0.1852 0.1572 0.1609 0.0019  -0.0084 0.0056  44  LYS   B O   
4682 C CB  . LYS   B 44  ? 0.2094 0.1869 0.1532 0.0179  -0.0249 0.0009  44  LYS   B CB  
4683 C CG  . LYS   B 44  ? 0.2467 0.2125 0.1980 0.0173  -0.0563 0.0063  44  LYS   B CG  
4684 C CD  . LYS   B 44  ? 0.2852 0.2288 0.2476 0.0016  -0.0647 -0.0095 44  LYS   B CD  
4685 C CE  . LYS   B 44  ? 0.3187 0.2533 0.2986 -0.0078 -0.0665 0.0014  44  LYS   B CE  
4686 N NZ  . LYS   B 44  ? 0.3290 0.2636 0.3262 -0.0067 -0.0784 0.0240  44  LYS   B NZ  
4700 N N   . HIS   B 45  ? 0.1636 0.1672 0.1252 0.0057  -0.0172 0.0107  45  HIS   B N   
4701 C CA  . HIS   B 45  ? 0.1603 0.1595 0.1280 0.0109  -0.0099 -0.0038 45  HIS   B CA  
4702 C C   . HIS   B 45  ? 0.1840 0.1746 0.1705 0.0185  -0.0223 -0.0059 45  HIS   B C   
4703 O O   . HIS   B 45  ? 0.1925 0.1974 0.2222 0.0452  0.0025  -0.0031 45  HIS   B O   
4704 C CB  . HIS   B 45  ? 0.1512 0.1612 0.1429 -0.0006 -0.0078 -0.0098 45  HIS   B CB  
4705 C CG  . HIS   B 45  ? 0.1524 0.1538 0.1411 -0.0038 -0.0057 -0.0106 45  HIS   B CG  
4706 N ND1 . HIS   B 45  ? 0.1559 0.1469 0.1439 -0.0004 -0.0128 -0.0112 45  HIS   B ND1 
4707 C CD2 . HIS   B 45  ? 0.1610 0.1592 0.1549 -0.0095 -0.0139 -0.0015 45  HIS   B CD2 
4708 C CE1 . HIS   B 45  ? 0.1658 0.1418 0.1270 -0.0037 -0.0237 -0.0078 45  HIS   B CE1 
4709 N NE2 . HIS   B 45  ? 0.1698 0.1496 0.1358 -0.0016 -0.0165 -0.0065 45  HIS   B NE2 
4717 N N   A GLY   B 46  ? 0.1952 0.1725 0.2043 0.0176  -0.0324 -0.0021 46  GLY   B N   
4718 N N   B GLY   B 46  ? 0.1990 0.1717 0.2040 0.0191  -0.0354 0.0032  46  GLY   B N   
4719 C CA  A GLY   B 46  ? 0.2051 0.1847 0.2388 0.0186  -0.0394 0.0012  46  GLY   B CA  
4720 C CA  B GLY   B 46  ? 0.2114 0.1898 0.2348 0.0208  -0.0457 0.0111  46  GLY   B CA  
4721 C C   A GLY   B 46  ? 0.2041 0.1972 0.2773 0.0248  -0.0337 -0.0001 46  GLY   B C   
4722 C C   B GLY   B 46  ? 0.2097 0.2075 0.2737 0.0283  -0.0400 0.0136  46  GLY   B C   
4723 O O   A GLY   B 46  ? 0.2094 0.2052 0.3421 0.0278  -0.0182 -0.0260 46  GLY   B O   
4724 O O   B GLY   B 46  ? 0.2201 0.2303 0.3312 0.0307  -0.0266 -0.0003 46  GLY   B O   
4731 N N   . GLY   B 47  ? 0.2069 0.2054 0.2609 0.0153  -0.0254 0.0054  47  GLY   B N   
4732 C CA  . GLY   B 47  ? 0.1942 0.1811 0.2276 0.0120  -0.0177 0.0007  47  GLY   B CA  
4733 C C   . GLY   B 47  ? 0.1690 0.1571 0.1836 0.0056  0.0011  0.0095  47  GLY   B C   
4734 O O   . GLY   B 47  ? 0.1848 0.1409 0.1917 0.0057  -0.0046 0.0120  47  GLY   B O   
4739 N N   . GLY   B 48  ? 0.1497 0.1474 0.1873 0.0042  -0.0095 0.0193  48  GLY   B N   
4740 C CA  . GLY   B 48  ? 0.1469 0.1442 0.1739 -0.0036 -0.0059 0.0085  48  GLY   B CA  
4741 C C   . GLY   B 48  ? 0.1445 0.1404 0.1583 -0.0015 0.0069  0.0076  48  GLY   B C   
4742 O O   . GLY   B 48  ? 0.1481 0.1420 0.1860 0.0056  -0.0039 0.0084  48  GLY   B O   
4746 N N   . VAL   B 49  ? 0.1460 0.1453 0.1573 0.0085  0.0008  0.0119  49  VAL   B N   
4747 C CA  . VAL   B 49  ? 0.1502 0.1518 0.1454 0.0079  -0.0142 -0.0042 49  VAL   B CA  
4748 C C   . VAL   B 49  ? 0.1400 0.1457 0.1221 0.0115  -0.0082 0.0059  49  VAL   B C   
4749 O O   . VAL   B 49  ? 0.1515 0.1453 0.1433 0.0051  -0.0067 0.0050  49  VAL   B O   
4750 C CB  . VAL   B 49  ? 0.1543 0.1655 0.1810 0.0013  -0.0209 -0.0013 49  VAL   B CB  
4751 C CG1 . VAL   B 49  ? 0.1548 0.1713 0.1699 0.0104  -0.0306 -0.0021 49  VAL   B CG1 
4752 C CG2 . VAL   B 49  ? 0.1724 0.1809 0.1986 -0.0084 -0.0358 -0.0026 49  VAL   B CG2 
4762 N N   . ALA   B 50  ? 0.1387 0.1458 0.1320 0.0035  -0.0052 0.0037  50  ALA   B N   
4763 C CA  . ALA   B 50  ? 0.1407 0.1324 0.1382 0.0097  -0.0066 0.0060  50  ALA   B CA  
4764 C C   . ALA   B 50  ? 0.1483 0.1329 0.1349 0.0055  0.0012  -0.0021 50  ALA   B C   
4765 O O   . ALA   B 50  ? 0.1469 0.1386 0.1361 0.0050  -0.0053 -0.0031 50  ALA   B O   
4766 C CB  . ALA   B 50  ? 0.1459 0.1365 0.1522 -0.0015 0.0010  0.0071  50  ALA   B CB  
4772 N N   . GLY   B 51  ? 0.1455 0.1442 0.1487 0.0082  -0.0136 0.0083  51  GLY   B N   
4773 C CA  . GLY   B 51  ? 0.1426 0.1544 0.1661 0.0184  -0.0163 0.0111  51  GLY   B CA  
4774 C C   . GLY   B 51  ? 0.1430 0.1456 0.1544 0.0179  -0.0102 0.0102  51  GLY   B C   
4775 O O   . GLY   B 51  ? 0.1442 0.1585 0.1784 0.0074  -0.0132 -0.0025 51  GLY   B O   
4779 N N   . ALA   B 52  ? 0.1404 0.1421 0.1494 0.0160  -0.0027 0.0109  52  ALA   B N   
4780 C CA  . ALA   B 52  ? 0.1489 0.1483 0.1525 0.0142  0.0036  -0.0044 52  ALA   B CA  
4781 C C   . ALA   B 52  ? 0.1382 0.1471 0.1472 0.0059  -0.0006 0.0010  52  ALA   B C   
4782 O O   . ALA   B 52  ? 0.1453 0.1514 0.1731 0.0107  -0.0017 -0.0011 52  ALA   B O   
4783 C CB  . ALA   B 52  ? 0.1756 0.1571 0.1580 0.0008  0.0065  0.0003  52  ALA   B CB  
4789 N N   . LEU   B 53  ? 0.1357 0.1435 0.1457 0.0102  0.0013  0.0055  53  LEU   B N   
4790 C CA  . LEU   B 53  ? 0.1371 0.1487 0.1409 0.0085  -0.0058 0.0089  53  LEU   B CA  
4791 C C   . LEU   B 53  ? 0.1422 0.1403 0.1389 0.0098  -0.0021 0.0098  53  LEU   B C   
4792 O O   . LEU   B 53  ? 0.1488 0.1461 0.1524 0.0008  0.0025  0.0134  53  LEU   B O   
4793 C CB  . LEU   B 53  ? 0.1390 0.1543 0.1526 0.0049  -0.0045 0.0177  53  LEU   B CB  
4794 C CG  . LEU   B 53  ? 0.1349 0.1660 0.1554 0.0011  -0.0050 0.0301  53  LEU   B CG  
4795 C CD1 . LEU   B 53  ? 0.1423 0.1940 0.1860 0.0142  -0.0087 0.0068  53  LEU   B CD1 
4796 C CD2 . LEU   B 53  ? 0.1531 0.1940 0.1840 -0.0167 -0.0147 -0.0038 53  LEU   B CD2 
4808 N N   . ASN   B 54  ? 0.1421 0.1353 0.1386 0.0040  -0.0079 0.0076  54  ASN   B N   
4809 C CA  . ASN   B 54  ? 0.1461 0.1475 0.1455 0.0030  -0.0083 0.0007  54  ASN   B CA  
4810 C C   . ASN   B 54  ? 0.1399 0.1508 0.1626 0.0041  0.0022  -0.0021 54  ASN   B C   
4811 O O   . ASN   B 54  ? 0.1370 0.1530 0.1800 -0.0012 0.0052  -0.0011 54  ASN   B O   
4812 C CB  . ASN   B 54  ? 0.1480 0.1613 0.1585 0.0074  -0.0044 0.0052  54  ASN   B CB  
4813 C CG  . ASN   B 54  ? 0.1465 0.1687 0.1545 0.0044  -0.0138 0.0040  54  ASN   B CG  
4814 O OD1 . ASN   B 54  ? 0.1397 0.1611 0.1760 0.0055  -0.0143 -0.0173 54  ASN   B OD1 
4815 N ND2 . ASN   B 54  ? 0.1658 0.1943 0.1840 -0.0041 -0.0321 0.0125  54  ASN   B ND2 
4822 N N   . LYS   B 55  ? 0.1362 0.1582 0.1797 0.0115  -0.0044 0.0065  55  LYS   B N   
4823 C CA  . LYS   B 55  ? 0.1431 0.1706 0.1907 0.0196  -0.0074 -0.0021 55  LYS   B CA  
4824 C C   . LYS   B 55  ? 0.1424 0.1643 0.1888 0.0121  0.0043  -0.0043 55  LYS   B C   
4825 O O   . LYS   B 55  ? 0.1373 0.1752 0.2131 0.0106  0.0076  -0.0031 55  LYS   B O   
4826 C CB  . LYS   B 55  ? 0.1522 0.1836 0.2318 0.0308  -0.0005 0.0101  55  LYS   B CB  
4827 C CG  . LYS   B 55  ? 0.1971 0.2122 0.3245 0.0380  0.0150  0.0249  55  LYS   B CG  
4828 C CD  . LYS   B 55  ? 0.2371 0.2366 0.3951 0.0446  0.0323  0.0399  55  LYS   B CD  
4829 C CE  . LYS   B 55  ? 0.2704 0.2590 0.4670 0.0418  0.0420  0.0501  55  LYS   B CE  
4830 N NZ  . LYS   B 55  ? 0.2773 0.2752 0.5022 0.0398  0.0282  0.0599  55  LYS   B NZ  
4844 N N   . ALA   B 56  ? 0.1407 0.1630 0.1648 0.0051  0.0003  -0.0088 56  ALA   B N   
4845 C CA  . ALA   B 56  ? 0.1543 0.1818 0.1622 0.0049  0.0089  -0.0086 56  ALA   B CA  
4846 C C   . ALA   B 56  ? 0.1547 0.1800 0.1636 0.0013  0.0130  0.0024  56  ALA   B C   
4847 O O   . ALA   B 56  ? 0.1641 0.1874 0.1868 0.0032  0.0277  0.0075  56  ALA   B O   
4848 C CB  . ALA   B 56  ? 0.1654 0.2030 0.1818 -0.0106 0.0071  -0.0048 56  ALA   B CB  
4854 N N   . THR   B 57  ? 0.1507 0.1737 0.1692 -0.0015 0.0195  0.0028  57  THR   B N   
4855 C CA  . THR   B 57  ? 0.1511 0.1714 0.1723 -0.0036 0.0139  0.0032  57  THR   B CA  
4856 C C   . THR   B 57  ? 0.1526 0.1791 0.1940 0.0016  0.0228  0.0017  57  THR   B C   
4857 O O   . THR   B 57  ? 0.1561 0.1860 0.2057 -0.0163 0.0144  0.0003  57  THR   B O   
4858 C CB  . THR   B 57  ? 0.1578 0.1562 0.1536 -0.0004 0.0087  0.0065  57  THR   B CB  
4859 O OG1 . THR   B 57  ? 0.1549 0.1603 0.1766 -0.0030 0.0117  0.0033  57  THR   B OG1 
4860 C CG2 . THR   B 57  ? 0.1588 0.1636 0.1497 -0.0017 0.0064  0.0043  57  THR   B CG2 
4868 N N   . ASN   B 58  ? 0.1354 0.1997 0.2128 -0.0090 0.0091  -0.0142 58  ASN   B N   
4869 C CA  . ASN   B 58  ? 0.1624 0.2404 0.2541 -0.0287 0.0340  -0.0057 58  ASN   B CA  
4870 C C   . ASN   B 58  ? 0.1463 0.2172 0.2181 -0.0214 -0.0039 -0.0068 58  ASN   B C   
4871 O O   . ASN   B 58  ? 0.1533 0.2286 0.2238 -0.0207 0.0056  -0.0181 58  ASN   B O   
4872 C CB  . ASN   B 58  ? 0.2735 0.3314 0.3835 -0.0491 0.0676  0.0073  58  ASN   B CB  
4873 C CG  . ASN   B 58  ? 0.4093 0.4336 0.5335 -0.0560 0.0867  0.0252  58  ASN   B CG  
4874 O OD1 . ASN   B 58  ? 0.4358 0.4439 0.5864 -0.0607 0.0932  0.0290  58  ASN   B OD1 
4875 N ND2 . ASN   B 58  ? 0.5033 0.5033 0.5849 -0.0570 0.0935  0.0290  58  ASN   B ND2 
4882 N N   . ASN   B 59  ? 0.1425 0.1993 0.1994 -0.0133 -0.0059 -0.0021 59  ASN   B N   
4883 C CA  . ASN   B 59  ? 0.1471 0.2034 0.1976 -0.0042 -0.0199 0.0033  59  ASN   B CA  
4884 C C   . ASN   B 59  ? 0.1378 0.1948 0.1902 -0.0106 -0.0142 -0.0068 59  ASN   B C   
4885 O O   . ASN   B 59  ? 0.1483 0.1981 0.1871 -0.0132 -0.0176 -0.0028 59  ASN   B O   
4886 C CB  . ASN   B 59  ? 0.1576 0.2229 0.2019 -0.0010 -0.0290 0.0083  59  ASN   B CB  
4887 C CG  . ASN   B 59  ? 0.1695 0.2390 0.2193 -0.0002 -0.0457 0.0035  59  ASN   B CG  
4888 O OD1 . ASN   B 59  ? 0.1718 0.2469 0.2088 -0.0012 -0.0295 0.0191  59  ASN   B OD1 
4889 N ND2 . ASN   B 59  ? 0.1796 0.2492 0.2285 -0.0069 -0.0477 -0.0040 59  ASN   B ND2 
4896 N N   . ALA   B 60  ? 0.1402 0.1859 0.1898 -0.0135 -0.0027 -0.0025 60  ALA   B N   
4897 C CA  . ALA   B 60  ? 0.1504 0.1709 0.1897 -0.0166 -0.0067 0.0061  60  ALA   B CA  
4898 C C   . ALA   B 60  ? 0.1565 0.1567 0.1611 -0.0136 -0.0070 0.0040  60  ALA   B C   
4899 O O   . ALA   B 60  ? 0.1557 0.1581 0.1838 -0.0143 -0.0005 -0.0090 60  ALA   B O   
4900 C CB  . ALA   B 60  ? 0.1576 0.1670 0.2198 -0.0193 -0.0007 0.0127  60  ALA   B CB  
4906 N N   . MET   B 61  ? 0.1497 0.1509 0.1574 -0.0133 -0.0046 0.0002  61  MET   B N   
4907 C CA  . MET   B 61  ? 0.1429 0.1448 0.1440 -0.0076 -0.0105 0.0051  61  MET   B CA  
4908 C C   . MET   B 61  ? 0.1454 0.1440 0.1541 -0.0087 -0.0089 0.0050  61  MET   B C   
4909 O O   . MET   B 61  ? 0.1488 0.1457 0.1485 -0.0037 -0.0069 -0.0137 61  MET   B O   
4910 C CB  . MET   B 61  ? 0.1395 0.1497 0.1440 -0.0044 -0.0075 -0.0013 61  MET   B CB  
4911 C CG  . MET   B 61  ? 0.1467 0.1494 0.1351 -0.0003 -0.0092 0.0021  61  MET   B CG  
4912 S SD  . MET   B 61  ? 0.1425 0.1505 0.1655 -0.0048 -0.0075 -0.0080 61  MET   B SD  
4913 C CE  . MET   B 61  ? 0.1468 0.1735 0.1795 0.0065  -0.0063 -0.0235 61  MET   B CE  
4923 N N   . GLN   B 62  ? 0.1442 0.1501 0.1576 0.0004  -0.0196 0.0050  62  GLN   B N   
4924 C CA  . GLN   B 62  ? 0.1494 0.1508 0.1653 0.0031  -0.0207 -0.0095 62  GLN   B CA  
4925 C C   . GLN   B 62  ? 0.1496 0.1585 0.1566 -0.0029 -0.0236 -0.0055 62  GLN   B C   
4926 O O   . GLN   B 62  ? 0.1605 0.1640 0.1590 -0.0023 -0.0298 -0.0154 62  GLN   B O   
4927 C CB  . GLN   B 62  ? 0.1489 0.1599 0.1595 0.0057  -0.0170 -0.0019 62  GLN   B CB  
4928 C CG  . GLN   B 62  ? 0.1574 0.1694 0.1522 0.0032  -0.0246 -0.0121 62  GLN   B CG  
4929 C CD  . GLN   B 62  ? 0.1569 0.1627 0.1456 0.0026  -0.0290 0.0068  62  GLN   B CD  
4930 O OE1 . GLN   B 62  ? 0.1566 0.1629 0.1772 0.0005  -0.0243 -0.0087 62  GLN   B OE1 
4931 N NE2 . GLN   B 62  ? 0.1597 0.1733 0.1575 -0.0014 -0.0260 -0.0130 62  GLN   B NE2 
4940 N N   . VAL   B 63  ? 0.1464 0.1633 0.1841 -0.0077 -0.0235 -0.0147 63  VAL   B N   
4941 C CA  . VAL   B 63  ? 0.1616 0.1656 0.1949 -0.0095 -0.0276 -0.0103 63  VAL   B CA  
4942 C C   . VAL   B 63  ? 0.1620 0.1602 0.1640 -0.0176 -0.0284 -0.0149 63  VAL   B C   
4943 O O   . VAL   B 63  ? 0.1758 0.1609 0.1773 -0.0135 -0.0374 -0.0144 63  VAL   B O   
4944 C CB  . VAL   B 63  ? 0.1609 0.1899 0.2352 -0.0225 -0.0334 -0.0144 63  VAL   B CB  
4945 C CG1 . VAL   B 63  ? 0.1677 0.1884 0.2470 -0.0314 -0.0251 -0.0190 63  VAL   B CG1 
4946 C CG2 . VAL   B 63  ? 0.1562 0.2023 0.2475 -0.0156 -0.0403 -0.0130 63  VAL   B CG2 
4956 N N   . GLU   B 64  ? 0.1604 0.1501 0.1674 -0.0099 -0.0214 -0.0117 64  GLU   B N   
4957 C CA  . GLU   B 64  ? 0.1587 0.1444 0.1591 -0.0097 -0.0270 -0.0099 64  GLU   B CA  
4958 C C   . GLU   B 64  ? 0.1564 0.1453 0.1589 -0.0034 -0.0260 -0.0202 64  GLU   B C   
4959 O O   . GLU   B 64  ? 0.1680 0.1538 0.1550 -0.0068 -0.0260 -0.0204 64  GLU   B O   
4960 C CB  . GLU   B 64  ? 0.1573 0.1516 0.1653 -0.0145 -0.0191 -0.0042 64  GLU   B CB  
4961 C CG  . GLU   B 64  ? 0.1614 0.1605 0.1694 -0.0210 -0.0263 -0.0163 64  GLU   B CG  
4962 C CD  . GLU   B 64  ? 0.1718 0.1748 0.1736 -0.0291 -0.0242 -0.0114 64  GLU   B CD  
4963 O OE1 . GLU   B 64  ? 0.1720 0.1924 0.1824 -0.0303 -0.0235 -0.0267 64  GLU   B OE1 
4964 O OE2 . GLU   B 64  ? 0.1882 0.1834 0.1685 -0.0376 -0.0392 -0.0087 64  GLU   B OE2 
4971 N N   . SER   B 65  ? 0.1573 0.1452 0.1494 -0.0075 -0.0169 -0.0183 65  SER   B N   
4972 C CA  . SER   B 65  ? 0.1608 0.1436 0.1528 -0.0043 -0.0171 -0.0158 65  SER   B CA  
4973 C C   . SER   B 65  ? 0.1594 0.1468 0.1529 -0.0037 -0.0218 -0.0160 65  SER   B C   
4974 O O   . SER   B 65  ? 0.1612 0.1592 0.1501 -0.0002 -0.0215 -0.0306 65  SER   B O   
4975 C CB  . SER   B 65  ? 0.1556 0.1494 0.1523 -0.0111 -0.0186 -0.0105 65  SER   B CB  
4976 O OG  . SER   B 65  ? 0.1601 0.1471 0.1557 -0.0096 -0.0189 -0.0178 65  SER   B OG  
4982 N N   . ASP   B 66  ? 0.1655 0.1549 0.1530 -0.0033 -0.0263 -0.0213 66  ASP   B N   
4983 C CA  . ASP   B 66  ? 0.1713 0.1602 0.1496 0.0027  -0.0328 -0.0132 66  ASP   B CA  
4984 C C   . ASP   B 66  ? 0.1816 0.1629 0.1488 -0.0021 -0.0256 -0.0152 66  ASP   B C   
4985 O O   . ASP   B 66  ? 0.1867 0.1733 0.1617 0.0060  -0.0343 -0.0224 66  ASP   B O   
4986 C CB  . ASP   B 66  ? 0.1845 0.1712 0.1702 0.0143  -0.0446 -0.0261 66  ASP   B CB  
4987 C CG  . ASP   B 66  ? 0.2159 0.1962 0.1908 0.0211  -0.0555 -0.0102 66  ASP   B CG  
4988 O OD1 . ASP   B 66  ? 0.2418 0.1900 0.1954 0.0114  -0.0512 0.0011  66  ASP   B OD1 
4989 O OD2 . ASP   B 66  ? 0.2356 0.2175 0.2575 0.0406  -0.0543 -0.0098 66  ASP   B OD2 
4994 N N   . ASP   B 67  ? 0.1756 0.1555 0.1473 -0.0088 -0.0299 -0.0222 67  ASP   B N   
4995 C CA  . ASP   B 67  ? 0.1918 0.1494 0.1586 -0.0072 -0.0307 -0.0162 67  ASP   B CA  
4996 C C   . ASP   B 67  ? 0.1860 0.1548 0.1653 0.0022  -0.0237 -0.0189 67  ASP   B C   
4997 O O   . ASP   B 67  ? 0.1871 0.1663 0.1653 0.0029  -0.0138 -0.0265 67  ASP   B O   
4998 C CB  . ASP   B 67  ? 0.2138 0.1598 0.1721 -0.0175 -0.0420 -0.0053 67  ASP   B CB  
4999 C CG  . ASP   B 67  ? 0.2529 0.1681 0.1735 -0.0121 -0.0687 -0.0134 67  ASP   B CG  
5000 O OD1 . ASP   B 67  ? 0.2724 0.1743 0.1895 -0.0089 -0.0682 -0.0088 67  ASP   B OD1 
5001 O OD2 . ASP   B 67  ? 0.2688 0.1772 0.1989 0.0016  -0.0710 -0.0158 67  ASP   B OD2 
5006 N N   . TYR   B 68  ? 0.1731 0.1522 0.1579 0.0019  -0.0336 -0.0302 68  TYR   B N   
5007 C CA  . TYR   B 68  ? 0.1693 0.1713 0.1720 0.0088  -0.0329 -0.0332 68  TYR   B CA  
5008 C C   . TYR   B 68  ? 0.1640 0.1692 0.1705 0.0045  -0.0318 -0.0424 68  TYR   B C   
5009 O O   . TYR   B 68  ? 0.1695 0.1798 0.1756 0.0071  -0.0318 -0.0566 68  TYR   B O   
5010 C CB  . TYR   B 68  ? 0.1765 0.1871 0.1704 0.0112  -0.0373 -0.0438 68  TYR   B CB  
5011 C CG  . TYR   B 68  ? 0.1915 0.2052 0.1827 0.0147  -0.0330 -0.0571 68  TYR   B CG  
5012 C CD1 . TYR   B 68  ? 0.1944 0.2093 0.2168 -0.0045 -0.0332 -0.0618 68  TYR   B CD1 
5013 C CD2 . TYR   B 68  ? 0.1981 0.2226 0.2051 0.0231  -0.0483 -0.0502 68  TYR   B CD2 
5014 C CE1 . TYR   B 68  ? 0.1969 0.2241 0.2413 -0.0034 -0.0338 -0.0586 68  TYR   B CE1 
5015 C CE2 . TYR   B 68  ? 0.1992 0.2283 0.2094 0.0194  -0.0452 -0.0612 68  TYR   B CE2 
5016 C CZ  . TYR   B 68  ? 0.1927 0.2297 0.2272 0.0078  -0.0395 -0.0680 68  TYR   B CZ  
5017 O OH  . TYR   B 68  ? 0.1839 0.2549 0.2608 0.0029  -0.0378 -0.0485 68  TYR   B OH  
5027 N N   . ILE   B 69  ? 0.1732 0.1628 0.1624 0.0045  -0.0366 -0.0372 69  ILE   B N   
5028 C CA  . ILE   B 69  ? 0.1830 0.1666 0.1692 -0.0002 -0.0199 -0.0375 69  ILE   B CA  
5029 C C   . ILE   B 69  ? 0.1801 0.1675 0.1598 0.0068  -0.0346 -0.0387 69  ILE   B C   
5030 O O   . ILE   B 69  ? 0.1845 0.1765 0.1620 0.0080  -0.0175 -0.0403 69  ILE   B O   
5031 C CB  . ILE   B 69  ? 0.1895 0.1679 0.1889 0.0010  -0.0003 -0.0368 69  ILE   B CB  
5032 C CG1 . ILE   B 69  ? 0.1883 0.1697 0.2053 -0.0071 0.0077  -0.0333 69  ILE   B CG1 
