data_7HDE
# 
_entry.id   7HDE 
# 
_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   7HDE         pdb_00007hde 10.2210/pdb7hde/pdb 
WWPDB D_1001407332 ?            ?                   
# 
_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                        7HDE 
_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 '[(2S,3aS,6aS)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-2-yl]methanol' 258.319   1   ? ? 
? ?                                                                                    
3 water       nat water                                                                                         18.015    430 ? ? 
? ?                                                                                    
# 
_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 '[(2S,3aS,6aS)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-2-yl]methanol' A1A76 
3 water                                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A76 non-polymer         . '[(2S,3aS,6aS)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-2-yl]methanol' ? 
'C14 H18 N4 O'   258.319 
ALA   'L-peptide linking' y ALANINE                                                                                       ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                      ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                    ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                               ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                      ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                     ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                               ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                       ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                     ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                         ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                    ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                       ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                        ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                    ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                 ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                       ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                        ? 
'C3 H7 N O3'     105.093 
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 A1A76 1   201 201  A1A76 LA1 A . 
D 3 HOH   1   301 39   HOH   HOH A . 
D 3 HOH   2   302 85   HOH   HOH A . 
D 3 HOH   3   303 292  HOH   HOH A . 
D 3 HOH   4   304 2    HOH   HOH A . 
D 3 HOH   5   305 625  HOH   HOH A . 
D 3 HOH   6   306 964  HOH   HOH A . 
D 3 HOH   7   307 26   HOH   HOH A . 
D 3 HOH   8   308 1301 HOH   HOH A . 
D 3 HOH   9   309 109  HOH   HOH A . 
D 3 HOH   10  310 196  HOH   HOH A . 
D 3 HOH   11  311 132  HOH   HOH A . 
D 3 HOH   12  312 1300 HOH   HOH A . 
D 3 HOH   13  313 209  HOH   HOH A . 
D 3 HOH   14  314 192  HOH   HOH A . 
D 3 HOH   15  315 153  HOH   HOH A . 
D 3 HOH   16  316 18   HOH   HOH A . 
D 3 HOH   17  317 1283 HOH   HOH A . 
D 3 HOH   18  318 493  HOH   HOH A . 
D 3 HOH   19  319 661  HOH   HOH A . 
D 3 HOH   20  320 393  HOH   HOH A . 
D 3 HOH   21  321 461  HOH   HOH A . 
D 3 HOH   22  322 1295 HOH   HOH A . 
D 3 HOH   23  323 229  HOH   HOH A . 
D 3 HOH   24  324 381  HOH   HOH A . 
D 3 HOH   25  325 337  HOH   HOH A . 
D 3 HOH   26  326 76   HOH   HOH A . 
D 3 HOH   27  327 36   HOH   HOH A . 
D 3 HOH   28  328 124  HOH   HOH A . 
D 3 HOH   29  329 93   HOH   HOH A . 
D 3 HOH   30  330 136  HOH   HOH A . 
D 3 HOH   31  331 140  HOH   HOH A . 
D 3 HOH   32  332 1309 HOH   HOH A . 
D 3 HOH   33  333 12   HOH   HOH A . 
D 3 HOH   34  334 1290 HOH   HOH A . 
D 3 HOH   35  335 165  HOH   HOH A . 
D 3 HOH   36  336 164  HOH   HOH A . 
D 3 HOH   37  337 199  HOH   HOH A . 
D 3 HOH   38  338 1275 HOH   HOH A . 
D 3 HOH   39  339 241  HOH   HOH A . 
D 3 HOH   40  340 78   HOH   HOH A . 
D 3 HOH   41  341 247  HOH   HOH A . 
D 3 HOH   42  342 33   HOH   HOH A . 
D 3 HOH   43  343 151  HOH   HOH A . 
D 3 HOH   44  344 18   HOH   HOH A . 
D 3 HOH   45  345 630  HOH   HOH A . 
D 3 HOH   46  346 10   HOH   HOH A . 
D 3 HOH   47  347 366  HOH   HOH A . 
D 3 HOH   48  348 1296 HOH   HOH A . 
D 3 HOH   49  349 57   HOH   HOH A . 
D 3 HOH   50  350 469  HOH   HOH A . 
D 3 HOH   51  351 396  HOH   HOH A . 
D 3 HOH   52  352 102  HOH   HOH A . 
D 3 HOH   53  353 236  HOH   HOH A . 
D 3 HOH   54  354 17   HOH   HOH A . 
D 3 HOH   55  355 42   HOH   HOH A . 
D 3 HOH   56  356 225  HOH   HOH A . 
D 3 HOH   57  357 281  HOH   HOH A . 
D 3 HOH   58  358 83   HOH   HOH A . 
D 3 HOH   59  359 1313 HOH   HOH A . 
D 3 HOH   60  360 320  HOH   HOH A . 
D 3 HOH   61  361 218  HOH   HOH A . 
D 3 HOH   62  362 169  HOH   HOH A . 
D 3 HOH   63  363 49   HOH   HOH A . 
D 3 HOH   64  364 96   HOH   HOH A . 
D 3 HOH   65  365 92   HOH   HOH A . 
D 3 HOH   66  366 162  HOH   HOH A . 
D 3 HOH   67  367 195  HOH   HOH A . 
D 3 HOH   68  368 45   HOH   HOH A . 
D 3 HOH   69  369 105  HOH   HOH A . 
D 3 HOH   70  370 139  HOH   HOH A . 
D 3 HOH   71  371 66   HOH   HOH A . 
D 3 HOH   72  372 56   HOH   HOH A . 
D 3 HOH   73  373 939  HOH   HOH A . 
D 3 HOH   74  374 5    HOH   HOH A . 
D 3 HOH   75  375 19   HOH   HOH A . 
D 3 HOH   76  376 1    HOH   HOH A . 
D 3 HOH   77  377 46   HOH   HOH A . 
D 3 HOH   78  378 2    HOH   HOH A . 
D 3 HOH   79  379 138  HOH   HOH A . 
D 3 HOH   80  380 662  HOH   HOH A . 
D 3 HOH   81  381 134  HOH   HOH A . 
D 3 HOH   82  382 354  HOH   HOH A . 
D 3 HOH   83  383 15   HOH   HOH A . 
D 3 HOH   84  384 3    HOH   HOH A . 
D 3 HOH   85  385 186  HOH   HOH A . 
D 3 HOH   86  386 159  HOH   HOH A . 
D 3 HOH   87  387 8    HOH   HOH A . 
D 3 HOH   88  388 86   HOH   HOH A . 
D 3 HOH   89  389 4    HOH   HOH A . 
D 3 HOH   90  390 155  HOH   HOH A . 
D 3 HOH   91  391 34   HOH   HOH A . 
D 3 HOH   92  392 74   HOH   HOH A . 
D 3 HOH   93  393 24   HOH   HOH A . 
D 3 HOH   94  394 148  HOH   HOH A . 
D 3 HOH   95  395 409  HOH   HOH A . 
D 3 HOH   96  396 35   HOH   HOH A . 
D 3 HOH   97  397 16   HOH   HOH A . 
D 3 HOH   98  398 12   HOH   HOH A . 
D 3 HOH   99  399 212  HOH   HOH A . 
D 3 HOH   100 400 296  HOH   HOH A . 
D 3 HOH   101 401 8    HOH   HOH A . 
D 3 HOH   102 402 1315 HOH   HOH A . 
D 3 HOH   103 403 58   HOH   HOH A . 
D 3 HOH   104 404 19   HOH   HOH A . 
D 3 HOH   105 405 67   HOH   HOH A . 
D 3 HOH   106 406 1289 HOH   HOH A . 
D 3 HOH   107 407 6    HOH   HOH A . 
D 3 HOH   108 408 116  HOH   HOH A . 
D 3 HOH   109 409 154  HOH   HOH A . 
D 3 HOH   110 410 303  HOH   HOH A . 
D 3 HOH   111 411 68   HOH   HOH A . 
D 3 HOH   112 412 122  HOH   HOH A . 
D 3 HOH   113 413 27   HOH   HOH A . 
D 3 HOH   114 414 21   HOH   HOH A . 
D 3 HOH   115 415 51   HOH   HOH A . 
D 3 HOH   116 416 1308 HOH   HOH A . 
D 3 HOH   117 417 1068 HOH   HOH A . 
D 3 HOH   118 418 123  HOH   HOH A . 
D 3 HOH   119 419 278  HOH   HOH A . 
D 3 HOH   120 420 4    HOH   HOH A . 
D 3 HOH   121 421 405  HOH   HOH A . 
D 3 HOH   122 422 397  HOH   HOH A . 
D 3 HOH   123 423 70   HOH   HOH A . 
D 3 HOH   124 424 1222 HOH   HOH A . 
D 3 HOH   125 425 156  HOH   HOH A . 
D 3 HOH   126 426 53   HOH   HOH A . 
D 3 HOH   127 427 125  HOH   HOH A . 
D 3 HOH   128 428 121  HOH   HOH A . 
D 3 HOH   129 429 95   HOH   HOH A . 
D 3 HOH   130 430 25   HOH   HOH A . 
D 3 HOH   131 431 7    HOH   HOH A . 
D 3 HOH   132 432 1310 HOH   HOH A . 
D 3 HOH   133 433 1094 HOH   HOH A . 
D 3 HOH   134 434 351  HOH   HOH A . 
D 3 HOH   135 435 582  HOH   HOH A . 
D 3 HOH   136 436 73   HOH   HOH A . 
D 3 HOH   137 437 115  HOH   HOH A . 
D 3 HOH   138 438 16   HOH   HOH A . 
D 3 HOH   139 439 333  HOH   HOH A . 
D 3 HOH   140 440 71   HOH   HOH A . 
D 3 HOH   141 441 1134 HOH   HOH A . 
D 3 HOH   142 442 944  HOH   HOH A . 
D 3 HOH   143 443 80   HOH   HOH A . 
D 3 HOH   144 444 1189 HOH   HOH A . 
D 3 HOH   145 445 1279 HOH   HOH A . 
D 3 HOH   146 446 6    HOH   HOH A . 
D 3 HOH   147 447 94   HOH   HOH A . 
D 3 HOH   148 448 952  HOH   HOH A . 
D 3 HOH   149 449 23   HOH   HOH A . 
D 3 HOH   150 450 97   HOH   HOH A . 
D 3 HOH   151 451 188  HOH   HOH A . 
D 3 HOH   152 452 104  HOH   HOH A . 
D 3 HOH   153 453 40   HOH   HOH A . 
D 3 HOH   154 454 1286 HOH   HOH A . 
D 3 HOH   155 455 711  HOH   HOH A . 
D 3 HOH   156 456 576  HOH   HOH A . 
D 3 HOH   157 457 1238 HOH   HOH A . 
D 3 HOH   158 458 330  HOH   HOH A . 
D 3 HOH   159 459 79   HOH   HOH A . 
D 3 HOH   160 460 5    HOH   HOH A . 
D 3 HOH   161 461 163  HOH   HOH A . 
D 3 HOH   162 462 1119 HOH   HOH A . 
D 3 HOH   163 463 107  HOH   HOH A . 
D 3 HOH   164 464 509  HOH   HOH A . 
D 3 HOH   165 465 267  HOH   HOH A . 
D 3 HOH   166 466 726  HOH   HOH A . 
D 3 HOH   167 467 756  HOH   HOH A . 
D 3 HOH   168 468 408  HOH   HOH A . 
D 3 HOH   169 469 3    HOH   HOH A . 
D 3 HOH   170 470 1276 HOH   HOH A . 
D 3 HOH   171 471 361  HOH   HOH A . 
D 3 HOH   172 472 319  HOH   HOH A . 
D 3 HOH   173 473 7    HOH   HOH A . 
D 3 HOH   174 474 17   HOH   HOH A . 
D 3 HOH   175 475 556  HOH   HOH A . 
D 3 HOH   176 476 63   HOH   HOH A . 
D 3 HOH   177 477 126  HOH   HOH A . 
D 3 HOH   178 478 801  HOH   HOH A . 
D 3 HOH   179 479 250  HOH   HOH A . 
D 3 HOH   180 480 342  HOH   HOH A . 
D 3 HOH   181 481 370  HOH   HOH A . 
D 3 HOH   182 482 1307 HOH   HOH A . 
D 3 HOH   183 483 11   HOH   HOH A . 
D 3 HOH   184 484 1306 HOH   HOH A . 
D 3 HOH   185 485 280  HOH   HOH A . 
D 3 HOH   186 486 135  HOH   HOH A . 
D 3 HOH   187 487 1287 HOH   HOH A . 
D 3 HOH   188 488 20   HOH   HOH A . 
D 3 HOH   189 489 202  HOH   HOH A . 
D 3 HOH   190 490 521  HOH   HOH A . 
D 3 HOH   191 491 224  HOH   HOH A . 
D 3 HOH   192 492 695  HOH   HOH A . 
D 3 HOH   193 493 919  HOH   HOH A . 
D 3 HOH   194 494 674  HOH   HOH A . 
D 3 HOH   195 495 318  HOH   HOH A . 
D 3 HOH   196 496 1299 HOH   HOH A . 
D 3 HOH   197 497 331  HOH   HOH A . 
D 3 HOH   198 498 326  HOH   HOH A . 
D 3 HOH   199 499 309  HOH   HOH A . 
D 3 HOH   200 500 1314 HOH   HOH A . 
D 3 HOH   201 501 315  HOH   HOH A . 
D 3 HOH   202 502 208  HOH   HOH A . 
D 3 HOH   203 503 941  HOH   HOH A . 
D 3 HOH   204 504 805  HOH   HOH A . 
D 3 HOH   205 505 152  HOH   HOH A . 
D 3 HOH   206 506 263  HOH   HOH A . 
D 3 HOH   207 507 356  HOH   HOH A . 
D 3 HOH   208 508 350  HOH   HOH A . 
D 3 HOH   209 509 9    HOH   HOH A . 
D 3 HOH   210 510 363  HOH   HOH A . 
D 3 HOH   211 511 1071 HOH   HOH A . 
D 3 HOH   212 512 180  HOH   HOH A . 
D 3 HOH   213 513 13   HOH   HOH A . 
D 3 HOH   214 514 371  HOH   HOH A . 
D 3 HOH   215 515 313  HOH   HOH A . 
D 3 HOH   216 516 1284 HOH   HOH A . 
D 3 HOH   217 517 429  HOH   HOH A . 
D 3 HOH   218 518 185  HOH   HOH A . 
D 3 HOH   219 519 14   HOH   HOH A . 
D 3 HOH   220 520 772  HOH   HOH A . 
D 3 HOH   221 521 22   HOH   HOH A . 
D 3 HOH   222 522 376  HOH   HOH A . 
D 3 HOH   223 523 1074 HOH   HOH A . 
D 3 HOH   224 524 346  HOH   HOH A . 
D 3 HOH   225 525 1292 HOH   HOH A . 
D 3 HOH   226 526 21   HOH   HOH A . 
D 3 HOH   227 527 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 240  HOH   HOH B . 
E 3 HOH   3   203 549  HOH   HOH B . 
E 3 HOH   4   204 398  HOH   HOH B . 
E 3 HOH   5   205 364  HOH   HOH B . 
E 3 HOH   6   206 900  HOH   HOH B . 
E 3 HOH   7   207 232  HOH   HOH B . 
E 3 HOH   8   208 654  HOH   HOH B . 
E 3 HOH   9   209 758  HOH   HOH B . 
E 3 HOH   10  210 1249 HOH   HOH B . 
E 3 HOH   11  211 120  HOH   HOH B . 
E 3 HOH   12  212 358  HOH   HOH B . 
E 3 HOH   13  213 444  HOH   HOH B . 
E 3 HOH   14  214 50   HOH   HOH B . 
E 3 HOH   15  215 332  HOH   HOH B . 
E 3 HOH   16  216 264  HOH   HOH B . 
E 3 HOH   17  217 166  HOH   HOH B . 
E 3 HOH   18  218 75   HOH   HOH B . 
E 3 HOH   19  219 172  HOH   HOH B . 
E 3 HOH   20  220 353  HOH   HOH B . 
E 3 HOH   21  221 276  HOH   HOH B . 
E 3 HOH   22  222 15   HOH   HOH B . 
E 3 HOH   23  223 743  HOH   HOH B . 
E 3 HOH   24  224 531  HOH   HOH B . 
E 3 HOH   25  225 205  HOH   HOH B . 
E 3 HOH   26  226 54   HOH   HOH B . 
E 3 HOH   27  227 452  HOH   HOH B . 
E 3 HOH   28  228 81   HOH   HOH B . 
E 3 HOH   29  229 82   HOH   HOH B . 
E 3 HOH   30  230 131  HOH   HOH B . 
E 3 HOH   31  231 325  HOH   HOH B . 
E 3 HOH   32  232 343  HOH   HOH B . 
E 3 HOH   33  233 181  HOH   HOH B . 
E 3 HOH   34  234 129  HOH   HOH B . 
E 3 HOH   35  235 60   HOH   HOH B . 
E 3 HOH   36  236 272  HOH   HOH B . 
E 3 HOH   37  237 110  HOH   HOH B . 
E 3 HOH   38  238 128  HOH   HOH B . 
E 3 HOH   39  239 41   HOH   HOH B . 
E 3 HOH   40  240 1312 HOH   HOH B . 
E 3 HOH   41  241 133  HOH   HOH B . 
E 3 HOH   42  242 127  HOH   HOH B . 
E 3 HOH   43  243 30   HOH   HOH B . 
E 3 HOH   44  244 1    HOH   HOH B . 
E 3 HOH   45  245 723  HOH   HOH B . 
E 3 HOH   46  246 300  HOH   HOH B . 
E 3 HOH   47  247 72   HOH   HOH B . 
E 3 HOH   48  248 69   HOH   HOH B . 
E 3 HOH   49  249 14   HOH   HOH B . 
E 3 HOH   50  250 391  HOH   HOH B . 
E 3 HOH   51  251 52   HOH   HOH B . 
E 3 HOH   52  252 62   HOH   HOH B . 
E 3 HOH   53  253 31   HOH   HOH B . 
E 3 HOH   54  254 150  HOH   HOH B . 
E 3 HOH   55  255 231  HOH   HOH B . 
E 3 HOH   56  256 1278 HOH   HOH B . 
E 3 HOH   57  257 9    HOH   HOH B . 
E 3 HOH   58  258 282  HOH   HOH B . 
E 3 HOH   59  259 243  HOH   HOH B . 
E 3 HOH   60  260 61   HOH   HOH B . 
E 3 HOH   61  261 144  HOH   HOH B . 
E 3 HOH   62  262 10   HOH   HOH B . 
E 3 HOH   63  263 47   HOH   HOH B . 
E 3 HOH   64  264 1140 HOH   HOH B . 
E 3 HOH   65  265 143  HOH   HOH B . 
E 3 HOH   66  266 302  HOH   HOH B . 
E 3 HOH   67  267 1285 HOH   HOH B . 
E 3 HOH   68  268 77   HOH   HOH B . 
E 3 HOH   69  269 59   HOH   HOH B . 
E 3 HOH   70  270 271  HOH   HOH B . 
E 3 HOH   71  271 175  HOH   HOH B . 
E 3 HOH   72  272 1277 HOH   HOH B . 
E 3 HOH   73  273 20   HOH   HOH B . 
E 3 HOH   74  274 103  HOH   HOH B . 
E 3 HOH   75  275 114  HOH   HOH B . 
E 3 HOH   76  276 84   HOH   HOH B . 
E 3 HOH   77  277 1106 HOH   HOH B . 
E 3 HOH   78  278 242  HOH   HOH B . 
E 3 HOH   79  279 117  HOH   HOH B . 
E 3 HOH   80  280 235  HOH   HOH B . 
E 3 HOH   81  281 11   HOH   HOH B . 
E 3 HOH   82  282 88   HOH   HOH B . 
E 3 HOH   83  283 221  HOH   HOH B . 
E 3 HOH   84  284 1066 HOH   HOH B . 
E 3 HOH   85  285 89   HOH   HOH B . 
E 3 HOH   86  286 1305 HOH   HOH B . 
E 3 HOH   87  287 287  HOH   HOH B . 
E 3 HOH   88  288 216  HOH   HOH B . 
E 3 HOH   89  289 347  HOH   HOH B . 
E 3 HOH   90  290 22   HOH   HOH B . 
E 3 HOH   91  291 13   HOH   HOH B . 
E 3 HOH   92  292 106  HOH   HOH B . 
E 3 HOH   93  293 43   HOH   HOH B . 
E 3 HOH   94  294 416  HOH   HOH B . 
E 3 HOH   95  295 387  HOH   HOH B . 
E 3 HOH   96  296 311  HOH   HOH B . 
E 3 HOH   97  297 445  HOH   HOH B . 
E 3 HOH   98  298 147  HOH   HOH B . 
E 3 HOH   99  299 137  HOH   HOH B . 
E 3 HOH   100 300 252  HOH   HOH B . 
E 3 HOH   101 301 38   HOH   HOH B . 
E 3 HOH   102 302 215  HOH   HOH B . 
E 3 HOH   103 303 316  HOH   HOH B . 
E 3 HOH   104 304 99   HOH   HOH B . 
E 3 HOH   105 305 297  HOH   HOH B . 
E 3 HOH   106 306 160  HOH   HOH B . 
E 3 HOH   107 307 32   HOH   HOH B . 
E 3 HOH   108 308 170  HOH   HOH B . 
E 3 HOH   109 309 142  HOH   HOH B . 
E 3 HOH   110 310 141  HOH   HOH B . 
E 3 HOH   111 311 112  HOH   HOH B . 
E 3 HOH   112 312 220  HOH   HOH B . 
E 3 HOH   113 313 299  HOH   HOH B . 
E 3 HOH   114 314 37   HOH   HOH B . 
E 3 HOH   115 315 91   HOH   HOH B . 
E 3 HOH   116 316 118  HOH   HOH B . 
E 3 HOH   117 317 23   HOH   HOH B . 
E 3 HOH   118 318 101  HOH   HOH B . 
E 3 HOH   119 319 341  HOH   HOH B . 
E 3 HOH   120 320 635  HOH   HOH B . 
E 3 HOH   121 321 44   HOH   HOH B . 
E 3 HOH   122 322 207  HOH   HOH B . 
E 3 HOH   123 323 48   HOH   HOH B . 
E 3 HOH   124 324 182  HOH   HOH B . 
E 3 HOH   125 325 1291 HOH   HOH B . 
E 3 HOH   126 326 177  HOH   HOH B . 
E 3 HOH   127 327 197  HOH   HOH B . 
E 3 HOH   128 328 1126 HOH   HOH B . 
E 3 HOH   129 329 1294 HOH   HOH B . 
E 3 HOH   130 330 717  HOH   HOH B . 
E 3 HOH   131 331 28   HOH   HOH B . 
E 3 HOH   132 332 55   HOH   HOH B . 
E 3 HOH   133 333 98   HOH   HOH B . 
E 3 HOH   134 334 100  HOH   HOH B . 
E 3 HOH   135 335 704  HOH   HOH B . 
E 3 HOH   136 336 29   HOH   HOH B . 
E 3 HOH   137 337 1274 HOH   HOH B . 
E 3 HOH   138 338 234  HOH   HOH B . 
E 3 HOH   139 339 161  HOH   HOH B . 
E 3 HOH   140 340 339  HOH   HOH B . 
E 3 HOH   141 341 362  HOH   HOH B . 
E 3 HOH   142 342 334  HOH   HOH B . 
E 3 HOH   143 343 65   HOH   HOH B . 
E 3 HOH   144 344 1293 HOH   HOH B . 
E 3 HOH   145 345 960  HOH   HOH B . 
E 3 HOH   146 346 619  HOH   HOH B . 
E 3 HOH   147 347 178  HOH   HOH B . 
E 3 HOH   148 348 90   HOH   HOH B . 
E 3 HOH   149 349 1304 HOH   HOH B . 
E 3 HOH   150 350 463  HOH   HOH B . 
E 3 HOH   151 351 1280 HOH   HOH B . 
E 3 HOH   152 352 87   HOH   HOH B . 
E 3 HOH   153 353 191  HOH   HOH B . 
E 3 HOH   154 354 203  HOH   HOH B . 
E 3 HOH   155 355 1046 HOH   HOH B . 
E 3 HOH   156 356 304  HOH   HOH B . 
E 3 HOH   157 357 335  HOH   HOH B . 
E 3 HOH   158 358 623  HOH   HOH B . 
E 3 HOH   159 359 541  HOH   HOH B . 
E 3 HOH   160 360 290  HOH   HOH B . 
E 3 HOH   161 361 1077 HOH   HOH B . 
E 3 HOH   162 362 718  HOH   HOH B . 
E 3 HOH   163 363 389  HOH   HOH B . 
E 3 HOH   164 364 1072 HOH   HOH B . 
E 3 HOH   165 365 283  HOH   HOH B . 
E 3 HOH   166 366 479  HOH   HOH B . 
E 3 HOH   167 367 373  HOH   HOH B . 
E 3 HOH   168 368 898  HOH   HOH B . 
E 3 HOH   169 369 291  HOH   HOH B . 
E 3 HOH   170 370 615  HOH   HOH B . 
E 3 HOH   171 371 1316 HOH   HOH B . 
E 3 HOH   172 372 340  HOH   HOH B . 
E 3 HOH   173 373 667  HOH   HOH B . 
E 3 HOH   174 374 190  HOH   HOH B . 
E 3 HOH   175 375 310  HOH   HOH B . 
E 3 HOH   176 376 1303 HOH   HOH B . 
E 3 HOH   177 377 1173 HOH   HOH B . 
E 3 HOH   178 378 431  HOH   HOH B . 
E 3 HOH   179 379 418  HOH   HOH B . 
E 3 HOH   180 380 183  HOH   HOH B . 
E 3 HOH   181 381 149  HOH   HOH B . 
E 3 HOH   182 382 1000 HOH   HOH B . 
E 3 HOH   183 383 1311 HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 1163 HOH   HOH B . 
E 3 HOH   186 386 176  HOH   HOH B . 
E 3 HOH   187 387 491  HOH   HOH B . 
E 3 HOH   188 388 981  HOH   HOH B . 
E 3 HOH   189 389 470  HOH   HOH B . 
E 3 HOH   190 390 265  HOH   HOH B . 
E 3 HOH   191 391 248  HOH   HOH B . 
E 3 HOH   192 392 1298 HOH   HOH B . 
E 3 HOH   193 393 184  HOH   HOH B . 
E 3 HOH   194 394 360  HOH   HOH B . 
E 3 HOH   195 395 410  HOH   HOH B . 
E 3 HOH   196 396 355  HOH   HOH B . 
E 3 HOH   197 397 314  HOH   HOH B . 
E 3 HOH   198 398 274  HOH   HOH B . 
E 3 HOH   199 399 566  HOH   HOH B . 
E 3 HOH   200 400 157  HOH   HOH B . 
E 3 HOH   201 401 321  HOH   HOH B . 
E 3 HOH   202 402 792  HOH   HOH B . 
E 3 HOH   203 403 558  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           7HDE 
_cell.length_a           88.867 
_cell.length_b           88.867 
_cell.length_c           39.444 
_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                         7HDE 
_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          7HDE 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.67 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDE 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.430 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175050 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.200 
_reflns.pdbx_Rmerge_I_obs            0.038 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.400 
_reflns.B_iso_Wilson_estimate        11.270 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.042 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1094955 
_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 0.980 1.000  ? 27538 7805 ? 0.916 ? ? ? 3.500 ? 1.000  ? ? ? ? ? ? 90.100 1.069 0.537 0.641 
1 2 5.370 44.430 ? 8041  1165 ? 0.028 ? ? ? 6.900 ? 64.000 ? ? ? ? ? ? 99.800 0.031 0.011 0.999 
# 
_refine.entry_id                                 7HDE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             39.7400 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1500 
_refine.ls_number_reflns_obs                     174976 
_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                          0.1430 
_refine.ls_R_factor_R_work                       0.1424 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1533 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  8455 
_refine.ls_number_reflns_R_work                  166521 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.9445 
_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                                79.540 
_refine.B_iso_min                                7.800 
_refine.pdbx_overall_phase_error                 16.1700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        39.7400 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             430 
_refine_hist.number_atoms_total               3009 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.00 
_refine_hist.pdbx_B_iso_mean_solvent          29.93 
_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 
0.9800 0.9900  30 88.0000  4896 . 0.3599 0.3559 . 261 0.0000 5157 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 93.0000  5187 . 0.3129 0.3218 . 267 0.0000 5454 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 95.0000  5308 . 0.2740 0.2596 . 278 0.0000 5586 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 99.0000  5514 . 0.2335 0.2361 . 238 0.0000 5752 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5543 . 0.2007 0.2087 . 313 0.0000 5856 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5554 . 0.1765 0.2029 . 285 0.0000 5839 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5573 . 0.1636 0.1877 . 330 0.0000 5903 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5534 . 0.1551 0.1658 . 254 0.0000 5788 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5589 . 0.1404 0.1626 . 277 0.0000 5866 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5560 . 0.1359 0.1622 . 290 0.0000 5850 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5626 . 0.1314 0.1535 . 250 0.0000 5876 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5603 . 0.1271 0.1581 . 267 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5546 . 0.1227 0.1349 . 291 0.0000 5837 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5559 . 0.1174 0.1520 . 314 0.0000 5873 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5635 . 0.1166 0.1339 . 243 0.0000 5878 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5573 . 0.1191 0.1355 . 283 0.0000 5856 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5545 . 0.1195 0.1402 . 283 0.0000 5828 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5570 . 0.1212 0.1509 . 311 0.0000 5881 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5625 . 0.1221 0.1466 . 291 0.0000 5916 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5605 . 0.1216 0.1340 . 245 0.0000 5850 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5596 . 0.1257 0.1397 . 306 0.0000 5902 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5599 . 0.1178 0.1306 . 259 0.0000 5858 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5563 . 0.1194 0.1266 . 305 0.0000 5868 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5643 . 0.1229 0.1314 . 280 0.0000 5923 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5621 . 0.1317 0.1428 . 262 0.0000 5883 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5593 . 0.1364 0.1400 . 306 0.0000 5899 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5624 . 0.1392 0.1411 . 288 0.0000 5912 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5641 . 0.1389 0.1342 . 306 0.0000 5947 . 'X-RAY DIFFRACTION' 
2.4200 3.0400  30 100.0000 5699 . 0.1512 0.1728 . 290 0.0000 5989 . 'X-RAY DIFFRACTION' 
3.0500 39.7400 30 100.0000 5797 . 0.1531 0.1624 . 282 0.0000 6079 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDE 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003720' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDE 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDE A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDE 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 7HDE SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDE MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDE SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDE MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HDE 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    224 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    327 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? A 54.00   -128.16 
2 1 HIS A 86  ? B 56.13   -135.91 
3 1 SER A 128 ? A 63.42   -0.17   
4 1 SER A 128 ? C 72.22   -7.09   
5 1 PHE A 132 ? B 66.52   -164.90 
6 1 ALA A 134 ? C -159.92 -157.87 
7 1 ASP A 135 ? B 90.50   109.27  
8 1 HIS B 86  ? ? 57.66   -127.28 
# 
_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 525 ? 5.91 . 
2 1 O B A HOH 526 ? 6.32 . 
3 1 O ? A HOH 527 ? 7.50 . 
4 1 O ? B HOH 403 ? 6.57 . 
# 
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 
A1A76 N2   N Y N 1   
A1A76 C3   C N N 2   
A1A76 C6   C N N 3   
A1A76 C9   C Y N 4   
A1A76 C12  C Y N 5   
A1A76 C14  C Y N 6   
A1A76 C1   C N N 7   
A1A76 C10  C Y N 8   
A1A76 C11  C Y N 9   
A1A76 C13  C Y N 10  
A1A76 C2   C N S 11  
A1A76 C4   C N S 12  
A1A76 C5   C N N 13  
A1A76 C7   C N N 14  
A1A76 C8   C N S 15  
A1A76 N1   N N N 16  
A1A76 N3   N Y N 17  
A1A76 N4   N Y N 18  
A1A76 O1   O N N 19  
A1A76 H8   H N N 20  
A1A76 H7   H N N 21  
A1A76 H11  H N N 22  
A1A76 H12  H N N 23  
A1A76 H17  H N N 24  
A1A76 H6   H N N 25  
A1A76 H5   H N N 26  
A1A76 H15  H N N 27  
A1A76 H16  H N N 28  
A1A76 H1   H N N 29  
A1A76 H2   H N N 30  
A1A76 H9   H N N 31  
A1A76 H10  H N N 32  
A1A76 H14  H N N 33  
A1A76 H13  H N N 34  
A1A76 H3   H N N 35  
A1A76 H18  H N N 36  
A1A76 H4   H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
LEU   N    N N N 220 
LEU   CA   C N S 221 
LEU   C    C N N 222 
LEU   O    O N N 223 
LEU   CB   C N N 224 
LEU   CG   C N N 225 
LEU   CD1  C N N 226 
LEU   CD2  C N N 227 
LEU   OXT  O N N 228 
LEU   H    H N N 229 
LEU   H2   H N N 230 
LEU   HA   H N N 231 
LEU   HB2  H N N 232 
LEU   HB3  H N N 233 
LEU   HG   H N N 234 
LEU   HD11 H N N 235 
LEU   HD12 H N N 236 
LEU   HD13 H N N 237 
LEU   HD21 H N N 238 
LEU   HD22 H N N 239 
LEU   HD23 H N N 240 
LEU   HXT  H N N 241 
LYS   N    N N N 242 
LYS   CA   C N S 243 
LYS   C    C N N 244 
LYS   O    O N N 245 
LYS   CB   C N N 246 
LYS   CG   C N N 247 
LYS   CD   C N N 248 
LYS   CE   C N N 249 
LYS   NZ   N N N 250 
LYS   OXT  O N N 251 
LYS   H    H N N 252 
LYS   H2   H N N 253 
LYS   HA   H N N 254 
LYS   HB2  H N N 255 
LYS   HB3  H N N 256 
LYS   HG2  H N N 257 
LYS   HG3  H N N 258 
LYS   HD2  H N N 259 
LYS   HD3  H N N 260 
LYS   HE2  H N N 261 
LYS   HE3  H N N 262 
LYS   HZ1  H N N 263 
LYS   HZ2  H N N 264 
LYS   HZ3  H N N 265 
LYS   HXT  H N N 266 
MET   N    N N N 267 
MET   CA   C N S 268 
MET   C    C N N 269 
MET   O    O N N 270 
MET   CB   C N N 271 
MET   CG   C N N 272 
MET   SD   S N N 273 
MET   CE   C N N 274 
MET   OXT  O N N 275 
MET   H    H N N 276 
MET   H2   H N N 277 
MET   HA   H N N 278 
MET   HB2  H N N 279 
MET   HB3  H N N 280 
MET   HG2  H N N 281 
MET   HG3  H N N 282 
MET   HE1  H N N 283 
MET   HE2  H N N 284 
MET   HE3  H N N 285 
MET   HXT  H N N 286 
PHE   N    N N N 287 
PHE   CA   C N S 288 
PHE   C    C N N 289 
PHE   O    O N N 290 
PHE   CB   C N N 291 
PHE   CG   C Y N 292 
PHE   CD1  C Y N 293 
PHE   CD2  C Y N 294 
PHE   CE1  C Y N 295 
PHE   CE2  C Y N 296 
PHE   CZ   C Y N 297 
PHE   OXT  O N N 298 
PHE   H    H N N 299 
PHE   H2   H N N 300 
PHE   HA   H N N 301 
PHE   HB2  H N N 302 
PHE   HB3  H N N 303 
PHE   HD1  H N N 304 
PHE   HD2  H N N 305 
PHE   HE1  H N N 306 
PHE   HE2  H N N 307 
PHE   HZ   H N N 308 
PHE   HXT  H N N 309 
PRO   N    N N N 310 
PRO   CA   C N S 311 
PRO   C    C N N 312 
PRO   O    O N N 313 
PRO   CB   C N N 314 
PRO   CG   C N N 315 
PRO   CD   C N N 316 
PRO   OXT  O N N 317 
PRO   H    H N N 318 
PRO   HA   H N N 319 
PRO   HB2  H N N 320 
PRO   HB3  H N N 321 
PRO   HG2  H N N 322 
PRO   HG3  H N N 323 
PRO   HD2  H N N 324 
PRO   HD3  H N N 325 
PRO   HXT  H N N 326 
SER   N    N N N 327 
SER   CA   C N S 328 
SER   C    C N N 329 
SER   O    O N N 330 
SER   CB   C N N 331 
SER   OG   O N N 332 
SER   OXT  O N N 333 
SER   H    H N N 334 
SER   H2   H N N 335 
SER   HA   H N N 336 
SER   HB2  H N N 337 
SER   HB3  H N N 338 
SER   HG   H N N 339 
SER   HXT  H N N 340 
THR   N    N N N 341 
THR   CA   C N S 342 
THR   C    C N N 343 
THR   O    O N N 344 
THR   CB   C N R 345 
THR   OG1  O N N 346 
THR   CG2  C N N 347 
THR   OXT  O N N 348 
THR   H    H N N 349 
THR   H2   H N N 350 
THR   HA   H N N 351 
THR   HB   H N N 352 
THR   HG1  H N N 353 
THR   HG21 H N N 354 
THR   HG22 H N N 355 
THR   HG23 H N N 356 
THR   HXT  H N N 357 
TYR   N    N N N 358 
TYR   CA   C N S 359 
TYR   C    C N N 360 
TYR   O    O N N 361 
TYR   CB   C N N 362 
TYR   CG   C Y N 363 
TYR   CD1  C Y N 364 
TYR   CD2  C Y N 365 
TYR   CE1  C Y N 366 
TYR   CE2  C Y N 367 
TYR   CZ   C Y N 368 
TYR   OH   O N N 369 
TYR   OXT  O N N 370 
TYR   H    H N N 371 
TYR   H2   H N N 372 
TYR   HA   H N N 373 
TYR   HB2  H N N 374 
TYR   HB3  H N N 375 
TYR   HD1  H N N 376 
TYR   HD2  H N N 377 
TYR   HE1  H N N 378 
TYR   HE2  H N N 379 
TYR   HH   H N N 380 
TYR   HXT  H N N 381 
VAL   N    N N N 382 
VAL   CA   C N S 383 
VAL   C    C N N 384 
VAL   O    O N N 385 
VAL   CB   C N N 386 
VAL   CG1  C N N 387 
VAL   CG2  C N N 388 
VAL   OXT  O N N 389 
VAL   H    H N N 390 
VAL   H2   H N N 391 
VAL   HA   H N N 392 
VAL   HB   H N N 393 
VAL   HG11 H N N 394 
VAL   HG12 H N N 395 
VAL   HG13 H N N 396 
VAL   HG21 H N N 397 
VAL   HG22 H N N 398 
VAL   HG23 H N N 399 
VAL   HXT  H N N 400 
# 
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 
A1A76 C5  C6   sing N N 1   
A1A76 C5  C4   sing N N 2   
A1A76 C6  C7   sing N N 3   
A1A76 C3  C4   sing N N 4   
A1A76 C3  C2   sing N N 5   
A1A76 C4  C8   sing N N 6   
A1A76 O1  C1   sing N N 7   
A1A76 C7  C8   sing N N 8   
A1A76 C1  C2   sing N N 9   
A1A76 C8  N1   sing N N 10  
A1A76 C2  N1   sing N N 11  
A1A76 N1  C9   sing N N 12  
A1A76 C9  N2   doub Y N 13  
A1A76 C9  C12  sing Y N 14  
A1A76 C13 C12  sing Y N 15  
A1A76 C13 C14  doub Y N 16  
A1A76 N2  C10  sing Y N 17  
A1A76 C12 C11  doub Y N 18  
A1A76 C14 N4   sing Y N 19  
A1A76 C10 N3   doub Y N 20  
A1A76 C11 N4   sing Y N 21  
A1A76 C11 N3   sing Y N 22  
A1A76 C3  H8   sing N N 23  
A1A76 C3  H7   sing N N 24  
A1A76 C6  H11  sing N N 25  
A1A76 C6  H12  sing N N 26  
A1A76 C14 H17  sing N N 27  
A1A76 C1  H6   sing N N 28  
A1A76 C1  H5   sing N N 29  
A1A76 C10 H15  sing N N 30  
A1A76 C13 H16  sing N N 31  
A1A76 C2  H1   sing N N 32  
A1A76 C4  H2   sing N N 33  
A1A76 C5  H9   sing N N 34  
A1A76 C5  H10  sing N N 35  
A1A76 C7  H14  sing N N 36  
A1A76 C7  H13  sing N N 37  
A1A76 C8  H3   sing N N 38  
A1A76 N4  H18  sing N N 39  
A1A76 O1  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TYR   N   CA   sing N N 346 
TYR   N   H    sing N N 347 
TYR   N   H2   sing N N 348 
TYR   CA  C    sing N N 349 
TYR   CA  CB   sing N N 350 
TYR   CA  HA   sing N N 351 
TYR   C   O    doub N N 352 
TYR   C   OXT  sing N N 353 
TYR   CB  CG   sing N N 354 
TYR   CB  HB2  sing N N 355 
TYR   CB  HB3  sing N N 356 
TYR   CG  CD1  doub Y N 357 
TYR   CG  CD2  sing Y N 358 
TYR   CD1 CE1  sing Y N 359 
TYR   CD1 HD1  sing N N 360 
TYR   CD2 CE2  doub Y N 361 
TYR   CD2 HD2  sing N N 362 
TYR   CE1 CZ   doub Y N 363 
TYR   CE1 HE1  sing N N 364 
TYR   CE2 CZ   sing Y N 365 
TYR   CE2 HE2  sing N N 366 
TYR   CZ  OH   sing N N 367 
TYR   OH  HH   sing N N 368 
TYR   OXT HXT  sing N N 369 
VAL   N   CA   sing N N 370 
VAL   N   H    sing N N 371 
VAL   N   H2   sing N N 372 
VAL   CA  C    sing N N 373 
VAL   CA  CB   sing N N 374 
VAL   CA  HA   sing N N 375 
VAL   C   O    doub N N 376 
VAL   C   OXT  sing N N 377 
VAL   CB  CG1  sing N N 378 
VAL   CB  CG2  sing N N 379 
VAL   CB  HB   sing N N 380 
VAL   CG1 HG11 sing N N 381 
VAL   CG1 HG12 sing N N 382 
VAL   CG1 HG13 sing N N 383 
VAL   CG2 HG21 sing N N 384 
VAL   CG2 HG22 sing N N 385 
VAL   CG2 HG23 sing N N 386 
VAL   OXT HXT  sing N N 387 
# 
_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                    7HDE 
_atom_sites.fract_transf_matrix[1][1]   0.011253 
_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]   0.011253 
_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]   0.025352 
_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   ? 19.762 -16.296 22.233  0.42 54.21 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.709 -15.962 22.388  0.58 55.03 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.796 -15.217 22.397  0.42 53.85 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.747 -14.885 22.583  0.58 54.59 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.452 -13.870 22.107  0.42 51.89 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.390 -13.540 22.256  0.58 52.44 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.570 -13.608 22.551  0.42 52.31 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.507 -13.258 22.690  0.58 52.88 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.155 -15.246 23.802  0.42 55.10 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.168 -14.904 24.014  0.58 55.92 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.135 -14.125 23.951  0.42 55.47 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.150 -13.787 24.194  0.58 56.29 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.506 -16.598 24.064  0.42 55.48 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.538 -16.257 24.314  0.58 56.34 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.084 -15.337 21.754  0.42 64.64 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.009 -15.013 21.972  0.58 65.54 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.845 -15.113 24.471  0.42 66.15 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.885 -14.761 24.651  0.58 67.13 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.623 -14.271 24.762  0.42 66.59 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.674 -13.926 25.028  0.58 67.58 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.601 -13.277 24.003  0.42 66.59 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.614 -12.935 24.217  0.58 67.58 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.544 -14.134 23.182  0.42 66.59 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.526 -13.807 23.452  0.58 67.58 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.055 -16.571 24.922  0.42 66.60 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.115 -16.222 25.186  0.58 67.64 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.865 -16.781 23.359  0.42 66.60 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.876 -16.454 23.633  0.58 67.64 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.193 -17.282 24.073  0.42 66.60 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.230 -16.937 24.309  0.58 67.64 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.757 -13.024 21.349  0.42 49.21 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.684 -12.716 21.482  0.58 49.49 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.203 -11.666 21.064  0.42 46.20 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.146 -11.380 21.128  0.58 46.17 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.053 -10.696 21.322  0.42 43.29 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 18.040 -10.367 21.408  0.58 43.25 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.946 -11.094 21.699  0.42 43.55 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.946 -10.716 21.865  0.58 43.44 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.763 -11.536 19.640  0.42 45.83 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.637 -11.313 19.674  0.58 45.54 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.763 -11.938 18.576  0.42 45.33 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.577 -11.727 18.676  0.58 44.77 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.620 -11.481 18.573  0.42 45.16 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.455 -11.222 18.696  0.58 44.46 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.193 -12.801 17.661  0.42 45.22 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.930 -12.657 17.794  0.58 44.60 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 18.007 -13.224 20.978  0.42 59.08 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.918 -12.919 21.145  0.58 59.41 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.919 -11.445 21.675  0.42 55.46 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.898 -11.158 21.691  0.58 55.43 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 20.014 -10.610 19.484  0.42 55.03 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.902 -10.401 19.471  0.58 54.68 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.541 -12.107 19.554  0.42 55.03 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.395 -11.908 19.570  0.58 54.68 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.667 -13.061 17.032  0.42 54.29 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.367 -12.926 17.203  0.58 53.55 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.999 -13.101 17.698  0.42 54.29 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.724 -12.989 17.814  0.58 53.55 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.321 -9.407  21.109  0.42 39.86 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.331 -9.097  21.125  0.58 39.90 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.400 -8.341  21.482  0.42 36.22 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.463 -7.988  21.496  0.58 36.37 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.536 -7.856  20.322  0.42 32.23 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.565 -7.519  20.356  0.58 32.12 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.857 -6.834  20.458  0.42 32.21 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.885 -6.498  20.500  0.58 32.05 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.170 -7.166  22.091  0.42 36.65 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.295 -6.814  22.018  0.58 37.23 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.169 -6.696  21.203  0.42 36.83 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 19.208 -6.362  21.035  0.58 37.66 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 19.041 -9.126  20.735  0.42 47.86 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 19.038 -8.855  20.701  0.58 47.91 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.808 -8.680  22.171  0.42 43.50 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.894 -8.280  22.225  0.58 43.67 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.547 -6.443  22.275  0.42 44.00 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.697 -6.086  22.254  0.58 44.71 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.590 -7.456  22.916  0.42 44.00 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.790 -7.102  22.801  0.58 44.71 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.582 -6.052  21.551  0.42 44.23 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.655 -5.717  21.335  0.58 45.22 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.548 -8.553  19.188  0.42 27.93 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.554 -8.224  19.228  0.58 27.52 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.660 -8.196  18.089  0.42 23.91 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.595 -7.916  18.177  0.58 23.43 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.224 -8.573  18.438  0.42 22.83 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.196 -8.290  18.645  0.58 23.45 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.952 -9.706  18.846  0.42 22.99 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 14.000 -9.317  19.299  0.58 24.68 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.090 -8.913  16.811  0.42 21.34 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.942 -8.679  16.899  0.58 20.18 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.356 -8.371  16.204  0.42 19.30 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.225 -8.228  16.250  0.58 17.58 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.340 -7.200  15.464  0.42 18.40 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.289 -7.022  15.569  0.58 16.48 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.558 -9.041  16.361  0.42 18.95 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.361 -9.017  16.308  0.58 17.54 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.503 -6.702  14.899  0.42 18.16 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.468 -6.610  14.969  0.58 16.42 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.723 -8.547  15.799  0.42 18.71 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.539 -8.610  15.709  0.58 17.48 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.694 -7.378  15.066  0.42 18.36 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.592 -7.407  15.038  0.58 16.79 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.063 -9.224  19.030  0.42 33.54 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 17.084 -8.876  19.050  0.58 33.06 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.700 -7.241  17.939  0.42 28.72 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.609 -6.970  17.991  0.58 28.14 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.235 -9.852  17.014  0.42 25.63 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 16.032 -9.621  17.111  0.58 24.24 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.383 -8.826  16.154  0.42 25.63 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.224 -8.555  16.258  0.58 24.24 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.541 -6.740  15.348  0.42 22.11 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.534 -6.478  15.519  0.58 19.81 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.582 -9.830  16.854  0.42 22.76 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.327 -9.830  16.761  0.58 21.07 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.482 -5.913  14.406  0.42 21.82 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.502 -5.795  14.517  0.58 19.73 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.525 -9.005  15.914  0.42 22.48 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.294 -9.150  15.760  0.58 21.00 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.475 -7.044  14.688  0.42 22.06 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.383 -7.130  14.637  0.58 20.18 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.300 -7.628  18.256  0.42 21.82 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.217 -7.446  18.321  0.58 22.52 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.927 -7.768  18.722  0.42 21.36 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.865 -7.603  18.840  0.58 22.72 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.941 -7.516  17.587  0.42 19.68 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.839 -7.453  17.726  0.58 20.42 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.163 -6.648  16.738  0.42 19.80 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.964 -6.582  16.861  0.58 20.49 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.649 -6.782  19.868  0.42 22.55 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.585 -6.568  19.938  0.58 25.12 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.263 -6.703  20.156  0.42 23.31 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.622 -7.053  20.856  0.58 26.94 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.454 -6.885  17.855  0.42 26.22 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.316 -6.770  17.799  0.58 27.05 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.786 -8.668  19.055  0.42 25.65 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.766 -8.487  19.224  0.58 27.29 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.129 -7.078  20.661  0.42 27.08 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.413 -6.378  20.411  0.58 30.17 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.961 -5.901  19.608  0.42 27.08 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.245 -5.757  19.530  0.58 30.17 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.135 -6.172  20.794  0.42 28.01 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.487 -6.483  21.458  0.58 32.36 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.852  -8.285  17.583  0.42 18.58 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.817  -8.306  17.759  0.58 19.10 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.749  -8.055  16.671  0.42 17.31 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.700  -8.187  16.850  0.58 18.08 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.936  -8.565  15.261  0.42 16.25 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.923  -8.709  15.452  0.58 16.40 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.208  -8.134  14.361  0.42 16.71 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.108  -8.417  14.569  0.58 16.48 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.733  -8.949  18.111  0.42 22.33 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.755  -8.962  18.308  0.58 22.95 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.951  -8.473  17.046  0.42 20.79 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.947  -8.674  17.217  0.58 21.72 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.580  -7.105  16.613  0.42 20.79 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.450  -7.256  16.779  0.58 21.72 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.883  -9.469  15.030  0.42 14.68 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.983  -9.478  15.214  0.58 15.24 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.127 -9.992  13.695  0.42 13.55 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.231 -10.006 13.881  0.58 14.33 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.238  -11.193 13.399  0.42 13.50 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.394  -11.248 13.613  0.58 13.86 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.795  -11.914 14.299  0.42 14.38 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.178  -12.086 14.499  0.58 14.59 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.594 -10.396 13.521  0.42 13.25 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.710 -10.356 13.699  0.58 14.24 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.525 -9.216  13.366  0.42 13.45 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.577 -9.142  13.462  0.58 14.00 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.855 -8.425  14.457  0.42 14.23 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.891 -8.283  14.504  0.58 14.78 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.064 -8.883  12.129  0.42 13.32 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.059 -8.840  12.194  0.58 13.40 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.694 -7.338  14.327  0.42 14.62 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.664 -7.158  14.296  0.58 14.87 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.907 -7.796  11.988  0.42 13.84 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.838 -7.720  11.976  0.58 13.69 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.216 -7.027  13.089  0.42 14.70 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.132 -6.881  13.027  0.58 14.45 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 15.052 -5.949  12.952  0.42 15.91 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.899 -5.766  12.801  0.58 15.65 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.398 -9.797  15.632  0.42 17.65 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.565 -9.716  15.805  0.58 18.31 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.925  -9.308  13.042  0.42 16.29 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 10.000 -9.330  13.226  0.58 17.22 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.880 -10.900 14.299  0.42 15.93 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 12.032 -10.810 14.493  0.58 17.12 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.676 -10.943 12.724  0.42 15.93 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.793 -10.941 12.927  0.58 17.12 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.497 -8.630  15.292  0.42 17.10 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.564 -8.471  15.358  0.58 17.76 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.854 -9.400  11.384  0.42 16.01 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.856 -9.404  11.481  0.58 16.10 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.902 -6.817  15.068  0.42 17.58 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.863 -6.597  15.007  0.58 17.87 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.263 -7.584  11.154  0.42 16.63 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.155 -7.533  11.123  0.58 16.46 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.158 -5.572  13.696  0.42 19.12 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.017 -5.350  13.520  0.58 18.81 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.986  -11.396 12.112  0.42 13.38 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.948  -11.373 12.367  0.58 13.17 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.348  -12.599 11.608  0.42 13.36 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.427  -12.634 11.865  0.58 13.41 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.436  -13.549 11.127  0.42 12.64 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.590  -13.533 11.479  0.58 12.34 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.376 -13.135 10.442  0.42 12.42 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.584 -13.072 10.922  0.58 11.77 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.427  -12.233 10.445  0.42 14.42 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.596  -12.394 10.609  0.58 15.27 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.728  -13.404 9.766   0.42 15.56 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.200  -11.810 10.722  0.58 17.15 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.631  -13.943 10.660  0.42 16.17 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.637  -11.653 9.325   0.58 18.47 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.174  -12.974 8.426   0.42 16.34 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 5.329  -12.724 11.551  0.58 17.16 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 9.183  -10.834 11.488  0.42 16.08 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.950  -10.732 11.785  0.58 15.83 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.824  -13.029 12.307  0.42 16.06 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.887  -13.068 12.544  0.58 16.12 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.737  -11.634 10.774  0.42 17.33 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 8.100  -11.795 10.034  0.58 18.35 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.954  -11.777 9.770   0.42 17.33 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.499  -13.247 10.159  0.58 18.35 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.366  -14.117 9.609   0.42 18.70 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 6.241  -10.936 11.144  0.58 20.60 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.307  -14.780 10.293  0.42 19.43 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 4.746  -11.286 9.388   0.58 22.19 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.986  -14.085 11.550  0.42 19.43 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.209  -11.058 8.816   0.58 22.19 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.908  -13.295 10.695  0.42 19.43 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.607  -12.526 8.900   0.58 22.19 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.726  -13.732 8.019   0.42 19.63 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 4.416  -12.408 11.511  0.58 20.62 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.546  -12.251 8.565   0.42 19.63 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.386  -13.623 11.185  0.58 20.62 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.906  -12.680 7.865   0.42 19.63 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 5.648  -12.719 12.465  0.58 20.62 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.307  -14.822 11.488  0.42 12.62 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.456  -14.818 11.761  0.58 13.43 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.339 -15.817 11.222  0.42 12.58 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.441 -15.806 11.350  0.58 13.31 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 10.048 -16.482 9.882   0.42 12.43 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 10.042 -16.321 9.975   0.58 13.13 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 9.090  -17.254 9.763   0.42 12.86 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.902  -16.757 9.785   0.58 14.07 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.356 -16.845 12.351  0.42 12.89 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.461 -16.945 12.370  0.58 13.35 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.407 -17.930 12.214  0.42 12.69 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.511 -18.021 12.149  0.58 13.07 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.496 -18.757 13.490  0.42 13.13 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.590 -18.916 13.383  0.58 13.34 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.484 -19.911 13.358  0.42 13.20 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.649 -20.000 13.262  0.58 13.20 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.856 -19.448 13.010  0.42 13.43 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.996 -19.414 13.065  0.58 13.39 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.619  -15.140 11.900  0.42 15.17 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.788  -15.142 12.189  0.58 16.14 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.203 -15.380 11.177  0.42 15.13 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.320 -15.401 11.301  0.58 16.00 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.519 -16.380 13.186  0.42 15.50 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.618 -16.561 13.248  0.58 16.04 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.489  -17.279 12.383  0.42 15.50 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.594  -17.377 12.358  0.58 16.04 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.170 -18.518 11.481  0.42 15.26 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.267 -18.565 11.383  0.58 15.71 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.272 -17.520 12.052  0.42 15.26 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.379 -17.607 12.008  0.58 15.71 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.788 -18.187 14.220  0.42 15.78 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.804 -18.369 14.155  0.58 16.04 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.621 -19.129 13.689  0.42 15.78 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.730 -19.348 13.512  0.58 16.04 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.535 -20.384 14.203  0.42 15.87 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.664 -20.528 14.077  0.58 15.87 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.184 -20.509 12.657  0.42 15.87 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.446 -20.564 12.500  0.58 15.87 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.403 -20.144 12.934  0.42 16.15 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.606 -20.057 13.030  0.58 16.09 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.841 -19.006 12.235  0.42 16.15 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 14.016 -18.954 12.300  0.58 16.09 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.165 -18.905 13.643  0.42 16.15 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 14.189 -18.863 13.736  0.58 16.09 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.883 -16.202 8.876   0.42 11.67 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.962 -16.250 9.010   0.58 12.62 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.678 -16.817 7.568   0.42 12.27 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.684 -16.778 7.676   0.58 13.22 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.274 -18.216 7.504   0.42 12.28 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.264 -18.166 7.450   0.58 12.72 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.649 -19.136 6.965   0.42 12.68 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.628 -18.997 6.796   0.58 12.43 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.280 -15.951 6.463   0.42 12.61 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.209 -15.841 6.586   0.58 14.01 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.592 -14.611 6.228   0.42 13.47 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.558 -14.465 6.484   0.58 14.88 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.363 -13.814 5.196   0.42 13.94 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.075 -13.743 5.250   0.58 15.83 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.143  -14.812 5.793   0.42 13.81 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 9.037  -14.570 6.460   0.58 14.77 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.569 -15.679 8.931   0.42 14.03 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.752 -15.906 9.104   0.58 15.17 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.729  -16.898 7.412   0.42 14.76 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.724  -16.849 7.573   0.58 15.89 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.206 -15.766 6.687   0.42 15.16 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.154 -15.702 6.742   0.58 16.84 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.241 -16.450 5.633   0.42 15.16 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.085 -16.283 5.733   0.58 16.84 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.588 -14.111 7.058   0.42 16.19 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.808 -13.946 7.261   0.58 17.88 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.906 -12.971 5.046   0.42 16.75 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.654 -12.871 5.197   0.58 19.02 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.258 -13.650 5.528   0.42 16.75 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.037 -13.643 5.322   0.58 19.02 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.402 -14.321 4.370   0.42 16.75 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.855 -14.265 4.461   0.58 19.02 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.786  -13.968 5.486   0.42 16.60 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.667  -13.712 6.210   0.58 17.75 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 9.118  -15.467 5.075   0.42 16.60 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.776  -15.246 5.815   0.58 17.75 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.627  -15.137 6.549   0.42 16.60 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.724  -14.822 7.345   0.58 17.75 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.485 -18.384 8.025   0.42 11.83 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.475 -18.414 7.943   0.58 12.39 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.196 -19.652 7.980   0.42 11.53 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 13.157 -19.697 7.813   0.58 12.37 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.934 -19.836 9.300   0.42 11.69 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.946 -19.939 9.094   0.58 12.03 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.792 -19.045 10.238  0.42 11.92 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.872 -19.158 10.048  0.58 12.13 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.197 -19.696 6.818   0.42 11.95 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 14.116 -19.723 6.615   0.58 12.98 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.214 -18.725 7.062   0.42 11.58 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 15.198 -18.821 6.865   0.58 13.47 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.538 -19.424 5.465   0.42 12.55 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.427 -19.344 5.316   0.58 13.59 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.930 -17.757 8.412   0.42 14.23 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.947 -17.828 8.365   0.58 14.89 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.568 -20.377 7.868   0.42 13.86 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.506 -20.409 7.702   0.58 14.87 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.607 -20.574 6.775   0.42 14.36 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.476 -20.618 6.514   0.58 15.60 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.836 -19.058 7.516   0.42 13.92 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.738 -18.824 6.221   0.58 16.19 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 14.194 -19.516 4.749   0.42 15.09 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 14.053 -19.430 4.575   0.58 16.34 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.822 -20.057 5.313   0.42 15.09 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.676 -19.933 5.160   0.58 16.34 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.179 -18.525 5.442   0.42 15.09 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.116 -18.430 5.359   0.58 16.34 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.760 -20.880 9.351   0.42 11.67 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.755 -21.000 9.093   0.58 12.40 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.583 -21.127 10.524  0.42 12.27 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.594 -21.276 10.251  0.58 12.63 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.393 -19.890 10.916  0.42 12.09 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.442 -20.067 10.639  0.58 11.87 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.549 -19.597 12.107  0.42 13.18 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.744 -19.883 11.822  0.58 12.27 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.511 -22.308 10.239  0.42 14.02 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.516 -22.459 9.957   0.58 15.09 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.495 -22.540 11.356  0.42 17.42 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.295 -22.908 11.178  0.58 18.33 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 17.055 -22.939 12.454  0.42 18.98 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.661 -23.300 12.182  0.58 19.42 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.704 -22.303 11.139  0.42 19.03 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.538 -22.894 11.128  0.58 20.44 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.858 -21.448 8.721   0.42 14.04 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.844 -21.555 8.438   0.58 14.91 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 15.013 -21.358 11.273  0.42 14.75 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 15.031 -21.516 11.000  0.58 15.18 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.959 -23.109 10.100  0.42 16.85 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.976 -23.218 9.675   0.58 18.14 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 17.020 -22.129 9.436   0.42 16.85 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 17.133 -22.214 9.252   0.58 18.14 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.901 -19.139 9.929   0.42 11.76 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.855 -19.241 9.664   0.58 11.01 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.859 -18.066 10.181  0.42 11.63 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.862 -18.214 9.927   0.58 11.44 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.446 -16.700 9.651   0.42 11.17 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.503 -16.815 9.436   0.58 11.62 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 18.100 -15.713 10.006  0.42 11.61 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.340 -15.911 9.555   0.58 11.95 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 19.240 -18.410 9.590   0.42 11.73 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.221 -18.633 9.349   0.58 11.25 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 19.208 -18.582 8.081   0.42 11.53 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.227 -18.656 7.838   0.58 11.80 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.392 -19.340 7.549   0.42 11.80 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.604 -19.523 7.214   0.58 11.99 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 20.088 -17.862 7.377   0.42 11.53 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.921 -17.691 7.234   0.58 12.16 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.691 -19.225 9.108   0.42 14.15 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.576 -19.276 8.853   0.58 13.25 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.978 -17.976 11.144  0.42 13.98 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.972 -18.141 10.883  0.58 13.76 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.862 -17.689 9.801   0.42 14.10 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.898 -18.000 9.644   0.58 13.53 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.555 -19.238 9.976   0.42 14.10 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.445 -19.523 9.669   0.58 13.53 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 20.105 -17.920 6.516   0.42 13.86 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.955 -17.661 6.376   0.58 14.61 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.641 -17.337 7.778   0.42 13.86 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.334 -17.098 7.702   0.58 14.61 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.408 -16.607 8.815   0.42 11.02 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.295 -16.592 8.917   0.58 12.31 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.969 -15.349 8.210   0.42 11.09 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.911 -15.298 8.358   0.58 12.19 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.684 -14.881 8.879   0.42 10.37 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.664 -14.789 9.067   0.58 12.09 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.687 -15.613 8.930   0.42 10.57 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.668 -15.513 9.200   0.58 12.40 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.775 -15.467 6.688   0.42 11.72 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.705 -15.357 6.833   0.58 12.11 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.321 -14.127 6.108   0.42 12.37 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.264 -13.999 6.290   0.58 12.89 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 17.051 -15.933 6.013   0.42 12.22 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.977 -15.820 6.132   0.58 12.70 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.938 -17.284 8.579   0.42 13.26 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.663 -17.183 8.890   0.58 14.80 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.648 -14.675 8.366   0.42 13.34 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.623 -14.665 8.530   0.58 14.65 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 15.089 -16.126 6.504   0.42 14.09 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 15.009 -15.998 6.638   0.58 14.56 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.403 -14.155 5.143   0.42 14.87 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.330 -14.017 5.322   0.58 15.50 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.396 -13.973 6.356   0.42 14.87 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.346 -13.837 6.555   0.58 15.50 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.883 -13.422 6.467   0.42 14.87 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.843 -13.312 6.649   0.58 15.50 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.916 -15.936 5.052   0.42 14.69 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.828 -15.813 5.174   0.58 15.26 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.770 -15.324 6.243   0.42 14.69 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.703 -15.217 6.358   0.58 15.26 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 17.263 -16.828 6.320   0.42 14.69 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 17.192 -16.719 6.427   0.58 15.26 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.704 -13.633 9.341   0.42 10.31 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.719 -13.524 9.486   0.58 11.91 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.600 -12.961 10.008  0.42 10.57 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.657 -12.840 10.205  0.58 11.44 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.310 -11.652 9.281   0.42 10.79 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.376 -11.521 9.499   0.58 11.67 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.162 -11.132 8.552   0.42 9.87  ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.285 -10.903 8.945   0.58 11.50 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.998 -12.653 11.453  0.42 11.02 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 14.098 -12.579 11.649  0.58 11.69 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 14.202 -13.892 12.294  0.42 12.26 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.321 -13.845 12.449  0.58 12.41 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.375 -14.638 12.217  0.42 12.82 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.526 -14.537 12.389  0.58 13.17 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 13.206 -14.335 13.151  0.42 12.51 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.315 -14.366 13.251  0.58 13.03 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.547 -15.791 12.981  0.42 13.17 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.724 -15.711 13.113  0.58 14.21 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.370 -15.480 13.917  0.42 13.00 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.504 -15.536 13.981  0.58 13.83 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.540 -16.205 13.831  0.42 13.45 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.710 -16.205 13.909  0.58 14.42 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.694 -17.343 14.597  0.42 14.11 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 14.902 -17.366 14.632  0.58 15.52 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.395 -13.138 9.264   0.42 12.40 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.399 -13.004 9.333   0.58 14.33 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.808 -13.531 9.995   0.42 12.72 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.853 -13.379 10.203  0.58 13.75 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.830 -12.157 11.445  0.42 13.25 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.934 -12.092 11.639  0.58 14.06 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.297 -12.128 11.860  0.42 13.25 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.417 -12.066 12.100  0.58 14.06 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 16.058 -14.367 11.645  0.42 15.42 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 16.216 -14.216 11.854  0.58 15.83 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.412 -13.860 13.215  0.42 15.04 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.499 -13.927 13.304  0.58 15.67 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.342 -16.276 12.925  0.42 15.83 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.539 -16.160 13.065  0.58 17.07 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.692 -15.760 14.490  0.42 15.62 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.818 -15.869 14.516  0.58 16.62 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 13.959 -17.549 14.945  0.42 16.96 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 15.673 -17.666 14.496  0.58 18.65 ?  17  TYR   A HH   1 
ATOM   473  N N    . ILE   A 1 18  ? 12.111 -11.097 9.492   1.00 11.77 ?  18  ILE   A N    1 
ATOM   474  C CA   . ILE   A 1 18  ? 11.697 -9.897  8.763   1.00 12.22 ?  18  ILE   A CA   1 
ATOM   475  C C    . ILE   A 1 18  ? 10.729 -9.051  9.579   1.00 12.51 ?  18  ILE   A C    1 
ATOM   476  O O    . ILE   A 1 18  ? 9.918  -9.569  10.351  1.00 12.99 ?  18  ILE   A O    1 
ATOM   477  C CB   . ILE   A 1 18  ? 11.112 -10.307 7.391   1.00 12.37 ?  18  ILE   A CB   1 
ATOM   478  C CG1  . ILE   A 1 18  ? 10.995 -9.123  6.432   1.00 13.36 ?  18  ILE   A CG1  1 
ATOM   479  C CG2  . ILE   A 1 18  ? 9.796  -11.048 7.563   1.00 12.86 ?  18  ILE   A CG2  1 
ATOM   480  C CD1  . ILE   A 1 18  ? 10.793 -9.570  5.002   1.00 15.81 ?  18  ILE   A CD1  1 
ATOM   481  H H    A ILE   A 1 18  ? 11.528 -11.401 10.049  0.42 14.15 ?  18  ILE   A H    1 
ATOM   482  H H    B ILE   A 1 18  ? 11.462 -11.515 9.879   0.58 14.15 ?  18  ILE   A H    1 
ATOM   483  H HA   . ILE   A 1 18  ? 12.485 -9.360  8.590   1.00 14.69 ?  18  ILE   A HA   1 
ATOM   484  H HB   . ILE   A 1 18  ? 11.730 -10.930 6.989   1.00 14.87 ?  18  ILE   A HB   1 
ATOM   485  H HG12 . ILE   A 1 18  ? 10.229 -8.580  6.681   1.00 16.06 ?  18  ILE   A HG12 1 
ATOM   486  H HG13 . ILE   A 1 18  ? 11.804 -8.599  6.468   1.00 16.06 ?  18  ILE   A HG13 1 
ATOM   487  H HG21 . ILE   A 1 18  ? 9.541  -11.432 6.710   1.00 15.45 ?  18  ILE   A HG21 1 
ATOM   488  H HG22 . ILE   A 1 18  ? 9.921  -11.752 8.218   1.00 15.45 ?  18  ILE   A HG22 1 
ATOM   489  H HG23 . ILE   A 1 18  ? 9.119  -10.427 7.865   1.00 15.45 ?  18  ILE   A HG23 1 
ATOM   490  H HD11 . ILE   A 1 18  ? 10.792 -8.789  4.424   1.00 19.00 ?  18  ILE   A HD11 1 
ATOM   491  H HD12 . ILE   A 1 18  ? 11.517 -10.163 4.753   1.00 19.00 ?  18  ILE   A HD12 1 
ATOM   492  H HD13 . ILE   A 1 18  ? 9.944  -10.033 4.930   1.00 19.00 ?  18  ILE   A HD13 1 
ATOM   493  N N    A LYS   A 1 19  ? 10.795 -7.729  9.387   0.42 12.67 ?  19  LYS   A N    1 
ATOM   494  N N    B LYS   A 1 19  ? 10.802 -7.741  9.358   0.58 12.58 ?  19  LYS   A N    1 
ATOM   495  C CA   A LYS   A 1 19  ? 10.002 -6.785  10.173  0.42 13.46 ?  19  LYS   A CA   1 
ATOM   496  C CA   B LYS   A 1 19  ? 9.944  -6.782  10.031  0.58 13.30 ?  19  LYS   A CA   1 
ATOM   497  C C    A LYS   A 1 19  ? 9.822  -5.493  9.384   0.42 13.23 ?  19  LYS   A C    1 
ATOM   498  C C    B LYS   A 1 19  ? 9.725  -5.594  9.105   0.58 13.27 ?  19  LYS   A C    1 
ATOM   499  O O    A LYS   A 1 19  ? 10.743 -5.057  8.691   0.42 13.10 ?  19  LYS   A O    1 
ATOM   500  O O    B LYS   A 1 19  ? 10.609 -5.227  8.327   0.58 12.72 ?  19  LYS   A O    1 
ATOM   501  C CB   A LYS   A 1 19  ? 10.719 -6.478  11.496  0.42 14.27 ?  19  LYS   A CB   1 
ATOM   502  C CB   B LYS   A 1 19  ? 10.629 -6.307  11.312  0.58 13.84 ?  19  LYS   A CB   1 
ATOM   503  C CG   A LYS   A 1 19  ? 10.066 -5.429  12.392  0.42 15.02 ?  19  LYS   A CG   1 
ATOM   504  C CG   B LYS   A 1 19  ? 9.800  -5.437  12.234  0.58 15.44 ?  19  LYS   A CG   1 
ATOM   505  C CD   A LYS   A 1 19  ? 10.991 -5.113  13.565  0.42 15.04 ?  19  LYS   A CD   1 
ATOM   506  C CD   B LYS   A 1 19  ? 10.627 -5.102  13.467  0.58 16.88 ?  19  LYS   A CD   1 
ATOM   507  C CE   A LYS   A 1 19  ? 10.353 -4.187  14.584  0.42 15.43 ?  19  LYS   A CE   1 
ATOM   508  C CE   B LYS   A 1 19  ? 9.896  -4.177  14.418  0.58 17.61 ?  19  LYS   A CE   1 
ATOM   509  N NZ   A LYS   A 1 19  ? 11.247 -4.029  15.768  0.42 15.88 ?  19  LYS   A NZ   1 
ATOM   510  N NZ   B LYS   A 1 19  ? 10.760 -3.790  15.567  0.58 17.96 ?  19  LYS   A NZ   1 
ATOM   511  H H    A LYS   A 1 19  ? 11.296 -7.346  8.798   0.42 15.23 ?  19  LYS   A H    1 
ATOM   512  H H    B LYS   A 1 19  ? 11.364 -7.381  8.811   0.58 15.12 ?  19  LYS   A H    1 
ATOM   513  H HA   A LYS   A 1 19  ? 9.127  -7.158  10.369  0.42 16.18 ?  19  LYS   A HA   1 
ATOM   514  H HA   B LYS   A 1 19  ? 9.092  -7.201  10.244  0.58 15.99 ?  19  LYS   A HA   1 
ATOM   515  H HB2  A LYS   A 1 19  ? 10.769 -7.298  12.013  0.42 17.15 ?  19  LYS   A HB2  1 
ATOM   516  H HB2  B LYS   A 1 19  ? 10.893 -7.089  11.817  0.58 16.64 ?  19  LYS   A HB2  1 
ATOM   517  H HB3  A LYS   A 1 19  ? 11.613 -6.167  11.297  0.42 17.15 ?  19  LYS   A HB3  1 
ATOM   518  H HB3  B LYS   A 1 19  ? 11.412 -5.801  11.060  0.58 16.64 ?  19  LYS   A HB3  1 
ATOM   519  H HG2  A LYS   A 1 19  ? 9.918  -4.609  11.896  0.42 18.05 ?  19  LYS   A HG2  1 
ATOM   520  H HG2  B LYS   A 1 19  ? 9.567  -4.608  11.785  0.58 18.56 ?  19  LYS   A HG2  1 
ATOM   521  H HG3  A LYS   A 1 19  ? 9.229  -5.772  12.743  0.42 18.05 ?  19  LYS   A HG3  1 
ATOM   522  H HG3  B LYS   A 1 19  ? 9.005  -5.913  12.515  0.58 18.56 ?  19  LYS   A HG3  1 
ATOM   523  H HD2  A LYS   A 1 19  ? 11.220 -5.940  14.017  0.42 18.07 ?  19  LYS   A HD2  1 
ATOM   524  H HD2  B LYS   A 1 19  ? 10.834 -5.924  13.943  0.58 20.28 ?  19  LYS   A HD2  1 
ATOM   525  H HD3  A LYS   A 1 19  ? 11.791 -4.683  13.230  0.42 18.07 ?  19  LYS   A HD3  1 
ATOM   526  H HD3  B LYS   A 1 19  ? 11.450 -4.666  13.190  0.58 20.28 ?  19  LYS   A HD3  1 
ATOM   527  H HE2  A LYS   A 1 19  ? 10.211 -3.313  14.185  0.42 18.54 ?  19  LYS   A HE2  1 
ATOM   528  H HE2  B LYS   A 1 19  ? 9.641  -3.370  13.945  0.58 21.15 ?  19  LYS   A HE2  1 
ATOM   529  H HE3  A LYS   A 1 19  ? 9.509  -4.563  14.883  0.42 18.54 ?  19  LYS   A HE3  1 
ATOM   530  H HE3  B LYS   A 1 19  ? 9.113  -4.629  14.766  0.58 21.15 ?  19  LYS   A HE3  1 
ATOM   531  H HZ1  A LYS   A 1 19  ? 10.874 -3.476  16.358  0.42 19.09 ?  19  LYS   A HZ1  1 
ATOM   532  H HZ1  B LYS   A 1 19  ? 10.316 -3.247  16.113  0.58 21.58 ?  19  LYS   A HZ1  1 
ATOM   533  H HZ2  A LYS   A 1 19  ? 11.381 -4.818  16.154  0.42 19.09 ?  19  LYS   A HZ2  1 
ATOM   534  H HZ2  B LYS   A 1 19  ? 11.010 -4.516  16.019  0.58 21.58 ?  19  LYS   A HZ2  1 
ATOM   535  H HZ3  A LYS   A 1 19  ? 12.030 -3.693  15.513  0.42 19.09 ?  19  LYS   A HZ3  1 
ATOM   536  H HZ3  B LYS   A 1 19  ? 11.489 -3.370  15.272  0.58 21.58 ?  19  LYS   A HZ3  1 
ATOM   537  N N    A ASN   A 1 20  ? 8.639  -4.879  9.492   0.42 13.28 ?  20  ASN   A N    1 
ATOM   538  N N    B ASN   A 1 20  ? 8.539  -4.997  9.187   0.58 14.00 ?  20  ASN   A N    1 
ATOM   539  C CA   A ASN   A 1 20  ? 8.426  -3.542  8.943   0.42 12.95 ?  20  ASN   A CA   1 
ATOM   540  C CA   B ASN   A 1 20  ? 8.277  -3.736  8.498   0.58 14.34 ?  20  ASN   A CA   1 
ATOM   541  C C    A ASN   A 1 20  ? 9.061  -2.543  9.899   0.42 12.73 ?  20  ASN   A C    1 
ATOM   542  C C    B ASN   A 1 20  ? 8.859  -2.633  9.371   0.58 14.45 ?  20  ASN   A C    1 
ATOM   543  O O    A ASN   A 1 20  ? 8.566  -2.335  11.011  0.42 13.08 ?  20  ASN   A O    1 
ATOM   544  O O    B ASN   A 1 20  ? 8.254  -2.231  10.368  0.58 15.72 ?  20  ASN   A O    1 
ATOM   545  C CB   A ASN   A 1 20  ? 6.936  -3.258  8.752   0.42 13.27 ?  20  ASN   A CB   1 
ATOM   546  C CB   B ASN   A 1 20  ? 6.777  -3.554  8.272   0.58 14.80 ?  20  ASN   A CB   1 
ATOM   547  C CG   A ASN   A 1 20  ? 6.645  -1.806  8.369   0.42 14.25 ?  20  ASN   A CG   1 
ATOM   548  C CG   B ASN   A 1 20  ? 6.417  -2.166  7.753   0.58 15.94 ?  20  ASN   A CG   1 
ATOM   549  O OD1  A ASN   A 1 20  ? 5.744  -1.181  8.931   0.42 15.41 ?  20  ASN   A OD1  1 
ATOM   550  O OD1  B ASN   A 1 20  ? 5.401  -1.582  8.153   0.58 17.72 ?  20  ASN   A OD1  1 
ATOM   551  N ND2  A ASN   A 1 20  ? 7.401  -1.269  7.414   0.42 14.78 ?  20  ASN   A ND2  1 
ATOM   552  N ND2  B ASN   A 1 20  ? 7.244  -1.634  6.856   0.58 16.08 ?  20  ASN   A ND2  1 
ATOM   553  H H    A ASN   A 1 20  ? 7.940  -5.214  9.875   0.42 15.97 ?  20  ASN   A H    1 
ATOM   554  H H    B ASN   A 1 20  ? 7.865  -5.309  9.635   0.58 16.82 ?  20  ASN   A H    1 
ATOM   555  H HA   A ASN   A 1 20  ? 8.862  -3.471  8.084   0.42 15.57 ?  20  ASN   A HA   1 
ATOM   556  H HA   B ASN   A 1 20  ? 8.724  -3.739  7.636   0.58 17.24 ?  20  ASN   A HA   1 
ATOM   557  H HB2  A ASN   A 1 20  ? 6.593  -3.825  8.044   0.42 15.95 ?  20  ASN   A HB2  1 
ATOM   558  H HB2  B ASN   A 1 20  ? 6.473  -4.204  7.617   0.58 17.78 ?  20  ASN   A HB2  1 
ATOM   559  H HB3  A ASN   A 1 20  ? 6.466  -3.441  9.581   0.42 15.95 ?  20  ASN   A HB3  1 
ATOM   560  H HB3  B ASN   A 1 20  ? 6.311  -3.699  9.110   0.58 17.78 ?  20  ASN   A HB3  1 
ATOM   561  H HD21 A ASN   A 1 20  ? 7.266  -0.455  7.162   0.42 17.76 ?  20  ASN   A HD21 1 
ATOM   562  H HD21 B ASN   A 1 20  ? 7.080  -0.856  6.538   0.58 19.32 ?  20  ASN   A HD21 1 
ATOM   563  H HD22 A ASN   A 1 20  ? 8.020  -1.735  7.045   0.42 17.76 ?  20  ASN   A HD22 1 
ATOM   564  H HD22 B ASN   A 1 20  ? 7.939  -2.070  6.595   0.58 19.32 ?  20  ASN   A HD22 1 