5033 C CG2 . ILE   B 69  ? 0.2056 0.1784 0.2011 0.0047  -0.0022 -0.0265 69  ILE   B CG2 
5034 C CD1 . ILE   B 69  ? 0.1854 0.1786 0.2176 -0.0176 0.0142  -0.0317 69  ILE   B CD1 
5046 N N   . ALA   B 70  ? 0.1719 0.1674 0.1675 0.0114  -0.0415 -0.0340 70  ALA   B N   
5047 C CA  . ALA   B 70  ? 0.1717 0.1715 0.1612 0.0072  -0.0402 -0.0269 70  ALA   B CA  
5048 C C   . ALA   B 70  ? 0.1785 0.1682 0.1624 0.0025  -0.0417 -0.0359 70  ALA   B C   
5049 O O   . ALA   B 70  ? 0.1886 0.1705 0.1753 0.0052  -0.0368 -0.0377 70  ALA   B O   
5050 C CB  . ALA   B 70  ? 0.1766 0.1881 0.1616 -0.0004 -0.0304 -0.0368 70  ALA   B CB  
5056 N N   . THR   B 71  ? 0.1864 0.1673 0.1802 0.0097  -0.0469 -0.0329 71  THR   B N   
5057 C CA  . THR   B 71  ? 0.1967 0.1683 0.1909 0.0137  -0.0569 -0.0412 71  THR   B CA  
5058 C C   . THR   B 71  ? 0.1933 0.1786 0.2220 0.0316  -0.0552 -0.0553 71  THR   B C   
5059 O O   . THR   B 71  ? 0.1995 0.1855 0.2738 0.0354  -0.0474 -0.0718 71  THR   B O   
5060 C CB  . THR   B 71  ? 0.2287 0.1935 0.2162 0.0028  -0.0765 -0.0202 71  THR   B CB  
5061 O OG1 . THR   B 71  ? 0.2489 0.2205 0.2606 -0.0179 -0.0781 -0.0007 71  THR   B OG1 
5062 C CG2 . THR   B 71  ? 0.2458 0.1917 0.2481 -0.0003 -0.0593 -0.0090 71  THR   B CG2 
5070 N N   . ASN   B 72  ? 0.1818 0.1845 0.2095 0.0232  -0.0588 -0.0680 72  ASN   B N   
5071 C CA  . ASN   B 72  ? 0.1811 0.1967 0.2218 0.0195  -0.0480 -0.0763 72  ASN   B CA  
5072 C C   . ASN   B 72  ? 0.1880 0.2111 0.2256 0.0060  -0.0217 -0.0740 72  ASN   B C   
5073 O O   . ASN   B 72  ? 0.1879 0.2285 0.2612 0.0085  0.0009  -0.0766 72  ASN   B O   
5074 C CB  . ASN   B 72  ? 0.1848 0.2081 0.2374 0.0123  -0.0577 -0.0654 72  ASN   B CB  
5075 C CG  . ASN   B 72  ? 0.2019 0.2228 0.2379 0.0244  -0.0553 -0.0451 72  ASN   B CG  
5076 O OD1 . ASN   B 72  ? 0.2240 0.2428 0.2492 0.0139  -0.0399 -0.0457 72  ASN   B OD1 
5077 N ND2 . ASN   B 72  ? 0.2148 0.2302 0.2884 0.0388  -0.0510 -0.0097 72  ASN   B ND2 
5084 N N   . GLY   B 73  ? 0.1944 0.2069 0.1980 0.0043  -0.0291 -0.0649 73  GLY   B N   
5085 C CA  . GLY   B 73  ? 0.1868 0.2159 0.1854 0.0088  -0.0261 -0.0522 73  GLY   B CA  
5086 C C   . GLY   B 73  ? 0.1790 0.2106 0.1356 0.0097  -0.0241 -0.0537 73  GLY   B C   
5087 O O   . GLY   B 73  ? 0.1693 0.1959 0.1581 0.0091  -0.0170 -0.0395 73  GLY   B O   
5091 N N   . PRO   B 74  ? 0.1853 0.2213 0.1353 0.0047  -0.0275 -0.0422 74  PRO   B N   
5092 C CA  . PRO   B 74  ? 0.1766 0.2214 0.1206 0.0045  -0.0198 -0.0228 74  PRO   B CA  
5093 C C   . PRO   B 74  ? 0.1642 0.2034 0.1340 0.0091  -0.0141 -0.0220 74  PRO   B C   
5094 O O   . PRO   B 74  ? 0.1636 0.2030 0.1735 0.0131  -0.0046 -0.0290 74  PRO   B O   
5095 C CB  . PRO   B 74  ? 0.1920 0.2348 0.1151 0.0045  -0.0194 -0.0183 74  PRO   B CB  
5096 C CG  . PRO   B 74  ? 0.2132 0.2448 0.1476 0.0023  -0.0173 -0.0186 74  PRO   B CG  
5097 C CD  . PRO   B 74  ? 0.2088 0.2362 0.1445 0.0099  -0.0169 -0.0319 74  PRO   B CD  
5105 N N   . LEU   B 75  ? 0.1650 0.1897 0.1198 0.0118  -0.0161 -0.0211 75  LEU   B N   
5106 C CA  . LEU   B 75  ? 0.1627 0.1871 0.1202 0.0033  -0.0218 -0.0045 75  LEU   B CA  
5107 C C   . LEU   B 75  ? 0.1656 0.1936 0.1194 0.0068  -0.0038 -0.0046 75  LEU   B C   
5108 O O   . LEU   B 75  ? 0.1847 0.2057 0.1339 -0.0008 -0.0052 -0.0015 75  LEU   B O   
5109 C CB  . LEU   B 75  ? 0.1665 0.1908 0.1089 -0.0049 -0.0266 0.0143  75  LEU   B CB  
5110 C CG  . LEU   B 75  ? 0.2013 0.2075 0.1293 -0.0284 -0.0105 0.0046  75  LEU   B CG  
5111 C CD1 . LEU   B 75  ? 0.2337 0.2213 0.1334 -0.0375 0.0131  -0.0078 75  LEU   B CD1 
5112 C CD2 . LEU   B 75  ? 0.2381 0.2265 0.2042 -0.0209 0.0075  0.0139  75  LEU   B CD2 
5124 N N   . LYS   B 76  ? 0.1690 0.2162 0.1532 0.0083  0.0056  0.0030  76  LYS   B N   
5125 C CA  . LYS   B 76  ? 0.1819 0.2236 0.1873 0.0026  0.0236  0.0036  76  LYS   B CA  
5126 C C   . LYS   B 76  ? 0.1675 0.2081 0.1536 0.0157  0.0072  0.0250  76  LYS   B C   
5127 O O   . LYS   B 76  ? 0.1725 0.1862 0.1587 0.0061  0.0008  0.0227  76  LYS   B O   
5128 C CB  . LYS   B 76  ? 0.2004 0.2312 0.2492 -0.0070 0.0435  -0.0310 76  LYS   B CB  
5129 C CG  . LYS   B 76  ? 0.2100 0.2466 0.2943 0.0051  0.0304  -0.0400 76  LYS   B CG  
5130 C CD  . LYS   B 76  ? 0.2094 0.2534 0.3237 0.0096  0.0151  -0.0576 76  LYS   B CD  
5131 C CE  . LYS   B 76  ? 0.2141 0.2712 0.3835 0.0132  -0.0032 -0.0663 76  LYS   B CE  
5132 N NZ  . LYS   B 76  ? 0.2167 0.2814 0.3942 0.0116  -0.0255 -0.0794 76  LYS   B NZ  
5146 N N   . VAL   B 77  ? 0.1789 0.2225 0.1602 0.0221  0.0156  0.0236  77  VAL   B N   
5147 C CA  . VAL   B 77  ? 0.1787 0.2117 0.1587 0.0249  0.0177  0.0424  77  VAL   B CA  
5148 C C   . VAL   B 77  ? 0.1647 0.1911 0.1525 0.0219  0.0240  0.0367  77  VAL   B C   
5149 O O   . VAL   B 77  ? 0.1694 0.1894 0.1556 0.0280  0.0305  0.0298  77  VAL   B O   
5150 C CB  . VAL   B 77  ? 0.1871 0.2184 0.1913 0.0222  0.0245  0.0582  77  VAL   B CB  
5151 C CG1 . VAL   B 77  ? 0.1911 0.2108 0.2291 0.0149  0.0252  0.0690  77  VAL   B CG1 
5152 C CG2 . VAL   B 77  ? 0.1980 0.2357 0.2153 0.0156  0.0087  0.0605  77  VAL   B CG2 
5162 N N   . GLY   B 78  ? 0.1572 0.1754 0.1542 0.0175  0.0215  0.0287  78  GLY   B N   
5163 C CA  . GLY   B 78  ? 0.1556 0.1687 0.1490 0.0155  0.0303  0.0174  78  GLY   B CA  
5164 C C   . GLY   B 78  ? 0.1537 0.1599 0.1442 0.0128  0.0210  0.0125  78  GLY   B C   
5165 O O   . GLY   B 78  ? 0.1587 0.1602 0.1544 0.0196  0.0131  0.0193  78  GLY   B O   
5169 N N   . GLY   B 79  ? 0.1514 0.1637 0.1395 0.0091  0.0149  0.0107  79  GLY   B N   
5170 C CA  . GLY   B 79  ? 0.1501 0.1560 0.1432 0.0105  0.0045  0.0084  79  GLY   B CA  
5171 C C   . GLY   B 79  ? 0.1356 0.1504 0.1422 0.0152  0.0059  0.0059  79  GLY   B C   
5172 O O   . GLY   B 79  ? 0.1473 0.1504 0.1559 0.0181  0.0184  0.0180  79  GLY   B O   
5176 N N   . SER   B 80  ? 0.1405 0.1422 0.1515 0.0085  0.0119  0.0043  80  SER   B N   
5177 C CA  . SER   B 80  ? 0.1343 0.1404 0.1406 0.0029  0.0061  0.0037  80  SER   B CA  
5178 C C   . SER   B 80  ? 0.1394 0.1387 0.1404 0.0107  -0.0094 -0.0025 80  SER   B C   
5179 O O   . SER   B 80  ? 0.1543 0.1421 0.1760 0.0145  0.0013  -0.0094 80  SER   B O   
5180 C CB  . SER   B 80  ? 0.1417 0.1422 0.1514 0.0008  0.0025  0.0051  80  SER   B CB  
5181 O OG  . SER   B 80  ? 0.1481 0.1599 0.1688 -0.0018 -0.0094 0.0036  80  SER   B OG  
5187 N N   . CYS   B 81  ? 0.1393 0.1251 0.1513 0.0029  -0.0090 -0.0031 81  CYS   B N   
5188 C CA  . CYS   B 81  ? 0.1509 0.1251 0.1444 0.0053  -0.0137 -0.0032 81  CYS   B CA  
5189 C C   . CYS   B 81  ? 0.1449 0.1231 0.1274 0.0012  -0.0148 -0.0094 81  CYS   B C   
5190 O O   . CYS   B 81  ? 0.1662 0.1283 0.1424 0.0086  -0.0037 -0.0041 81  CYS   B O   
5191 C CB  . CYS   B 81  ? 0.1653 0.1391 0.1475 -0.0019 -0.0146 -0.0021 81  CYS   B CB  
5192 S SG  . CYS   B 81  ? 0.1598 0.1591 0.1503 -0.0022 -0.0294 -0.0138 81  CYS   B SG  
5198 N N   . VAL   B 82  ? 0.1439 0.1158 0.1469 0.0008  -0.0115 -0.0105 82  VAL   B N   
5199 C CA  . VAL   B 82  ? 0.1531 0.1262 0.1298 -0.0077 -0.0137 0.0007  82  VAL   B CA  
5200 C C   . VAL   B 82  ? 0.1586 0.1211 0.1536 -0.0038 -0.0077 -0.0005 82  VAL   B C   
5201 O O   . VAL   B 82  ? 0.1665 0.1209 0.1790 -0.0065 -0.0086 -0.0101 82  VAL   B O   
5202 C CB  . VAL   B 82  ? 0.1619 0.1508 0.1523 -0.0055 -0.0113 0.0035  82  VAL   B CB  
5203 C CG1 . VAL   B 82  ? 0.1810 0.1749 0.1642 0.0019  -0.0080 0.0185  82  VAL   B CG1 
5204 C CG2 . VAL   B 82  ? 0.1682 0.1672 0.1670 -0.0040 -0.0303 0.0149  82  VAL   B CG2 
5214 N N   . LEU   B 83  ? 0.1483 0.1197 0.1463 -0.0143 -0.0209 -0.0124 83  LEU   B N   
5215 C CA  . LEU   B 83  ? 0.1479 0.1279 0.1344 -0.0103 -0.0160 -0.0035 83  LEU   B CA  
5216 C C   . LEU   B 83  ? 0.1498 0.1291 0.1305 -0.0192 -0.0233 -0.0001 83  LEU   B C   
5217 O O   . LEU   B 83  ? 0.1500 0.1403 0.1287 -0.0200 -0.0231 0.0048  83  LEU   B O   
5218 C CB  . LEU   B 83  ? 0.1560 0.1411 0.1394 -0.0149 -0.0213 -0.0064 83  LEU   B CB  
5219 C CG  . LEU   B 83  ? 0.1723 0.1649 0.1405 -0.0207 -0.0070 -0.0080 83  LEU   B CG  
5220 C CD1 . LEU   B 83  ? 0.1836 0.1740 0.1538 -0.0174 -0.0224 -0.0062 83  LEU   B CD1 
5221 C CD2 . LEU   B 83  ? 0.1866 0.1711 0.1560 -0.0075 -0.0128 -0.0286 83  LEU   B CD2 
5233 N N   . SER   B 84  ? 0.1562 0.1366 0.1562 -0.0230 -0.0211 -0.0013 84  SER   B N   
5234 C CA  . SER   B 84  ? 0.1562 0.1550 0.1484 -0.0244 -0.0216 0.0121  84  SER   B CA  
5235 C C   . SER   B 84  ? 0.1454 0.1720 0.1159 -0.0216 -0.0135 0.0156  84  SER   B C   
5236 O O   . SER   B 84  ? 0.1491 0.1600 0.1194 -0.0176 -0.0103 0.0031  84  SER   B O   
5237 C CB  . SER   B 84  ? 0.1762 0.1597 0.1998 -0.0273 0.0081  0.0104  84  SER   B CB  
5238 O OG  . SER   B 84  ? 0.1753 0.1669 0.2469 -0.0318 0.0029  0.0209  84  SER   B OG  
5244 N N   . GLY   B 85  ? 0.1490 0.1909 0.1370 -0.0229 -0.0144 0.0180  85  GLY   B N   
5245 C CA  . GLY   B 85  ? 0.1489 0.2008 0.1440 -0.0344 0.0014  -0.0062 85  GLY   B CA  
5246 C C   . GLY   B 85  ? 0.1450 0.1797 0.1301 -0.0353 0.0011  0.0040  85  GLY   B C   
5247 O O   . GLY   B 85  ? 0.1534 0.1795 0.1335 -0.0496 0.0160  -0.0072 85  GLY   B O   
5251 N N   . HIS   B 86  ? 0.1501 0.1632 0.1490 -0.0267 -0.0191 0.0200  86  HIS   B N   
5252 C CA  . HIS   B 86  ? 0.1490 0.1634 0.1529 -0.0283 -0.0225 0.0193  86  HIS   B CA  
5253 C C   . HIS   B 86  ? 0.1472 0.1811 0.1449 -0.0415 -0.0145 0.0319  86  HIS   B C   
5254 O O   . HIS   B 86  ? 0.1593 0.1949 0.1548 -0.0341 0.0021  0.0317  86  HIS   B O   
5255 C CB  . HIS   B 86  ? 0.1563 0.1665 0.1599 -0.0212 -0.0232 0.0057  86  HIS   B CB  
5256 C CG  . HIS   B 86  ? 0.1613 0.1737 0.1519 -0.0099 -0.0251 0.0107  86  HIS   B CG  
5257 N ND1 . HIS   B 86  ? 0.1711 0.2002 0.1767 -0.0236 -0.0265 -0.0080 86  HIS   B ND1 
5258 C CD2 . HIS   B 86  ? 0.1632 0.1783 0.1622 -0.0045 -0.0203 0.0102  86  HIS   B CD2 
5259 C CE1 . HIS   B 86  ? 0.1766 0.1953 0.1706 -0.0172 -0.0109 -0.0244 86  HIS   B CE1 
5260 N NE2 . HIS   B 86  ? 0.1697 0.1909 0.1502 0.0022  -0.0066 0.0009  86  HIS   B NE2 
5268 N N   . ASN   B 87  ? 0.1510 0.1873 0.1458 -0.0353 -0.0059 0.0231  87  ASN   B N   
5269 C CA  . ASN   B 87  ? 0.1620 0.2043 0.1401 -0.0379 0.0128  0.0159  87  ASN   B CA  
5270 C C   . ASN   B 87  ? 0.1760 0.1892 0.1356 -0.0364 0.0290  0.0185  87  ASN   B C   
5271 O O   . ASN   B 87  ? 0.2018 0.2039 0.1652 -0.0328 0.0413  0.0076  87  ASN   B O   
5272 C CB  . ASN   B 87  ? 0.1639 0.2413 0.1776 -0.0300 0.0228  0.0181  87  ASN   B CB  
5273 C CG  . ASN   B 87  ? 0.1706 0.2614 0.1908 -0.0010 0.0205  0.0314  87  ASN   B CG  
5274 O OD1 . ASN   B 87  ? 0.1629 0.2391 0.1738 -0.0019 0.0389  0.0390  87  ASN   B OD1 
5275 N ND2 . ASN   B 87  ? 0.2055 0.2767 0.2311 0.0018  0.0242  0.0313  87  ASN   B ND2 
5282 N N   . LEU   B 88  ? 0.1641 0.1725 0.1253 -0.0361 0.0101  0.0137  88  LEU   B N   
5283 C CA  . LEU   B 88  ? 0.1725 0.1678 0.1286 -0.0359 0.0064  -0.0004 88  LEU   B CA  
5284 C C   . LEU   B 88  ? 0.1727 0.1560 0.1331 -0.0376 0.0015  0.0030  88  LEU   B C   
5285 O O   . LEU   B 88  ? 0.1986 0.1646 0.1672 -0.0233 -0.0261 -0.0067 88  LEU   B O   
5286 C CB  . LEU   B 88  ? 0.1843 0.1729 0.1409 -0.0359 -0.0063 0.0163  88  LEU   B CB  
5287 C CG  . LEU   B 88  ? 0.2235 0.2055 0.1681 -0.0280 -0.0273 0.0311  88  LEU   B CG  
5288 C CD1 . LEU   B 88  ? 0.2322 0.2343 0.1900 -0.0383 -0.0277 0.0412  88  LEU   B CD1 
5289 C CD2 . LEU   B 88  ? 0.2563 0.2280 0.2362 0.0156  -0.0544 0.0160  88  LEU   B CD2 
5301 N N   . ALA   B 89  ? 0.1619 0.1531 0.1249 -0.0370 0.0118  0.0084  89  ALA   B N   
5302 C CA  . ALA   B 89  ? 0.1570 0.1481 0.1168 -0.0369 -0.0000 0.0062  89  ALA   B CA  
5303 C C   . ALA   B 89  ? 0.1670 0.1528 0.1290 -0.0384 0.0149  0.0062  89  ALA   B C   
5304 O O   . ALA   B 89  ? 0.1555 0.1597 0.1634 -0.0420 0.0125  -0.0235 89  ALA   B O   
5305 C CB  . ALA   B 89  ? 0.1547 0.1496 0.1284 -0.0375 0.0034  0.0146  89  ALA   B CB  
5311 N N   . LYS   B 90  ? 0.2003 0.1367 0.1372 -0.0405 -0.0053 0.0128  90  LYS   B N   
5312 C CA  . LYS   B 90  ? 0.2141 0.1390 0.1302 -0.0394 -0.0117 0.0106  90  LYS   B CA  
5313 C C   . LYS   B 90  ? 0.1958 0.1325 0.1413 -0.0432 -0.0125 0.0042  90  LYS   B C   
5314 O O   . LYS   B 90  ? 0.2129 0.1520 0.1551 -0.0646 -0.0069 0.0030  90  LYS   B O   
5315 C CB  . LYS   B 90  ? 0.2302 0.1496 0.1613 -0.0346 -0.0077 0.0208  90  LYS   B CB  
5316 C CG  . LYS   B 90  ? 0.2278 0.1608 0.1603 -0.0198 0.0211  0.0160  90  LYS   B CG  
5317 C CD  . LYS   B 90  ? 0.2594 0.1832 0.2254 -0.0104 0.0432  -0.0081 90  LYS   B CD  
5318 C CE  . LYS   B 90  ? 0.2707 0.2011 0.2928 -0.0188 0.0569  -0.0117 90  LYS   B CE  
5319 N NZ  . LYS   B 90  ? 0.2885 0.1979 0.2930 -0.0289 0.0757  -0.0023 90  LYS   B NZ  
5333 N N   . HIS   B 91  ? 0.1711 0.1188 0.1308 -0.0286 -0.0156 0.0028  91  HIS   B N   
5334 C CA  . HIS   B 91  ? 0.1609 0.1257 0.1341 -0.0228 -0.0173 0.0021  91  HIS   B CA  
5335 C C   . HIS   B 91  ? 0.1516 0.1292 0.1161 -0.0295 -0.0040 -0.0028 91  HIS   B C   
5336 O O   . HIS   B 91  ? 0.1596 0.1353 0.1215 -0.0275 -0.0210 0.0054  91  HIS   B O   
5337 C CB  . HIS   B 91  ? 0.1743 0.1312 0.1708 -0.0075 -0.0141 0.0143  91  HIS   B CB  
5338 C CG  . HIS   B 91  ? 0.2091 0.1471 0.2361 -0.0014 0.0154  0.0314  91  HIS   B CG  
5339 N ND1 . HIS   B 91  ? 0.2366 0.1606 0.3034 -0.0028 0.0224  0.0163  91  HIS   B ND1 
5340 C CD2 . HIS   B 91  ? 0.2250 0.1801 0.2858 0.0152  0.0013  0.0573  91  HIS   B CD2 
5341 C CE1 . HIS   B 91  ? 0.2427 0.1764 0.3148 0.0125  0.0159  0.0230  91  HIS   B CE1 
5342 N NE2 . HIS   B 91  ? 0.2345 0.1898 0.3156 0.0260  0.0164  0.0620  91  HIS   B NE2 
5350 N N   . CYS   B 92  ? 0.1432 0.1291 0.1201 -0.0257 -0.0147 -0.0090 92  CYS   B N   
5351 C CA  . CYS   B 92  ? 0.1388 0.1219 0.1157 -0.0217 -0.0069 -0.0009 92  CYS   B CA  
5352 C C   . CYS   B 92  ? 0.1374 0.1200 0.1130 -0.0124 -0.0079 -0.0003 92  CYS   B C   
5353 O O   . CYS   B 92  ? 0.1434 0.1282 0.1343 -0.0184 -0.0038 -0.0048 92  CYS   B O   
5354 C CB  . CYS   B 92  ? 0.1370 0.1315 0.1207 -0.0181 -0.0058 0.0022  92  CYS   B CB  
5355 S SG  . CYS   B 92  ? 0.1408 0.1361 0.1257 -0.0122 -0.0123 0.0045  92  CYS   B SG  
5361 N N   . LEU   B 93  ? 0.1296 0.1233 0.1176 -0.0138 -0.0085 -0.0065 93  LEU   B N   
5362 C CA  . LEU   B 93  ? 0.1307 0.1227 0.1230 -0.0011 -0.0123 0.0041  93  LEU   B CA  
5363 C C   . LEU   B 93  ? 0.1238 0.1230 0.1151 -0.0043 -0.0083 0.0072  93  LEU   B C   
5364 O O   . LEU   B 93  ? 0.1318 0.1237 0.1320 -0.0082 -0.0095 0.0002  93  LEU   B O   
5365 C CB  . LEU   B 93  ? 0.1388 0.1242 0.1323 -0.0072 -0.0119 0.0032  93  LEU   B CB  
5366 C CG  . LEU   B 93  ? 0.1323 0.1347 0.1490 -0.0034 -0.0104 0.0107  93  LEU   B CG  
5367 C CD1 . LEU   B 93  ? 0.1392 0.1470 0.1579 0.0052  -0.0039 0.0013  93  LEU   B CD1 
5368 C CD2 . LEU   B 93  ? 0.1347 0.1389 0.1573 -0.0062 -0.0120 0.0063  93  LEU   B CD2 
5380 N N   . HIS   B 94  ? 0.1282 0.1174 0.1105 -0.0053 -0.0114 0.0044  94  HIS   B N   
5381 C CA  . HIS   B 94  ? 0.1304 0.1181 0.1174 0.0002  -0.0064 0.0016  94  HIS   B CA  
5382 C C   . HIS   B 94  ? 0.1286 0.1190 0.1304 -0.0012 -0.0068 0.0082  94  HIS   B C   
5383 O O   . HIS   B 94  ? 0.1305 0.1317 0.1719 -0.0040 0.0143  -0.0073 94  HIS   B O   
5384 C CB  . HIS   B 94  ? 0.1317 0.1265 0.1361 0.0037  -0.0104 -0.0024 94  HIS   B CB  
5385 C CG  . HIS   B 94  ? 0.1347 0.1241 0.1243 -0.0041 -0.0214 -0.0013 94  HIS   B CG  
5386 N ND1 . HIS   B 94  ? 0.1374 0.1269 0.1280 -0.0043 -0.0170 -0.0017 94  HIS   B ND1 
5387 C CD2 . HIS   B 94  ? 0.1373 0.1241 0.1289 -0.0046 -0.0189 0.0050  94  HIS   B CD2 
5388 C CE1 . HIS   B 94  ? 0.1400 0.1285 0.1357 -0.0086 -0.0188 0.0008  94  HIS   B CE1 
5389 N NE2 . HIS   B 94  ? 0.1341 0.1371 0.1412 -0.0122 -0.0186 0.0007  94  HIS   B NE2 
5397 N N   . VAL   B 95  ? 0.1262 0.1188 0.1318 -0.0015 0.0007  0.0058  95  VAL   B N   
5398 C CA  . VAL   B 95  ? 0.1307 0.1302 0.1281 0.0018  0.0015  0.0086  95  VAL   B CA  
5399 C C   . VAL   B 95  ? 0.1317 0.1274 0.1294 0.0026  0.0104  0.0031  95  VAL   B C   
5400 O O   . VAL   B 95  ? 0.1369 0.1308 0.1484 0.0050  0.0077  0.0173  95  VAL   B O   
5401 C CB  . VAL   B 95  ? 0.1366 0.1262 0.1330 -0.0012 -0.0049 -0.0014 95  VAL   B CB  
5402 C CG1 . VAL   B 95  ? 0.1388 0.1451 0.1484 -0.0084 -0.0006 0.0125  95  VAL   B CG1 
5403 C CG2 . VAL   B 95  ? 0.1450 0.1258 0.1331 0.0026  -0.0099 0.0037  95  VAL   B CG2 
5413 N N   . VAL   B 96  ? 0.1390 0.1311 0.1318 0.0108  0.0055  0.0122  96  VAL   B N   