ATOM   565  N N    A ALA   A 1 21  ? 10.169 -1.938  9.482   0.42 12.68 ?  21  ALA   A N    1 
ATOM   566  N N    B ALA   A 1 21  ? 10.051 -2.154  9.010   0.58 13.54 ?  21  ALA   A N    1 
ATOM   567  C CA   A ALA   A 1 21  ? 10.853 -0.997  10.356  0.42 13.36 ?  21  ALA   A CA   1 
ATOM   568  C CA   B ALA   A 1 21  ? 10.754 -1.179  9.834   0.58 13.25 ?  21  ALA   A CA   1 
ATOM   569  C C    A ALA   A 1 21  ? 11.847 -0.185  9.546   0.42 13.55 ?  21  ALA   A C    1 
ATOM   570  C C    B ALA   A 1 21  ? 11.781 -0.432  8.995   0.58 11.92 ?  21  ALA   A C    1 
ATOM   571  O O    A ALA   A 1 21  ? 12.335 -0.635  8.505   0.42 13.89 ?  21  ALA   A O    1 
ATOM   572  O O    B ALA   A 1 21  ? 12.249 -0.925  7.966   0.58 11.90 ?  21  ALA   A O    1 
ATOM   573  C CB   A ALA   A 1 21  ? 11.577 -1.728  11.488  0.42 14.56 ?  21  ALA   A CB   1 
ATOM   574  C CB   B ALA   A 1 21  ? 11.442 -1.853  11.027  0.58 14.64 ?  21  ALA   A CB   1 
ATOM   575  H H    A ALA   A 1 21  ? 10.540 -2.051  8.712   0.42 15.24 ?  21  ALA   A H    1 
ATOM   576  H H    B ALA   A 1 21  ? 10.462 -2.382  8.290   0.58 16.27 ?  21  ALA   A H    1 
ATOM   577  H HA   A ALA   A 1 21  ? 10.207 -0.384  10.742  0.42 16.06 ?  21  ALA   A HA   1 
ATOM   578  H HA   B ALA   A 1 21  ? 10.108 -0.542  10.174  0.58 15.93 ?  21  ALA   A HA   1 
ATOM   579  H HB1  A ALA   A 1 21  ? 11.941 -1.068  12.093  0.42 17.50 ?  21  ALA   A HB1  1 
ATOM   580  H HB1  B ALA   A 1 21  ? 11.883 -1.170  11.555  0.58 17.59 ?  21  ALA   A HB1  1 
ATOM   581  H HB2  A ALA   A 1 21  ? 10.934 -2.287  11.951  0.42 17.50 ?  21  ALA   A HB2  1 
ATOM   582  H HB2  B ALA   A 1 21  ? 10.769 -2.304  11.568  0.58 17.59 ?  21  ALA   A HB2  1 
ATOM   583  H HB3  A ALA   A 1 21  ? 12.281 -2.271  11.109  0.42 17.50 ?  21  ALA   A HB3  1 
ATOM   584  H HB3  B ALA   A 1 21  ? 12.087 -2.495  10.701  0.58 17.59 ?  21  ALA   A HB3  1 
ATOM   585  N N    A ASP   A 1 22  ? 12.124 1.021   10.037  0.42 14.09 ?  22  ASP   A N    1 
ATOM   586  N N    B ASP   A 1 22  ? 12.115 0.773   9.463   0.58 11.56 ?  22  ASP   A N    1 
ATOM   587  C CA   A ASP   A 1 22  ? 13.195 1.858   9.518   0.42 14.56 ?  22  ASP   A CA   1 
ATOM   588  C CA   B ASP   A 1 22  ? 13.216 1.571   8.935   0.58 11.02 ?  22  ASP   A CA   1 
ATOM   589  C C    A ASP   A 1 22  ? 14.516 1.354   10.085  0.42 13.70 ?  22  ASP   A C    1 
ATOM   590  C C    B ASP   A 1 22  ? 14.508 1.077   9.577   0.58 10.61 ?  22  ASP   A C    1 
ATOM   591  O O    A ASP   A 1 22  ? 14.704 1.344   11.306  0.42 13.79 ?  22  ASP   A O    1 
ATOM   592  O O    B ASP   A 1 22  ? 14.634 1.093   10.807  0.58 11.05 ?  22  ASP   A O    1 
ATOM   593  C CB   A ASP   A 1 22  ? 12.948 3.298   9.964   0.42 15.76 ?  22  ASP   A CB   1 
ATOM   594  C CB   B ASP   A 1 22  ? 12.966 3.030   9.316   0.58 12.00 ?  22  ASP   A CB   1 
ATOM   595  C CG   A ASP   A 1 22  ? 13.998 4.267   9.444   0.42 16.44 ?  22  ASP   A CG   1 
ATOM   596  C CG   B ASP   A 1 22  ? 13.982 3.997   8.728   0.58 13.00 ?  22  ASP   A CG   1 
ATOM   597  O OD1  A ASP   A 1 22  ? 14.982 3.830   8.810   0.42 16.53 ?  22  ASP   A OD1  1 
ATOM   598  O OD1  B ASP   A 1 22  ? 15.123 3.594   8.409   0.58 12.28 ?  22  ASP   A OD1  1 
ATOM   599  O OD2  A ASP   A 1 22  ? 13.830 5.483   9.666   0.42 17.38 -1 22  ASP   A OD2  1 
ATOM   600  O OD2  B ASP   A 1 22  ? 13.626 5.186   8.590   0.58 15.58 -1 22  ASP   A OD2  1 
ATOM   601  H H    A ASP   A 1 22  ? 11.688 1.386   10.683  0.42 16.93 ?  22  ASP   A H    1 
ATOM   602  H H    B ASP   A 1 22  ? 11.693 1.154   10.110  0.58 13.90 ?  22  ASP   A H    1 
ATOM   603  H HA   A ASP   A 1 22  ? 13.222 1.822   8.548   0.42 17.50 ?  22  ASP   A HA   1 
ATOM   604  H HA   B ASP   A 1 22  ? 13.266 1.474   7.973   0.58 13.25 ?  22  ASP   A HA   1 
ATOM   605  H HB2  A ASP   A 1 22  ? 12.082 3.587   9.634   0.42 18.94 ?  22  ASP   A HB2  1 
ATOM   606  H HB2  B ASP   A 1 22  ? 12.096 3.290   8.995   0.58 14.43 ?  22  ASP   A HB2  1 
ATOM   607  H HB3  A ASP   A 1 22  ? 12.948 3.327   10.940  0.42 18.94 ?  22  ASP   A HB3  1 
ATOM   608  H HB3  B ASP   A 1 22  ? 13.002 3.104   10.285  0.58 14.43 ?  22  ASP   A HB3  1 
ATOM   609  N N    A ILE   A 1 23  ? 15.429 0.931   9.204   0.42 12.88 ?  23  ILE   A N    1 
ATOM   610  N N    B ILE   A 1 23  ? 15.459 0.613   8.755   0.58 10.60 ?  23  ILE   A N    1 
ATOM   611  C CA   A ILE   A 1 23  ? 16.698 0.366   9.660   0.42 12.15 ?  23  ILE   A CA   1 
ATOM   612  C CA   B ILE   A 1 23  ? 16.701 0.052   9.288   0.58 10.42 ?  23  ILE   A CA   1 
ATOM   613  C C    A ILE   A 1 23  ? 17.454 1.354   10.537  0.42 12.12 ?  23  ILE   A C    1 
ATOM   614  C C    B ILE   A 1 23  ? 17.408 1.044   10.201  0.58 10.64 ?  23  ILE   A C    1 
ATOM   615  O O    A ILE   A 1 23  ? 18.197 0.951   11.441  0.42 12.59 ?  23  ILE   A O    1 
ATOM   616  O O    B ILE   A 1 23  ? 18.077 0.644   11.160  0.58 10.94 ?  23  ILE   A O    1 
ATOM   617  C CB   A ILE   A 1 23  ? 17.539 -0.132  8.463   0.42 11.97 ?  23  ILE   A CB   1 
ATOM   618  C CB   B ILE   A 1 23  ? 17.627 -0.472  8.163   0.58 10.43 ?  23  ILE   A CB   1 
ATOM   619  C CG1  A ILE   A 1 23  ? 18.697 -1.016  8.944   0.42 12.44 ?  23  ILE   A CG1  1 
ATOM   620  C CG1  B ILE   A 1 23  ? 18.671 -1.428  8.755   0.58 11.08 ?  23  ILE   A CG1  1 
ATOM   621  C CG2  A ILE   A 1 23  ? 18.041 1.042   7.621   0.42 11.84 ?  23  ILE   A CG2  1 
ATOM   622  C CG2  B ILE   A 1 23  ? 18.305 0.680   7.410   0.58 10.52 ?  23  ILE   A CG2  1 
ATOM   623  C CD1  A ILE   A 1 23  ? 19.409 -1.752  7.819   0.42 12.72 ?  23  ILE   A CD1  1 
ATOM   624  C CD1  B ILE   A 1 23  ? 19.619 -2.015  7.737   0.58 11.15 ?  23  ILE   A CD1  1 
ATOM   625  H H    A ILE   A 1 23  ? 15.335 0.959   8.352   0.42 15.48 ?  23  ILE   A H    1 
ATOM   626  H H    B ILE   A 1 23  ? 15.402 0.595   7.905   0.58 12.75 ?  23  ILE   A H    1 
ATOM   627  H HA   A ILE   A 1 23  ? 16.506 -0.405  10.210  0.42 14.60 ?  23  ILE   A HA   1 
ATOM   628  H HA   B ILE   A 1 23  ? 16.469 -0.725  9.823   0.58 12.54 ?  23  ILE   A HA   1 
ATOM   629  H HB   A ILE   A 1 23  ? 16.967 -0.673  7.902   0.42 14.39 ?  23  ILE   A HB   1 
ATOM   630  H HB   B ILE   A 1 23  ? 17.095 -0.974  7.523   0.58 12.54 ?  23  ILE   A HB   1 
ATOM   631  H HG12 A ILE   A 1 23  ? 19.353 -0.463  9.396   0.42 14.95 ?  23  ILE   A HG12 1 
ATOM   632  H HG12 B ILE   A 1 23  ? 19.203 -0.948  9.408   0.58 13.32 ?  23  ILE   A HG12 1 
ATOM   633  H HG13 A ILE   A 1 23  ? 18.350 -1.682  9.558   0.42 14.95 ?  23  ILE   A HG13 1 
ATOM   634  H HG13 B ILE   A 1 23  ? 18.212 -2.167  9.185   0.58 13.32 ?  23  ILE   A HG13 1 
ATOM   635  H HG21 A ILE   A 1 23  ? 18.417 0.699   6.793   0.42 14.24 ?  23  ILE   A HG21 1 
ATOM   636  H HG21 B ILE   A 1 23  ? 18.698 0.337   6.588   0.58 12.65 ?  23  ILE   A HG21 1 
ATOM   637  H HG22 A ILE   A 1 23  ? 17.295 1.630   7.424   0.42 14.24 ?  23  ILE   A HG22 1 
ATOM   638  H HG22 B ILE   A 1 23  ? 17.641 1.352   7.202   0.58 12.65 ?  23  ILE   A HG22 1 
ATOM   639  H HG23 A ILE   A 1 23  ? 18.721 1.524   8.116   0.42 14.24 ?  23  ILE   A HG23 1 
ATOM   640  H HG23 B ILE   A 1 23  ? 19.000 1.060   7.970   0.58 12.65 ?  23  ILE   A HG23 1 
ATOM   641  H HD11 A ILE   A 1 23  ? 20.092 -2.329  8.199   0.42 15.30 ?  23  ILE   A HD11 1 
ATOM   642  H HD11 B ILE   A 1 23  ? 20.162 -2.697  8.168   0.58 13.41 ?  23  ILE   A HD11 1 
ATOM   643  H HD12 A ILE   A 1 23  ? 18.762 -2.285  7.330   0.42 15.30 ?  23  ILE   A HD12 1 
ATOM   644  H HD12 B ILE   A 1 23  ? 19.107 -2.407  7.016   0.58 13.41 ?  23  ILE   A HD12 1 
ATOM   645  H HD13 A ILE   A 1 23  ? 19.819 -1.103  7.225   0.42 15.30 ?  23  ILE   A HD13 1 
ATOM   646  H HD13 B ILE   A 1 23  ? 20.192 -1.310  7.394   0.58 13.41 ?  23  ILE   A HD13 1 
ATOM   647  N N    A VAL   A 1 24  ? 17.279 2.654   10.296  0.42 12.49 ?  24  VAL   A N    1 
ATOM   648  N N    B VAL   A 1 24  ? 17.285 2.343   9.920   0.58 11.17 ?  24  VAL   A N    1 
ATOM   649  C CA   A VAL   A 1 24  ? 17.943 3.660   11.122  0.42 13.13 ?  24  VAL   A CA   1 
ATOM   650  C CA   B VAL   A 1 24  ? 17.940 3.346   10.755  0.58 12.22 ?  24  VAL   A CA   1 
ATOM   651  C C    A VAL   A 1 24  ? 17.434 3.591   12.555  0.42 13.96 ?  24  VAL   A C    1 
ATOM   652  C C    B VAL   A 1 24  ? 17.346 3.347   12.157  0.58 12.63 ?  24  VAL   A C    1 
ATOM   653  O O    A VAL   A 1 24  ? 18.216 3.540   13.513  0.42 14.07 ?  24  VAL   A O    1 
ATOM   654  O O    B VAL   A 1 24  ? 18.074 3.409   13.155  0.58 13.19 ?  24  VAL   A O    1 
ATOM   655  C CB   A VAL   A 1 24  ? 17.746 5.062   10.522  0.42 13.16 ?  24  VAL   A CB   1 
ATOM   656  C CB   B VAL   A 1 24  ? 17.853 4.733   10.096  0.58 12.75 ?  24  VAL   A CB   1 
ATOM   657  C CG1  A VAL   A 1 24  ? 18.185 6.125   11.518  0.42 13.25 ?  24  VAL   A CG1  1 
ATOM   658  C CG1  B VAL   A 1 24  ? 18.561 5.762   10.955  0.58 14.05 ?  24  VAL   A CG1  1 
ATOM   659  C CG2  A VAL   A 1 24  ? 18.507 5.187   9.213   0.42 13.32 ?  24  VAL   A CG2  1 
ATOM   660  C CG2  B VAL   A 1 24  ? 18.445 4.698   8.699   0.58 13.57 ?  24  VAL   A CG2  1 
ATOM   661  H H    A VAL   A 1 24  ? 16.787 2.978   9.667   0.42 15.02 ?  24  VAL   A H    1 
ATOM   662  H H    B VAL   A 1 24  ? 16.831 2.657   9.263   0.58 13.43 ?  24  VAL   A H    1 
ATOM   663  H HA   A VAL   A 1 24  ? 18.894 3.478   11.135  0.42 15.78 ?  24  VAL   A HA   1 
ATOM   664  H HA   B VAL   A 1 24  ? 18.875 3.114   10.837  0.58 14.70 ?  24  VAL   A HA   1 
ATOM   665  H HB   A VAL   A 1 24  ? 16.802 5.199   10.334  0.42 15.82 ?  24  VAL   A HB   1 
ATOM   666  H HB   B VAL   A 1 24  ? 16.918 4.989   10.023  0.58 15.32 ?  24  VAL   A HB   1 
ATOM   667  H HG11 A VAL   A 1 24  ? 18.340 6.955   11.043  0.42 15.93 ?  24  VAL   A HG11 1 
ATOM   668  H HG11 B VAL   A 1 24  ? 18.659 6.579   10.446  0.58 16.89 ?  24  VAL   A HG11 1 
ATOM   669  H HG12 A VAL   A 1 24  ? 17.488 6.249   12.181  0.42 15.93 ?  24  VAL   A HG12 1 
ATOM   670  H HG12 B VAL   A 1 24  ? 18.031 5.930   11.752  0.58 16.89 ?  24  VAL   A HG12 1 
ATOM   671  H HG13 A VAL   A 1 24  ? 19.005 5.833   11.947  0.42 15.93 ?  24  VAL   A HG13 1 
ATOM   672  H HG13 B VAL   A 1 24  ? 19.432 5.417   11.203  0.58 16.89 ?  24  VAL   A HG13 1 
ATOM   673  H HG21 A VAL   A 1 24  ? 18.284 6.033   8.795   0.42 16.01 ?  24  VAL   A HG21 1 
ATOM   674  H HG21 B VAL   A 1 24  ? 18.472 5.598   8.346   0.58 16.31 ?  24  VAL   A HG21 1 
ATOM   675  H HG22 A VAL   A 1 24  ? 19.459 5.151   9.398   0.42 16.01 ?  24  VAL   A HG22 1 
ATOM   676  H HG22 B VAL   A 1 24  ? 19.343 4.332   8.749   0.58 16.31 ?  24  VAL   A HG22 1 
ATOM   677  H HG23 A VAL   A 1 24  ? 18.256 4.454   8.628   0.42 16.01 ?  24  VAL   A HG23 1 
ATOM   678  H HG23 B VAL   A 1 24  ? 17.892 4.134   8.134   0.58 16.31 ?  24  VAL   A HG23 1 
ATOM   679  N N    A GLU   A 1 25  ? 16.110 3.614   12.724  0.42 14.71 ?  25  GLU   A N    1 
ATOM   680  N N    B GLU   A 1 25  ? 16.014 3.280   12.257  0.58 13.46 ?  25  GLU   A N    1 
ATOM   681  C CA   A GLU   A 1 25  ? 15.539 3.544   14.063  0.42 16.21 ?  25  GLU   A CA   1 
ATOM   682  C CA   B GLU   A 1 25  ? 15.373 3.237   13.569  0.58 14.09 ?  25  GLU   A CA   1 
ATOM   683  C C    A GLU   A 1 25  ? 15.755 2.175   14.693  0.42 15.16 ?  25  GLU   A C    1 
ATOM   684  C C    B GLU   A 1 25  ? 15.663 1.925   14.283  0.58 13.66 ?  25  GLU   A C    1 
ATOM   685  O O    A GLU   A 1 25  ? 15.951 2.082   15.911  0.42 15.24 ?  25  GLU   A O    1 
ATOM   686  O O    B GLU   A 1 25  ? 15.900 1.915   15.497  0.58 14.43 ?  25  GLU   A O    1 
ATOM   687  C CB   A GLU   A 1 25  ? 14.053 3.904   14.025  0.42 18.73 ?  25  GLU   A CB   1 
ATOM   688  C CB   B GLU   A 1 25  ? 13.866 3.478   13.439  0.58 16.05 ?  25  GLU   A CB   1 
ATOM   689  C CG   A GLU   A 1 25  ? 13.794 5.364   13.680  0.42 21.07 ?  25  GLU   A CG   1 
ATOM   690  C CG   B GLU   A 1 25  ? 13.516 4.891   13.008  0.58 19.75 ?  25  GLU   A CG   1 
ATOM   691  C CD   A GLU   A 1 25  ? 14.581 6.329   14.556  0.42 23.03 ?  25  GLU   A CD   1 
ATOM   692  C CD   B GLU   A 1 25  ? 14.150 5.946   13.887  0.58 23.27 ?  25  GLU   A CD   1 
ATOM   693  O OE1  A GLU   A 1 25  ? 14.636 6.115   15.787  0.42 23.58 ?  25  GLU   A OE1  1 
ATOM   694  O OE1  B GLU   A 1 25  ? 14.155 5.764   15.123  0.58 24.99 ?  25  GLU   A OE1  1 
ATOM   695  O OE2  A GLU   A 1 25  ? 15.163 7.288   14.009  0.42 23.99 -1 25  GLU   A OE2  1 
ATOM   696  O OE2  B GLU   A 1 25  ? 14.652 6.949   13.340  0.58 24.55 -1 25  GLU   A OE2  1 
ATOM   697  H H    A GLU   A 1 25  ? 15.533 3.675   12.087  0.42 17.68 ?  25  GLU   A H    1 
ATOM   698  H H    B GLU   A 1 25  ? 15.468 3.259   11.591  0.58 16.18 ?  25  GLU   A H    1 
ATOM   699  H HA   A GLU   A 1 25  ? 15.992 4.190   14.624  0.42 19.48 ?  25  GLU   A HA   1 
ATOM   700  H HA   B GLU   A 1 25  ? 15.746 3.937   14.117  0.58 16.94 ?  25  GLU   A HA   1 
ATOM   701  H HB2  A GLU   A 1 25  ? 13.613 3.355   13.354  0.42 22.50 ?  25  GLU   A HB2  1 
ATOM   702  H HB2  B GLU   A 1 25  ? 13.505 2.871   12.775  0.58 19.29 ?  25  GLU   A HB2  1 
ATOM   703  H HB3  A GLU   A 1 25  ? 13.665 3.730   14.897  0.42 22.50 ?  25  GLU   A HB3  1 
ATOM   704  H HB3  B GLU   A 1 25  ? 13.447 3.316   14.298  0.58 19.29 ?  25  GLU   A HB3  1 
ATOM   705  H HG2  A GLU   A 1 25  ? 14.059 5.518   12.761  0.42 25.31 ?  25  GLU   A HG2  1 
ATOM   706  H HG2  B GLU   A 1 25  ? 13.833 5.037   12.106  0.58 23.72 ?  25  GLU   A HG2  1 
ATOM   707  H HG3  A GLU   A 1 25  ? 12.848 5.547   13.792  0.42 25.31 ?  25  GLU   A HG3  1 
ATOM   708  H HG3  B GLU   A 1 25  ? 12.558 5.011   13.056  0.58 23.72 ?  25  GLU   A HG3  1 
ATOM   709  N N    A GLU   A 1 26  ? 15.733 1.110   13.889  0.42 14.79 ?  26  GLU   A N    1 
ATOM   710  N N    B GLU   A 1 26  ? 15.656 0.809   13.549  0.58 13.76 ?  26  GLU   A N    1 
ATOM   711  C CA   A GLU   A 1 26  ? 16.043 -0.216  14.416  0.42 14.68 ?  26  GLU   A CA   1 
ATOM   712  C CA   B GLU   A 1 26  ? 16.009 -0.470  14.159  0.58 14.45 ?  26  GLU   A CA   1 
ATOM   713  C C    A GLU   A 1 26  ? 17.461 -0.256  14.972  0.42 14.47 ?  26  GLU   A C    1 
ATOM   714  C C    B GLU   A 1 26  ? 17.425 -0.431  14.716  0.58 12.87 ?  26  GLU   A C    1 
ATOM   715  O O    A GLU   A 1 26  ? 17.686 -0.699  16.104  0.42 14.74 ?  26  GLU   A O    1 
ATOM   716  O O    B GLU   A 1 26  ? 17.691 -0.952  15.805  0.58 13.63 ?  26  GLU   A O    1 
ATOM   717  C CB   A GLU   A 1 26  ? 15.879 -1.273  13.320  0.42 15.90 ?  26  GLU   A CB   1 
ATOM   718  C CB   B GLU   A 1 26  ? 15.889 -1.598  13.129  0.58 16.39 ?  26  GLU   A CB   1 
ATOM   719  C CG   A GLU   A 1 26  ? 14.488 -1.834  13.167  0.42 17.93 ?  26  GLU   A CG   1 
ATOM   720  C CG   B GLU   A 1 26  ? 14.485 -2.100  12.886  0.58 18.06 ?  26  GLU   A CG   1 
ATOM   721  C CD   A GLU   A 1 26  ? 14.074 -2.696  14.351  0.42 18.93 ?  26  GLU   A CD   1 
ATOM   722  C CD   B GLU   A 1 26  ? 13.845 -2.669  14.130  0.58 19.06 ?  26  GLU   A CD   1 
ATOM   723  O OE1  A GLU   A 1 26  ? 14.400 -3.908  14.381  0.42 19.22 ?  26  GLU   A OE1  1 
ATOM   724  O OE1  B GLU   A 1 26  ? 14.427 -3.603  14.728  0.58 19.46 ?  26  GLU   A OE1  1 
ATOM   725  O OE2  A GLU   A 1 26  ? 13.434 -2.152  15.265  0.42 19.05 -1 26  GLU   A OE2  1 
ATOM   726  O OE2  B GLU   A 1 26  ? 12.771 -2.165  14.512  0.58 18.36 -1 26  GLU   A OE2  1 
ATOM   727  H H    A GLU   A 1 26  ? 15.553 1.134   13.048  0.42 17.78 ?  26  GLU   A H    1 
ATOM   728  H H    B GLU   A 1 26  ? 15.452 0.765   12.710  0.58 16.54 ?  26  GLU   A H    1 
ATOM   729  H HA   A GLU   A 1 26  ? 15.430 -0.422  15.133  0.42 17.64 ?  26  GLU   A HA   1 
ATOM   730  H HA   B GLU   A 1 26  ? 15.397 -0.657  14.886  0.58 17.36 ?  26  GLU   A HA   1 
ATOM   731  H HB2  A GLU   A 1 26  ? 16.129 -0.877  12.470  0.42 19.11 ?  26  GLU   A HB2  1 
ATOM   732  H HB2  B GLU   A 1 26  ? 16.231 -1.280  12.276  0.58 19.69 ?  26  GLU   A HB2  1 
ATOM   733  H HB3  A GLU   A 1 26  ? 16.469 -2.014  13.519  0.42 19.11 ?  26  GLU   A HB3  1 
ATOM   734  H HB3  B GLU   A 1 26  ? 16.422 -2.352  13.428  0.58 19.69 ?  26  GLU   A HB3  1 
ATOM   735  H HG2  A GLU   A 1 26  ? 13.869 -1.090  13.069  0.42 21.55 ?  26  GLU   A HG2  1 
ATOM   736  H HG2  B GLU   A 1 26  ? 13.937 -1.366  12.574  0.58 21.70 ?  26  GLU   A HG2  1 
ATOM   737  H HG3  A GLU   A 1 26  ? 14.458 -2.392  12.376  0.42 21.55 ?  26  GLU   A HG3  1 
ATOM   738  H HG3  B GLU   A 1 26  ? 14.508 -2.808  12.227  0.58 21.70 ?  26  GLU   A HG3  1 
ATOM   739  N N    A ALA   A 1 27  ? 18.434 0.212   14.187  0.42 14.70 ?  27  ALA   A N    1 
ATOM   740  N N    B ALA   A 1 27  ? 18.354 0.176   13.977  0.58 11.67 ?  27  ALA   A N    1 
ATOM   741  C CA   A ALA   A 1 27  ? 19.826 0.142   14.622  0.42 15.22 ?  27  ALA   A CA   1 
ATOM   742  C CA   B ALA   A 1 27  ? 19.733 0.246   14.446  0.58 11.46 ?  27  ALA   A CA   1 
ATOM   743  C C    A ALA   A 1 27  ? 20.048 0.938   15.903  0.42 16.82 ?  27  ALA   A C    1 
ATOM   744  C C    B ALA   A 1 27  ? 19.843 1.107   15.698  0.58 12.16 ?  27  ALA   A C    1 
ATOM   745  O O    A ALA   A 1 27  ? 20.736 0.473   16.820  0.42 16.79 ?  27  ALA   A O    1 
ATOM   746  O O    B ALA   A 1 27  ? 20.489 0.719   16.679  0.58 12.59 ?  27  ALA   A O    1 
ATOM   747  C CB   A ALA   A 1 27  ? 20.757 0.624   13.507  0.42 14.78 ?  27  ALA   A CB   1 
ATOM   748  C CB   B ALA   A 1 27  ? 20.637 0.784   13.336  0.58 11.26 ?  27  ALA   A CB   1 
ATOM   749  H H    A ALA   A 1 27  ? 18.315 0.574   13.414  0.42 17.67 ?  27  ALA   A H    1 
ATOM   750  H H    B ALA   A 1 27  ? 18.208 0.549   13.214  0.58 14.03 ?  27  ALA   A H    1 
ATOM   751  H HA   A ALA   A 1 27  ? 20.046 -0.780  14.807  0.42 18.29 ?  27  ALA   A HA   1 
ATOM   752  H HA   B ALA   A 1 27  ? 20.030 -0.646  14.668  0.58 13.78 ?  27  ALA   A HA   1 
ATOM   753  H HB1  A ALA   A 1 27  ? 21.676 0.570   13.817  0.42 17.77 ?  27  ALA   A HB1  1 
ATOM   754  H HB1  B ALA   A 1 27  ? 21.546 0.824   13.666  0.58 13.54 ?  27  ALA   A HB1  1 
ATOM   755  H HB2  A ALA   A 1 27  ? 20.639 0.056   12.728  0.42 17.77 ?  27  ALA   A HB2  1 
ATOM   756  H HB2  B ALA   A 1 27  ? 20.584 0.192   12.571  0.58 13.54 ?  27  ALA   A HB2  1 
ATOM   757  H HB3  A ALA   A 1 27  ? 20.539 1.542   13.281  0.42 17.77 ?  27  ALA   A HB3  1 
ATOM   758  H HB3  B ALA   A 1 27  ? 20.335 1.674   13.087  0.58 13.54 ?  27  ALA   A HB3  1 
ATOM   759  N N    A LYS   A 1 28  ? 19.459 2.134   15.995  0.42 18.96 ?  28  LYS   A N    1 
ATOM   760  N N    B LYS   A 1 28  ? 19.200 2.278   15.692  0.58 13.53 ?  28  LYS   A N    1 
ATOM   761  C CA   A LYS   A 1 28  ? 19.633 2.943   17.198  0.42 21.58 ?  28  LYS   A CA   1 
ATOM   762  C CA   B LYS   A 1 28  ? 19.277 3.163   16.850  0.58 16.47 ?  28  LYS   A CA   1 
ATOM   763  C C    A LYS   A 1 28  ? 19.070 2.246   18.431  0.42 22.35 ?  28  LYS   A C    1 
ATOM   764  C C    B LYS   A 1 28  ? 18.726 2.497   18.103  0.58 17.31 ?  28  LYS   A C    1 
ATOM   765  O O    A LYS   A 1 28  ? 19.615 2.398   19.530  0.42 22.90 ?  28  LYS   A O    1 
ATOM   766  O O    B LYS   A 1 28  ? 19.265 2.683   19.200  0.58 18.42 ?  28  LYS   A O    1 
ATOM   767  C CB   A LYS   A 1 28  ? 19.008 4.328   17.007  0.42 23.63 ?  28  LYS   A CB   1 
ATOM   768  C CB   B LYS   A 1 28  ? 18.550 4.477   16.563  0.58 19.17 ?  28  LYS   A CB   1 
ATOM   769  C CG   A LYS   A 1 28  ? 19.854 5.262   16.154  0.42 25.68 ?  28  LYS   A CG   1 
ATOM   770  C CG   B LYS   A 1 28  ? 19.359 5.432   15.711  0.58 22.49 ?  28  LYS   A CG   1 
ATOM   771  C CD   A LYS   A 1 28  ? 19.350 6.695   16.200  0.42 27.50 ?  28  LYS   A CD   1 
ATOM   772  C CD   B LYS   A 1 28  ? 18.822 6.850   15.770  0.58 26.13 ?  28  LYS   A CD   1 
ATOM   773  C CE   A LYS   A 1 28  ? 18.035 6.849   15.458  0.42 28.68 ?  28  LYS   A CE   1 
ATOM   774  C CE   B LYS   A 1 28  ? 17.549 6.998   14.963  0.58 28.53 ?  28  LYS   A CE   1 
ATOM   775  N NZ   A LYS   A 1 28  ? 17.623 8.277   15.362  0.42 29.48 ?  28  LYS   A NZ   1 
ATOM   776  N NZ   B LYS   A 1 28  ? 17.143 8.426   14.845  0.58 29.66 ?  28  LYS   A NZ   1 
ATOM   777  H H    A LYS   A 1 28  ? 18.961 2.489   15.392  0.42 22.78 ?  28  LYS   A H    1 
ATOM   778  H H    B LYS   A 1 28  ? 18.713 2.575   15.047  0.58 16.27 ?  28  LYS   A H    1 
ATOM   779  H HA   A LYS   A 1 28  ? 20.579 3.074   17.352  0.42 25.92 ?  28  LYS   A HA   1 
ATOM   780  H HA   B LYS   A 1 28  ? 20.199 3.375   17.023  0.58 19.79 ?  28  LYS   A HA   1 
ATOM   781  H HB2  A LYS   A 1 28  ? 18.148 4.232   16.569  0.42 28.39 ?  28  LYS   A HB2  1 
ATOM   782  H HB2  B LYS   A 1 28  ? 17.724 4.289   16.089  0.58 23.03 ?  28  LYS   A HB2  1 
ATOM   783  H HB3  A LYS   A 1 28  ? 18.892 4.749   17.873  0.42 28.39 ?  28  LYS   A HB3  1 
ATOM   784  H HB3  B LYS   A 1 28  ? 18.353 4.924   17.401  0.58 23.03 ?  28  LYS   A HB3  1 
ATOM   785  H HG2  A LYS   A 1 28  ? 20.767 5.254   16.481  0.42 30.85 ?  28  LYS   A HG2  1 
ATOM   786  H HG2  B LYS   A 1 28  ? 20.274 5.443   16.029  0.58 27.01 ?  28  LYS   A HG2  1 
ATOM   787  H HG3  A LYS   A 1 28  ? 19.827 4.964   15.231  0.42 30.85 ?  28  LYS   A HG3  1 
ATOM   788  H HG3  B LYS   A 1 28  ? 19.327 5.138   14.788  0.58 27.01 ?  28  LYS   A HG3  1 
ATOM   789  H HD2  A LYS   A 1 28  ? 19.210 6.957   17.124  0.42 33.02 ?  28  LYS   A HD2  1 
ATOM   790  H HD2  B LYS   A 1 28  ? 18.627 7.083   16.693  0.58 31.38 ?  28  LYS   A HD2  1 
ATOM   791  H HD3  A LYS   A 1 28  ? 20.003 7.280   15.783  0.42 33.02 ?  28  LYS   A HD3  1 
ATOM   792  H HD3  B LYS   A 1 28  ? 19.486 7.459   15.407  0.58 31.38 ?  28  LYS   A HD3  1 
ATOM   793  H HE2  A LYS   A 1 28  ? 18.133 6.500   14.558  0.42 34.45 ?  28  LYS   A HE2  1 
ATOM   794  H HE2  B LYS   A 1 28  ? 17.695 6.648   14.070  0.58 34.26 ?  28  LYS   A HE2  1 
ATOM   795  H HE3  A LYS   A 1 28  ? 17.342 6.364   15.933  0.42 34.45 ?  28  LYS   A HE3  1 
ATOM   796  H HE3  B LYS   A 1 28  ? 16.834 6.513   15.402  0.58 34.26 ?  28  LYS   A HE3  1 
ATOM   797  H HZ1  A LYS   A 1 28  ? 16.851 8.343   14.924  0.42 35.41 ?  28  LYS   A HZ1  1 
ATOM   798  H HZ1  B LYS   A 1 28  ? 16.396 8.491   14.367  0.58 35.62 ?  28  LYS   A HZ1  1 
ATOM   799  H HZ2  A LYS   A 1 28  ? 17.523 8.621   16.177  0.42 35.41 ?  28  LYS   A HZ2  1 
ATOM   800  H HZ2  B LYS   A 1 28  ? 17.002 8.769   15.654  0.58 35.62 ?  28  LYS   A HZ2  1 
ATOM   801  H HZ3  A LYS   A 1 28  ? 18.243 8.744   14.926  0.42 35.41 ?  28  LYS   A HZ3  1 
ATOM   802  H HZ3  B LYS   A 1 28  ? 17.786 8.892   14.442  0.58 35.62 ?  28  LYS   A HZ3  1 
ATOM   803  N N    A LYS   A 1 29  ? 18.000 1.467   18.270  0.42 22.97 ?  29  LYS   A N    1 
ATOM   804  N N    B LYS   A 1 29  ? 17.652 1.719   17.961  0.58 17.77 ?  29  LYS   A N    1 
ATOM   805  C CA   A LYS   A 1 29  ? 17.394 0.782   19.409  0.42 23.96 ?  29  LYS   A CA   1 
ATOM   806  C CA   B LYS   A 1 29  ? 17.040 1.070   19.115  0.58 19.22 ?  29  LYS   A CA   1 
ATOM   807  C C    A LYS   A 1 29  ? 18.185 -0.463  19.800  0.42 22.33 ?  29  LYS   A C    1 
ATOM   808  C C    B LYS   A 1 29  ? 17.858 -0.131  19.573  0.58 17.89 ?  29  LYS   A C    1 
ATOM   809  O O    A LYS   A 1 29  ? 18.459 -0.688  20.984  0.42 22.81 ?  29  LYS   A O    1 
ATOM   810  O O    B LYS   A 1 29  ? 18.125 -0.291  20.769  0.58 19.14 ?  29  LYS   A O    1 
ATOM   811  C CB   A LYS   A 1 29  ? 15.952 0.401   19.072  0.42 26.55 ?  29  LYS   A CB   1 
ATOM   812  C CB   B LYS   A 1 29  ? 15.613 0.637   18.768  0.58 22.28 ?  29  LYS   A CB   1 
ATOM   813  C CG   A LYS   A 1 29  ? 15.220 -0.332  20.187  0.42 29.19 ?  29  LYS   A CG   1 
ATOM   814  C CG   B LYS   A 1 29  ? 14.902 -0.114  19.886  0.58 26.11 ?  29  LYS   A CG   1 
ATOM   815  C CD   A LYS   A 1 29  ? 14.899 0.593   21.349  0.42 31.68 ?  29  LYS   A CD   1 
ATOM   816  C CD   B LYS   A 1 29  ? 14.638 0.792   21.076  0.58 29.74 ?  29  LYS   A CD   1 
ATOM   817  C CE   A LYS   A 1 29  ? 14.014 -0.099  22.374  0.42 33.32 ?  29  LYS   A CE   1 
ATOM   818  C CE   B LYS   A 1 29  ? 13.871 0.065   22.168  0.58 32.12 ?  29  LYS   A CE   1 
ATOM   819  N NZ   A LYS   A 1 29  ? 13.539 0.841   23.425  0.42 34.33 ?  29  LYS   A NZ   1 
ATOM   820  N NZ   B LYS   A 1 29  ? 13.536 0.971   23.300  0.58 33.49 ?  29  LYS   A NZ   1 
ATOM   821  H H    A LYS   A 1 29  ? 17.611 1.324   17.516  0.42 27.59 ?  29  LYS   A H    1 
ATOM   822  H H    B LYS   A 1 29  ? 17.256 1.558   17.212  0.58 21.35 ?  29  LYS   A H    1 
ATOM   823  H HA   A LYS   A 1 29  ? 17.376 1.386   20.168  0.42 28.78 ?  29  LYS   A HA   1 
ATOM   824  H HA   B LYS   A 1 29  ? 16.990 1.701   19.850  0.58 23.09 ?  29  LYS   A HA   1 
ATOM   825  H HB2  A LYS   A 1 29  ? 15.454 1.210   18.877  0.42 31.89 ?  29  LYS   A HB2  1 
ATOM   826  H HB2  B LYS   A 1 29  ? 15.083 1.426   18.567  0.58 26.76 ?  29  LYS   A HB2  1 
ATOM   827  H HB3  A LYS   A 1 29  ? 15.958 -0.176  18.294  0.42 31.89 ?  29  LYS   A HB3  1 
ATOM   828  H HB3  B LYS   A 1 29  ? 15.640 0.054   17.994  0.58 26.76 ?  29  LYS   A HB3  1 
ATOM   829  H HG2  A LYS   A 1 29  ? 14.385 -0.679  19.840  0.42 35.06 ?  29  LYS   A HG2  1 
ATOM   830  H HG2  B LYS   A 1 29  ? 14.049 -0.438  19.558  0.58 31.36 ?  29  LYS   A HG2  1 
ATOM   831  H HG3  A LYS   A 1 29  ? 15.769 -1.061  20.519  0.42 35.06 ?  29  LYS   A HG3  1 
ATOM   832  H HG3  B LYS   A 1 29  ? 15.447 -0.862  20.182  0.58 31.36 ?  29  LYS   A HG3  1 
ATOM   833  H HD2  A LYS   A 1 29  ? 15.724 0.857   21.787  0.42 38.04 ?  29  LYS   A HD2  1 
ATOM   834  H HD2  B LYS   A 1 29  ? 15.484 1.090   21.446  0.58 35.72 ?  29  LYS   A HD2  1 
ATOM   835  H HD3  A LYS   A 1 29  ? 14.429 1.374   21.017  0.42 38.04 ?  29  LYS   A HD3  1 
ATOM   836  H HD3  B LYS   A 1 29  ? 14.111 1.553   20.787  0.58 35.72 ?  29  LYS   A HD3  1 
ATOM   837  H HE2  A LYS   A 1 29  ? 13.237 -0.470  21.926  0.42 40.01 ?  29  LYS   A HE2  1 
ATOM   838  H HE2  B LYS   A 1 29  ? 13.043 -0.282  21.800  0.58 38.57 ?  29  LYS   A HE2  1 
ATOM   839  H HE3  A LYS   A 1 29  ? 14.519 -0.806  22.806  0.42 40.01 ?  29  LYS   A HE3  1 
ATOM   840  H HE3  B LYS   A 1 29  ? 14.415 -0.662  22.512  0.58 38.57 ?  29  LYS   A HE3  1 
ATOM   841  H HZ1  A LYS   A 1 29  ? 13.024 0.410   24.009  0.42 41.22 ?  29  LYS   A HZ1  1 
ATOM   842  H HZ1  B LYS   A 1 29  ? 13.087 0.523   23.925  0.58 40.21 ?  29  LYS   A HZ1  1 
ATOM   843  H HZ2  A LYS   A 1 29  ? 14.234 1.192   23.856  0.42 41.22 ?  29  LYS   A HZ2  1 
ATOM   844  H HZ2  B LYS   A 1 29  ? 14.281 1.300   23.658  0.58 40.21 ?  29  LYS   A HZ2  1 
ATOM   845  H HZ3  A LYS   A 1 29  ? 13.067 1.498   23.054  0.42 41.22 ?  29  LYS   A HZ3  1 
ATOM   846  H HZ3  B LYS   A 1 29  ? 13.032 1.645   23.010  0.58 40.21 ?  29  LYS   A HZ3  1 
ATOM   847  N N    A VAL   A 1 30  ? 18.544 -1.289  18.818  0.42 20.53 ?  30  VAL   A N    1 
ATOM   848  N N    B VAL   A 1 30  ? 18.247 -0.993  18.631  0.58 16.75 ?  30  VAL   A N    1 
ATOM   849  C CA   A VAL   A 1 30  ? 19.188 -2.567  19.107  0.42 18.99 ?  30  VAL   A CA   1 
ATOM   850  C CA   B VAL   A 1 30  ? 18.893 -2.253  18.984  0.58 15.78 ?  30  VAL   A CA   1 
ATOM   851  C C    A VAL   A 1 30  ? 20.692 -2.408  19.310  0.42 17.12 ?  30  VAL   A C    1 
ATOM   852  C C    B VAL   A 1 30  ? 20.394 -2.083  19.223  0.58 15.03 ?  30  VAL   A C    1 
ATOM   853  O O    A VAL   A 1 30  ? 21.295 -3.139  20.104  0.42 17.10 ?  30  VAL   A O    1 
ATOM   854  O O    B VAL   A 1 30  ? 20.973 -2.781  20.065  0.58 15.82 ?  30  VAL   A O    1 
ATOM   855  C CB   A VAL   A 1 30  ? 18.878 -3.568  17.979  0.42 19.45 ?  30  VAL   A CB   1 
ATOM   856  C CB   B VAL   A 1 30  ? 18.605 -3.302  17.894  0.58 16.06 ?  30  VAL   A CB   1 
ATOM   857  C CG1  A VAL   A 1 30  ? 19.656 -4.864  18.173  0.42 19.83 ?  30  VAL   A CG1  1 
ATOM   858  C CG1  B VAL   A 1 30  ? 19.364 -4.590  18.171  0.58 16.75 ?  30  VAL   A CG1  1 
ATOM   859  C CG2  A VAL   A 1 30  ? 17.386 -3.842  17.907  0.42 19.96 ?  30  VAL   A CG2  1 
ATOM   860  C CG2  B VAL   A 1 30  ? 17.107 -3.572  17.795  0.58 16.97 ?  30  VAL   A CG2  1 
ATOM   861  H H    A VAL   A 1 30  ? 18.422 -1.133  17.983  0.42 24.67 ?  30  VAL   A H    1 
ATOM   862  H H    B VAL   A 1 30  ? 18.122 -0.877  17.784  0.58 20.13 ?  30  VAL   A H    1 
ATOM   863  H HA   A VAL   A 1 30  ? 18.806 -2.921  19.926  0.42 22.82 ?  30  VAL   A HA   1 
ATOM   864  H HA   B VAL   A 1 30  ? 18.490 -2.577  19.804  0.58 18.97 ?  30  VAL   A HA   1 
ATOM   865  H HB   A VAL   A 1 30  ? 19.152 -3.181  17.133  0.42 23.37 ?  30  VAL   A HB   1 
ATOM   866  H HB   B VAL   A 1 30  ? 18.903 -2.959  17.036  0.58 19.30 ?  30  VAL   A HB   1 
ATOM   867  H HG11 A VAL   A 1 30  ? 19.282 -5.545  17.591  0.42 23.82 ?  30  VAL   A HG11 1 
ATOM   868  H HG11 B VAL   A 1 30  ? 18.997 -5.298  17.619  0.58 20.13 ?  30  VAL   A HG11 1 
ATOM   869  H HG12 A VAL   A 1 30  ? 20.587 -4.715  17.948  0.42 23.82 ?  30  VAL   A HG12 1 
ATOM   870  H HG12 B VAL   A 1 30  ? 20.301 -4.459  17.958  0.58 20.13 ?  30  VAL   A HG12 1 
ATOM   871  H HG13 A VAL   A 1 30  ? 19.578 -5.145  19.098  0.42 23.82 ?  30  VAL   A HG13 1 
ATOM   872  H HG13 B VAL   A 1 30  ? 19.264 -4.818  19.108  0.58 20.13 ?  30  VAL   A HG13 1 
ATOM   873  H HG21 A VAL   A 1 30  ? 17.221 -4.500  17.214  0.42 23.98 ?  30  VAL   A HG21 1 
ATOM   874  H HG21 B VAL   A 1 30  ? 16.955 -4.270  17.137  0.58 20.39 ?  30  VAL   A HG21 1 
ATOM   875  H HG22 A VAL   A 1 30  ? 17.087 -4.181  18.765  0.42 23.98 ?  30  VAL   A HG22 1 
ATOM   876  H HG22 B VAL   A 1 30  ? 16.781 -3.859  18.662  0.58 20.39 ?  30  VAL   A HG22 1 
ATOM   877  H HG23 A VAL   A 1 30  ? 16.924 -3.016  17.697  0.42 23.98 ?  30  VAL   A HG23 1 
ATOM   878  H HG23 B VAL   A 1 30  ? 16.656 -2.759  17.522  0.58 20.39 ?  30  VAL   A HG23 1 
ATOM   879  N N    A LYS   A 1 31  ? 21.316 -1.470  18.608  0.42 16.18 ?  31  LYS   A N    1 
ATOM   880  N N    B LYS   A 1 31  ? 21.043 -1.174  18.503  0.58 14.73 ?  31  LYS   A N    1 
ATOM   881  C CA   A LYS   A 1 31  ? 22.768 -1.351  18.558  0.42 16.37 ?  31  LYS   A CA   1 
ATOM   882  C CA   B LYS   A 1 31  ? 22.497 -1.070  18.481  0.58 15.19 ?  31  LYS   A CA   1 
ATOM   883  C C    A LYS   A 1 31  ? 23.396 -2.706  18.216  0.42 14.02 ?  31  LYS   A C    1 
ATOM   884  C C    B LYS   A 1 31  ? 23.135 -2.442  18.244  0.58 13.90 ?  31  LYS   A C    1 
ATOM   885  O O    A LYS   A 1 31  ? 24.185 -3.248  18.996  0.42 14.26 ?  31  LYS   A O    1 
ATOM   886  O O    B LYS   A 1 31  ? 23.885 -2.943  19.088  0.58 15.17 ?  31  LYS   A O    1 
ATOM   887  C CB   A LYS   A 1 31  ? 23.341 -0.797  19.855  0.42 19.90 ?  31  LYS   A CB   1 
ATOM   888  C CB   B LYS   A 1 31  ? 23.042 -0.418  19.744  0.58 18.37 ?  31  LYS   A CB   1 
ATOM   889  C CG   A LYS   A 1 31  ? 22.654 0.461   20.363  0.42 23.69 ?  31  LYS   A CG   1 
ATOM   890  C CG   B LYS   A 1 31  ? 22.358 0.893   20.103  0.58 22.91 ?  31  LYS   A CG   1 
ATOM   891  C CD   A LYS   A 1 31  ? 23.668 1.484   20.851  0.42 26.51 ?  31  LYS   A CD   1 
ATOM   892  C CD   B LYS   A 1 31  ? 23.324 1.860   20.767  0.58 26.63 ?  31  LYS   A CD   1 
ATOM   893  C CE   A LYS   A 1 31  ? 23.021 2.526   21.750  0.42 28.31 ?  31  LYS   A CE   1 
ATOM   894  C CE   B LYS   A 1 31  ? 22.586 2.924   21.560  0.58 29.42 ?  31  LYS   A CE   1 
ATOM   895  N NZ   A LYS   A 1 31  ? 21.870 3.212   21.100  0.42 29.14 ?  31  LYS   A NZ   1 
ATOM   896  N NZ   B LYS   A 1 31  ? 21.478 3.552   20.791  0.58 31.07 ?  31  LYS   A NZ   1 
ATOM   897  H H    A LYS   A 1 31  ? 20.903 -0.884  18.138  0.42 19.44 ?  31  LYS   A H    1 
ATOM   898  H H    B LYS   A 1 31  ? 20.643 -0.579  18.018  0.58 17.70 ?  31  LYS   A H    1 
ATOM   899  H HA   A LYS   A 1 31  ? 22.989 -0.729  17.854  0.42 19.67 ?  31  LYS   A HA   1 
ATOM   900  H HA   B LYS   A 1 31  ? 22.736 -0.499  17.739  0.58 18.25 ?  31  LYS   A HA   1 
ATOM   901  H HB2  A LYS   A 1 31  ? 23.267 -1.475  20.541  0.42 23.91 ?  31  LYS   A HB2  1 
ATOM   902  H HB2  B LYS   A 1 31  ? 22.925 -1.024  20.488  0.58 22.07 ?  31  LYS   A HB2  1 
ATOM   903  H HB3  A LYS   A 1 31  ? 24.277 -0.581  19.708  0.42 23.91 ?  31  LYS   A HB3  1 
ATOM   904  H HB3  B LYS   A 1 31  ? 23.984 -0.232  19.611  0.58 22.07 ?  31  LYS   A HB3  1 
ATOM   905  H HG2  A LYS   A 1 31  ? 22.140 0.861   19.645  0.42 28.45 ?  31  LYS   A HG2  1 
ATOM   906  H HG2  B LYS   A 1 31  ? 22.018 1.311   19.296  0.58 27.52 ?  31  LYS   A HG2  1 
ATOM   907  H HG3  A LYS   A 1 31  ? 22.073 0.232   21.106  0.42 28.45 ?  31  LYS   A HG3  1 
ATOM   908  H HG3  B LYS   A 1 31  ? 21.632 0.717   20.722  0.58 27.52 ?  31  LYS   A HG3  1 
ATOM   909  H HD2  A LYS   A 1 31  ? 24.361 1.032   21.358  0.42 31.83 ?  31  LYS   A HD2  1 
ATOM   910  H HD2  B LYS   A 1 31  ? 23.902 1.369   21.374  0.58 31.99 ?  31  LYS   A HD2  1 
ATOM   911  H HD3  A LYS   A 1 31  ? 24.056 1.939   20.086  0.42 31.83 ?  31  LYS   A HD3  1 
ATOM   912  H HD3  B LYS   A 1 31  ? 23.855 2.302   20.084  0.58 31.99 ?  31  LYS   A HD3  1 
ATOM   913  H HE2  A LYS   A 1 31  ? 22.696 2.091   22.553  0.42 34.00 ?  31  LYS   A HE2  1 
ATOM   914  H HE2  B LYS   A 1 31  ? 22.210 2.514   22.352  0.58 35.33 ?  31  LYS   A HE2  1 
ATOM   915  H HE3  A LYS   A 1 31  ? 23.681 3.199   21.979  0.42 34.00 ?  31  LYS   A HE3  1 
ATOM   916  H HE3  B LYS   A 1 31  ? 23.210 3.620   21.813  0.58 35.33 ?  31  LYS   A HE3  1 
ATOM   917  H HZ1  A LYS   A 1 31  ? 21.531 3.826   21.650  0.42 34.99 ?  31  LYS   A HZ1  1 
ATOM   918  H HZ1  B LYS   A 1 31  ? 21.112 4.208   21.269  0.58 37.31 ?  31  LYS   A HZ1  1 
ATOM   919  H HZ2  A LYS   A 1 31  ? 22.136 3.613   20.351  0.42 34.99 ?  31  LYS   A HZ2  1 
ATOM   920  H HZ2  B LYS   A 1 31  ? 21.790 3.887   20.029  0.58 37.31 ?  31  LYS   A HZ2  1 
ATOM   921  H HZ3  A LYS   A 1 31  ? 21.235 2.621   20.901  0.42 34.99 ?  31  LYS   A HZ3  1 
ATOM   922  H HZ3  B LYS   A 1 31  ? 20.853 2.945   20.607  0.58 37.31 ?  31  LYS   A HZ3  1 
ATOM   923  N N    A PRO   A 1 32  ? 23.069 -3.271  17.056  0.42 13.31 ?  32  PRO   A N    1 
ATOM   924  N N    B PRO   A 1 32  ? 22.865 -3.059  17.099  0.58 13.04 ?  32  PRO   A N    1 
ATOM   925  C CA   A PRO   A 1 32  ? 23.554 -4.612  16.727  0.42 13.42 ?  32  PRO   A CA   1 
ATOM   926  C CA   B PRO   A 1 32  ? 23.362 -4.411  16.840  0.58 13.09 ?  32  PRO   A CA   1 
ATOM   927  C C    A PRO   A 1 32  ? 25.055 -4.626  16.502  0.42 12.93 ?  32  PRO   A C    1 
ATOM   928  C C    B PRO   A 1 32  ? 24.869 -4.416  16.641  0.58 13.40 ?  32  PRO   A C    1 
ATOM   929  O O    A PRO   A 1 32  ? 25.685 -3.604  16.219  0.42 12.48 ?  32  PRO   A O    1 
ATOM   930  O O    B PRO   A 1 32  ? 25.523 -3.380  16.505  0.58 14.03 ?  32  PRO   A O    1 
ATOM   931  C CB   A PRO   A 1 32  ? 22.818 -4.936  15.425  0.42 14.18 ?  32  PRO   A CB   1 
ATOM   932  C CB   B PRO   A 1 32  ? 22.640 -4.782  15.542  0.58 13.90 ?  32  PRO   A CB   1 
ATOM   933  C CG   A PRO   A 1 32  ? 22.629 -3.603  14.782  0.42 13.89 ?  32  PRO   A CG   1 
ATOM   934  C CG   B PRO   A 1 32  ? 22.480 -3.469  14.834  0.58 13.46 ?  32  PRO   A CG   1 
ATOM   935  C CD   A PRO   A 1 32  ? 22.348 -2.659  15.926  0.42 13.36 ?  32  PRO   A CD   1 
ATOM   936  C CD   B PRO   A 1 32  ? 22.166 -2.493  15.932  0.58 13.00 ?  32  PRO   A CD   1 
ATOM   937  H HA   A PRO   A 1 32  ? 23.305 -5.249  17.419  0.42 16.13 ?  32  PRO   A HA   1 
ATOM   938  H HA   B PRO   A 1 32  ? 23.103 -5.022  17.551  0.58 15.74 ?  32  PRO   A HA   1 
ATOM   939  H HB2  A PRO   A 1 32  ? 23.368 -5.515  14.873  0.42 17.05 ?  32  PRO   A HB2  1 
ATOM   940  H HB2  B PRO   A 1 32  ? 23.185 -5.391  15.024  0.58 16.70 ?  32  PRO   A HB2  1 
ATOM   941  H HB3  A PRO   A 1 32  ? 21.964 -5.355  15.621  0.42 17.05 ?  32  PRO   A HB3  1 
ATOM   942  H HB3  B PRO   A 1 32  ? 21.772 -5.176  15.740  0.58 16.70 ?  32  PRO   A HB3  1 
ATOM   943  H HG2  A PRO   A 1 32  ? 23.440 -3.350  14.315  0.42 16.70 ?  32  PRO   A HG2  1 
ATOM   944  H HG2  B PRO   A 1 32  ? 23.307 -3.235  14.388  0.58 16.18 ?  32  PRO   A HG2  1 
ATOM   945  H HG3  A PRO   A 1 32  ? 21.877 -3.642  14.170  0.42 16.70 ?  32  PRO   A HG3  1 
ATOM   946  H HG3  B PRO   A 1 32  ? 21.747 -3.525  14.199  0.58 16.18 ?  32  PRO   A HG3  1 
ATOM   947  H HD2  A PRO   A 1 32  ? 22.708 -1.780  15.724  0.42 16.06 ?  32  PRO   A HD2  1 
ATOM   948  H HD2  B PRO   A 1 32  ? 22.524 -1.617  15.711  0.58 15.63 ?  32  PRO   A HD2  1 
ATOM   949  H HD3  A PRO   A 1 32  ? 21.395 -2.621  16.100  0.42 16.06 ?  32  PRO   A HD3  1 
ATOM   950  H HD3  B PRO   A 1 32  ? 21.206 -2.453  16.082  0.58 15.63 ?  32  PRO   A HD3  1 
ATOM   951  N N    A THR   A 1 33  ? 25.625 -5.826  16.608  0.42 12.91 ?  33  THR   A N    1 
ATOM   952  N N    B THR   A 1 33  ? 25.420 -5.628  16.610  0.58 13.49 ?  33  THR   A N    1 
ATOM   953  C CA   A THR   A 1 33  ? 27.031 -5.995  16.268  0.42 13.45 ?  33  THR   A CA   1 
ATOM   954  C CA   B THR   A 1 33  ? 26.840 -5.785  16.320  0.58 13.56 ?  33  THR   A CA   1 
ATOM   955  C C    A THR   A 1 33  ? 27.301 -5.540  14.839  0.42 12.76 ?  33  THR   A C    1 
ATOM   956  C C    B THR   A 1 33  ? 27.164 -5.346  14.894  0.58 12.74 ?  33  THR   A C    1 
ATOM   957  O O    A THR   A 1 33  ? 28.364 -4.975  14.554  0.42 12.30 ?  33  THR   A O    1 
ATOM   958  O O    B THR   A 1 33  ? 28.158 -4.647  14.660  0.58 12.87 ?  33  THR   A O    1 
ATOM   959  C CB   A THR   A 1 33  ? 27.443 -7.457  16.458  0.42 15.06 ?  33  THR   A CB   1 
ATOM   960  C CB   B THR   A 1 33  ? 27.244 -7.240  16.552  0.58 15.36 ?  33  THR   A CB   1 
ATOM   961  O OG1  A THR   A 1 33  ? 27.192 -7.864  17.808  0.42 16.47 ?  33  THR   A OG1  1 
ATOM   962  O OG1  B THR   A 1 33  ? 26.890 -7.620  17.887  0.58 17.14 ?  33  THR   A OG1  1 
ATOM   963  C CG2  A THR   A 1 33  ? 28.921 -7.645  16.164  0.42 15.26 ?  33  THR   A CG2  1 
ATOM   964  C CG2  B THR   A 1 33  ? 28.745 -7.427  16.346  0.58 16.01 ?  33  THR   A CG2  1 
ATOM   965  H H    A THR   A 1 33  ? 25.225 -6.542  16.865  0.42 15.52 ?  33  THR   A H    1 
ATOM   966  H H    B THR   A 1 33  ? 24.995 -6.360  16.767  0.58 16.22 ?  33  THR   A H    1 
ATOM   967  H HA   A THR   A 1 33  ? 27.570 -5.449  16.864  0.42 16.16 ?  33  THR   A HA   1 
ATOM   968  H HA   B THR   A 1 33  ? 27.348 -5.235  16.938  0.58 16.30 ?  33  THR   A HA   1 
ATOM   969  H HB   A THR   A 1 33  ? 26.932 -8.016  15.852  0.42 18.10 ?  33  THR   A HB   1 
ATOM   970  H HB   B THR   A 1 33  ? 26.776 -7.816  15.925  0.58 18.46 ?  33  THR   A HB   1 
ATOM   971  H HG1  A THR   A 1 33  ? 27.615 -7.370  18.341  0.42 19.80 ?  33  THR   A HG1  1 
ATOM   972  H HG1  B THR   A 1 33  ? 27.305 -7.148  18.446  0.58 20.59 ?  33  THR   A HG1  1 
ATOM   973  H HG21 A THR   A 1 33  ? 29.199 -8.533  16.440  0.42 18.34 ?  33  THR   A HG21 1 
ATOM   974  H HG21 B THR   A 1 33  ? 29.015 -8.311  16.639  0.58 19.24 ?  33  THR   A HG21 1 
ATOM   975  H HG22 A THR   A 1 33  ? 29.090 -7.542  15.217  0.42 18.34 ?  33  THR   A HG22 1 
ATOM   976  H HG22 B THR   A 1 33  ? 28.964 -7.328  15.405  0.58 19.24 ?  33  THR   A HG22 1 
ATOM   977  H HG23 A THR   A 1 33  ? 29.441 -6.988  16.653  0.42 18.34 ?  33  THR   A HG23 1 
ATOM   978  H HG23 B THR   A 1 33  ? 29.233 -6.763  16.856  0.58 19.24 ?  33  THR   A HG23 1 
ATOM   979  N N    . VAL   A 1 34  ? 26.351 -5.770  13.927  1.00 12.07 ?  34  VAL   A N    1 
ATOM   980  C CA   . VAL   A 1 34  ? 26.543 -5.440  12.517  1.00 11.27 ?  34  VAL   A CA   1 
ATOM   981  C C    . VAL   A 1 34  ? 25.247 -4.904  11.933  1.00 10.60 ?  34  VAL   A C    1 
ATOM   982  O O    . VAL   A 1 34  ? 24.216 -5.586  11.970  1.00 11.37 ?  34  VAL   A O    1 
ATOM   983  C CB   . VAL   A 1 34  ? 27.010 -6.656  11.689  1.00 11.74 ?  34  VAL   A CB   1 
ATOM   984  C CG1  . VAL   A 1 34  ? 27.210 -6.262  10.233  1.00 12.23 ?  34  VAL   A CG1  1 
ATOM   985  C CG2  . VAL   A 1 34  ? 28.289 -7.270  12.255  1.00 13.07 ?  34  VAL   A CG2  1 
ATOM   986  H H    A VAL   A 1 34  ? 25.586 -6.125  14.108  0.42 14.51 ?  34  VAL   A H    1 
ATOM   987  H H    B VAL   A 1 34  ? 25.663 -6.270  14.071  0.58 14.51 ?  34  VAL   A H    1 
ATOM   988  H HA   . VAL   A 1 34  ? 27.216 -4.748  12.444  1.00 13.56 ?  34  VAL   A HA   1 
ATOM   989  H HB   . VAL   A 1 34  ? 26.317 -7.335  11.723  1.00 14.12 ?  34  VAL   A HB   1 
ATOM   990  H HG11 . VAL   A 1 34  ? 27.704 -6.968  9.784   1.00 14.71 ?  34  VAL   A HG11 1 
ATOM   991  H HG12 . VAL   A 1 34  ? 26.347 -6.145  9.811   1.00 14.71 ?  34  VAL   A HG12 1 
ATOM   992  H HG13 . VAL   A 1 34  ? 27.716 -5.435  10.196  1.00 14.71 ?  34  VAL   A HG13 1 
ATOM   993  H HG21 . VAL   A 1 34  ? 28.580 -7.989  11.669  1.00 15.71 ?  34  VAL   A HG21 1 
ATOM   994  H HG22 . VAL   A 1 34  ? 28.975 -6.589  12.306  1.00 15.71 ?  34  VAL   A HG22 1 
ATOM   995  H HG23 . VAL   A 1 34  ? 28.108 -7.626  13.141  1.00 15.71 ?  34  VAL   A HG23 1 
ATOM   996  N N    . VAL   A 1 35  ? 25.315 -3.708  11.349  1.00 10.30 ?  35  VAL   A N    1 
ATOM   997  C CA   . VAL   A 1 35  ? 24.278 -3.208  10.455  1.00 10.10 ?  35  VAL   A CA   1 
ATOM   998  C C    . VAL   A 1 35  ? 24.834 -3.215  9.039   1.00 9.31  ?  35  VAL   A C    1 
ATOM   999  O O    . VAL   A 1 35  ? 25.977 -2.798  8.809   1.00 10.13 ?  35  VAL   A O    1 
ATOM   1000 C CB   . VAL   A 1 35  ? 23.741 -1.814  10.857  1.00 10.66 ?  35  VAL   A CB   1 
ATOM   1001 C CG1  . VAL   A 1 35  ? 24.795 -0.714  10.727  1.00 10.92 ?  35  VAL   A CG1  1 
ATOM   1002 C CG2  . VAL   A 1 35  ? 22.500 -1.464  10.035  1.00 11.62 ?  35  VAL   A CG2  1 
ATOM   1003 H H    . VAL   A 1 35  ? 25.975 -3.163  11.447  1.00 12.38 ?  35  VAL   A H    1 
ATOM   1004 H HA   . VAL   A 1 35  ? 23.530 -3.819  10.477  1.00 12.15 ?  35  VAL   A HA   1 
ATOM   1005 H HB   . VAL   A 1 35  ? 23.466 -1.841  11.783  1.00 12.82 ?  35  VAL   A HB   1 
ATOM   1006 H HG11 . VAL   A 1 35  ? 24.441 0.113   11.092  1.00 13.13 ?  35  VAL   A HG11 1 
ATOM   1007 H HG12 . VAL   A 1 35  ? 25.588 -0.978  11.216  1.00 13.13 ?  35  VAL   A HG12 1 
ATOM   1008 H HG13 . VAL   A 1 35  ? 25.014 -0.588  9.787   1.00 13.13 ?  35  VAL   A HG13 1 
ATOM   1009 H HG21 . VAL   A 1 35  ? 22.142 -0.616  10.337  1.00 13.97 ?  35  VAL   A HG21 1 
ATOM   1010 H HG22 . VAL   A 1 35  ? 22.745 -1.401  9.094   1.00 13.97 ?  35  VAL   A HG22 1 
ATOM   1011 H HG23 . VAL   A 1 35  ? 21.835 -2.164  10.151  1.00 13.97 ?  35  VAL   A HG23 1 
ATOM   1012 N N    . VAL   A 1 36  ? 24.022 -3.674  8.089   1.00 9.16  ?  36  VAL   A N    1 
ATOM   1013 C CA   . VAL   A 1 36  ? 24.403 -3.685  6.685   1.00 8.91  ?  36  VAL   A CA   1 
ATOM   1014 C C    . VAL   A 1 36  ? 23.938 -2.400  6.012   1.00 8.94  ?  36  VAL   A C    1 
ATOM   1015 O O    . VAL   A 1 36  ? 22.772 -2.001  6.148   1.00 9.64  ?  36  VAL   A O    1 
ATOM   1016 C CB   . VAL   A 1 36  ? 23.812 -4.910  5.972   1.00 9.11  ?  36  VAL   A CB   1 
ATOM   1017 C CG1  . VAL   A 1 36  ? 24.076 -4.845  4.483   1.00 9.47  ?  36  VAL   A CG1  1 
ATOM   1018 C CG2  . VAL   A 1 36  ? 24.351 -6.195  6.578   1.00 9.69  ?  36  VAL   A CG2  1 
ATOM   1019 H H    . VAL   A 1 36  ? 23.232 -3.987  8.241   1.00 11.02 ?  36  VAL   A H    1 
ATOM   1020 H HA   . VAL   A 1 36  ? 25.373 -3.738  6.624   1.00 10.72 ?  36  VAL   A HA   1 
ATOM   1021 H HB   . VAL   A 1 36  ? 22.851 -4.906  6.102   1.00 10.96 ?  36  VAL   A HB   1 
ATOM   1022 H HG11 . VAL   A 1 36  ? 23.939 -5.729  4.103   1.00 11.39 ?  36  VAL   A HG11 1 
ATOM   1023 H HG12 . VAL   A 1 36  ? 23.463 -4.214  4.078   1.00 11.39 ?  36  VAL   A HG12 1 
ATOM   1024 H HG13 . VAL   A 1 36  ? 24.992 -4.564  4.338   1.00 11.39 ?  36  VAL   A HG13 1 
ATOM   1025 H HG21 . VAL   A 1 36  ? 23.977 -6.953  6.097   1.00 11.65 ?  36  VAL   A HG21 1 
ATOM   1026 H HG22 . VAL   A 1 36  ? 25.317 -6.201  6.502   1.00 11.65 ?  36  VAL   A HG22 1 
ATOM   1027 H HG23 . VAL   A 1 36  ? 24.092 -6.242  7.513   1.00 11.65 ?  36  VAL   A HG23 1 
ATOM   1028 N N    A ASN   A 1 37  ? 24.870 -1.722  5.347   0.42 8.62  ?  37  ASN   A N    1 
ATOM   1029 N N    B ASN   A 1 37  ? 24.839 -1.792  5.228   0.58 8.39  ?  37  ASN   A N    1 
ATOM   1030 C CA   A ASN   A 1 37  ? 24.542 -0.589  4.503   0.42 8.58  ?  37  ASN   A CA   1 
ATOM   1031 C CA   B ASN   A 1 37  ? 24.501 -0.707  4.318   0.58 8.34  ?  37  ASN   A CA   1 
ATOM   1032 C C    A ASN   A 1 37  ? 24.402 -1.054  3.062   0.42 8.19  ?  37  ASN   A C    1 
ATOM   1033 C C    B ASN   A 1 37  ? 24.401 -1.223  2.887   0.58 8.51  ?  37  ASN   A C    1 
ATOM   1034 O O    A ASN   A 1 37  ? 25.186 -1.881  2.584   0.42 8.63  ?  37  ASN   A O    1 
ATOM   1035 O O    B ASN   A 1 37  ? 25.217 -2.040  2.447   0.58 9.11  ?  37  ASN   A O    1 
ATOM   1036 C CB   A ASN   A 1 37  ? 25.618 0.491   4.584   0.42 8.35  ?  37  ASN   A CB   1 
ATOM   1037 C CB   B ASN   A 1 37  ? 25.557 0.398   4.385   0.58 8.91  ?  37  ASN   A CB   1 
ATOM   1038 C CG   A ASN   A 1 37  ? 25.257 1.701   3.778   0.42 7.91  ?  37  ASN   A CG   1 
ATOM   1039 C CG   B ASN   A 1 37  ? 25.241 1.564   3.464   0.58 8.74  ?  37  ASN   A CG   1 
ATOM   1040 O OD1  A ASN   A 1 37  ? 24.073 2.003   3.615   0.42 7.99  ?  37  ASN   A OD1  1 
ATOM   1041 O OD1  B ASN   A 1 37  ? 24.070 1.874   3.198   0.58 8.92  ?  37  ASN   A OD1  1 
ATOM   1042 N ND2  A ASN   A 1 37  ? 26.264 2.401   3.262   0.42 7.80  ?  37  ASN   A ND2  1 
ATOM   1043 N ND2  B ASN   A 1 37  ? 26.288 2.204   2.959   0.58 8.99  ?  37  ASN   A ND2  1 
ATOM   1044 H H    A ASN   A 1 37  ? 25.712 -1.904  5.370   0.42 10.37 ?  37  ASN   A H    1 
ATOM   1045 H H    B ASN   A 1 37  ? 25.675 -2.010  5.210   0.58 10.09 ?  37  ASN   A H    1 
ATOM   1046 H HA   A ASN   A 1 37  ? 23.699 -0.203  4.787   0.42 10.32 ?  37  ASN   A HA   1 
ATOM   1047 H HA   B ASN   A 1 37  ? 23.648 -0.333  4.573   0.58 10.03 ?  37  ASN   A HA   1 
ATOM   1048 H HB2  A ASN   A 1 37  ? 25.719 0.773   5.507   0.42 10.05 ?  37  ASN   A HB2  1 
ATOM   1049 H HB2  B ASN   A 1 37  ? 25.608 0.729   5.297   0.58 10.72 ?  37  ASN   A HB2  1 
ATOM   1050 H HB3  A ASN   A 1 37  ? 26.457 0.142   4.247   0.42 10.05 ?  37  ASN   A HB3  1 
ATOM   1051 H HB3  B ASN   A 1 37  ? 26.418 0.025   4.124   0.58 10.72 ?  37  ASN   A HB3  1 
ATOM   1052 H HD21 A ASN   A 1 37  ? 26.112 3.107   2.792   0.42 9.39  ?  37  ASN   A HD21 1 
ATOM   1053 H HD21 B ASN   A 1 37  ? 26.168 2.865   2.434   0.58 10.81 ?  37  ASN   A HD21 1 
ATOM   1054 H HD22 A ASN   A 1 37  ? 27.074 2.156   3.400   0.42 9.39  ?  37  ASN   A HD22 1 
ATOM   1055 H HD22 B ASN   A 1 37  ? 27.083 1.952   3.162   0.58 10.81 ?  37  ASN   A HD22 1 
ATOM   1056 N N    A ALA   A 1 38  ? 23.391 -0.517  2.378   0.42 8.61  ?  38  ALA   A N    1 
ATOM   1057 N N    B ALA   A 1 38  ? 23.388 -0.737  2.162   0.58 8.61  ?  38  ALA   A N    1 
ATOM   1058 C CA   A ALA   A 1 38  ? 23.205 -0.709  0.941   0.42 8.55  ?  38  ALA   A CA   1 
ATOM   1059 C CA   B ALA   A 1 38  ? 23.259 -0.984  0.726   0.58 9.34  ?  38  ALA   A CA   1 
ATOM   1060 C C    A ALA   A 1 38  ? 24.107 0.292   0.227   0.42 8.80  ?  38  ALA   A C    1 
ATOM   1061 C C    B ALA   A 1 38  ? 24.079 0.075   -0.008  0.58 9.06  ?  38  ALA   A C    1 
ATOM   1062 O O    A ALA   A 1 38  ? 23.689 1.394   -0.127  0.42 8.72  ?  38  ALA   A O    1 
ATOM   1063 O O    B ALA   A 1 38  ? 23.580 1.115   -0.451  0.58 9.26  ?  38  ALA   A O    1 
ATOM   1064 C CB   A ALA   A 1 38  ? 21.741 -0.506  0.566   0.42 8.91  ?  38  ALA   A CB   1 
ATOM   1065 C CB   B ALA   A 1 38  ? 21.794 -0.967  0.308   0.58 9.37  ?  38  ALA   A CB   1 
ATOM   1066 H H    A ALA   A 1 38  ? 22.782 -0.026  2.737   0.42 10.36 ?  38  ALA   A H    1 
ATOM   1067 H H    B ALA   A 1 38  ? 22.757 -0.260  2.493   0.58 10.36 ?  38  ALA   A H    1 
ATOM   1068 H HA   A ALA   A 1 38  ? 23.474 -1.604  0.688   0.42 10.29 ?  38  ALA   A HA   1 
ATOM   1069 H HA   B ALA   A 1 38  ? 23.625 -1.862  0.518   0.58 11.24 ?  38  ALA   A HA   1 
ATOM   1070 H HB1  A ALA   A 1 38  ? 21.637 -0.630  -0.391  0.42 10.72 ?  38  ALA   A HB1  1 
ATOM   1071 H HB1  B ALA   A 1 38  ? 21.740 -1.134  -0.647  0.58 11.27 ?  38  ALA   A HB1  1 
ATOM   1072 H HB2  A ALA   A 1 38  ? 21.197 -1.153  1.043   0.42 10.72 ?  38  ALA   A HB2  1 
ATOM   1073 H HB2  B ALA   A 1 38  ? 21.317 -1.661  0.791   0.58 11.27 ?  38  ALA   A HB2  1 
ATOM   1074 H HB3  A ALA   A 1 38  ? 21.470 0.395   0.810   0.42 10.72 ?  38  ALA   A HB3  1 
ATOM   1075 H HB3  B ALA   A 1 38  ? 21.419 -0.099  0.515   0.58 11.27 ?  38  ALA   A HB3  1 
ATOM   1076 N N    A ALA   A 1 39  ? 25.365 -0.095  0.023   0.42 9.31  ?  39  ALA   A N    1 
ATOM   1077 N N    B ALA   A 1 39  ? 25.379 -0.198  -0.116  0.58 10.16 ?  39  ALA   A N    1 
ATOM   1078 C CA   A ALA   A 1 39  ? 26.425 0.786   -0.447  0.42 9.25  ?  39  ALA   A CA   1 
ATOM   1079 C CA   B ALA   A 1 39  ? 26.339 0.772   -0.613  0.58 9.71  ?  39  ALA   A CA   1 
ATOM   1080 C C    A ALA   A 1 39  ? 26.596 0.717   -1.963  0.42 9.45  ?  39  ALA   A C    1 
ATOM   1081 C C    B ALA   A 1 39  ? 26.457 0.715   -2.133  0.58 9.58  ?  39  ALA   A C    1 
ATOM   1082 O O    A ALA   A 1 39  ? 26.142 -0.219  -2.625  0.42 9.82  ?  39  ALA   A O    1 
ATOM   1083 O O    B ALA   A 1 39  ? 26.031 -0.241  -2.784  0.58 10.33 ?  39  ALA   A O    1 
ATOM   1084 C CB   A ALA   A 1 39  ? 27.748 0.391   0.217   0.42 9.63  ?  39  ALA   A CB   1 
ATOM   1085 C CB   B ALA   A 1 39  ? 27.711 0.513   0.013   0.58 10.36 ?  39  ALA   A CB   1 
ATOM   1086 H H    A ALA   A 1 39  ? 25.634 -0.897  0.159   0.42 11.20 ?  39  ALA   A H    1 
ATOM   1087 H H    B ALA   A 1 39  ? 25.731 -0.959  0.106   0.58 12.22 ?  39  ALA   A H    1 
ATOM   1088 H HA   A ALA   A 1 39  ? 26.223 1.702   -0.204  0.42 11.13 ?  39  ALA   A HA   1 
ATOM   1089 H HA   B ALA   A 1 39  ? 26.045 1.659   -0.354  0.58 11.68 ?  39  ALA   A HA   1 
ATOM   1090 H HB1  A ALA   A 1 39  ? 28.451 0.980   -0.101  0.42 11.58 ?  39  ALA   A HB1  1 
ATOM   1091 H HB1  B ALA   A 1 39  ? 28.336 1.173   -0.326  0.58 12.45 ?  39  ALA   A HB1  1 
ATOM   1092 H HB2  A ALA   A 1 39  ? 27.655 0.480   1.180   0.42 11.58 ?  39  ALA   A HB2  1 
ATOM   1093 H HB2  B ALA   A 1 39  ? 27.640 0.596   0.980   0.58 12.45 ?  39  ALA   A HB2  1 
ATOM   1094 H HB3  A ALA   A 1 39  ? 27.956 -0.527  -0.011  0.42 11.58 ?  39  ALA   A HB3  1 
ATOM   1095 H HB3  B ALA   A 1 39  ? 28.005 -0.377  -0.221  0.58 12.45 ?  39  ALA   A HB3  1 
ATOM   1096 N N    A ASN   A 1 40  ? 27.285 1.725   -2.506  0.42 9.58  ?  40  ASN   A N    1 
ATOM   1097 N N    B ASN   A 1 40  ? 27.044 1.768   -2.696  0.58 8.94  ?  40  ASN   A N    1 
ATOM   1098 C CA   A ASN   A 1 40  ? 27.840 1.684   -3.855  0.42 9.37  ?  40  ASN   A CA   1 
ATOM   1099 C CA   B ASN   A 1 40  ? 27.586 1.717   -4.046  0.58 8.95  ?  40  ASN   A CA   1 
ATOM   1100 C C    A ASN   A 1 40  ? 29.364 1.585   -3.778  0.42 9.25  ?  40  ASN   A C    1 
ATOM   1101 C C    B ASN   A 1 40  ? 29.106 1.578   -3.977  0.58 8.44  ?  40  ASN   A C    1 
ATOM   1102 O O    A ASN   A 1 40  ? 29.959 1.718   -2.705  0.42 9.74  ?  40  ASN   A O    1 
ATOM   1103 O O    B ASN   A 1 40  ? 29.710 1.672   -2.908  0.58 8.39  ?  40  ASN   A O    1 
ATOM   1104 C CB   A ASN   A 1 40  ? 27.364 2.871   -4.714  0.42 10.47 ?  40  ASN   A CB   1 
ATOM   1105 C CB   B ASN   A 1 40  ? 27.144 2.925   -4.882  0.58 9.43  ?  40  ASN   A CB   1 
ATOM   1106 C CG   A ASN   A 1 40  ? 27.728 4.219   -4.124  0.42 11.69 ?  40  ASN   A CG   1 
ATOM   1107 C CG   B ASN   A 1 40  ? 27.513 4.242   -4.253  0.58 9.74  ?  40  ASN   A CG   1 
ATOM   1108 O OD1  A ASN   A 1 40  ? 28.883 4.466   -3.783  0.42 11.54 ?  40  ASN   A OD1  1 
ATOM   1109 O OD1  B ASN   A 1 40  ? 28.692 4.535   -4.056  0.58 10.39 ?  40  ASN   A OD1  1 
ATOM   1110 N ND2  A ASN   A 1 40  ? 26.736 5.102   -4.007  0.42 13.01 ?  40  ASN   A ND2  1 
ATOM   1111 N ND2  B ASN   A 1 40  ? 26.506 5.054   -3.946  0.58 10.90 ?  40  ASN   A ND2  1 
ATOM   1112 H H    A ASN   A 1 40  ? 27.458 2.464   -2.097  0.42 11.52 ?  40  ASN   A H    1 
ATOM   1113 H H    B ASN   A 1 40  ? 27.134 2.529   -2.308  0.58 10.75 ?  40  ASN   A H    1 
ATOM   1114 H HA   A ASN   A 1 40  ? 27.522 0.884   -4.292  0.42 11.27 ?  40  ASN   A HA   1 
ATOM   1115 H HA   B ASN   A 1 40  ? 27.234 0.918   -4.480  0.58 10.77 ?  40  ASN   A HA   1 
ATOM   1116 H HB2  A ASN   A 1 40  ? 27.771 2.808   -5.599  0.42 12.59 ?  40  ASN   A HB2  1 
ATOM   1117 H HB2  B ASN   A 1 40  ? 27.571 2.873   -5.745  0.58 11.35 ?  40  ASN   A HB2  1 
ATOM   1118 H HB3  A ASN   A 1 40  ? 26.400 2.838   -4.799  0.42 12.59 ?  40  ASN   A HB3  1 
ATOM   1119 H HB3  B ASN   A 1 40  ? 26.178 2.897   -4.983  0.58 11.35 ?  40  ASN   A HB3  1 
ATOM   1120 H HD21 A ASN   A 1 40  ? 26.889 5.889   -3.689  0.42 15.64 ?  40  ASN   A HD21 1 
ATOM   1121 H HD21 B ASN   A 1 40  ? 26.670 5.819   -3.584  0.58 13.11 ?  40  ASN   A HD21 1 
ATOM   1122 H HD22 A ASN   A 1 40  ? 25.939 4.886   -4.246  0.42 15.64 ?  40  ASN   A HD22 1 
ATOM   1123 H HD22 B ASN   A 1 40  ? 25.697 4.820   -4.108  0.58 13.11 ?  40  ASN   A HD22 1 
ATOM   1124 N N    A VAL   A 1 41  ? 29.996 1.330   -4.932  0.42 9.13  ?  41  VAL   A N    1 
ATOM   1125 N N    B VAL   A 1 41  ? 29.722 1.345   -5.139  0.58 9.06  ?  41  VAL   A N    1 
ATOM   1126 C CA   A VAL   A 1 41  ? 31.425 1.009   -4.933  0.42 9.27  ?  41  VAL   A CA   1 
ATOM   1127 C CA   B VAL   A 1 41  ? 31.150 1.036   -5.178  0.58 9.52  ?  41  VAL   A CA   1 
ATOM   1128 C C    A VAL   A 1 41  ? 32.265 2.166   -4.412  0.42 9.27  ?  41  VAL   A C    1 
ATOM   1129 C C    B VAL   A 1 41  ? 32.015 2.188   -4.687  0.58 9.23  ?  41  VAL   A C    1 
ATOM   1130 O O    A VAL   A 1 41  ? 33.362 1.951   -3.878  0.42 9.41  ?  41  VAL   A O    1 
ATOM   1131 O O    B VAL   A 1 41  ? 33.180 1.972   -4.326  0.58 8.99  ?  41  VAL   A O    1 
ATOM   1132 C CB   A VAL   A 1 41  ? 31.926 0.506   -6.309  0.42 8.74  ?  41  VAL   A CB   1 
ATOM   1133 C CB   B VAL   A 1 41  ? 31.603 0.595   -6.588  0.58 11.12 ?  41  VAL   A CB   1 
ATOM   1134 C CG1  A VAL   A 1 41  ? 31.210 -0.772  -6.721  0.42 9.34  ?  41  VAL   A CG1  1 
ATOM   1135 C CG1  B VAL   A 1 41  ? 30.915 -0.697  -7.007  0.58 12.23 ?  41  VAL   A CG1  1 
ATOM   1136 C CG2  A VAL   A 1 41  ? 31.802 1.571   -7.392  0.42 8.39  ?  41  VAL   A CG2  1 
ATOM   1137 C CG2  B VAL   A 1 41  ? 31.368 1.701   -7.617  0.58 11.70 ?  41  VAL   A CG2  1 
ATOM   1138 H H    A VAL   A 1 41  ? 29.630 1.324   -5.707  0.42 10.98 ?  41  VAL   A H    1 
ATOM   1139 H H    B VAL   A 1 41  ? 29.328 1.336   -5.901  0.58 10.90 ?  41  VAL   A H    1 
ATOM   1140 H HA   A VAL   A 1 41  ? 31.571 0.286   -4.314  0.42 11.15 ?  41  VAL   A HA   1 
ATOM   1141 H HA   B VAL   A 1 41  ? 31.307 0.283   -4.584  0.58 11.45 ?  41  VAL   A HA   1 
ATOM   1142 H HB   A VAL   A 1 41  ? 32.872 0.293   -6.236  0.42 10.51 ?  41  VAL   A HB   1 
ATOM   1143 H HB   B VAL   A 1 41  ? 32.556 0.422   -6.559  0.58 13.37 ?  41  VAL   A HB   1 
ATOM   1144 H HG11 A VAL   A 1 41  ? 31.560 -1.076  -7.574  0.42 11.24 ?  41  VAL   A HG11 1 
ATOM   1145 H HG11 B VAL   A 1 41  ? 31.211 -0.936  -7.898  0.58 14.70 ?  41  VAL   A HG11 1 
ATOM   1146 H HG12 A VAL   A 1 41  ? 31.355 -1.448  -6.043  0.42 11.24 ?  41  VAL   A HG12 1 
ATOM   1147 H HG12 B VAL   A 1 41  ? 31.153 -1.398  -6.380  0.58 14.70 ?  41  VAL   A HG12 1 
ATOM   1148 H HG13 A VAL   A 1 41  ? 30.260 -0.585  -6.805  0.42 11.24 ?  41  VAL   A HG13 1 
ATOM   1149 H HG13 B VAL   A 1 41  ? 29.955 -0.561  -7.001  0.58 14.70 ?  41  VAL   A HG13 1 
ATOM   1150 H HG21 A VAL   A 1 41  ? 32.045 1.183   -8.250  0.42 10.10 ?  41  VAL   A HG21 1 
ATOM   1151 H HG21 B VAL   A 1 41  ? 31.620 1.370   -8.493  0.58 14.07 ?  41  VAL   A HG21 1 
ATOM   1152 H HG22 A VAL   A 1 41  ? 30.886 1.884   -7.420  0.42 10.10 ?  41  VAL   A HG22 1 
ATOM   1153 H HG22 B VAL   A 1 41  ? 30.429 1.943   -7.612  0.58 14.07 ?  41  VAL   A HG22 1 
ATOM   1154 H HG23 A VAL   A 1 41  ? 32.399 2.306   -7.184  0.42 10.10 ?  41  VAL   A HG23 1 
ATOM   1155 H HG23 B VAL   A 1 41  ? 31.910 2.470   -7.384  0.58 14.07 ?  41  VAL   A HG23 1 
ATOM   1156 N N    A TYR   A 1 42  ? 31.782 3.397   -4.554  0.42 9.64  ?  42  TYR   A N    1 
ATOM   1157 N N    B TYR   A 1 42  ? 31.492 3.415   -4.707  0.58 9.43  ?  42  TYR   A N    1 
ATOM   1158 C CA   A TYR   A 1 42  ? 32.515 4.579   -4.118  0.42 9.77  ?  42  TYR   A CA   1 
ATOM   1159 C CA   B TYR   A 1 42  ? 32.233 4.603   -4.294  0.58 9.61  ?  42  TYR   A CA   1 
ATOM   1160 C C    A TYR   A 1 42  ? 32.195 4.957   -2.681  0.42 9.70  ?  42  TYR   A C    1 
ATOM   1161 C C    B TYR   A 1 42  ? 32.012 4.970   -2.835  0.58 9.71  ?  42  TYR   A C    1 
ATOM   1162 O O    A TYR   A 1 42  ? 32.767 5.925   -2.167  0.42 10.04 ?  42  TYR   A O    1 
ATOM   1163 O O    B TYR   A 1 42  ? 32.568 5.975   -2.374  0.58 10.19 ?  42  TYR   A O    1 
ATOM   1164 C CB   A TYR   A 1 42  ? 32.217 5.767   -5.051  0.42 10.35 ?  42  TYR   A CB   1 
ATOM   1165 C CB   B TYR   A 1 42  ? 31.851 5.799   -5.181  0.58 10.10 ?  42  TYR   A CB   1 
ATOM   1166 C CG   A TYR   A 1 42  ? 32.378 5.432   -6.522  0.42 10.60 ?  42  TYR   A CG   1 
ATOM   1167 C CG   B TYR   A 1 42  ? 32.004 5.512   -6.652  0.58 10.59 ?  42  TYR   A CG   1 
ATOM   1168 C CD1  A TYR   A 1 42  ? 33.635 5.222   -7.068  0.42 11.11 ?  42  TYR   A CD1  1 
ATOM   1169 C CD1  B TYR   A 1 42  ? 33.257 5.326   -7.216  0.58 11.03 ?  42  TYR   A CD1  1 
ATOM   1170 C CD2  A TYR   A 1 42  ? 31.274 5.308   -7.362  0.42 10.89 ?  42  TYR   A CD2  1 
ATOM   1171 C CD2  B TYR   A 1 42  ? 30.895 5.410   -7.478  0.58 12.21 ?  42  TYR   A CD2  1 
ATOM   1172 C CE1  A TYR   A 1 42  ? 33.795 4.900   -8.403  0.42 11.05 ?  42  TYR   A CE1  1 
ATOM   1173 C CE1  B TYR   A 1 42  ? 33.399 5.047   -8.566  0.58 11.60 ?  42  TYR   A CE1  1 
ATOM   1174 C CE2  A TYR   A 1 42  ? 31.427 4.994   -8.708  0.42 11.45 ?  42  TYR   A CE2  1 
ATOM   1175 C CE2  B TYR   A 1 42  ? 31.026 5.145   -8.824  0.58 13.13 ?  42  TYR   A CE2  1 
ATOM   1176 C CZ   A TYR   A 1 42  ? 32.694 4.792   -9.219  0.42 11.43 ?  42  TYR   A CZ   1 
ATOM   1177 C CZ   B TYR   A 1 42  ? 32.274 4.958   -9.365  0.58 12.71 ?  42  TYR   A CZ   1 
ATOM   1178 O OH   A TYR   A 1 42  ? 32.873 4.472   -10.546 0.42 12.62 ?  42  TYR   A OH   1 
ATOM   1179 O OH   B TYR   A 1 42  ? 32.380 4.695   -10.711 0.58 13.87 ?  42  TYR   A OH   1 
ATOM   1180 H H    A TYR   A 1 42  ? 31.018 3.579   -4.886  0.42 11.60 ?  42  TYR   A H    1 
ATOM   1181 H H    B TYR   A 1 42  ? 30.692 3.589   -4.983  0.58 11.34 ?  42  TYR   A H    1 
ATOM   1182 H HA   A TYR   A 1 42  ? 33.470 4.404   -4.166  0.42 11.75 ?  42  TYR   A HA   1 
ATOM   1183 H HA   B TYR   A 1 42  ? 33.175 4.442   -4.415  0.58 11.56 ?  42  TYR   A HA   1 
ATOM   1184 H HB2  A TYR   A 1 42  ? 31.305 6.058   -4.907  0.42 12.45 ?  42  TYR   A HB2  1 
ATOM   1185 H HB2  B TYR   A 1 42  ? 30.922 6.034   -5.022  0.58 12.15 ?  42  TYR   A HB2  1 
ATOM   1186 H HB3  A TYR   A 1 42  ? 32.830 6.495   -4.841  0.42 12.45 ?  42  TYR   A HB3  1 
ATOM   1187 H HB3  B TYR   A 1 42  ? 32.423 6.552   -4.963  0.58 12.15 ?  42  TYR   A HB3  1 
ATOM   1188 H HD1  A TYR   A 1 42  ? 34.387 5.294   -6.525  0.42 13.35 ?  42  TYR   A HD1  1 
ATOM   1189 H HD1  B TYR   A 1 42  ? 34.016 5.380   -6.676  0.58 13.26 ?  42  TYR   A HD1  1 
ATOM   1190 H HD2  A TYR   A 1 42  ? 30.420 5.449   -7.018  0.42 13.09 ?  42  TYR   A HD2  1 
ATOM   1191 H HD2  B TYR   A 1 42  ? 30.046 5.537   -7.119  0.58 14.67 ?  42  TYR   A HD2  1 
ATOM   1192 H HE1  A TYR   A 1 42  ? 34.646 4.768   -8.754  0.42 13.29 ?  42  TYR   A HE1  1 
ATOM   1193 H HE1  B TYR   A 1 42  ? 34.248 4.924   -8.927  0.58 13.94 ?  42  TYR   A HE1  1 
ATOM   1194 H HE2  A TYR   A 1 42  ? 30.678 4.921   -9.260  0.42 13.77 ?  42  TYR   A HE2  1 
ATOM   1195 H HE2  B TYR   A 1 42  ? 30.271 5.084   -9.362  0.58 15.78 ?  42  TYR   A HE2  1 
ATOM   1196 H HH   A TYR   A 1 42  ? 33.675 4.277   -10.691 0.42 15.17 ?  42  TYR   A HH   1 
ATOM   1197 H HH   B TYR   A 1 42  ? 33.191 4.607   -10.917 0.58 16.68 ?  42  TYR   A HH   1 
ATOM   1198 N N    A LEU   A 1 43  ? 31.293 4.223   -2.032  0.42 9.32  ?  43  LEU   A N    1 
ATOM   1199 N N    B LEU   A 1 43  ? 31.199 4.201   -2.113  0.58 9.57  ?  43  LEU   A N    1 
ATOM   1200 C CA   A LEU   A 1 43  ? 30.838 4.542   -0.682  0.42 9.40  ?  43  LEU   A CA   1 
ATOM   1201 C CA   B LEU   A 1 43  ? 30.756 4.563   -0.767  0.58 9.37  ?  43  LEU   A CA   1 
ATOM   1202 C C    A LEU   A 1 43  ? 30.364 5.990   -0.577  0.42 9.50  ?  43  LEU   A C    1 
ATOM   1203 C C    B LEU   A 1 43  ? 30.269 6.009   -0.700  0.58 9.30  ?  43  LEU   A C    1 
ATOM   1204 O O    A LEU   A 1 43  ? 30.604 6.677   0.419   0.42 10.34 ?  43  LEU   A O    1 
ATOM   1205 O O    B LEU   A 1 43  ? 30.517 6.725   0.271   0.58 10.08 ?  43  LEU   A O    1 
ATOM   1206 C CB   A LEU   A 1 43  ? 31.895 4.216   0.372   0.42 9.77  ?  43  LEU   A CB   1 
ATOM   1207 C CB   B LEU   A 1 43  ? 31.813 4.277   0.298   0.58 9.56  ?  43  LEU   A CB   1 
ATOM   1208 C CG   A LEU   A 1 43  ? 32.403 2.774   0.421   0.42 10.08 ?  43  LEU   A CG   1 
ATOM   1209 C CG   B LEU   A 1 43  ? 32.293 2.830   0.430   0.58 10.01 ?  43  LEU   A CG   1 
ATOM   1210 C CD1  A LEU   A 1 43  ? 33.501 2.661   1.459   0.42 10.53 ?  43  LEU   A CD1  1 
ATOM   1211 C CD1  B LEU   A 1 43  ? 33.298 2.732   1.564   0.58 10.84 ?  43  LEU   A CD1  1 
ATOM   1212 C CD2  A LEU   A 1 43  ? 31.284 1.788   0.717   0.42 10.16 ?  43  LEU   A CD2  1 
ATOM   1213 C CD2  B LEU   A 1 43  ? 31.140 1.849   0.635   0.58 10.37 ?  43  LEU   A CD2  1 
ATOM   1214 H H    A LEU   A 1 43  ? 30.918 3.523   -2.361  0.42 11.21 ?  43  LEU   A H    1 
ATOM   1215 H H    B LEU   A 1 43  ? 30.873 3.452   -2.386  0.58 11.52 ?  43  LEU   A H    1 
ATOM   1216 H HA   A LEU   A 1 43  ? 30.068 3.983   -0.490  0.42 11.30 ?  43  LEU   A HA   1 
ATOM   1217 H HA   B LEU   A 1 43  ? 29.988 4.004   -0.551  0.58 11.27 ?  43  LEU   A HA   1 
ATOM   1218 H HB2  A LEU   A 1 43  ? 32.662 4.782   0.221   0.42 11.75 ?  43  LEU   A HB2  1 
ATOM   1219 H HB2  B LEU   A 1 43  ? 32.588 4.820   0.108   0.58 11.50 ?  43  LEU   A HB2  1 
ATOM   1220 H HB3  A LEU   A 1 43  ? 31.517 4.406   1.245   0.42 11.75 ?  43  LEU   A HB3  1 
ATOM   1221 H HB3  B LEU   A 1 43  ? 31.444 4.530   1.161   0.58 11.50 ?  43  LEU   A HB3  1 
ATOM   1222 H HG   A LEU   A 1 43  ? 32.786 2.540   -0.440  0.42 12.12 ?  43  LEU   A HG   1 
ATOM   1223 H HG   B LEU   A 1 43  ? 32.750 2.577   -0.386  0.58 12.04 ?  43  LEU   A HG   1 
ATOM   1224 H HD11 A LEU   A 1 43  ? 33.820 1.745   1.486   0.42 12.66 ?  43  LEU   A HD11 1 
ATOM   1225 H HD11 B LEU   A 1 43  ? 33.601 1.814   1.641   0.58 13.04 ?  43  LEU   A HD11 1 
ATOM   1226 H HD12 A LEU   A 1 43  ? 34.226 3.258   1.217   0.42 12.66 ?  43  LEU   A HD12 1 
ATOM   1227 H HD12 B LEU   A 1 43  ? 34.051 3.313   1.367   0.58 13.04 ?  43  LEU   A HD12 1 
ATOM   1228 H HD13 A LEU   A 1 43  ? 33.141 2.911   2.325   0.42 12.66 ?  43  LEU   A HD13 1 
ATOM   1229 H HD13 B LEU   A 1 43  ? 32.872 3.010   2.389   0.58 13.04 ?  43  LEU   A HD13 1 
ATOM   1230 H HD21 A LEU   A 1 43  ? 31.661 0.900   0.813   0.42 12.22 ?  43  LEU   A HD21 1 
ATOM   1231 H HD21 B LEU   A 1 43  ? 31.503 0.969   0.819   0.58 12.47 ?  43  LEU   A HD21 1 
ATOM   1232 H HD22 A LEU   A 1 43  ? 30.844 2.053   1.540   0.42 12.22 ?  43  LEU   A HD22 1 
ATOM   1233 H HD22 B LEU   A 1 43  ? 30.600 2.150   1.382   0.58 12.47 ?  43  LEU   A HD22 1 
ATOM   1234 H HD23 A LEU   A 1 43  ? 30.652 1.803   -0.018  0.42 12.22 ?  43  LEU   A HD23 1 
ATOM   1235 H HD23 B LEU   A 1 43  ? 30.604 1.824   -0.173  0.58 12.47 ?  43  LEU   A HD23 1 
ATOM   1236 N N    A LYS   A 1 44  ? 29.671 6.452   -1.618  0.42 9.86  ?  44  LYS   A N    1 
ATOM   1237 N N    B LYS   A 1 44  ? 29.536 6.430   -1.734  0.58 9.27  ?  44  LYS   A N    1 
ATOM   1238 C CA   A LYS   A 1 44  ? 29.035 7.766   -1.614  0.42 10.41 ?  44  LYS   A CA   1 
ATOM   1239 C CA   B LYS   A 1 44  ? 28.880 7.738   -1.757  0.58 9.79  ?  44  LYS   A CA   1 
ATOM   1240 C C    A LYS   A 1 44  ? 27.592 7.581   -1.163  0.42 9.89  ?  44  LYS   A C    1 
ATOM   1241 C C    B LYS   A 1 44  ? 27.469 7.554   -1.217  0.58 9.40  ?  44  LYS   A C    1 
ATOM   1242 O O    A LYS   A 1 44  ? 26.754 7.068   -1.913  0.42 10.81 ?  44  LYS   A O    1 
ATOM   1243 O O    B LYS   A 1 44  ? 26.577 7.063   -1.914  0.58 10.15 ?  44  LYS   A O    1 
ATOM   1244 C CB   A LYS   A 1 44  ? 29.115 8.415   -2.993  0.42 11.61 ?  44  LYS   A CB   1 
ATOM   1245 C CB   B LYS   A 1 44  ? 28.888 8.327   -3.164  0.58 12.19 ?  44  LYS   A CB   1 
ATOM   1246 C CG   A LYS   A 1 44  ? 30.522 8.790   -3.425  0.42 13.56 ?  44  LYS   A CG   1 
ATOM   1247 C CG   B LYS   A 1 44  ? 30.219 8.926   -3.583  0.58 15.25 ?  44  LYS   A CG   1 
ATOM   1248 C CD   A LYS   A 1 44  ? 31.210 9.694   -2.412  0.42 17.66 ?  44  LYS   A CD   1 
ATOM   1249 C CD   B LYS   A 1 44  ? 30.769 9.870   -2.517  0.58 19.11 ?  44  LYS   A CD   1 
ATOM   1250 C CE   A LYS   A 1 44  ? 32.547 10.175  -2.931  0.42 20.26 ?  44  LYS   A CE   1 
ATOM   1251 C CE   B LYS   A 1 44  ? 32.029 10.565  -2.981  0.58 21.65 ?  44  LYS   A CE   1 
ATOM   1252 N NZ   A LYS   A 1 44  ? 33.325 10.856  -1.870  0.42 21.52 ?  44  LYS   A NZ   1 
ATOM   1253 N NZ   B LYS   A 1 44  ? 32.846 11.044  -1.834  0.58 23.58 ?  44  LYS   A NZ   1 
ATOM   1254 H H    A LYS   A 1 44  ? 29.558 6.015   -2.351  0.42 11.86 ?  44  LYS   A H    1 
ATOM   1255 H H    B LYS   A 1 44  ? 29.409 5.973   -2.452  0.58 11.15 ?  44  LYS   A H    1 
ATOM   1256 H HA   A LYS   A 1 44  ? 29.476 8.339   -0.968  0.42 12.52 ?  44  LYS   A HA   1 
ATOM   1257 H HA   B LYS   A 1 44  ? 29.335 8.336   -1.146  0.58 11.78 ?  44  LYS   A HA   1 
ATOM   1258 H HB2  A LYS   A 1 44  ? 28.757 7.797   -3.647  0.42 13.96 ?  44  LYS   A HB2  1 
ATOM   1259 H HB2  B LYS   A 1 44  ? 28.667 7.626   -3.798  0.58 14.66 ?  44  LYS   A HB2  1 
ATOM   1260 H HB3  A LYS   A 1 44  ? 28.580 9.226   -2.982  0.42 13.96 ?  44  LYS   A HB3  1 
ATOM   1261 H HB3  B LYS   A 1 44  ? 28.218 9.031   -3.213  0.58 14.66 ?  44  LYS   A HB3  1 
ATOM   1262 H HG2  A LYS   A 1 44  ? 31.052 7.987   -3.522  0.42 16.30 ?  44  LYS   A HG2  1 
ATOM   1263 H HG2  B LYS   A 1 44  ? 30.861 8.217   -3.726  0.58 18.33 ?  44  LYS   A HG2  1 
ATOM   1264 H HG3  A LYS   A 1 44  ? 30.478 9.268   -4.271  0.42 16.30 ?  44  LYS   A HG3  1 
ATOM   1265 H HG3  B LYS   A 1 44  ? 30.098 9.439   -4.402  0.58 18.33 ?  44  LYS   A HG3  1 
ATOM   1266 H HD2  A LYS   A 1 44  ? 30.643 10.465  -2.236  0.42 21.22 ?  44  LYS   A HD2  1 
ATOM   1267 H HD2  B LYS   A 1 44  ? 30.097 10.534  -2.299  0.58 22.96 ?  44  LYS   A HD2  1 
ATOM   1268 H HD3  A LYS   A 1 44  ? 31.363 9.197   -1.593  0.42 21.22 ?  44  LYS   A HD3  1 
ATOM   1269 H HD3  B LYS   A 1 44  ? 31.003 9.353   -1.726  0.58 22.96 ?  44  LYS   A HD3  1 
ATOM   1270 H HE2  A LYS   A 1 44  ? 33.056 9.414   -3.245  0.42 24.34 ?  44  LYS   A HE2  1 
ATOM   1271 H HE2  B LYS   A 1 44  ? 32.567 9.939   -3.495  0.58 26.01 ?  44  LYS   A HE2  1 
ATOM   1272 H HE3  A LYS   A 1 44  ? 32.397 10.803  -3.656  0.42 24.34 ?  44  LYS   A HE3  1 
ATOM   1273 H HE3  B LYS   A 1 44  ? 31.790 11.327  -3.524  0.58 26.01 ?  44  LYS   A HE3  1 
ATOM   1274 H HZ1  A LYS   A 1 44  ? 34.110 11.117  -2.192  0.42 25.85 ?  44  LYS   A HZ1  1 
ATOM   1275 H HZ1  B LYS   A 1 44  ? 33.582 11.448  -2.132  0.58 28.32 ?  44  LYS   A HZ1  1 
ATOM   1276 H HZ2  A LYS   A 1 44  ? 32.878 11.573  -1.582  0.42 25.85 ?  44  LYS   A HZ2  1 
ATOM   1277 H HZ2  B LYS   A 1 44  ? 32.378 11.620  -1.346  0.58 28.32 ?  44  LYS   A HZ2  1 
ATOM   1278 H HZ3  A LYS   A 1 44  ? 33.455 10.304  -1.187  0.42 25.85 ?  44  LYS   A HZ3  1 
ATOM   1279 H HZ3  B LYS   A 1 44  ? 33.085 10.356  -1.319  0.58 28.32 ?  44  LYS   A HZ3  1 
ATOM   1280 N N    A HIS   A 1 45  ? 27.310 7.980   0.072   0.42 9.27  ?  45  HIS   A N    1 
ATOM   1281 N N    B HIS   A 1 45  ? 27.273 7.927   0.048   0.58 9.29  ?  45  HIS   A N    1 
ATOM   1282 C CA   A HIS   A 1 45  ? 26.070 7.600   0.745   0.42 8.97  ?  45  HIS   A CA   1 
ATOM   1283 C CA   B HIS   A 1 45  ? 26.033 7.632   0.766   0.58 9.83  ?  45  HIS   A CA   1 
ATOM   1284 C C    A HIS   A 1 45  ? 25.025 8.707   0.597   0.42 9.01  ?  45  HIS   A C    1 
ATOM   1285 C C    B HIS   A 1 45  ? 25.040 8.775   0.571   0.58 10.39 ?  45  HIS   A C    1 
ATOM   1286 O O    A HIS   A 1 45  ? 24.620 9.366   1.553   0.42 9.60  ?  45  HIS   A O    1 
ATOM   1287 O O    B HIS   A 1 45  ? 24.843 9.626   1.439   0.58 11.39 ?  45  HIS   A O    1 
ATOM   1288 C CB   A HIS   A 1 45  ? 26.357 7.267   2.203   0.42 8.68  ?  45  HIS   A CB   1 
ATOM   1289 C CB   B HIS   A 1 45  ? 26.321 7.420   2.243   0.58 9.78  ?  45  HIS   A CB   1 
ATOM   1290 C CG   A HIS   A 1 45  ? 27.476 6.291   2.389   0.42 8.21  ?  45  HIS   A CG   1 
ATOM   1291 C CG   B HIS   A 1 45  ? 27.438 6.467   2.512   0.58 9.41  ?  45  HIS   A CG   1 
ATOM   1292 N ND1  A HIS   A 1 45  ? 27.452 5.018   1.860   0.42 8.39  ?  45  HIS   A ND1  1 
ATOM   1293 N ND1  B HIS   A 1 45  ? 27.452 5.177   2.032   0.58 9.65  ?  45  HIS   A ND1  1 
ATOM   1294 C CD2  A HIS   A 1 45  ? 28.659 6.411   3.037   0.42 9.10  ?  45  HIS   A CD2  1 
ATOM   1295 C CD2  B HIS   A 1 45  ? 28.585 6.630   3.211   0.58 8.83  ?  45  HIS   A CD2  1 
ATOM   1296 C CE1  A HIS   A 1 45  ? 28.572 4.394   2.185   0.42 9.22  ?  45  HIS   A CE1  1 
ATOM   1297 C CE1  B HIS   A 1 45  ? 28.565 4.585   2.431   0.58 8.47  ?  45  HIS   A CE1  1 
ATOM   1298 N NE2  A HIS   A 1 45  ? 29.321 5.217   2.898   0.42 9.76  ?  45  HIS   A NE2  1 
ATOM   1299 N NE2  B HIS   A 1 45  ? 29.269 5.444   3.148   0.58 8.31  ?  45  HIS   A NE2  1 
ATOM   1300 H H    A HIS   A 1 45  ? 27.826 8.479   0.549   0.42 11.15 ?  45  HIS   A H    1 
ATOM   1301 H H    B HIS   A 1 45  ? 27.854 8.350   0.521   0.58 11.17 ?  45  HIS   A H    1 
ATOM   1302 H HA   A HIS   A 1 45  ? 25.714 6.804   0.327   0.42 10.79 ?  45  HIS   A HA   1 
ATOM   1303 H HA   B HIS   A 1 45  ? 25.637 6.821   0.408   0.58 11.83 ?  45  HIS   A HA   1 
ATOM   1304 H HB2  A HIS   A 1 45  ? 26.591 8.077   2.677   0.42 10.45 ?  45  HIS   A HB2  1 
ATOM   1305 H HB2  B HIS   A 1 45  ? 26.550 8.272   2.642   0.58 11.77 ?  45  HIS   A HB2  1 
ATOM   1306 H HB3  A HIS   A 1 45  ? 25.559 6.873   2.599   0.42 10.45 ?  45  HIS   A HB3  1 
ATOM   1307 H HB3  B HIS   A 1 45  ? 25.520 7.065   2.666   0.58 11.77 ?  45  HIS   A HB3  1 
ATOM   1308 H HD2  A HIS   A 1 45  ? 28.966 7.161   3.489   0.42 10.94 ?  45  HIS   A HD2  1 
ATOM   1309 H HD2  B HIS   A 1 45  ? 28.858 7.404   3.649   0.58 10.63 ?  45  HIS   A HD2  1 
ATOM   1310 H HE1  A HIS   A 1 45  ? 28.799 3.515   1.959   0.42 11.09 ?  45  HIS   A HE1  1 
ATOM   1311 H HE1  B HIS   A 1 45  ? 28.806 3.707   2.244   0.58 10.19 ?  45  HIS   A HE1  1 
ATOM   1312 H HE2  A HIS   A 1 45  ? 30.101 5.034   3.222   0.42 11.73 ?  45  HIS   A HE2  1 
ATOM   1313 H HE2  B HIS   A 1 45  ? 30.031 5.286   3.512   0.58 10.00 ?  45  HIS   A HE2  1 
ATOM   1314 N N    A GLY   A 1 46  ? 24.577 8.886   -0.644  0.42 9.54  ?  46  GLY   A N    1 
ATOM   1315 N N    B GLY   A 1 46  ? 24.381 8.775   -0.582  0.58 10.63 ?  46  GLY   A N    1 
ATOM   1316 C CA   A GLY   A 1 46  ? 23.773 10.042  -0.999  0.42 9.97  ?  46  GLY   A CA   1 
ATOM   1317 C CA   B GLY   A 1 46  ? 23.560 9.915   -0.942  0.58 11.20 ?  46  GLY   A CA   1 
ATOM   1318 C C    A GLY   A 1 46  ? 22.273 9.908   -0.801  0.42 9.60  ?  46  GLY   A C    1 
ATOM   1319 C C    B GLY   A 1 46  ? 22.102 9.818   -0.544  0.58 10.32 ?  46  GLY   A C    1 
ATOM   1320 O O    A GLY   A 1 46  ? 21.588 10.911  -0.570  0.42 9.54  ?  46  GLY   A O    1 
ATOM   1321 O O    B GLY   A 1 46  ? 21.507 10.805  -0.097  0.58 11.30 ?  46  GLY   A O    1 
ATOM   1322 H H    A GLY   A 1 46  ? 24.740 8.351   -1.295  0.42 11.47 ?  46  GLY   A H    1 
ATOM   1323 H H    B GLY   A 1 46  ? 24.386 8.133   -1.155  0.58 12.79 ?  46  GLY   A H    1 
ATOM   1324 H HA2  A GLY   A 1 46  ? 24.081 10.800  -0.476  0.42 11.99 ?  46  GLY   A HA2  1 
ATOM   1325 H HA2  B GLY   A 1 46  ? 23.923 10.709  -0.519  0.58 13.46 ?  46  GLY   A HA2  1 
ATOM   1326 H HA3  A GLY   A 1 46  ? 23.933 10.245  -1.934  0.42 11.99 ?  46  GLY   A HA3  1 
ATOM   1327 H HA3  B GLY   A 1 46  ? 23.602 10.038  -1.899  0.58 13.46 ?  46  GLY   A HA3  1 
ATOM   1328 N N    A GLY   A 1 47  ? 21.744 8.692   -0.915  0.42 9.88  ?  47  GLY   A N    1 
ATOM   1329 N N    B GLY   A 1 47  ? 21.510 8.638   -0.711  0.58 10.40 ?  47  GLY   A N    1 
ATOM   1330 C CA   A GLY   A 1 47  ? 20.308 8.488   -0.866  0.42 9.47  ?  47  GLY   A CA   1 
ATOM   1331 C CA   B GLY   A 1 47  ? 20.081 8.472   -0.530  0.58 10.05 ?  47  GLY   A CA   1 
ATOM   1332 C C    A GLY   A 1 47  ? 19.987 7.053   -0.506  0.42 9.45  ?  47  GLY   A C    1 
ATOM   1333 C C    B GLY   A 1 47  ? 19.741 7.041   -0.178  0.58 9.35  ?  47  GLY   A C    1 
ATOM   1334 O O    A GLY   A 1 47  ? 20.879 6.231   -0.289  0.42 9.97  ?  47  GLY   A O    1 
ATOM   1335 O O    B GLY   A 1 47  ? 20.619 6.191   -0.017  0.58 9.68  ?  47  GLY   A O    1 
ATOM   1336 H H    A GLY   A 1 47  ? 22.199 7.969   -1.021  0.42 11.89 ?  47  GLY   A H    1 
ATOM   1337 H H    B GLY   A 1 47  ? 21.921 7.916   -0.924  0.58 12.51 ?  47  GLY   A H    1 
ATOM   1338 H HA2  A GLY   A 1 47  ? 19.915 9.083   -0.205  0.42 11.39 ?  47  GLY   A HA2  1 
ATOM   1339 H HA2  B GLY   A 1 47  ? 19.767 9.048   0.182   0.58 12.08 ?  47  GLY   A HA2  1 
ATOM   1340 H HA3  A GLY   A 1 47  ? 19.923 8.696   -1.736  0.42 11.39 ?  47  GLY   A HA3  1 
ATOM   1341 H HA3  B GLY   A 1 47  ? 19.615 8.709   -1.350  0.58 12.08 ?  47  GLY   A HA3  1 
ATOM   1342 N N    A GLY   A 1 48  ? 18.693 6.752   -0.451  0.42 9.21  ?  48  GLY   A N    1 
ATOM   1343 N N    B GLY   A 1 48  ? 18.441 6.782   -0.060  0.58 9.71  ?  48  GLY   A N    1 
ATOM   1344 C CA   A GLY   A 1 48  ? 18.294 5.407   -0.072  0.42 9.32  ?  48  GLY   A CA   1 
ATOM   1345 C CA   B GLY   A 1 48  ? 18.010 5.452   0.320   0.58 9.62  ?  48  GLY   A CA   1 
ATOM   1346 C C    A GLY   A 1 48  ? 18.710 5.070   1.351   0.42 9.04  ?  48  GLY   A C    1 
ATOM   1347 C C    B GLY   A 1 48  ? 18.586 5.043   1.664   0.58 9.73  ?  48  GLY   A C    1 
ATOM   1348 O O    A GLY   A 1 48  ? 18.840 5.946   2.214   0.42 9.09  ?  48  GLY   A O    1 
ATOM   1349 O O    B GLY   A 1 48  ? 18.748 5.856   2.584   0.58 9.97  ?  48  GLY   A O    1 
ATOM   1350 H H    A GLY   A 1 48  ? 18.048 7.292   -0.628  0.42 11.08 ?  48  GLY   A H    1 
ATOM   1351 H H    B GLY   A 1 48  ? 17.797 7.347   -0.186  0.58 11.68 ?  48  GLY   A H    1 
ATOM   1352 H HA2  A GLY   A 1 48  ? 17.333 5.322   -0.138  0.42 11.22 ?  48  GLY   A HA2  1 
ATOM   1353 H HA2  B GLY   A 1 48  ? 17.039 5.418   0.373   0.58 11.57 ?  48  GLY   A HA2  1 
ATOM   1354 H HA3  A GLY   A 1 48  ? 18.706 4.763   -0.670  0.42 11.22 ?  48  GLY   A HA3  1 
ATOM   1355 H HA3  B GLY   A 1 48  ? 18.301 4.807   -0.349  0.58 11.57 ?  48  GLY   A HA3  1 
ATOM   1356 N N    A VAL   A 1 49  ? 18.924 3.774   1.605   0.42 9.78  ?  49  VAL   A N    1 
ATOM   1357 N N    B VAL   A 1 49  ? 18.893 3.750   1.779   0.58 10.02 ?  49  VAL   A N    1 
ATOM   1358 C CA   A VAL   A 1 49  ? 19.377 3.347   2.929   0.42 10.14 ?  49  VAL   A CA   1 
ATOM   1359 C CA   B VAL   A 1 49  ? 19.482 3.216   3.005   0.58 9.80  ?  49  VAL   A CA   1 
ATOM   1360 C C    A VAL   A 1 49  ? 20.695 4.022   3.288   0.42 9.44  ?  49  VAL   A C    1 
ATOM   1361 C C    B VAL   A 1 49  ? 20.740 3.988   3.379   0.58 9.12  ?  49  VAL   A C    1 
ATOM   1362 O O    A VAL   A 1 49  ? 20.898 4.453   4.429   0.42 9.79  ?  49  VAL   A O    1 
ATOM   1363 O O    B VAL   A 1 49  ? 20.917 4.411   4.526   0.58 9.29  ?  49  VAL   A O    1 
ATOM   1364 C CB   A VAL   A 1 49  ? 19.488 1.809   3.009   0.42 11.25 ?  49  VAL   A CB   1 
ATOM   1365 C CB   B VAL   A 1 49  ? 19.787 1.716   2.836   0.58 9.66  ?  49  VAL   A CB   1 
ATOM   1366 C CG1  A VAL   A 1 49  ? 20.271 1.387   4.256   0.42 11.40 ?  49  VAL   A CG1  1 
ATOM   1367 C CG1  B VAL   A 1 49  ? 20.624 1.214   4.011   0.58 9.34  ?  49  VAL   A CG1  1 
ATOM   1368 C CG2  A VAL   A 1 49  ? 18.111 1.159   3.022   0.42 12.17 ?  49  VAL   A CG2  1 
ATOM   1369 C CG2  B VAL   A 1 49  ? 18.495 0.915   2.686   0.58 9.94  ?  49  VAL   A CG2  1 
ATOM   1370 H H    A VAL   A 1 49  ? 18.817 3.133   1.039   0.42 11.77 ?  49  VAL   A H    1 
ATOM   1371 H H    B VAL   A 1 49  ? 18.766 3.166   1.165   0.58 12.05 ?  49  VAL   A H    1 
ATOM   1372 H HA   A VAL   A 1 49  ? 18.719 3.617   3.586   0.42 12.20 ?  49  VAL   A HA   1 
ATOM   1373 H HA   B VAL   A 1 49  ? 18.846 3.310   3.731   0.58 11.79 ?  49  VAL   A HA   1 
ATOM   1374 H HB   A VAL   A 1 49  ? 19.965 1.478   2.233   0.42 13.52 ?  49  VAL   A HB   1 
ATOM   1375 H HB   B VAL   A 1 49  ? 20.309 1.590   2.028   0.58 11.62 ?  49  VAL   A HB   1 
ATOM   1376 H HG11 A VAL   A 1 49  ? 20.086 0.451   4.444   0.42 13.71 ?  49  VAL   A HG11 1 
ATOM   1377 H HG11 B VAL   A 1 49  ? 20.553 0.248   4.058   0.58 11.24 ?  49  VAL   A HG11 1 
ATOM   1378 H HG12 A VAL   A 1 49  ? 21.219 1.506   4.094   0.42 13.71 ?  49  VAL   A HG12 1 
ATOM   1379 H HG12 B VAL   A 1 49  ? 21.551 1.469   3.874   0.58 11.24 ?  49  VAL   A HG12 1 
ATOM   1380 H HG13 A VAL   A 1 49  ? 19.988 1.932   5.007   0.42 13.71 ?  49  VAL   A HG13 1 
ATOM   1381 H HG13 B VAL   A 1 49  ? 20.287 1.609   4.830   0.58 11.24 ?  49  VAL   A HG13 1 
ATOM   1382 H HG21 A VAL   A 1 49  ? 18.214 0.194   3.059   0.42 14.63 ?  49  VAL   A HG21 1 
ATOM   1383 H HG21 B VAL   A 1 49  ? 18.713 -0.024  2.588   0.58 11.96 ?  49  VAL   A HG21 1 
ATOM   1384 H HG22 A VAL   A 1 49  ? 17.625 1.467   3.806   0.42 14.63 ?  49  VAL   A HG22 1 
ATOM   1385 H HG22 B VAL   A 1 49  ? 17.948 1.048   3.477   0.58 11.96 ?  49  VAL   A HG22 1 
ATOM   1386 H HG23 A VAL   A 1 49  ? 17.636 1.412   2.218   0.42 14.63 ?  49  VAL   A HG23 1 
ATOM   1387 H HG23 B VAL   A 1 49  ? 18.020 1.229   1.900   0.58 11.96 ?  49  VAL   A HG23 1 
ATOM   1388 N N    A ALA   A 1 50  ? 21.620 4.102   2.330   0.42 8.89  ?  50  ALA   A N    1 
ATOM   1389 N N    B ALA   A 1 50  ? 21.653 4.140   2.421   0.58 8.85  ?  50  ALA   A N    1 
ATOM   1390 C CA   A ALA   A 1 50  ? 22.939 4.655   2.615   0.42 8.59  ?  50  ALA   A CA   1 
ATOM   1391 C CA   B ALA   A 1 50  ? 22.963 4.697   2.731   0.58 8.91  ?  50  ALA   A CA   1 
ATOM   1392 C C    A ALA   A 1 50  ? 22.845 6.111   3.041   0.42 8.51  ?  50  ALA   A C    1 
ATOM   1393 C C    B ALA   A 1 50  ? 22.852 6.149   3.163   0.58 9.05  ?  50  ALA   A C    1 
ATOM   1394 O O    A ALA   A 1 50  ? 23.498 6.535   4.001   0.42 8.54  ?  50  ALA   A O    1 
ATOM   1395 O O    B ALA   A 1 50  ? 23.454 6.561   4.162   0.58 9.54  ?  50  ALA   A O    1 
ATOM   1396 C CB   A ALA   A 1 50  ? 23.834 4.514   1.388   0.42 9.09  ?  50  ALA   A CB   1 
ATOM   1397 C CB   B ALA   A 1 50  ? 23.872 4.574   1.515   0.58 9.23  ?  50  ALA   A CB   1 
ATOM   1398 H H    A ALA   A 1 50  ? 21.509 3.836   1.523   0.42 10.69 ?  50  ALA   A H    1 
ATOM   1399 H H    B ALA   A 1 50  ? 21.537 3.936   1.595   0.58 10.65 ?  50  ALA   A H    1 
ATOM   1400 H HA   A ALA   A 1 50  ? 23.343 4.163   3.346   0.42 10.33 ?  50  ALA   A HA   1 
ATOM   1401 H HA   B ALA   A 1 50  ? 23.358 4.201   3.461   0.58 10.72 ?  50  ALA   A HA   1 
ATOM   1402 H HB1  A ALA   A 1 50  ? 24.705 4.892   1.591   0.42 10.94 ?  50  ALA   A HB1  1 
ATOM   1403 H HB1  B ALA   A 1 50  ? 24.740 4.950   1.731   0.58 11.10 ?  50  ALA   A HB1  1 
ATOM   1404 H HB2  A ALA   A 1 50  ? 23.922 3.576   1.166   0.42 10.94 ?  50  ALA   A HB2  1 
ATOM   1405 H HB2  B ALA   A 1 50  ? 23.964 3.637   1.286   0.58 11.10 ?  50  ALA   A HB2  1 
ATOM   1406 H HB3  A ALA   A 1 50  ? 23.430 4.995   0.649   0.42 10.94 ?  50  ALA   A HB3  1 
ATOM   1407 H HB3  B ALA   A 1 50  ? 23.477 5.060   0.774   0.58 11.10 ?  50  ALA   A HB3  1 
ATOM   1408 N N    A GLY   A 1 51  ? 22.050 6.905   2.323   0.42 8.85  ?  51  GLY   A N    1 
ATOM   1409 N N    B GLY   A 1 51  ? 22.089 6.948   2.415   0.58 9.32  ?  51  GLY   A N    1 
ATOM   1410 C CA   A GLY   A 1 51  ? 21.861 8.288   2.728   0.42 9.46  ?  51  GLY   A CA   1 
ATOM   1411 C CA   B GLY   A 1 51  ? 21.949 8.348   2.773   0.58 9.48  ?  51  GLY   A CA   1 
ATOM   1412 C C    A GLY   A 1 51  ? 21.256 8.400   4.113   0.42 9.61  ?  51  GLY   A C    1 
ATOM   1413 C C    B GLY   A 1 51  ? 21.304 8.527   4.132   0.58 9.17  ?  51  GLY   A C    1 
ATOM   1414 O O    A GLY   A 1 51  ? 21.629 9.277   4.897   0.42 10.26 ?  51  GLY   A O    1 
ATOM   1415 O O    B GLY   A 1 51  ? 21.670 9.431   4.889   0.58 9.43  ?  51  GLY   A O    1 
ATOM   1416 H H    A GLY   A 1 51  ? 21.628 6.675   1.611   0.42 10.64 ?  51  GLY   A H    1 
ATOM   1417 H H    B GLY   A 1 51  ? 21.651 6.713   1.712   0.58 11.22 ?  51  GLY   A H    1 
ATOM   1418 H HA2  A GLY   A 1 51  ? 22.713 8.749   2.732   0.42 11.38 ?  51  GLY   A HA2  1 
ATOM   1419 H HA2  B GLY   A 1 51  ? 22.821 8.773   2.792   0.58 11.40 ?  51  GLY   A HA2  1 
ATOM   1420 H HA3  A GLY   A 1 51  ? 21.271 8.735   2.099   0.42 11.38 ?  51  GLY   A HA3  1 
ATOM   1421 H HA3  B GLY   A 1 51  ? 21.400 8.806   2.114   0.58 11.40 ?  51  GLY   A HA3  1 
ATOM   1422 N N    A ALA   A 1 52  ? 20.312 7.511   4.433   0.42 9.52  ?  52  ALA   A N    1 
ATOM   1423 N N    B ALA   A 1 52  ? 20.322 7.677   4.454   0.58 9.01  ?  52  ALA   A N    1 
ATOM   1424 C CA   A ALA   A 1 52  ? 19.647 7.551   5.730   0.42 9.69  ?  52  ALA   A CA   1 
ATOM   1425 C CA   B ALA   A 1 52  ? 19.652 7.773   5.746   0.58 9.77  ?  52  ALA   A CA   1 
ATOM   1426 C C    A ALA   A 1 52  ? 20.593 7.146   6.855   0.42 9.62  ?  52  ALA   A C    1 
ATOM   1427 C C    B ALA   A 1 52  ? 20.564 7.324   6.885   0.58 9.44  ?  52  ALA   A C    1 
ATOM   1428 O O    A ALA   A 1 52  ? 20.622 7.790   7.910   0.42 10.00 ?  52  ALA   A O    1 
ATOM   1429 O O    B ALA   A 1 52  ? 20.623 7.980   7.932   0.58 10.18 ?  52  ALA   A O    1 
ATOM   1430 C CB   A ALA   A 1 52  ? 18.418 6.641   5.706   0.42 10.33 ?  52  ALA   A CB   1 
ATOM   1431 C CB   B ALA   A 1 52  ? 18.351 6.971   5.724   0.58 10.96 ?  52  ALA   A CB   1 
ATOM   1432 H H    A ALA   A 1 52  ? 20.051 6.872   3.923   0.42 11.45 ?  52  ALA   A H    1 
ATOM   1433 H H    B ALA   A 1 52  ? 20.035 7.043   3.947   0.58 10.84 ?  52  ALA   A H    1 
ATOM   1434 H HA   A ALA   A 1 52  ? 19.346 8.454   5.906   0.42 11.66 ?  52  ALA   A HA   1 