5414 C CA  . VAL   B 96  ? 0.1487 0.1506 0.1242 0.0106  0.0025  0.0142  96  VAL   B CA  
5415 C C   . VAL   B 96  ? 0.1493 0.1489 0.1343 0.0128  0.0095  0.0113  96  VAL   B C   
5416 O O   . VAL   B 96  ? 0.1513 0.1524 0.1653 0.0011  0.0216  0.0026  96  VAL   B O   
5417 C CB  . VAL   B 96  ? 0.1551 0.1670 0.1294 0.0119  0.0051  0.0080  96  VAL   B CB  
5418 C CG1 . VAL   B 96  ? 0.1499 0.1825 0.1551 0.0150  0.0096  0.0107  96  VAL   B CG1 
5419 C CG2 . VAL   B 96  ? 0.1632 0.1697 0.1434 0.0052  0.0120  0.0036  96  VAL   B CG2 
5429 N N   . GLY   B 97  ? 0.1508 0.1497 0.1295 0.0089  0.0054  0.0197  97  GLY   B N   
5430 C CA  . GLY   B 97  ? 0.1695 0.1492 0.1409 0.0042  0.0106  0.0133  97  GLY   B CA  
5431 C C   . GLY   B 97  ? 0.1866 0.1572 0.1545 0.0131  0.0092  0.0147  97  GLY   B C   
5432 O O   . GLY   B 97  ? 0.1986 0.1663 0.1526 0.0078  0.0059  0.0139  97  GLY   B O   
5436 N N   . PRO   B 98  ? 0.1991 0.1621 0.1730 0.0118  0.0346  0.0310  98  PRO   B N   
5437 C CA  . PRO   B 98  ? 0.2117 0.1811 0.1810 0.0202  0.0448  0.0300  98  PRO   B CA  
5438 C C   . PRO   B 98  ? 0.2252 0.1826 0.1492 0.0386  0.0405  0.0477  98  PRO   B C   
5439 O O   . PRO   B 98  ? 0.2126 0.1772 0.1757 0.0320  0.0405  0.0470  98  PRO   B O   
5440 C CB  . PRO   B 98  ? 0.1988 0.1855 0.2009 0.0168  0.0510  0.0329  98  PRO   B CB  
5441 C CG  . PRO   B 98  ? 0.1913 0.1804 0.1960 0.0128  0.0465  0.0492  98  PRO   B CG  
5442 C CD  . PRO   B 98  ? 0.1791 0.1668 0.1904 0.0092  0.0431  0.0441  98  PRO   B CD  
5450 N N   . ASN   B 99  ? 0.2347 0.1994 0.1590 0.0488  0.0460  0.0284  99  ASN   B N   
5451 C CA  . ASN   B 99  ? 0.2565 0.2112 0.1643 0.0605  0.0414  0.0457  99  ASN   B CA  
5452 C C   . ASN   B 99  ? 0.2856 0.2441 0.1957 0.0641  0.0699  0.0781  99  ASN   B C   
5453 O O   . ASN   B 99  ? 0.3049 0.2571 0.2106 0.0661  0.0616  0.0795  99  ASN   B O   
5454 C CB  . ASN   B 99  ? 0.2684 0.2111 0.1708 0.0586  0.0274  0.0385  99  ASN   B CB  
5455 C CG  . ASN   B 99  ? 0.2764 0.2159 0.1903 0.0579  0.0192  0.0344  99  ASN   B CG  
5456 O OD1 . ASN   B 99  ? 0.2822 0.2205 0.2181 0.0591  0.0269  0.0494  99  ASN   B OD1 
5457 N ND2 . ASN   B 99  ? 0.2787 0.2129 0.2021 0.0570  -0.0083 0.0276  99  ASN   B ND2 
5464 N N   A VAL   B 100 ? 0.3057 0.2575 0.2447 0.0558  0.0656  0.0933  100 VAL   B N   
5465 N N   B VAL   B 100 ? 0.3014 0.2544 0.2465 0.0542  0.0702  0.0960  100 VAL   B N   
5466 C CA  A VAL   B 100 ? 0.3352 0.2747 0.2922 0.0438  0.0600  0.1059  100 VAL   B CA  
5467 C CA  B VAL   B 100 ? 0.3315 0.2714 0.2975 0.0384  0.0697  0.1125  100 VAL   B CA  
5468 C C   A VAL   B 100 ? 0.3582 0.2812 0.2951 0.0476  0.0572  0.1260  100 VAL   B C   
5469 C C   B VAL   B 100 ? 0.3566 0.2772 0.2925 0.0434  0.0660  0.1324  100 VAL   B C   
5470 O O   A VAL   B 100 ? 0.3667 0.2910 0.3039 0.0461  0.0621  0.1234  100 VAL   B O   
5471 O O   B VAL   B 100 ? 0.3675 0.2871 0.2997 0.0399  0.0751  0.1295  100 VAL   B O   
5472 C CB  A VAL   B 100 ? 0.3444 0.2870 0.3386 0.0277  0.0538  0.1003  100 VAL   B CB  
5473 C CB  B VAL   B 100 ? 0.3407 0.2859 0.3568 0.0162  0.0668  0.1137  100 VAL   B CB  
5474 C CG1 A VAL   B 100 ? 0.3491 0.2918 0.3593 0.0246  0.0523  0.0948  100 VAL   B CG1 
5475 C CG1 B VAL   B 100 ? 0.3465 0.2924 0.3830 0.0130  0.0670  0.1095  100 VAL   B CG1 
5476 C CG2 A VAL   B 100 ? 0.3455 0.2906 0.3545 0.0201  0.0530  0.1001  100 VAL   B CG2 
5477 C CG2 B VAL   B 100 ? 0.3404 0.2895 0.3760 0.0051  0.0679  0.1173  100 VAL   B CG2 
5496 N N   . ASN   B 101 ? 0.3734 0.2841 0.2984 0.0542  0.0468  0.1359  101 ASN   B N   
5497 C CA  . ASN   B 101 ? 0.4122 0.3039 0.3048 0.0615  0.0218  0.1432  101 ASN   B CA  
5498 C C   . ASN   B 101 ? 0.4601 0.3452 0.3081 0.0610  0.0060  0.1585  101 ASN   B C   
5499 O O   . ASN   B 101 ? 0.4683 0.3598 0.3396 0.0669  0.0078  0.1305  101 ASN   B O   
5500 C CB  . ASN   B 101 ? 0.4069 0.2879 0.3232 0.0556  0.0288  0.1245  101 ASN   B CB  
5501 C CG  . ASN   B 101 ? 0.4029 0.2736 0.3255 0.0514  0.0348  0.1244  101 ASN   B CG  
5502 O OD1 . ASN   B 101 ? 0.4043 0.2752 0.3468 0.0409  0.0501  0.1197  101 ASN   B OD1 
5503 N ND2 . ASN   B 101 ? 0.3986 0.2674 0.3158 0.0529  0.0305  0.1129  101 ASN   B ND2 
5511 N N   . LYS   B 102 ? 0.4958 0.3791 0.3302 0.0481  0.0053  0.1594  102 LYS   B N   
5512 C CA  . LYS   B 102 ? 0.5286 0.4213 0.3539 0.0301  0.0093  0.1367  102 LYS   B CA  
5513 C C   . LYS   B 102 ? 0.5224 0.4243 0.3291 0.0292  0.0181  0.1445  102 LYS   B C   
5514 O O   . LYS   B 102 ? 0.5338 0.4317 0.3486 0.0321  -0.0019 0.1377  102 LYS   B O   
5515 C CB  . LYS   B 102 ? 0.5635 0.4598 0.4254 0.0138  0.0175  0.0886  102 LYS   B CB  
5516 C CG  . LYS   B 102 ? 0.5928 0.4939 0.4906 0.0003  0.0271  0.0439  102 LYS   B CG  
5517 C CD  . LYS   B 102 ? 0.6172 0.5235 0.5720 -0.0084 0.0381  0.0088  102 LYS   B CD  
5518 C CE  . LYS   B 102 ? 0.6347 0.5415 0.6294 -0.0152 0.0440  -0.0175 102 LYS   B CE  
5519 N NZ  . LYS   B 102 ? 0.6436 0.5524 0.6638 -0.0176 0.0442  -0.0321 102 LYS   B NZ  
5533 N N   . GLY   B 103 ? 0.5015 0.4171 0.3256 0.0245  0.0482  0.1428  103 GLY   B N   
5534 C CA  . GLY   B 103 ? 0.4780 0.4095 0.3415 0.0235  0.0683  0.1162  103 GLY   B CA  
5535 C C   . GLY   B 103 ? 0.4510 0.3959 0.3364 0.0215  0.0867  0.0926  103 GLY   B C   
5536 O O   . GLY   B 103 ? 0.4579 0.4063 0.3542 0.0211  0.0873  0.0900  103 GLY   B O   
5540 N N   A GLU   B 104 ? 0.4346 0.3855 0.3304 0.0212  0.0851  0.0755  104 GLU   B N   
5541 N N   B GLU   B 104 ? 0.4297 0.3780 0.3122 0.0212  0.1000  0.0825  104 GLU   B N   
5542 C CA  A GLU   B 104 ? 0.4165 0.3745 0.3209 0.0234  0.0793  0.0514  104 GLU   B CA  
5543 C CA  B GLU   B 104 ? 0.4063 0.3605 0.2913 0.0260  0.1029  0.0619  104 GLU   B CA  
5544 C C   A GLU   B 104 ? 0.4137 0.3756 0.3334 0.0137  0.0979  0.0453  104 GLU   B C   
5545 C C   B GLU   B 104 ? 0.4028 0.3624 0.3039 0.0119  0.1337  0.0624  104 GLU   B C   
5546 O O   A GLU   B 104 ? 0.4170 0.3801 0.3409 0.0112  0.0950  0.0421  104 GLU   B O   
5547 O O   B GLU   B 104 ? 0.4086 0.3684 0.3246 0.0080  0.1275  0.0561  104 GLU   B O   
5548 C CB  A GLU   B 104 ? 0.4041 0.3619 0.3075 0.0352  0.0521  0.0277  104 GLU   B CB  
5549 C CB  B GLU   B 104 ? 0.3911 0.3393 0.2757 0.0450  0.0652  0.0338  104 GLU   B CB  
5550 C CG  A GLU   B 104 ? 0.3959 0.3533 0.2943 0.0470  0.0254  0.0017  104 GLU   B CG  
5551 C CG  B GLU   B 104 ? 0.3794 0.3219 0.2560 0.0657  0.0284  0.0018  104 GLU   B CG  
5552 C CD  A GLU   B 104 ? 0.3920 0.3477 0.2798 0.0575  -0.0003 -0.0137 104 GLU   B CD  
5553 C CD  B GLU   B 104 ? 0.3722 0.3065 0.2287 0.0845  -0.0065 -0.0127 104 GLU   B CD  
5554 O OE1 A GLU   B 104 ? 0.3864 0.3400 0.2561 0.0649  0.0015  -0.0179 104 GLU   B OE1 
5555 O OE1 B GLU   B 104 ? 0.3598 0.2876 0.1848 0.1057  0.0026  -0.0210 104 GLU   B OE1 
5556 O OE2 A GLU   B 104 ? 0.3945 0.3513 0.2833 0.0576  -0.0221 -0.0221 104 GLU   B OE2 
5557 O OE2 B GLU   B 104 ? 0.3769 0.3122 0.2274 0.0777  -0.0396 -0.0181 104 GLU   B OE2 
5570 N N   A ASP   B 105 ? 0.4062 0.3719 0.3286 0.0063  0.1157  0.0412  105 ASP   B N   
5571 N N   B ASP   B 105 ? 0.3912 0.3575 0.2831 0.0013  0.1629  0.0667  105 ASP   B N   
5572 C CA  A ASP   B 105 ? 0.4024 0.3695 0.3478 -0.0001 0.1271  0.0290  105 ASP   B CA  
5573 C CA  B ASP   B 105 ? 0.3852 0.3541 0.3010 -0.0073 0.1795  0.0525  105 ASP   B CA  
5574 C C   A ASP   B 105 ? 0.3920 0.3513 0.3219 -0.0054 0.1342  0.0251  105 ASP   B C   
5575 C C   B ASP   B 105 ? 0.3719 0.3281 0.2756 -0.0164 0.1794  0.0445  105 ASP   B C   
5576 O O   A ASP   B 105 ? 0.3879 0.3481 0.3075 -0.0035 0.1426  0.0285  105 ASP   B O   
5577 O O   B ASP   B 105 ? 0.3515 0.3209 0.2697 -0.0138 0.1732  0.0456  105 ASP   B O   
5578 C CB  A ASP   B 105 ? 0.4079 0.3832 0.3933 0.0006  0.1282  0.0171  105 ASP   B CB  
5579 C CB  B ASP   B 105 ? 0.3941 0.3745 0.3623 -0.0036 0.1827  0.0372  105 ASP   B CB  
5580 C CG  A ASP   B 105 ? 0.4123 0.3946 0.4401 -0.0002 0.1314  0.0080  105 ASP   B CG  
5581 C CG  B ASP   B 105 ? 0.3991 0.3900 0.4148 -0.0047 0.1925  0.0306  105 ASP   B CG  
5582 O OD1 A ASP   B 105 ? 0.4121 0.3973 0.4478 -0.0035 0.1388  0.0091  105 ASP   B OD1 
5583 O OD1 B ASP   B 105 ? 0.3963 0.3948 0.4199 -0.0132 0.2045  0.0338  105 ASP   B OD1 
5584 O OD2 A ASP   B 105 ? 0.4147 0.4002 0.4669 0.0026  0.1252  0.0004  105 ASP   B OD2 
5585 O OD2 B ASP   B 105 ? 0.4007 0.3967 0.4366 -0.0009 0.1941  0.0275  105 ASP   B OD2 
5594 N N   A ILE   B 106 ? 0.3826 0.3339 0.3219 -0.0103 0.1271  0.0219  106 ILE   B N   
5595 N N   B ILE   B 106 ? 0.3679 0.3063 0.2905 -0.0255 0.1735  0.0390  106 ILE   B N   
5596 C CA  A ILE   B 106 ? 0.3672 0.3146 0.3269 -0.0171 0.1233  0.0169  106 ILE   B CA  
5597 C CA  B ILE   B 106 ? 0.3527 0.2815 0.3047 -0.0403 0.1775  0.0313  106 ILE   B CA  
5598 C C   A ILE   B 106 ? 0.3437 0.3061 0.3270 -0.0119 0.1188  0.0074  106 ILE   B C   
5599 C C   B ILE   B 106 ? 0.3213 0.2730 0.3045 -0.0351 0.1762  0.0127  106 ILE   B C   
5600 O O   A ILE   B 106 ? 0.3372 0.2948 0.3267 -0.0123 0.1180  0.0062  106 ILE   B O   
5601 O O   B ILE   B 106 ? 0.3079 0.2501 0.3009 -0.0436 0.1719  0.0137  106 ILE   B O   
5602 C CB  A ILE   B 106 ? 0.3765 0.3067 0.3383 -0.0262 0.1204  0.0180  106 ILE   B CB  
5603 C CB  B ILE   B 106 ? 0.3746 0.2744 0.3317 -0.0505 0.1666  0.0310  106 ILE   B CB  
5604 C CG1 A ILE   B 106 ? 0.3768 0.3016 0.3386 -0.0269 0.1197  0.0146  106 ILE   B CG1 
5605 C CG1 B ILE   B 106 ? 0.3831 0.2762 0.3442 -0.0415 0.1568  0.0163  106 ILE   B CG1 
5606 C CG2 A ILE   B 106 ? 0.3822 0.3084 0.3498 -0.0311 0.1196  0.0202  106 ILE   B CG2 
5607 C CG2 B ILE   B 106 ? 0.3828 0.2751 0.3468 -0.0627 0.1670  0.0375  106 ILE   B CG2 
5608 C CD1 A ILE   B 106 ? 0.3762 0.2990 0.3332 -0.0255 0.1200  0.0146  106 ILE   B CD1 
5609 C CD1 B ILE   B 106 ? 0.3865 0.2774 0.3398 -0.0339 0.1545  0.0132  106 ILE   B CD1 
5632 N N   A GLN   B 107 ? 0.3288 0.3099 0.3382 -0.0090 0.1121  0.0058  107 GLN   B N   
5633 N N   B GLN   B 107 ? 0.3096 0.2877 0.3235 -0.0259 0.1663  0.0071  107 GLN   B N   
5634 C CA  A GLN   B 107 ? 0.3138 0.3134 0.3497 -0.0059 0.1011  0.0081  107 GLN   B CA  
5635 C CA  B GLN   B 107 ? 0.2960 0.3037 0.3417 -0.0207 0.1505  0.0108  107 GLN   B CA  
5636 C C   A GLN   B 107 ? 0.2797 0.2883 0.3159 0.0013  0.0937  0.0074  107 GLN   B C   
5637 C C   B GLN   B 107 ? 0.2681 0.2834 0.3117 -0.0112 0.1209  0.0085  107 GLN   B C   
5638 O O   A GLN   B 107 ? 0.2758 0.2867 0.3296 0.0049  0.0753  -0.0055 107 GLN   B O   
5639 O O   B GLN   B 107 ? 0.2636 0.2832 0.3363 -0.0088 0.0933  -0.0122 107 GLN   B O   
5640 C CB  A GLN   B 107 ? 0.3381 0.3422 0.4076 -0.0080 0.0849  0.0083  107 GLN   B CB  
5641 C CB  B GLN   B 107 ? 0.3269 0.3411 0.4117 -0.0187 0.1296  0.0100  107 GLN   B CB  
5642 C CG  A GLN   B 107 ? 0.3609 0.3676 0.4658 -0.0083 0.0614  0.0075  107 GLN   B CG  
5643 C CG  B GLN   B 107 ? 0.3605 0.3762 0.4850 -0.0133 0.0923  0.0063  107 GLN   B CG  
5644 C CD  A GLN   B 107 ? 0.3773 0.3877 0.5134 -0.0108 0.0448  0.0082  107 GLN   B CD  
5645 C CD  B GLN   B 107 ? 0.3850 0.4036 0.5431 -0.0126 0.0667  0.0055  107 GLN   B CD  
5646 O OE1 A GLN   B 107 ? 0.3831 0.3957 0.5280 -0.0133 0.0434  0.0054  107 GLN   B OE1 
5647 O OE1 B GLN   B 107 ? 0.3944 0.4145 0.5597 -0.0153 0.0645  0.0031  107 GLN   B OE1 
5648 N NE2 A GLN   B 107 ? 0.3827 0.3935 0.5276 -0.0087 0.0375  0.0115  107 GLN   B NE2 
5649 N NE2 B GLN   B 107 ? 0.3935 0.4121 0.5614 -0.0078 0.0559  0.0081  107 GLN   B NE2 
5666 N N   . LEU   B 108 ? 0.2502 0.2635 0.2816 0.0134  0.0980  0.0135  108 LEU   B N   
5667 C CA  . LEU   B 108 ? 0.2284 0.2338 0.2319 0.0295  0.0681  0.0317  108 LEU   B CA  
5668 C C   . LEU   B 108 ? 0.1945 0.1903 0.2235 0.0282  0.0419  0.0355  108 LEU   B C   
5669 O O   . LEU   B 108 ? 0.1930 0.1785 0.2110 0.0232  0.0325  0.0228  108 LEU   B O   
5670 C CB  . LEU   B 108 ? 0.2481 0.2575 0.2070 0.0296  0.0681  0.0382  108 LEU   B CB  
5671 C CG  . LEU   B 108 ? 0.2670 0.2933 0.2176 0.0293  0.0592  0.0060  108 LEU   B CG  
5672 C CD1 . LEU   B 108 ? 0.2722 0.3079 0.2014 0.0212  0.0646  0.0030  108 LEU   B CD1 
5673 C CD2 . LEU   B 108 ? 0.2808 0.3072 0.2317 0.0388  0.0435  -0.0169 108 LEU   B CD2 
5686 N N   . LEU   B 109 ? 0.1759 0.1725 0.2163 0.0170  0.0406  0.0268  109 LEU   B N   
5687 C CA  . LEU   B 109 ? 0.1606 0.1508 0.2280 0.0085  0.0359  0.0327  109 LEU   B CA  
5688 C C   . LEU   B 109 ? 0.1493 0.1341 0.2220 0.0058  0.0326  0.0238  109 LEU   B C   
5689 O O   . LEU   B 109 ? 0.1479 0.1291 0.2205 0.0036  0.0309  0.0300  109 LEU   B O   
5690 C CB  . LEU   B 109 ? 0.1645 0.1414 0.2269 0.0070  0.0242  0.0396  109 LEU   B CB  
5691 C CG  . LEU   B 109 ? 0.1642 0.1376 0.2265 0.0026  0.0209  0.0224  109 LEU   B CG  
5692 C CD1 . LEU   B 109 ? 0.1609 0.1473 0.2011 0.0097  0.0257  0.0236  109 LEU   B CD1 
5693 C CD2 . LEU   B 109 ? 0.1777 0.1434 0.2344 0.0097  0.0127  0.0182  109 LEU   B CD2 
5705 N N   . LYS   B 110 ? 0.1437 0.1349 0.2209 -0.0003 0.0299  0.0200  110 LYS   B N   
5706 C CA  . LYS   B 110 ? 0.1421 0.1346 0.2188 0.0047  0.0271  0.0204  110 LYS   B CA  
5707 C C   . LYS   B 110 ? 0.1363 0.1368 0.2007 0.0022  0.0271  0.0162  110 LYS   B C   
5708 O O   . LYS   B 110 ? 0.1343 0.1359 0.2021 -0.0026 0.0223  0.0074  110 LYS   B O   
5709 C CB  . LYS   B 110 ? 0.1424 0.1376 0.2421 -0.0035 0.0333  0.0110  110 LYS   B CB  
5710 C CG  . LYS   B 110 ? 0.1395 0.1385 0.2631 -0.0007 0.0178  0.0165  110 LYS   B CG  
5711 C CD  . LYS   B 110 ? 0.1455 0.1336 0.2702 -0.0044 0.0179  0.0107  110 LYS   B CD  
5712 C CE  . LYS   B 110 ? 0.1420 0.1495 0.2986 -0.0063 0.0113  0.0054  110 LYS   B CE  
5713 N NZ  . LYS   B 110 ? 0.1459 0.1579 0.2834 0.0014  0.0051  -0.0012 110 LYS   B NZ  
5727 N N   . SER   B 111 ? 0.1434 0.1373 0.2140 -0.0045 0.0299  0.0187  111 SER   B N   
5728 C CA  . SER   B 111 ? 0.1516 0.1421 0.2012 0.0037  0.0271  0.0166  111 SER   B CA  
5729 C C   . SER   B 111 ? 0.1443 0.1343 0.1797 0.0019  0.0107  0.0116  111 SER   B C   
5730 O O   . SER   B 111 ? 0.1400 0.1354 0.2036 0.0010  0.0116  0.0119  111 SER   B O   
5731 C CB  . SER   B 111 ? 0.1659 0.1639 0.2080 0.0069  0.0370  0.0238  111 SER   B CB  
5732 O OG  . SER   B 111 ? 0.1793 0.2004 0.2123 0.0100  0.0443  0.0226  111 SER   B OG  
5738 N N   . ALA   B 112 ? 0.1377 0.1371 0.1903 0.0077  0.0194  0.0167  112 ALA   B N   
5739 C CA  . ALA   B 112 ? 0.1369 0.1389 0.1784 0.0018  0.0152  0.0065  112 ALA   B CA  
5740 C C   . ALA   B 112 ? 0.1297 0.1286 0.1707 0.0044  0.0140  0.0069  112 ALA   B C   
5741 O O   . ALA   B 112 ? 0.1319 0.1314 0.1781 0.0000  0.0109  -0.0039 112 ALA   B O   
5742 C CB  . ALA   B 112 ? 0.1447 0.1457 0.1994 0.0084  0.0100  0.0186  112 ALA   B CB  
5748 N N   . TYR   B 113 ? 0.1300 0.1205 0.1883 0.0021  0.0097  0.0147  113 TYR   B N   
5749 C CA  . TYR   B 113 ? 0.1263 0.1183 0.1784 0.0007  0.0120  0.0021  113 TYR   B CA  
5750 C C   . TYR   B 113 ? 0.1226 0.1170 0.1721 -0.0083 0.0018  0.0085  113 TYR   B C   
5751 O O   . TYR   B 113 ? 0.1297 0.1215 0.1661 -0.0062 0.0050  -0.0003 113 TYR   B O   
5752 C CB  . TYR   B 113 ? 0.1321 0.1172 0.1978 -0.0040 0.0145  0.0100  113 TYR   B CB  
5753 C CG  . TYR   B 113 ? 0.1350 0.1237 0.1972 -0.0010 0.0111  0.0141  113 TYR   B CG  
5754 C CD1 . TYR   B 113 ? 0.1367 0.1235 0.2119 -0.0039 0.0142  0.0169  113 TYR   B CD1 
5755 C CD2 . TYR   B 113 ? 0.1410 0.1249 0.1965 -0.0019 0.0109  0.0136  113 TYR   B CD2 
5756 C CE1 . TYR   B 113 ? 0.1380 0.1244 0.2111 -0.0053 0.0200  0.0057  113 TYR   B CE1 
5757 C CE2 . TYR   B 113 ? 0.1415 0.1178 0.2071 0.0033  0.0093  0.0203  113 TYR   B CE2 
5758 C CZ  . TYR   B 113 ? 0.1297 0.1221 0.2184 0.0052  0.0097  0.0082  113 TYR   B CZ  
5759 O OH  . TYR   B 113 ? 0.1394 0.1236 0.2338 0.0099  0.0193  0.0060  113 TYR   B OH  
5769 N N   . GLU   B 114 ? 0.1198 0.1168 0.2036 -0.0012 0.0050  0.0074  114 GLU   B N   
5770 C CA  . GLU   B 114 ? 0.1178 0.1136 0.1911 0.0036  0.0066  0.0030  114 GLU   B CA  
5771 C C   . GLU   B 114 ? 0.1229 0.1191 0.1781 0.0041  0.0066  -0.0003 114 GLU   B C   
5772 O O   . GLU   B 114 ? 0.1251 0.1173 0.1858 -0.0014 0.0006  0.0083  114 GLU   B O   
5773 C CB  . GLU   B 114 ? 0.1226 0.1233 0.1933 -0.0035 0.0067  0.0050  114 GLU   B CB  
5774 C CG  . GLU   B 114 ? 0.1333 0.1183 0.1928 -0.0001 0.0120  0.0060  114 GLU   B CG  
5775 C CD  . GLU   B 114 ? 0.1291 0.1266 0.2057 -0.0072 0.0125  0.0056  114 GLU   B CD  
5776 O OE1 . GLU   B 114 ? 0.1286 0.1377 0.1970 -0.0101 0.0191  0.0082  114 GLU   B OE1 
5777 O OE2 . GLU   B 114 ? 0.1278 0.1466 0.2222 -0.0172 0.0137  0.0116  114 GLU   B OE2 
5784 N N   . ASN   B 115 ? 0.1257 0.1122 0.1752 -0.0002 -0.0017 0.0022  115 ASN   B N   
5785 C CA  . ASN   B 115 ? 0.1295 0.1187 0.1572 -0.0049 -0.0017 0.0031  115 ASN   B CA  
5786 C C   . ASN   B 115 ? 0.1247 0.1135 0.1622 -0.0106 -0.0046 0.0004  115 ASN   B C   
5787 O O   . ASN   B 115 ? 0.1372 0.1184 0.1723 -0.0148 -0.0019 -0.0015 115 ASN   B O   
5788 C CB  . ASN   B 115 ? 0.1363 0.1292 0.1553 -0.0052 0.0027  -0.0007 115 ASN   B CB  
5789 C CG  . ASN   B 115 ? 0.1440 0.1351 0.1628 -0.0021 -0.0022 -0.0026 115 ASN   B CG  
5790 O OD1 . ASN   B 115 ? 0.1766 0.1504 0.1879 -0.0038 0.0129  -0.0132 115 ASN   B OD1 
5791 N ND2 . ASN   B 115 ? 0.1452 0.1445 0.1703 -0.0047 0.0099  0.0005  115 ASN   B ND2 
5798 N N   . PHE   B 116 ? 0.1198 0.1210 0.1560 -0.0056 -0.0002 0.0046  116 PHE   B N   
5799 C CA  . PHE   B 116 ? 0.1257 0.1253 0.1610 -0.0104 -0.0015 0.0069  116 PHE   B CA  
5800 C C   . PHE   B 116 ? 0.1337 0.1161 0.1563 -0.0120 -0.0026 0.0052  116 PHE   B C   
5801 O O   . PHE   B 116 ? 0.1363 0.1242 0.1640 -0.0053 -0.0058 0.0023  116 PHE   B O   
5802 C CB  . PHE   B 116 ? 0.1278 0.1194 0.1646 -0.0086 -0.0117 0.0035  116 PHE   B CB  
5803 C CG  . PHE   B 116 ? 0.1234 0.1190 0.1530 -0.0064 -0.0004 0.0020  116 PHE   B CG  
5804 C CD1 . PHE   B 116 ? 0.1292 0.1246 0.1707 -0.0023 0.0014  0.0028  116 PHE   B CD1 
5805 C CD2 . PHE   B 116 ? 0.1294 0.1261 0.1534 -0.0032 0.0049  -0.0025 116 PHE   B CD2 
5806 C CE1 . PHE   B 116 ? 0.1313 0.1278 0.1627 -0.0060 -0.0044 0.0064  116 PHE   B CE1 
5807 C CE2 . PHE   B 116 ? 0.1318 0.1284 0.1566 -0.0007 0.0074  0.0039  116 PHE   B CE2 
5808 C CZ  . PHE   B 116 ? 0.1240 0.1298 0.1633 -0.0054 -0.0071 0.0046  116 PHE   B CZ  
5818 N N   . ASN   B 117 ? 0.1307 0.1196 0.1734 -0.0072 -0.0080 0.0042  117 ASN   B N   
5819 C CA  . ASN   B 117 ? 0.1334 0.1209 0.1671 -0.0023 -0.0080 0.0073  117 ASN   B CA  
5820 C C   . ASN   B 117 ? 0.1371 0.1204 0.1746 -0.0000 -0.0053 0.0034  117 ASN   B C   
5821 O O   . ASN   B 117 ? 0.1437 0.1281 0.1987 0.0004  -0.0274 0.0126  117 ASN   B O   
5822 C CB  . ASN   B 117 ? 0.1344 0.1265 0.1752 -0.0010 -0.0082 -0.0073 117 ASN   B CB  
5823 C CG  . ASN   B 117 ? 0.1328 0.1258 0.1830 0.0006  -0.0051 -0.0095 117 ASN   B CG  
5824 O OD1 . ASN   B 117 ? 0.1551 0.1262 0.1955 -0.0151 0.0047  -0.0069 117 ASN   B OD1 
5825 N ND2 . ASN   B 117 ? 0.1318 0.1292 0.1880 -0.0012 0.0020  -0.0040 117 ASN   B ND2 
5832 N N   . GLN   B 118 ? 0.1352 0.1135 0.1835 -0.0093 -0.0114 -0.0006 118 GLN   B N   
5833 C CA  . GLN   B 118 ? 0.1418 0.1190 0.1848 -0.0003 -0.0067 -0.0038 118 GLN   B CA  
5834 C C   . GLN   B 118 ? 0.1487 0.1205 0.1926 0.0016  -0.0119 0.0017  118 GLN   B C   
5835 O O   . GLN   B 118 ? 0.1685 0.1174 0.2234 -0.0087 0.0032  0.0055  118 GLN   B O   
5836 C CB  . GLN   B 118 ? 0.1509 0.1264 0.1910 -0.0030 -0.0146 -0.0098 118 GLN   B CB  
5837 C CG  . GLN   B 118 ? 0.1580 0.1251 0.1814 0.0033  -0.0083 -0.0115 118 GLN   B CG  
5838 C CD  . GLN   B 118 ? 0.1610 0.1256 0.1844 -0.0048 -0.0029 -0.0170 118 GLN   B CD  
5839 O OE1 . GLN   B 118 ? 0.1655 0.1218 0.2150 0.0046  0.0076  0.0016  118 GLN   B OE1 
5840 N NE2 . GLN   B 118 ? 0.1650 0.1214 0.1800 0.0030  -0.0098 0.0000  118 GLN   B NE2 
5849 N N   . HIS   B 119 ? 0.1441 0.1258 0.1605 -0.0024 -0.0065 0.0030  119 HIS   B N   
5850 C CA  . HIS   B 119 ? 0.1511 0.1388 0.1493 -0.0026 -0.0166 0.0065  119 HIS   B CA  
5851 C C   . HIS   B 119 ? 0.1573 0.1381 0.1544 -0.0026 -0.0291 0.0056  119 HIS   B C   
5852 O O   . HIS   B 119 ? 0.1637 0.1327 0.1716 -0.0230 -0.0202 0.0070  119 HIS   B O   
5853 C CB  . HIS   B 119 ? 0.1601 0.1492 0.1592 0.0004  -0.0125 -0.0023 119 HIS   B CB  
5854 C CG  . HIS   B 119 ? 0.1665 0.1672 0.1762 0.0127  -0.0315 -0.0171 119 HIS   B CG  
5855 N ND1 . HIS   B 119 ? 0.1758 0.1805 0.2077 0.0002  -0.0393 -0.0326 119 HIS   B ND1 
5856 C CD2 . HIS   B 119 ? 0.1795 0.1809 0.1799 0.0420  -0.0488 -0.0179 119 HIS   B CD2 
5857 C CE1 . HIS   B 119 ? 0.1947 0.2011 0.2186 0.0167  -0.0522 -0.0438 119 HIS   B CE1 
5858 N NE2 . HIS   B 119 ? 0.1948 0.2073 0.2000 0.0338  -0.0479 -0.0401 119 HIS   B NE2 
5866 N N   . GLU   B 120 ? 0.1675 0.1400 0.1581 -0.0052 -0.0296 0.0077  120 GLU   B N   
5867 C CA  . GLU   B 120 ? 0.2004 0.1525 0.1687 -0.0013 -0.0403 0.0244  120 GLU   B CA  
5868 C C   . GLU   B 120 ? 0.1826 0.1388 0.1549 -0.0089 -0.0351 0.0272  120 GLU   B C   
5869 O O   . GLU   B 120 ? 0.1785 0.1484 0.1602 -0.0138 -0.0323 0.0121  120 GLU   B O   
5870 C CB  . GLU   B 120 ? 0.2790 0.1857 0.2481 0.0189  -0.0691 0.0445  120 GLU   B CB  
5871 C CG  . GLU   B 120 ? 0.3406 0.2682 0.3524 0.0304  -0.0989 0.0740  120 GLU   B CG  
5872 C CD  . GLU   B 120 ? 0.4000 0.3571 0.4682 0.0358  -0.1103 0.0933  120 GLU   B CD  
5873 O OE1 . GLU   B 120 ? 0.4221 0.3787 0.5020 0.0303  -0.1078 0.1064  120 GLU   B OE1 
5874 O OE2 . GLU   B 120 ? 0.4278 0.3995 0.5198 0.0389  -0.1107 0.0932  120 GLU   B OE2 
5881 N N   . VAL   B 121 ? 0.1706 0.1364 0.1538 -0.0191 -0.0211 0.0137  121 VAL   B N   
5882 C CA  . VAL   B 121 ? 0.1663 0.1473 0.1437 -0.0187 -0.0225 0.0085  121 VAL   B CA  
5883 C C   . VAL   B 121 ? 0.1626 0.1406 0.1423 -0.0220 -0.0189 0.0099  121 VAL   B C   
5884 O O   . VAL   B 121 ? 0.1694 0.1341 0.1570 -0.0297 -0.0232 0.0047  121 VAL   B O   
5885 C CB  . VAL   B 121 ? 0.1870 0.1902 0.1485 -0.0075 -0.0185 0.0157  121 VAL   B CB  
5886 C CG1 . VAL   B 121 ? 0.1901 0.2056 0.1725 -0.0165 -0.0055 0.0146  121 VAL   B CG1 
5887 C CG2 . VAL   B 121 ? 0.2065 0.2216 0.1503 0.0003  -0.0106 0.0091  121 VAL   B CG2 
5897 N N   . LEU   B 122 ? 0.1512 0.1329 0.1368 -0.0192 -0.0219 0.0064  122 LEU   B N   
5898 C CA  . LEU   B 122 ? 0.1434 0.1457 0.1246 -0.0165 -0.0179 0.0066  122 LEU   B CA  
5899 C C   . LEU   B 122 ? 0.1437 0.1334 0.1280 -0.0273 -0.0206 0.0065  122 LEU   B C   
5900 O O   . LEU   B 122 ? 0.1507 0.1353 0.1624 -0.0294 -0.0232 0.0000  122 LEU   B O   
5901 C CB  . LEU   B 122 ? 0.1692 0.1531 0.1563 -0.0049 -0.0234 0.0115  122 LEU   B CB  
5902 C CG  . LEU   B 122 ? 0.1519 0.1572 0.1668 -0.0136 -0.0130 0.0145  122 LEU   B CG  
5903 C CD1 . LEU   B 122 ? 0.1532 0.1794 0.1696 -0.0190 -0.0160 0.0041  122 LEU   B CD1 
5904 C CD2 . LEU   B 122 ? 0.1501 0.1635 0.1466 -0.0057 -0.0121 0.0027  122 LEU   B CD2 
5916 N N   . LEU   B 123 ? 0.1459 0.1198 0.1279 -0.0212 -0.0132 0.0048  123 LEU   B N   
5917 C CA  . LEU   B 123 ? 0.1502 0.1238 0.1229 -0.0210 -0.0188 -0.0003 123 LEU   B CA  
5918 C C   . LEU   B 123 ? 0.1463 0.1215 0.1271 -0.0253 -0.0156 -0.0062 123 LEU   B C   
5919 O O   . LEU   B 123 ? 0.1535 0.1262 0.1355 -0.0310 -0.0178 -0.0000 123 LEU   B O   
5920 C CB  . LEU   B 123 ? 0.1529 0.1251 0.1477 -0.0238 -0.0123 -0.0121 123 LEU   B CB  
5921 C CG  . LEU   B 123 ? 0.1471 0.1360 0.1494 -0.0187 -0.0101 0.0029  123 LEU   B CG  
5922 C CD1 . LEU   B 123 ? 0.1519 0.1439 0.1567 -0.0142 0.0022  -0.0091 123 LEU   B CD1 
5923 C CD2 . LEU   B 123 ? 0.1581 0.1424 0.1637 -0.0197 -0.0048 0.0136  123 LEU   B CD2 
5935 N N   . ALA   B 124 ? 0.1407 0.1212 0.1272 -0.0239 -0.0099 -0.0031 124 ALA   B N   
5936 C CA  . ALA   B 124 ? 0.1346 0.1219 0.1442 -0.0158 -0.0096 -0.0065 124 ALA   B CA  
5937 C C   . ALA   B 124 ? 0.1279 0.1180 0.1384 -0.0148 -0.0090 -0.0006 124 ALA   B C   
5938 O O   . ALA   B 124 ? 0.1387 0.1249 0.1469 -0.0107 -0.0076 -0.0028 124 ALA   B O   
5939 C CB  . ALA   B 124 ? 0.1397 0.1212 0.1561 -0.0076 0.0024  -0.0029 124 ALA   B CB  
5945 N N   . PRO   B 125 ? 0.1369 0.1204 0.1310 -0.0205 -0.0124 0.0089  125 PRO   B N   
5946 C CA  . PRO   B 125 ? 0.1439 0.1239 0.1516 -0.0151 -0.0132 0.0209  125 PRO   B CA  
5947 C C   . PRO   B 125 ? 0.1413 0.1221 0.1587 -0.0154 -0.0110 0.0088  125 PRO   B C   
5948 O O   . PRO   B 125 ? 0.1421 0.1188 0.1819 -0.0081 -0.0017 0.0134  125 PRO   B O   
5949 C CB  . PRO   B 125 ? 0.1484 0.1531 0.1652 -0.0193 -0.0167 0.0348  125 PRO   B CB  
5950 C CG  . PRO   B 125 ? 0.1529 0.1576 0.1450 -0.0260 -0.0187 0.0157  125 PRO   B CG  
5951 C CD  . PRO   B 125 ? 0.1471 0.1358 0.1370 -0.0263 -0.0082 0.0090  125 PRO   B CD  
5959 N N   . LEU   B 126 ? 0.1410 0.1149 0.1869 -0.0142 0.0071  0.0136  126 LEU   B N   
5960 C CA  . LEU   B 126 ? 0.1506 0.1273 0.1913 -0.0139 0.0191  0.0141  126 LEU   B CA  
5961 C C   . LEU   B 126 ? 0.1493 0.1380 0.1900 -0.0021 0.0212  0.0231  126 LEU   B C   
5962 O O   . LEU   B 126 ? 0.1672 0.1646 0.2035 0.0193  -0.0023 -0.0018 126 LEU   B O   
5963 C CB  . LEU   B 126 ? 0.1719 0.1266 0.2289 -0.0113 0.0232  0.0098  126 LEU   B CB  
5964 C CG  . LEU   B 126 ? 0.1903 0.1346 0.2344 -0.0233 0.0225  -0.0109 126 LEU   B CG  
5965 C CD1 . LEU   B 126 ? 0.2094 0.1429 0.2811 -0.0265 0.0159  -0.0231 126 LEU   B CD1 
5966 C CD2 . LEU   B 126 ? 0.1893 0.1446 0.2276 -0.0275 0.0127  -0.0215 126 LEU   B CD2 
5978 N N   . LEU   B 127 ? 0.1433 0.1259 0.1976 0.0040  0.0306  0.0112  127 LEU   B N   
5979 C CA  . LEU   B 127 ? 0.1438 0.1332 0.2068 -0.0055 0.0314  0.0175  127 LEU   B CA  
5980 C C   . LEU   B 127 ? 0.1379 0.1285 0.2091 -0.0028 0.0199  0.0253  127 LEU   B C   
5981 O O   . LEU   B 127 ? 0.1412 0.1324 0.2124 -0.0137 0.0120  0.0192  127 LEU   B O   
5982 C CB  . LEU   B 127 ? 0.1593 0.1318 0.2071 -0.0029 0.0202  0.0166  127 LEU   B CB  
5983 C CG  . LEU   B 127 ? 0.1694 0.1278 0.2154 0.0010  0.0242  0.0141  127 LEU   B CG  
5984 C CD1 . LEU   B 127 ? 0.1776 0.1286 0.2151 0.0052  0.0132  0.0087  127 LEU   B CD1 
5985 C CD2 . LEU   B 127 ? 0.1721 0.1324 0.2419 -0.0129 0.0282  0.0226  127 LEU   B CD2 
5997 N N   . SER   B 128 ? 0.1428 0.1292 0.2034 -0.0005 0.0069  0.0194  128 SER   B N   
5998 C CA  . SER   B 128 ? 0.1575 0.1338 0.2005 0.0080  -0.0014 0.0228  128 SER   B CA  
5999 C C   . SER   B 128 ? 0.1702 0.1438 0.2223 0.0107  -0.0189 0.0225  128 SER   B C   
6000 O O   . SER   B 128 ? 0.1854 0.1454 0.2581 0.0030  -0.0055 0.0346  128 SER   B O   
6001 C CB  . SER   B 128 ? 0.1710 0.1405 0.2042 0.0061  0.0043  0.0295  128 SER   B CB  
6002 O OG  . SER   B 128 ? 0.1726 0.1573 0.2069 0.0086  0.0135  0.0303  128 SER   B OG  
6008 N N   . ALA   B 129 ? 0.1812 0.1462 0.2472 0.0283  -0.0118 0.0022  129 ALA   B N   
6009 C CA  . ALA   B 129 ? 0.1994 0.1496 0.2520 0.0308  -0.0055 -0.0006 129 ALA   B CA  
6010 C C   . ALA   B 129 ? 0.1838 0.1395 0.2438 0.0153  0.0158  0.0104  129 ALA   B C   
6011 O O   . ALA   B 129 ? 0.1693 0.1462 0.2411 0.0147  0.0034  0.0188  129 ALA   B O   
6012 C CB  . ALA   B 129 ? 0.2243 0.1785 0.2952 0.0374  -0.0012 -0.0061 129 ALA   B CB  
6018 N N   . GLY   B 130 ? 0.1832 0.1444 0.2472 0.0231  0.0132  0.0009  130 GLY   B N   
6019 C CA  . GLY   B 130 ? 0.1857 0.1558 0.2546 0.0253  0.0237  -0.0042 130 GLY   B CA  
6020 C C   . GLY   B 130 ? 0.1879 0.1587 0.2468 0.0185  0.0191  0.0115  130 GLY   B C   
6021 O O   . GLY   B 130 ? 0.2077 0.1667 0.2609 0.0202  0.0137  0.0189  130 GLY   B O   
6025 N N   . ILE   B 131 ? 0.1772 0.1669 0.2584 0.0316  0.0122  0.0110  131 ILE   B N   
6026 C CA  . ILE   B 131 ? 0.1960 0.1806 0.2636 0.0291  0.0040  0.0171  131 ILE   B CA  
6027 C C   . ILE   B 131 ? 0.2081 0.1734 0.2360 0.0198  0.0079  0.0201  131 ILE   B C   
6028 O O   . ILE   B 131 ? 0.2359 0.1882 0.2496 0.0207  -0.0145 0.0194  131 ILE   B O   
6029 C CB  . ILE   B 131 ? 0.2007 0.2190 0.2961 0.0218  -0.0130 0.0283  131 ILE   B CB  
6030 C CG1 . ILE   B 131 ? 0.2086 0.2423 0.3129 -0.0006 -0.0127 0.0366  131 ILE   B CG1 
6031 C CG2 . ILE   B 131 ? 0.1995 0.2366 0.3253 0.0259  -0.0128 0.0159  131 ILE   B CG2 
6032 C CD1 . ILE   B 131 ? 0.2140 0.2602 0.3214 -0.0166 -0.0223 0.0494  131 ILE   B CD1 
6044 N N   . PHE   B 132 ? 0.1963 0.1550 0.2272 0.0207  0.0193  0.0185  132 PHE   B N   
6045 C CA  . PHE   B 132 ? 0.2116 0.1542 0.2126 0.0110  0.0316  0.0137  132 PHE   B CA  
6046 C C   . PHE   B 132 ? 0.2324 0.1745 0.2249 0.0103  0.0401  0.0167  132 PHE   B C   
6047 O O   . PHE   B 132 ? 0.2529 0.2016 0.2451 0.0011  0.0563  0.0229  132 PHE   B O   
6048 C CB  . PHE   B 132 ? 0.2009 0.1602 0.1988 0.0140  0.0310  0.0230  132 PHE   B CB  
6049 C CG  . PHE   B 132 ? 0.1933 0.1656 0.1867 0.0163  0.0254  0.0265  132 PHE   B CG  
6050 C CD1 . PHE   B 132 ? 0.1969 0.1656 0.2245 0.0116  0.0282  0.0250  132 PHE   B CD1 
6051 C CD2 . PHE   B 132 ? 0.1907 0.1682 0.1619 0.0225  0.0141  0.0294  132 PHE   B CD2 
6052 C CE1 . PHE   B 132 ? 0.1983 0.1695 0.2407 0.0041  0.0203  0.0275  132 PHE   B CE1 
6053 C CE2 . PHE   B 132 ? 0.2009 0.1713 0.1815 0.0166  0.0064  0.0231  132 PHE   B CE2 
6054 C CZ  . PHE   B 132 ? 0.2004 0.1726 0.2166 0.0039  0.0031  0.0306  132 PHE   B CZ  
6064 N N   . GLY   B 133 ? 0.2300 0.1668 0.2354 0.0028  0.0286  0.0413  133 GLY   B N   
6065 C CA  . GLY   B 133 ? 0.2359 0.1818 0.2512 -0.0187 0.0300  0.0535  133 GLY   B CA  
6066 C C   . GLY   B 133 ? 0.2384 0.1880 0.2518 -0.0310 0.0397  0.0493  133 GLY   B C   
6067 O O   . GLY   B 133 ? 0.2591 0.1999 0.2965 -0.0465 0.0396  0.0608  133 GLY   B O   
6071 N N   . ALA   B 134 ? 0.2155 0.1855 0.2326 -0.0257 0.0428  0.0344  134 ALA   B N   
6072 C CA  . ALA   B 134 ? 0.2090 0.1842 0.2442 -0.0181 0.0384  0.0172  134 ALA   B CA  
6073 C C   . ALA   B 134 ? 0.2165 0.1714 0.2510 -0.0112 0.0358  0.0317  134 ALA   B C   
6074 O O   . ALA   B 134 ? 0.2222 0.1957 0.2641 0.0037  0.0287  0.0231  134 ALA   B O   
6075 C CB  . ALA   B 134 ? 0.2095 0.1873 0.2610 -0.0100 0.0304  0.0113  134 ALA   B CB  
6081 N N   . ASP   B 135 ? 0.2286 0.1650 0.2501 -0.0148 0.0188  0.0444  135 ASP   B N   
6082 C CA  . ASP   B 135 ? 0.2435 0.1635 0.2761 -0.0113 0.0042  0.0376  135 ASP   B CA  
6083 C C   . ASP   B 135 ? 0.2194 0.1531 0.2665 -0.0005 0.0022  0.0318  135 ASP   B C   
6084 O O   . ASP   B 135 ? 0.2114 0.1494 0.2801 -0.0014 0.0028  0.0369  135 ASP   B O   
6085 C CB  . ASP   B 135 ? 0.2768 0.1740 0.2989 -0.0369 0.0024  0.0486  135 ASP   B CB  
6086 C CG  . ASP   B 135 ? 0.3087 0.1757 0.3499 -0.0615 0.0030  0.0427  135 ASP   B CG  
6087 O OD1 . ASP   B 135 ? 0.3139 0.1654 0.3462 -0.0446 -0.0071 0.0380  135 ASP   B OD1 
6088 O OD2 . ASP   B 135 ? 0.3350 0.2051 0.4076 -0.0817 0.0001  0.0217  135 ASP   B OD2 
6093 N N   . PRO   B 136 ? 0.2149 0.1536 0.2705 0.0238  -0.0027 0.0260  136 PRO   B N   
6094 C CA  . PRO   B 136 ? 0.1971 0.1483 0.2669 0.0163  -0.0071 0.0140  136 PRO   B CA  
6095 C C   . PRO   B 136 ? 0.1741 0.1308 0.2764 0.0118  -0.0028 0.0080  136 PRO   B C   
6096 O O   . PRO   B 136 ? 0.1593 0.1279 0.2654 0.0104  0.0105  0.0060  136 PRO   B O   
6097 C CB  . PRO   B 136 ? 0.2083 0.1699 0.2857 0.0295  -0.0108 0.0019  136 PRO   B CB  
6098 C CG  . PRO   B 136 ? 0.2271 0.1800 0.3039 0.0348  -0.0031 0.0044  136 PRO   B CG  
6099 C CD  . PRO   B 136 ? 0.2273 0.1708 0.2877 0.0400  0.0032  0.0123  136 PRO   B CD  
6107 N N   . ILE   B 137 ? 0.1847 0.1270 0.2828 0.0173  -0.0118 0.0087  137 ILE   B N   
6108 C CA  . ILE   B 137 ? 0.1946 0.1299 0.2908 0.0027  -0.0020 -0.0001 137 ILE   B CA  
6109 C C   . ILE   B 137 ? 0.1813 0.1338 0.2823 -0.0048 0.0116  0.0108  137 ILE   B C   
6110 O O   . ILE   B 137 ? 0.1680 0.1376 0.2778 -0.0072 0.0047  0.0045  137 ILE   B O   
6111 C CB  . ILE   B 137 ? 0.2227 0.1366 0.3425 -0.0029 -0.0038 0.0071  137 ILE   B CB  
6112 C CG1 . ILE   B 137 ? 0.2532 0.1527 0.3941 0.0024  0.0019  -0.0061 137 ILE   B CG1 
6113 C CG2 . ILE   B 137 ? 0.2323 0.1384 0.3511 -0.0256 -0.0042 0.0111  137 ILE   B CG2 
6114 C CD1 . ILE   B 137 ? 0.2789 0.1810 0.4416 0.0162  -0.0008 -0.0015 137 ILE   B CD1 
6126 N N   . HIS   B 138 ? 0.1896 0.1304 0.2742 -0.0030 0.0172  0.0147  138 HIS   B N   
6127 C CA  . HIS   B 138 ? 0.1952 0.1404 0.2652 -0.0031 0.0270  0.0208  138 HIS   B CA  
6128 C C   . HIS   B 138 ? 0.1794 0.1392 0.2568 -0.0018 0.0302  0.0188  138 HIS   B C   
6129 O O   . HIS   B 138 ? 0.1722 0.1440 0.2802 0.0064  0.0357  0.0297  138 HIS   B O   
6130 C CB  . HIS   B 138 ? 0.2217 0.1560 0.2883 -0.0084 0.0489  0.0177  138 HIS   B CB  
6131 C CG  . HIS   B 138 ? 0.2445 0.1773 0.2962 -0.0150 0.0734  0.0349  138 HIS   B CG  
6132 N ND1 . HIS   B 138 ? 0.2545 0.1964 0.3261 -0.0122 0.0897  0.0238  138 HIS   B ND1 
6133 C CD2 . HIS   B 138 ? 0.2597 0.1906 0.2912 -0.0147 0.0791  0.0363  138 HIS   B CD2 
6134 C CE1 . HIS   B 138 ? 0.2623 0.1976 0.3219 -0.0134 0.0932  0.0218  138 HIS   B CE1 
6135 N NE2 . HIS   B 138 ? 0.2654 0.1918 0.2973 -0.0074 0.0875  0.0263  138 HIS   B NE2 
6143 N N   . SER   B 139 ? 0.1764 0.1303 0.2549 0.0065  0.0230  0.0183  139 SER   B N   