ATOM   1435 H HA   B ALA   A 1 52  ? 19.415 8.701   5.902   0.58 11.75 ?  52  ALA   A HA   1 
ATOM   1436 H HB1  A ALA   A 1 52  ? 17.976 6.679   6.570   0.42 12.42 ?  52  ALA   A HB1  1 
ATOM   1437 H HB1  B ALA   A 1 52  ? 17.913 7.051   6.588   0.58 13.18 ?  52  ALA   A HB1  1 
ATOM   1438 H HB2  A ALA   A 1 52  ? 17.812 6.950   5.013   0.42 12.42 ?  52  ALA   A HB2  1 
ATOM   1439 H HB2  B ALA   A 1 52  ? 17.770 7.321   5.029   0.58 13.18 ?  52  ALA   A HB2  1 
ATOM   1440 H HB3  A ALA   A 1 52  ? 18.698 5.732   5.518   0.42 12.42 ?  52  ALA   A HB3  1 
ATOM   1441 H HB3  B ALA   A 1 52  ? 18.553 6.039   5.545   0.58 13.18 ?  52  ALA   A HB3  1 
ATOM   1442 N N    A LEU   A 1 53  ? 21.365 6.074   6.661   0.42 9.48  ?  53  LEU   A N    1 
ATOM   1443 N N    B LEU   A 1 53  ? 21.284 6.212   6.711   0.58 9.03  ?  53  LEU   A N    1 
ATOM   1444 C CA   A LEU   A 1 53  ? 22.321 5.672   7.690   0.42 9.87  ?  53  LEU   A CA   1 
ATOM   1445 C CA   B LEU   A 1 53  ? 22.249 5.802   7.731   0.58 9.26  ?  53  LEU   A CA   1 
ATOM   1446 C C    A LEU   A 1 53  ? 23.368 6.753   7.905   0.42 9.67  ?  53  LEU   A C    1 
ATOM   1447 C C    B LEU   A 1 53  ? 23.292 6.889   7.937   0.58 8.67  ?  53  LEU   A C    1 
ATOM   1448 O O    A LEU   A 1 53  ? 23.758 7.033   9.043   0.42 9.91  ?  53  LEU   A O    1 
ATOM   1449 O O    B LEU   A 1 53  ? 23.570 7.293   9.070   0.58 8.96  ?  53  LEU   A O    1 
ATOM   1450 C CB   A LEU   A 1 53  ? 22.992 4.351   7.312   0.42 10.44 ?  53  LEU   A CB   1 
ATOM   1451 C CB   B LEU   A 1 53  ? 22.937 4.491   7.340   0.58 9.45  ?  53  LEU   A CB   1 
ATOM   1452 C CG   A LEU   A 1 53  ? 22.081 3.120   7.365   0.42 11.13 ?  53  LEU   A CG   1 
ATOM   1453 C CG   B LEU   A 1 53  ? 22.171 3.161   7.423   0.58 10.08 ?  53  LEU   A CG   1 
ATOM   1454 C CD1  A LEU   A 1 53  ? 22.774 1.901   6.791   0.42 11.50 ?  53  LEU   A CD1  1 
ATOM   1455 C CD1  B LEU   A 1 53  ? 22.982 2.068   6.754   0.58 10.93 ?  53  LEU   A CD1  1 
ATOM   1456 C CD2  A LEU   A 1 53  ? 21.614 2.850   8.791   0.42 12.10 ?  53  LEU   A CD2  1 
ATOM   1457 C CD2  B LEU   A 1 53  ? 21.861 2.774   8.861   0.58 10.85 ?  53  LEU   A CD2  1 
ATOM   1458 H H    A LEU   A 1 53  ? 21.349 5.572   5.963   0.42 11.41 ?  53  LEU   A H    1 
ATOM   1459 H H    B LEU   A 1 53  ? 21.225 5.690   6.033   0.58 10.87 ?  53  LEU   A H    1 
ATOM   1460 H HA   A LEU   A 1 53  ? 21.848 5.543   8.527   0.42 11.87 ?  53  LEU   A HA   1 
ATOM   1461 H HA   B LEU   A 1 53  ? 21.783 5.667   8.572   0.58 11.14 ?  53  LEU   A HA   1 
ATOM   1462 H HB2  A LEU   A 1 53  ? 23.331 4.424   6.405   0.42 12.56 ?  53  LEU   A HB2  1 
ATOM   1463 H HB2  B LEU   A 1 53  ? 23.227 4.581   6.420   0.58 11.37 ?  53  LEU   A HB2  1 
ATOM   1464 H HB3  A LEU   A 1 53  ? 23.730 4.194   7.922   0.42 12.56 ?  53  LEU   A HB3  1 
ATOM   1465 H HB3  B LEU   A 1 53  ? 23.713 4.393   7.907   0.58 11.37 ?  53  LEU   A HB3  1 
ATOM   1466 H HG   A LEU   A 1 53  ? 21.294 3.295   6.823   0.42 13.39 ?  53  LEU   A HG   1 
ATOM   1467 H HG   B LEU   A 1 53  ? 21.330 3.252   6.943   0.58 12.13 ?  53  LEU   A HG   1 
ATOM   1468 H HD11 A LEU   A 1 53  ? 22.171 1.145   6.843   0.42 13.83 ?  53  LEU   A HD11 1 
ATOM   1469 H HD11 B LEU   A 1 53  ? 22.493 1.234   6.820   0.58 13.15 ?  53  LEU   A HD11 1 
ATOM   1470 H HD12 A LEU   A 1 53  ? 23.008 2.078   5.867   0.42 13.83 ?  53  LEU   A HD12 1 
ATOM   1471 H HD12 B LEU   A 1 53  ? 23.117 2.303   5.823   0.58 13.15 ?  53  LEU   A HD12 1 
ATOM   1472 H HD13 A LEU   A 1 53  ? 23.575 1.725   7.308   0.42 13.83 ?  53  LEU   A HD13 1 
ATOM   1473 H HD13 B LEU   A 1 53  ? 23.835 1.993   7.206   0.58 13.15 ?  53  LEU   A HD13 1 
ATOM   1474 H HD21 A LEU   A 1 53  ? 21.133 2.008   8.811   0.42 14.55 ?  53  LEU   A HD21 1 
ATOM   1475 H HD21 B LEU   A 1 53  ? 21.303 1.979   8.859   0.58 13.05 ?  53  LEU   A HD21 1 
ATOM   1476 H HD22 A LEU   A 1 53  ? 22.389 2.801   9.372   0.42 14.55 ?  53  LEU   A HD22 1 
ATOM   1477 H HD22 B LEU   A 1 53  ? 22.689 2.600   9.328   0.58 13.05 ?  53  LEU   A HD22 1 
ATOM   1478 H HD23 A LEU   A 1 53  ? 21.029 3.570   9.079   0.42 14.55 ?  53  LEU   A HD23 1 
ATOM   1479 H HD23 B LEU   A 1 53  ? 21.385 3.506   9.291   0.58 13.05 ?  53  LEU   A HD23 1 
ATOM   1480 N N    A ASN   A 1 54  ? 23.830 7.374   6.824   0.42 9.47  ?  54  ASN   A N    1 
ATOM   1481 N N    B ASN   A 1 54  ? 23.876 7.377   6.844   0.58 8.70  ?  54  ASN   A N    1 
ATOM   1482 C CA   A ASN   A 1 54  ? 24.886 8.364   6.967   0.42 9.59  ?  54  ASN   A CA   1 
ATOM   1483 C CA   B ASN   A 1 54  ? 24.913 8.386   6.983   0.58 9.13  ?  54  ASN   A CA   1 
ATOM   1484 C C    A ASN   A 1 54  ? 24.382 9.611   7.685   0.42 9.75  ?  54  ASN   A C    1 
ATOM   1485 C C    B ASN   A 1 54  ? 24.382 9.620   7.703   0.58 9.53  ?  54  ASN   A C    1 
ATOM   1486 O O    A ASN   A 1 54  ? 25.081 10.170  8.538   0.42 10.09 ?  54  ASN   A O    1 
ATOM   1487 O O    B ASN   A 1 54  ? 25.056 10.176  8.578   0.58 9.87  ?  54  ASN   A O    1 
ATOM   1488 C CB   A ASN   A 1 54  ? 25.467 8.711   5.604   0.42 9.44  ?  54  ASN   A CB   1 
ATOM   1489 C CB   B ASN   A 1 54  ? 25.487 8.761   5.626   0.58 9.03  ?  54  ASN   A CB   1 
ATOM   1490 C CG   A ASN   A 1 54  ? 26.538 9.769   5.704   0.42 9.66  ?  54  ASN   A CG   1 
ATOM   1491 C CG   B ASN   A 1 54  ? 26.461 9.903   5.740   0.58 8.89  ?  54  ASN   A CG   1 
ATOM   1492 O OD1  A ASN   A 1 54  ? 27.531 9.592   6.411   0.42 9.83  ?  54  ASN   A OD1  1 
ATOM   1493 O OD1  B ASN   A 1 54  ? 27.474 9.782   6.437   0.58 8.72  ?  54  ASN   A OD1  1 
ATOM   1494 N ND2  A ASN   A 1 54  ? 26.340 10.882  5.019   0.42 9.94  ?  54  ASN   A ND2  1 
ATOM   1495 N ND2  B ASN   A 1 54  ? 26.148 11.031  5.108   0.58 9.64  ?  54  ASN   A ND2  1 
ATOM   1496 H H    A ASN   A 1 54  ? 23.551 7.244   6.019   0.42 11.40 ?  54  ASN   A H    1 
ATOM   1497 H H    B ASN   A 1 54  ? 23.686 7.150   6.035   0.58 10.47 ?  54  ASN   A H    1 
ATOM   1498 H HA   A ASN   A 1 54  ? 25.592 7.979   7.503   0.42 11.53 ?  54  ASN   A HA   1 
ATOM   1499 H HA   B ASN   A 1 54  ? 25.627 8.021   7.518   0.58 10.98 ?  54  ASN   A HA   1 
ATOM   1500 H HB2  A ASN   A 1 54  ? 25.859 7.909   5.217   0.42 11.36 ?  54  ASN   A HB2  1 
ATOM   1501 H HB2  B ASN   A 1 54  ? 25.963 7.996   5.262   0.58 10.87 ?  54  ASN   A HB2  1 
ATOM   1502 H HB3  A ASN   A 1 54  ? 24.761 9.045   5.031   0.42 11.36 ?  54  ASN   A HB3  1 
ATOM   1503 H HB3  B ASN   A 1 54  ? 24.771 9.026   5.033   0.58 10.87 ?  54  ASN   A HB3  1 
ATOM   1504 H HD21 A ASN   A 1 54  ? 26.926 11.509  5.048   0.42 11.95 ?  54  ASN   A HD21 1 
ATOM   1505 H HD21 B ASN   A 1 54  ? 26.671 11.714  5.153   0.58 11.59 ?  54  ASN   A HD21 1 
ATOM   1506 H HD22 A ASN   A 1 54  ? 25.632 10.971  4.542   0.42 11.95 ?  54  ASN   A HD22 1 
ATOM   1507 H HD22 B ASN   A 1 54  ? 25.429 11.073  4.637   0.58 11.59 ?  54  ASN   A HD22 1 
ATOM   1508 N N    . LYS   A 1 55  ? 23.170 10.065  7.352   1.00 9.77  ?  55  LYS   A N    1 
ATOM   1509 C CA   . LYS   A 1 55  ? 22.595 11.226  8.025   1.00 10.19 ?  55  LYS   A CA   1 
ATOM   1510 C C    . LYS   A 1 55  ? 22.491 10.988  9.527   1.00 10.36 ?  55  LYS   A C    1 
ATOM   1511 O O    . LYS   A 1 55  ? 22.771 11.885  10.332  1.00 10.81 ?  55  LYS   A O    1 
ATOM   1512 C CB   . LYS   A 1 55  ? 21.226 11.547  7.413   1.00 11.24 ?  55  LYS   A CB   1 
ATOM   1513 C CG   . LYS   A 1 55  ? 20.488 12.701  8.069   1.00 12.56 ?  55  LYS   A CG   1 
ATOM   1514 C CD   . LYS   A 1 55  ? 19.171 12.982  7.356   1.00 14.15 ?  55  LYS   A CD   1 
ATOM   1515 C CE   . LYS   A 1 55  ? 18.346 14.044  8.074   1.00 15.94 ?  55  LYS   A CE   1 
ATOM   1516 N NZ   . LYS   A 1 55  ? 17.024 14.261  7.425   1.00 16.63 ?  55  LYS   A NZ   1 
ATOM   1517 H H    A LYS   A 1 55  ? 22.663 9.721   6.747   0.42 11.75 ?  55  LYS   A H    1 
ATOM   1518 H H    B LYS   A 1 55  ? 22.664 9.713   6.751   0.58 11.75 ?  55  LYS   A H    1 
ATOM   1519 H HA   . LYS   A 1 55  ? 23.174 11.994  7.883   1.00 12.26 ?  55  LYS   A HA   1 
ATOM   1520 H HB2  . LYS   A 1 55  ? 21.353 11.776  6.480   1.00 13.51 ?  55  LYS   A HB2  1 
ATOM   1521 H HB3  . LYS   A 1 55  ? 20.665 10.763  7.487   1.00 13.51 ?  55  LYS   A HB3  1 
ATOM   1522 H HG2  . LYS   A 1 55  ? 20.293 12.477  8.993   1.00 15.10 ?  55  LYS   A HG2  1 
ATOM   1523 H HG3  . LYS   A 1 55  ? 21.038 13.501  8.026   1.00 15.10 ?  55  LYS   A HG3  1 
ATOM   1524 H HD2  . LYS   A 1 55  ? 19.359 13.298  6.457   1.00 17.01 ?  55  LYS   A HD2  1 
ATOM   1525 H HD3  . LYS   A 1 55  ? 18.651 12.163  7.318   1.00 17.01 ?  55  LYS   A HD3  1 
ATOM   1526 H HE2  . LYS   A 1 55  ? 18.191 13.756  8.988   1.00 19.15 ?  55  LYS   A HE2  1 
ATOM   1527 H HE3  . LYS   A 1 55  ? 18.832 14.881  8.065   1.00 19.15 ?  55  LYS   A HE3  1 
ATOM   1528 H HZ1  . LYS   A 1 55  ? 16.465 14.649  8.001   1.00 19.98 ?  55  LYS   A HZ1  1 
ATOM   1529 H HZ2  . LYS   A 1 55  ? 17.116 14.792  6.716   1.00 19.98 ?  55  LYS   A HZ2  1 
ATOM   1530 H HZ3  . LYS   A 1 55  ? 16.677 13.485  7.166   1.00 19.98 ?  55  LYS   A HZ3  1 
ATOM   1531 N N    . ALA   A 1 56  ? 22.098 9.776   9.925   1.00 10.62 ?  56  ALA   A N    1 
ATOM   1532 C CA   . ALA   A 1 56  ? 21.971 9.456   11.341  1.00 11.03 ?  56  ALA   A CA   1 
ATOM   1533 C C    . ALA   A 1 56  ? 23.306 9.483   12.070  1.00 11.10 ?  56  ALA   A C    1 
ATOM   1534 O O    . ALA   A 1 56  ? 23.321 9.675   13.290  1.00 12.62 ?  56  ALA   A O    1 
ATOM   1535 C CB   . ALA   A 1 56  ? 21.280 8.098   11.510  1.00 12.02 ?  56  ALA   A CB   1 
ATOM   1536 H H    . ALA   A 1 56  ? 21.907 9.135   9.396   1.00 12.77 ?  56  ALA   A H    1 
ATOM   1537 H HA   . ALA   A 1 56  ? 21.416 10.116  11.763  1.00 13.26 ?  56  ALA   A HA   1 
ATOM   1538 H HB1  . ALA   A 1 56  ? 21.215 7.891   12.458  1.00 14.45 ?  56  ALA   A HB1  1 
ATOM   1539 H HB2  . ALA   A 1 56  ? 20.392 8.150   11.124  1.00 14.45 ?  56  ALA   A HB2  1 
ATOM   1540 H HB3  . ALA   A 1 56  ? 21.798 7.413   11.059  1.00 14.45 ?  56  ALA   A HB3  1 
ATOM   1541 N N    . THR   A 1 57  ? 24.422 9.298   11.353  1.00 10.18 ?  57  THR   A N    1 
ATOM   1542 C CA   . THR   A 1 57  ? 25.765 9.431   11.928  1.00 10.61 ?  57  THR   A CA   1 
ATOM   1543 C C    . THR   A 1 57  ? 26.309 10.853  11.857  1.00 10.77 ?  57  THR   A C    1 
ATOM   1544 O O    . THR   A 1 57  ? 27.491 11.067  12.162  1.00 11.40 ?  57  THR   A O    1 
ATOM   1545 C CB   . THR   A 1 57  ? 26.787 8.488   11.258  1.00 10.63 ?  57  THR   A CB   1 
ATOM   1546 O OG1  . THR   A 1 57  ? 27.179 8.985   9.964   1.00 10.11 ?  57  THR   A OG1  1 
ATOM   1547 C CG2  . THR   A 1 57  ? 26.275 7.050   11.169  1.00 10.70 ?  57  THR   A CG2  1 
ATOM   1548 H H    . THR   A 1 57  ? 24.435 9.075   10.514  1.00 12.24 ?  57  THR   A H    1 
ATOM   1549 H HA   . THR   A 1 57  ? 25.721 9.174   12.866  1.00 12.76 ?  57  THR   A HA   1 
ATOM   1550 H HB   . THR   A 1 57  ? 27.587 8.458   11.823  1.00 12.79 ?  57  THR   A HB   1 
ATOM   1551 H HG1  . THR   A 1 57  ? 26.504 9.048   9.475   1.00 12.15 ?  57  THR   A HG1  1 
ATOM   1552 H HG21 . THR   A 1 57  ? 26.931 6.484   10.731  1.00 12.86 ?  57  THR   A HG21 1 
ATOM   1553 H HG22 . THR   A 1 57  ? 26.105 6.698   12.059  1.00 12.86 ?  57  THR   A HG22 1 
ATOM   1554 H HG23 . THR   A 1 57  ? 25.450 7.023   10.662  1.00 12.86 ?  57  THR   A HG23 1 
ATOM   1555 N N    . ASN   A 1 58  ? 25.493 11.824  11.448  1.00 11.02 ?  58  ASN   A N    1 
ATOM   1556 C CA   . ASN   A 1 58  ? 25.952 13.206  11.341  1.00 12.38 ?  58  ASN   A CA   1 
ATOM   1557 C C    . ASN   A 1 58  ? 27.104 13.336  10.339  1.00 11.15 ?  58  ASN   A C    1 
ATOM   1558 O O    . ASN   A 1 58  ? 28.002 14.164  10.507  1.00 12.14 ?  58  ASN   A O    1 
ATOM   1559 C CB   . ASN   A 1 58  ? 26.326 13.761  12.728  1.00 15.46 ?  58  ASN   A CB   1 
ATOM   1560 C CG   . ASN   A 1 58  ? 26.658 15.236  12.714  1.00 20.08 ?  58  ASN   A CG   1 
ATOM   1561 O OD1  . ASN   A 1 58  ? 26.031 16.015  12.008  1.00 21.73 ?  58  ASN   A OD1  1 
ATOM   1562 N ND2  . ASN   A 1 58  ? 27.643 15.630  13.514  1.00 21.85 ?  58  ASN   A ND2  1 
ATOM   1563 H H    . ASN   A 1 58  ? 24.671 11.701  11.219  1.00 13.26 ?  58  ASN   A H    1 
ATOM   1564 H HA   . ASN   A 1 58  ? 25.218 13.736  11.006  1.00 14.88 ?  58  ASN   A HA   1 
ATOM   1565 H HB2  . ASN   A 1 58  ? 25.572 13.623  13.333  1.00 18.58 ?  58  ASN   A HB2  1 
ATOM   1566 H HB3  . ASN   A 1 58  ? 27.101 13.291  13.064  1.00 18.58 ?  58  ASN   A HB3  1 
ATOM   1567 H HD21 . ASN   A 1 58  ? 27.857 16.465  13.544  1.00 26.25 ?  58  ASN   A HD21 1 
ATOM   1568 H HD22 . ASN   A 1 58  ? 28.054 15.060  13.997  1.00 26.25 ?  58  ASN   A HD22 1 
ATOM   1569 N N    . ASN   A 1 59  ? 27.099 12.511  9.291   1.00 10.25 ?  59  ASN   A N    1 
ATOM   1570 C CA   . ASN   A 1 59  ? 28.086 12.491  8.208   1.00 9.94  ?  59  ASN   A CA   1 
ATOM   1571 C C    . ASN   A 1 59  ? 29.401 11.818  8.606   1.00 9.76  ?  59  ASN   A C    1 
ATOM   1572 O O    . ASN   A 1 59  ? 30.318 11.774  7.776   1.00 10.33 ?  59  ASN   A O    1 
ATOM   1573 C CB   . ASN   A 1 59  ? 28.379 13.879  7.611   1.00 10.43 ?  59  ASN   A CB   1 
ATOM   1574 C CG   . ASN   A 1 59  ? 28.748 13.816  6.144   1.00 10.27 ?  59  ASN   A CG   1 
ATOM   1575 O OD1  . ASN   A 1 59  ? 28.056 13.184  5.346   1.00 10.77 ?  59  ASN   A OD1  1 
ATOM   1576 N ND2  . ASN   A 1 59  ? 29.823 14.490  5.770   1.00 11.32 ?  59  ASN   A ND2  1 
ATOM   1577 H H    . ASN   A 1 59  ? 26.491 11.911  9.184   1.00 12.32 ?  59  ASN   A H    1 
ATOM   1578 H HA   . ASN   A 1 59  ? 27.709 11.961  7.493   1.00 11.95 ?  59  ASN   A HA   1 
ATOM   1579 H HB2  . ASN   A 1 59  ? 27.589 14.437  7.695   1.00 12.54 ?  59  ASN   A HB2  1 
ATOM   1580 H HB3  . ASN   A 1 59  ? 29.122 14.282  8.083   1.00 12.54 ?  59  ASN   A HB3  1 
ATOM   1581 H HD21 . ASN   A 1 59  ? 30.072 14.493  4.944   1.00 13.61 ?  59  ASN   A HD21 1 
ATOM   1582 H HD22 . ASN   A 1 59  ? 30.284 14.933  6.351   1.00 13.61 ?  59  ASN   A HD22 1 
ATOM   1583 N N    . ALA   A 1 60  ? 29.521 11.273  9.818   1.00 9.89  ?  60  ALA   A N    1 
ATOM   1584 C CA   . ALA   A 1 60  ? 30.756 10.584  10.181  1.00 10.30 ?  60  ALA   A CA   1 
ATOM   1585 C C    . ALA   A 1 60  ? 30.989 9.350   9.318   1.00 10.05 ?  60  ALA   A C    1 
ATOM   1586 O O    . ALA   A 1 60  ? 32.136 9.035   8.983   1.00 10.49 ?  60  ALA   A O    1 
ATOM   1587 C CB   . ALA   A 1 60  ? 30.762 10.232  11.668  1.00 11.03 ?  60  ALA   A CB   1 
ATOM   1588 H H    . ALA   A 1 60  ? 28.915 11.284  10.433  1.00 11.90 ?  60  ALA   A H    1 
ATOM   1589 H HA   . ALA   A 1 60  ? 31.496 11.194  10.023  1.00 12.38 ?  60  ALA   A HA   1 
ATOM   1590 H HB1  . ALA   A 1 60  ? 31.595 9.783   11.882  1.00 13.26 ?  60  ALA   A HB1  1 
ATOM   1591 H HB2  . ALA   A 1 60  ? 30.688 11.051  12.189  1.00 13.26 ?  60  ALA   A HB2  1 
ATOM   1592 H HB3  . ALA   A 1 60  ? 30.012 9.652   11.859  1.00 13.26 ?  60  ALA   A HB3  1 
ATOM   1593 N N    . MET   A 1 61  ? 29.923 8.650   8.933   1.00 9.46  ?  61  MET   A N    1 
ATOM   1594 C CA   . MET   A 1 61  ? 30.071 7.520   8.024   1.00 9.34  ?  61  MET   A CA   1 
ATOM   1595 C C    . MET   A 1 61  ? 30.700 7.949   6.700   1.00 9.52  ?  61  MET   A C    1 
ATOM   1596 O O    . MET   A 1 61  ? 31.597 7.272   6.181   1.00 9.90  ?  61  MET   A O    1 
ATOM   1597 C CB   . MET   A 1 61  ? 28.709 6.854   7.811   1.00 9.62  ?  61  MET   A CB   1 
ATOM   1598 C CG   . MET   A 1 61  ? 28.723 5.685   6.833   1.00 10.26 ?  61  MET   A CG   1 
ATOM   1599 S SD   . MET   A 1 61  ? 27.109 4.926   6.621   1.00 10.80 ?  61  MET   A SD   1 
ATOM   1600 C CE   . MET   A 1 61  ? 26.979 4.039   8.177   1.00 12.15 ?  61  MET   A CE   1 
ATOM   1601 H H    . MET   A 1 61  ? 29.112 8.811   9.176   1.00 11.38 ?  61  MET   A H    1 
ATOM   1602 H HA   . MET   A 1 61  ? 30.651 6.863   8.444   1.00 11.23 ?  61  MET   A HA   1 
ATOM   1603 H HB2  . MET   A 1 61  ? 28.394 6.512   8.663   1.00 11.57 ?  61  MET   A HB2  1 
ATOM   1604 H HB3  . MET   A 1 61  ? 28.088 7.510   7.472   1.00 11.57 ?  61  MET   A HB3  1 
ATOM   1605 H HG2  . MET   A 1 61  ? 29.010 5.994   5.960   1.00 12.34 ?  61  MET   A HG2  1 
ATOM   1606 H HG3  . MET   A 1 61  ? 29.325 4.997   7.156   1.00 12.34 ?  61  MET   A HG3  1 
ATOM   1607 H HE1  . MET   A 1 61  ? 26.137 3.551   8.191   1.00 14.60 ?  61  MET   A HE1  1 
ATOM   1608 H HE2  . MET   A 1 61  ? 27.720 3.423   8.251   1.00 14.60 ?  61  MET   A HE2  1 
ATOM   1609 H HE3  . MET   A 1 61  ? 26.998 4.676   8.910   1.00 14.60 ?  61  MET   A HE3  1 
ATOM   1610 N N    . GLN   A 1 62  ? 30.256 9.075   6.141   1.00 9.40  ?  62  GLN   A N    1 
ATOM   1611 C CA   . GLN   A 1 62  ? 30.825 9.540   4.878   1.00 9.42  ?  62  GLN   A CA   1 
ATOM   1612 C C    . GLN   A 1 62  ? 32.293 9.926   5.029   1.00 9.54  ?  62  GLN   A C    1 
ATOM   1613 O O    . GLN   A 1 62  ? 33.111 9.616   4.157   1.00 10.03 ?  62  GLN   A O    1 
ATOM   1614 C CB   . GLN   A 1 62  ? 30.026 10.715  4.333   1.00 9.58  ?  62  GLN   A CB   1 
ATOM   1615 C CG   . GLN   A 1 62  ? 30.401 11.073  2.905   1.00 9.76  ?  62  GLN   A CG   1 
ATOM   1616 C CD   . GLN   A 1 62  ? 30.071 9.933   1.963   1.00 9.90  ?  62  GLN   A CD   1 
ATOM   1617 O OE1  . GLN   A 1 62  ? 28.901 9.626   1.751   1.00 10.42 ?  62  GLN   A OE1  1 
ATOM   1618 N NE2  . GLN   A 1 62  ? 31.096 9.260   1.438   1.00 10.39 ?  62  GLN   A NE2  1 
ATOM   1619 H H    . GLN   A 1 62  ? 29.632 9.572   6.465   1.00 11.31 ?  62  GLN   A H    1 
ATOM   1620 H HA   . GLN   A 1 62  ? 30.772 8.815   4.237   1.00 11.33 ?  62  GLN   A HA   1 
ATOM   1621 H HB2  . GLN   A 1 62  ? 29.085 10.503  4.355   1.00 11.52 ?  62  GLN   A HB2  1 
ATOM   1622 H HB3  . GLN   A 1 62  ? 30.203 11.499  4.887   1.00 11.52 ?  62  GLN   A HB3  1 
ATOM   1623 H HG2  . GLN   A 1 62  ? 29.887 11.849  2.627   1.00 11.75 ?  62  GLN   A HG2  1 
ATOM   1624 H HG3  . GLN   A 1 62  ? 31.347 11.254  2.851   1.00 11.75 ?  62  GLN   A HG3  1 
ATOM   1625 H HE21 . GLN   A 1 62  ? 31.905 9.489   1.626   1.00 12.49 ?  62  GLN   A HE21 1 
ATOM   1626 H HE22 . GLN   A 1 62  ? 30.952 8.594   0.912   1.00 12.49 ?  62  GLN   A HE22 1 
ATOM   1627 N N    . VAL   A 1 63  ? 32.642 10.617  6.115   1.00 10.01 ?  63  VAL   A N    1 
ATOM   1628 C CA   . VAL   A 1 63  ? 34.030 11.014  6.334   1.00 10.81 ?  63  VAL   A CA   1 
ATOM   1629 C C    . VAL   A 1 63  ? 34.932 9.782   6.401   1.00 10.50 ?  63  VAL   A C    1 
ATOM   1630 O O    . VAL   A 1 63  ? 35.990 9.721   5.759   1.00 10.93 ?  63  VAL   A O    1 
ATOM   1631 C CB   . VAL   A 1 63  ? 34.124 11.886  7.599   1.00 12.09 ?  63  VAL   A CB   1 
ATOM   1632 C CG1  . VAL   A 1 63  ? 35.568 12.105  8.001   1.00 14.19 ?  63  VAL   A CG1  1 
ATOM   1633 C CG2  . VAL   A 1 63  ? 33.419 13.222  7.365   1.00 12.81 ?  63  VAL   A CG2  1 
ATOM   1634 H H    . VAL   A 1 63  ? 32.097 10.866  6.733   1.00 12.04 ?  63  VAL   A H    1 
ATOM   1635 H HA   . VAL   A 1 63  ? 34.323 11.554  5.586   1.00 12.99 ?  63  VAL   A HA   1 
ATOM   1636 H HB   . VAL   A 1 63  ? 33.676 11.438  8.333   1.00 14.54 ?  63  VAL   A HB   1 
ATOM   1637 H HG11 . VAL   A 1 63  ? 35.610 12.846  8.628   1.00 17.06 ?  63  VAL   A HG11 1 
ATOM   1638 H HG12 . VAL   A 1 63  ? 35.906 11.300  8.418   1.00 17.06 ?  63  VAL   A HG12 1 
ATOM   1639 H HG13 . VAL   A 1 63  ? 36.085 12.316  7.209   1.00 17.06 ?  63  VAL   A HG13 1 
ATOM   1640 H HG21 . VAL   A 1 63  ? 33.494 13.769  8.165   1.00 15.39 ?  63  VAL   A HG21 1 
ATOM   1641 H HG22 . VAL   A 1 63  ? 33.842 13.678  6.618   1.00 15.39 ?  63  VAL   A HG22 1 
ATOM   1642 H HG23 . VAL   A 1 63  ? 32.485 13.058  7.165   1.00 15.39 ?  63  VAL   A HG23 1 
ATOM   1643 N N    . GLU   A 1 64  ? 34.511 8.773   7.168   1.00 10.28 ?  64  GLU   A N    1 
ATOM   1644 C CA   . GLU   A 1 64  ? 35.279 7.538   7.273   1.00 10.09 ?  64  GLU   A CA   1 
ATOM   1645 C C    . GLU   A 1 64  ? 35.377 6.845   5.922   1.00 10.13 ?  64  GLU   A C    1 
ATOM   1646 O O    . GLU   A 1 64  ? 36.429 6.302   5.552   1.00 10.49 ?  64  GLU   A O    1 
ATOM   1647 C CB   . GLU   A 1 64  ? 34.585 6.628   8.290   1.00 10.87 ?  64  GLU   A CB   1 
ATOM   1648 C CG   . GLU   A 1 64  ? 35.244 5.275   8.450   1.00 11.28 ?  64  GLU   A CG   1 
ATOM   1649 C CD   . GLU   A 1 64  ? 34.370 4.272   9.178   1.00 12.07 ?  64  GLU   A CD   1 
ATOM   1650 O OE1  . GLU   A 1 64  ? 33.133 4.370   9.043   1.00 12.90 ?  64  GLU   A OE1  1 
ATOM   1651 O OE2  . GLU   A 1 64  ? 34.938 3.383   9.861   1.00 12.30 -1 64  GLU   A OE2  1 
ATOM   1652 H H    . GLU   A 1 64  ? 33.777 8.775   7.621   1.00 12.36 ?  64  GLU   A H    1 
ATOM   1653 H HA   . GLU   A 1 64  ? 36.174 7.741   7.592   1.00 12.14 ?  64  GLU   A HA   1 
ATOM   1654 H HB2  . GLU   A 1 64  ? 34.598 7.066   9.159   1.00 13.07 ?  64  GLU   A HB2  1 
ATOM   1655 H HB3  . GLU   A 1 64  ? 33.672 6.486   8.007   1.00 13.07 ?  64  GLU   A HB3  1 
ATOM   1656 H HG2  . GLU   A 1 64  ? 35.452 4.908   7.573   1.00 13.56 ?  64  GLU   A HG2  1 
ATOM   1657 H HG3  . GLU   A 1 64  ? 36.065 5.384   8.957   1.00 13.56 ?  64  GLU   A HG3  1 
ATOM   1658 N N    . SER   A 1 65  ? 34.265 6.831   5.184   1.00 9.73  ?  65  SER   A N    1 
ATOM   1659 C CA   . SER   A 1 65  ? 34.216 6.165   3.888   1.00 9.75  ?  65  SER   A CA   1 
ATOM   1660 C C    . SER   A 1 65  ? 35.132 6.837   2.877   1.00 10.04 ?  65  SER   A C    1 
ATOM   1661 O O    . SER   A 1 65  ? 35.774 6.153   2.072   1.00 10.89 ?  65  SER   A O    1 
ATOM   1662 C CB   . SER   A 1 65  ? 32.783 6.159   3.354   1.00 9.99  ?  65  SER   A CB   1 
ATOM   1663 O OG   . SER   A 1 65  ? 31.933 5.351   4.156   1.00 10.22 ?  65  SER   A OG   1 
ATOM   1664 H H    . SER   A 1 65  ? 33.526 7.201   5.417   1.00 11.71 ?  65  SER   A H    1 
ATOM   1665 H HA   . SER   A 1 65  ? 34.507 5.244   3.990   1.00 11.72 ?  65  SER   A HA   1 
ATOM   1666 H HB2  . SER   A 1 65  ? 32.442 7.064   3.356   1.00 12.02 ?  65  SER   A HB2  1 
ATOM   1667 H HB3  . SER   A 1 65  ? 32.788 5.807   2.451   1.00 12.02 ?  65  SER   A HB3  1 
ATOM   1668 H HG   . SER   A 1 65  ? 31.930 5.643   4.947   1.00 12.29 ?  65  SER   A HG   1 
ATOM   1669 N N    . ASP   A 1 66  ? 35.201 8.170   2.892   1.00 10.04 ?  66  ASP   A N    1 
ATOM   1670 C CA   . ASP   A 1 66  ? 36.064 8.860   1.940   1.00 10.74 ?  66  ASP   A CA   1 
ATOM   1671 C C    . ASP   A 1 66  ? 37.531 8.514   2.188   1.00 10.89 ?  66  ASP   A C    1 
ATOM   1672 O O    . ASP   A 1 66  ? 38.308 8.341   1.240   1.00 11.80 ?  66  ASP   A O    1 
ATOM   1673 C CB   . ASP   A 1 66  ? 35.840 10.364  2.030   1.00 11.87 ?  66  ASP   A CB   1 
ATOM   1674 C CG   . ASP   A 1 66  ? 34.499 10.814  1.425   1.00 13.52 ?  66  ASP   A CG   1 
ATOM   1675 O OD1  . ASP   A 1 66  ? 33.800 10.012  0.774   1.00 13.64 ?  66  ASP   A OD1  1 
ATOM   1676 O OD2  . ASP   A 1 66  ? 34.181 12.011  1.577   1.00 16.10 -1 66  ASP   A OD2  1 
ATOM   1677 H H    . ASP   A 1 66  ? 34.766 8.686   3.433   1.00 12.08 ?  66  ASP   A H    1 
ATOM   1678 H HA   . ASP   A 1 66  ? 35.831 8.572   1.043   1.00 12.92 ?  66  ASP   A HA   1 
ATOM   1679 H HB2  . ASP   A 1 66  ? 35.844 10.630  2.961   1.00 14.27 ?  66  ASP   A HB2  1 
ATOM   1680 H HB3  . ASP   A 1 66  ? 36.557 10.816  1.553   1.00 14.27 ?  66  ASP   A HB3  1 
ATOM   1681 N N    . ASP   A 1 67  ? 37.924 8.398   3.456   1.00 11.04 ?  67  ASP   A N    1 
ATOM   1682 C CA   . ASP   A 1 67  ? 39.281 7.957   3.767   1.00 12.04 ?  67  ASP   A CA   1 
ATOM   1683 C C    . ASP   A 1 67  ? 39.512 6.522   3.298   1.00 11.81 ?  67  ASP   A C    1 
ATOM   1684 O O    . ASP   A 1 67  ? 40.570 6.205   2.745   1.00 12.50 ?  67  ASP   A O    1 
ATOM   1685 C CB   . ASP   A 1 67  ? 39.543 8.099   5.268   1.00 13.06 ?  67  ASP   A CB   1 
ATOM   1686 C CG   . ASP   A 1 67  ? 40.838 7.451   5.695   1.00 14.31 ?  67  ASP   A CG   1 
ATOM   1687 O OD1  . ASP   A 1 67  ? 41.900 8.089   5.556   1.00 17.44 ?  67  ASP   A OD1  1 
ATOM   1688 O OD2  . ASP   A 1 67  ? 40.786 6.291   6.157   1.00 14.15 -1 67  ASP   A OD2  1 
ATOM   1689 H H    . ASP   A 1 67  ? 37.431 8.565   4.142   1.00 13.28 ?  67  ASP   A H    1 
ATOM   1690 H HA   . ASP   A 1 67  ? 39.908 8.527   3.298   1.00 14.48 ?  67  ASP   A HA   1 
ATOM   1691 H HB2  . ASP   A 1 67  ? 39.585 9.039   5.490   1.00 15.69 ?  67  ASP   A HB2  1 
ATOM   1692 H HB3  . ASP   A 1 67  ? 38.815 7.675   5.754   1.00 15.69 ?  67  ASP   A HB3  1 
ATOM   1693 N N    . TYR   A 1 68  ? 38.521 5.642   3.490   1.00 11.40 ?  68  TYR   A N    1 
ATOM   1694 C CA   . TYR   A 1 68  ? 38.647 4.264   3.019   1.00 11.66 ?  68  TYR   A CA   1 
ATOM   1695 C C    . TYR   A 1 68  ? 38.893 4.219   1.512   1.00 11.52 ?  68  TYR   A C    1 
ATOM   1696 O O    . TYR   A 1 68  ? 39.776 3.491   1.039   1.00 12.04 ?  68  TYR   A O    1 
ATOM   1697 C CB   . TYR   A 1 68  ? 37.397 3.436   3.399   1.00 12.03 ?  68  TYR   A CB   1 
ATOM   1698 C CG   . TYR   A 1 68  ? 37.428 2.049   2.772   1.00 13.19 ?  68  TYR   A CG   1 
ATOM   1699 C CD1  . TYR   A 1 68  ? 36.985 1.860   1.466   1.00 14.05 ?  68  TYR   A CD1  1 
ATOM   1700 C CD2  . TYR   A 1 68  ? 37.968 0.968   3.441   1.00 14.74 ?  68  TYR   A CD2  1 
ATOM   1701 C CE1  . TYR   A 1 68  ? 37.063 0.655   0.846   1.00 14.90 ?  68  TYR   A CE1  1 
ATOM   1702 C CE2  . TYR   A 1 68  ? 38.039 -0.283  2.821   1.00 15.10 ?  68  TYR   A CE2  1 
ATOM   1703 C CZ   . TYR   A 1 68  ? 37.588 -0.414  1.521   1.00 15.39 ?  68  TYR   A CZ   1 
ATOM   1704 O OH   . TYR   A 1 68  ? 37.680 -1.625  0.884   1.00 16.98 ?  68  TYR   A OH   1 
ATOM   1705 H H    . TYR   A 1 68  ? 37.773 5.819   3.882   1.00 13.71 ?  68  TYR   A H    1 
ATOM   1706 H HA   . TYR   A 1 68  ? 39.407 3.857   3.455   1.00 14.02 ?  68  TYR   A HA   1 
ATOM   1707 H HB2  . TYR   A 1 68  ? 37.363 3.331   4.365   1.00 14.46 ?  68  TYR   A HB2  1 
ATOM   1708 H HB3  . TYR   A 1 68  ? 36.599 3.897   3.088   1.00 14.46 ?  68  TYR   A HB3  1 
ATOM   1709 H HD1  . TYR   A 1 68  ? 36.637 2.592   1.000   1.00 16.89 ?  68  TYR   A HD1  1 
ATOM   1710 H HD2  . TYR   A 1 68  ? 38.286 1.075   4.305   1.00 17.71 ?  68  TYR   A HD2  1 
ATOM   1711 H HE1  . TYR   A 1 68  ? 36.748 0.556   -0.024  1.00 17.91 ?  68  TYR   A HE1  1 
ATOM   1712 H HE2  . TYR   A 1 68  ? 38.401 -1.009  3.264   1.00 18.15 ?  68  TYR   A HE2  1 
ATOM   1713 H HH   . TYR   A 1 68  ? 38.001 -2.200  1.410   1.00 20.41 ?  68  TYR   A HH   1 
ATOM   1714 N N    . ILE   A 1 69  ? 38.106 4.974   0.739   1.00 10.98 ?  69  ILE   A N    1 
ATOM   1715 C CA   . ILE   A 1 69  ? 38.246 4.954   -0.715  1.00 11.14 ?  69  ILE   A CA   1 
ATOM   1716 C C    . ILE   A 1 69  ? 39.574 5.570   -1.142  1.00 11.15 ?  69  ILE   A C    1 
ATOM   1717 O O    . ILE   A 1 69  ? 40.224 5.089   -2.080  1.00 11.41 ?  69  ILE   A O    1 
ATOM   1718 C CB   . ILE   A 1 69  ? 37.051 5.667   -1.377  1.00 11.74 ?  69  ILE   A CB   1 
ATOM   1719 C CG1  . ILE   A 1 69  ? 35.743 4.921   -1.108  1.00 12.21 ?  69  ILE   A CG1  1 
ATOM   1720 C CG2  . ILE   A 1 69  ? 37.294 5.860   -2.875  1.00 13.11 ?  69  ILE   A CG2  1 
ATOM   1721 C CD1  . ILE   A 1 69  ? 35.582 3.631   -1.885  1.00 13.34 ?  69  ILE   A CD1  1 
ATOM   1722 H H    . ILE   A 1 69  ? 37.489 5.500   1.031   1.00 13.20 ?  69  ILE   A H    1 
ATOM   1723 H HA   . ILE   A 1 69  ? 38.244 4.032   -1.014  1.00 13.40 ?  69  ILE   A HA   1 
ATOM   1724 H HB   . ILE   A 1 69  ? 36.976 6.546   -0.979  1.00 14.12 ?  69  ILE   A HB   1 
ATOM   1725 H HG12 . ILE   A 1 69  ? 35.703 4.704   -0.160  1.00 14.68 ?  69  ILE   A HG12 1 
ATOM   1726 H HG13 . ILE   A 1 69  ? 35.005 5.505   -1.337  1.00 14.68 ?  69  ILE   A HG13 1 
ATOM   1727 H HG21 . ILE   A 1 69  ? 36.447 6.053   -3.310  1.00 15.75 ?  69  ILE   A HG21 1 
ATOM   1728 H HG22 . ILE   A 1 69  ? 37.904 6.605   -3.006  1.00 15.75 ?  69  ILE   A HG22 1 
ATOM   1729 H HG23 . ILE   A 1 69  ? 37.676 5.049   -3.244  1.00 15.75 ?  69  ILE   A HG23 1 
ATOM   1730 H HD11 . ILE   A 1 69  ? 34.789 3.178   -1.571  1.00 16.03 ?  69  ILE   A HD11 1 
ATOM   1731 H HD12 . ILE   A 1 69  ? 35.493 3.846   -2.828  1.00 16.03 ?  69  ILE   A HD12 1 
ATOM   1732 H HD13 . ILE   A 1 69  ? 36.364 3.078   -1.742  1.00 16.03 ?  69  ILE   A HD13 1 
ATOM   1733 N N    . ALA   A 1 70  ? 39.987 6.654   -0.484  1.00 11.20 ?  70  ALA   A N    1 
ATOM   1734 C CA   . ALA   A 1 70  ? 41.259 7.274   -0.833  1.00 12.07 ?  70  ALA   A CA   1 
ATOM   1735 C C    . ALA   A 1 70  ? 42.412 6.292   -0.668  1.00 12.37 ?  70  ALA   A C    1 
ATOM   1736 O O    . ALA   A 1 70  ? 43.381 6.334   -1.433  1.00 14.27 ?  70  ALA   A O    1 
ATOM   1737 C CB   . ALA   A 1 70  ? 41.472 8.525   0.017   1.00 12.79 ?  70  ALA   A CB   1 
ATOM   1738 H H    . ALA   A 1 70  ? 39.551 7.041   0.147   1.00 13.47 ?  70  ALA   A H    1 
ATOM   1739 H HA   . ALA   A 1 70  ? 41.229 7.555   -1.760  1.00 14.51 ?  70  ALA   A HA   1 
ATOM   1740 H HB1  . ALA   A 1 70  ? 42.322 8.928   -0.220  1.00 15.38 ?  70  ALA   A HB1  1 
ATOM   1741 H HB2  . ALA   A 1 70  ? 40.750 9.152   -0.149  1.00 15.38 ?  70  ALA   A HB2  1 
ATOM   1742 H HB3  . ALA   A 1 70  ? 41.478 8.272   0.956   1.00 15.38 ?  70  ALA   A HB3  1 
ATOM   1743 N N    . THR   A 1 71  ? 42.308 5.378   0.296   1.00 12.06 ?  71  THR   A N    1 
ATOM   1744 C CA   . THR   A 1 71  ? 43.365 4.404   0.545   1.00 13.59 ?  71  THR   A CA   1 
ATOM   1745 C C    . THR   A 1 71  ? 43.247 3.182   -0.355  1.00 13.76 ?  71  THR   A C    1 
ATOM   1746 O O    . THR   A 1 71  ? 44.256 2.688   -0.872  1.00 15.99 ?  71  THR   A O    1 
ATOM   1747 C CB   . THR   A 1 71  ? 43.299 3.967   2.005   1.00 15.70 ?  71  THR   A CB   1 
ATOM   1748 O OG1  . THR   A 1 71  ? 43.530 5.105   2.840   1.00 16.72 ?  71  THR   A OG1  1 
ATOM   1749 C CG2  . THR   A 1 71  ? 44.321 2.869   2.307   1.00 16.94 ?  71  THR   A CG2  1 
ATOM   1750 H H    . THR   A 1 71  ? 41.632 5.294   0.816   1.00 14.50 ?  71  THR   A H    1 
ATOM   1751 H HA   . THR   A 1 71  ? 44.228 4.808   0.379   1.00 16.33 ?  71  THR   A HA   1 
ATOM   1752 H HB   . THR   A 1 71  ? 42.420 3.607   2.190   1.00 18.87 ?  71  THR   A HB   1 
ATOM   1753 H HG1  . THR   A 1 71  ? 43.507 4.873   3.646   1.00 20.09 ?  71  THR   A HG1  1 
ATOM   1754 H HG21 . THR   A 1 71  ? 44.444 2.789   3.266   1.00 20.36 ?  71  THR   A HG21 1 
ATOM   1755 H HG22 . THR   A 1 71  ? 44.018 2.017   1.958   1.00 20.36 ?  71  THR   A HG22 1 
ATOM   1756 H HG23 . THR   A 1 71  ? 45.177 3.090   1.902   1.00 20.36 ?  71  THR   A HG23 1 
ATOM   1757 N N    . ASN   A 1 72  ? 42.028 2.671   -0.538  1.00 12.73 ?  72  ASN   A N    1 
ATOM   1758 C CA   . ASN   A 1 72  ? 41.811 1.345   -1.104  1.00 12.96 ?  72  ASN   A CA   1 
ATOM   1759 C C    . ASN   A 1 72  ? 41.190 1.336   -2.489  1.00 12.84 ?  72  ASN   A C    1 
ATOM   1760 O O    . ASN   A 1 72  ? 41.193 0.280   -3.137  1.00 14.05 ?  72  ASN   A O    1 
ATOM   1761 C CB   . ASN   A 1 72  ? 40.928 0.514   -0.166  1.00 13.69 ?  72  ASN   A CB   1 
ATOM   1762 C CG   . ASN   A 1 72  ? 41.546 0.359   1.199   1.00 14.61 ?  72  ASN   A CG   1 
ATOM   1763 O OD1  . ASN   A 1 72  ? 41.081 0.945   2.176   1.00 16.47 ?  72  ASN   A OD1  1 
ATOM   1764 N ND2  . ASN   A 1 72  ? 42.616 -0.399  1.271   1.00 15.50 ?  72  ASN   A ND2  1 
ATOM   1765 H H    . ASN   A 1 72  ? 41.292 3.080   -0.337  1.00 15.31 ?  72  ASN   A H    1 
ATOM   1766 H HA   . ASN   A 1 72  ? 42.664 0.897   -1.174  1.00 15.58 ?  72  ASN   A HA   1 
ATOM   1767 H HB2  . ASN   A 1 72  ? 40.066 0.945   -0.067  1.00 16.46 ?  72  ASN   A HB2  1 
ATOM   1768 H HB3  . ASN   A 1 72  ? 40.812 -0.377  -0.543  1.00 16.46 ?  72  ASN   A HB3  1 
ATOM   1769 H HD21 . ASN   A 1 72  ? 43.011 -0.508  2.028   1.00 18.63 ?  72  ASN   A HD21 1 
ATOM   1770 H HD22 . ASN   A 1 72  ? 42.921 -0.780  0.566   1.00 18.63 ?  72  ASN   A HD22 1 
ATOM   1771 N N    . GLY   A 1 73  ? 40.631 2.449   -2.946  1.00 12.27 ?  73  GLY   A N    1 
ATOM   1772 C CA   . GLY   A 1 73  ? 39.894 2.464   -4.182  1.00 12.15 ?  73  GLY   A CA   1 
ATOM   1773 C C    . GLY   A 1 73  ? 38.509 1.872   -4.015  1.00 11.90 ?  73  GLY   A C    1 
ATOM   1774 O O    . GLY   A 1 73  ? 38.124 1.416   -2.930  1.00 12.34 ?  73  GLY   A O    1 
ATOM   1775 H H    . GLY   A 1 73  ? 40.670 3.218   -2.549  1.00 14.75 ?  73  GLY   A H    1 
ATOM   1776 H HA2  . GLY   A 1 73  ? 39.811 3.382   -4.494  1.00 14.61 ?  73  GLY   A HA2  1 
ATOM   1777 H HA3  . GLY   A 1 73  ? 40.373 1.953   -4.851  1.00 14.61 ?  73  GLY   A HA3  1 
ATOM   1778 N N    . PRO   A 1 74  ? 37.732 1.877   -5.096  1.00 11.94 ?  74  PRO   A N    1 
ATOM   1779 C CA   . PRO   A 1 74  ? 36.339 1.433   -5.014  1.00 12.05 ?  74  PRO   A CA   1 
ATOM   1780 C C    . PRO   A 1 74  ? 36.205 -0.050  -4.695  1.00 11.40 ?  74  PRO   A C    1 
ATOM   1781 O O    . PRO   A 1 74  ? 37.080 -0.874  -4.987  1.00 12.54 ?  74  PRO   A O    1 
ATOM   1782 C CB   . PRO   A 1 74  ? 35.789 1.731   -6.414  1.00 13.53 ?  74  PRO   A CB   1 
ATOM   1783 C CG   . PRO   A 1 74  ? 36.717 2.753   -6.997  1.00 16.11 ?  74  PRO   A CG   1 
ATOM   1784 C CD   . PRO   A 1 74  ? 38.064 2.414   -6.424  1.00 13.81 ?  74  PRO   A CD   1 
ATOM   1785 H HA   . PRO   A 1 74  ? 35.853 1.952   -4.352  1.00 14.49 ?  74  PRO   A HA   1 
ATOM   1786 H HB2  . PRO   A 1 74  ? 35.788 0.921   -6.942  1.00 16.26 ?  74  PRO   A HB2  1 
ATOM   1787 H HB3  . PRO   A 1 74  ? 34.888 2.092   -6.336  1.00 16.26 ?  74  PRO   A HB3  1 
ATOM   1788 H HG2  . PRO   A 1 74  ? 36.726 2.675   -7.962  1.00 19.36 ?  74  PRO   A HG2  1 
ATOM   1789 H HG3  . PRO   A 1 74  ? 36.444 3.642   -6.723  1.00 19.36 ?  74  PRO   A HG3  1 
ATOM   1790 H HD2  . PRO   A 1 74  ? 38.506 1.738   -6.964  1.00 16.60 ?  74  PRO   A HD2  1 
ATOM   1791 H HD3  . PRO   A 1 74  ? 38.608 3.219   -6.354  1.00 16.60 ?  74  PRO   A HD3  1 
ATOM   1792 N N    . LEU   A 1 75  ? 35.070 -0.385  -4.094  1.00 10.73 ?  75  LEU   A N    1 
ATOM   1793 C CA   . LEU   A 1 75  ? 34.694 -1.777  -3.924  1.00 10.59 ?  75  LEU   A CA   1 
ATOM   1794 C C    . LEU   A 1 75  ? 34.325 -2.385  -5.275  1.00 11.04 ?  75  LEU   A C    1 
ATOM   1795 O O    . LEU   A 1 75  ? 34.117 -1.689  -6.269  1.00 12.39 ?  75  LEU   A O    1 
ATOM   1796 C CB   . LEU   A 1 75  ? 33.500 -1.900  -2.980  1.00 10.66 ?  75  LEU   A CB   1 
ATOM   1797 C CG   . LEU   A 1 75  ? 33.701 -1.481  -1.525  1.00 12.52 ?  75  LEU   A CG   1 
ATOM   1798 C CD1  . LEU   A 1 75  ? 32.401 -1.643  -0.743  1.00 14.39 ?  75  LEU   A CD1  1 
ATOM   1799 C CD2  . LEU   A 1 75  ? 34.810 -2.237  -0.855  1.00 15.38 ?  75  LEU   A CD2  1 
ATOM   1800 H H    . LEU   A 1 75  ? 34.500 0.178   -3.778  1.00 12.91 ?  75  LEU   A H    1 
ATOM   1801 H HA   . LEU   A 1 75  ? 35.442 -2.270  -3.552  1.00 12.74 ?  75  LEU   A HA   1 
ATOM   1802 H HB2  . LEU   A 1 75  ? 32.780 -1.355  -3.336  1.00 12.81 ?  75  LEU   A HB2  1 
ATOM   1803 H HB3  . LEU   A 1 75  ? 33.221 -2.829  -2.974  1.00 12.81 ?  75  LEU   A HB3  1 
ATOM   1804 H HG   . LEU   A 1 75  ? 33.947 -0.541  -1.511  1.00 15.05 ?  75  LEU   A HG   1 
ATOM   1805 H HD11 . LEU   A 1 75  ? 32.555 -1.364  0.174   1.00 17.30 ?  75  LEU   A HD11 1 
ATOM   1806 H HD12 . LEU   A 1 75  ? 31.725 -1.077  -1.150  1.00 17.30 ?  75  LEU   A HD12 1 
ATOM   1807 H HD13 . LEU   A 1 75  ? 32.129 -2.566  -0.774  1.00 17.30 ?  75  LEU   A HD13 1 
ATOM   1808 H HD21 . LEU   A 1 75  ? 34.855 -1.973  0.077   1.00 18.49 ?  75  LEU   A HD21 1 
ATOM   1809 H HD22 . LEU   A 1 75  ? 34.633 -3.188  -0.922  1.00 18.49 ?  75  LEU   A HD22 1 
ATOM   1810 H HD23 . LEU   A 1 75  ? 35.654 -2.029  -1.294  1.00 18.49 ?  75  LEU   A HD23 1 
ATOM   1811 N N    . LYS   A 1 76  ? 34.232 -3.711  -5.292  1.00 11.25 ?  76  LYS   A N    1 
ATOM   1812 C CA   . LYS   A 1 76  ? 33.656 -4.445  -6.411  1.00 11.59 ?  76  LYS   A CA   1 
ATOM   1813 C C    . LYS   A 1 76  ? 32.142 -4.525  -6.246  1.00 10.62 ?  76  LYS   A C    1 
ATOM   1814 O O    . LYS   A 1 76  ? 31.632 -4.606  -5.131  1.00 11.04 ?  76  LYS   A O    1 
ATOM   1815 C CB   . LYS   A 1 76  ? 34.205 -5.881  -6.426  1.00 12.63 ?  76  LYS   A CB   1 
ATOM   1816 C CG   . LYS   A 1 76  ? 35.708 -5.980  -6.641  1.00 14.03 ?  76  LYS   A CG   1 
ATOM   1817 C CD   . LYS   A 1 76  ? 36.236 -7.384  -6.417  1.00 15.37 ?  76  LYS   A CD   1 
ATOM   1818 C CE   . LYS   A 1 76  ? 37.725 -7.457  -6.675  1.00 17.36 ?  76  LYS   A CE   1 
ATOM   1819 N NZ   . LYS   A 1 76  ? 38.257 -8.813  -6.452  1.00 18.73 ?  76  LYS   A NZ   1 
ATOM   1820 H H    . LYS   A 1 76  ? 34.500 -4.217  -4.650  1.00 13.52 ?  76  LYS   A H    1 
ATOM   1821 H HA   . LYS   A 1 76  ? 33.873 -4.004  -7.251  1.00 13.93 ?  76  LYS   A HA   1 
ATOM   1822 H HB2  . LYS   A 1 76  ? 34.006 -6.297  -5.578  1.00 15.19 ?  76  LYS   A HB2  1 
ATOM   1823 H HB3  . LYS   A 1 76  ? 33.779 -6.366  -7.146  1.00 15.19 ?  76  LYS   A HB3  1 
ATOM   1824 H HG2  . LYS   A 1 76  ? 35.921 -5.720  -7.552  1.00 16.86 ?  76  LYS   A HG2  1 
ATOM   1825 H HG3  . LYS   A 1 76  ? 36.162 -5.388  -6.017  1.00 16.86 ?  76  LYS   A HG3  1 
ATOM   1826 H HD2  . LYS   A 1 76  ? 36.071 -7.647  -5.499  1.00 18.47 ?  76  LYS   A HD2  1 
ATOM   1827 H HD3  . LYS   A 1 76  ? 35.789 -7.994  -7.027  1.00 18.47 ?  76  LYS   A HD3  1 
ATOM   1828 H HE2  . LYS   A 1 76  ? 37.898 -7.212  -7.597  1.00 20.85 ?  76  LYS   A HE2  1 
ATOM   1829 H HE3  . LYS   A 1 76  ? 38.180 -6.852  -6.074  1.00 20.85 ?  76  LYS   A HE3  1 
ATOM   1830 H HZ1  . LYS   A 1 76  ? 39.132 -8.835  -6.612  1.00 22.50 ?  76  LYS   A HZ1  1 
ATOM   1831 H HZ2  . LYS   A 1 76  ? 38.111 -9.071  -5.611  1.00 22.50 ?  76  LYS   A HZ2  1 
ATOM   1832 H HZ3  . LYS   A 1 76  ? 37.854 -9.399  -6.999  1.00 22.50 ?  76  LYS   A HZ3  1 
ATOM   1833 N N    A VAL   A 1 77  ? 31.427 -4.560  -7.370  0.42 11.12 ?  77  VAL   A N    1 
ATOM   1834 N N    B VAL   A 1 77  ? 31.426 -4.512  -7.370  0.58 11.19 ?  77  VAL   A N    1 
ATOM   1835 C CA   A VAL   A 1 77  ? 30.009 -4.899  -7.311  0.42 11.19 ?  77  VAL   A CA   1 
ATOM   1836 C CA   B VAL   A 1 77  ? 30.027 -4.915  -7.323  0.58 11.32 ?  77  VAL   A CA   1 
ATOM   1837 C C    A VAL   A 1 77  ? 29.892 -6.357  -6.884  0.42 10.80 ?  77  VAL   A C    1 
ATOM   1838 C C    B VAL   A 1 77  ? 29.978 -6.349  -6.820  0.58 10.83 ?  77  VAL   A C    1 
ATOM   1839 O O    A VAL   A 1 77  ? 30.479 -7.248  -7.509  0.42 11.07 ?  77  VAL   A O    1 
ATOM   1840 O O    B VAL   A 1 77  ? 30.705 -7.218  -7.317  0.58 11.01 ?  77  VAL   A O    1 
ATOM   1841 C CB   A VAL   A 1 77  ? 29.310 -4.639  -8.652  0.42 12.02 ?  77  VAL   A CB   1 
ATOM   1842 C CB   B VAL   A 1 77  ? 29.374 -4.766  -8.705  0.58 12.48 ?  77  VAL   A CB   1 
ATOM   1843 C CG1  A VAL   A 1 77  ? 27.845 -5.066  -8.581  0.42 12.89 ?  77  VAL   A CG1  1 
ATOM   1844 C CG1  B VAL   A 1 77  ? 27.899 -5.146  -8.642  0.58 13.60 ?  77  VAL   A CG1  1 
ATOM   1845 C CG2  A VAL   A 1 77  ? 29.409 -3.169  -9.017  0.42 12.37 ?  77  VAL   A CG2  1 
ATOM   1846 C CG2  B VAL   A 1 77  ? 29.535 -3.344  -9.218  0.58 12.97 ?  77  VAL   A CG2  1 
ATOM   1847 H H    A VAL   A 1 77  ? 31.734 -4.411  -8.160  0.42 13.37 ?  77  VAL   A H    1 
ATOM   1848 H H    B VAL   A 1 77  ? 31.724 -4.291  -8.146  0.58 13.45 ?  77  VAL   A H    1 
ATOM   1849 H HA   A VAL   A 1 77  ? 29.582 -4.356  -6.637  0.42 13.45 ?  77  VAL   A HA   1 
ATOM   1850 H HA   B VAL   A 1 77  ? 29.555 -4.355  -6.693  0.58 13.61 ?  77  VAL   A HA   1 
ATOM   1851 H HB   A VAL   A 1 77  ? 29.746 -5.153  -9.352  0.42 14.45 ?  77  VAL   A HB   1 
ATOM   1852 H HB   B VAL   A 1 77  ? 29.818 -5.362  -9.331  0.58 15.01 ?  77  VAL   A HB   1 
ATOM   1853 H HG11 A VAL   A 1 77  ? 27.384 -4.737  -9.369  0.42 15.50 ?  77  VAL   A HG11 1 
ATOM   1854 H HG11 B VAL   A 1 77  ? 27.486 -4.934  -9.494  0.58 16.34 ?  77  VAL   A HG11 1 
ATOM   1855 H HG12 A VAL   A 1 77  ? 27.796 -6.033  -8.551  0.42 15.50 ?  77  VAL   A HG12 1 
ATOM   1856 H HG12 B VAL   A 1 77  ? 27.822 -6.094  -8.464  0.58 16.34 ?  77  VAL   A HG12 1 
ATOM   1857 H HG13 A VAL   A 1 77  ? 27.447 -4.686  -7.783  0.42 15.50 ?  77  VAL   A HG13 1 
ATOM   1858 H HG13 B VAL   A 1 77  ? 27.474 -4.637  -7.934  0.58 16.34 ?  77  VAL   A HG13 1 
ATOM   1859 H HG21 A VAL   A 1 77  ? 28.934 -3.016  -9.847  0.42 14.87 ?  77  VAL   A HG21 1 
ATOM   1860 H HG21 B VAL   A 1 77  ? 29.012 -3.239  -10.025 0.58 15.60 ?  77  VAL   A HG21 1 
ATOM   1861 H HG22 A VAL   A 1 77  ? 29.014 -2.642  -8.305  0.42 14.87 ?  77  VAL   A HG22 1 
ATOM   1862 H HG22 B VAL   A 1 77  ? 29.224 -2.727  -8.537  0.58 15.60 ?  77  VAL   A HG22 1 
ATOM   1863 H HG23 A VAL   A 1 77  ? 30.346 -2.932  -9.122  0.42 14.87 ?  77  VAL   A HG23 1 
ATOM   1864 H HG23 B VAL   A 1 77  ? 30.474 -3.176  -9.408  0.58 15.60 ?  77  VAL   A HG23 1 
ATOM   1865 N N    . GLY   A 1 78  ? 29.142 -6.602  -5.808  1.00 10.47 ?  78  GLY   A N    1 
ATOM   1866 C CA   . GLY   A 1 78  ? 29.103 -7.885  -5.139  1.00 10.85 ?  78  GLY   A CA   1 
ATOM   1867 C C    . GLY   A 1 78  ? 30.009 -7.969  -3.928  1.00 10.55 ?  78  GLY   A C    1 
ATOM   1868 O O    . GLY   A 1 78  ? 29.941 -8.968  -3.193  1.00 10.87 ?  78  GLY   A O    1 
ATOM   1869 H H    A GLY   A 1 78  ? 28.635 -6.011  -5.440  0.42 12.59 ?  78  GLY   A H    1 