6144 C CA  . SER   B 139 ? 0.1721 0.1247 0.2459 -0.0004 0.0220  0.0042  139 SER   B CA  
6145 C C   . SER   B 139 ? 0.1496 0.1178 0.2392 -0.0012 0.0126  0.0047  139 SER   B C   
6146 O O   . SER   B 139 ? 0.1496 0.1212 0.2336 0.0024  0.0049  0.0102  139 SER   B O   
6147 C CB  . SER   B 139 ? 0.1793 0.1249 0.2427 0.0000  0.0048  0.0044  139 SER   B CB  
6148 O OG  . SER   B 139 ? 0.1806 0.1266 0.2356 0.0009  -0.0045 0.0159  139 SER   B OG  
6154 N N   . LEU   B 140 ? 0.1521 0.1164 0.2369 -0.0054 0.0190  0.0003  140 LEU   B N   
6155 C CA  . LEU   B 140 ? 0.1466 0.1185 0.2374 -0.0046 0.0123  0.0037  140 LEU   B CA  
6156 C C   . LEU   B 140 ? 0.1435 0.1157 0.2435 -0.0041 0.0057  -0.0093 140 LEU   B C   
6157 O O   . LEU   B 140 ? 0.1466 0.1254 0.2453 -0.0049 0.0071  0.0011  140 LEU   B O   
6158 C CB  . LEU   B 140 ? 0.1465 0.1185 0.2436 -0.0126 0.0168  -0.0075 140 LEU   B CB  
6159 C CG  . LEU   B 140 ? 0.1545 0.1231 0.2379 -0.0131 0.0006  -0.0001 140 LEU   B CG  
6160 C CD1 . LEU   B 140 ? 0.1657 0.1303 0.2442 -0.0123 0.0101  -0.0024 140 LEU   B CD1 
6161 C CD2 . LEU   B 140 ? 0.1752 0.1296 0.2474 -0.0166 -0.0088 -0.0067 140 LEU   B CD2 
6173 N N   . ARG   B 141 ? 0.1392 0.1129 0.2631 -0.0104 0.0099  -0.0003 141 ARG   B N   
6174 C CA  . ARG   B 141 ? 0.1448 0.1203 0.3045 -0.0143 0.0239  -0.0057 141 ARG   B CA  
6175 C C   . ARG   B 141 ? 0.1349 0.1203 0.2914 -0.0121 0.0162  -0.0045 141 ARG   B C   
6176 O O   . ARG   B 141 ? 0.1421 0.1233 0.2908 -0.0141 0.0098  -0.0111 141 ARG   B O   
6177 C CB  . ARG   B 141 ? 0.1608 0.1320 0.3211 -0.0218 0.0354  -0.0017 141 ARG   B CB  
6178 C CG  . ARG   B 141 ? 0.1888 0.1640 0.3265 -0.0196 0.0305  -0.0066 141 ARG   B CG  
6179 C CD  . ARG   B 141 ? 0.2252 0.1887 0.3245 -0.0153 0.0089  -0.0149 141 ARG   B CD  
6180 N NE  . ARG   B 141 ? 0.2443 0.1853 0.3123 -0.0289 0.0132  -0.0226 141 ARG   B NE  
6181 C CZ  . ARG   B 141 ? 0.2582 0.1709 0.2887 -0.0233 0.0197  -0.0309 141 ARG   B CZ  
6182 N NH1 . ARG   B 141 ? 0.2671 0.1608 0.2783 -0.0206 0.0158  -0.0259 141 ARG   B NH1 
6183 N NH2 . ARG   B 141 ? 0.2685 0.1798 0.3135 -0.0112 0.0078  -0.0192 141 ARG   B NH2 
6197 N N   . VAL   B 142 ? 0.1383 0.1172 0.2755 -0.0092 0.0151  -0.0029 142 VAL   B N   
6198 C CA  . VAL   B 142 ? 0.1338 0.1211 0.2713 -0.0053 0.0249  -0.0017 142 VAL   B CA  
6199 C C   . VAL   B 142 ? 0.1319 0.1204 0.2581 -0.0039 0.0104  -0.0086 142 VAL   B C   
6200 O O   . VAL   B 142 ? 0.1420 0.1208 0.2596 0.0006  0.0057  -0.0013 142 VAL   B O   
6201 C CB  . VAL   B 142 ? 0.1482 0.1336 0.2726 -0.0012 0.0256  0.0111  142 VAL   B CB  
6202 C CG1 . VAL   B 142 ? 0.1457 0.1318 0.2761 0.0076  0.0254  0.0087  142 VAL   B CG1 
6203 C CG2 . VAL   B 142 ? 0.1687 0.1333 0.2844 0.0003  0.0184  0.0099  142 VAL   B CG2 
6213 N N   . CYS   B 143 ? 0.1340 0.1225 0.2456 -0.0007 0.0129  0.0059  143 CYS   B N   
6214 C CA  . CYS   B 143 ? 0.1290 0.1171 0.2419 -0.0030 0.0010  0.0025  143 CYS   B CA  
6215 C C   . CYS   B 143 ? 0.1279 0.1222 0.2401 -0.0037 0.0088  -0.0058 143 CYS   B C   
6216 O O   . CYS   B 143 ? 0.1384 0.1244 0.2338 -0.0070 0.0009  -0.0014 143 CYS   B O   
6217 C CB  . CYS   B 143 ? 0.1432 0.1288 0.2390 -0.0093 -0.0019 -0.0054 143 CYS   B CB  
6218 S SG  . CYS   B 143 ? 0.1398 0.1428 0.2284 -0.0055 0.0079  0.0029  143 CYS   B SG  
6224 N N   . VAL   B 144 ? 0.1350 0.1214 0.2510 -0.0105 0.0021  -0.0146 144 VAL   B N   
6225 C CA  . VAL   B 144 ? 0.1404 0.1323 0.2730 -0.0150 -0.0060 -0.0214 144 VAL   B CA  
6226 C C   . VAL   B 144 ? 0.1323 0.1336 0.2782 -0.0152 -0.0125 -0.0052 144 VAL   B C   
6227 O O   . VAL   B 144 ? 0.1450 0.1549 0.3006 0.0003  -0.0078 0.0187  144 VAL   B O   
6228 C CB  . VAL   B 144 ? 0.1597 0.1486 0.3239 -0.0174 -0.0147 -0.0330 144 VAL   B CB  
6229 C CG1 . VAL   B 144 ? 0.1825 0.1864 0.3582 -0.0040 -0.0201 -0.0232 144 VAL   B CG1 
6230 C CG2 . VAL   B 144 ? 0.1711 0.1461 0.3183 -0.0040 -0.0314 -0.0394 144 VAL   B CG2 
6240 N N   . ASP   B 145 ? 0.1388 0.1274 0.2855 -0.0076 -0.0004 -0.0129 145 ASP   B N   
6241 C CA  . ASP   B 145 ? 0.1337 0.1311 0.3144 -0.0087 0.0082  -0.0139 145 ASP   B CA  
6242 C C   . ASP   B 145 ? 0.1352 0.1328 0.2980 -0.0041 0.0041  -0.0115 145 ASP   B C   
6243 O O   . ASP   B 145 ? 0.1376 0.1462 0.3474 -0.0109 0.0076  -0.0275 145 ASP   B O   
6244 C CB  . ASP   B 145 ? 0.1426 0.1425 0.3626 -0.0192 0.0319  -0.0087 145 ASP   B CB  
6245 C CG  . ASP   B 145 ? 0.1614 0.1412 0.4079 -0.0266 0.0410  -0.0030 145 ASP   B CG  
6246 O OD1 . ASP   B 145 ? 0.1663 0.1465 0.4094 -0.0211 0.0046  -0.0140 145 ASP   B OD1 
6247 O OD2 . ASP   B 145 ? 0.1958 0.1447 0.4492 -0.0281 0.0607  0.0016  145 ASP   B OD2 
6252 N N   . THR   B 146 ? 0.1291 0.1264 0.2454 -0.0054 0.0011  -0.0020 146 THR   B N   
6253 C CA  . THR   B 146 ? 0.1392 0.1249 0.2249 -0.0077 0.0082  -0.0079 146 THR   B CA  
6254 C C   . THR   B 146 ? 0.1332 0.1214 0.2173 -0.0057 0.0049  -0.0043 146 THR   B C   
6255 O O   . THR   B 146 ? 0.1410 0.1211 0.2324 0.0003  0.0024  -0.0046 146 THR   B O   
6256 C CB  . THR   B 146 ? 0.1418 0.1199 0.2341 -0.0030 0.0193  -0.0041 146 THR   B CB  
6257 O OG1 . THR   B 146 ? 0.1470 0.1226 0.2416 -0.0038 0.0228  0.0077  146 THR   B OG1 
6258 C CG2 . THR   B 146 ? 0.1514 0.1314 0.2320 -0.0035 0.0162  -0.0095 146 THR   B CG2 
6266 N N   . VAL   B 147 ? 0.1416 0.1263 0.2060 -0.0057 0.0078  0.0002  147 VAL   B N   
6267 C CA  . VAL   B 147 ? 0.1433 0.1200 0.1947 -0.0073 -0.0039 0.0032  147 VAL   B CA  
6268 C C   . VAL   B 147 ? 0.1383 0.1230 0.2020 -0.0134 -0.0074 -0.0027 147 VAL   B C   
6269 O O   . VAL   B 147 ? 0.1487 0.1369 0.2170 -0.0217 -0.0251 -0.0158 147 VAL   B O   
6270 C CB  . VAL   B 147 ? 0.1480 0.1300 0.1875 -0.0109 -0.0072 0.0011  147 VAL   B CB  
6271 C CG1 . VAL   B 147 ? 0.1438 0.1486 0.1798 -0.0108 -0.0037 -0.0008 147 VAL   B CG1 
6272 C CG2 . VAL   B 147 ? 0.1454 0.1300 0.1949 -0.0096 0.0010  -0.0015 147 VAL   B CG2 
6282 N N   . ARG   B 148 ? 0.1403 0.1259 0.1947 -0.0109 -0.0195 -0.0061 148 ARG   B N   
6283 C CA  . ARG   B 148 ? 0.1440 0.1342 0.1938 -0.0096 -0.0275 -0.0034 148 ARG   B CA  
6284 C C   . ARG   B 148 ? 0.1502 0.1432 0.1854 -0.0151 -0.0267 -0.0058 148 ARG   B C   
6285 O O   . ARG   B 148 ? 0.1676 0.1745 0.1925 -0.0250 -0.0359 -0.0023 148 ARG   B O   
6286 C CB  . ARG   B 148 ? 0.1474 0.1425 0.1974 -0.0043 -0.0338 -0.0155 148 ARG   B CB  
6287 C CG  . ARG   B 148 ? 0.1474 0.1585 0.2201 -0.0106 -0.0223 -0.0364 148 ARG   B CG  
6288 C CD  . ARG   B 148 ? 0.1539 0.1714 0.2254 0.0091  -0.0245 -0.0382 148 ARG   B CD  
6289 N NE  . ARG   B 148 ? 0.1619 0.1751 0.2154 0.0199  -0.0258 -0.0304 148 ARG   B NE  
6290 C CZ  . ARG   B 148 ? 0.1551 0.1657 0.1963 0.0148  -0.0139 -0.0287 148 ARG   B CZ  
6291 N NH1 . ARG   B 148 ? 0.1489 0.1664 0.2060 -0.0035 0.0025  -0.0244 148 ARG   B NH1 
6292 N NH2 . ARG   B 148 ? 0.1733 0.1511 0.1956 0.0164  -0.0130 -0.0169 148 ARG   B NH2 
6306 N N   . THR   B 149 ? 0.1524 0.1376 0.1887 -0.0145 -0.0213 -0.0026 149 THR   B N   
6307 C CA  . THR   B 149 ? 0.1571 0.1432 0.1833 -0.0139 -0.0205 0.0033  149 THR   B CA  
6308 C C   . THR   B 149 ? 0.1493 0.1414 0.1628 -0.0167 -0.0257 0.0016  149 THR   B C   
6309 O O   . THR   B 149 ? 0.1586 0.1370 0.1845 -0.0192 -0.0112 -0.0055 149 THR   B O   
6310 C CB  . THR   B 149 ? 0.1616 0.1395 0.1872 -0.0168 -0.0229 0.0022  149 THR   B CB  
6311 O OG1 . THR   B 149 ? 0.1605 0.1510 0.1750 -0.0252 -0.0261 0.0021  149 THR   B OG1 
6312 C CG2 . THR   B 149 ? 0.1710 0.1398 0.2104 -0.0085 -0.0216 -0.0051 149 THR   B CG2 
6320 N N   . ASN   B 150 ? 0.1584 0.1441 0.1552 -0.0142 -0.0274 -0.0037 150 ASN   B N   
6321 C CA  . ASN   B 150 ? 0.1648 0.1567 0.1627 -0.0184 -0.0300 -0.0031 150 ASN   B CA  
6322 C C   . ASN   B 150 ? 0.1564 0.1450 0.1557 -0.0176 -0.0232 -0.0054 150 ASN   B C   
6323 O O   . ASN   B 150 ? 0.1621 0.1427 0.1802 -0.0302 -0.0380 -0.0013 150 ASN   B O   
6324 C CB  . ASN   B 150 ? 0.1877 0.1857 0.1751 -0.0213 -0.0383 0.0034  150 ASN   B CB  
6325 C CG  . ASN   B 150 ? 0.2144 0.2282 0.2150 -0.0193 -0.0469 0.0197  150 ASN   B CG  
6326 O OD1 . ASN   B 150 ? 0.2295 0.2432 0.2286 -0.0302 -0.0554 0.0132  150 ASN   B OD1 
6327 N ND2 . ASN   B 150 ? 0.2222 0.2470 0.2530 -0.0042 -0.0520 0.0598  150 ASN   B ND2 
6334 N N   . VAL   B 151 ? 0.1489 0.1403 0.1612 -0.0188 -0.0228 -0.0009 151 VAL   B N   
6335 C CA  . VAL   B 151 ? 0.1544 0.1459 0.1593 -0.0203 -0.0145 -0.0033 151 VAL   B CA  
6336 C C   . VAL   B 151 ? 0.1532 0.1421 0.1639 -0.0268 -0.0277 -0.0063 151 VAL   B C   
6337 O O   . VAL   B 151 ? 0.1598 0.1495 0.1846 -0.0327 -0.0209 -0.0127 151 VAL   B O   
6338 C CB  . VAL   B 151 ? 0.1746 0.1561 0.1757 -0.0065 -0.0160 -0.0066 151 VAL   B CB  
6339 C CG1 . VAL   B 151 ? 0.1740 0.1611 0.2060 -0.0164 -0.0048 -0.0107 151 VAL   B CG1 
6340 C CG2 . VAL   B 151 ? 0.1882 0.1686 0.1749 0.0054  -0.0097 0.0009  151 VAL   B CG2 
6350 N N   . TYR   B 152 ? 0.1480 0.1325 0.1542 -0.0213 -0.0188 -0.0066 152 TYR   B N   
6351 C CA  . TYR   B 152 ? 0.1551 0.1477 0.1448 -0.0311 -0.0202 -0.0093 152 TYR   B CA  
6352 C C   . TYR   B 152 ? 0.1532 0.1296 0.1448 -0.0253 -0.0090 -0.0151 152 TYR   B C   
6353 O O   . TYR   B 152 ? 0.1562 0.1345 0.1569 -0.0251 -0.0088 -0.0063 152 TYR   B O   
6354 C CB  . TYR   B 152 ? 0.1689 0.1623 0.1459 -0.0319 -0.0102 0.0012  152 TYR   B CB  
6355 C CG  . TYR   B 152 ? 0.1807 0.1715 0.1414 -0.0387 -0.0081 -0.0027 152 TYR   B CG  
6356 C CD1 . TYR   B 152 ? 0.1941 0.1822 0.1400 -0.0348 -0.0178 0.0010  152 TYR   B CD1 
6357 C CD2 . TYR   B 152 ? 0.2021 0.1874 0.1459 -0.0393 -0.0031 -0.0035 152 TYR   B CD2 
6358 C CE1 . TYR   B 152 ? 0.2115 0.2029 0.1597 -0.0274 -0.0274 0.0104  152 TYR   B CE1 
6359 C CE2 . TYR   B 152 ? 0.2165 0.2091 0.1602 -0.0428 -0.0143 -0.0099 152 TYR   B CE2 
6360 C CZ  . TYR   B 152 ? 0.2212 0.2259 0.1536 -0.0348 -0.0390 0.0141  152 TYR   B CZ  
6361 O OH  . TYR   B 152 ? 0.2420 0.2593 0.1894 -0.0225 -0.0459 0.0270  152 TYR   B OH  
6371 N N   . LEU   B 153 ? 0.1481 0.1295 0.1576 -0.0272 -0.0150 -0.0069 153 LEU   B N   
6372 C CA  . LEU   B 153 ? 0.1513 0.1266 0.1424 -0.0199 -0.0040 -0.0104 153 LEU   B CA  
6373 C C   . LEU   B 153 ? 0.1564 0.1233 0.1582 -0.0263 0.0018  -0.0132 153 LEU   B C   
6374 O O   . LEU   B 153 ? 0.1623 0.1437 0.1766 -0.0135 -0.0050 -0.0325 153 LEU   B O   
6375 C CB  . LEU   B 153 ? 0.1560 0.1260 0.1604 -0.0212 -0.0061 -0.0061 153 LEU   B CB  
6376 C CG  . LEU   B 153 ? 0.1507 0.1358 0.1914 -0.0215 -0.0066 -0.0017 153 LEU   B CG  
6377 C CD1 . LEU   B 153 ? 0.1576 0.1442 0.2042 -0.0221 -0.0033 0.0008  153 LEU   B CD1 
6378 C CD2 . LEU   B 153 ? 0.1549 0.1503 0.1944 -0.0307 0.0093  -0.0050 153 LEU   B CD2 
6390 N N   . ALA   B 154 ? 0.1506 0.1305 0.1775 -0.0121 -0.0083 -0.0139 154 ALA   B N   
6391 C CA  . ALA   B 154 ? 0.1613 0.1392 0.2004 -0.0006 -0.0104 -0.0253 154 ALA   B CA  
6392 C C   . ALA   B 154 ? 0.1756 0.1380 0.2067 0.0025  -0.0225 -0.0283 154 ALA   B C   
6393 O O   . ALA   B 154 ? 0.2047 0.1404 0.2232 0.0034  -0.0072 -0.0073 154 ALA   B O   
6394 C CB  . ALA   B 154 ? 0.1563 0.1507 0.2167 -0.0003 -0.0164 -0.0289 154 ALA   B CB  
6400 N N   . VAL   B 155 ? 0.1438 0.1302 0.2130 -0.0012 -0.0023 -0.0137 155 VAL   B N   
6401 C CA  . VAL   B 155 ? 0.1345 0.1291 0.2325 -0.0014 -0.0082 -0.0118 155 VAL   B CA  
6402 C C   . VAL   B 155 ? 0.1377 0.1328 0.2292 -0.0048 -0.0055 -0.0200 155 VAL   B C   
6403 O O   . VAL   B 155 ? 0.1530 0.1470 0.2662 0.0062  -0.0087 -0.0395 155 VAL   B O   
6404 C CB  . VAL   B 155 ? 0.1428 0.1427 0.2632 -0.0100 -0.0141 -0.0049 155 VAL   B CB  
6405 C CG1 . VAL   B 155 ? 0.1543 0.1363 0.2570 -0.0149 -0.0099 -0.0135 155 VAL   B CG1 
6406 C CG2 . VAL   B 155 ? 0.1342 0.1577 0.2989 -0.0091 -0.0131 0.0227  155 VAL   B CG2 
6416 N N   . PHE   B 156 ? 0.1263 0.1380 0.2422 -0.0007 -0.0023 -0.0157 156 PHE   B N   
6417 C CA  . PHE   B 156 ? 0.1359 0.1506 0.2786 0.0062  -0.0094 -0.0215 156 PHE   B CA  
6418 C C   . PHE   B 156 ? 0.1360 0.1560 0.3092 0.0099  -0.0098 -0.0453 156 PHE   B C   
6419 O O   . PHE   B 156 ? 0.1580 0.1801 0.3413 0.0213  -0.0060 -0.0437 156 PHE   B O   
6420 C CB  . PHE   B 156 ? 0.1458 0.1353 0.2760 0.0004  -0.0232 -0.0137 156 PHE   B CB  
6421 C CG  . PHE   B 156 ? 0.1433 0.1515 0.2941 -0.0038 -0.0135 0.0098  156 PHE   B CG  
6422 C CD1 . PHE   B 156 ? 0.1441 0.1762 0.3251 0.0008  -0.0062 0.0418  156 PHE   B CD1 
6423 C CD2 . PHE   B 156 ? 0.1463 0.1699 0.2904 0.0117  -0.0158 0.0115  156 PHE   B CD2 
6424 C CE1 . PHE   B 156 ? 0.1505 0.1954 0.3375 0.0050  -0.0051 0.0426  156 PHE   B CE1 
6425 C CE2 . PHE   B 156 ? 0.1556 0.1834 0.3047 0.0151  -0.0125 0.0165  156 PHE   B CE2 
6426 C CZ  . PHE   B 156 ? 0.1473 0.1908 0.3270 0.0149  -0.0183 0.0275  156 PHE   B CZ  
6436 N N   . ASP   B 157 ? 0.1347 0.1488 0.3257 0.0115  -0.0140 -0.0188 157 ASP   B N   
6437 C CA  . ASP   B 157 ? 0.1431 0.1525 0.3669 0.0082  -0.0192 -0.0297 157 ASP   B CA  
6438 C C   . ASP   B 157 ? 0.1452 0.1474 0.3776 0.0054  -0.0205 -0.0457 157 ASP   B C   
6439 O O   . ASP   B 157 ? 0.1409 0.1493 0.3616 0.0069  -0.0214 -0.0442 157 ASP   B O   
6440 C CB  . ASP   B 157 ? 0.1809 0.1740 0.3816 -0.0001 -0.0474 -0.0130 157 ASP   B CB  
6441 C CG  . ASP   B 157 ? 0.2117 0.1837 0.3964 -0.0005 -0.0429 -0.0161 157 ASP   B CG  
6442 O OD1 . ASP   B 157 ? 0.2172 0.1740 0.4151 0.0070  -0.0368 -0.0150 157 ASP   B OD1 
6443 O OD2 . ASP   B 157 ? 0.2382 0.2106 0.4107 -0.0014 -0.0257 -0.0139 157 ASP   B OD2 
6448 N N   . LYS   B 158 ? 0.1462 0.1761 0.3913 0.0067  -0.0069 -0.0832 158 LYS   B N   
6449 C CA  . LYS   B 158 ? 0.1688 0.1923 0.3963 0.0081  0.0047  -0.1001 158 LYS   B CA  
6450 C C   . LYS   B 158 ? 0.1648 0.1787 0.4041 0.0095  -0.0030 -0.0928 158 LYS   B C   
6451 O O   . LYS   B 158 ? 0.1677 0.1825 0.4045 -0.0001 0.0001  -0.0994 158 LYS   B O   
6452 C CB  . LYS   B 158 ? 0.1990 0.2351 0.3947 0.0101  0.0116  -0.1156 158 LYS   B CB  
6453 C CG  . LYS   B 158 ? 0.2345 0.2760 0.4043 0.0108  0.0178  -0.1221 158 LYS   B CG  
6454 C CD  . LYS   B 158 ? 0.2682 0.3268 0.4251 0.0052  0.0215  -0.1183 158 LYS   B CD  
6455 C CE  . LYS   B 158 ? 0.2906 0.3615 0.4396 0.0034  0.0207  -0.1181 158 LYS   B CE  
6456 N NZ  . LYS   B 158 ? 0.2911 0.3775 0.4386 -0.0010 0.0244  -0.1202 158 LYS   B NZ  
6470 N N   . ASN   B 159 ? 0.1640 0.1684 0.4210 0.0143  -0.0188 -0.0718 159 ASN   B N   
6471 C CA  . ASN   B 159 ? 0.1757 0.1610 0.4349 0.0184  -0.0397 -0.0584 159 ASN   B CA  
6472 C C   . ASN   B 159 ? 0.1653 0.1516 0.4221 0.0144  -0.0511 -0.0417 159 ASN   B C   
6473 O O   . ASN   B 159 ? 0.1658 0.1469 0.4455 -0.0010 -0.0626 -0.0269 159 ASN   B O   
6474 C CB  . ASN   B 159 ? 0.1949 0.1805 0.4627 0.0254  -0.0395 -0.0494 159 ASN   B CB  
6475 C CG  . ASN   B 159 ? 0.2228 0.2044 0.4922 0.0236  -0.0479 -0.0648 159 ASN   B CG  
6476 O OD1 . ASN   B 159 ? 0.2420 0.2102 0.4836 0.0285  -0.0466 -0.0754 159 ASN   B OD1 
6477 N ND2 . ASN   B 159 ? 0.2252 0.2165 0.5031 0.0255  -0.0553 -0.0526 159 ASN   B ND2 
6484 N N   . LEU   B 160 ? 0.1551 0.1484 0.3956 0.0072  -0.0439 -0.0369 160 LEU   B N   
6485 C CA  . LEU   B 160 ? 0.1503 0.1451 0.3536 0.0118  -0.0384 -0.0276 160 LEU   B CA  
6486 C C   . LEU   B 160 ? 0.1454 0.1327 0.3356 0.0075  -0.0253 -0.0336 160 LEU   B C   
6487 O O   . LEU   B 160 ? 0.1369 0.1421 0.3370 0.0008  -0.0286 -0.0259 160 LEU   B O   
6488 C CB  . LEU   B 160 ? 0.1509 0.1591 0.3395 0.0037  -0.0371 -0.0143 160 LEU   B CB  
6489 C CG  . LEU   B 160 ? 0.1509 0.1683 0.3219 0.0082  -0.0279 -0.0056 160 LEU   B CG  
6490 C CD1 . LEU   B 160 ? 0.1688 0.1838 0.3195 -0.0016 -0.0136 0.0007  160 LEU   B CD1 
6491 C CD2 . LEU   B 160 ? 0.1534 0.1642 0.3223 0.0212  -0.0234 -0.0118 160 LEU   B CD2 
6503 N N   . TYR   B 161 ? 0.1450 0.1432 0.3440 -0.0056 0.0014  -0.0425 161 TYR   B N   
6504 C CA  . TYR   B 161 ? 0.1543 0.1439 0.3324 -0.0077 0.0147  -0.0455 161 TYR   B CA  
6505 C C   . TYR   B 161 ? 0.1608 0.1458 0.3219 -0.0087 0.0144  -0.0410 161 TYR   B C   
6506 O O   . TYR   B 161 ? 0.1669 0.1432 0.3024 -0.0174 0.0015  -0.0388 161 TYR   B O   
6507 C CB  . TYR   B 161 ? 0.1674 0.1509 0.3309 -0.0165 0.0400  -0.0482 161 TYR   B CB  
6508 C CG  . TYR   B 161 ? 0.1966 0.1585 0.3144 -0.0274 0.0418  -0.0576 161 TYR   B CG  
6509 C CD1 . TYR   B 161 ? 0.2038 0.1594 0.3059 -0.0420 0.0521  -0.0542 161 TYR   B CD1 
6510 C CD2 . TYR   B 161 ? 0.2217 0.1689 0.3028 -0.0288 0.0312  -0.0654 161 TYR   B CD2 
6511 C CE1 . TYR   B 161 ? 0.2239 0.1828 0.3103 -0.0432 0.0531  -0.0572 161 TYR   B CE1 
6512 C CE2 . TYR   B 161 ? 0.2415 0.1853 0.3200 -0.0339 0.0352  -0.0667 161 TYR   B CE2 
6513 C CZ  . TYR   B 161 ? 0.2405 0.1883 0.3084 -0.0505 0.0346  -0.0608 161 TYR   B CZ  
6514 O OH  . TYR   B 161 ? 0.2696 0.2103 0.3259 -0.0503 0.0259  -0.0516 161 TYR   B OH  
6524 N N   . ASP   B 162 ? 0.1629 0.1459 0.3427 -0.0070 -0.0024 -0.0538 162 ASP   B N   
6525 C CA  . ASP   B 162 ? 0.1731 0.1525 0.3407 -0.0025 -0.0040 -0.0557 162 ASP   B CA  
6526 C C   . ASP   B 162 ? 0.1679 0.1404 0.3291 -0.0086 -0.0178 -0.0407 162 ASP   B C   
6527 O O   . ASP   B 162 ? 0.1724 0.1466 0.3337 -0.0108 -0.0293 -0.0364 162 ASP   B O   
6528 C CB  . ASP   B 162 ? 0.1923 0.1706 0.3649 0.0032  -0.0079 -0.0823 162 ASP   B CB  
6529 C CG  . ASP   B 162 ? 0.1972 0.1976 0.3951 0.0076  -0.0050 -0.0958 162 ASP   B CG  
6530 O OD1 . ASP   B 162 ? 0.1968 0.2197 0.3804 -0.0066 0.0177  -0.0914 162 ASP   B OD1 
6531 O OD2 . ASP   B 162 ? 0.2106 0.2168 0.4285 0.0244  -0.0096 -0.0895 162 ASP   B OD2 
6536 N N   A LYS   B 163 ? 0.1682 0.1457 0.3231 -0.0091 -0.0240 -0.0264 163 LYS   B N   
6537 N N   B LYS   B 163 ? 0.1636 0.1298 0.3221 -0.0091 -0.0297 -0.0287 163 LYS   B N   
6538 C CA  A LYS   B 163 ? 0.1757 0.1601 0.3250 -0.0137 -0.0217 -0.0103 163 LYS   B CA  
6539 C CA  B LYS   B 163 ? 0.1696 0.1362 0.3234 -0.0188 -0.0278 -0.0105 163 LYS   B CA  
6540 C C   A LYS   B 163 ? 0.1516 0.1455 0.3092 -0.0132 -0.0244 -0.0008 163 LYS   B C   
6541 C C   B LYS   B 163 ? 0.1467 0.1336 0.3105 -0.0156 -0.0262 -0.0034 163 LYS   B C   
6542 O O   A LYS   B 163 ? 0.1534 0.1508 0.3250 -0.0158 -0.0273 0.0037  163 LYS   B O   
6543 O O   B LYS   B 163 ? 0.1482 0.1398 0.3315 -0.0182 -0.0253 -0.0076 163 LYS   B O   
6544 C CB  A LYS   B 163 ? 0.2078 0.1926 0.3516 -0.0118 -0.0210 0.0001  163 LYS   B CB  
6545 C CB  B LYS   B 163 ? 0.2007 0.1557 0.3529 -0.0163 -0.0305 0.0107  163 LYS   B CB  
6546 C CG  A LYS   B 163 ? 0.2478 0.2350 0.3858 -0.0138 -0.0158 0.0023  163 LYS   B CG  
6547 C CG  B LYS   B 163 ? 0.2502 0.2083 0.3907 -0.0218 -0.0238 0.0144  163 LYS   B CG  
6548 C CD  A LYS   B 163 ? 0.2830 0.2677 0.4199 -0.0197 -0.0120 -0.0038 163 LYS   B CD  
6549 C CD  B LYS   B 163 ? 0.3002 0.2555 0.4316 -0.0329 -0.0197 0.0061  163 LYS   B CD  
6550 C CE  A LYS   B 163 ? 0.3110 0.3029 0.4409 -0.0243 -0.0062 -0.0064 163 LYS   B CE  
6551 C CE  B LYS   B 163 ? 0.3376 0.2978 0.4553 -0.0403 -0.0117 0.0017  163 LYS   B CE  
6552 N NZ  A LYS   B 163 ? 0.3230 0.3117 0.4581 -0.0271 -0.0021 -0.0103 163 LYS   B NZ  
6553 N NZ  B LYS   B 163 ? 0.3593 0.3174 0.4747 -0.0436 -0.0070 -0.0030 163 LYS   B NZ  
6580 N N   . LEU   B 164 ? 0.1333 0.1334 0.2924 -0.0119 -0.0223 -0.0042 164 LEU   B N   
6581 C CA  . LEU   B 164 ? 0.1337 0.1331 0.2689 -0.0106 -0.0235 -0.0040 164 LEU   B CA  
6582 C C   . LEU   B 164 ? 0.1464 0.1297 0.2694 -0.0178 -0.0235 0.0051  164 LEU   B C   
6583 O O   . LEU   B 164 ? 0.1479 0.1556 0.2965 -0.0158 -0.0271 0.0008  164 LEU   B O   
6584 C CB  . LEU   B 164 ? 0.1334 0.1343 0.2556 -0.0042 -0.0195 -0.0059 164 LEU   B CB  
6585 C CG  . LEU   B 164 ? 0.1485 0.1463 0.2607 -0.0110 -0.0070 -0.0014 164 LEU   B CG  
6586 C CD1 . LEU   B 164 ? 0.1577 0.1434 0.2576 -0.0097 -0.0119 -0.0152 164 LEU   B CD1 
6587 C CD2 . LEU   B 164 ? 0.1628 0.1818 0.2787 -0.0185 0.0097  -0.0221 164 LEU   B CD2 
6600 N N   . VAL   B 165 ? 0.1762 0.1401 0.2857 -0.0197 -0.0312 -0.0131 165 VAL   B N   
6601 C CA  . VAL   B 165 ? 0.2151 0.1504 0.2960 -0.0317 -0.0460 -0.0103 165 VAL   B CA  
6602 C C   . VAL   B 165 ? 0.2390 0.1608 0.3266 -0.0402 -0.0730 -0.0110 165 VAL   B C   
6603 O O   . VAL   B 165 ? 0.2531 0.1805 0.3326 -0.0459 -0.0844 -0.0049 165 VAL   B O   
6604 C CB  . VAL   B 165 ? 0.2411 0.1714 0.2970 -0.0154 -0.0127 -0.0222 165 VAL   B CB  
6605 C CG1 . VAL   B 165 ? 0.2579 0.1797 0.3121 -0.0232 -0.0044 -0.0227 165 VAL   B CG1 
6606 C CG2 . VAL   B 165 ? 0.2370 0.1728 0.2828 -0.0109 0.0044  -0.0183 165 VAL   B CG2 
6616 N N   . SER   B 166 ? 0.2443 0.1506 0.3591 -0.0382 -0.0809 -0.0280 166 SER   B N   
6617 C CA  . SER   B 166 ? 0.2374 0.1561 0.4170 -0.0386 -0.0690 -0.0354 166 SER   B CA  
6618 C C   . SER   B 166 ? 0.2234 0.1686 0.4343 -0.0394 -0.0656 -0.0033 166 SER   B C   
6619 O O   . SER   B 166 ? 0.2287 0.1930 0.4702 -0.0571 -0.0701 -0.0312 166 SER   B O   
6620 C CB  . SER   B 166 ? 0.2358 0.1703 0.4423 -0.0299 -0.0689 -0.0538 166 SER   B CB  
6621 O OG  . SER   B 166 ? 0.2223 0.1636 0.4569 -0.0258 -0.0703 -0.0314 166 SER   B OG  
6627 N N   . SER   B 167 ? 0.2030 0.1574 0.4065 -0.0377 -0.0762 0.0418  167 SER   B N   
6628 C CA  . SER   B 167 ? 0.1956 0.1695 0.3849 -0.0335 -0.0527 0.0353  167 SER   B CA  
6629 C C   . SER   B 167 ? 0.1887 0.1742 0.3627 -0.0481 -0.0483 0.0457  167 SER   B C   
6630 O O   . SER   B 167 ? 0.1847 0.1858 0.3559 -0.0511 -0.0507 0.0452  167 SER   B O   
6631 C CB  . SER   B 167 ? 0.1840 0.1776 0.3889 -0.0301 -0.0233 0.0282  167 SER   B CB  
6632 O OG  . SER   B 167 ? 0.1748 0.1823 0.3646 -0.0196 -0.0124 0.0280  167 SER   B OG  
6638 N N   . PHE   B 168 ? 0.1912 0.1749 0.3537 -0.0412 -0.0351 0.0538  168 PHE   B N   
6639 C CA  . PHE   B 168 ? 0.1914 0.1706 0.3190 -0.0443 -0.0316 0.0306  168 PHE   B CA  
6640 C C   . PHE   B 168 ? 0.1646 0.1638 0.2700 -0.0290 -0.0047 0.0191  168 PHE   B C   
6641 O O   . PHE   B 168 ? 0.1935 0.1530 0.2667 -0.0037 -0.0089 0.0002  168 PHE   B O   
6642 C CB  . PHE   B 168 ? 0.2096 0.1741 0.3242 -0.0520 -0.0498 0.0408  168 PHE   B CB  
6643 C CG  . PHE   B 168 ? 0.2308 0.1651 0.3089 -0.0492 -0.0450 0.0196  168 PHE   B CG  
6644 C CD1 . PHE   B 168 ? 0.2606 0.1703 0.3179 -0.0450 -0.0492 0.0153  168 PHE   B CD1 
6645 C CD2 . PHE   B 168 ? 0.2155 0.1633 0.3055 -0.0387 -0.0441 0.0186  168 PHE   B CD2 
6646 C CE1 . PHE   B 168 ? 0.2723 0.1802 0.3106 -0.0351 -0.0438 0.0214  168 PHE   B CE1 
6647 C CE2 . PHE   B 168 ? 0.2435 0.1690 0.3134 -0.0272 -0.0474 0.0177  168 PHE   B CE2 
6648 C CZ  . PHE   B 168 ? 0.2588 0.1677 0.3066 -0.0225 -0.0523 0.0257  168 PHE   B CZ  
6658 N N   . LEU   B 169 ? 0.1709 0.1787 0.2667 -0.0059 0.0142  0.0060  169 LEU   B N   
6659 C CA  . LEU   B 169 ? 0.1955 0.2013 0.2986 -0.0131 0.0086  -0.0225 169 LEU   B CA  
6660 C C   . LEU   B 169 ? 0.2269 0.2266 0.3563 0.0006  0.0013  -0.0506 169 LEU   B C   
6661 O O   . LEU   B 169 ? 0.2504 0.2476 0.4041 -0.0034 0.0031  -0.0752 169 LEU   B O   
6662 C CB  . LEU   B 169 ? 0.2169 0.2433 0.3053 -0.0259 0.0036  -0.0031 169 LEU   B CB  
6663 C CG  . LEU   B 169 ? 0.2608 0.2810 0.3450 -0.0133 0.0028  -0.0048 169 LEU   B CG  
6664 C CD1 . LEU   B 169 ? 0.2748 0.3055 0.3564 -0.0143 -0.0003 0.0116  169 LEU   B CD1 
6665 C CD2 . LEU   B 169 ? 0.2542 0.2870 0.3408 -0.0016 0.0186  -0.0260 169 LEU   B CD2 
6666 O OXT . LEU   B 169 ? 0.2449 0.2459 0.3603 0.0260  -0.0032 -0.0515 169 LEU   B OXT 
6678 N N2  B A1BAB C .   ? 0.1393 0.1395 0.2157 -0.0091 -0.0081 0.0371  201 A1BAB A N2  
6679 C C3  B A1BAB C .   ? 0.1377 0.1931 0.2200 0.0082  -0.0106 0.0148  201 A1BAB A C3  
6680 C C6  B A1BAB C .   ? 0.1547 0.1921 0.1895 -0.0040 -0.0111 -0.0051 201 A1BAB A C6  
6681 C C9  B A1BAB C .   ? 0.1326 0.1381 0.1648 0.0034  -0.0541 -0.0396 201 A1BAB A C9  
6682 C C12 B A1BAB C .   ? 0.1404 0.1601 0.1991 -0.0200 -0.0172 0.0372  201 A1BAB A C12 
6683 C C14 B A1BAB C .   ? 0.1487 0.1546 0.2151 -0.0204 -0.0201 0.0492  201 A1BAB A C14 
6684 C C17 B A1BAB C .   ? 0.1319 0.1413 0.1869 -0.0090 0.0192  0.0371  201 A1BAB A C17 
6685 C C1  B A1BAB C .   ? 0.1430 0.1995 0.2250 -0.0019 -0.0099 0.0291  201 A1BAB A C1  
6686 C C10 B A1BAB C .   ? 0.1531 0.1667 0.1811 -0.0115 -0.0149 -0.0192 201 A1BAB A C10 
6687 C C11 B A1BAB C .   ? 0.1625 0.1856 0.1855 -0.0082 -0.0049 -0.0114 201 A1BAB A C11 
6688 C C13 B A1BAB C .   ? 0.1372 0.1490 0.2008 -0.0193 -0.0104 0.0421  201 A1BAB A C13 
6689 C C15 B A1BAB C .   ? 0.1430 0.1483 0.2288 -0.0227 -0.0185 0.0445  201 A1BAB A C15 
6690 C C16 B A1BAB C .   ? 0.1303 0.1371 0.1970 -0.0121 0.0041  0.0404  201 A1BAB A C16 
6691 C C2  B A1BAB C .   ? 0.1463 0.1935 0.2193 -0.0019 -0.0141 0.0271  201 A1BAB A C2  
6692 C C4  B A1BAB C .   ? 0.1398 0.2000 0.2289 0.0073  -0.0040 0.0060  201 A1BAB A C4  
6693 C C5  B A1BAB C .   ? 0.1387 0.1967 0.1939 -0.0040 -0.0033 -0.0094 201 A1BAB A C5  
6694 C C7  B A1BAB C .   ? 0.1509 0.1946 0.1903 -0.0004 -0.0220 0.0042  201 A1BAB A C7  
6695 C C8  B A1BAB C .   ? 0.1556 0.1817 0.1859 -0.0004 -0.0386 -0.0100 201 A1BAB A C8  
6696 N N1  B A1BAB C .   ? 0.1519 0.1787 0.2138 -0.0180 -0.0176 0.0415  201 A1BAB A N1  
6697 N N3  B A1BAB C .   ? 0.1237 0.1349 0.1774 -0.0112 0.0317  0.0448  201 A1BAB A N3  
6698 N N4  B A1BAB C .   ? 0.1387 0.1474 0.2000 -0.0137 0.0009  0.0281  201 A1BAB A N4  
6699 O O1  B A1BAB C .   ? 0.1488 0.2135 0.2446 -0.0024 0.0121  0.0340  201 A1BAB A O1  
6718 O O1  C A1BAC D .   ? 0.1741 0.2176 0.2961 -0.0412 -0.0883 -0.0022 202 A1BAC A O1  
6719 C C1  C A1BAC D .   ? 0.1631 0.2056 0.2693 -0.0368 -0.0860 0.0017  202 A1BAC A C1  
6720 C C2  C A1BAC D .   ? 0.1440 0.1903 0.2257 -0.0257 -0.0827 -0.0042 202 A1BAC A C2  
6721 C C3  C A1BAC D .   ? 0.1496 0.1963 0.2128 -0.0167 -0.0534 -0.0054 202 A1BAC A C3  
6722 C C4  C A1BAC D .   ? 0.1519 0.1997 0.2090 -0.0140 -0.0465 -0.0097 202 A1BAC A C4  
6723 C C5  C A1BAC D .   ? 0.1534 0.2006 0.2085 -0.0088 -0.0328 -0.0124 202 A1BAC A C5  
6724 C C6  C A1BAC D .   ? 0.1552 0.2006 0.2052 -0.0065 -0.0200 -0.0066 202 A1BAC A C6  
6725 C C7  C A1BAC D .   ? 0.1564 0.1986 0.2099 -0.0081 -0.0274 -0.0014 202 A1BAC A C7  
6726 C C8  C A1BAC D .   ? 0.1544 0.1983 0.2018 -0.0055 -0.0262 0.0047  202 A1BAC A C8  
6727 C C10 C A1BAC D .   ? 0.1558 0.2030 0.2028 -0.0064 -0.0190 0.0058  202 A1BAC A C10 
6728 C C11 C A1BAC D .   ? 0.1551 0.2035 0.2028 -0.0073 -0.0149 0.0005  202 A1BAC A C11 
6729 C C12 C A1BAC D .   ? 0.1251 0.1718 0.2041 -0.0162 -0.0489 0.0145  202 A1BAC A C12 
6730 C C13 C A1BAC D .   ? 0.1224 0.1666 0.2008 -0.0071 -0.0306 0.0275  202 A1BAC A C13 
6731 C C14 C A1BAC D .   ? 0.1290 0.1700 0.2046 -0.0064 -0.0259 0.0393  202 A1BAC A C14 
6732 C C15 C A1BAC D .   ? 0.1270 0.1694 0.2107 -0.0070 -0.0297 0.0373  202 A1BAC A C15 
6733 C C16 C A1BAC D .   ? 0.1215 0.1653 0.2019 -0.0013 -0.0272 0.0251  202 A1BAC A C16 
6734 C C17 C A1BAC D .   ? 0.1232 0.1681 0.1998 -0.0052 -0.0279 0.0157  202 A1BAC A C17 
6735 C C9  C A1BAC D .   ? 0.1526 0.1986 0.1969 -0.0049 -0.0247 0.0067  202 A1BAC A C9  
6736 N N1  C A1BAC D .   ? 0.1293 0.1765 0.2224 -0.0295 -0.0697 0.0040  202 A1BAC A N1  
6737 N N2  C A1BAC D .   ? 0.1253 0.1656 0.2039 0.0028  -0.0306 0.0319  202 A1BAC A N2  
6738 N N3  C A1BAC D .   ? 0.1219 0.1671 0.2056 -0.0030 -0.0203 0.0186  202 A1BAC A N3  
6739 N N4  C A1BAC D .   ? 0.1211 0.1673 0.1968 -0.0135 -0.0406 0.0107  202 A1BAC A N4  
6758 O O   . HOH   E .   ? 0.3803 0.9024 0.5841 -0.1007 -0.1199 0.1578  301 HOH   A O   
6759 O O   A HOH   E .   ? 0.2926 0.5482 0.3390 -0.0873 -0.0063 0.0595  302 HOH   A O   
6760 O O   . HOH   E .   ? 0.6649 0.5115 0.7000 0.0704  -0.1050 0.0842  303 HOH   A O   
6761 O O   C HOH   E .   ? 0.1789 0.2168 0.3161 0.0230  -0.0231 -0.0154 304 HOH   A O   
6762 O O   . HOH   E .   ? 0.6071 0.5119 0.3388 0.2225  -0.0838 0.1103  305 HOH   A O   
6763 O O   B HOH   E .   ? 0.3524 0.2202 0.4612 0.0826  -0.0742 0.0679  306 HOH   A O   
6764 O O   . HOH   E .   ? 0.2872 0.3280 0.1674 -0.0431 0.0280  0.0556  307 HOH   A O   
6765 O O   . HOH   E .   ? 0.7328 0.5738 0.3870 -0.1552 -0.0541 0.1810  308 HOH   A O   
6766 O O   . HOH   E .   ? 0.6225 0.5010 0.5129 -0.0962 0.1662  0.1427  309 HOH   A O   
6767 O O   . HOH   E .   ? 0.3192 0.4757 0.4354 0.0291  -0.0815 0.0291  310 HOH   A O   
6768 O O   A HOH   E .   ? 0.2398 0.1043 0.3152 0.0156  -0.0053 0.0544  311 HOH   A O   
6769 O O   . HOH   E .   ? 0.6363 0.5168 0.4512 -0.1350 -0.1080 -0.0307 312 HOH   A O   
6770 O O   . HOH   E .   ? 0.4732 0.3603 0.6011 -0.0331 0.1391  -0.0155 313 HOH   A O   
6771 O O   . HOH   E .   ? 0.3203 0.2940 0.5607 -0.0312 -0.1579 0.1502  314 HOH   A O   
6772 O O   . HOH   E .   ? 0.4444 0.5942 0.5835 0.1998  0.1034  -0.1093 315 HOH   A O   
6773 O O   . HOH   E .   ? 0.6582 0.5714 0.3379 -0.0289 -0.0870 0.1098  316 HOH   A O   
6774 O O   B HOH   E .   ? 0.2150 0.1447 0.3715 0.0391  -0.0095 0.0120  317 HOH   A O   
6775 O O   A HOH   E .   ? 0.2566 0.3289 0.4216 0.0371  -0.0067 0.0226  318 HOH   A O   
6776 O O   . HOH   E .   ? 0.2127 0.1945 0.3937 -0.0586 0.0307  -0.0405 319 HOH   A O   
6777 O O   . HOH   E .   ? 0.3750 0.3524 0.3219 -0.1254 0.0004  0.1180  320 HOH   A O   
6778 O O   . HOH   E .   ? 0.5229 0.2764 0.3220 -0.1160 0.0557  0.0452  321 HOH   A O   
6779 O O   . HOH   E .   ? 0.1731 0.3452 0.2897 0.0398  -0.0175 -0.0033 322 HOH   A O   
6780 O O   B HOH   E .   ? 0.2485 0.2783 0.3818 -0.0737 0.0331  0.0529  323 HOH   A O   
6781 O O   A HOH   E .   ? 0.1769 0.1723 0.2673 0.0400  0.0429  0.0070  324 HOH   A O   
6782 O O   A HOH   E .   ? 0.4386 0.3873 0.2725 0.0834  -0.1040 0.0441  325 HOH   A O   
6783 O O   . HOH   E .   ? 0.1684 0.1843 0.2574 -0.0241 0.0188  0.0492  326 HOH   A O   
6784 O O   . HOH   E .   ? 0.1594 0.1470 0.2231 -0.0207 0.0057  0.0056  327 HOH   A O   
6785 O O   . HOH   E .   ? 0.6500 0.5475 0.5805 -0.0566 0.1840  0.2352  328 HOH   A O   
6786 O O   . HOH   E .   ? 0.4454 0.2021 0.4328 -0.0092 -0.1662 0.0675  329 HOH   A O   
6787 O O   . HOH   E .   ? 0.2111 0.3538 0.4136 -0.0506 0.0494  -0.1058 330 HOH   A O   
6788 O O   . HOH   E .   ? 0.2319 0.2158 0.3229 -0.0058 -0.0290 -0.0111 331 HOH   A O   
6789 O O   A HOH   E .   ? 0.2110 0.3247 0.3003 0.0370  -0.0043 0.0343  332 HOH   A O   
6790 O O   . HOH   E .   ? 0.3984 0.3573 0.3210 0.0266  -0.0419 -0.0537 333 HOH   A O   
6791 O O   . HOH   E .   ? 0.1586 0.3322 0.3345 0.0077  0.0242  0.0172  334 HOH   A O   
6792 O O   B HOH   E .   ? 0.1944 0.1883 0.1496 -0.0039 -0.0025 -0.0061 335 HOH   A O   
6793 O O   . HOH   E .   ? 0.4134 0.3984 0.4144 -0.0289 0.2079  0.0667  336 HOH   A O   
6794 O O   . HOH   E .   ? 0.3177 0.4325 0.2907 0.0017  0.0588  0.0676  337 HOH   A O   
6795 O O   . HOH   E .   ? 0.2458 0.2273 0.2632 0.0391  0.0244  0.0381  338 HOH   A O   
6796 O O   . HOH   E .   ? 0.6402 0.3575 0.3468 -0.0112 0.0171  0.1433  339 HOH   A O   
6797 O O   . HOH   E .   ? 0.5544 0.2070 0.5672 0.0733  0.0334  -0.0240 340 HOH   A O   
6798 O O   . HOH   E .   ? 0.2080 0.2016 0.3298 0.0163  0.0873  -0.0111 341 HOH   A O   
6799 O O   A HOH   E .   ? 0.1532 0.3768 0.1965 0.0660  0.0537  0.1214  342 HOH   A O   
6800 O O   A HOH   E .   ? 0.5159 0.3220 0.4454 0.0414  -0.1129 0.0050  343 HOH   A O   
6801 O O   . HOH   E .   ? 0.3617 0.4089 0.2451 0.0132  -0.1155 -0.0010 344 HOH   A O   
6802 O O   . HOH   E .   ? 0.3786 0.4787 0.3778 0.1032  -0.0446 -0.0918 345 HOH   A O   
6803 O O   . HOH   E .   ? 0.5216 0.5315 0.3307 -0.0998 0.1480  0.1029  346 HOH   A O   
6804 O O   . HOH   E .   ? 0.2379 0.4079 0.3556 0.1031  -0.0466 0.0002  347 HOH   A O   
6805 O O   . HOH   E .   ? 0.1522 0.2274 0.1994 0.0060  -0.0040 0.0520  348 HOH   A O   
6806 O O   B HOH   E .   ? 0.1700 0.2217 0.4451 0.0476  -0.0238 -0.0446 349 HOH   A O   
6807 O O   . HOH   E .   ? 0.2795 0.4118 0.3629 -0.0957 -0.0539 -0.0519 350 HOH   A O   
6808 O O   . HOH   E .   ? 0.2371 0.2078 0.2221 -0.0438 0.0129  0.0452  351 HOH   A O   
6809 O O   . HOH   E .   ? 0.2383 0.2418 0.3239 -0.0148 0.0209  -0.0306 352 HOH   A O   
6810 O O   . HOH   E .   ? 0.4997 0.2545 0.4453 -0.1457 0.2039  -0.0793 353 HOH   A O   
6811 O O   . HOH   E .   ? 0.1844 0.1770 0.1709 0.0051  0.0045  0.0135  354 HOH   A O   
6812 O O   . HOH   E .   ? 0.3516 0.3805 0.2146 -0.1114 -0.0146 -0.0779 355 HOH   A O   
6813 O O   A HOH   E .   ? 0.2594 0.4016 0.2925 0.1089  -0.0353 -0.0872 356 HOH   A O   
6814 O O   . HOH   E .   ? 0.2954 0.3540 0.4977 -0.0844 -0.1034 -0.0795 357 HOH   A O   
6815 O O   . HOH   E .   ? 0.2258 0.4877 0.3836 0.0088  -0.0438 0.1931  358 HOH   A O   
6816 O O   . HOH   E .   ? 0.3419 0.7589 0.4436 -0.0219 -0.1667 0.0287  359 HOH   A O   
6817 O O   . HOH   E .   ? 0.3722 0.4756 0.3438 0.2116  0.0651  0.0401  360 HOH   A O   
6818 O O   . HOH   E .   ? 0.3915 0.2007 0.2418 0.0993  0.0560  0.0178  361 HOH   A O   
6819 O O   . HOH   E .   ? 0.4718 0.6173 0.3780 -0.0513 0.0510  0.1414  362 HOH   A O   
6820 O O   . HOH   E .   ? 0.2475 0.1940 0.2748 -0.0025 0.0259  0.0210  363 HOH   A O   