ATOM   1870 H H    B GLY   A 1 78  ? 28.574 -6.031  -5.501  0.58 12.59 ?  78  GLY   A H    1 
ATOM   1871 H HA2  . GLY   A 1 78  ? 28.195 -8.064  -4.852  1.00 13.04 ?  78  GLY   A HA2  1 
ATOM   1872 H HA3  . GLY   A 1 78  ? 29.365 -8.578  -5.765  1.00 13.04 ?  78  GLY   A HA3  1 
ATOM   1873 N N    . GLY   A 1 79  ? 30.865 -6.963  -3.706  1.00 10.49 ?  79  GLY   A N    1 
ATOM   1874 C CA   . GLY   A 1 79  ? 31.811 -6.964  -2.612  1.00 10.63 ?  79  GLY   A CA   1 
ATOM   1875 C C    . GLY   A 1 79  ? 31.341 -6.166  -1.404  1.00 9.98  ?  79  GLY   A C    1 
ATOM   1876 O O    . GLY   A 1 79  ? 30.218 -5.663  -1.346  1.00 10.68 ?  79  GLY   A O    1 
ATOM   1877 H H    . GLY   A 1 79  ? 30.921 -6.259  -4.198  1.00 12.62 ?  79  GLY   A H    1 
ATOM   1878 H HA2  . GLY   A 1 79  ? 31.968 -7.884  -2.327  1.00 12.78 ?  79  GLY   A HA2  1 
ATOM   1879 H HA3  . GLY   A 1 79  ? 32.654 -6.597  -2.911  1.00 12.78 ?  79  GLY   A HA3  1 
ATOM   1880 N N    . SER   A 1 80  ? 32.233 -6.067  -0.418  1.00 10.84 ?  80  SER   A N    1 
ATOM   1881 C CA   . SER   A 1 80  ? 31.901 -5.423  0.843   1.00 10.21 ?  80  SER   A CA   1 
ATOM   1882 C C    . SER   A 1 80  ? 33.161 -4.956  1.551   1.00 10.18 ?  80  SER   A C    1 
ATOM   1883 O O    . SER   A 1 80  ? 34.279 -5.383  1.242   1.00 11.50 ?  80  SER   A O    1 
ATOM   1884 C CB   . SER   A 1 80  ? 31.138 -6.374  1.771   1.00 11.00 ?  80  SER   A CB   1 
ATOM   1885 O OG   . SER   A 1 80  ? 31.970 -7.414  2.255   1.00 12.71 ?  80  SER   A OG   1 
ATOM   1886 H H    . SER   A 1 80  ? 33.041 -6.354  -0.464  1.00 13.03 ?  80  SER   A H    1 
ATOM   1887 H HA   . SER   A 1 80  ? 31.348 -4.652  0.658   1.00 12.28 ?  80  SER   A HA   1 
ATOM   1888 H HB2  . SER   A 1 80  ? 30.801 -5.865  2.526   1.00 13.23 ?  80  SER   A HB2  1 
ATOM   1889 H HB3  . SER   A 1 80  ? 30.399 -6.762  1.280   1.00 13.23 ?  80  SER   A HB3  1 
ATOM   1890 H HG   . SER   A 1 80  ? 32.267 -7.866  1.612   1.00 15.28 ?  80  SER   A HG   1 
ATOM   1891 N N    . CYS   A 1 81  ? 32.955 -4.098  2.544   1.00 9.79  ?  81  CYS   A N    1 
ATOM   1892 C CA   . CYS   A 1 81  ? 33.997 -3.797  3.512   1.00 10.06 ?  81  CYS   A CA   1 
ATOM   1893 C C    . CYS   A 1 81  ? 33.349 -3.568  4.869   1.00 9.86  ?  81  CYS   A C    1 
ATOM   1894 O O    . CYS   A 1 81  ? 32.178 -3.176  4.955   1.00 10.84 ?  81  CYS   A O    1 
ATOM   1895 C CB   . CYS   A 1 81  ? 34.864 -2.603  3.092   1.00 10.57 ?  81  CYS   A CB   1 
ATOM   1896 S SG   . CYS   A 1 81  ? 33.951 -1.040  3.095   1.00 10.75 ?  81  CYS   A SG   1 
ATOM   1897 H H    . CYS   A 1 81  ? 32.218 -3.675  2.675   1.00 11.78 ?  81  CYS   A H    1 
ATOM   1898 H HA   . CYS   A 1 81  ? 34.578 -4.566  3.591   1.00 12.09 ?  81  CYS   A HA   1 
ATOM   1899 H HB2  . CYS   A 1 81  ? 35.611 -2.524  3.706   1.00 12.71 ?  81  CYS   A HB2  1 
ATOM   1900 H HB3  . CYS   A 1 81  ? 35.194 -2.758  2.190   1.00 12.71 ?  81  CYS   A HB3  1 
ATOM   1901 H HG   . CYS   A 1 81  ? 34.687 -0.153  2.763   1.00 12.93 ?  81  CYS   A HG   1 
ATOM   1902 N N    . VAL   A 1 82  ? 34.113 -3.829  5.926   1.00 10.12 ?  82  VAL   A N    1 
ATOM   1903 C CA   . VAL   A 1 82  ? 33.686 -3.586  7.298   1.00 10.54 ?  82  VAL   A CA   1 
ATOM   1904 C C    . VAL   A 1 82  ? 34.273 -2.263  7.766   1.00 10.54 ?  82  VAL   A C    1 
ATOM   1905 O O    . VAL   A 1 82  ? 35.496 -2.080  7.764   1.00 11.77 ?  82  VAL   A O    1 
ATOM   1906 C CB   . VAL   A 1 82  ? 34.111 -4.719  8.243   1.00 12.12 ?  82  VAL   A CB   1 
ATOM   1907 C CG1  . VAL   A 1 82  ? 33.659 -4.410  9.666   1.00 13.72 ?  82  VAL   A CG1  1 
ATOM   1908 C CG2  . VAL   A 1 82  ? 33.560 -6.056  7.788   1.00 12.87 ?  82  VAL   A CG2  1 
ATOM   1909 H H    . VAL   A 1 82  ? 34.908 -4.169  5.871   1.00 12.17 ?  82  VAL   A H    1 
ATOM   1910 H HA   . VAL   A 1 82  ? 32.722 -3.515  7.325   1.00 12.67 ?  82  VAL   A HA   1 
ATOM   1911 H HB   . VAL   A 1 82  ? 35.078 -4.780  8.250   1.00 14.57 ?  82  VAL   A HB   1 
ATOM   1912 H HG11 . VAL   A 1 82  ? 33.731 -5.216  10.203  1.00 16.49 ?  82  VAL   A HG11 1 
ATOM   1913 H HG12 . VAL   A 1 82  ? 34.222 -3.715  10.040  1.00 16.49 ?  82  VAL   A HG12 1 
ATOM   1914 H HG13 . VAL   A 1 82  ? 32.734 -4.112  9.647   1.00 16.49 ?  82  VAL   A HG13 1 
ATOM   1915 H HG21 . VAL   A 1 82  ? 33.822 -6.738  8.425   1.00 15.47 ?  82  VAL   A HG21 1 
ATOM   1916 H HG22 . VAL   A 1 82  ? 32.593 -5.997  7.743   1.00 15.47 ?  82  VAL   A HG22 1 
ATOM   1917 H HG23 . VAL   A 1 82  ? 33.921 -6.261  6.913   1.00 15.47 ?  82  VAL   A HG23 1 
ATOM   1918 N N    . LEU   A 1 83  ? 33.408 -1.345  8.174   1.00 10.33 ?  83  LEU   A N    1 
ATOM   1919 C CA   . LEU   A 1 83  ? 33.808 -0.068  8.750   1.00 10.26 ?  83  LEU   A CA   1 
ATOM   1920 C C    . LEU   A 1 83  ? 33.085 0.107   10.082  1.00 10.31 ?  83  LEU   A C    1 
ATOM   1921 O O    . LEU   A 1 83  ? 32.365 -0.785  10.543  1.00 10.94 ?  83  LEU   A O    1 
ATOM   1922 C CB   . LEU   A 1 83  ? 33.554 1.085   7.768   1.00 10.92 ?  83  LEU   A CB   1 
ATOM   1923 C CG   . LEU   A 1 83  ? 34.454 1.089   6.524   1.00 11.93 ?  83  LEU   A CG   1 
ATOM   1924 C CD1  . LEU   A 1 83  ? 33.990 2.144   5.530   1.00 12.27 ?  83  LEU   A CD1  1 
ATOM   1925 C CD2  . LEU   A 1 83  ? 35.923 1.304   6.890   1.00 12.46 ?  83  LEU   A CD2  1 
ATOM   1926 H H    . LEU   A 1 83  ? 32.558 -1.437  8.119   1.00 12.42 ?  83  LEU   A H    1 
ATOM   1927 H HA   . LEU   A 1 83  ? 34.760 -0.083  8.937   1.00 12.34 ?  83  LEU   A HA   1 
ATOM   1928 H HB2  . LEU   A 1 83  ? 32.634 1.035   7.459   1.00 13.14 ?  83  LEU   A HB2  1 
ATOM   1929 H HB3  . LEU   A 1 83  ? 33.688 1.929   8.230   1.00 13.14 ?  83  LEU   A HB3  1 
ATOM   1930 H HG   . LEU   A 1 83  ? 34.384 0.229   6.091   1.00 14.34 ?  83  LEU   A HG   1 
ATOM   1931 H HD11 . LEU   A 1 83  ? 34.572 2.124   4.756   1.00 14.75 ?  83  LEU   A HD11 1 
ATOM   1932 H HD12 . LEU   A 1 83  ? 33.078 1.943   5.265   1.00 14.75 ?  83  LEU   A HD12 1 
ATOM   1933 H HD13 . LEU   A 1 83  ? 34.026 3.016   5.953   1.00 14.75 ?  83  LEU   A HD13 1 
ATOM   1934 H HD21 . LEU   A 1 83  ? 36.436 1.440   6.075   1.00 14.98 ?  83  LEU   A HD21 1 
ATOM   1935 H HD22 . LEU   A 1 83  ? 36.000 2.090   7.457   1.00 14.98 ?  83  LEU   A HD22 1 
ATOM   1936 H HD23 . LEU   A 1 83  ? 36.253 0.525   7.360   1.00 14.98 ?  83  LEU   A HD23 1 
ATOM   1937 N N    . SER   A 1 84  ? 33.281 1.257   10.713  1.00 11.40 ?  84  SER   A N    1 
ATOM   1938 C CA   . SER   A 1 84  ? 32.622 1.502   11.983  1.00 11.26 ?  84  SER   A CA   1 
ATOM   1939 C C    . SER   A 1 84  ? 31.107 1.597   11.817  1.00 11.25 ?  84  SER   A C    1 
ATOM   1940 O O    . SER   A 1 84  ? 30.596 2.053   10.794  1.00 11.19 ?  84  SER   A O    1 
ATOM   1941 C CB   . SER   A 1 84  ? 33.117 2.825   12.560  1.00 12.29 ?  84  SER   A CB   1 
ATOM   1942 O OG   . SER   A 1 84  ? 32.478 3.124   13.781  1.00 13.10 ?  84  SER   A OG   1 
ATOM   1943 H H    . SER   A 1 84  ? 33.772 1.907   10.430  1.00 13.71 ?  84  SER   A H    1 
ATOM   1944 H HA   . SER   A 1 84  ? 32.831 0.786   12.607  1.00 13.54 ?  84  SER   A HA   1 
ATOM   1945 H HB2  . SER   A 1 84  ? 34.076 2.767   12.706  1.00 14.78 ?  84  SER   A HB2  1 
ATOM   1946 H HB3  . SER   A 1 84  ? 32.921 3.536   11.934  1.00 14.78 ?  84  SER   A HB3  1 
ATOM   1947 H HG   . SER   A 1 84  ? 32.776 3.851   14.096  1.00 15.75 ?  84  SER   A HG   1 
ATOM   1948 N N    A GLY   A 1 85  ? 30.388 1.133   12.835  0.42 11.72 ?  85  GLY   A N    1 
ATOM   1949 N N    B GLY   A 1 85  ? 30.384 1.223   12.872  0.58 12.18 ?  85  GLY   A N    1 
ATOM   1950 C CA   A GLY   A 1 85  ? 28.967 1.369   12.935  0.42 11.78 ?  85  GLY   A CA   1 
ATOM   1951 C CA   B GLY   A 1 85  ? 28.958 1.464   12.947  0.58 12.49 ?  85  GLY   A CA   1 
ATOM   1952 C C    A GLY   A 1 85  ? 28.619 2.683   13.587  0.42 11.27 ?  85  GLY   A C    1 
ATOM   1953 C C    B GLY   A 1 85  ? 28.565 2.778   13.583  0.58 12.29 ?  85  GLY   A C    1 
ATOM   1954 O O    A GLY   A 1 85  ? 27.437 3.005   13.735  0.42 11.14 ?  85  GLY   A O    1 
ATOM   1955 O O    B GLY   A 1 85  ? 27.373 3.088   13.651  0.58 12.84 ?  85  GLY   A O    1 
ATOM   1956 H H    A GLY   A 1 85  ? 30.711 0.673   13.487  0.42 14.09 ?  85  GLY   A H    1 
ATOM   1957 H H    B GLY   A 1 85  ? 30.703 0.820   13.564  0.58 14.64 ?  85  GLY   A H    1 
ATOM   1958 H HA2  A GLY   A 1 85  ? 28.580 1.355   12.045  0.42 14.16 ?  85  GLY   A HA2  1 
ATOM   1959 H HA2  B GLY   A 1 85  ? 28.589 1.449   12.049  0.58 15.02 ?  85  GLY   A HA2  1 
ATOM   1960 H HA3  A GLY   A 1 85  ? 28.559 0.659   13.452  0.42 14.16 ?  85  GLY   A HA3  1 
ATOM   1961 H HA3  B GLY   A 1 85  ? 28.541 0.752   13.452  0.58 15.02 ?  85  GLY   A HA3  1 
ATOM   1962 N N    A HIS   A 1 86  ? 29.628 3.449   13.997  0.42 11.16 ?  86  HIS   A N    1 
ATOM   1963 N N    B HIS   A 1 86  ? 29.528 3.559   14.056  0.58 12.10 ?  86  HIS   A N    1 
ATOM   1964 C CA   A HIS   A 1 86  ? 29.451 4.785   14.572  0.42 11.46 ?  86  HIS   A CA   1 
ATOM   1965 C CA   B HIS   A 1 86  ? 29.264 4.898   14.614  0.58 12.19 ?  86  HIS   A CA   1 
ATOM   1966 C C    A HIS   A 1 86  ? 28.472 4.682   15.739  0.42 11.62 ?  86  HIS   A C    1 
ATOM   1967 C C    B HIS   A 1 86  ? 28.242 4.759   15.746  0.58 13.39 ?  86  HIS   A C    1 
ATOM   1968 O O    A HIS   A 1 86  ? 28.694 3.858   16.639  0.42 11.92 ?  86  HIS   A O    1 
ATOM   1969 O O    B HIS   A 1 86  ? 28.370 3.851   16.582  0.58 14.74 ?  86  HIS   A O    1 
ATOM   1970 C CB   A HIS   A 1 86  ? 29.100 5.776   13.469  0.42 12.40 ?  86  HIS   A CB   1 
ATOM   1971 C CB   B HIS   A 1 86  ? 28.904 5.857   13.491  0.58 11.80 ?  86  HIS   A CB   1 
ATOM   1972 C CG   A HIS   A 1 86  ? 30.161 5.875   12.424  0.42 12.97 ?  86  HIS   A CG   1 
ATOM   1973 C CG   B HIS   A 1 86  ? 29.972 5.948   12.456  0.58 11.14 ?  86  HIS   A CG   1 
ATOM   1974 N ND1  A HIS   A 1 86  ? 31.261 6.694   12.561  0.42 13.71 ?  86  HIS   A ND1  1 
ATOM   1975 N ND1  B HIS   A 1 86  ? 31.047 6.802   12.577  0.58 12.54 ?  86  HIS   A ND1  1 
ATOM   1976 C CD2  A HIS   A 1 86  ? 30.326 5.213   11.255  0.42 13.10 ?  86  HIS   A CD2  1 
ATOM   1977 C CD2  B HIS   A 1 86  ? 30.176 5.237   11.323  0.58 11.21 ?  86  HIS   A CD2  1 
ATOM   1978 C CE1  A HIS   A 1 86  ? 32.046 6.549   11.509  0.42 13.74 ?  86  HIS   A CE1  1 
ATOM   1979 C CE1  B HIS   A 1 86  ? 31.855 6.629   11.546  0.58 12.68 ?  86  HIS   A CE1  1 
ATOM   1980 N NE2  A HIS   A 1 86  ? 31.503 5.655   10.703  0.42 13.30 ?  86  HIS   A NE2  1 
ATOM   1981 N NE2  B HIS   A 1 86  ? 31.353 5.682   10.774  0.58 11.78 ?  86  HIS   A NE2  1 
ATOM   1982 H H    A HIS   A 1 86  ? 30.450 3.208   13.963  0.42 13.42 ?  86  HIS   A H    1 
ATOM   1983 H H    B HIS   A 1 86  ? 30.357 3.348   14.071  0.58 14.55 ?  86  HIS   A H    1 
ATOM   1984 H HA   A HIS   A 1 86  ? 30.294 5.070   14.944  0.42 13.78 ?  86  HIS   A HA   1 
ATOM   1985 H HA   B HIS   A 1 86  ? 30.090 5.228   15.003  0.58 14.65 ?  86  HIS   A HA   1 
ATOM   1986 H HB2  A HIS   A 1 86  ? 28.277 5.498   13.036  0.42 14.91 ?  86  HIS   A HB2  1 
ATOM   1987 H HB2  B HIS   A 1 86  ? 28.091 5.557   13.056  0.58 14.19 ?  86  HIS   A HB2  1 
ATOM   1988 H HB3  A HIS   A 1 86  ? 28.981 6.660   13.860  0.42 14.91 ?  86  HIS   A HB3  1 
ATOM   1989 H HB3  B HIS   A 1 86  ? 28.773 6.750   13.856  0.58 14.19 ?  86  HIS   A HB3  1 
ATOM   1990 H HD2  A HIS   A 1 86  ? 29.750 4.579   10.893  0.42 15.75 ?  86  HIS   A HD2  1 
ATOM   1991 H HD2  B HIS   A 1 86  ? 29.625 4.569   10.978  0.58 13.48 ?  86  HIS   A HD2  1 
ATOM   1992 H HE1  A HIS   A 1 86  ? 32.843 7.006   11.359  0.42 16.52 ?  86  HIS   A HE1  1 
ATOM   1993 H HE1  B HIS   A 1 86  ? 32.643 7.099   11.382  0.58 15.24 ?  86  HIS   A HE1  1 
ATOM   1994 H HE2  A HIS   A 1 86  ? 31.831 5.396   9.951   0.42 15.98 ?  86  HIS   A HE2  1 
ATOM   1995 H HE2  B HIS   A 1 86  ? 31.699 5.402   10.033  0.58 14.17 ?  86  HIS   A HE2  1 
ATOM   1996 N N    A ASN   A 1 87  ? 27.424 5.494   15.780  0.42 12.22 ?  87  ASN   A N    1 
ATOM   1997 N N    B ASN   A 1 87  ? 27.246 5.637   15.802  0.58 14.35 ?  87  ASN   A N    1 
ATOM   1998 C CA   A ASN   A 1 87  ? 26.442 5.460   16.851  0.42 13.03 ?  87  ASN   A CA   1 
ATOM   1999 C CA   B ASN   A 1 87  ? 26.233 5.647   16.846  0.58 14.52 ?  87  ASN   A CA   1 
ATOM   2000 C C    A ASN   A 1 87  ? 25.339 4.435   16.621  0.42 13.59 ?  87  ASN   A C    1 
ATOM   2001 C C    B ASN   A 1 87  ? 25.084 4.697   16.555  0.58 15.07 ?  87  ASN   A C    1 
ATOM   2002 O O    A ASN   A 1 87  ? 24.460 4.304   17.476  0.42 14.16 ?  87  ASN   A O    1 
ATOM   2003 O O    B ASN   A 1 87  ? 24.060 4.762   17.245  0.58 16.48 ?  87  ASN   A O    1 
ATOM   2004 C CB   A ASN   A 1 87  ? 25.840 6.861   17.053  0.42 13.96 ?  87  ASN   A CB   1 
ATOM   2005 C CB   B ASN   A 1 87  ? 25.658 7.058   16.980  0.58 15.08 ?  87  ASN   A CB   1 
ATOM   2006 C CG   A ASN   A 1 87  ? 25.404 7.509   15.748  0.42 14.48 ?  87  ASN   A CG   1 
ATOM   2007 C CG   B ASN   A 1 87  ? 25.061 7.572   15.677  0.58 15.64 ?  87  ASN   A CG   1 
ATOM   2008 O OD1  A ASN   A 1 87  ? 26.149 7.522   14.768  0.42 14.49 ?  87  ASN   A OD1  1 
ATOM   2009 O OD1  B ASN   A 1 87  ? 25.582 7.309   14.596  0.58 15.19 ?  87  ASN   A OD1  1 
ATOM   2010 N ND2  A ASN   A 1 87  ? 24.193 8.056   15.734  0.42 15.63 ?  87  ASN   A ND2  1 
ATOM   2011 N ND2  B ASN   A 1 87  ? 23.964 8.306   15.777  0.58 17.44 ?  87  ASN   A ND2  1 
ATOM   2012 H H    A ASN   A 1 87  ? 27.256 6.092   15.185  0.42 14.69 ?  87  ASN   A H    1 
ATOM   2013 H H    B ASN   A 1 87  ? 27.117 6.254   15.219  0.58 17.25 ?  87  ASN   A H    1 
ATOM   2014 H HA   A ASN   A 1 87  ? 26.876 5.209   17.675  0.42 15.67 ?  87  ASN   A HA   1 
ATOM   2015 H HA   B ASN   A 1 87  ? 26.648 5.403   17.697  0.58 17.45 ?  87  ASN   A HA   1 
ATOM   2016 H HB2  A ASN   A 1 87  ? 25.061 6.798   17.631  0.42 16.78 ?  87  ASN   A HB2  1 
ATOM   2017 H HB2  B ASN   A 1 87  ? 24.953 7.045   17.650  0.58 18.13 ?  87  ASN   A HB2  1 
ATOM   2018 H HB3  A ASN   A 1 87  ? 26.508 7.434   17.466  0.42 16.78 ?  87  ASN   A HB3  1 
ATOM   2019 H HB3  B ASN   A 1 87  ? 26.362 7.661   17.248  0.58 18.13 ?  87  ASN   A HB3  1 
ATOM   2020 H HD21 A ASN   A 1 87  ? 23.900 8.440   15.021  0.42 18.79 ?  87  ASN   A HD21 1 
ATOM   2021 H HD21 B ASN   A 1 87  ? 23.590 8.611   15.066  0.58 20.96 ?  87  ASN   A HD21 1 
ATOM   2022 H HD22 A ASN   A 1 87  ? 23.700 8.035   16.440  0.42 18.79 ?  87  ASN   A HD22 1 
ATOM   2023 H HD22 B ASN   A 1 87  ? 23.628 8.469   16.548  0.58 20.96 ?  87  ASN   A HD22 1 
ATOM   2024 N N    A LEU   A 1 88  ? 25.389 3.671   15.529  0.42 13.45 ?  88  LEU   A N    1 
ATOM   2025 N N    B LEU   A 1 88  ? 25.209 3.845   15.536  0.58 13.85 ?  88  LEU   A N    1 
ATOM   2026 C CA   A LEU   A 1 88  ? 24.285 2.800   15.132  0.42 13.49 ?  88  LEU   A CA   1 
ATOM   2027 C CA   B LEU   A 1 88  ? 24.116 2.972   15.133  0.58 13.80 ?  88  LEU   A CA   1 
ATOM   2028 C C    A LEU   A 1 88  ? 24.520 1.327   15.436  0.42 13.62 ?  88  LEU   A C    1 
ATOM   2029 C C    B LEU   A 1 88  ? 24.357 1.497   15.417  0.58 13.22 ?  88  LEU   A C    1 
ATOM   2030 O O    A LEU   A 1 88  ? 23.553 0.583   15.626  0.42 14.96 ?  88  LEU   A O    1 
ATOM   2031 O O    B LEU   A 1 88  ? 23.387 0.745   15.550  0.58 14.51 ?  88  LEU   A O    1 
ATOM   2032 C CB   A LEU   A 1 88  ? 24.029 2.943   13.628  0.42 13.76 ?  88  LEU   A CB   1 
ATOM   2033 C CB   B LEU   A 1 88  ? 23.842 3.148   13.634  0.58 14.29 ?  88  LEU   A CB   1 
ATOM   2034 C CG   A LEU   A 1 88  ? 23.769 4.351   13.098  0.42 14.79 ?  88  LEU   A CG   1 
ATOM   2035 C CG   B LEU   A 1 88  ? 23.563 4.592   13.205  0.58 15.21 ?  88  LEU   A CG   1 
ATOM   2036 C CD1  A LEU   A 1 88  ? 23.680 4.324   11.583  0.42 15.02 ?  88  LEU   A CD1  1 
ATOM   2037 C CD1  B LEU   A 1 88  ? 23.337 4.693   11.703  0.58 15.08 ?  88  LEU   A CD1  1 
ATOM   2038 C CD2  A LEU   A 1 88  ? 22.497 4.931   13.703  0.42 16.27 ?  88  LEU   A CD2  1 
ATOM   2039 C CD2  B LEU   A 1 88  ? 22.371 5.159   13.959  0.58 16.45 ?  88  LEU   A CD2  1 
ATOM   2040 H H    A LEU   A 1 88  ? 26.071 3.624   15.010  0.42 16.16 ?  88  LEU   A H    1 
ATOM   2041 H H    B LEU   A 1 88  ? 25.917 3.773   15.047  0.58 16.65 ?  88  LEU   A H    1 
ATOM   2042 H HA   A LEU   A 1 88  ? 23.481 3.076   15.594  0.42 16.22 ?  88  LEU   A HA   1 
ATOM   2043 H HA   B LEU   A 1 88  ? 23.318 3.240   15.613  0.58 16.58 ?  88  LEU   A HA   1 
ATOM   2044 H HB2  A LEU   A 1 88  ? 24.797 2.600   13.153  0.42 16.53 ?  88  LEU   A HB2  1 
ATOM   2045 H HB2  B LEU   A 1 88  ? 24.612 2.837   13.137  0.58 17.18 ?  88  LEU   A HB2  1 
ATOM   2046 H HB3  A LEU   A 1 88  ? 23.248 2.411   13.403  0.42 16.53 ?  88  LEU   A HB3  1 
ATOM   2047 H HB3  B LEU   A 1 88  ? 23.063 2.619   13.400  0.58 17.18 ?  88  LEU   A HB3  1 
ATOM   2048 H HG   A LEU   A 1 88  ? 24.508 4.929   13.345  0.42 17.78 ?  88  LEU   A HG   1 
ATOM   2049 H HG   B LEU   A 1 88  ? 24.337 5.137   13.420  0.58 18.27 ?  88  LEU   A HG   1 
ATOM   2050 H HD11 A LEU   A 1 88  ? 23.561 5.230   11.255  0.42 18.05 ?  88  LEU   A HD11 1 
ATOM   2051 H HD11 B LEU   A 1 88  ? 23.204 5.626   11.466  0.58 18.13 ?  88  LEU   A HD11 1 
ATOM   2052 H HD12 A LEU   A 1 88  ? 24.498 3.947   11.225  0.42 18.05 ?  88  LEU   A HD12 1 
ATOM   2053 H HD12 B LEU   A 1 88  ? 24.115 4.344   11.241  0.58 18.13 ?  88  LEU   A HD12 1 
ATOM   2054 H HD13 A LEU   A 1 88  ? 22.922 3.778   11.323  0.42 18.05 ?  88  LEU   A HD13 1 
ATOM   2055 H HD13 B LEU   A 1 88  ? 22.551 4.177   11.466  0.58 18.13 ?  88  LEU   A HD13 1 
ATOM   2056 H HD21 A LEU   A 1 88  ? 22.328 5.803   13.310  0.42 19.55 ?  88  LEU   A HD21 1 
ATOM   2057 H HD21 B LEU   A 1 88  ? 22.121 6.003   13.554  0.58 19.76 ?  88  LEU   A HD21 1 
ATOM   2058 H HD22 A LEU   A 1 88  ? 21.757 4.335   13.514  0.42 19.55 ?  88  LEU   A HD22 1 
ATOM   2059 H HD22 B LEU   A 1 88  ? 21.639 4.529   13.900  0.58 19.76 ?  88  LEU   A HD22 1 
ATOM   2060 H HD23 A LEU   A 1 88  ? 22.616 5.020   14.662  0.42 19.55 ?  88  LEU   A HD23 1 
ATOM   2061 H HD23 B LEU   A 1 88  ? 22.625 5.294   14.884  0.58 19.76 ?  88  LEU   A HD23 1 
ATOM   2062 N N    A ALA   A 1 89  ? 25.773 0.892   15.483  0.42 12.98 ?  89  ALA   A N    1 
ATOM   2063 N N    B ALA   A 1 89  ? 25.611 1.074   15.519  0.58 12.76 ?  89  ALA   A N    1 
ATOM   2064 C CA   A ALA   A 1 89  ? 26.123 -0.518  15.581  0.42 12.33 ?  89  ALA   A CA   1 
ATOM   2065 C CA   B ALA   A 1 89  ? 25.976 -0.331  15.622  0.58 12.44 ?  89  ALA   A CA   1 
ATOM   2066 C C    A ALA   A 1 89  ? 27.607 -0.586  15.897  0.42 12.39 ?  89  ALA   A C    1 
ATOM   2067 C C    B ALA   A 1 89  ? 27.457 -0.364  15.955  0.58 12.82 ?  89  ALA   A C    1 
ATOM   2068 O O    A ALA   A 1 89  ? 28.319 0.416   15.812  0.42 12.71 ?  89  ALA   A O    1 
ATOM   2069 O O    B ALA   A 1 89  ? 28.151 0.646   15.836  0.58 13.86 ?  89  ALA   A O    1 
ATOM   2070 C CB   A ALA   A 1 89  ? 25.830 -1.244  14.267  0.42 12.29 ?  89  ALA   A CB   1 
ATOM   2071 C CB   B ALA   A 1 89  ? 25.729 -1.054  14.299  0.58 12.42 ?  89  ALA   A CB   1 
ATOM   2072 H H    A ALA   A 1 89  ? 26.455 1.412   15.457  0.42 15.60 ?  89  ALA   A H    1 
ATOM   2073 H H    B ALA   A 1 89  ? 26.287 1.603   15.527  0.58 15.34 ?  89  ALA   A H    1 
ATOM   2074 H HA   A ALA   A 1 89  ? 25.622 -0.938  16.299  0.42 14.82 ?  89  ALA   A HA   1 
ATOM   2075 H HA   B ALA   A 1 89  ? 25.469 -0.761  16.332  0.58 14.95 ?  89  ALA   A HA   1 
ATOM   2076 H HB1  A ALA   A 1 89  ? 26.101 -2.171  14.350  0.42 14.78 ?  89  ALA   A HB1  1 
ATOM   2077 H HB1  B ALA   A 1 89  ? 25.982 -1.983  14.397  0.58 14.94 ?  89  ALA   A HB1  1 
ATOM   2078 H HB2  A ALA   A 1 89  ? 24.878 -1.193  14.081  0.42 14.78 ?  89  ALA   A HB2  1 
ATOM   2079 H HB2  B ALA   A 1 89  ? 24.787 -0.987  14.073  0.58 14.94 ?  89  ALA   A HB2  1 
ATOM   2080 H HB3  A ALA   A 1 89  ? 26.329 -0.817  13.553  0.42 14.78 ?  89  ALA   A HB3  1 
ATOM   2081 H HB3  B ALA   A 1 89  ? 26.265 -0.634  13.608  0.58 14.94 ?  89  ALA   A HB3  1 
ATOM   2082 N N    A LYS   A 1 90  ? 28.080 -1.779  16.256  0.42 13.11 ?  90  LYS   A N    1 
ATOM   2083 N N    B LYS   A 1 90  ? 27.950 -1.532  16.359  0.58 12.84 ?  90  LYS   A N    1 
ATOM   2084 C CA   A LYS   A 1 90  ? 29.522 -1.942  16.423  0.42 14.44 ?  90  LYS   A CA   1 
ATOM   2085 C CA   B LYS   A 1 90  ? 29.397 -1.662  16.512  0.58 13.07 ?  90  LYS   A CA   1 
ATOM   2086 C C    A LYS   A 1 90  ? 30.238 -1.793  15.087  0.42 14.28 ?  90  LYS   A C    1 
ATOM   2087 C C    B LYS   A 1 90  ? 30.097 -1.486  15.167  0.58 11.77 ?  90  LYS   A C    1 
ATOM   2088 O O    A LYS   A 1 90  ? 31.233 -1.063  14.980  0.42 15.57 ?  90  LYS   A O    1 
ATOM   2089 O O    B LYS   A 1 90  ? 31.019 -0.666  15.028  0.58 12.01 ?  90  LYS   A O    1 
ATOM   2090 C CB   A LYS   A 1 90  ? 29.851 -3.286  17.070  0.42 16.70 ?  90  LYS   A CB   1 
ATOM   2091 C CB   B LYS   A 1 90  ? 29.750 -3.008  17.144  0.58 15.14 ?  90  LYS   A CB   1 
ATOM   2092 C CG   A LYS   A 1 90  ? 31.332 -3.444  17.392  0.42 20.11 ?  90  LYS   A CG   1 
ATOM   2093 C CG   B LYS   A 1 90  ? 31.228 -3.155  17.469  0.58 18.97 ?  90  LYS   A CG   1 
ATOM   2094 C CD   A LYS   A 1 90  ? 31.579 -4.635  18.303  0.42 22.98 ?  90  LYS   A CD   1 
ATOM   2095 C CD   B LYS   A 1 90  ? 31.486 -4.403  18.304  0.58 22.54 ?  90  LYS   A CD   1 
ATOM   2096 C CE   A LYS   A 1 90  ? 33.006 -4.657  18.835  0.42 25.12 ?  90  LYS   A CE   1 
ATOM   2097 C CE   B LYS   A 1 90  ? 32.878 -4.395  18.920  0.58 25.38 ?  90  LYS   A CE   1 
ATOM   2098 N NZ   A LYS   A 1 90  ? 34.003 -5.045  17.800  0.42 26.56 ?  90  LYS   A NZ   1 
ATOM   2099 N NZ   B LYS   A 1 90  ? 33.957 -4.548  17.908  0.58 27.19 ?  90  LYS   A NZ   1 
ATOM   2100 H H    A LYS   A 1 90  ? 27.606 -2.480  16.409  0.42 15.76 ?  90  LYS   A H    1 
ATOM   2101 H H    B LYS   A 1 90  ? 27.486 -2.228  16.552  0.58 15.44 ?  90  LYS   A H    1 
ATOM   2102 H HA   A LYS   A 1 90  ? 29.847 -1.243  17.006  0.42 17.36 ?  90  LYS   A HA   1 
ATOM   2103 H HA   B LYS   A 1 90  ? 29.711 -0.960  17.103  0.58 15.71 ?  90  LYS   A HA   1 
ATOM   2104 H HB2  A LYS   A 1 90  ? 29.352 -3.364  17.899  0.42 20.07 ?  90  LYS   A HB2  1 
ATOM   2105 H HB2  B LYS   A 1 90  ? 29.250 -3.103  17.971  0.58 18.19 ?  90  LYS   A HB2  1 
ATOM   2106 H HB3  A LYS   A 1 90  ? 29.597 -3.999  16.463  0.42 20.07 ?  90  LYS   A HB3  1 
ATOM   2107 H HB3  B LYS   A 1 90  ? 29.505 -3.714  16.528  0.58 18.19 ?  90  LYS   A HB3  1 
ATOM   2108 H HG2  A LYS   A 1 90  ? 31.827 -3.580  16.568  0.42 24.16 ?  90  LYS   A HG2  1 
ATOM   2109 H HG2  B LYS   A 1 90  ? 31.733 -3.231  16.644  0.58 22.79 ?  90  LYS   A HG2  1 
ATOM   2110 H HG3  A LYS   A 1 90  ? 31.648 -2.644  17.842  0.42 24.16 ?  90  LYS   A HG3  1 
ATOM   2111 H HG3  B LYS   A 1 90  ? 31.526 -2.384  17.976  0.58 22.79 ?  90  LYS   A HG3  1 
ATOM   2112 H HD2  A LYS   A 1 90  ? 30.974 -4.587  19.060  0.42 27.60 ?  90  LYS   A HD2  1 
ATOM   2113 H HD2  B LYS   A 1 90  ? 30.837 -4.449  19.025  0.58 27.07 ?  90  LYS   A HD2  1 
ATOM   2114 H HD3  A LYS   A 1 90  ? 31.429 -5.453  17.805  0.42 27.60 ?  90  LYS   A HD3  1 
ATOM   2115 H HD3  B LYS   A 1 90  ? 31.411 -5.190  17.739  0.58 27.07 ?  90  LYS   A HD3  1 
ATOM   2116 H HE2  A LYS   A 1 90  ? 33.238 -3.770  19.157  0.42 30.17 ?  90  LYS   A HE2  1 
ATOM   2117 H HE2  B LYS   A 1 90  ? 33.017 -3.551  19.378  0.58 30.49 ?  90  LYS   A HE2  1 
ATOM   2118 H HE3  A LYS   A 1 90  ? 33.063 -5.297  19.561  0.42 30.17 ?  90  LYS   A HE3  1 
ATOM   2119 H HE3  B LYS   A 1 90  ? 32.953 -5.129  19.551  0.58 30.49 ?  90  LYS   A HE3  1 
ATOM   2120 H HZ1  A LYS   A 1 90  ? 34.815 -5.089  18.162  0.42 31.90 ?  90  LYS   A HZ1  1 
ATOM   2121 H HZ1  B LYS   A 1 90  ? 34.753 -4.542  18.307  0.58 32.66 ?  90  LYS   A HZ1  1 
ATOM   2122 H HZ2  A LYS   A 1 90  ? 33.793 -5.839  17.460  0.42 31.90 ?  90  LYS   A HZ2  1 
ATOM   2123 H HZ2  B LYS   A 1 90  ? 33.859 -5.321  17.475  0.58 32.66 ?  90  LYS   A HZ2  1 
ATOM   2124 H HZ3  A LYS   A 1 90  ? 34.011 -4.441  17.146  0.42 31.90 ?  90  LYS   A HZ3  1 
ATOM   2125 H HZ3  B LYS   A 1 90  ? 33.922 -3.882  17.321  0.58 32.66 ?  90  LYS   A HZ3  1 
ATOM   2126 N N    A HIS   A 1 91  ? 29.733 -2.465  14.054  0.42 13.24 ?  91  HIS   A N    1 
ATOM   2127 N N    B HIS   A 1 91  ? 29.642 -2.230  14.157  0.58 10.53 ?  91  HIS   A N    1 
ATOM   2128 C CA   A HIS   A 1 91  ? 30.314 -2.421  12.724  0.42 12.77 ?  91  HIS   A CA   1 
ATOM   2129 C CA   B HIS   A 1 91  ? 30.231 -2.227  12.831  0.58 10.47 ?  91  HIS   A CA   1 
ATOM   2130 C C    A HIS   A 1 91  ? 29.221 -2.164  11.704  0.42 11.16 ?  91  HIS   A C    1 
ATOM   2131 C C    B HIS   A 1 91  ? 29.154 -1.980  11.787  0.58 10.09 ?  91  HIS   A C    1 
ATOM   2132 O O    A HIS   A 1 91  ? 28.080 -2.609  11.863  0.42 10.33 ?  91  HIS   A O    1 
ATOM   2133 O O    B HIS   A 1 91  ? 27.974 -2.287  11.990  0.58 10.39 ?  91  HIS   A O    1 
ATOM   2134 C CB   A HIS   A 1 91  ? 30.965 -3.755  12.354  0.42 14.71 ?  91  HIS   A CB   1 
ATOM   2135 C CB   B HIS   A 1 91  ? 30.860 -3.581  12.497  0.58 12.59 ?  91  HIS   A CB   1 
ATOM   2136 C CG   A HIS   A 1 91  ? 31.931 -4.262  13.375  0.42 17.37 ?  91  HIS   A CG   1 
ATOM   2137 C CG   B HIS   A 1 91  ? 31.828 -4.068  13.522  0.58 16.20 ?  91  HIS   A CG   1 
ATOM   2138 N ND1  A HIS   A 1 91  ? 33.194 -3.733  13.531  0.42 18.78 ?  91  HIS   A ND1  1 
ATOM   2139 N ND1  B HIS   A 1 91  ? 33.096 -3.546  13.653  0.58 18.33 ?  91  HIS   A ND1  1 
ATOM   2140 C CD2  A HIS   A 1 91  ? 31.825 -5.257  14.287  0.42 18.64 ?  91  HIS   A CD2  1 
ATOM   2141 C CD2  B HIS   A 1 91  ? 31.722 -5.038  14.461  0.58 18.12 ?  91  HIS   A CD2  1 
ATOM   2142 C CE1  A HIS   A 1 91  ? 33.822 -4.377  14.499  0.42 19.33 ?  91  HIS   A CE1  1 
ATOM   2143 C CE1  B HIS   A 1 91  ? 33.729 -4.171  14.630  0.58 19.17 ?  91  HIS   A CE1  1 
ATOM   2144 N NE2  A HIS   A 1 91  ? 33.014 -5.307  14.974  0.42 19.56 ?  91  HIS   A NE2  1 
ATOM   2145 N NE2  B HIS   A 1 91  ? 32.917 -5.081  15.137  0.58 19.48 ?  91  HIS   A NE2  1 
ATOM   2146 H H    A HIS   A 1 91  ? 29.028 -2.967  14.101  0.42 15.92 ?  91  HIS   A H    1 
ATOM   2147 H H    B HIS   A 1 91  ? 28.957 -2.760  14.226  0.58 12.66 ?  91  HIS   A H    1 
ATOM   2148 H HA   A HIS   A 1 91  ? 30.973 -1.716  12.665  0.42 15.35 ?  91  HIS   A HA   1 
ATOM   2149 H HA   B HIS   A 1 91  ? 30.901 -1.531  12.771  0.58 12.59 ?  91  HIS   A HA   1 
ATOM   2150 H HB2  A HIS   A 1 91  ? 30.271 -4.423  12.246  0.42 17.68 ?  91  HIS   A HB2  1 
ATOM   2151 H HB2  B HIS   A 1 91  ? 30.154 -4.241  12.420  0.58 15.14 ?  91  HIS   A HB2  1 
ATOM   2152 H HB3  A HIS   A 1 91  ? 31.446 -3.644  11.518  0.42 17.68 ?  91  HIS   A HB3  1 
ATOM   2153 H HB3  B HIS   A 1 91  ? 31.330 -3.501  11.654  0.58 15.14 ?  91  HIS   A HB3  1 
ATOM   2154 H HD1  A HIS   A 1 91  ? 33.520 -3.082  13.070  0.42 22.56 ?  91  HIS   A HD1  1 
ATOM   2155 H HD1  B HIS   A 1 91  ? 33.426 -2.911  13.171  0.58 22.02 ?  91  HIS   A HD1  1 
ATOM   2156 H HD2  A HIS   A 1 91  ? 31.085 -5.799  14.426  0.42 22.39 ?  91  HIS   A HD2  1 
ATOM   2157 H HD2  B HIS   A 1 91  ? 30.982 -5.574  14.617  0.58 21.77 ?  91  HIS   A HD2  1 
ATOM   2158 H HE1  A HIS   A 1 91  ? 34.688 -4.199  14.794  0.42 23.23 ?  91  HIS   A HE1  1 
ATOM   2159 H HE1  B HIS   A 1 91  ? 34.601 -3.999  14.910  0.58 23.04 ?  91  HIS   A HE1  1 
ATOM   2160 N N    . CYS   A 1 92  ? 29.585 -1.459  10.640  1.00 10.37 ?  92  CYS   A N    1 
ATOM   2161 C CA   . CYS   A 1 92  ? 28.757 -1.378  9.448   1.00 9.97  ?  92  CYS   A CA   1 
ATOM   2162 C C    . CYS   A 1 92  ? 29.416 -2.200  8.351   1.00 9.53  ?  92  CYS   A C    1 
ATOM   2163 O O    . CYS   A 1 92  ? 30.574 -1.952  7.984   1.00 10.60 ?  92  CYS   A O    1 
ATOM   2164 C CB   . CYS   A 1 92  ? 28.527 0.059   8.986   1.00 10.51 ?  92  CYS   A CB   1 
ATOM   2165 S SG   . CYS   A 1 92  ? 27.528 0.142   7.466   1.00 10.08 ?  92  CYS   A SG   1 
ATOM   2166 H H    A CYS   A 1 92  ? 30.319 -1.018  10.585  0.42 12.48 ?  92  CYS   A H    1 
ATOM   2167 H H    B CYS   A 1 92  ? 30.380 -1.155  10.524  0.58 12.48 ?  92  CYS   A H    1 
ATOM   2168 H HA   . CYS   A 1 92  ? 27.891 -1.768  9.638   1.00 11.99 ?  92  CYS   A HA   1 
ATOM   2169 H HB2  . CYS   A 1 92  ? 28.055 0.548   9.681   1.00 12.64 ?  92  CYS   A HB2  1 
ATOM   2170 H HB3  . CYS   A 1 92  ? 29.381 0.479   8.805   1.00 12.64 ?  92  CYS   A HB3  1 
ATOM   2171 H HG   . CYS   A 1 92  ? 27.375 1.292   7.167   1.00 12.12 ?  92  CYS   A HG   1 
ATOM   2172 N N    . LEU   A 1 93  ? 28.686 -3.191  7.847   1.00 9.38  ?  93  LEU   A N    1 
ATOM   2173 C CA   . LEU   A 1 93  ? 29.107 -3.956  6.680   1.00 9.34  ?  93  LEU   A CA   1 
ATOM   2174 C C    . LEU   A 1 93  ? 28.512 -3.275  5.451   1.00 9.00  ?  93  LEU   A C    1 
ATOM   2175 O O    . LEU   A 1 93  ? 27.298 -3.343  5.219   1.00 9.03  ?  93  LEU   A O    1 
ATOM   2176 C CB   . LEU   A 1 93  ? 28.642 -5.408  6.791   1.00 9.71  ?  93  LEU   A CB   1 
ATOM   2177 C CG   . LEU   A 1 93  ? 29.043 -6.306  5.624   1.00 9.92  ?  93  LEU   A CG   1 
ATOM   2178 C CD1  . LEU   A 1 93  ? 30.553 -6.537  5.627   1.00 11.16 ?  93  LEU   A CD1  1 
ATOM   2179 C CD2  . LEU   A 1 93  ? 28.293 -7.642  5.667   1.00 10.62 ?  93  LEU   A CD2  1 
ATOM   2180 H H    . LEU   A 1 93  ? 27.924 -3.438  8.174   1.00 11.28 ?  93  LEU   A H    1 
ATOM   2181 H HA   . LEU   A 1 93  ? 30.071 -3.934  6.617   1.00 11.24 ?  93  LEU   A HA   1 
ATOM   2182 H HB2  . LEU   A 1 93  ? 29.020 -5.789  7.601   1.00 11.68 ?  93  LEU   A HB2  1 
ATOM   2183 H HB3  . LEU   A 1 93  ? 27.676 -5.419  6.848   1.00 11.68 ?  93  LEU   A HB3  1 
ATOM   2184 H HG   . LEU   A 1 93  ? 28.822 -5.866  4.793   1.00 11.93 ?  93  LEU   A HG   1 
ATOM   2185 H HD11 . LEU   A 1 93  ? 30.786 -7.156  4.920   1.00 13.42 ?  93  LEU   A HD11 1 
ATOM   2186 H HD12 . LEU   A 1 93  ? 31.008 -5.689  5.486   1.00 13.42 ?  93  LEU   A HD12 1 
ATOM   2187 H HD13 . LEU   A 1 93  ? 30.819 -6.907  6.489   1.00 13.42 ?  93  LEU   A HD13 1 
ATOM   2188 H HD21 . LEU   A 1 93  ? 28.580 -8.189  4.915   1.00 12.78 ?  93  LEU   A HD21 1 
ATOM   2189 H HD22 . LEU   A 1 93  ? 28.506 -8.099  6.499   1.00 12.78 ?  93  LEU   A HD22 1 
ATOM   2190 H HD23 . LEU   A 1 93  ? 27.345 -7.474  5.612   1.00 12.78 ?  93  LEU   A HD23 1 
ATOM   2191 N N    . HIS   A 1 94  ? 29.357 -2.578  4.693   1.00 8.84  ?  94  HIS   A N    1 
ATOM   2192 C CA   . HIS   A 1 94  ? 28.938 -1.920  3.460   1.00 8.78  ?  94  HIS   A CA   1 
ATOM   2193 C C    . HIS   A 1 94  ? 28.968 -2.955  2.347   1.00 8.90  ?  94  HIS   A C    1 
ATOM   2194 O O    . HIS   A 1 94  ? 30.043 -3.472  2.021   1.00 10.38 ?  94  HIS   A O    1 
ATOM   2195 C CB   . HIS   A 1 94  ? 29.885 -0.766  3.131   1.00 9.27  ?  94  HIS   A CB   1 
ATOM   2196 C CG   . HIS   A 1 94  ? 29.859 0.330   4.139   1.00 8.95  ?  94  HIS   A CG   1 
ATOM   2197 N ND1  . HIS   A 1 94  ? 28.976 1.387   4.072   1.00 9.29  ?  94  HIS   A ND1  1 
ATOM   2198 C CD2  . HIS   A 1 94  ? 30.593 0.510   5.261   1.00 9.87  ?  94  HIS   A CD2  1 
ATOM   2199 C CE1  . HIS   A 1 94  ? 29.178 2.174   5.112   1.00 9.43  ?  94  HIS   A CE1  1 
ATOM   2200 N NE2  . HIS   A 1 94  ? 30.152 1.665   5.847   1.00 9.83  ?  94  HIS   A NE2  1 
ATOM   2201 H H    . HIS   A 1 94  ? 30.188 -2.475  4.876   1.00 10.63 ?  94  HIS   A H    1 
ATOM   2202 H HA   . HIS   A 1 94  ? 28.036 -1.577  3.551   1.00 10.56 ?  94  HIS   A HA   1 
ATOM   2203 H HB2  . HIS   A 1 94  ? 30.791 -1.109  3.085   1.00 11.15 ?  94  HIS   A HB2  1 
ATOM   2204 H HB3  . HIS   A 1 94  ? 29.631 -0.388  2.274   1.00 11.15 ?  94  HIS   A HB3  1 
ATOM   2205 H HD2  . HIS   A 1 94  ? 31.271 -0.039  5.577   1.00 11.87 ?  94  HIS   A HD2  1 
ATOM   2206 H HE1  . HIS   A 1 94  ? 28.711 2.961   5.287   1.00 11.34 ?  94  HIS   A HE1  1 
ATOM   2207 H HE2  . HIS   A 1 94  ? 30.462 2.020   6.568   1.00 11.83 ?  94  HIS   A HE2  1 
ATOM   2208 N N    . VAL   A 1 95  ? 27.808 -3.280  1.779   1.00 8.69  ?  95  VAL   A N    1 
ATOM   2209 C CA   . VAL   A 1 95  ? 27.686 -4.327  0.770   1.00 8.83  ?  95  VAL   A CA   1 
ATOM   2210 C C    . VAL   A 1 95  ? 27.150 -3.707  -0.509  1.00 8.64  ?  95  VAL   A C    1 
ATOM   2211 O O    . VAL   A 1 95  ? 26.136 -2.998  -0.474  1.00 9.66  ?  95  VAL   A O    1 
ATOM   2212 C CB   . VAL   A 1 95  ? 26.759 -5.472  1.228   1.00 9.34  ?  95  VAL   A CB   1 
ATOM   2213 C CG1  . VAL   A 1 95  ? 26.670 -6.525  0.134   1.00 10.35 ?  95  VAL   A CG1  1 
ATOM   2214 C CG2  . VAL   A 1 95  ? 27.242 -6.066  2.536   1.00 9.58  ?  95  VAL   A CG2  1 
ATOM   2215 H H    . VAL   A 1 95  ? 27.057 -2.900  1.971   1.00 10.45 ?  95  VAL   A H    1 
ATOM   2216 H HA   . VAL   A 1 95  ? 28.564 -4.701  0.586   1.00 10.62 ?  95  VAL   A HA   1 
ATOM   2217 H HB   . VAL   A 1 95  ? 25.872 -5.114  1.374   1.00 11.24 ?  95  VAL   A HB   1 
ATOM   2218 H HG11 . VAL   A 1 95  ? 26.278 -7.336  0.509   1.00 12.45 ?  95  VAL   A HG11 1 
ATOM   2219 H HG12 . VAL   A 1 95  ? 26.104 -6.199  -0.584  1.00 12.45 ?  95  VAL   A HG12 1 
ATOM   2220 H HG13 . VAL   A 1 95  ? 27.557 -6.720  -0.202  1.00 12.45 ?  95  VAL   A HG13 1 
ATOM   2221 H HG21 . VAL   A 1 95  ? 26.676 -6.821  2.761   1.00 11.52 ?  95  VAL   A HG21 1 
ATOM   2222 H HG22 . VAL   A 1 95  ? 28.159 -6.359  2.426   1.00 11.52 ?  95  VAL   A HG22 1 
ATOM   2223 H HG23 . VAL   A 1 95  ? 27.187 -5.390  3.226   1.00 11.52 ?  95  VAL   A HG23 1 
ATOM   2224 N N    . VAL   A 1 96  ? 27.789 -4.013  -1.638  1.00 8.99  ?  96  VAL   A N    1 
ATOM   2225 C CA   . VAL   A 1 96  ? 27.385 -3.474  -2.932  1.00 9.67  ?  96  VAL   A CA   1 
ATOM   2226 C C    . VAL   A 1 96  ? 26.610 -4.536  -3.709  1.00 9.88  ?  96  VAL   A C    1 
ATOM   2227 O O    . VAL   A 1 96  ? 27.189 -5.485  -4.246  1.00 10.63 ?  96  VAL   A O    1 
ATOM   2228 C CB   . VAL   A 1 96  ? 28.585 -2.985  -3.746  1.00 10.13 ?  96  VAL   A CB   1 
ATOM   2229 C CG1  . VAL   A 1 96  ? 28.099 -2.359  -5.033  1.00 10.24 ?  96  VAL   A CG1  1 
ATOM   2230 C CG2  . VAL   A 1 96  ? 29.427 -1.998  -2.943  1.00 10.62 ?  96  VAL   A CG2  1 
ATOM   2231 H H    . VAL   A 1 96  ? 28.484 -4.523  -1.675  1.00 10.82 ?  96  VAL   A H    1 
ATOM   2232 H HA   . VAL   A 1 96  ? 26.796 -2.718  -2.788  1.00 11.63 ?  96  VAL   A HA   1 
ATOM   2233 H HB   . VAL   A 1 96  ? 29.146 -3.737  -3.970  1.00 12.19 ?  96  VAL   A HB   1 
ATOM   2234 H HG11 . VAL   A 1 96  ? 28.837 -1.876  -5.444  1.00 12.32 ?  96  VAL   A HG11 1 
ATOM   2235 H HG12 . VAL   A 1 96  ? 27.793 -3.057  -5.629  1.00 12.32 ?  96  VAL   A HG12 1 
ATOM   2236 H HG13 . VAL   A 1 96  ? 27.377 -1.744  -4.835  1.00 12.32 ?  96  VAL   A HG13 1 
ATOM   2237 H HG21 . VAL   A 1 96  ? 30.133 -1.647  -3.506  1.00 12.78 ?  96  VAL   A HG21 1 
ATOM   2238 H HG22 . VAL   A 1 96  ? 28.860 -1.271  -2.633  1.00 12.78 ?  96  VAL   A HG22 1 
ATOM   2239 H HG23 . VAL   A 1 96  ? 29.814 -2.458  -2.179  1.00 12.78 ?  96  VAL   A HG23 1 
ATOM   2240 N N    A GLY   A 1 97  ? 25.288 -4.394  -3.721  0.42 10.02 ?  97  GLY   A N    1 
ATOM   2241 N N    B GLY   A 1 97  ? 25.293 -4.377  -3.817  0.58 9.81  ?  97  GLY   A N    1 
ATOM   2242 C CA   A GLY   A 1 97  ? 24.452 -5.147  -4.615  0.42 10.61 ?  97  GLY   A CA   1 
ATOM   2243 C CA   B GLY   A 1 97  ? 24.529 -5.170  -4.752  0.58 10.24 ?  97  GLY   A CA   1 
ATOM   2244 C C    A GLY   A 1 97  ? 24.408 -4.471  -5.968  0.42 10.87 ?  97  GLY   A C    1 
ATOM   2245 C C    B GLY   A 1 97  ? 24.632 -4.595  -6.154  0.58 10.34 ?  97  GLY   A C    1 
ATOM   2246 O O    A GLY   A 1 97  ? 24.644 -3.265  -6.093  0.42 11.21 ?  97  GLY   A O    1 
ATOM   2247 O O    B GLY   A 1 97  ? 24.979 -3.423  -6.337  0.58 10.90 ?  97  GLY   A O    1 
ATOM   2248 H H    A GLY   A 1 97  ? 24.853 -3.850  -3.212  0.42 12.05 ?  97  GLY   A H    1 
ATOM   2249 H H    B GLY   A 1 97  ? 24.824 -3.815  -3.360  0.58 11.79 ?  97  GLY   A H    1 
ATOM   2250 H HA2  A GLY   A 1 97  ? 24.811 -6.039  -4.718  0.42 12.75 ?  97  GLY   A HA2  1 
ATOM   2251 H HA2  B GLY   A 1 97  ? 24.866 -6.081  -4.753  0.58 12.31 ?  97  GLY   A HA2  1 
ATOM   2252 H HA3  A GLY   A 1 97  ? 23.551 -5.207  -4.257  0.42 12.75 ?  97  GLY   A HA3  1 
ATOM   2253 H HA3  B GLY   A 1 97  ? 23.596 -5.186  -4.488  0.58 12.31 ?  97  GLY   A HA3  1 
ATOM   2254 N N    A PRO   A 1 98  ? 24.107 -5.234  -7.013  0.42 10.51 ?  98  PRO   A N    1 
ATOM   2255 N N    B PRO   A 1 98  ? 24.333 -5.401  -7.174  0.58 10.83 ?  98  PRO   A N    1 
ATOM   2256 C CA   A PRO   A 1 98  ? 24.016 -4.637  -8.350  0.42 10.87 ?  98  PRO   A CA   1 
ATOM   2257 C CA   B PRO   A 1 98  ? 24.318 -4.871  -8.543  0.58 11.48 ?  98  PRO   A CA   1 
ATOM   2258 C C    A PRO   A 1 98  ? 22.916 -3.591  -8.404  0.42 10.85 ?  98  PRO   A C    1 
ATOM   2259 C C    B PRO   A 1 98  ? 23.215 -3.841  -8.737  0.58 11.60 ?  98  PRO   A C    1 
ATOM   2260 O O    A PRO   A 1 98  ? 21.852 -3.749  -7.800  0.42 10.76 ?  98  PRO   A O    1 
ATOM   2261 O O    B PRO   A 1 98  ? 22.109 -3.970  -8.205  0.58 12.25 ?  98  PRO   A O    1 
ATOM   2262 C CB   A PRO   A 1 98  ? 23.691 -5.837  -9.248  0.42 10.99 ?  98  PRO   A CB   1 
ATOM   2263 C CB   B PRO   A 1 98  ? 24.066 -6.117  -9.404  0.58 11.80 ?  98  PRO   A CB   1 
ATOM   2264 C CG   A PRO   A 1 98  ? 23.038 -6.831  -8.331  0.42 10.49 ?  98  PRO   A CG   1 
ATOM   2265 C CG   B PRO   A 1 98  ? 23.424 -7.100  -8.480  0.58 12.34 ?  98  PRO   A CG   1 
ATOM   2266 C CD   A PRO   A 1 98  ? 23.747 -6.662  -7.014  0.42 10.09 ?  98  PRO   A CD   1 
ATOM   2267 C CD   B PRO   A 1 98  ? 24.075 -6.852  -7.149  0.58 11.55 ?  98  PRO   A CD   1 
ATOM   2268 H HA   A PRO   A 1 98  ? 24.861 -4.246  -8.610  0.42 13.07 ?  98  PRO   A HA   1 
ATOM   2269 H HA   B PRO   A 1 98  ? 25.180 -4.490  -8.771  0.58 13.80 ?  98  PRO   A HA   1 
ATOM   2270 H HB2  A PRO   A 1 98  ? 23.079 -5.566  -9.950  0.42 13.22 ?  98  PRO   A HB2  1 
ATOM   2271 H HB2  B PRO   A 1 98  ? 23.467 -5.894  -10.135 0.58 14.19 ?  98  PRO   A HB2  1 
ATOM   2272 H HB3  A PRO   A 1 98  ? 24.509 -6.197  -9.621  0.42 13.22 ?  98  PRO   A HB3  1 
ATOM   2273 H HB3  B PRO   A 1 98  ? 24.907 -6.463  -9.742  0.58 14.19 ?  98  PRO   A HB3  1 
ATOM   2274 H HG2  A PRO   A 1 98  ? 22.095 -6.631  -8.237  0.42 12.61 ?  98  PRO   A HG2  1 
ATOM   2275 H HG2  B PRO   A 1 98  ? 22.469 -6.931  -8.428  0.58 14.84 ?  98  PRO   A HG2  1 
ATOM   2276 H HG3  A PRO   A 1 98  ? 23.167 -7.731  -8.671  0.42 12.61 ?  98  PRO   A HG3  1 
ATOM   2277 H HG3  B PRO   A 1 98  ? 23.596 -8.005  -8.787  0.58 14.84 ?  98  PRO   A HG3  1 
ATOM   2278 H HD2  A PRO   A 1 98  ? 23.149 -6.868  -6.274  0.42 12.13 ?  98  PRO   A HD2  1 
ATOM   2279 H HD2  B PRO   A 1 98  ? 23.474 -7.086  -6.426  0.58 13.89 ?  98  PRO   A HD2  1 
ATOM   2280 H HD3  A PRO   A 1 98  ? 24.550 -7.207  -6.981  0.42 12.13 ?  98  PRO   A HD3  1 
ATOM   2281 H HD3  B PRO   A 1 98  ? 24.913 -7.349  -7.087  0.58 13.89 ?  98  PRO   A HD3  1 
ATOM   2282 N N    A ASN   A 1 99  ? 23.185 -2.510  -9.133  0.42 11.98 ?  99  ASN   A N    1 
ATOM   2283 N N    B ASN   A 1 99  ? 23.531 -2.815  -9.522  0.58 12.29 ?  99  ASN   A N    1 
ATOM   2284 C CA   A ASN   A 1 99  ? 22.206 -1.455  -9.370  0.42 14.08 ?  99  ASN   A CA   1 
ATOM   2285 C CA   B ASN   A 1 99  ? 22.587 -1.764  -9.890  0.58 13.57 ?  99  ASN   A CA   1 
ATOM   2286 C C    A ASN   A 1 99  ? 21.629 -1.668  -10.765 0.42 15.87 ?  99  ASN   A C    1 
ATOM   2287 C C    B ASN   A 1 99  ? 22.087 -2.094  -11.292 0.58 14.01 ?  99  ASN   A C    1 
ATOM   2288 O O    A ASN   A 1 99  ? 22.317 -1.455  -11.770 0.42 16.45 ?  99  ASN   A O    1 
ATOM   2289 O O    B ASN   A 1 99  ? 22.792 -1.881  -12.281 0.58 13.74 ?  99  ASN   A O    1 
ATOM   2290 C CB   A ASN   A 1 99  ? 22.847 -0.073  -9.243  0.42 15.19 ?  99  ASN   A CB   1 
ATOM   2291 C CB   B ASN   A 1 99  ? 23.281 -0.408  -9.854  0.58 15.06 ?  99  ASN   A CB   1 
ATOM   2292 C CG   A ASN   A 1 99  ? 21.814 1.053   -9.149  0.42 16.71 ?  99  ASN   A CG   1 
ATOM   2293 C CG   B ASN   A 1 99  ? 22.334 0.738   -10.104 0.58 15.94 ?  99  ASN   A CG   1 
ATOM   2294 O OD1  A ASN   A 1 99  ? 20.759 1.006   -9.783  0.42 17.36 ?  99  ASN   A OD1  1 
ATOM   2295 O OD1  B ASN   A 1 99  ? 21.325 0.583   -10.785 0.58 16.10 ?  99  ASN   A OD1  1 
ATOM   2296 N ND2  A ASN   A 1 99  ? 22.123 2.069   -8.349  0.42 17.24 ?  99  ASN   A ND2  1 
ATOM   2297 N ND2  B ASN   A 1 99  ? 22.656 1.902   -9.552  0.58 17.32 ?  99  ASN   A ND2  1 
ATOM   2298 H H    A ASN   A 1 99  ? 23.946 -2.361  -9.506  0.42 14.41 ?  99  ASN   A H    1 
ATOM   2299 H H    B ASN   A 1 99  ? 24.318 -2.708  -9.860  0.58 14.77 ?  99  ASN   A H    1 
ATOM   2300 H HA   A ASN   A 1 99  ? 21.487 -1.524  -8.724  0.42 16.92 ?  99  ASN   A HA   1 
ATOM   2301 H HA   B ASN   A 1 99  ? 21.837 -1.766  -9.277  0.58 16.32 ?  99  ASN   A HA   1 
ATOM   2302 H HB2  A ASN   A 1 99  ? 23.392 -0.051  -8.442  0.42 18.26 ?  99  ASN   A HB2  1 
ATOM   2303 H HB2  B ASN   A 1 99  ? 23.690 -0.285  -8.985  0.58 18.11 ?  99  ASN   A HB2  1 
ATOM   2304 H HB3  A ASN   A 1 99  ? 23.399 0.091   -10.025 0.42 18.26 ?  99  ASN   A HB3  1 