6821 O O   . HOH   E .   ? 0.5646 0.4420 0.4387 -0.1750 -0.1042 0.2261  364 HOH   A O   
6822 O O   . HOH   E .   ? 0.2164 0.1761 0.2239 0.0193  -0.0408 0.0005  365 HOH   A O   
6823 O O   . HOH   E .   ? 0.3308 0.3405 0.3422 -0.0983 -0.0007 -0.0433 366 HOH   A O   
6824 O O   . HOH   E .   ? 0.3240 0.3952 0.3715 -0.1391 0.1153  -0.0101 367 HOH   A O   
6825 O O   . HOH   E .   ? 0.2699 0.4701 0.3320 -0.0710 0.0642  -0.0334 368 HOH   A O   
6826 O O   . HOH   E .   ? 0.2021 0.3357 0.3266 0.0638  0.0547  -0.0692 369 HOH   A O   
6827 O O   . HOH   E .   ? 0.1373 0.1345 0.1338 -0.0017 0.0050  0.0104  370 HOH   A O   
6828 O O   . HOH   E .   ? 0.2814 0.3867 0.3772 -0.0474 0.1059  0.0092  371 HOH   A O   
6829 O O   B HOH   E .   ? 0.3990 0.2994 0.4739 0.0274  0.0972  -0.0334 372 HOH   A O   
6830 O O   . HOH   E .   ? 0.2478 0.4773 0.3171 0.0711  0.0763  0.2052  373 HOH   A O   
6831 O O   . HOH   E .   ? 0.1896 0.1680 0.2113 0.0241  -0.0272 0.0192  374 HOH   A O   
6832 O O   . HOH   E .   ? 0.1484 0.1882 0.2548 0.0124  0.0032  0.0120  375 HOH   A O   
6833 O O   . HOH   E .   ? 0.1404 0.1464 0.1793 0.0020  -0.0189 0.0041  376 HOH   A O   
6834 O O   . HOH   E .   ? 0.5760 0.4295 0.5471 0.0150  0.2151  -0.1065 377 HOH   A O   
6835 O O   . HOH   E .   ? 0.2394 0.2223 0.3305 0.0007  -0.0285 0.0739  378 HOH   A O   
6836 O O   . HOH   E .   ? 0.2526 0.2071 0.1773 -0.0541 0.0208  0.0375  379 HOH   A O   
6837 O O   . HOH   E .   ? 0.1520 0.1292 0.2154 -0.0066 0.0122  -0.0085 380 HOH   A O   
6838 O O   . HOH   E .   ? 0.1497 0.1519 0.1449 -0.0021 -0.0161 -0.0012 381 HOH   A O   
6839 O O   . HOH   E .   ? 0.4089 0.2312 0.4117 -0.1087 0.0740  0.0464  382 HOH   A O   
6840 O O   . HOH   E .   ? 0.3301 0.6096 0.3481 0.0831  0.1032  -0.1152 383 HOH   A O   
6841 O O   . HOH   E .   ? 0.3712 0.2432 0.5054 -0.0690 0.0024  0.0431  384 HOH   A O   
6842 O O   A HOH   E .   ? 0.3436 0.2856 0.3887 0.0571  0.0987  0.0419  385 HOH   A O   
6843 O O   . HOH   E .   ? 0.2128 0.3833 0.3042 -0.0126 0.0141  0.0688  386 HOH   A O   
6844 O O   . HOH   E .   ? 0.2095 0.1571 0.1565 -0.0073 0.0126  0.0124  387 HOH   A O   
6845 O O   A HOH   E .   ? 0.1309 0.1520 0.1052 0.0057  -0.0105 -0.0346 388 HOH   A O   
6846 O O   B HOH   E .   ? 0.1751 0.2599 0.6022 0.0179  0.0449  0.1760  389 HOH   A O   
6847 O O   . HOH   E .   ? 0.1897 0.1882 0.2342 -0.0302 0.0114  0.0292  390 HOH   A O   
6848 O O   . HOH   E .   ? 0.5992 0.3842 0.5300 0.0014  0.1391  -0.1195 391 HOH   A O   
6849 O O   . HOH   E .   ? 0.2096 0.2218 0.2172 -0.0222 -0.0414 0.0410  392 HOH   A O   
6850 O O   . HOH   E .   ? 0.3549 0.2664 0.1977 0.0117  0.0847  0.0063  393 HOH   A O   
6851 O O   B HOH   E .   ? 0.2359 0.4295 0.4168 -0.0674 -0.0818 0.0670  394 HOH   A O   
6852 O O   . HOH   E .   ? 0.5531 0.5812 0.6305 -0.0652 0.0676  0.0529  395 HOH   A O   
6853 O O   B HOH   E .   ? 0.5267 0.4647 0.4835 0.1724  0.0139  -0.0745 396 HOH   A O   
6854 O O   . HOH   E .   ? 0.1843 0.1966 0.3605 0.0383  0.1001  0.0999  397 HOH   A O   
6855 O O   . HOH   E .   ? 0.4785 0.6222 0.4037 0.0842  -0.1154 -0.1315 398 HOH   A O   
6856 O O   . HOH   E .   ? 0.1948 0.2089 0.2059 -0.0109 -0.0229 0.0635  399 HOH   A O   
6857 O O   . HOH   E .   ? 0.3445 0.2615 0.3246 -0.0188 -0.0284 0.0977  400 HOH   A O   
6858 O O   . HOH   E .   ? 0.5467 0.5895 0.4737 -0.1514 -0.0793 0.1942  401 HOH   A O   
6859 O O   . HOH   E .   ? 0.2574 0.3861 0.2974 -0.0373 0.0957  -0.0564 402 HOH   A O   
6860 O O   . HOH   E .   ? 0.2121 0.2258 0.2616 -0.0227 -0.0286 0.0903  403 HOH   A O   
6861 O O   A HOH   E .   ? 0.1523 0.2134 0.1713 0.0359  -0.0375 -0.0457 404 HOH   A O   
6862 O O   . HOH   E .   ? 0.4534 0.4208 0.1890 -0.0359 0.0795  0.0623  405 HOH   A O   
6863 O O   A HOH   E .   ? 0.2299 0.2477 0.1957 -0.0033 0.0469  -0.0150 406 HOH   A O   
6864 O O   . HOH   E .   ? 0.6485 0.6168 0.6684 -0.0581 -0.0335 0.2275  407 HOH   A O   
6865 O O   B HOH   E .   ? 0.1575 0.1286 0.1802 -0.0066 -0.0299 0.0170  408 HOH   A O   
6866 O O   . HOH   E .   ? 0.2919 0.2627 0.2107 -0.0749 -0.0684 0.0279  409 HOH   A O   
6867 O O   A HOH   E .   ? 0.2930 0.2857 0.3287 0.0460  0.1087  0.1070  410 HOH   A O   
6868 O O   . HOH   E .   ? 0.1900 0.2625 0.3591 -0.0077 -0.0245 0.0239  411 HOH   A O   
6869 O O   A HOH   E .   ? 0.4112 0.4390 0.3447 -0.0608 0.0440  0.0038  412 HOH   A O   
6870 O O   . HOH   E .   ? 0.1792 0.1361 0.1492 -0.0192 0.0075  0.0055  413 HOH   A O   
6871 O O   A HOH   E .   ? 0.1595 0.1405 0.2339 0.0317  -0.0592 0.0209  414 HOH   A O   
6872 O O   . HOH   E .   ? 0.3690 0.6124 0.6219 0.1177  0.1026  0.0950  415 HOH   A O   
6873 O O   . HOH   E .   ? 0.5935 0.3988 0.4444 0.1452  -0.0959 0.1352  416 HOH   A O   
6874 O O   . HOH   E .   ? 0.2256 0.1773 0.3034 0.0009  -0.0402 0.0153  417 HOH   A O   
6875 O O   . HOH   E .   ? 0.3103 0.6012 0.1721 -0.0713 0.0501  0.0005  418 HOH   A O   
6876 O O   A HOH   E .   ? 0.1350 0.1181 0.1170 -0.0081 -0.0112 -0.0016 419 HOH   A O   
6877 O O   . HOH   E .   ? 0.2075 0.3030 0.2614 -0.0048 -0.0518 0.0507  420 HOH   A O   
6878 O O   B HOH   E .   ? 0.2802 0.4048 0.2053 -0.0411 0.0677  -0.0087 421 HOH   A O   
6879 O O   A HOH   E .   ? 0.3620 0.2177 0.3198 -0.0194 -0.0407 -0.0744 422 HOH   A O   
6880 O O   . HOH   E .   ? 0.1573 0.1685 0.3231 -0.0061 0.0043  0.0191  423 HOH   A O   
6881 O O   . HOH   E .   ? 0.6580 0.7518 0.7348 -0.0068 -0.0818 -0.0306 424 HOH   A O   
6882 O O   . HOH   E .   ? 0.3279 0.1341 0.1939 0.0048  -0.0418 0.0039  425 HOH   A O   
6883 O O   . HOH   E .   ? 0.1710 0.2160 0.2796 -0.0148 0.0097  0.0107  426 HOH   A O   
6884 O O   . HOH   E .   ? 0.9299 0.9143 0.6911 -0.0994 0.1294  0.0633  427 HOH   A O   
6885 O O   A HOH   E .   ? 0.1055 0.2087 0.2827 0.0054  0.0547  0.0210  428 HOH   A O   
6886 O O   . HOH   E .   ? 0.4496 0.4187 0.2501 -0.1016 0.0289  0.0613  429 HOH   A O   
6887 O O   . HOH   E .   ? 0.5254 0.6638 0.6096 0.1073  0.0624  0.0619  430 HOH   A O   
6888 O O   . HOH   E .   ? 0.2310 0.4419 0.2366 0.1672  0.0031  0.0426  431 HOH   A O   
6889 O O   . HOH   E .   ? 0.9758 0.9913 0.7761 0.0140  -0.1167 0.0114  432 HOH   A O   
6890 O O   . HOH   E .   ? 0.4500 0.5861 0.3238 -0.0922 -0.0434 0.1456  433 HOH   A O   
6891 O O   . HOH   E .   ? 0.2430 0.2100 0.4179 0.0106  -0.1099 0.0523  434 HOH   A O   
6892 O O   . HOH   E .   ? 0.6156 0.7033 0.4954 0.0710  0.3116  -0.0677 435 HOH   A O   
6893 O O   B HOH   E .   ? 0.4182 0.1832 0.2485 0.0474  -0.0424 -0.0103 436 HOH   A O   
6894 O O   . HOH   E .   ? 0.4130 0.2270 0.5376 -0.0815 -0.2352 0.1145  437 HOH   A O   
6895 O O   . HOH   E .   ? 0.3464 0.3494 0.7119 -0.0075 0.0820  -0.0470 438 HOH   A O   
6896 O O   . HOH   E .   ? 0.5175 0.3000 0.4560 0.0392  0.0029  -0.0452 439 HOH   A O   
6897 O O   A HOH   E .   ? 0.1925 0.2716 0.1925 -0.0200 -0.0337 -0.0605 440 HOH   A O   
6898 O O   . HOH   E .   ? 0.5699 0.7916 0.4441 0.1862  -0.0920 0.2323  441 HOH   A O   
6899 O O   . HOH   E .   ? 0.5855 0.5009 0.5198 -0.0447 -0.1288 -0.1252 442 HOH   A O   
6900 O O   B HOH   E .   ? 0.4216 0.4547 0.2526 0.2617  0.0053  0.0159  443 HOH   A O   
6901 O O   A HOH   E .   ? 0.3521 0.4382 0.2552 0.1296  0.0106  -0.0085 444 HOH   A O   
6902 O O   A HOH   E .   ? 0.2439 0.2065 0.2673 0.0573  0.0025  0.0254  445 HOH   A O   
6903 O O   A HOH   E .   ? 0.1472 0.1785 0.2462 0.0133  -0.0310 -0.0376 446 HOH   A O   
6904 O O   . HOH   E .   ? 0.5108 0.4785 0.4041 -0.0036 -0.1497 -0.0262 447 HOH   A O   
6905 O O   . HOH   E .   ? 0.2558 0.1661 0.2962 0.0059  -0.0124 -0.0028 448 HOH   A O   
6906 O O   . HOH   E .   ? 0.3843 0.2776 0.1757 -0.0666 0.0384  0.0655  449 HOH   A O   
6907 O O   . HOH   E .   ? 0.6844 0.6807 0.6740 0.1013  -0.1187 -0.0203 450 HOH   A O   
6908 O O   . HOH   E .   ? 0.2199 0.2654 0.2406 -0.0094 -0.0186 -0.0343 451 HOH   A O   
6909 O O   . HOH   E .   ? 0.7529 0.6370 0.7968 0.0740  -0.0842 0.2610  452 HOH   A O   
6910 O O   B HOH   E .   ? 0.2858 0.3162 0.2217 0.1198  -0.0404 -0.0743 453 HOH   A O   
6911 O O   . HOH   E .   ? 0.5843 0.3423 0.5952 0.0233  0.1750  -0.1110 454 HOH   A O   
6912 O O   A HOH   E .   ? 0.2211 0.2570 0.4185 0.0725  -0.1001 -0.1752 455 HOH   A O   
6913 O O   . HOH   E .   ? 0.4645 0.4009 0.2983 0.2518  -0.0704 -0.0355 456 HOH   A O   
6914 O O   B HOH   E .   ? 0.3332 0.3022 0.2588 -0.1033 0.0312  -0.0200 457 HOH   A O   
6915 O O   A HOH   E .   ? 0.3758 0.4008 0.3935 -0.0620 -0.0649 -0.0372 458 HOH   A O   
6916 O O   . HOH   E .   ? 0.2413 0.2101 0.2620 0.0185  0.0285  0.0309  459 HOH   A O   
6917 O O   . HOH   E .   ? 0.6624 0.6491 0.7397 -0.1335 -0.0227 -0.1264 460 HOH   A O   
6918 O O   . HOH   E .   ? 0.1908 0.2413 0.4624 -0.0245 -0.0882 0.0704  461 HOH   A O   
6919 O O   A HOH   E .   ? 0.4326 0.1955 0.2757 -0.0057 0.0406  0.0745  462 HOH   A O   
6920 O O   B HOH   E .   ? 0.2034 0.2170 0.2592 0.0162  -0.0468 -0.0059 463 HOH   A O   
6921 O O   . HOH   E .   ? 0.4981 0.3727 0.4101 0.0583  0.0477  0.0703  464 HOH   A O   
6922 O O   . HOH   E .   ? 0.5630 0.5755 0.5183 -0.0881 0.1242  0.0436  465 HOH   A O   
6923 O O   . HOH   E .   ? 0.4667 0.4623 0.4976 0.0398  -0.0296 0.1109  466 HOH   A O   
6924 O O   . HOH   E .   ? 0.4615 0.4830 0.4365 0.1873  -0.1109 0.1314  467 HOH   A O   
6925 O O   . HOH   E .   ? 0.4605 0.3652 0.4493 0.0446  -0.0039 0.0375  468 HOH   A O   
6926 O O   . HOH   E .   ? 0.2747 0.2688 0.4065 -0.0532 0.0526  -0.0988 469 HOH   A O   
6927 O O   . HOH   E .   ? 0.7098 0.6808 0.4638 0.1408  -0.0602 -0.0695 470 HOH   A O   
6928 O O   B HOH   E .   ? 0.5063 0.2255 0.2625 0.0862  0.0215  -0.0253 471 HOH   A O   
6929 O O   . HOH   E .   ? 0.6396 0.3429 0.7416 0.1683  0.0654  0.1882  472 HOH   A O   
6930 O O   . HOH   E .   ? 0.3397 0.4399 0.5447 -0.1152 0.0795  -0.1733 473 HOH   A O   
6931 O O   . HOH   E .   ? 0.4159 0.4615 0.4590 0.0161  -0.0717 0.0867  474 HOH   A O   
6932 O O   . HOH   E .   ? 0.2770 0.3068 0.4189 -0.1152 0.0737  -0.0490 475 HOH   A O   
6933 O O   . HOH   E .   ? 0.3744 0.4527 0.4616 -0.0995 0.0183  -0.0266 476 HOH   A O   
6934 O O   . HOH   E .   ? 0.2682 0.4389 0.5084 0.0683  0.0043  -0.1893 477 HOH   A O   
6935 O O   . HOH   E .   ? 0.5758 0.7441 0.6306 0.0818  0.2177  0.1329  478 HOH   A O   
6936 O O   . HOH   E .   ? 0.4228 0.5564 0.3797 -0.0946 -0.1226 0.2021  479 HOH   A O   
6937 O O   . HOH   E .   ? 0.4246 0.5004 0.4019 0.0403  -0.0706 -0.0768 480 HOH   A O   
6938 O O   . HOH   E .   ? 0.2571 0.1734 0.2696 0.0270  -0.0822 -0.0315 481 HOH   A O   
6939 O O   . HOH   E .   ? 0.4245 0.4093 0.4065 0.1582  0.1506  0.0903  482 HOH   A O   
6940 O O   . HOH   E .   ? 0.4863 0.4820 0.4707 0.0197  0.1162  0.0298  483 HOH   A O   
6941 O O   . HOH   E .   ? 0.5541 0.5614 0.5125 -0.0119 0.0043  -0.0780 484 HOH   A O   
6942 O O   A HOH   E .   ? 0.2536 0.2386 0.3606 0.0764  -0.0833 -0.0143 485 HOH   A O   
6943 O O   . HOH   E .   ? 0.2467 0.2331 0.2609 0.0220  -0.0143 0.0205  486 HOH   A O   
6944 O O   . HOH   E .   ? 0.5079 0.4540 0.3515 0.0046  -0.0811 -0.0218 487 HOH   A O   
6945 O O   . HOH   E .   ? 0.4636 0.4546 0.5372 -0.2198 -0.0737 -0.0090 488 HOH   A O   
6946 O O   . HOH   E .   ? 0.5613 0.5624 0.5694 -0.1582 -0.1055 0.1020  489 HOH   A O   
6947 O O   . HOH   E .   ? 0.4005 0.5448 0.2937 0.0321  -0.0150 -0.0122 490 HOH   A O   
6948 O O   . HOH   E .   ? 0.5156 0.3430 0.3536 -0.1291 -0.1086 0.0896  491 HOH   A O   
6949 O O   . HOH   E .   ? 0.6267 0.4320 0.5245 -0.0321 -0.0454 -0.1230 492 HOH   A O   
6950 O O   . HOH   E .   ? 0.6615 0.4560 0.5424 -0.1004 -0.0866 -0.0757 493 HOH   A O   
6951 O O   . HOH   E .   ? 0.7700 0.6182 0.6724 -0.1109 0.0699  -0.0853 494 HOH   A O   
6952 O O   . HOH   E .   ? 0.6371 0.7596 0.6465 0.1463  -0.1355 0.1510  495 HOH   A O   
6953 O O   . HOH   E .   ? 0.7933 0.3696 0.3061 -0.0461 -0.1392 0.0506  496 HOH   A O   
6954 O O   . HOH   E .   ? 0.5287 0.6642 0.7115 0.1214  0.1938  -0.1201 497 HOH   A O   
6955 O O   . HOH   E .   ? 0.5289 0.3518 0.2442 -0.0905 0.1333  -0.0416 498 HOH   A O   
6956 O O   B HOH   E .   ? 0.3721 0.2486 0.3944 -0.0508 -0.1311 0.0815  499 HOH   A O   
6957 O O   . HOH   E .   ? 0.6342 0.4019 0.3370 -0.0037 0.0974  -0.0165 500 HOH   A O   
6958 O O   . HOH   E .   ? 0.2902 0.5037 0.3824 0.1246  0.1255  0.2342  501 HOH   A O   
6959 O O   . HOH   E .   ? 0.2931 0.3602 0.4519 -0.0430 0.1001  0.0670  502 HOH   A O   
6960 O O   . HOH   E .   ? 0.2595 0.2383 0.7749 -0.0061 -0.1386 0.0466  503 HOH   A O   
6961 O O   . HOH   E .   ? 0.3919 0.3269 0.4302 -0.0906 0.0039  0.1159  504 HOH   A O   
6962 O O   . HOH   E .   ? 0.7306 0.7290 0.5187 -0.0683 0.1209  0.1596  505 HOH   A O   
6963 O O   . HOH   E .   ? 0.5684 0.4969 0.5965 0.0066  -0.1260 0.0547  506 HOH   A O   
6964 O O   . HOH   E .   ? 0.5109 0.3262 0.4279 0.0099  0.2296  0.0391  507 HOH   A O   
6965 O O   . HOH   E .   ? 0.2860 0.3303 0.5105 0.0226  0.1295  -0.0132 508 HOH   A O   
6966 O O   B HOH   E .   ? 0.1871 0.2653 0.3124 0.0291  -0.0903 0.0229  509 HOH   A O   
6967 O O   . HOH   E .   ? 0.6331 0.2701 0.3683 -0.0453 0.0748  0.0560  510 HOH   A O   
6968 O O   . HOH   E .   ? 0.2763 0.2272 0.6114 0.0091  0.0098  0.1160  511 HOH   A O   
6969 O O   . HOH   E .   ? 0.2562 0.3314 0.3202 0.0736  -0.0394 0.0431  512 HOH   A O   
6970 O O   . HOH   E .   ? 0.4786 0.2582 0.4260 -0.1339 0.0008  0.0344  513 HOH   A O   
6971 O O   B HOH   E .   ? 0.3070 0.3807 0.2986 -0.0261 -0.0381 0.1249  514 HOH   A O   
6972 O O   . HOH   E .   ? 0.4249 0.8039 0.4722 -0.0940 -0.0296 0.2826  515 HOH   A O   
6973 O O   . HOH   E .   ? 0.8242 0.6208 0.6038 -0.0347 0.0018  -0.0092 516 HOH   A O   
6974 O O   . HOH   E .   ? 0.3038 0.4226 0.4480 0.0636  0.0123  0.0414  517 HOH   A O   
6975 O O   . HOH   E .   ? 0.5544 0.8240 0.5954 0.1444  -0.0763 0.0810  518 HOH   A O   
6976 O O   . HOH   E .   ? 0.3297 0.5380 0.3150 -0.0253 -0.0313 -0.0969 519 HOH   A O   
6977 O O   B HOH   E .   ? 0.4559 0.6147 0.5218 0.1333  0.1229  0.0300  520 HOH   A O   
6978 O O   . HOH   E .   ? 0.2771 0.2274 0.5032 0.0170  0.0368  0.0600  521 HOH   A O   
6979 O O   . HOH   E .   ? 0.5515 0.6759 0.4864 0.2970  -0.0819 0.0559  522 HOH   A O   
6980 O O   B HOH   E .   ? 0.3233 0.3656 0.4377 0.0579  0.0411  0.0913  523 HOH   A O   
6981 O O   B HOH   E .   ? 0.2860 0.3139 0.3490 0.0799  -0.1320 0.0678  524 HOH   A O   
6982 O O   . HOH   E .   ? 0.5719 0.5971 0.4996 -0.0738 -0.0789 -0.1382 525 HOH   A O   
6983 O O   A HOH   E .   ? 0.3025 0.4510 0.1985 0.0835  0.0552  -0.0379 526 HOH   A O   
6984 O O   . HOH   E .   ? 0.3821 0.6844 0.5115 0.0269  0.0819  -0.0905 527 HOH   A O   
6985 O O   . HOH   E .   ? 0.5489 0.6919 0.5948 -0.0392 -0.0751 0.0525  528 HOH   A O   
6986 O O   . HOH   E .   ? 0.5095 0.5134 0.4407 0.0970  0.0703  0.1482  529 HOH   A O   
6987 O O   . HOH   E .   ? 0.4179 0.4666 0.5626 -0.0070 -0.1220 0.2698  530 HOH   A O   
6988 O O   . HOH   F .   ? 0.2335 0.2167 0.3142 0.0202  0.0816  0.0395  201 HOH   B O   
6989 O O   . HOH   F .   ? 0.3503 0.3980 0.4920 -0.0797 0.0641  -0.1251 202 HOH   B O   
6990 O O   . HOH   F .   ? 0.4930 0.3451 0.4152 -0.0137 -0.0226 -0.1597 203 HOH   B O   
6991 O O   . HOH   F .   ? 0.3062 0.4151 0.6755 -0.0327 0.0104  -0.1012 204 HOH   B O   
6992 O O   . HOH   F .   ? 0.5106 0.6397 0.2845 0.1362  -0.0198 -0.1340 205 HOH   B O   
6993 O O   . HOH   F .   ? 0.7348 0.2938 0.4424 0.0442  0.1128  0.0265  206 HOH   B O   
6994 O O   . HOH   F .   ? 0.3056 0.2024 0.5364 0.0363  0.1938  0.0992  207 HOH   B O   
6995 O O   . HOH   F .   ? 0.2779 0.5556 0.4931 -0.0229 0.1527  -0.1818 208 HOH   B O   
6996 O O   . HOH   F .   ? 0.6437 0.2965 0.4094 -0.1936 0.0803  0.0248  209 HOH   B O   
6997 O O   . HOH   F .   ? 0.2112 0.2545 0.2592 0.0190  0.0034  -0.0349 210 HOH   B O   
6998 O O   . HOH   F .   ? 0.3028 0.6806 0.3682 0.0797  0.0260  0.2668  211 HOH   B O   
6999 O O   . HOH   F .   ? 0.4137 0.4505 0.3571 -0.0140 -0.1275 0.1203  212 HOH   B O   
7000 O O   . HOH   F .   ? 0.4625 0.6005 0.3447 0.2877  -0.1016 -0.0430 213 HOH   B O   
7001 O O   . HOH   F .   ? 0.1584 0.1879 0.2722 -0.0110 -0.0125 0.0154  214 HOH   B O   
7002 O O   . HOH   F .   ? 0.4996 0.4202 0.5755 0.0283  -0.1099 0.2624  215 HOH   B O   
7003 O O   . HOH   F .   ? 0.3495 0.5125 0.5035 0.2224  0.0268  -0.0413 216 HOH   B O   
7004 O O   . HOH   F .   ? 0.4137 0.6122 0.4224 0.2655  -0.0359 0.0086  217 HOH   B O   