ATOM   2305 H HB3  B ASN   A 1 99  ? 23.953 -0.398  -10.548 0.58 18.11 ?  99  ASN   A HB3  1 
ATOM   2306 H HD21 A ASN   A 1 99  ? 21.577 2.725   -8.257  0.42 20.72 ?  99  ASN   A HD21 1 
ATOM   2307 H HD21 B ASN   A 1 99  ? 22.155 2.588   -9.655  0.58 20.81 ?  99  ASN   A HD21 1 
ATOM   2308 H HD22 A ASN   A 1 99  ? 22.869 2.066   -7.917  0.42 20.72 ?  99  ASN   A HD22 1 
ATOM   2309 H HD22 B ASN   A 1 99  ? 23.373 1.963   -9.089  0.58 20.81 ?  99  ASN   A HD22 1 
ATOM   2310 N N    A VAL   A 1 100 ? 20.370 -2.108  -10.821 0.42 17.06 ?  100 VAL   A N    1 
ATOM   2311 N N    B VAL   A 1 100 ? 20.866 -2.627  -11.375 0.58 16.12 ?  100 VAL   A N    1 
ATOM   2312 C CA   A VAL   A 1 100 ? 19.715 -2.344  -12.105 0.42 18.91 ?  100 VAL   A CA   1 
ATOM   2313 C CA   B VAL   A 1 100 ? 20.338 -3.059  -12.664 0.58 18.78 ?  100 VAL   A CA   1 
ATOM   2314 C C    A VAL   A 1 100 ? 19.634 -1.058  -12.916 0.42 20.06 ?  100 VAL   A C    1 
ATOM   2315 C C    B VAL   A 1 100 ? 20.070 -1.880  -13.589 0.58 20.14 ?  100 VAL   A C    1 
ATOM   2316 O O    A VAL   A 1 100 ? 19.720 -1.086  -14.151 0.42 20.59 ?  100 VAL   A O    1 
ATOM   2317 O O    B VAL   A 1 100 ? 20.065 -2.046  -14.814 0.58 20.58 ?  100 VAL   A O    1 
ATOM   2318 C CB   A VAL   A 1 100 ? 18.331 -2.995  -11.887 0.42 19.92 ?  100 VAL   A CB   1 
ATOM   2319 C CB   B VAL   A 1 100 ? 19.088 -3.935  -12.457 0.58 20.70 ?  100 VAL   A CB   1 
ATOM   2320 C CG1  A VAL   A 1 100 ? 17.614 -3.210  -13.212 0.42 20.38 ?  100 VAL   A CG1  1 
ATOM   2321 C CG1  B VAL   A 1 100 ? 18.369 -4.189  -13.778 0.58 21.65 ?  100 VAL   A CG1  1 
ATOM   2322 C CG2  A VAL   A 1 100 ? 18.482 -4.317  -11.144 0.42 20.23 ?  100 VAL   A CG2  1 
ATOM   2323 C CG2  B VAL   A 1 100 ? 19.480 -5.250  -11.809 0.58 21.33 ?  100 VAL   A CG2  1 
ATOM   2324 H H    A VAL   A 1 100 ? 19.880 -2.279  -10.136 0.42 20.50 ?  100 VAL   A H    1 
ATOM   2325 H H    B VAL   A 1 100 ? 20.333 -2.745  -10.712 0.58 19.37 ?  100 VAL   A H    1 
ATOM   2326 H HA   A VAL   A 1 100 ? 20.246 -2.969  -12.615 0.42 22.71 ?  100 VAL   A HA   1 
ATOM   2327 H HA   B VAL   A 1 100 ? 21.006 -3.623  -13.091 0.58 22.56 ?  100 VAL   A HA   1 
ATOM   2328 H HB   A VAL   A 1 100 ? 17.782 -2.410  -11.342 0.42 23.93 ?  100 VAL   A HB   1 
ATOM   2329 H HB   B VAL   A 1 100 ? 18.472 -3.477  -11.866 0.58 24.87 ?  100 VAL   A HB   1 
ATOM   2330 H HG11 A VAL   A 1 100 ? 16.837 -3.775  -13.064 0.42 24.48 ?  100 VAL   A HG11 1 
ATOM   2331 H HG11 B VAL   A 1 100 ? 17.712 -4.893  -13.647 0.58 26.00 ?  100 VAL   A HG11 1 
ATOM   2332 H HG12 A VAL   A 1 100 ? 17.331 -2.352  -13.564 0.42 24.48 ?  100 VAL   A HG12 1 
ATOM   2333 H HG12 B VAL   A 1 100 ? 17.923 -3.375  -14.061 0.58 26.00 ?  100 VAL   A HG12 1 
ATOM   2334 H HG13 A VAL   A 1 100 ? 18.220 -3.642  -13.833 0.42 24.48 ?  100 VAL   A HG13 1 
ATOM   2335 H HG13 B VAL   A 1 100 ? 19.016 -4.465  -14.444 0.58 26.00 ?  100 VAL   A HG13 1 
ATOM   2336 H HG21 A VAL   A 1 100 ? 17.615 -4.748  -11.084 0.42 24.30 ?  100 VAL   A HG21 1 
ATOM   2337 H HG21 B VAL   A 1 100 ? 18.684 -5.794  -11.692 0.58 25.62 ?  100 VAL   A HG21 1 
ATOM   2338 H HG22 A VAL   A 1 100 ? 19.100 -4.883  -11.633 0.42 24.30 ?  100 VAL   A HG22 1 
ATOM   2339 H HG22 B VAL   A 1 100 ? 20.112 -5.710  -12.384 0.58 25.62 ?  100 VAL   A HG22 1 
ATOM   2340 H HG23 A VAL   A 1 100 ? 18.827 -4.142  -10.254 0.42 24.30 ?  100 VAL   A HG23 1 
ATOM   2341 H HG23 B VAL   A 1 100 ? 19.886 -5.068  -10.949 0.58 25.62 ?  100 VAL   A HG23 1 
ATOM   2342 N N    A ASN   A 1 101 ? 19.477 0.087   -12.246 0.42 20.93 ?  101 ASN   A N    1 
ATOM   2343 N N    B ASN   A 1 101 ? 19.838 -0.690  -13.044 0.58 21.10 ?  101 ASN   A N    1 
ATOM   2344 C CA   A ASN   A 1 101 ? 19.397 1.368   -12.941 0.42 22.30 ?  101 ASN   A CA   1 
ATOM   2345 C CA   B ASN   A 1 101 ? 19.704 0.483   -13.896 0.58 22.51 ?  101 ASN   A CA   1 
ATOM   2346 C C    A ASN   A 1 101 ? 20.732 1.806   -13.526 0.42 23.99 ?  101 ASN   A C    1 
ATOM   2347 C C    B ASN   A 1 101 ? 21.042 0.974   -14.432 0.58 22.30 ?  101 ASN   A C    1 
ATOM   2348 O O    A ASN   A 1 101 ? 20.771 2.798   -14.262 0.42 24.65 ?  101 ASN   A O    1 
ATOM   2349 O O    B ASN   A 1 101 ? 21.053 1.849   -15.304 0.58 22.15 ?  101 ASN   A O    1 
ATOM   2350 C CB   A ASN   A 1 101 ? 18.852 2.438   -11.996 0.42 21.94 ?  101 ASN   A CB   1 
ATOM   2351 C CB   B ASN   A 1 101 ? 18.942 1.587   -13.163 0.58 24.76 ?  101 ASN   A CB   1 
ATOM   2352 C CG   A ASN   A 1 101 ? 17.530 2.039   -11.380 0.42 21.45 ?  101 ASN   A CG   1 
ATOM   2353 C CG   B ASN   A 1 101 ? 17.568 1.133   -12.714 0.58 26.67 ?  101 ASN   A CG   1 
ATOM   2354 O OD1  A ASN   A 1 101 ? 16.652 1.502   -12.062 0.42 21.68 ?  101 ASN   A OD1  1 
ATOM   2355 O OD1  B ASN   A 1 101 ? 16.938 0.296   -13.358 0.58 27.53 ?  101 ASN   A OD1  1 
ATOM   2356 N ND2  A ASN   A 1 101 ? 17.381 2.288   -10.083 0.42 20.81 ?  101 ASN   A ND2  1 
ATOM   2357 N ND2  B ASN   A 1 101 ? 17.105 1.669   -11.599 0.58 27.50 ?  101 ASN   A ND2  1 
ATOM   2358 H H    A ASN   A 1 101 ? 19.407 0.145   -11.390 0.42 25.15 ?  101 ASN   A H    1 
ATOM   2359 H H    B ASN   A 1 101 ? 19.734 -0.550  -12.204 0.58 25.34 ?  101 ASN   A H    1 
ATOM   2360 H HA   A ASN   A 1 101 ? 18.771 1.285   -13.673 0.42 26.79 ?  101 ASN   A HA   1 
ATOM   2361 H HA   B ASN   A 1 101 ? 19.180 0.235   -14.666 0.58 27.03 ?  101 ASN   A HA   1 
ATOM   2362 H HB2  A ASN   A 1 101 ? 19.483 2.589   -11.276 0.42 26.35 ?  101 ASN   A HB2  1 
ATOM   2363 H HB2  B ASN   A 1 101 ? 19.438 1.842   -12.376 0.58 29.74 ?  101 ASN   A HB2  1 
ATOM   2364 H HB3  A ASN   A 1 101 ? 18.715 3.265   -12.493 0.42 26.35 ?  101 ASN   A HB3  1 
ATOM   2365 H HB3  B ASN   A 1 101 ? 18.830 2.345   -13.757 0.58 29.74 ?  101 ASN   A HB3  1 
ATOM   2366 H HD21 A ASN   A 1 101 ? 16.645 2.085   -9.685  0.42 25.00 ?  101 ASN   A HD21 1 
ATOM   2367 H HD21 B ASN   A 1 101 ? 16.327 1.443   -11.307 0.58 33.03 ?  101 ASN   A HD21 1 
ATOM   2368 H HD22 A ASN   A 1 101 ? 18.018 2.661   -9.640  0.42 25.00 ?  101 ASN   A HD22 1 
ATOM   2369 H HD22 B ASN   A 1 101 ? 17.571 2.254   -11.179 0.58 33.03 ?  101 ASN   A HD22 1 
ATOM   2370 N N    A LYS   A 1 102 ? 21.817 1.101   -13.215 0.42 25.22 ?  102 LYS   A N    1 
ATOM   2371 N N    B LYS   A 1 102 ? 22.156 0.417   -13.951 0.58 22.79 ?  102 LYS   A N    1 
ATOM   2372 C CA   A LYS   A 1 102 ? 23.098 1.293   -13.877 0.42 26.43 ?  102 LYS   A CA   1 
ATOM   2373 C CA   B LYS   A 1 102 ? 23.476 0.621   -14.536 0.58 23.28 ?  102 LYS   A CA   1 
ATOM   2374 C C    A LYS   A 1 102 ? 23.400 0.185   -14.874 0.42 25.64 ?  102 LYS   A C    1 
ATOM   2375 C C    B LYS   A 1 102 ? 23.879 -0.513  -15.474 0.58 21.80 ?  102 LYS   A C    1 
ATOM   2376 O O    A LYS   A 1 102 ? 24.477 0.189   -15.478 0.42 25.72 ?  102 LYS   A O    1 
ATOM   2377 O O    B LYS   A 1 102 ? 25.017 -0.531  -15.952 0.58 22.62 ?  102 LYS   A O    1 
ATOM   2378 C CB   A LYS   A 1 102 ? 24.225 1.369   -12.843 0.42 28.35 ?  102 LYS   A CB   1 
ATOM   2379 C CB   B LYS   A 1 102 ? 24.544 0.727   -13.438 0.58 25.96 ?  102 LYS   A CB   1 
ATOM   2380 C CG   A LYS   A 1 102 ? 24.119 2.538   -11.883 0.42 30.04 ?  102 LYS   A CG   1 
ATOM   2381 C CG   B LYS   A 1 102 ? 24.495 1.971   -12.566 0.58 28.68 ?  102 LYS   A CG   1 
ATOM   2382 C CD   A LYS   A 1 102 ? 25.242 2.501   -10.860 0.42 31.58 ?  102 LYS   A CD   1 
ATOM   2383 C CD   B LYS   A 1 102 ? 25.545 1.874   -11.460 0.58 31.19 ?  102 LYS   A CD   1 
ATOM   2384 C CE   A LYS   A 1 102 ? 25.234 3.732   -9.969  0.42 32.67 ?  102 LYS   A CE   1 
ATOM   2385 C CE   B LYS   A 1 102 ? 25.498 3.063   -10.517 0.58 33.19 ?  102 LYS   A CE   1 
ATOM   2386 N NZ   A LYS   A 1 102 ? 26.255 3.635   -8.888  0.42 33.25 ?  102 LYS   A NZ   1 
ATOM   2387 N NZ   B LYS   A 1 102 ? 26.001 2.701   -9.160  0.58 34.29 ?  102 LYS   A NZ   1 
ATOM   2388 H H    A LYS   A 1 102 ? 21.832 0.489   -12.610 0.42 30.30 ?  102 LYS   A H    1 
ATOM   2389 H H    B LYS   A 1 102 ? 22.173 -0.108  -13.265 0.58 27.38 ?  102 LYS   A H    1 
ATOM   2390 H HA   A LYS   A 1 102 ? 23.081 2.133   -14.360 0.42 31.74 ?  102 LYS   A HA   1 
ATOM   2391 H HA   B LYS   A 1 102 ? 23.477 1.456   -15.029 0.58 27.96 ?  102 LYS   A HA   1 
ATOM   2392 H HB2  A LYS   A 1 102 ? 24.219 0.555   -12.316 0.42 34.05 ?  102 LYS   A HB2  1 
ATOM   2393 H HB2  B LYS   A 1 102 ? 24.457 -0.038  -12.850 0.58 31.18 ?  102 LYS   A HB2  1 
ATOM   2394 H HB3  A LYS   A 1 102 ? 25.071 1.449   -13.312 0.42 34.05 ?  102 LYS   A HB3  1 
ATOM   2395 H HB3  B LYS   A 1 102 ? 25.418 0.710   -13.859 0.58 31.18 ?  102 LYS   A HB3  1 
ATOM   2396 H HG2  A LYS   A 1 102 ? 24.183 3.370   -12.379 0.42 36.07 ?  102 LYS   A HG2  1 
ATOM   2397 H HG2  B LYS   A 1 102 ? 24.691 2.754   -13.103 0.58 34.45 ?  102 LYS   A HG2  1 
ATOM   2398 H HG3  A LYS   A 1 102 ? 23.272 2.492   -11.411 0.42 36.07 ?  102 LYS   A HG3  1 
ATOM   2399 H HG3  B LYS   A 1 102 ? 23.621 2.047   -12.155 0.58 34.45 ?  102 LYS   A HG3  1 
ATOM   2400 H HD2  A LYS   A 1 102 ? 25.135 1.719   -10.296 0.42 37.92 ?  102 LYS   A HD2  1 
ATOM   2401 H HD2  B LYS   A 1 102 ? 25.397 1.069   -10.938 0.58 37.45 ?  102 LYS   A HD2  1 
ATOM   2402 H HD3  A LYS   A 1 102 ? 26.094 2.466   -11.323 0.42 37.92 ?  102 LYS   A HD3  1 
ATOM   2403 H HD3  B LYS   A 1 102 ? 26.426 1.845   -11.863 0.58 37.45 ?  102 LYS   A HD3  1 
ATOM   2404 H HE2  A LYS   A 1 102 ? 25.434 4.516   -10.506 0.42 39.23 ?  102 LYS   A HE2  1 
ATOM   2405 H HE2  B LYS   A 1 102 ? 26.058 3.773   -10.870 0.58 39.85 ?  102 LYS   A HE2  1 
ATOM   2406 H HE3  A LYS   A 1 102 ? 24.361 3.823   -9.557  0.42 39.23 ?  102 LYS   A HE3  1 
ATOM   2407 H HE3  B LYS   A 1 102 ? 24.583 3.367   -10.434 0.58 39.85 ?  102 LYS   A HE3  1 
ATOM   2408 H HZ1  A LYS   A 1 102 ? 26.232 4.366   -8.381  0.42 39.93 ?  102 LYS   A HZ1  1 
ATOM   2409 H HZ1  B LYS   A 1 102 ? 25.914 3.393   -8.608  0.58 41.17 ?  102 LYS   A HZ1  1 
ATOM   2410 H HZ2  A LYS   A 1 102 ? 26.091 2.924   -8.378  0.42 39.93 ?  102 LYS   A HZ2  1 
ATOM   2411 H HZ2  B LYS   A 1 102 ? 25.534 2.014   -8.838  0.58 41.17 ?  102 LYS   A HZ2  1 
ATOM   2412 H HZ3  A LYS   A 1 102 ? 27.067 3.555   -9.243  0.42 39.93 ?  102 LYS   A HZ3  1 
ATOM   2413 H HZ3  B LYS   A 1 102 ? 26.859 2.470   -9.205  0.58 41.17 ?  102 LYS   A HZ3  1 
ATOM   2414 N N    A GLY   A 1 103 ? 22.481 -0.762  -15.053 0.42 25.28 ?  103 GLY   A N    1 
ATOM   2415 N N    B GLY   A 1 103 ? 22.993 -1.473  -15.727 0.58 19.79 ?  103 GLY   A N    1 
ATOM   2416 C CA   A GLY   A 1 103 ? 22.704 -1.871  -15.956 0.42 24.96 ?  103 GLY   A CA   1 
ATOM   2417 C CA   B GLY   A 1 103 ? 23.341 -2.625  -16.536 0.58 19.49 ?  103 GLY   A CA   1 
ATOM   2418 C C    A GLY   A 1 103 ? 23.585 -2.966  -15.404 0.42 24.93 ?  103 GLY   A C    1 
ATOM   2419 C C    B GLY   A 1 103 ? 24.122 -3.709  -15.821 0.58 18.58 ?  103 GLY   A C    1 
ATOM   2420 O O    A GLY   A 1 103 ? 24.188 -3.710  -16.183 0.42 25.54 ?  103 GLY   A O    1 
ATOM   2421 O O    B GLY   A 1 103 ? 24.640 -4.618  -16.482 0.58 19.52 ?  103 GLY   A O    1 
ATOM   2422 H H    A GLY   A 1 103 ? 21.719 -0.783  -14.657 0.42 30.36 ?  103 GLY   A H    1 
ATOM   2423 H H    B GLY   A 1 103 ? 22.182 -1.467  -15.442 0.58 23.78 ?  103 GLY   A H    1 
ATOM   2424 H HA2  A GLY   A 1 103 ? 21.845 -2.253  -16.207 0.42 29.98 ?  103 GLY   A HA2  1 
ATOM   2425 H HA2  B GLY   A 1 103 ? 22.523 -3.024  -16.866 0.58 23.41 ?  103 GLY   A HA2  1 
ATOM   2426 H HA3  A GLY   A 1 103 ? 23.129 -1.539  -16.759 0.42 29.98 ?  103 GLY   A HA3  1 
ATOM   2427 H HA3  B GLY   A 1 103 ? 23.852 -2.316  -17.305 0.58 23.41 ?  103 GLY   A HA3  1 
ATOM   2428 N N    A GLU   A 1 104 ? 23.690 -3.084  -14.084 0.42 24.02 ?  104 GLU   A N    1 
ATOM   2429 N N    B GLU   A 1 104 ? 24.213 -3.657  -14.497 0.58 16.32 ?  104 GLU   A N    1 
ATOM   2430 C CA   A GLU   A 1 104 ? 24.572 -4.073  -13.483 0.42 23.25 ?  104 GLU   A CA   1 
ATOM   2431 C CA   B GLU   A 1 104 ? 25.000 -4.631  -13.756 0.58 14.48 ?  104 GLU   A CA   1 
ATOM   2432 C C    A GLU   A 1 104 ? 23.889 -5.433  -13.371 0.42 23.47 ?  104 GLU   A C    1 
ATOM   2433 C C    B GLU   A 1 104 ? 24.223 -5.936  -13.587 0.58 14.69 ?  104 GLU   A C    1 
ATOM   2434 O O    A GLU   A 1 104 ? 22.674 -5.536  -13.177 0.42 23.64 ?  104 GLU   A O    1 
ATOM   2435 O O    B GLU   A 1 104 ? 22.993 -5.949  -13.489 0.58 15.87 ?  104 GLU   A O    1 
ATOM   2436 C CB   A GLU   A 1 104 ? 25.066 -3.579  -12.122 0.42 22.41 ?  104 GLU   A CB   1 
ATOM   2437 C CB   B GLU   A 1 104 ? 25.437 -4.045  -12.409 0.58 13.39 ?  104 GLU   A CB   1 
ATOM   2438 C CG   A GLU   A 1 104 ? 26.022 -2.394  -12.256 0.42 22.11 ?  104 GLU   A CG   1 
ATOM   2439 C CG   B GLU   A 1 104 ? 26.352 -2.832  -12.590 0.58 13.47 ?  104 GLU   A CG   1 
ATOM   2440 C CD   A GLU   A 1 104 ? 26.296 -1.672  -10.948 0.42 21.92 ?  104 GLU   A CD   1 
ATOM   2441 C CD   B GLU   A 1 104 ? 26.650 -2.044  -11.316 0.58 13.30 ?  104 GLU   A CD   1 
ATOM   2442 O OE1  A GLU   A 1 104 ? 25.730 -2.062  -9.907  0.42 21.51 ?  104 GLU   A OE1  1 
ATOM   2443 O OE1  B GLU   A 1 104 ? 26.112 -2.361  -10.236 0.58 13.40 ?  104 GLU   A OE1  1 
ATOM   2444 O OE2  A GLU   A 1 104 ? 27.076 -0.695  -10.968 0.42 22.48 -1 104 GLU   A OE2  1 
ATOM   2445 O OE2  B GLU   A 1 104 ? 27.440 -1.079  -11.412 0.58 14.01 -1 104 GLU   A OE2  1 
ATOM   2446 H H    A GLU   A 1 104 ? 23.271 -2.592  -13.516 0.42 28.85 ?  104 GLU   A H    1 
ATOM   2447 H H    B GLU   A 1 104 ? 23.825 -3.067  -14.011 0.58 19.61 ?  104 GLU   A H    1 
ATOM   2448 H HA   A GLU   A 1 104 ? 25.346 -4.180  -14.052 0.42 27.92 ?  104 GLU   A HA   1 
ATOM   2449 H HA   B GLU   A 1 104 ? 25.803 -4.829  -14.268 0.58 17.40 ?  104 GLU   A HA   1 
ATOM   2450 H HB2  A GLU   A 1 104 ? 24.307 -3.295  -11.588 0.42 26.91 ?  104 GLU   A HB2  1 
ATOM   2451 H HB2  B GLU   A 1 104 ? 24.657 -3.764  -11.917 0.58 16.10 ?  104 GLU   A HB2  1 
ATOM   2452 H HB3  A GLU   A 1 104 ? 25.538 -4.299  -11.674 0.42 26.91 ?  104 GLU   A HB3  1 
ATOM   2453 H HB3  B GLU   A 1 104 ? 25.928 -4.722  -11.917 0.58 16.10 ?  104 GLU   A HB3  1 
ATOM   2454 H HG2  A GLU   A 1 104 ? 26.866 -2.714  -12.614 0.42 26.56 ?  104 GLU   A HG2  1 
ATOM   2455 H HG2  B GLU   A 1 104 ? 27.195 -3.137  -12.969 0.58 16.20 ?  104 GLU   A HG2  1 
ATOM   2456 H HG3  A GLU   A 1 104 ? 25.634 -1.747  -12.866 0.42 26.56 ?  104 GLU   A HG3  1 
ATOM   2457 H HG3  B GLU   A 1 104 ? 25.928 -2.215  -13.205 0.58 16.20 ?  104 GLU   A HG3  1 
ATOM   2458 N N    A ASP   A 1 105 ? 24.700 -6.483  -13.497 0.42 23.56 ?  105 ASP   A N    1 
ATOM   2459 N N    B ASP   A 1 105 ? 24.965 -7.042  -13.569 0.58 14.67 ?  105 ASP   A N    1 
ATOM   2460 C CA   A ASP   A 1 105 ? 24.206 -7.852  -13.606 0.42 23.92 ?  105 ASP   A CA   1 
ATOM   2461 C CA   B ASP   A 1 105 ? 24.380 -8.379  -13.641 0.58 15.66 ?  105 ASP   A CA   1 
ATOM   2462 C C    A ASP   A 1 105 ? 23.516 -8.274  -12.314 0.42 23.15 ?  105 ASP   A C    1 
ATOM   2463 C C    B ASP   A 1 105 ? 23.693 -8.740  -12.327 0.58 14.02 ?  105 ASP   A C    1 
ATOM   2464 O O    A ASP   A 1 105 ? 24.145 -8.320  -11.252 0.42 22.79 ?  105 ASP   A O    1 
ATOM   2465 O O    B ASP   A 1 105 ? 24.331 -8.769  -11.273 0.58 12.88 ?  105 ASP   A O    1 
ATOM   2466 C CB   A ASP   A 1 105 ? 25.390 -8.771  -13.898 0.42 25.22 ?  105 ASP   A CB   1 
ATOM   2467 C CB   B ASP   A 1 105 ? 25.498 -9.371  -13.958 0.58 18.61 ?  105 ASP   A CB   1 
ATOM   2468 C CG   A ASP   A 1 105 ? 24.972 -10.191 -14.206 0.42 26.43 ?  105 ASP   A CG   1 
ATOM   2469 C CG   B ASP   A 1 105 ? 25.049 -10.817 -13.912 0.58 21.46 ?  105 ASP   A CG   1 
ATOM   2470 O OD1  A ASP   A 1 105 ? 23.758 -10.439 -14.351 0.42 26.76 ?  105 ASP   A OD1  1 
ATOM   2471 O OD1  B ASP   A 1 105 ? 23.832 -11.078 -13.991 0.58 21.76 ?  105 ASP   A OD1  1 
ATOM   2472 O OD2  A ASP   A 1 105 ? 25.868 -11.057 -14.310 0.42 27.10 -1 105 ASP   A OD2  1 
ATOM   2473 O OD2  B ASP   A 1 105 ? 25.933 -11.697 -13.791 0.58 23.87 -1 105 ASP   A OD2  1 
ATOM   2474 H H    A ASP   A 1 105 ? 25.557 -6.425  -13.521 0.42 28.30 ?  105 ASP   A H    1 
ATOM   2475 H H    B ASP   A 1 105 ? 25.825 -7.041  -13.518 0.58 17.63 ?  105 ASP   A H    1 
ATOM   2476 H HA   A ASP   A 1 105 ? 23.570 -7.918  -14.335 0.42 28.73 ?  105 ASP   A HA   1 
ATOM   2477 H HA   B ASP   A 1 105 ? 23.722 -8.408  -14.351 0.58 18.82 ?  105 ASP   A HA   1 
ATOM   2478 H HB2  A ASP   A 1 105 ? 25.868 -8.434  -14.670 0.42 30.29 ?  105 ASP   A HB2  1 
ATOM   2479 H HB2  B ASP   A 1 105 ? 25.838 -9.184  -14.850 0.58 22.36 ?  105 ASP   A HB2  1 
ATOM   2480 H HB3  A ASP   A 1 105 ? 25.975 -8.786  -13.124 0.42 30.29 ?  105 ASP   A HB3  1 
ATOM   2481 H HB3  B ASP   A 1 105 ? 26.203 -9.273  -13.306 0.58 22.36 ?  105 ASP   A HB3  1 
ATOM   2482 N N    A ILE   A 1 106 ? 22.222 -8.599  -12.406 0.42 22.89 ?  106 ILE   A N    1 
ATOM   2483 N N    B ILE   A 1 106 ? 22.392 -9.040  -12.389 0.58 14.91 ?  106 ILE   A N    1 
ATOM   2484 C CA   A ILE   A 1 106 ? 21.470 -9.015  -11.227 0.42 22.50 ?  106 ILE   A CA   1 
ATOM   2485 C CA   B ILE   A 1 106 ? 21.644 -9.377  -11.182 0.58 15.10 ?  106 ILE   A CA   1 
ATOM   2486 C C    A ILE   A 1 106 ? 22.013 -10.312 -10.642 0.42 21.91 ?  106 ILE   A C    1 
ATOM   2487 C C    B ILE   A 1 106 ? 22.185 -10.628 -10.509 0.58 14.08 ?  106 ILE   A C    1 
ATOM   2488 O O    A ILE   A 1 106 ? 21.811 -10.584 -9.454  0.42 21.47 ?  106 ILE   A O    1 
ATOM   2489 O O    B ILE   A 1 106 ? 21.959 -10.825 -9.311  0.58 13.78 ?  106 ILE   A O    1 
ATOM   2490 C CB   A ILE   A 1 106 ? 19.960 -9.110  -11.546 0.42 23.05 ?  106 ILE   A CB   1 
ATOM   2491 C CB   B ILE   A 1 106 ? 20.130 -9.482  -11.478 0.58 17.68 ?  106 ILE   A CB   1 
ATOM   2492 C CG1  A ILE   A 1 106 ? 19.132 -9.160  -10.260 0.42 23.41 ?  106 ILE   A CG1  1 
ATOM   2493 C CG1  B ILE   A 1 106 ? 19.313 -9.438  -10.183 0.58 19.27 ?  106 ILE   A CG1  1 
ATOM   2494 C CG2  A ILE   A 1 106 ? 19.664 -10.341 -12.373 0.42 23.14 ?  106 ILE   A CG2  1 
ATOM   2495 C CG2  B ILE   A 1 106 ? 19.814 -10.754 -12.236 0.58 18.88 ?  106 ILE   A CG2  1 
ATOM   2496 C CD1  A ILE   A 1 106 ? 19.304 -7.952  -9.373  0.42 23.76 ?  106 ILE   A CD1  1 
ATOM   2497 C CD1  B ILE   A 1 106 ? 19.445 -8.144  -9.409  0.58 20.22 ?  106 ILE   A CD1  1 
ATOM   2498 H H    A ILE   A 1 106 ? 21.764 -8.580  -13.131 0.42 27.50 ?  106 ILE   A H    1 
ATOM   2499 H H    B ILE   A 1 106 ? 21.932 -9.055  -13.107 0.58 17.92 ?  106 ILE   A H    1 
ATOM   2500 H HA   A ILE   A 1 106 ? 21.583 -8.333  -10.552 0.42 27.03 ?  106 ILE   A HA   1 
ATOM   2501 H HA   B ILE   A 1 106 ? 21.769 -8.663  -10.547 0.58 18.15 ?  106 ILE   A HA   1 
ATOM   2502 H HB   A ILE   A 1 106 ? 19.697 -8.325  -12.053 0.42 27.69 ?  106 ILE   A HB   1 
ATOM   2503 H HB   B ILE   A 1 106 ? 19.880 -8.723  -12.025 0.58 21.25 ?  106 ILE   A HB   1 
ATOM   2504 H HG12 A ILE   A 1 106 ? 18.192 -9.221  -10.495 0.42 28.12 ?  106 ILE   A HG12 1 
ATOM   2505 H HG12 B ILE   A 1 106 ? 18.376 -9.551  -10.403 0.58 23.16 ?  106 ILE   A HG12 1 
ATOM   2506 H HG13 A ILE   A 1 106 ? 19.393 -9.942  -9.750  0.42 28.12 ?  106 ILE   A HG13 1 
ATOM   2507 H HG13 B ILE   A 1 106 ? 19.603 -10.158 -9.602  0.58 23.16 ?  106 ILE   A HG13 1 
ATOM   2508 H HG21 A ILE   A 1 106 ? 18.787 -10.247 -12.775 0.42 27.80 ?  106 ILE   A HG21 1 
ATOM   2509 H HG21 B ILE   A 1 106 ? 18.918 -10.682 -12.599 0.58 22.68 ?  106 ILE   A HG21 1 
ATOM   2510 H HG22 A ILE   A 1 106 ? 20.340 -10.424 -13.060 0.42 27.80 ?  106 ILE   A HG22 1 
ATOM   2511 H HG22 B ILE   A 1 106 ? 20.457 -10.857 -12.951 0.58 22.68 ?  106 ILE   A HG22 1 
ATOM   2512 H HG23 A ILE   A 1 106 ? 19.681 -11.120 -11.794 0.42 27.80 ?  106 ILE   A HG23 1 
ATOM   2513 H HG23 B ILE   A 1 106 ? 19.867 -11.505 -11.626 0.58 22.68 ?  106 ILE   A HG23 1 
ATOM   2514 H HD11 A ILE   A 1 106 ? 18.561 -7.909  -8.754  0.42 28.54 ?  106 ILE   A HD11 1 
ATOM   2515 H HD11 B ILE   A 1 106 ? 18.730 -8.090  -8.757  0.58 24.29 ?  106 ILE   A HD11 1 
ATOM   2516 H HD12 A ILE   A 1 106 ? 20.138 -8.035  -8.885  0.42 28.54 ?  106 ILE   A HD12 1 
ATOM   2517 H HD12 B ILE   A 1 106 ? 20.305 -8.128  -8.957  0.58 24.29 ?  106 ILE   A HD12 1 
ATOM   2518 H HD13 A ILE   A 1 106 ? 19.320 -7.156  -9.928  0.42 28.54 ?  106 ILE   A HD13 1 
ATOM   2519 H HD13 B ILE   A 1 106 ? 19.384 -7.398  -10.028 0.58 24.29 ?  106 ILE   A HD13 1 
ATOM   2520 N N    A GLN   A 1 107 ? 22.710 -11.118 -11.447 0.42 22.41 ?  107 GLN   A N    1 
ATOM   2521 N N    B GLN   A 1 107 ? 22.918 -11.475 -11.242 0.58 14.92 ?  107 GLN   A N    1 
ATOM   2522 C CA   A GLN   A 1 107 ? 23.311 -12.347 -10.938 0.42 23.16 ?  107 GLN   A CA   1 
ATOM   2523 C CA   B GLN   A 1 107 ? 23.541 -12.642 -10.622 0.58 17.01 ?  107 GLN   A CA   1 
ATOM   2524 C C    A GLN   A 1 107 ? 24.302 -12.073 -9.816  0.42 20.63 ?  107 GLN   A C    1 
ATOM   2525 C C    B GLN   A 1 107 ? 24.514 -12.240 -9.518  0.58 14.73 ?  107 GLN   A C    1 
ATOM   2526 O O    A GLN   A 1 107 ? 24.557 -12.962 -8.998  0.42 21.53 ?  107 GLN   A O    1 
ATOM   2527 O O    B GLN   A 1 107 ? 24.749 -13.014 -8.581  0.58 15.44 ?  107 GLN   A O    1 
ATOM   2528 C CB   A GLN   A 1 107 ? 24.012 -13.099 -12.074 0.42 26.91 ?  107 GLN   A CB   1 
ATOM   2529 C CB   B GLN   A 1 107 ? 24.228 -13.501 -11.691 0.58 22.25 ?  107 GLN   A CB   1 
ATOM   2530 C CG   A GLN   A 1 107 ? 23.128 -13.358 -13.284 0.42 30.64 ?  107 GLN   A CG   1 
ATOM   2531 C CG   B GLN   A 1 107 ? 23.278 -14.015 -12.773 0.58 27.72 ?  107 GLN   A CG   1 
ATOM   2532 C CD   A GLN   A 1 107 ? 21.869 -14.124 -12.935 0.42 33.70 ?  107 GLN   A CD   1 
ATOM   2533 C CD   B GLN   A 1 107 ? 22.227 -14.963 -12.225 0.58 32.33 ?  107 GLN   A CD   1 
ATOM   2534 O OE1  A GLN   A 1 107 ? 21.924 -15.179 -12.302 0.42 34.94 ?  107 GLN   A OE1  1 
ATOM   2535 O OE1  B GLN   A 1 107 ? 22.520 -15.815 -11.386 0.58 33.88 ?  107 GLN   A OE1  1 
ATOM   2536 N NE2  A GLN   A 1 107 ? 20.723 -13.591 -13.339 0.42 34.70 ?  107 GLN   A NE2  1 
ATOM   2537 N NE2  B GLN   A 1 107 ? 20.992 -14.815 -12.697 0.58 33.85 ?  107 GLN   A NE2  1 
ATOM   2538 H H    A GLN   A 1 107 ? 22.851 -10.973 -12.278 0.42 26.92 ?  107 GLN   A H    1 
ATOM   2539 H H    B GLN   A 1 107 ? 23.068 -11.401 -12.087 0.58 17.93 ?  107 GLN   A H    1 
ATOM   2540 H HA   A GLN   A 1 107 ? 22.613 -12.921 -10.586 0.42 27.82 ?  107 GLN   A HA   1 
ATOM   2541 H HA   B GLN   A 1 107 ? 22.858 -13.188 -10.216 0.58 20.44 ?  107 GLN   A HA   1 
ATOM   2542 H HB2  A GLN   A 1 107 ? 24.775 -12.578 -12.371 0.42 32.32 ?  107 GLN   A HB2  1 
ATOM   2543 H HB2  B GLN   A 1 107 ? 24.915 -12.977 -12.133 0.58 26.73 ?  107 GLN   A HB2  1 
ATOM   2544 H HB3  A GLN   A 1 107 ? 24.314 -13.960 -11.742 0.42 32.32 ?  107 GLN   A HB3  1 
ATOM   2545 H HB3  B GLN   A 1 107 ? 24.632 -14.277 -11.269 0.58 26.73 ?  107 GLN   A HB3  1 
ATOM   2546 H HG2  A GLN   A 1 107 ? 22.864 -12.510 -13.673 0.42 36.80 ?  107 GLN   A HG2  1 
ATOM   2547 H HG2  B GLN   A 1 107 ? 22.820 -13.261 -13.178 0.58 33.29 ?  107 GLN   A HG2  1 
ATOM   2548 H HG3  A GLN   A 1 107 ? 23.627 -13.878 -13.933 0.42 36.80 ?  107 GLN   A HG3  1 
ATOM   2549 H HG3  B GLN   A 1 107 ? 23.788 -14.492 -13.448 0.58 33.29 ?  107 GLN   A HG3  1 
ATOM   2550 H HE21 A GLN   A 1 107 ? 20.723 -12.851 -13.778 0.42 41.67 ?  107 GLN   A HE21 1 
ATOM   2551 H HE21 B GLN   A 1 107 ? 20.824 -14.207 -13.281 0.58 40.65 ?  107 GLN   A HE21 1 
ATOM   2552 H HE22 A GLN   A 1 107 ? 19.981 -13.988 -13.164 0.42 41.67 ?  107 GLN   A HE22 1 
ATOM   2553 H HE22 B GLN   A 1 107 ? 20.360 -15.329 -12.418 0.58 40.65 ?  107 GLN   A HE22 1 
ATOM   2554 N N    A LEU   A 1 108 ? 24.860 -10.862 -9.757  0.42 17.51 ?  108 LEU   A N    1 
ATOM   2555 N N    B LEU   A 1 108 ? 25.075 -11.029 -9.593  0.58 12.61 ?  108 LEU   A N    1 
ATOM   2556 C CA   A LEU   A 1 108 ? 25.793 -10.492 -8.699  0.42 15.14 ?  108 LEU   A CA   1 
ATOM   2557 C CA   B LEU   A 1 108 ? 25.979 -10.554 -8.554  0.58 12.51 ?  108 LEU   A CA   1 
ATOM   2558 C C    A LEU   A 1 108 ? 25.112 -10.317 -7.349  0.42 13.30 ?  108 LEU   A C    1 
ATOM   2559 C C    B LEU   A 1 108 ? 25.264 -10.307 -7.233  0.58 11.68 ?  108 LEU   A C    1 
ATOM   2560 O O    A LEU   A 1 108 ? 25.807 -10.123 -6.347  0.42 13.33 ?  108 LEU   A O    1 
ATOM   2561 O O    B LEU   A 1 108 ? 25.934 -10.126 -6.211  0.58 12.29 ?  108 LEU   A O    1 
ATOM   2562 C CB   A LEU   A 1 108 ? 26.530 -9.206  -9.082  0.42 14.93 ?  108 LEU   A CB   1 
ATOM   2563 C CB   B LEU   A 1 108 ? 26.707 -9.290  -9.016  0.58 13.14 ?  108 LEU   A CB   1 
ATOM   2564 C CG   A LEU   A 1 108 ? 27.517 -9.357  -10.240 0.42 15.61 ?  108 LEU   A CG   1 
ATOM   2565 C CG   B LEU   A 1 108 ? 27.711 -9.518  -10.147 0.58 14.94 ?  108 LEU   A CG   1 
ATOM   2566 C CD1  A LEU   A 1 108 ? 27.935 -8.004  -10.789 0.42 15.83 ?  108 LEU   A CD1  1 
ATOM   2567 C CD1  B LEU   A 1 108 ? 28.178 -8.206  -10.741 0.58 15.37 ?  108 LEU   A CD1  1 
ATOM   2568 C CD2  A LEU   A 1 108 ? 28.738 -10.152 -9.798  0.42 16.53 ?  108 LEU   A CD2  1 
ATOM   2569 C CD2  B LEU   A 1 108 ? 28.903 -10.322 -9.645  0.58 16.38 ?  108 LEU   A CD2  1 
ATOM   2570 H H    A LEU   A 1 108 ? 24.714 -10.242 -10.325 0.42 21.04 ?  108 LEU   A H    1 
ATOM   2571 H H    B LEU   A 1 108 ? 24.948 -10.473 -10.234 0.58 15.16 ?  108 LEU   A H    1 
ATOM   2572 H HA   A LEU   A 1 108 ? 26.453 -11.199 -8.604  0.42 18.19 ?  108 LEU   A HA   1 
ATOM   2573 H HA   B LEU   A 1 108 ? 26.653 -11.240 -8.398  0.58 15.04 ?  108 LEU   A HA   1 
ATOM   2574 H HB2  A LEU   A 1 108 ? 25.873 -8.542  -9.341  0.42 17.95 ?  108 LEU   A HB2  1 
ATOM   2575 H HB2  B LEU   A 1 108 ? 26.051 -8.654  -9.330  0.58 15.79 ?  108 LEU   A HB2  1 
ATOM   2576 H HB3  A LEU   A 1 108 ? 27.025 -8.894  -8.310  0.42 17.95 ?  108 LEU   A HB3  1 
ATOM   2577 H HB3  B LEU   A 1 108 ? 27.193 -8.922  -8.263  0.58 15.79 ?  108 LEU   A HB3  1 
ATOM   2578 H HG   A LEU   A 1 108 ? 27.088 -9.849  -10.956 0.42 18.76 ?  108 LEU   A HG   1 
ATOM   2579 H HG   B LEU   A 1 108 ? 27.283 -10.031 -10.852 0.58 17.95 ?  108 LEU   A HG   1 
ATOM   2580 H HD11 A LEU   A 1 108 ? 28.474 -8.140  -11.585 0.42 19.02 ?  108 LEU   A HD11 1 
ATOM   2581 H HD11 B LEU   A 1 108 ? 28.804 -8.388  -11.459 0.58 18.47 ?  108 LEU   A HD11 1 
ATOM   2582 H HD12 A LEU   A 1 108 ? 27.142 -7.493  -11.009 0.42 19.02 ?  108 LEU   A HD12 1 
ATOM   2583 H HD12 B LEU   A 1 108 ? 27.409 -7.725  -11.086 0.58 18.47 ?  108 LEU   A HD12 1 
ATOM   2584 H HD13 A LEU   A 1 108 ? 28.455 -7.537  -10.115 0.42 19.02 ?  108 LEU   A HD13 1 
ATOM   2585 H HD13 B LEU   A 1 108 ? 28.612 -7.684  -10.048 0.58 18.47 ?  108 LEU   A HD13 1 
ATOM   2586 H HD21 A LEU   A 1 108 ? 29.395 -10.145 -10.511 0.42 19.86 ?  108 LEU   A HD21 1 
ATOM   2587 H HD21 B LEU   A 1 108 ? 29.594 -10.318 -10.325 0.58 19.69 ?  108 LEU   A HD21 1 
ATOM   2588 H HD22 A LEU   A 1 108 ? 29.111 -9.742  -9.001  0.42 19.86 ?  108 LEU   A HD22 1 
ATOM   2589 H HD22 B LEU   A 1 108 ? 29.236 -9.912  -8.831  0.58 19.69 ?  108 LEU   A HD22 1 
ATOM   2590 H HD23 A LEU   A 1 108 ? 28.471 -11.065 -9.604  0.42 19.86 ?  108 LEU   A HD23 1 
ATOM   2591 H HD23 B LEU   A 1 108 ? 28.619 -11.231 -9.466  0.58 19.69 ?  108 LEU   A HD23 1 
ATOM   2592 N N    A LEU   A 1 109 ? 23.780 -10.399 -7.290  0.42 12.55 ?  109 LEU   A N    1 
ATOM   2593 N N    B LEU   A 1 109 ? 23.930 -10.319 -7.221  0.58 11.77 ?  109 LEU   A N    1 
ATOM   2594 C CA   A LEU   A 1 109 ? 23.092 -10.240 -6.016  0.42 11.83 ?  109 LEU   A CA   1 
ATOM   2595 C CA   B LEU   A 1 109 ? 23.209 -10.193 -5.962  0.58 11.37 ?  109 LEU   A CA   1 
ATOM   2596 C C    A LEU   A 1 109 ? 23.432 -11.373 -5.059  0.42 11.29 ?  109 LEU   A C    1 
ATOM   2597 C C    B LEU   A 1 109 ? 23.509 -11.367 -5.036  0.58 10.80 ?  109 LEU   A C    1 
ATOM   2598 O O    A LEU   A 1 109 ? 23.517 -11.160 -3.845  0.42 11.41 ?  109 LEU   A O    1 
ATOM   2599 O O    B LEU   A 1 109 ? 23.638 -11.190 -3.821  0.58 10.81 ?  109 LEU   A O    1 
ATOM   2600 C CB   A LEU   A 1 109 ? 21.586 -10.166 -6.257  0.42 12.48 ?  109 LEU   A CB   1 
ATOM   2601 C CB   B LEU   A 1 109 ? 21.712 -10.068 -6.237  0.58 12.32 ?  109 LEU   A CB   1 
ATOM   2602 C CG   A LEU   A 1 109 ? 20.700 -9.872  -5.047  0.42 12.96 ?  109 LEU   A CG   1 
ATOM   2603 C CG   B LEU   A 1 109 ? 20.816 -9.827  -5.024  0.58 13.01 ?  109 LEU   A CG   1 
ATOM   2604 C CD1  A LEU   A 1 109 ? 21.121 -8.576  -4.377  0.42 12.98 ?  109 LEU   A CD1  1 
ATOM   2605 C CD1  B LEU   A 1 109 ? 21.303 -8.625  -4.224  0.58 13.12 ?  109 LEU   A CD1  1 
ATOM   2606 C CD2  A LEU   A 1 109 ? 19.237 -9.813  -5.466  0.42 13.74 ?  109 LEU   A CD2  1 
ATOM   2607 C CD2  B LEU   A 1 109 ? 19.367 -9.640  -5.458  0.58 14.00 ?  109 LEU   A CD2  1 
ATOM   2608 H H    A LEU   A 1 109 ? 23.266 -10.559 -7.957  0.42 15.09 ?  109 LEU   A H    1 
ATOM   2609 H H    B LEU   A 1 109 ? 23.435 -10.398 -7.915  0.58 14.16 ?  109 LEU   A H    1 
ATOM   2610 H HA   A LEU   A 1 109 ? 23.373 -9.408  -5.611  0.42 14.22 ?  109 LEU   A HA   1 
ATOM   2611 H HA   B LEU   A 1 109 ? 23.506 -9.381  -5.519  0.58 13.68 ?  109 LEU   A HA   1 
ATOM   2612 H HB2  A LEU   A 1 109 ? 21.422 -9.463  -6.906  0.42 15.00 ?  109 LEU   A HB2  1 
ATOM   2613 H HB2  B LEU   A 1 109 ? 21.577 -9.322  -6.845  0.58 14.82 ?  109 LEU   A HB2  1 
ATOM   2614 H HB3  A LEU   A 1 109 ? 21.296 -11.014 -6.623  0.42 15.00 ?  109 LEU   A HB3  1 
ATOM   2615 H HB3  B LEU   A 1 109 ? 21.410 -10.885 -6.658  0.58 14.82 ?  109 LEU   A HB3  1 
ATOM   2616 H HG   A LEU   A 1 109 ? 20.796 -10.588 -4.400  0.42 15.58 ?  109 LEU   A HG   1 
ATOM   2617 H HG   B LEU   A 1 109 ? 20.856 -10.602 -4.445  0.58 15.63 ?  109 LEU   A HG   1 
ATOM   2618 H HD11 A LEU   A 1 109 ? 20.457 -8.331  -3.714  0.42 15.60 ?  109 LEU   A HD11 1 
ATOM   2619 H HD11 B LEU   A 1 109 ? 20.614 -8.359  -3.598  0.58 15.78 ?  109 LEU   A HD11 1 
ATOM   2620 H HD12 A LEU   A 1 109 ? 21.982 -8.706  -3.949  0.42 15.60 ?  109 LEU   A HD12 1 
ATOM   2621 H HD12 B LEU   A 1 109 ? 22.111 -8.870  -3.744  0.58 15.78 ?  109 LEU   A HD12 1 
ATOM   2622 H HD13 A LEU   A 1 109 ? 21.188 -7.879  -5.050  0.42 15.60 ?  109 LEU   A HD13 1 
ATOM   2623 H HD13 B LEU   A 1 109 ? 21.493 -7.894  -4.836  0.58 15.78 ?  109 LEU   A HD13 1 
ATOM   2624 H HD21 A LEU   A 1 109 ? 18.709 -9.478  -4.724  0.42 16.51 ?  109 LEU   A HD21 1 
ATOM   2625 H HD21 B LEU   A 1 109 ? 18.823 -9.452  -4.676  0.58 16.82 ?  109 LEU   A HD21 1 
ATOM   2626 H HD22 A LEU   A 1 109 ? 19.151 -9.216  -6.227  0.42 16.51 ?  109 LEU   A HD22 1 
ATOM   2627 H HD22 B LEU   A 1 109 ? 19.314 -8.899  -6.082  0.58 16.82 ?  109 LEU   A HD22 1 
ATOM   2628 H HD23 A LEU   A 1 109 ? 18.941 -10.703 -5.710  0.42 16.51 ?  109 LEU   A HD23 1 
ATOM   2629 H HD23 B LEU   A 1 109 ? 19.058 -10.455 -5.886  0.58 16.82 ?  109 LEU   A HD23 1 
ATOM   2630 N N    . LYS   A 1 110 ? 23.633 -12.579 -5.583  1.00 11.19 ?  110 LYS   A N    1 
ATOM   2631 C CA   . LYS   A 1 110 ? 24.004 -13.701 -4.734  1.00 10.97 ?  110 LYS   A CA   1 
ATOM   2632 C C    . LYS   A 1 110 ? 25.377 -13.467 -4.112  1.00 10.56 ?  110 LYS   A C    1 
ATOM   2633 O O    . LYS   A 1 110 ? 25.566 -13.677 -2.911  1.00 10.72 ?  110 LYS   A O    1 
ATOM   2634 C CB   . LYS   A 1 110 ? 23.961 -15.017 -5.512  1.00 12.00 ?  110 LYS   A CB   1 
ATOM   2635 C CG   . LYS   A 1 110 ? 24.140 -16.230 -4.607  1.00 11.88 ?  110 LYS   A CG   1 
ATOM   2636 C CD   . LYS   A 1 110 ? 23.877 -17.549 -5.320  1.00 12.42 ?  110 LYS   A CD   1 
ATOM   2637 C CE   . LYS   A 1 110 ? 23.973 -18.740 -4.373  1.00 13.28 ?  110 LYS   A CE   1 
ATOM   2638 N NZ   . LYS   A 1 110 ? 22.794 -18.866 -3.478  1.00 13.74 ?  110 LYS   A NZ   1 
ATOM   2639 H H    A LYS   A 1 110 ? 23.563 -12.769 -6.417  0.42 13.46 ?  110 LYS   A H    1 
ATOM   2640 H H    B LYS   A 1 110 ? 23.516 -12.769 -6.411  0.58 13.46 ?  110 LYS   A H    1 
ATOM   2641 H HA   . LYS   A 1 110 ? 23.363 -13.769 -4.007  1.00 13.19 ?  110 LYS   A HA   1 
ATOM   2642 H HB2  . LYS   A 1 110 ? 23.106 -15.099 -5.954  1.00 14.43 ?  110 LYS   A HB2  1 
ATOM   2643 H HB3  . LYS   A 1 110 ? 24.680 -15.024 -6.163  1.00 14.43 ?  110 LYS   A HB3  1 
ATOM   2644 H HG2  . LYS   A 1 110 ? 25.054 -16.249 -4.274  1.00 14.28 ?  110 LYS   A HG2  1 
ATOM   2645 H HG3  . LYS   A 1 110 ? 23.522 -16.166 -3.863  1.00 14.28 ?  110 LYS   A HG3  1 
ATOM   2646 H HD2  . LYS   A 1 110 ? 22.986 -17.530 -5.693  1.00 14.93 ?  110 LYS   A HD2  1 
ATOM   2647 H HD3  . LYS   A 1 110 ? 24.537 -17.662 -6.021  1.00 14.93 ?  110 LYS   A HD3  1 
ATOM   2648 H HE2  . LYS   A 1 110 ? 24.047 -19.554 -4.895  1.00 15.96 ?  110 LYS   A HE2  1 
ATOM   2649 H HE3  . LYS   A 1 110 ? 24.766 -18.637 -3.813  1.00 15.96 ?  110 LYS   A HE3  1 
ATOM   2650 H HZ1  . LYS   A 1 110 ? 22.889 -19.569 -2.945  1.00 16.52 ?  110 LYS   A HZ1  1 
ATOM   2651 H HZ2  . LYS   A 1 110 ? 22.712 -18.132 -2.981  1.00 16.52 ?  110 LYS   A HZ2  1 
ATOM   2652 H HZ3  . LYS   A 1 110 ? 22.057 -18.967 -3.967  1.00 16.52 ?  110 LYS   A HZ3  1 
ATOM   2653 N N    . SER   A 1 111 ? 26.344 -13.015 -4.918  1.00 10.66 ?  111 SER   A N    1 
ATOM   2654 C CA   . SER   A 1 111 ? 27.670 -12.715 -4.389  1.00 10.61 ?  111 SER   A CA   1 
ATOM   2655 C C    . SER   A 1 111 ? 27.592 -11.669 -3.282  1.00 10.16 ?  111 SER   A C    1 
ATOM   2656 O O    . SER   A 1 111 ? 28.288 -11.767 -2.263  1.00 10.51 ?  111 SER   A O    1 
ATOM   2657 C CB   . SER   A 1 111 ? 28.571 -12.235 -5.523  1.00 12.44 ?  111 SER   A CB   1 
ATOM   2658 O OG   . SER   A 1 111 ? 28.615 -13.202 -6.560  1.00 14.42 ?  111 SER   A OG   1 
ATOM   2659 H H    . SER   A 1 111 ? 26.248 -12.864 -5.758  1.00 12.82 ?  111 SER   A H    1 
ATOM   2660 H HA   . SER   A 1 111 ? 28.055 -13.526 -4.020  1.00 12.76 ?  111 SER   A HA   1 
ATOM   2661 H HB2  . SER   A 1 111 ? 28.215 -11.408 -5.887  1.00 14.95 ?  111 SER   A HB2  1 
ATOM   2662 H HB3  . SER   A 1 111 ? 29.466 -12.086 -5.179  1.00 14.95 ?  111 SER   A HB3  1 
ATOM   2663 H HG   . SER   A 1 111 ? 29.129 -12.933 -7.178  1.00 17.33 ?  111 SER   A HG   1 
ATOM   2664 N N    . ALA   A 1 112 ? 26.747 -10.652 -3.471  1.00 10.08 ?  112 ALA   A N    1 
ATOM   2665 C CA   . ALA   A 1 112 ? 26.578 -9.615  -2.457  1.00 9.88  ?  112 ALA   A CA   1 
ATOM   2666 C C    . ALA   A 1 112 ? 26.095 -10.218 -1.142  1.00 9.52  ?  112 ALA   A C    1 
ATOM   2667 O O    . ALA   A 1 112 ? 26.646 -9.937  -0.071  1.00 10.06 ?  112 ALA   A O    1 
ATOM   2668 C CB   . ALA   A 1 112 ? 25.612 -8.540  -2.962  1.00 10.77 ?  112 ALA   A CB   1 
ATOM   2669 H H    . ALA   A 1 112 ? 26.269 -10.537 -4.176  1.00 12.13 ?  112 ALA   A H    1 
ATOM   2670 H HA   . ALA   A 1 112 ? 27.438 -9.192  -2.293  1.00 11.89 ?  112 ALA   A HA   1 
ATOM   2671 H HB1  . ALA   A 1 112 ? 25.520 -7.853  -2.280  1.00 12.95 ?  112 ALA   A HB1  1 
ATOM   2672 H HB2  . ALA   A 1 112 ? 25.971 -8.148  -3.774  1.00 12.95 ?  112 ALA   A HB2  1 
ATOM   2673 H HB3  . ALA   A 1 112 ? 24.752 -8.945  -3.140  1.00 12.95 ?  112 ALA   A HB3  1 
ATOM   2674 N N    A TYR   A 1 113 ? 25.061 -11.061 -1.206  0.42 9.83  ?  113 TYR   A N    1 
ATOM   2675 N N    B TYR   A 1 113 ? 25.053 -11.052 -1.197  0.58 9.85  ?  113 TYR   A N    1 
ATOM   2676 C CA   A TYR   A 1 113 ? 24.533 -11.667 0.011   0.42 9.77  ?  113 TYR   A CA   1 
ATOM   2677 C CA   B TYR   A 1 113 ? 24.545 -11.652 0.034   0.58 9.62  ?  113 TYR   A CA   1 
ATOM   2678 C C    A TYR   A 1 113 ? 25.528 -12.626 0.666   0.42 9.42  ?  113 TYR   A C    1 
ATOM   2679 C C    B TYR   A 1 113 ? 25.548 -12.609 0.677   0.58 9.41  ?  113 TYR   A C    1 
ATOM   2680 O O    A TYR   A 1 113 ? 25.473 -12.827 1.883   0.42 9.62  ?  113 TYR   A O    1 
ATOM   2681 O O    B TYR   A 1 113 ? 25.518 -12.794 1.897   0.58 9.82  ?  113 TYR   A O    1 
ATOM   2682 C CB   A TYR   A 1 113 ? 23.206 -12.376 -0.282  0.42 10.20 ?  113 TYR   A CB   1 
ATOM   2683 C CB   B TYR   A 1 113 ? 23.217 -12.369 -0.217  0.58 9.91  ?  113 TYR   A CB   1 
ATOM   2684 C CG   A TYR   A 1 113 ? 21.989 -11.472 -0.217  0.42 10.26 ?  113 TYR   A CG   1 
ATOM   2685 C CG   B TYR   A 1 113 ? 22.011 -11.457 -0.225  0.58 10.03 ?  113 TYR   A CG   1 
ATOM   2686 C CD1  A TYR   A 1 113 ? 21.630 -10.849 0.970   0.42 10.55 ?  113 TYR   A CD1  1 
ATOM   2687 C CD1  B TYR   A 1 113 ? 21.646 -10.747 0.913   0.58 10.34 ?  113 TYR   A CD1  1 
ATOM   2688 C CD2  A TYR   A 1 113 ? 21.194 -11.256 -1.336  0.42 10.62 ?  113 TYR   A CD2  1 
ATOM   2689 C CD2  B TYR   A 1 113 ? 21.233 -11.318 -1.363  0.58 10.80 ?  113 TYR   A CD2  1 
ATOM   2690 C CE1  A TYR   A 1 113 ? 20.513 -10.033 1.044   0.42 10.89 ?  113 TYR   A CE1  1 
ATOM   2691 C CE1  B TYR   A 1 113 ? 20.535 -9.921  0.914   0.58 10.99 ?  113 TYR   A CE1  1 
ATOM   2692 C CE2  A TYR   A 1 113 ? 20.063 -10.441 -1.272  0.42 10.77 ?  113 TYR   A CE2  1 
ATOM   2693 C CE2  B TYR   A 1 113 ? 20.112 -10.499 -1.374  0.58 11.30 ?  113 TYR   A CE2  1 
ATOM   2694 C CZ   A TYR   A 1 113 ? 19.733 -9.829  -0.078  0.42 10.55 ?  113 TYR   A CZ   1 
ATOM   2695 C CZ   B TYR   A 1 113 ? 19.770 -9.801  -0.232  0.58 11.28 ?  113 TYR   A CZ   1 
ATOM   2696 O OH   A TYR   A 1 113 ? 18.622 -9.014  0.013   0.42 10.75 ?  113 TYR   A OH   1 
ATOM   2697 O OH   B TYR   A 1 113 ? 18.664 -8.978  -0.233  0.58 12.69 ?  113 TYR   A OH   1 
ATOM   2698 H H    A TYR   A 1 113 ? 24.656 -11.290 -1.930  0.42 11.83 ?  113 TYR   A H    1 
ATOM   2699 H H    B TYR   A 1 113 ? 24.636 -11.278 -1.913  0.58 11.85 ?  113 TYR   A H    1 
ATOM   2700 H HA   A TYR   A 1 113 ? 24.354 -10.963 0.648   0.42 11.75 ?  113 TYR   A HA   1 
ATOM   2701 H HA   B TYR   A 1 113 ? 24.380 -10.945 0.674   0.58 11.58 ?  113 TYR   A HA   1 
ATOM   2702 H HB2  A TYR   A 1 113 ? 23.246 -12.753 -1.175  0.42 12.27 ?  113 TYR   A HB2  1 
ATOM   2703 H HB2  B TYR   A 1 113 ? 23.259 -12.805 -1.082  0.58 11.92 ?  113 TYR   A HB2  1 
ATOM   2704 H HB3  A TYR   A 1 113 ? 23.082 -13.084 0.367   0.42 12.27 ?  113 TYR   A HB3  1 
ATOM   2705 H HB3  B TYR   A 1 113 ? 23.082 -13.029 0.478   0.58 11.92 ?  113 TYR   A HB3  1 
ATOM   2706 H HD1  A TYR   A 1 113 ? 22.149 -10.986 1.729   0.42 12.69 ?  113 TYR   A HD1  1 
ATOM   2707 H HD1  B TYR   A 1 113 ? 22.158 -10.833 1.688   0.58 12.44 ?  113 TYR   A HD1  1 
ATOM   2708 H HD2  A TYR   A 1 113 ? 21.414 -11.671 -2.140  0.42 12.77 ?  113 TYR   A HD2  1 
ATOM   2709 H HD2  B TYR   A 1 113 ? 21.460 -11.791 -2.131  0.58 12.98 ?  113 TYR   A HD2  1 
ATOM   2710 H HE1  A TYR   A 1 113 ? 20.288 -9.628  1.850   0.42 13.10 ?  113 TYR   A HE1  1 
ATOM   2711 H HE1  B TYR   A 1 113 ? 20.304 -9.459  1.687   0.58 13.21 ?  113 TYR   A HE1  1 
ATOM   2712 H HE2  A TYR   A 1 113 ? 19.538 -10.306 -2.030  0.42 12.95 ?  113 TYR   A HE2  1 
ATOM   2713 H HE2  B TYR   A 1 113 ? 19.597 -10.418 -2.146  0.58 13.59 ?  113 TYR   A HE2  1 
ATOM   2714 H HH   A TYR   A 1 113 ? 18.228 -8.977  -0.731  0.42 12.92 ?  113 TYR   A HH   1 
ATOM   2715 H HH   B TYR   A 1 113 ? 18.284 -9.007  -0.984  0.58 15.26 ?  113 TYR   A HH   1 
ATOM   2716 N N    . GLU   A 1 114 ? 26.442 -13.222 -0.110  1.00 9.64  ?  114 GLU   A N    1 
ATOM   2717 C CA   . GLU   A 1 114 ? 27.439 -14.120 0.482   1.00 10.06 ?  114 GLU   A CA   1 
ATOM   2718 C C    . GLU   A 1 114 ? 28.284 -13.412 1.538   1.00 9.79  ?  114 GLU   A C    1 
ATOM   2719 O O    . GLU   A 1 114 ? 28.769 -14.050 2.482   1.00 10.13 ?  114 GLU   A O    1 
ATOM   2720 C CB   . GLU   A 1 114 ? 28.313 -14.747 -0.608  1.00 10.11 ?  114 GLU   A CB   1 
ATOM   2721 C CG   . GLU   A 1 114 ? 27.560 -15.813 -1.392  1.00 10.65 ?  114 GLU   A CG   1 
ATOM   2722 C CD   . GLU   A 1 114 ? 28.281 -16.341 -2.629  1.00 10.97 ?  114 GLU   A CD   1 
ATOM   2723 O OE1  . GLU   A 1 114 ? 29.233 -15.697 -3.133  1.00 11.40 ?  114 GLU   A OE1  1 
ATOM   2724 O OE2  . GLU   A 1 114 ? 27.848 -17.408 -3.124  1.00 12.27 -1 114 GLU   A OE2  1 
ATOM   2725 H H    A GLU   A 1 114 ? 26.498 -13.126 -0.965  0.42 11.60 ?  114 GLU   A H    1 
ATOM   2726 H H    B GLU   A 1 114 ? 26.487 -13.134 -0.966  0.58 11.60 ?  114 GLU   A H    1 
ATOM   2727 H HA   . GLU   A 1 114 ? 26.967 -14.842 0.921   1.00 12.10 ?  114 GLU   A HA   1 
ATOM   2728 H HB2  . GLU   A 1 114 ? 28.597 -14.058 -1.233  1.00 12.16 ?  114 GLU   A HB2  1 
ATOM   2729 H HB3  . GLU   A 1 114 ? 29.085 -15.165 -0.199  1.00 12.16 ?  114 GLU   A HB3  1 
ATOM   2730 H HG2  . GLU   A 1 114 ? 27.401 -16.568 -0.810  1.00 12.81 ?  114 GLU   A HG2  1 
ATOM   2731 H HG3  . GLU   A 1 114 ? 26.712 -15.440 -1.683  1.00 12.81 ?  114 GLU   A HG3  1 
ATOM   2732 N N    . ASN   A 1 115 ? 28.468 -12.095 1.405   1.00 9.57  ?  115 ASN   A N    1 
ATOM   2733 C CA   . ASN   A 1 115 ? 29.241 -11.365 2.404   1.00 9.95  ?  115 ASN   A CA   1 
ATOM   2734 C C    . ASN   A 1 115 ? 28.619 -11.490 3.791   1.00 9.74  ?  115 ASN   A C    1 
ATOM   2735 O O    . ASN   A 1 115 ? 29.328 -11.406 4.800   1.00 10.28 ?  115 ASN   A O    1 
ATOM   2736 C CB   . ASN   A 1 115 ? 29.350 -9.891  2.015   1.00 10.33 ?  115 ASN   A CB   1 
ATOM   2737 C CG   . ASN   A 1 115 ? 30.154 -9.684  0.758   1.00 10.94 ?  115 ASN   A CG   1 
ATOM   2738 O OD1  . ASN   A 1 115 ? 31.371 -9.781  0.777   1.00 14.51 ?  115 ASN   A OD1  1 
ATOM   2739 N ND2  . ASN   A 1 115 ? 29.485 -9.376  -0.334  1.00 10.61 ?  115 ASN   A ND2  1 