7005 O O   . HOH   F .   ? 0.2834 0.2902 0.6681 0.0769  -0.1010 0.0531  218 HOH   B O   
7006 O O   . HOH   F .   ? 0.2406 0.2126 0.4015 -0.0474 -0.0114 -0.0591 219 HOH   B O   
7007 O O   . HOH   F .   ? 0.7180 0.6701 0.5951 0.1690  0.0031  0.0528  220 HOH   B O   
7008 O O   . HOH   F .   ? 0.4227 0.5658 0.6405 0.0199  -0.1482 -0.1242 221 HOH   B O   
7009 O O   . HOH   F .   ? 0.4762 0.4112 0.4076 0.0248  0.0854  -0.1826 222 HOH   B O   
7010 O O   . HOH   F .   ? 0.4858 0.2061 0.2758 -0.0105 -0.0773 0.0107  223 HOH   B O   
7011 O O   . HOH   F .   ? 0.3006 0.3612 0.6117 0.0408  0.0746  0.1198  224 HOH   B O   
7012 O O   . HOH   F .   ? 0.4836 0.5947 0.3577 0.2403  0.0207  0.0276  225 HOH   B O   
7013 O O   . HOH   F .   ? 0.3058 0.2076 0.5407 -0.0029 0.1744  0.0332  226 HOH   B O   
7014 O O   . HOH   F .   ? 0.5231 0.4218 0.2351 -0.0214 0.0305  -0.0078 227 HOH   B O   
7015 O O   . HOH   F .   ? 0.1650 0.2011 0.3079 -0.0168 0.0010  -0.0098 228 HOH   B O   
7016 O O   . HOH   F .   ? 0.5058 0.6508 0.2685 -0.0544 -0.1053 0.0392  229 HOH   B O   
7017 O O   . HOH   F .   ? 0.2353 0.1778 0.2733 -0.0260 0.1048  -0.0068 230 HOH   B O   
7018 O O   . HOH   F .   ? 0.3950 0.3405 0.2153 0.0508  0.0861  0.0438  231 HOH   B O   
7019 O O   . HOH   F .   ? 0.5122 0.3040 0.3928 -0.2213 -0.0057 0.0106  232 HOH   B O   
7020 O O   . HOH   F .   ? 0.2648 0.4045 0.3000 -0.0694 0.0534  -0.1154 233 HOH   B O   
7021 O O   . HOH   F .   ? 0.3744 0.3001 0.4062 0.0937  -0.0922 -0.0337 234 HOH   B O   
7022 O O   . HOH   F .   ? 0.3754 0.1716 0.2007 0.0215  -0.0847 -0.0118 235 HOH   B O   
7023 O O   . HOH   F .   ? 0.1494 0.1441 0.1529 -0.0078 -0.0113 -0.0025 236 HOH   B O   
7024 O O   . HOH   F .   ? 0.3655 0.3267 0.3978 0.0621  -0.1011 -0.1757 237 HOH   B O   
7025 O O   . HOH   F .   ? 0.2100 0.2267 0.3012 -0.0478 -0.0021 -0.0260 238 HOH   B O   
7026 O O   . HOH   F .   ? 0.6227 0.5482 0.3056 0.0854  0.0084  0.0230  239 HOH   B O   
7027 O O   . HOH   F .   ? 0.2150 0.3832 0.2454 -0.0541 -0.0090 0.0464  240 HOH   B O   
7028 O O   . HOH   F .   ? 0.2208 0.3862 0.2971 -0.0545 -0.0658 -0.0363 241 HOH   B O   
7029 O O   . HOH   F .   ? 0.2516 0.2527 0.3182 0.0216  0.0283  -0.0848 242 HOH   B O   
7030 O O   . HOH   F .   ? 0.2315 0.2207 0.2537 0.0729  -0.0782 -0.0672 243 HOH   B O   
7031 O O   . HOH   F .   ? 0.3991 0.3885 0.5327 -0.1452 -0.0131 0.1070  244 HOH   B O   
7032 O O   . HOH   F .   ? 0.2208 0.2019 0.2030 -0.0367 -0.0494 0.0102  245 HOH   B O   
7033 O O   . HOH   F .   ? 0.3177 0.2586 0.3329 -0.0347 0.0076  -0.0773 246 HOH   B O   
7034 O O   . HOH   F .   ? 0.1646 0.1533 0.2476 -0.0007 0.0100  -0.0116 247 HOH   B O   
7035 O O   . HOH   F .   ? 0.2508 0.2155 0.1925 0.0083  -0.0143 0.0094  248 HOH   B O   
7036 O O   . HOH   F .   ? 0.2169 0.1350 0.3707 0.0072  -0.0726 -0.0187 249 HOH   B O   
7037 O O   . HOH   F .   ? 0.1491 0.1318 0.1579 -0.0003 -0.0015 0.0055  250 HOH   B O   
7038 O O   . HOH   F .   ? 0.3946 0.2591 0.3827 0.0837  -0.0251 -0.0576 251 HOH   B O   
7039 O O   . HOH   F .   ? 0.3127 0.1730 0.5800 -0.0291 -0.1463 -0.0133 252 HOH   B O   
7040 O O   . HOH   F .   ? 0.2810 0.2273 0.2926 0.0823  0.0833  0.0150  253 HOH   B O   
7041 O O   . HOH   F .   ? 0.7161 0.5650 0.5332 0.1524  -0.0469 -0.0348 254 HOH   B O   
7042 O O   . HOH   F .   ? 0.3084 0.4863 0.3516 -0.0082 -0.1080 0.0973  255 HOH   B O   
7043 O O   . HOH   F .   ? 0.3392 0.3898 0.2027 0.0385  0.0728  0.0086  256 HOH   B O   
7044 O O   . HOH   F .   ? 0.2306 0.5130 0.5282 0.1312  -0.0445 -0.0919 257 HOH   B O   
7045 O O   . HOH   F .   ? 0.2429 0.3359 0.2259 -0.0652 0.0187  0.0509  258 HOH   B O   
7046 O O   . HOH   F .   ? 0.1394 0.1664 0.2052 -0.0045 0.0100  0.0131  259 HOH   B O   
7047 O O   . HOH   F .   ? 0.2773 0.3919 0.3184 -0.0863 -0.0500 -0.0490 260 HOH   B O   
7048 O O   . HOH   F .   ? 0.2118 0.3950 0.4694 -0.0427 -0.0200 -0.1479 261 HOH   B O   
7049 O O   . HOH   F .   ? 0.2082 0.1879 0.3416 0.0002  -0.0437 -0.0315 262 HOH   B O   
7050 O O   . HOH   F .   ? 0.2479 0.4305 0.3520 0.0251  0.1003  -0.0192 263 HOH   B O   
7051 O O   . HOH   F .   ? 0.2630 0.4602 0.5414 0.0159  0.0594  -0.0748 264 HOH   B O   
7052 O O   . HOH   F .   ? 0.1650 0.1716 0.2839 -0.0252 -0.0230 0.0006  265 HOH   B O   
7053 O O   . HOH   F .   ? 0.1796 0.2793 0.2564 0.0503  0.0497  0.0898  266 HOH   B O   
7054 O O   . HOH   F .   ? 0.1900 0.1833 0.1662 -0.0497 -0.0449 0.0083  267 HOH   B O   
7055 O O   . HOH   F .   ? 0.4192 0.3602 0.3790 -0.1065 0.0869  -0.1006 268 HOH   B O   
7056 O O   . HOH   F .   ? 0.2134 0.1576 0.1985 -0.0336 -0.0393 0.0261  269 HOH   B O   
7057 O O   . HOH   F .   ? 0.2668 0.1991 0.2981 -0.0700 0.0207  -0.0234 270 HOH   B O   
7058 O O   . HOH   F .   ? 0.3174 0.3871 0.5068 -0.0543 0.0321  -0.0622 271 HOH   B O   
7059 O O   . HOH   F .   ? 0.4404 0.3211 0.2731 0.0733  -0.0196 -0.0628 272 HOH   B O   
7060 O O   . HOH   F .   ? 0.2537 0.3024 0.2365 -0.0404 -0.0789 0.0187  273 HOH   B O   
7061 O O   . HOH   F .   ? 0.2329 0.2293 0.1880 0.0168  -0.0148 0.0017  274 HOH   B O   
7062 O O   . HOH   F .   ? 0.1732 0.1436 0.3784 -0.0067 -0.0307 -0.0169 275 HOH   B O   
7063 O O   . HOH   F .   ? 0.2415 0.2569 0.2363 -0.0407 -0.0694 -0.0307 276 HOH   B O   
7064 O O   . HOH   F .   ? 0.2020 0.1505 0.2241 -0.0249 -0.0141 0.0198  277 HOH   B O   
7065 O O   . HOH   F .   ? 0.2758 0.2153 0.5046 0.0146  0.0562  0.0633  278 HOH   B O   
7066 O O   . HOH   F .   ? 0.3985 0.6900 0.4128 0.1743  -0.0623 0.1700  279 HOH   B O   
7067 O O   . HOH   F .   ? 0.1638 0.1520 0.3400 -0.0143 0.0009  -0.0090 280 HOH   B O   
7068 O O   . HOH   F .   ? 0.3503 0.3130 0.1977 0.0493  -0.0814 -0.0171 281 HOH   B O   
7069 O O   . HOH   F .   ? 0.2520 0.3428 0.2323 0.1243  -0.0267 -0.0340 282 HOH   B O   
7070 O O   . HOH   F .   ? 0.2539 0.6869 0.2526 0.0658  -0.0551 -0.0710 283 HOH   B O   
7071 O O   . HOH   F .   ? 0.1672 0.1578 0.1789 -0.0008 0.0063  0.0044  284 HOH   B O   
7072 O O   . HOH   F .   ? 0.2424 0.2704 0.2806 0.0083  -0.0799 0.0104  285 HOH   B O   
7073 O O   . HOH   F .   ? 0.4390 0.4865 0.2211 0.1462  -0.0697 -0.0148 286 HOH   B O   
7074 O O   . HOH   F .   ? 0.3414 0.3870 0.4570 0.1387  -0.0621 -0.0692 287 HOH   B O   
7075 O O   . HOH   F .   ? 0.2864 0.6688 0.7263 0.1416  -0.0789 -0.0723 288 HOH   B O   
7076 O O   . HOH   F .   ? 0.1717 0.1984 0.2995 0.0211  -0.0135 0.0143  289 HOH   B O   
7077 O O   . HOH   F .   ? 0.2073 0.4151 0.3107 -0.0226 0.0311  -0.1537 290 HOH   B O   
7078 O O   . HOH   F .   ? 0.4073 0.4204 0.3830 0.0095  -0.1171 -0.0244 291 HOH   B O   
7079 O O   . HOH   F .   ? 0.5692 0.3862 0.3135 0.2626  0.0987  0.0852  292 HOH   B O   
7080 O O   . HOH   F .   ? 0.2862 0.4876 0.4564 -0.1127 -0.1340 0.0872  293 HOH   B O   
7081 O O   . HOH   F .   ? 0.1655 0.2076 0.1453 -0.0129 -0.0175 0.0025  294 HOH   B O   
7082 O O   . HOH   F .   ? 0.3118 0.2875 0.2757 -0.0296 0.0249  -0.1205 295 HOH   B O   
7083 O O   . HOH   F .   ? 0.3695 0.2261 0.4011 -0.1004 -0.2025 0.0994  296 HOH   B O   
7084 O O   . HOH   F .   ? 0.1776 0.3796 0.4488 0.0403  -0.0055 -0.1398 297 HOH   B O   
7085 O O   . HOH   F .   ? 0.4815 0.2921 0.4525 -0.0776 0.0770  0.0958  298 HOH   B O   
7086 O O   . HOH   F .   ? 0.1756 0.1664 0.2104 0.0053  0.0026  0.0125  299 HOH   B O   
7087 O O   . HOH   F .   ? 0.4096 0.4656 0.2107 -0.0011 0.0340  0.0626  300 HOH   B O   
7088 O O   . HOH   F .   ? 0.2082 0.1602 0.3141 0.0271  -0.0843 -0.0004 301 HOH   B O   
7089 O O   . HOH   F .   ? 0.3566 0.1933 0.3754 0.0830  0.1315  0.0656  302 HOH   B O   
7090 O O   . HOH   F .   ? 0.2144 0.1661 0.2783 -0.0220 -0.0365 0.0007  303 HOH   B O   
7091 O O   . HOH   F .   ? 0.4706 0.3891 0.2572 0.1153  -0.0900 0.0582  304 HOH   B O   
7092 O O   . HOH   F .   ? 0.4141 0.5304 0.4896 0.0486  -0.1465 0.0004  305 HOH   B O   
7093 O O   . HOH   F .   ? 0.2283 0.3177 0.5605 -0.0064 -0.0687 -0.0372 306 HOH   B O   
7094 O O   . HOH   F .   ? 0.1994 0.2640 0.6547 0.0375  -0.0409 -0.0853 307 HOH   B O   
7095 O O   . HOH   F .   ? 0.1587 0.1517 0.3080 0.0139  -0.0005 -0.0014 308 HOH   B O   
7096 O O   . HOH   F .   ? 0.5351 0.3085 0.2380 -0.1785 0.0941  -0.0226 309 HOH   B O   
7097 O O   . HOH   F .   ? 0.6192 0.6470 0.5086 0.2651  0.0046  -0.0019 310 HOH   B O   
7098 O O   . HOH   F .   ? 0.4366 0.2419 0.2614 0.1657  0.1094  0.0441  311 HOH   B O   
7099 O O   . HOH   F .   ? 0.3241 0.3939 0.4256 -0.1490 0.1337  -0.0820 312 HOH   B O   
7100 O O   . HOH   F .   ? 0.1489 0.1852 0.3015 -0.0257 -0.0119 0.0010  313 HOH   B O   
7101 O O   . HOH   F .   ? 0.2634 0.3035 0.3659 -0.0416 0.0946  -0.0997 314 HOH   B O   
7102 O O   . HOH   F .   ? 0.3018 0.2840 0.5313 -0.0376 -0.1010 0.1169  315 HOH   B O   
7103 O O   . HOH   F .   ? 0.2175 0.1992 0.1784 -0.0039 0.0237  0.0123  316 HOH   B O   
7104 O O   . HOH   F .   ? 0.2409 0.1535 0.2483 -0.0225 -0.0149 0.0386  317 HOH   B O   
7105 O O   . HOH   F .   ? 0.4248 0.3201 0.4800 0.0924  0.1795  0.1598  318 HOH   B O   
7106 O O   . HOH   F .   ? 0.1553 0.1691 0.3034 -0.0090 -0.0219 -0.0145 319 HOH   B O   
7107 O O   . HOH   F .   ? 0.1760 0.2901 0.2417 -0.0174 -0.0210 0.0761  320 HOH   B O   
7108 O O   . HOH   F .   ? 0.2175 0.6099 0.4770 -0.0698 -0.0066 -0.0476 321 HOH   B O   
7109 O O   . HOH   F .   ? 0.5061 0.4652 0.2531 0.0449  -0.0638 -0.0971 322 HOH   B O   
7110 O O   . HOH   F .   ? 0.3597 0.4097 0.6630 0.0010  -0.0890 0.1448  323 HOH   B O   
7111 O O   . HOH   F .   ? 0.2728 0.3178 0.5142 -0.0788 -0.1723 0.1600  324 HOH   B O   
7112 O O   . HOH   F .   ? 0.1834 0.3021 0.3247 0.0426  -0.0157 -0.0887 325 HOH   B O   
7113 O O   . HOH   F .   ? 0.5693 0.4384 0.5241 0.1388  0.1434  -0.0128 326 HOH   B O   
7114 O O   . HOH   F .   ? 0.1927 0.1968 0.2874 0.0368  0.0472  0.0234  327 HOH   B O   
7115 O O   . HOH   F .   ? 0.6055 0.5824 0.5372 -0.1116 -0.0101 0.1685  328 HOH   B O   
7116 O O   . HOH   F .   ? 0.2924 0.2305 0.2250 0.0307  -0.0244 0.0229  329 HOH   B O   
7117 O O   . HOH   F .   ? 0.4164 0.3871 0.5740 0.0576  -0.0341 0.0690  330 HOH   B O   
7118 O O   . HOH   F .   ? 0.4477 0.2546 0.2982 0.0268  0.0563  0.0915  331 HOH   B O   
7119 O O   . HOH   F .   ? 0.7755 0.2100 0.3551 0.0511  -0.1148 0.0033  332 HOH   B O   
7120 O O   . HOH   F .   ? 0.5236 0.4671 0.6877 0.1160  -0.0469 0.1961  333 HOH   B O   
7121 O O   . HOH   F .   ? 0.2626 0.2064 0.5058 -0.0088 0.0176  0.0287  334 HOH   B O   
7122 O O   . HOH   F .   ? 0.5534 0.3727 0.4272 0.0521  0.1787  0.1653  335 HOH   B O   
7123 O O   . HOH   F .   ? 0.1734 0.1452 0.2269 0.0086  -0.0226 0.0136  336 HOH   B O   
7124 O O   . HOH   F .   ? 0.2232 0.2393 0.5509 -0.0551 -0.0083 0.1401  337 HOH   B O   
7125 O O   . HOH   F .   ? 0.4425 0.7040 0.4144 -0.0292 -0.0690 0.2001  338 HOH   B O   
7126 O O   . HOH   F .   ? 0.5201 0.3828 0.5131 -0.0326 -0.0532 -0.1070 339 HOH   B O   
7127 O O   . HOH   F .   ? 0.5737 0.3716 0.4307 0.0085  0.1205  -0.1679 340 HOH   B O   
7128 O O   . HOH   F .   ? 0.7150 0.6090 0.2951 -0.0492 -0.0579 0.1220  341 HOH   B O   
7129 O O   . HOH   F .   ? 0.4857 0.6343 0.3445 0.0027  -0.1045 0.0344  342 HOH   B O   
7130 O O   . HOH   F .   ? 0.4999 0.3636 0.3118 0.0525  -0.1234 -0.0610 343 HOH   B O   
7131 O O   . HOH   F .   ? 0.2820 0.5797 0.6957 0.0031  0.1133  0.0886  344 HOH   B O   
7132 O O   . HOH   F .   ? 0.2125 0.2016 0.3185 -0.0074 0.0610  -0.0025 345 HOH   B O   
7133 O O   . HOH   F .   ? 0.3986 0.5790 0.4383 -0.0929 -0.1272 -0.0893 346 HOH   B O   
7134 O O   . HOH   F .   ? 0.5314 0.5443 0.5007 -0.1367 0.0747  0.0354  347 HOH   B O   
7135 O O   . HOH   F .   ? 0.4039 0.4790 0.5914 0.0181  -0.1148 0.1192  348 HOH   B O   
7136 O O   . HOH   F .   ? 0.3046 0.1995 0.3902 0.0299  -0.1124 -0.0554 349 HOH   B O   
7137 O O   . HOH   F .   ? 0.2249 0.4010 0.4814 0.0506  0.0355  0.0388  350 HOH   B O   
7138 O O   . HOH   F .   ? 0.2858 0.2418 0.4683 -0.0381 -0.0784 -0.0497 351 HOH   B O   
7139 O O   . HOH   F .   ? 0.4338 0.5607 0.6709 -0.0180 -0.0430 -0.0599 352 HOH   B O   
7140 O O   . HOH   F .   ? 0.2281 0.6022 0.4319 0.1389  -0.0528 -0.1441 353 HOH   B O   
7141 O O   . HOH   F .   ? 0.4243 0.2141 0.3263 -0.0775 0.0431  -0.0908 354 HOH   B O   
7142 O O   . HOH   F .   ? 0.5030 0.3560 0.5340 -0.1318 0.1264  0.0722  355 HOH   B O   
7143 O O   . HOH   F .   ? 0.3615 0.3970 0.5172 -0.1410 0.0522  -0.0332 356 HOH   B O   
7144 O O   . HOH   F .   ? 0.5710 0.3725 0.4378 0.0791  0.1798  -0.0344 357 HOH   B O   
7145 O O   . HOH   F .   ? 0.3597 0.2746 0.4044 -0.0930 0.0011  -0.0367 358 HOH   B O   
7146 O O   . HOH   F .   ? 0.5839 0.4885 0.5333 -0.0630 -0.0009 0.0094  359 HOH   B O   
7147 O O   . HOH   F .   ? 0.4738 0.5512 0.4620 0.1947  -0.1263 0.1349  360 HOH   B O   
7148 O O   . HOH   F .   ? 0.4908 0.3005 0.5016 -0.0005 -0.1619 0.0036  361 HOH   B O   
7149 O O   . HOH   F .   ? 0.4704 0.4041 0.6274 0.0397  0.1038  0.1383  362 HOH   B O   
7150 O O   . HOH   F .   ? 0.4630 0.6493 0.3830 0.2166  -0.0411 0.0301  363 HOH   B O   
7151 O O   . HOH   F .   ? 0.2171 0.3794 0.6509 -0.0804 -0.0521 -0.0877 364 HOH   B O   
7152 O O   . HOH   F .   ? 0.5254 0.5252 0.3500 0.0758  -0.1759 0.0799  365 HOH   B O   
7153 O O   . HOH   F .   ? 0.6134 0.4719 0.4196 0.1285  0.0668  0.0659  366 HOH   B O   
7154 O O   . HOH   F .   ? 0.5495 0.6064 0.4691 -0.0993 -0.0792 -0.1109 367 HOH   B O   
7155 O O   . HOH   F .   ? 0.4637 0.4237 0.5346 0.1454  -0.1318 0.0521  368 HOH   B O   
7156 O O   . HOH   F .   ? 0.7758 0.7844 0.5517 0.2853  -0.1253 0.1490  369 HOH   B O   
7157 O O   . HOH   F .   ? 0.4528 0.3375 0.5260 -0.1330 -0.0847 0.0385  370 HOH   B O   
7158 O O   . HOH   F .   ? 0.5841 0.2393 0.3655 0.0036  -0.0265 0.0718  371 HOH   B O   
7159 O O   . HOH   F .   ? 0.4852 0.3363 0.4003 0.0743  -0.1521 -0.0731 372 HOH   B O   
7160 O O   . HOH   F .   ? 0.4264 0.6066 0.5076 0.2666  0.0955  0.0820  373 HOH   B O   
7161 O O   . HOH   F .   ? 0.4390 0.4939 0.4662 -0.0469 -0.0571 0.0116  374 HOH   B O   
7162 O O   . HOH   F .   ? 0.5678 0.4163 0.3024 -0.0840 -0.0920 -0.0576 375 HOH   B O   
7163 O O   . HOH   F .   ? 0.2397 0.4679 0.3728 0.0342  -0.0416 -0.0748 376 HOH   B O   
7164 O O   . HOH   F .   ? 0.7335 0.4094 0.6006 -0.1129 -0.0501 -0.0820 377 HOH   B O   
7165 O O   . HOH   F .   ? 0.5321 0.6766 0.6787 0.1405  -0.0301 0.3012  378 HOH   B O   
7166 O O   . HOH   F .   ? 0.3408 0.4509 0.2204 0.1119  0.0511  0.0256  379 HOH   B O   
7167 O O   . HOH   F .   ? 0.5482 0.6846 0.4142 -0.1442 -0.0005 -0.1510 380 HOH   B O   
7168 O O   . HOH   F .   ? 0.3046 0.2519 0.3025 -0.0010 0.0357  0.0227  381 HOH   B O   
7169 O O   . HOH   F .   ? 0.3870 0.4552 0.4819 0.0688  -0.0319 0.0037  382 HOH   B O   
7170 O O   . HOH   F .   ? 0.5752 0.6240 0.5901 0.0070  0.1954  0.1502  383 HOH   B O   
7171 O O   . HOH   F .   ? 0.7218 0.3713 0.4539 0.0826  0.0705  -0.0600 384 HOH   B O   
7172 O O   . HOH   F .   ? 0.4279 0.7936 0.5894 -0.0041 0.2123  0.1028  385 HOH   B O   
7173 O O   . HOH   F .   ? 0.2349 0.4270 0.3770 -0.0638 -0.0761 -0.0478 386 HOH   B O   
7174 O O   . HOH   F .   ? 0.7406 0.6366 0.5189 0.1763  0.0222  0.0305  387 HOH   B O   
7175 O O   . HOH   F .   ? 0.5642 0.4097 0.5300 -0.0737 0.0233  0.0383  388 HOH   B O   
7176 O O   . HOH   F .   ? 0.4528 0.4008 0.3202 0.0028  0.0742  -0.0106 389 HOH   B O   
7177 O O   . HOH   F .   ? 0.5373 0.5330 0.4443 0.0530  -0.1108 -0.0218 390 HOH   B O   
7178 O O   . HOH   F .   ? 0.4814 0.4065 0.4052 -0.0031 0.0365  0.0365  391 HOH   B O   
7179 O O   . HOH   F .   ? 0.3939 0.2537 0.3370 0.0925  -0.0450 0.0004  392 HOH   B O   
7180 O O   . HOH   F .   ? 0.4038 0.2187 0.5293 -0.0317 0.0670  0.0534  393 HOH   B O   
7181 O O   . HOH   F .   ? 0.2464 0.3887 0.6882 -0.1002 -0.0774 0.0274  394 HOH   B O   
7182 O O   . HOH   F .   ? 0.4416 0.4518 0.3874 0.0432  0.0966  0.0859  395 HOH   B O   
7183 O O   . HOH   F .   ? 0.4329 0.5870 0.3430 0.0986  -0.0330 -0.0993 396 HOH   B O   
7184 O O   . HOH   F .   ? 0.1969 0.2707 0.5193 -0.0424 -0.0861 -0.0215 397 HOH   B O   
7185 O O   . HOH   F .   ? 0.3412 0.3578 0.3732 0.0244  0.0225  -0.0424 398 HOH   B O   
7186 O O   . HOH   F .   ? 0.5866 0.6301 0.7116 0.1196  -0.1330 0.1618  399 HOH   B O   
7187 O O   . HOH   F .   ? 0.5463 0.4410 0.3337 -0.2337 -0.0542 0.1398  400 HOH   B O   
7188 O O   . HOH   F .   ? 0.5702 0.5596 0.3974 0.1884  -0.0023 0.0024  401 HOH   B O   
# 