ATOM   2740 H H    . ASN   A 1 115 ? 28.156 -11.609 0.762   1.00 11.52 ?  115 ASN   A H    1 
ATOM   2741 H HA   . ASN   A 1 115 ? 30.136 -11.737 2.440   1.00 11.96 ?  115 ASN   A HA   1 
ATOM   2742 H HB2  . ASN   A 1 115 ? 28.462 -9.535  1.872   1.00 12.42 ?  115 ASN   A HB2  1 
ATOM   2743 H HB3  . ASN   A 1 115 ? 29.788 -9.410  2.738   1.00 12.42 ?  115 ASN   A HB3  1 
ATOM   2744 H HD21 . ASN   A 1 115 ? 29.909 -9.238  -1.071  1.00 12.76 ?  115 ASN   A HD21 1 
ATOM   2745 H HD22 . ASN   A 1 115 ? 28.630 -9.320  -0.311  1.00 12.76 ?  115 ASN   A HD22 1 
ATOM   2746 N N    . PHE   A 1 116 ? 27.294 -11.660 3.868   1.00 9.69  ?  116 PHE   A N    1 
ATOM   2747 C CA   . PHE   A 1 116 ? 26.642 -11.748 5.171   1.00 9.78  ?  116 PHE   A CA   1 
ATOM   2748 C C    . PHE   A 1 116 ? 27.110 -12.975 5.951   1.00 9.95  ?  116 PHE   A C    1 
ATOM   2749 O O    . PHE   A 1 116 ? 27.031 -12.986 7.179   1.00 10.81 ?  116 PHE   A O    1 
ATOM   2750 C CB   . PHE   A 1 116 ? 25.117 -11.878 5.034   1.00 10.10 ?  116 PHE   A CB   1 
ATOM   2751 C CG   . PHE   A 1 116 ? 24.353 -10.644 4.534   1.00 9.74  ?  116 PHE   A CG   1 
ATOM   2752 C CD1  . PHE   A 1 116 ? 24.911 -9.643  3.740   1.00 10.09 ?  116 PHE   A CD1  1 
ATOM   2753 C CD2  . PHE   A 1 116 ? 23.005 -10.531 4.865   1.00 10.20 ?  116 PHE   A CD2  1 
ATOM   2754 C CE1  . PHE   A 1 116 ? 24.142 -8.582  3.295   1.00 10.33 ?  116 PHE   A CE1  1 
ATOM   2755 C CE2  . PHE   A 1 116 ? 22.237 -9.470  4.430   1.00 10.66 ?  116 PHE   A CE2  1 
ATOM   2756 C CZ   . PHE   A 1 116 ? 22.797 -8.497  3.642   1.00 10.32 ?  116 PHE   A CZ   1 
ATOM   2757 H H    . PHE   A 1 116 ? 26.766 -11.723 3.191   1.00 11.66 ?  116 PHE   A H    1 
ATOM   2758 H HA   . PHE   A 1 116 ? 26.843 -10.951 5.688   1.00 11.77 ?  116 PHE   A HA   1 
ATOM   2759 H HB2  . PHE   A 1 116 ? 24.934 -12.606 4.417   1.00 12.14 ?  116 PHE   A HB2  1 
ATOM   2760 H HB3  . PHE   A 1 116 ? 24.762 -12.111 5.909   1.00 12.14 ?  116 PHE   A HB3  1 
ATOM   2761 H HD1  . PHE   A 1 116 ? 25.799 -9.705  3.499   1.00 12.13 ?  116 PHE   A HD1  1 
ATOM   2762 H HD2  . PHE   A 1 116 ? 22.604 -11.199 5.389   1.00 12.27 ?  116 PHE   A HD2  1 
ATOM   2763 H HE1  . PHE   A 1 116 ? 24.520 -7.919  2.770   1.00 12.43 ?  116 PHE   A HE1  1 
ATOM   2764 H HE2  . PHE   A 1 116 ? 21.335 -9.422  4.663   1.00 12.81 ?  116 PHE   A HE2  1 
ATOM   2765 H HZ   . PHE   A 1 116 ? 22.281 -7.779  3.354   1.00 12.41 ?  116 PHE   A HZ   1 
ATOM   2766 N N    . ASN   A 1 117 ? 27.562 -14.023 5.258   1.00 10.01 ?  117 ASN   A N    1 
ATOM   2767 C CA   . ASN   A 1 117 ? 27.928 -15.261 5.936   1.00 10.22 ?  117 ASN   A CA   1 
ATOM   2768 C C    . ASN   A 1 117 ? 29.191 -15.139 6.769   1.00 10.73 ?  117 ASN   A C    1 
ATOM   2769 O O    . ASN   A 1 117 ? 29.486 -16.054 7.546   1.00 11.46 ?  117 ASN   A O    1 
ATOM   2770 C CB   . ASN   A 1 117 ? 28.054 -16.384 4.917   1.00 10.34 ?  117 ASN   A CB   1 
ATOM   2771 C CG   . ASN   A 1 117 ? 26.705 -16.777 4.370   1.00 10.63 ?  117 ASN   A CG   1 
ATOM   2772 O OD1  . ASN   A 1 117 ? 25.731 -16.817 5.120   1.00 11.44 ?  117 ASN   A OD1  1 
ATOM   2773 N ND2  . ASN   A 1 117 ? 26.625 -17.040 3.076   1.00 10.73 ?  117 ASN   A ND2  1 
ATOM   2774 H H    . ASN   A 1 117 ? 27.665 -14.039 4.403   1.00 12.03 ?  117 ASN   A H    1 
ATOM   2775 H HA   . ASN   A 1 117 ? 27.202 -15.490 6.539   1.00 12.29 ?  117 ASN   A HA   1 
ATOM   2776 H HB2  . ASN   A 1 117 ? 28.612 -16.085 4.180   1.00 12.44 ?  117 ASN   A HB2  1 
ATOM   2777 H HB3  . ASN   A 1 117 ? 28.452 -17.157 5.346   1.00 12.44 ?  117 ASN   A HB3  1 
ATOM   2778 H HD21 . ASN   A 1 117 ? 25.876 -17.267 2.731   1.00 12.91 ?  117 ASN   A HD21 1 
ATOM   2779 H HD22 . ASN   A 1 117 ? 27.333 -16.990 2.587   1.00 12.91 ?  117 ASN   A HD22 1 
ATOM   2780 N N    . GLN   A 1 118 ? 29.920 -14.030 6.648   1.00 10.50 ?  118 GLN   A N    1 
ATOM   2781 C CA   . GLN   A 1 118 ? 31.089 -13.789 7.480   1.00 11.47 ?  118 GLN   A CA   1 
ATOM   2782 C C    . GLN   A 1 118 ? 30.739 -13.210 8.843   1.00 11.45 ?  118 GLN   A C    1 
ATOM   2783 O O    . GLN   A 1 118 ? 31.656 -12.914 9.619   1.00 12.82 ?  118 GLN   A O    1 
ATOM   2784 C CB   . GLN   A 1 118 ? 32.089 -12.885 6.748   1.00 11.54 ?  118 GLN   A CB   1 
ATOM   2785 C CG   . GLN   A 1 118 ? 32.545 -13.471 5.418   1.00 11.91 ?  118 GLN   A CG   1 
ATOM   2786 C CD   . GLN   A 1 118 ? 33.383 -14.730 5.594   1.00 12.06 ?  118 GLN   A CD   1 
ATOM   2787 O OE1  . GLN   A 1 118 ? 34.246 -14.794 6.475   1.00 13.07 ?  118 GLN   A OE1  1 
ATOM   2788 N NE2  . GLN   A 1 118 ? 33.146 -15.733 4.747   1.00 12.53 ?  118 GLN   A NE2  1 
ATOM   2789 H H    . GLN   A 1 118 ? 29.752 -13.391 6.090   1.00 12.63 ?  118 GLN   A H    1 
ATOM   2790 H HA   . GLN   A 1 118 ? 31.523 -14.639 7.635   1.00 13.79 ?  118 GLN   A HA   1 
ATOM   2791 H HB2  . GLN   A 1 118 ? 31.681 -12.026 6.576   1.00 13.88 ?  118 GLN   A HB2  1 
ATOM   2792 H HB3  . GLN   A 1 118 ? 32.878 -12.771 7.309   1.00 13.88 ?  118 GLN   A HB3  1 
ATOM   2793 H HG2  . GLN   A 1 118 ? 31.766 -13.697 4.887   1.00 14.32 ?  118 GLN   A HG2  1 
ATOM   2794 H HG3  . GLN   A 1 118 ? 33.085 -12.813 4.950   1.00 14.32 ?  118 GLN   A HG3  1 
ATOM   2795 H HE21 . GLN   A 1 118 ? 32.528 -15.649 4.146   1.00 15.06 ?  118 GLN   A HE21 1 
ATOM   2796 H HE22 . GLN   A 1 118 ? 33.586 -16.463 4.805   1.00 15.06 ?  118 GLN   A HE22 1 
ATOM   2797 N N    . HIS   A 1 119 ? 29.448 -13.049 9.150   1.00 11.09 ?  119 HIS   A N    1 
ATOM   2798 C CA   . HIS   A 1 119 ? 28.988 -12.437 10.393  1.00 11.58 ?  119 HIS   A CA   1 
ATOM   2799 C C    . HIS   A 1 119 ? 27.858 -13.274 10.962  1.00 11.87 ?  119 HIS   A C    1 
ATOM   2800 O O    . HIS   A 1 119 ? 26.918 -13.619 10.243  1.00 12.13 ?  119 HIS   A O    1 
ATOM   2801 C CB   . HIS   A 1 119 ? 28.521 -11.006 10.126  1.00 11.84 ?  119 HIS   A CB   1 
ATOM   2802 C CG   . HIS   A 1 119 ? 29.590 -10.193 9.501   1.00 13.38 ?  119 HIS   A CG   1 
ATOM   2803 N ND1  . HIS   A 1 119 ? 30.560 -9.570  10.250  1.00 15.52 ?  119 HIS   A ND1  1 
ATOM   2804 C CD2  . HIS   A 1 119 ? 29.932 -10.018 8.205   1.00 14.60 ?  119 HIS   A CD2  1 
ATOM   2805 C CE1  . HIS   A 1 119 ? 31.429 -8.997  9.437   1.00 15.95 ?  119 HIS   A CE1  1 
ATOM   2806 N NE2  . HIS   A 1 119 ? 31.076 -9.260  8.191   1.00 15.98 ?  119 HIS   A NE2  1 
ATOM   2807 H H    . HIS   A 1 119 ? 28.798 -13.309 8.642   1.00 13.33 ?  119 HIS   A H    1 
ATOM   2808 H HA   . HIS   A 1 119 ? 29.710 -12.421 11.037  1.00 13.92 ?  119 HIS   A HA   1 
ATOM   2809 H HB2  . HIS   A 1 119 ? 27.760 -11.026 9.530   1.00 14.23 ?  119 HIS   A HB2  1 
ATOM   2810 H HB3  . HIS   A 1 119 ? 28.277 -10.595 10.972  1.00 14.23 ?  119 HIS   A HB3  1 
ATOM   2811 H HD2  . HIS   A 1 119 ? 29.477 -10.347 7.465   1.00 17.55 ?  119 HIS   A HD2  1 
ATOM   2812 H HE1  . HIS   A 1 119 ? 32.163 -8.483  9.694   1.00 19.16 ?  119 HIS   A HE1  1 
ATOM   2813 H HE2  . HIS   A 1 119 ? 31.480 -8.976  7.485   1.00 19.20 ?  119 HIS   A HE2  1 
ATOM   2814 N N    A GLU   A 1 120 ? 27.946 -13.595 12.254  0.42 12.10 ?  120 GLU   A N    1 
ATOM   2815 N N    B GLU   A 1 120 ? 27.947 -13.579 12.258  0.58 12.64 ?  120 GLU   A N    1 
ATOM   2816 C CA   A GLU   A 1 120 ? 26.990 -14.534 12.838  0.42 13.15 ?  120 GLU   A CA   1 
ATOM   2817 C CA   B GLU   A 1 120 ? 27.008 -14.517 12.871  0.58 14.53 ?  120 GLU   A CA   1 
ATOM   2818 C C    A GLU   A 1 120 ? 25.577 -13.965 12.912  0.42 12.46 ?  120 GLU   A C    1 
ATOM   2819 C C    B GLU   A 1 120 ? 25.587 -13.966 12.916  0.58 13.13 ?  120 GLU   A C    1 
ATOM   2820 O O    A GLU   A 1 120 ? 24.605 -14.724 12.796  0.42 12.58 ?  120 GLU   A O    1 
ATOM   2821 O O    B GLU   A 1 120 ? 24.620 -14.729 12.790  0.58 13.29 ?  120 GLU   A O    1 
ATOM   2822 C CB   A GLU   A 1 120 ? 27.451 -14.978 14.226  0.42 15.66 ?  120 GLU   A CB   1 
ATOM   2823 C CB   B GLU   A 1 120 ? 27.476 -14.881 14.280  0.58 18.58 ?  120 GLU   A CB   1 
ATOM   2824 C CG   A GLU   A 1 120 ? 28.599 -15.968 14.205  0.42 19.77 ?  120 GLU   A CG   1 
ATOM   2825 C CG   B GLU   A 1 120 ? 28.720 -15.746 14.311  0.58 24.44 ?  120 GLU   A CG   1 
ATOM   2826 C CD   A GLU   A 1 120 ? 28.712 -16.745 15.500  0.42 23.88 ?  120 GLU   A CD   1 
ATOM   2827 C CD   B GLU   A 1 120 ? 28.953 -16.374 15.668  0.58 30.00 ?  120 GLU   A CD   1 
ATOM   2828 O OE1  A GLU   A 1 120 ? 28.506 -16.149 16.578  0.42 25.32 ?  120 GLU   A OE1  1 
ATOM   2829 O OE1  B GLU   A 1 120 ? 28.345 -15.900 16.654  0.58 31.45 ?  120 GLU   A OE1  1 
ATOM   2830 O OE2  A GLU   A 1 120 ? 28.985 -17.961 15.435  0.42 25.33 -1 120 GLU   A OE2  1 
ATOM   2831 O OE2  B GLU   A 1 120 ? 29.739 -17.342 15.748  0.58 32.16 -1 120 GLU   A OE2  1 
ATOM   2832 H H    A GLU   A 1 120 ? 28.540 -13.298 12.800  0.42 14.55 ?  120 GLU   A H    1 
ATOM   2833 H H    B GLU   A 1 120 ? 28.542 -13.270 12.798  0.58 15.20 ?  120 GLU   A H    1 
ATOM   2834 H HA   A GLU   A 1 120 ? 26.957 -15.325 12.282  0.42 15.81 ?  120 GLU   A HA   1 
ATOM   2835 H HA   B GLU   A 1 120 ? 26.991 -15.333 12.351  0.58 17.47 ?  120 GLU   A HA   1 
ATOM   2836 H HB2  A GLU   A 1 120 ? 27.739 -14.202 14.729  0.42 18.82 ?  120 GLU   A HB2  1 
ATOM   2837 H HB2  B GLU   A 1 120 ? 27.673 -14.069 14.771  0.58 22.33 ?  120 GLU   A HB2  1 
ATOM   2838 H HB3  A GLU   A 1 120 ? 26.706 -15.406 14.683  0.42 18.82 ?  120 GLU   A HB3  1 
ATOM   2839 H HB3  B GLU   A 1 120 ? 26.768 -15.372 14.733  0.58 22.33 ?  120 GLU   A HB3  1 
ATOM   2840 H HG2  A GLU   A 1 120 ? 28.452 -16.616 13.502  0.42 23.75 ?  120 GLU   A HG2  1 
ATOM   2841 H HG2  B GLU   A 1 120 ? 28.634 -16.451 13.647  0.58 29.36 ?  120 GLU   A HG2  1 
ATOM   2842 H HG3  A GLU   A 1 120 ? 29.429 -15.487 14.048  0.42 23.75 ?  120 GLU   A HG3  1 
ATOM   2843 H HG3  B GLU   A 1 120 ? 29.494 -15.199 14.117  0.58 29.36 ?  120 GLU   A HG3  1 
ATOM   2844 N N    . VAL   A 1 121 ? 25.441 -12.656 13.125  1.00 12.18 ?  121 VAL   A N    1 
ATOM   2845 C CA   . VAL   A 1 121 ? 24.138 -12.004 13.242  1.00 12.37 ?  121 VAL   A CA   1 
ATOM   2846 C C    . VAL   A 1 121 ? 24.236 -10.622 12.601  1.00 11.49 ?  121 VAL   A C    1 
ATOM   2847 O O    . VAL   A 1 121 ? 25.191 -9.878  12.853  1.00 12.10 ?  121 VAL   A O    1 
ATOM   2848 C CB   . VAL   A 1 121 ? 23.688 -11.862 14.718  1.00 15.67 ?  121 VAL   A CB   1 
ATOM   2849 C CG1  . VAL   A 1 121 ? 22.284 -11.281 14.786  1.00 16.32 ?  121 VAL   A CG1  1 
ATOM   2850 C CG2  . VAL   A 1 121 ? 23.744 -13.174 15.478  1.00 18.11 ?  121 VAL   A CG2  1 
ATOM   2851 H H    A VAL   A 1 121 ? 26.105 -12.113 13.207  0.42 14.65 ?  121 VAL   A H    1 
ATOM   2852 H H    B VAL   A 1 121 ? 26.103 -12.110 13.202  0.58 14.65 ?  121 VAL   A H    1 
ATOM   2853 H HA   . VAL   A 1 121 ? 23.474 -12.524 12.765  1.00 14.87 ?  121 VAL   A HA   1 
ATOM   2854 H HB   . VAL   A 1 121 ? 24.281 -11.239 15.163  1.00 18.83 ?  121 VAL   A HB   1 
ATOM   2855 H HG11 . VAL   A 1 121 ? 21.967 -11.328 15.703  1.00 19.61 ?  121 VAL   A HG11 1 
ATOM   2856 H HG12 . VAL   A 1 121 ? 22.303 -10.357 14.493  1.00 19.61 ?  121 VAL   A HG12 1 
ATOM   2857 H HG13 . VAL   A 1 121 ? 21.697 -11.799 14.211  1.00 19.61 ?  121 VAL   A HG13 1 
ATOM   2858 H HG21 . VAL   A 1 121 ? 23.393 -13.035 16.379  1.00 21.76 ?  121 VAL   A HG21 1 
ATOM   2859 H HG22 . VAL   A 1 121 ? 23.195 -13.834 15.021  1.00 21.76 ?  121 VAL   A HG22 1 
ATOM   2860 H HG23 . VAL   A 1 121 ? 24.658 -13.480 15.528  1.00 21.76 ?  121 VAL   A HG23 1 
ATOM   2861 N N    . LEU   A 1 122 ? 23.233 -10.259 11.795  1.00 10.74 ?  122 LEU   A N    1 
ATOM   2862 C CA   . LEU   A 1 122 ? 23.222 -8.960  11.120  1.00 10.82 ?  122 LEU   A CA   1 
ATOM   2863 C C    . LEU   A 1 122 ? 21.817 -8.386  11.088  1.00 10.52 ?  122 LEU   A C    1 
ATOM   2864 O O    . LEU   A 1 122 ? 20.840 -9.121  10.943  1.00 11.50 ?  122 LEU   A O    1 
ATOM   2865 C CB   . LEU   A 1 122 ? 23.634 -9.055  9.647   1.00 12.50 ?  122 LEU   A CB   1 
ATOM   2866 C CG   . LEU   A 1 122 ? 24.860 -9.885  9.297   1.00 12.58 ?  122 LEU   A CG   1 
ATOM   2867 C CD1  . LEU   A 1 122 ? 24.487 -11.344 9.094   1.00 13.31 ?  122 LEU   A CD1  1 
ATOM   2868 C CD2  . LEU   A 1 122 ? 25.520 -9.335  8.055   1.00 11.92 ?  122 LEU   A CD2  1 
ATOM   2869 H H    . LEU   A 1 122 ? 22.538 -10.746 11.632  1.00 12.91 ?  122 LEU   A H    1 
ATOM   2870 H HA   . LEU   A 1 122 ? 23.814 -8.342  11.577  1.00 13.01 ?  122 LEU   A HA   1 
ATOM   2871 H HB2  . LEU   A 1 122 ? 22.892 -9.438  9.152   1.00 15.02 ?  122 LEU   A HB2  1 
ATOM   2872 H HB3  . LEU   A 1 122 ? 23.804 -8.161  9.324   1.00 15.02 ?  122 LEU   A HB3  1 
ATOM   2873 H HG   . LEU   A 1 122 ? 25.504 -9.838  10.022  1.00 15.13 ?  122 LEU   A HG   1 
ATOM   2874 H HD11 . LEU   A 1 122 ? 25.272 -11.841 8.813   1.00 16.00 ?  122 LEU   A HD11 1 
ATOM   2875 H HD12 . LEU   A 1 122 ? 24.156 -11.708 9.933   1.00 16.00 ?  122 LEU   A HD12 1 
ATOM   2876 H HD13 . LEU   A 1 122 ? 23.797 -11.406 8.415   1.00 16.00 ?  122 LEU   A HD13 1 
ATOM   2877 H HD21 . LEU   A 1 122 ? 26.281 -9.897  7.818   1.00 14.34 ?  122 LEU   A HD21 1 
ATOM   2878 H HD22 . LEU   A 1 122 ? 24.880 -9.331  7.327   1.00 14.34 ?  122 LEU   A HD22 1 
ATOM   2879 H HD23 . LEU   A 1 122 ? 25.827 -8.431  8.230   1.00 14.34 ?  122 LEU   A HD23 1 
ATOM   2880 N N    . LEU   A 1 123 ? 21.742 -7.055  11.164  1.00 10.27 ?  123 LEU   A N    1 
ATOM   2881 C CA   . LEU   A 1 123 ? 20.559 -6.279  10.790  1.00 10.10 ?  123 LEU   A CA   1 
ATOM   2882 C C    . LEU   A 1 123 ? 20.801 -5.752  9.379   1.00 9.70  ?  123 LEU   A C    1 
ATOM   2883 O O    . LEU   A 1 123 ? 21.846 -5.142  9.131   1.00 10.38 ?  123 LEU   A O    1 
ATOM   2884 C CB   . LEU   A 1 123 ? 20.415 -5.098  11.750  1.00 10.51 ?  123 LEU   A CB   1 
ATOM   2885 C CG   . LEU   A 1 123 ? 19.364 -4.052  11.401  1.00 11.24 ?  123 LEU   A CG   1 
ATOM   2886 C CD1  . LEU   A 1 123 ? 17.962 -4.662  11.393  1.00 12.49 ?  123 LEU   A CD1  1 
ATOM   2887 C CD2  . LEU   A 1 123 ? 19.439 -2.879  12.364  1.00 12.08 ?  123 LEU   A CD2  1 
ATOM   2888 H H    . LEU   A 1 123 ? 22.398 -6.559  11.424  1.00 12.35 ?  123 LEU   A H    1 
ATOM   2889 H HA   . LEU   A 1 123 ? 19.760 -6.829  10.810  1.00 12.15 ?  123 LEU   A HA   1 
ATOM   2890 H HB2  . LEU   A 1 123 ? 20.190 -5.442  12.628  1.00 12.64 ?  123 LEU   A HB2  1 
ATOM   2891 H HB3  . LEU   A 1 123 ? 21.265 -4.635  11.795  1.00 12.64 ?  123 LEU   A HB3  1 
ATOM   2892 H HG   . LEU   A 1 123 ? 19.531 -3.704  10.511  1.00 13.52 ?  123 LEU   A HG   1 
ATOM   2893 H HD11 . LEU   A 1 123 ? 17.313 -3.965  11.209  1.00 15.01 ?  123 LEU   A HD11 1 
ATOM   2894 H HD12 . LEU   A 1 123 ? 17.921 -5.344  10.706  1.00 15.01 ?  123 LEU   A HD12 1 
ATOM   2895 H HD13 . LEU   A 1 123 ? 17.788 -5.055  12.263  1.00 15.01 ?  123 LEU   A HD13 1 
ATOM   2896 H HD21 . LEU   A 1 123 ? 18.761 -2.229  12.129  1.00 14.53 ?  123 LEU   A HD21 1 
ATOM   2897 H HD22 . LEU   A 1 123 ? 19.285 -3.207  13.266  1.00 14.53 ?  123 LEU   A HD22 1 
ATOM   2898 H HD23 . LEU   A 1 123 ? 20.320 -2.483  12.302  1.00 14.53 ?  123 LEU   A HD23 1 
ATOM   2899 N N    A ALA   A 1 124 ? 19.842 -5.935  8.473   0.42 9.78  ?  124 ALA   A N    1 
ATOM   2900 N N    B ALA   A 1 124 ? 19.861 -5.990  8.464   0.29 9.78  ?  124 ALA   A N    1 
ATOM   2901 N N    C ALA   A 1 124 ? 19.858 -5.983  8.466   0.29 9.56  ?  124 ALA   A N    1 
ATOM   2902 C CA   A ALA   A 1 124 ? 20.130 -5.674  7.070   0.42 9.55  ?  124 ALA   A CA   1 
ATOM   2903 C CA   B ALA   A 1 124 ? 20.124 -5.705  7.060   0.29 9.93  ?  124 ALA   A CA   1 
ATOM   2904 C CA   C ALA   A 1 124 ? 20.120 -5.687  7.064   0.29 9.42  ?  124 ALA   A CA   1 
ATOM   2905 C C    A ALA   A 1 124 ? 18.891 -5.196  6.326   0.42 9.15  ?  124 ALA   A C    1 
ATOM   2906 C C    B ALA   A 1 124 ? 18.881 -5.225  6.330   0.29 10.13 ?  124 ALA   A C    1 
ATOM   2907 C C    C ALA   A 1 124 ? 18.867 -5.236  6.332   0.29 9.45  ?  124 ALA   A C    1 
ATOM   2908 O O    A ALA   A 1 124 ? 17.756 -5.501  6.723   0.42 10.25 ?  124 ALA   A O    1 
ATOM   2909 O O    B ALA   A 1 124 ? 17.754 -5.556  6.721   0.29 10.57 ?  124 ALA   A O    1 
ATOM   2910 O O    C ALA   A 1 124 ? 17.753 -5.655  6.677   0.29 9.46  ?  124 ALA   A O    1 
ATOM   2911 C CB   A ALA   A 1 124 ? 20.691 -6.922  6.383   0.42 10.20 ?  124 ALA   A CB   1 
ATOM   2912 C CB   B ALA   A 1 124 ? 20.679 -6.938  6.333   0.29 10.17 ?  124 ALA   A CB   1 
ATOM   2913 C CB   C ALA   A 1 124 ? 20.705 -6.905  6.338   0.29 9.59  ?  124 ALA   A CB   1 
ATOM   2914 H H    A ALA   A 1 124 ? 19.036 -6.197  8.641   0.42 11.77 ?  124 ALA   A H    1 
ATOM   2915 H H    B ALA   A 1 124 ? 19.076 -6.306  8.628   0.29 11.77 ?  124 ALA   A H    1 
ATOM   2916 H H    C ALA   A 1 124 ? 19.072 -6.301  8.630   0.29 11.50 ?  124 ALA   A H    1 
ATOM   2917 H HA   A ALA   A 1 124 ? 20.810 -4.986  7.027   0.42 11.49 ?  124 ALA   A HA   1 
ATOM   2918 H HA   B ALA   A 1 124 ? 20.792 -5.010  7.012   0.29 11.94 ?  124 ALA   A HA   1 
ATOM   2919 H HA   C ALA   A 1 124 ? 20.776 -4.978  7.024   0.29 11.33 ?  124 ALA   A HA   1 
ATOM   2920 H HB1  A ALA   A 1 124 ? 20.877 -6.721  5.455   0.42 12.27 ?  124 ALA   A HB1  1 
ATOM   2921 H HB1  B ALA   A 1 124 ? 20.843 -6.714  5.403   0.29 12.23 ?  124 ALA   A HB1  1 
ATOM   2922 H HB1  C ALA   A 1 124 ? 20.870 -6.677  5.410   0.29 11.53 ?  124 ALA   A HB1  1 
ATOM   2923 H HB2  A ALA   A 1 124 ? 21.514 -7.193  6.832   0.42 12.27 ?  124 ALA   A HB2  1 
ATOM   2924 H HB2  B ALA   A 1 124 ? 21.511 -7.208  6.758   0.29 12.23 ?  124 ALA   A HB2  1 
ATOM   2925 H HB2  C ALA   A 1 124 ? 21.539 -7.160  6.768   0.29 11.53 ?  124 ALA   A HB2  1 
ATOM   2926 H HB3  A ALA   A 1 124 ? 20.039 -7.639  6.444   0.42 12.27 ?  124 ALA   A HB3  1 
ATOM   2927 H HB3  B ALA   A 1 124 ? 20.033 -7.660  6.389   0.29 12.23 ?  124 ALA   A HB3  1 
ATOM   2928 H HB3  C ALA   A 1 124 ? 20.073 -7.641  6.390   0.29 11.53 ?  124 ALA   A HB3  1 
ATOM   2929 N N    A PRO   A 1 125 ? 19.083 -4.474  5.220   0.42 8.43  ?  125 PRO   A N    1 
ATOM   2930 N N    B PRO   A 1 125 ? 19.063 -4.459  5.245   0.29 10.41 ?  125 PRO   A N    1 
ATOM   2931 N N    C PRO   A 1 125 ? 19.023 -4.411  5.301   0.29 10.10 ?  125 PRO   A N    1 
ATOM   2932 C CA   A PRO   A 1 125 ? 18.015 -4.221  4.255   0.42 9.03  ?  125 PRO   A CA   1 
ATOM   2933 C CA   B PRO   A 1 125 ? 17.965 -4.166  4.324   0.29 10.89 ?  125 PRO   A CA   1 
ATOM   2934 C CA   C PRO   A 1 125 ? 17.942 -4.152  4.352   0.29 10.74 ?  125 PRO   A CA   1 
ATOM   2935 C C    A PRO   A 1 125 ? 18.041 -5.293  3.172   0.42 9.17  ?  125 PRO   A C    1 
ATOM   2936 C C    B PRO   A 1 125 ? 17.982 -5.174  3.186   0.29 11.13 ?  125 PRO   A C    1 
ATOM   2937 C C    C PRO   A 1 125 ? 18.004 -5.179  3.225   0.29 10.96 ?  125 PRO   A C    1 
ATOM   2938 O O    A PRO   A 1 125 ? 18.995 -6.061  3.045   0.42 9.88  ?  125 PRO   A O    1 
ATOM   2939 O O    B PRO   A 1 125 ? 18.901 -5.995  3.111   0.29 11.28 ?  125 PRO   A O    1 
ATOM   2940 O O    C PRO   A 1 125 ? 18.957 -5.951  3.104   0.29 11.08 ?  125 PRO   A O    1 
ATOM   2941 C CB   A PRO   A 1 125 ? 18.480 -2.898  3.635   0.42 8.68  ?  125 PRO   A CB   1 
ATOM   2942 C CB   B PRO   A 1 125 ? 18.344 -2.774  3.812   0.29 10.86 ?  125 PRO   A CB   1 
ATOM   2943 C CB   C PRO   A 1 125 ? 18.324 -2.767  3.816   0.29 10.87 ?  125 PRO   A CB   1 
ATOM   2944 C CG   A PRO   A 1 125 ? 19.991 -3.108  3.517   0.42 7.92  ?  125 PRO   A CG   1 
ATOM   2945 C CG   B PRO   A 1 125 ? 19.866 -2.867  3.709   0.29 11.07 ?  125 PRO   A CG   1 
ATOM   2946 C CG   C PRO   A 1 125 ? 19.832 -2.838  3.750   0.29 11.14 ?  125 PRO   A CG   1 
ATOM   2947 C CD   A PRO   A 1 125 ? 20.369 -3.911  4.760   0.42 8.33  ?  125 PRO   A CD   1 
ATOM   2948 C CD   B PRO   A 1 125 ? 20.320 -3.833  4.793   0.29 10.88 ?  125 PRO   A CD   1 
ATOM   2949 C CD   C PRO   A 1 125 ? 20.255 -3.687  4.931   0.29 10.87 ?  125 PRO   A CD   1 
ATOM   2950 H HA   A PRO   A 1 125 ? 17.142 -4.151  4.668   0.42 10.87 ?  125 PRO   A HA   1 
ATOM   2951 H HA   B PRO   A 1 125 ? 17.103 -4.150  4.770   0.29 13.09 ?  125 PRO   A HA   1 
ATOM   2952 H HA   C PRO   A 1 125 ? 17.073 -4.136  4.780   0.29 12.92 ?  125 PRO   A HA   1 
ATOM   2953 H HB2  A PRO   A 1 125 ? 18.067 -2.781  2.762   0.42 10.44 ?  125 PRO   A HB2  1 
ATOM   2954 H HB2  B PRO   A 1 125 ? 17.943 -2.613  2.943   0.29 13.06 ?  125 PRO   A HB2  1 
ATOM   2955 H HB2  C PRO   A 1 125 ? 17.943 -2.629  2.935   0.29 13.07 ?  125 PRO   A HB2  1 
ATOM   2956 H HB3  A PRO   A 1 125 ? 18.268 -2.166  4.228   0.42 10.44 ?  125 PRO   A HB3  1 
ATOM   2957 H HB3  B PRO   A 1 125 ? 18.077 -2.094  4.453   0.29 13.06 ?  125 PRO   A HB3  1 
ATOM   2958 H HB3  C PRO   A 1 125 ? 18.036 -2.075  4.434   0.29 13.07 ?  125 PRO   A HB3  1 
ATOM   2959 H HG2  A PRO   A 1 125 ? 20.191 -3.605  2.703   0.42 9.53  ?  125 PRO   A HG2  1 
ATOM   2960 H HG2  B PRO   A 1 125 ? 20.110 -3.203  2.833   0.29 13.31 ?  125 PRO   A HG2  1 
ATOM   2961 H HG2  C PRO   A 1 125 ? 20.103 -3.254  2.916   0.29 13.40 ?  125 PRO   A HG2  1 
ATOM   2962 H HG3  A PRO   A 1 125 ? 20.436 -2.245  3.504   0.42 9.53  ?  125 PRO   A HG3  1 
ATOM   2963 H HG3  B PRO   A 1 125 ? 20.255 -1.991  3.855   0.29 13.31 ?  125 PRO   A HG3  1 
ATOM   2964 H HG3  C PRO   A 1 125 ? 20.207 -1.945  3.821   0.29 13.40 ?  125 PRO   A HG3  1 
ATOM   2965 H HD2  A PRO   A 1 125 ? 20.995 -4.615  4.528   0.42 10.03 ?  125 PRO   A HD2  1 
ATOM   2966 H HD2  B PRO   A 1 125 ? 20.919 -4.503  4.421   0.29 13.08 ?  125 PRO   A HD2  1 
ATOM   2967 H HD2  C PRO   A 1 125 ? 20.952 -4.311  4.667   0.29 13.07 ?  125 PRO   A HD2  1 
ATOM   2968 H HD3  A PRO   A 1 125 ? 20.736 -3.321  5.438   0.42 10.03 ?  125 PRO   A HD3  1 
ATOM   2969 H HD3  B PRO   A 1 125 ? 20.741 -3.349  5.521   0.29 13.08 ?  125 PRO   A HD3  1 
ATOM   2970 H HD3  C PRO   A 1 125 ? 20.546 -3.124  5.665   0.29 13.07 ?  125 PRO   A HD3  1 
ATOM   2971 N N    A LEU   A 1 126 ? 16.993 -5.299  2.352   0.42 9.78  ?  126 LEU   A N    1 
ATOM   2972 N N    B LEU   A 1 126 ? 17.002 -5.125  2.290   0.29 11.61 ?  126 LEU   A N    1 
ATOM   2973 N N    C LEU   A 1 126 ? 16.970 -5.167  2.386   0.29 11.60 ?  126 LEU   A N    1 
ATOM   2974 C CA   A LEU   A 1 126 ? 17.033 -6.069  1.116   0.42 10.60 ?  126 LEU   A CA   1 
ATOM   2975 C CA   B LEU   A 1 126 ? 17.080 -5.902  1.060   0.29 11.35 ?  126 LEU   A CA   1 
ATOM   2976 C CA   C LEU   A 1 126 ? 17.045 -5.904  1.132   0.29 11.96 ?  126 LEU   A CA   1 
ATOM   2977 C C    A LEU   A 1 126 ? 17.947 -5.393  0.101   0.42 11.31 ?  126 LEU   A C    1 
ATOM   2978 C C    B LEU   A 1 126 ? 18.004 -5.206  0.065   0.29 11.13 ?  126 LEU   A C    1 
ATOM   2979 C C    C LEU   A 1 126 ? 17.990 -5.183  0.178   0.29 12.36 ?  126 LEU   A C    1 
ATOM   2980 O O    A LEU   A 1 126 ? 17.674 -4.275  -0.356  0.42 11.90 ?  126 LEU   A O    1 
ATOM   2981 O O    B LEU   A 1 126 ? 17.934 -3.987  -0.118  0.29 11.92 ?  126 LEU   A O    1 
ATOM   2982 O O    C LEU   A 1 126 ? 17.955 -3.955  0.057   0.29 13.35 ?  126 LEU   A O    1 
ATOM   2983 C CB   A LEU   A 1 126 ? 15.632 -6.248  0.549   0.42 11.38 ?  126 LEU   A CB   1 
ATOM   2984 C CB   B LEU   A 1 126 ? 15.692 -6.055  0.442   0.29 11.96 ?  126 LEU   A CB   1 
ATOM   2985 C CB   C LEU   A 1 126 ? 15.661 -6.015  0.496   0.29 12.59 ?  126 LEU   A CB   1 
ATOM   2986 C CG   A LEU   A 1 126 ? 14.774 -7.216  1.357   0.42 12.41 ?  126 LEU   A CG   1 
ATOM   2987 C CG   B LEU   A 1 126 ? 14.700 -6.998  1.119   0.29 12.60 ?  126 LEU   A CG   1 
ATOM   2988 C CG   C LEU   A 1 126 ? 14.675 -6.995  1.130   0.29 13.21 ?  126 LEU   A CG   1 
ATOM   2989 C CD1  A LEU   A 1 126 ? 13.325 -7.120  0.933   0.42 13.10 ?  126 LEU   A CD1  1 
ATOM   2990 C CD1  B LEU   A 1 126 ? 13.365 -6.930  0.399   0.29 13.05 ?  126 LEU   A CD1  1 
ATOM   2991 C CD1  C LEU   A 1 126 ? 13.352 -6.938  0.388   0.29 13.63 ?  126 LEU   A CD1  1 
ATOM   2992 C CD2  A LEU   A 1 126 ? 15.286 -8.648  1.209   0.42 12.87 ?  126 LEU   A CD2  1 
ATOM   2993 C CD2  B LEU   A 1 126 ? 15.219 -8.432  1.142   0.29 13.08 ?  126 LEU   A CD2  1 
ATOM   2994 C CD2  C LEU   A 1 126 ? 15.230 -8.414  1.120   0.29 13.69 ?  126 LEU   A CD2  1 
ATOM   2995 H H    A LEU   A 1 126 ? 16.271 -4.858  2.475   0.42 11.77 ?  126 LEU   A H    1 
ATOM   2996 H H    B LEU   A 1 126 ? 16.291 -4.651  2.370   0.29 13.96 ?  126 LEU   A H    1 
ATOM   2997 H H    C LEU   A 1 126 ? 16.236 -4.739  2.507   0.29 13.95 ?  126 LEU   A H    1 
ATOM   2998 H HA   A LEU   A 1 126 ? 17.399 -6.943  1.298   0.42 12.75 ?  126 LEU   A HA   1 
ATOM   2999 H HA   B LEU   A 1 126 ? 17.434 -6.783  1.253   0.29 13.65 ?  126 LEU   A HA   1 
ATOM   3000 H HA   C LEU   A 1 126 ? 17.387 -6.797  1.295   0.29 14.38 ?  126 LEU   A HA   1 
ATOM   3001 H HB2  A LEU   A 1 126 ? 15.180 -5.389  0.541   0.42 13.69 ?  126 LEU   A HB2  1 
ATOM   3002 H HB2  B LEU   A 1 126 ? 15.275 -5.179  0.426   0.29 14.38 ?  126 LEU   A HB2  1 
ATOM   3003 H HB2  C LEU   A 1 126 ? 15.243 -5.141  0.525   0.29 15.14 ?  126 LEU   A HB2  1 
ATOM   3004 H HB3  A LEU   A 1 126 ? 15.696 -6.592  -0.357  0.42 13.69 ?  126 LEU   A HB3  1 
ATOM   3005 H HB3  B LEU   A 1 126 ? 15.803 -6.371  -0.465  0.29 14.38 ?  126 LEU   A HB3  1 
ATOM   3006 H HB3  C LEU   A 1 126 ? 15.771 -6.287  -0.428  0.29 15.14 ?  126 LEU   A HB3  1 
ATOM   3007 H HG   A LEU   A 1 126 ? 14.827 -6.978  2.295   0.42 14.91 ?  126 LEU   A HG   1 
ATOM   3008 H HG   B LEU   A 1 126 ? 14.559 -6.715  2.036   0.29 15.15 ?  126 LEU   A HG   1 
ATOM   3009 H HG   C LEU   A 1 126 ? 14.513 -6.741  2.052   0.29 15.88 ?  126 LEU   A HG   1 
ATOM   3010 H HD11 A LEU   A 1 126 ? 12.797 -7.743  1.459   0.42 15.75 ?  126 LEU   A HD11 1 
ATOM   3011 H HD11 B LEU   A 1 126 ? 12.739 -7.535  0.832   0.29 15.68 ?  126 LEU   A HD11 1 
ATOM   3012 H HD11 C LEU   A 1 126 ? 12.730 -7.562  0.798   0.29 16.38 ?  126 LEU   A HD11 1 
ATOM   3013 H HD12 A LEU   A 1 126 ? 13.010 -6.214  1.085   0.42 15.75 ?  126 LEU   A HD12 1 
ATOM   3014 H HD12 B LEU   A 1 126 ? 13.028 -6.022  0.439   0.29 15.68 ?  126 LEU   A HD12 1 
ATOM   3015 H HD12 C LEU   A 1 126 ? 12.998 -6.037  0.443   0.29 16.38 ?  126 LEU   A HD12 1 
ATOM   3016 H HD13 A LEU   A 1 126 ? 13.253 -7.341  -0.009  0.42 15.75 ?  126 LEU   A HD13 1 
ATOM   3017 H HD13 B LEU   A 1 126 ? 13.490 -7.197  -0.526  0.29 15.68 ?  126 LEU   A HD13 1 
ATOM   3018 H HD13 C LEU   A 1 126 ? 13.498 -7.181  -0.540  0.29 16.38 ?  126 LEU   A HD13 1 
ATOM   3019 H HD21 A LEU   A 1 126 ? 14.631 -9.259  1.581   0.42 15.48 ?  126 LEU   A HD21 1 
ATOM   3020 H HD21 B LEU   A 1 126 ? 14.522 -9.018  1.476   0.29 15.73 ?  126 LEU   A HD21 1 
ATOM   3021 H HD21 C LEU   A 1 126 ? 14.525 -9.034  1.362   0.29 16.45 ?  126 LEU   A HD21 1 
ATOM   3022 H HD22 A LEU   A 1 126 ? 15.420 -8.840  0.267   0.42 15.48 ?  126 LEU   A HD22 1 
ATOM   3023 H HD22 B LEU   A 1 126 ? 15.465 -8.693  0.239   0.29 15.73 ?  126 LEU   A HD22 1 
ATOM   3024 H HD22 C LEU   A 1 126 ? 15.557 -8.617  0.228   0.29 16.45 ?  126 LEU   A HD22 1 
ATOM   3025 H HD23 A LEU   A 1 126 ? 16.127 -8.736  1.686   0.42 15.48 ?  126 LEU   A HD23 1 
ATOM   3026 H HD23 B LEU   A 1 126 ? 15.996 -8.478  1.721   0.29 15.73 ?  126 LEU   A HD23 1 
ATOM   3027 H HD23 C LEU   A 1 126 ? 15.958 -8.472  1.759   0.29 16.45 ?  126 LEU   A HD23 1 
ATOM   3028 N N    A LEU   A 1 127 ? 19.020 -6.094  -0.259  0.42 11.60 ?  127 LEU   A N    1 
ATOM   3029 N N    B LEU   A 1 127 ? 18.866 -5.986  -0.585  0.29 10.38 ?  127 LEU   A N    1 
ATOM   3030 N N    C LEU   A 1 127 ? 18.846 -5.945  -0.495  0.29 12.00 ?  127 LEU   A N    1 
ATOM   3031 C CA   A LEU   A 1 127 ? 19.998 -5.584  -1.206  0.42 11.79 ?  127 LEU   A CA   1 
ATOM   3032 C CA   B LEU   A 1 127 ? 19.844 -5.446  -1.519  0.29 10.82 ?  127 LEU   A CA   1 
ATOM   3033 C CA   C LEU   A 1 127 ? 19.844 -5.357  -1.374  0.29 12.35 ?  127 LEU   A CA   1 
ATOM   3034 C C    A LEU   A 1 127 ? 19.376 -5.395  -2.584  0.42 11.45 ?  127 LEU   A C    1 
ATOM   3035 C C    B LEU   A 1 127 ? 19.344 -5.569  -2.956  0.29 10.90 ?  127 LEU   A C    1 
ATOM   3036 C C    C LEU   A 1 127 ? 19.336 -5.246  -2.807  0.29 12.51 ?  127 LEU   A C    1 
ATOM   3037 O O    A LEU   A 1 127 ? 18.469 -6.125  -2.997  0.42 11.46 ?  127 LEU   A O    1 
ATOM   3038 O O    B LEU   A 1 127 ? 18.590 -6.484  -3.296  0.29 10.42 ?  127 LEU   A O    1 
ATOM   3039 O O    C LEU   A 1 127 ? 18.547 -6.068  -3.283  0.29 12.63 ?  127 LEU   A O    1 
ATOM   3040 C CB   A LEU   A 1 127 ? 21.171 -6.560  -1.316  0.42 11.88 ?  127 LEU   A CB   1 
ATOM   3041 C CB   B LEU   A 1 127 ? 21.183 -6.177  -1.379  0.29 11.28 ?  127 LEU   A CB   1 
ATOM   3042 C CB   C LEU   A 1 127 ? 21.139 -6.174  -1.351  0.29 12.62 ?  127 LEU   A CB   1 
ATOM   3043 C CG   A LEU   A 1 127 ? 21.955 -6.798  -0.027  0.42 12.41 ?  127 LEU   A CG   1 
ATOM   3044 C CG   B LEU   A 1 127 ? 21.900 -6.141  -0.024  0.29 11.70 ?  127 LEU   A CG   1 
ATOM   3045 C CG   C LEU   A 1 127 ? 21.908 -6.169  -0.027  0.29 12.94 ?  127 LEU   A CG   1 
ATOM   3046 C CD1  A LEU   A 1 127 ? 23.064 -7.806  -0.276  0.42 12.58 ?  127 LEU   A CD1  1 
ATOM   3047 C CD1  B LEU   A 1 127 ? 23.108 -7.063  -0.050  0.29 12.12 ?  127 LEU   A CD1  1 
ATOM   3048 C CD1  C LEU   A 1 127 ? 23.109 -7.098  -0.088  0.29 13.33 ?  127 LEU   A CD1  1 
ATOM   3049 C CD2  A LEU   A 1 127 ? 22.525 -5.496  0.515   0.42 13.11 ?  127 LEU   A CD2  1 
ATOM   3050 C CD2  B LEU   A 1 127 ? 22.318 -4.723  0.344   0.29 12.61 ?  127 LEU   A CD2  1 
ATOM   3051 C CD2  C LEU   A 1 127 ? 22.341 -4.754  0.341   0.29 13.70 ?  127 LEU   A CD2  1 
ATOM   3052 H H    A LEU   A 1 127 ? 19.208 -6.877  0.046   0.42 13.95 ?  127 LEU   A H    1 
ATOM   3053 H H    B LEU   A 1 127 ? 18.905 -6.846  -0.500  0.29 12.48 ?  127 LEU   A H    1 
ATOM   3054 H H    C LEU   A 1 127 ? 18.877 -6.806  -0.451  0.29 14.43 ?  127 LEU   A H    1 
ATOM   3055 H HA   A LEU   A 1 127 ? 20.341 -4.731  -0.895  0.42 14.17 ?  127 LEU   A HA   1 
ATOM   3056 H HA   B LEU   A 1 127 ? 19.988 -4.509  -1.323  0.29 13.01 ?  127 LEU   A HA   1 
ATOM   3057 H HA   C LEU   A 1 127 ? 20.047 -4.463  -1.058  0.29 14.85 ?  127 LEU   A HA   1 
ATOM   3058 H HB2  A LEU   A 1 127 ? 20.831 -7.421  -1.611  0.42 14.29 ?  127 LEU   A HB2  1 
ATOM   3059 H HB2  B LEU   A 1 127 ? 21.035 -7.111  -1.588  0.29 13.57 ?  127 LEU   A HB2  1 
ATOM   3060 H HB2  C LEU   A 1 127 ? 20.924 -7.096  -1.560  0.29 15.17 ?  127 LEU   A HB2  1 
ATOM   3061 H HB3  A LEU   A 1 127 ? 21.798 -6.219  -1.975  0.42 14.29 ?  127 LEU   A HB3  1 
ATOM   3062 H HB3  B LEU   A 1 127 ? 21.796 -5.800  -2.026  0.29 13.57 ?  127 LEU   A HB3  1 
ATOM   3063 H HB3  C LEU   A 1 127 ? 21.733 -5.819  -2.033  0.29 15.17 ?  127 LEU   A HB3  1 
ATOM   3064 H HG   A LEU   A 1 127 ? 21.360 -7.171  0.643   0.42 14.91 ?  127 LEU   A HG   1 
ATOM   3065 H HG   B LEU   A 1 127 ? 21.299 -6.464  0.664   0.29 14.06 ?  127 LEU   A HG   1 
ATOM   3066 H HG   C LEU   A 1 127 ? 21.323 -6.493  0.674   0.29 15.56 ?  127 LEU   A HG   1 
ATOM   3067 H HD11 A LEU   A 1 127 ? 23.549 -7.953  0.551   0.42 15.12 ?  127 LEU   A HD11 1 
ATOM   3068 H HD11 B LEU   A 1 127 ? 23.552 -7.028  0.812   0.29 14.57 ?  127 LEU   A HD11 1 
ATOM   3069 H HD11 C LEU   A 1 127 ? 23.568 -7.075  0.767   0.29 16.02 ?  127 LEU   A HD11 1 
ATOM   3070 H HD12 A LEU   A 1 127 ? 22.672 -8.638  -0.583  0.42 15.12 ?  127 LEU   A HD12 1 
ATOM   3071 H HD12 B LEU   A 1 127 ? 22.809 -7.969  -0.231  0.29 14.57 ?  127 LEU   A HD12 1 
ATOM   3072 H HD12 C LEU   A 1 127 ? 22.801 -8.000  -0.273  0.29 16.02 ?  127 LEU   A HD12 1 
ATOM   3073 H HD13 A LEU   A 1 127 ? 23.663 -7.453  -0.952  0.42 15.12 ?  127 LEU   A HD13 1 
ATOM   3074 H HD13 B LEU   A 1 127 ? 23.715 -6.770  -0.747  0.29 14.57 ?  127 LEU   A HD13 1 
ATOM   3075 H HD13 C LEU   A 1 127 ? 23.705 -6.800  -0.792  0.29 16.02 ?  127 LEU   A HD13 1 
ATOM   3076 H HD21 A LEU   A 1 127 ? 23.141 -5.697  1.236   0.42 15.76 ?  127 LEU   A HD21 1 
ATOM   3077 H HD21 B LEU   A 1 127 ? 22.788 -4.742  1.194   0.29 15.16 ?  127 LEU   A HD21 1 
ATOM   3078 H HD21 C LEU   A 1 127 ? 22.965 -4.798  1.082   0.29 16.46 ?  127 LEU   A HD21 1 
ATOM   3079 H HD22 A LEU   A 1 127 ? 22.994 -5.038  -0.202  0.42 15.76 ?  127 LEU   A HD22 1 
ATOM   3080 H HD22 B LEU   A 1 127 ? 22.904 -4.376  -0.348  0.29 15.16 ?  127 LEU   A HD22 1 
ATOM   3081 H HD22 C LEU   A 1 127 ? 22.768 -4.344  -0.428  0.29 16.46 ?  127 LEU   A HD22 1 
ATOM   3082 H HD23 A LEU   A 1 127 ? 21.798 -4.945  0.840   0.42 15.76 ?  127 LEU   A HD23 1 
ATOM   3083 H HD23 B LEU   A 1 127 ? 21.526 -4.170  0.417   0.29 15.16 ?  127 LEU   A HD23 1 
ATOM   3084 H HD23 C LEU   A 1 127 ? 21.559 -4.241  0.597   0.29 16.46 ?  127 LEU   A HD23 1 
ATOM   3085 N N    A SER   A 1 128 ? 19.886 -4.389  -3.287  0.42 11.82 ?  128 SER   A N    1 
ATOM   3086 N N    B SER   A 1 128 ? 19.775 -4.629  -3.799  0.29 11.70 ?  128 SER   A N    1 
ATOM   3087 N N    C SER   A 1 128 ? 19.792 -4.190  -3.482  0.29 12.78 ?  128 SER   A N    1 
ATOM   3088 C CA   A SER   A 1 128 ? 19.484 -4.017  -4.639  0.42 12.10 ?  128 SER   A CA   1 
ATOM   3089 C CA   B SER   A 1 128 ? 19.412 -4.605  -5.218  0.29 13.25 ?  128 SER   A CA   1 
ATOM   3090 C CA   C SER   A 1 128 ? 19.626 -3.982  -4.918  0.29 12.91 ?  128 SER   A CA   1 
ATOM   3091 C C    A SER   A 1 128 ? 18.034 -3.560  -4.746  0.42 12.52 ?  128 SER   A C    1 
ATOM   3092 C C    B SER   A 1 128 ? 17.899 -4.631  -5.395  0.29 15.75 ?  128 SER   A C    1 
ATOM   3093 C C    C SER   A 1 128 ? 18.212 -3.625  -5.353  0.29 13.12 ?  128 SER   A C    1 
ATOM   3094 O O    A SER   A 1 128 ? 17.589 -3.212  -5.843  0.42 13.37 ?  128 SER   A O    1 
ATOM   3095 O O    B SER   A 1 128 ? 17.343 -5.477  -6.101  0.29 16.23 ?  128 SER   A O    1 
ATOM   3096 O O    C SER   A 1 128 ? 18.002 -3.297  -6.524  0.29 12.12 ?  128 SER   A O    1 
ATOM   3097 C CB   A SER   A 1 128 ? 19.798 -5.105  -5.675  0.42 12.00 ?  128 SER   A CB   1 
ATOM   3098 C CB   B SER   A 1 128 ? 20.061 -5.753  -5.993  0.29 12.39 ?  128 SER   A CB   1 
ATOM   3099 C CB   C SER   A 1 128 ? 20.119 -5.188  -5.716  0.29 12.58 ?  128 SER   A CB   1 
ATOM   3100 O OG   A SER   A 1 128 ? 21.197 -5.328  -5.760  0.42 11.66 ?  128 SER   A OG   1 
ATOM   3101 O OG   B SER   A 1 128 ? 21.471 -5.694  -5.915  0.29 12.02 ?  128 SER   A OG   1 
ATOM   3102 O OG   C SER   A 1 128 ? 21.529 -5.205  -5.738  0.29 12.52 ?  128 SER   A OG   1 
ATOM   3103 H H    A SER   A 1 128 ? 20.501 -3.875  -2.979  0.42 14.21 ?  128 SER   A H    1 
ATOM   3104 H H    B SER   A 1 128 ? 20.287 -3.980  -3.565  0.29 14.07 ?  128 SER   A H    1 
ATOM   3105 H H    C SER   A 1 128 ? 20.230 -3.553  -3.108  0.29 15.36 ?  128 SER   A H    1 
ATOM   3106 H HA   A SER   A 1 128 ? 20.019 -3.257  -4.880  0.42 14.55 ?  128 SER   A HA   1 
ATOM   3107 H HA   B SER   A 1 128 ? 19.747 -3.778  -5.601  0.29 15.93 ?  128 SER   A HA   1 
ATOM   3108 H HA   C SER   A 1 128 ? 20.183 -3.233  -5.169  0.29 15.52 ?  128 SER   A HA   1 
ATOM   3109 H HB2  A SER   A 1 128 ? 19.354 -5.926  -5.431  0.42 14.43 ?  128 SER   A HB2  1 
ATOM   3110 H HB2  B SER   A 1 128 ? 19.756 -6.593  -5.618  0.29 14.89 ?  128 SER   A HB2  1 
ATOM   3111 H HB2  C SER   A 1 128 ? 19.799 -6.003  -5.307  0.29 15.12 ?  128 SER   A HB2  1 
ATOM   3112 H HB3  A SER   A 1 128 ? 19.482 -4.802  -6.549  0.42 14.43 ?  128 SER   A HB3  1 
ATOM   3113 H HB3  B SER   A 1 128 ? 19.787 -5.692  -6.925  0.29 14.89 ?  128 SER   A HB3  1 
ATOM   3114 H HB3  C SER   A 1 128 ? 19.785 -5.118  -6.626  0.29 15.12 ?  128 SER   A HB3  1 
ATOM   3115 H HG   A SER   A 1 128 ? 21.591 -4.611  -5.957  0.42 14.02 ?  128 SER   A HG   1 
ATOM   3116 H HG   B SER   A 1 128 ? 21.741 -4.973  -6.250  0.29 14.45 ?  128 SER   A HG   1 
ATOM   3117 H HG   C SER   A 1 128 ? 21.800 -5.858  -6.182  0.29 15.05 ?  128 SER   A HG   1 
ATOM   3118 N N    A ALA   A 1 129 ? 17.292 -3.546  -3.636  0.42 13.82 ?  129 ALA   A N    1 
ATOM   3119 N N    B ALA   A 1 129 ? 17.227 -3.682  -4.753  0.29 17.71 ?  129 ALA   A N    1 
ATOM   3120 N N    C ALA   A 1 129 ? 17.239 -3.674  -4.441  0.29 14.93 ?  129 ALA   A N    1 
ATOM   3121 C CA   A ALA   A 1 129 ? 15.935 -3.016  -3.633  0.42 15.50 ?  129 ALA   A CA   1 
ATOM   3122 C CA   B ALA   A 1 129 ? 15.775 -3.633  -4.807  0.29 19.80 ?  129 ALA   A CA   1 
ATOM   3123 C CA   C ALA   A 1 129 ? 15.846 -3.431  -4.794  0.29 17.35 ?  129 ALA   A CA   1 
ATOM   3124 C C    A ALA   A 1 129 ? 15.987 -1.492  -3.631  0.42 15.58 ?  129 ALA   A C    1 
ATOM   3125 C C    B ALA   A 1 129 ? 15.304 -2.227  -4.457  0.29 21.51 ?  129 ALA   A C    1 
ATOM   3126 C C    C ALA   A 1 129 ? 15.331 -2.078  -4.305  0.29 19.16 ?  129 ALA   A C    1 
ATOM   3127 O O    A ALA   A 1 129 ? 17.050 -0.876  -3.754  0.42 16.29 ?  129 ALA   A O    1 
ATOM   3128 O O    B ALA   A 1 129 ? 16.101 -1.293  -4.319  0.29 22.25 ?  129 ALA   A O    1 
ATOM   3129 O O    C ALA   A 1 129 ? 14.117 -1.891  -4.178  0.29 19.99 ?  129 ALA   A O    1 
ATOM   3130 C CB   A ALA   A 1 129 ? 15.140 -3.579  -2.458  0.42 16.50 ?  129 ALA   A CB   1 
ATOM   3131 C CB   B ALA   A 1 129 ? 15.170 -4.669  -3.858  0.29 19.93 ?  129 ALA   A CB   1 
ATOM   3132 C CB   C ALA   A 1 129 ? 14.959 -4.558  -4.270  0.29 18.06 ?  129 ALA   A CB   1 
ATOM   3133 H H    A ALA   A 1 129 ? 17.542 -3.834  -2.861  0.42 16.62 ?  129 ALA   A H    1 
ATOM   3134 H H    B ALA   A 1 129 ? 17.586 -3.052  -4.280  0.29 21.28 ?  129 ALA   A H    1 
ATOM   3135 H H    C ALA   A 1 129 ? 17.363 -3.841  -3.608  0.29 17.95 ?  129 ALA   A H    1 
ATOM   3136 H HA   A ALA   A 1 129 ? 15.492 -3.268  -4.448  0.42 18.63 ?  129 ALA   A HA   1 
ATOM   3137 H HA   B ALA   A 1 129 ? 15.482 -3.840  -5.711  0.29 23.79 ?  129 ALA   A HA   1 
ATOM   3138 H HA   C ALA   A 1 129 ? 15.773 -3.444  -5.764  0.29 20.85 ?  129 ALA   A HA   1 
ATOM   3139 H HB1  A ALA   A 1 129 ? 14.239 -3.216  -2.481  0.42 19.82 ?  129 ALA   A HB1  1 
ATOM   3140 H HB1  B ALA   A 1 129 ? 14.206 -4.659  -3.953  0.29 23.95 ?  129 ALA   A HB1  1 
ATOM   3141 H HB1  C ALA   A 1 129 ? 14.040 -4.377  -4.524  0.29 21.70 ?  129 ALA   A HB1  1 
ATOM   3142 H HB2  A ALA   A 1 129 ? 15.108 -4.545  -2.536  0.42 19.82 ?  129 ALA   A HB2  1 
ATOM   3143 H HB2  B ALA   A 1 129 ? 15.518 -5.541  -4.089  0.29 23.95 ?  129 ALA   A HB2  1 
ATOM   3144 H HB2  C ALA   A 1 129 ? 15.253 -5.395  -4.661  0.29 21.70 ?  129 ALA   A HB2  1 
ATOM   3145 H HB3  A ALA   A 1 129 ? 15.573 -3.330  -1.626  0.42 19.82 ?  129 ALA   A HB3  1 
ATOM   3146 H HB3  B ALA   A 1 129 ? 15.418 -4.440  -2.949  0.29 23.95 ?  129 ALA   A HB3  1 
ATOM   3147 H HB3  C ALA   A 1 129 ? 15.037 -4.594  -3.306  0.29 21.70 ?  129 ALA   A HB3  1 
ATOM   3148 N N    A GLY   A 1 130 ? 14.824 -0.862  -3.518  0.42 15.34 ?  130 GLY   A N    1 
ATOM   3149 N N    B GLY   A 1 130 ? 13.991 -2.094  -4.322  0.29 22.23 ?  130 GLY   A N    1 
ATOM   3150 N N    C GLY   A 1 130 ? 16.223 -1.131  -4.037  0.29 19.76 ?  130 GLY   A N    1 
ATOM   3151 C CA   A GLY   A 1 130 ? 14.796 0.587   -3.468  0.42 15.77 ?  130 GLY   A CA   1 
ATOM   3152 C CA   B GLY   A 1 130 ? 13.311 -0.886  -3.909  0.29 22.29 ?  130 GLY   A CA   1 
ATOM   3153 C CA   C GLY   A 1 130 ? 15.798 0.201   -3.658  0.29 19.61 ?  130 GLY   A CA   1 
ATOM   3154 C C    A GLY   A 1 130 ? 15.416 1.184   -4.715  0.42 15.54 ?  130 GLY   A C    1 
ATOM   3155 C C    B GLY   A 1 130 ? 11.875 -1.300  -3.688  0.29 22.32 ?  130 GLY   A C    1 
ATOM   3156 C C    C GLY   A 1 130 ? 16.017 1.183   -4.786  0.29 19.12 ?  130 GLY   A C    1 
ATOM   3157 O O    A GLY   A 1 130 ? 15.168 0.734   -5.840  0.42 15.13 ?  130 GLY   A O    1 
ATOM   3158 O O    B GLY   A 1 130 ? 11.540 -1.835  -2.630  0.29 21.22 ?  130 GLY   A O    1 
ATOM   3159 O O    C GLY   A 1 130 ? 15.374 1.082   -5.835  0.29 19.48 ?  130 GLY   A O    1 
ATOM   3160 H H    A GLY   A 1 130 ? 14.051 -1.243  -3.489  0.42 18.44 ?  130 GLY   A H    1 
ATOM   3161 H H    B GLY   A 1 130 ? 13.440 -2.736  -4.468  0.29 26.70 ?  130 GLY   A H    1 
ATOM   3162 H H    C GLY   A 1 130 ? 17.076 -1.232  -4.076  0.29 23.74 ?  130 GLY   A H    1 
ATOM   3163 H HA2  A GLY   A 1 130 ? 13.876 0.897   -3.392  0.42 18.95 ?  130 GLY   A HA2  1 
ATOM   3164 H HA2  B GLY   A 1 130 ? 13.684 -0.541  -3.082  0.29 26.78 ?  130 GLY   A HA2  1 
ATOM   3165 H HA2  C GLY   A 1 130 ? 14.856 0.194   -3.422  0.29 23.56 ?  130 GLY   A HA2  1 
ATOM   3166 H HA3  A GLY   A 1 130 ? 15.290 0.904   -2.696  0.42 18.95 ?  130 GLY   A HA3  1 
ATOM   3167 H HA3  B GLY   A 1 130 ? 13.352 -0.204  -4.597  0.29 26.78 ?  130 GLY   A HA3  1 
ATOM   3168 H HA3  C GLY   A 1 130 ? 16.308 0.496   -2.895  0.29 23.56 ?  130 GLY   A HA3  1 
ATOM   3169 N N    A ILE   A 1 131 ? 16.263 2.197   -4.518  0.42 15.40 ?  131 ILE   A N    1 
ATOM   3170 N N    B ILE   A 1 131 ? 11.026 -1.088  -4.693  0.29 23.08 ?  131 ILE   A N    1 
ATOM   3171 N N    C ILE   A 1 131 ? 16.936 2.133   -4.591  0.29 18.45 ?  131 ILE   A N    1 
ATOM   3172 C CA   A ILE   A 1 131 ? 16.790 2.967   -5.642  0.42 14.24 ?  131 ILE   A CA   1 
ATOM   3173 C CA   B ILE   A 1 131 ? 9.737  -1.769  -4.775  0.29 24.45 ?  131 ILE   A CA   1 
ATOM   3174 C CA   C ILE   A 1 131 ? 17.294 3.050   -5.668  0.29 17.53 ?  131 ILE   A CA   1 
ATOM   3175 C C    A ILE   A 1 131 ? 17.771 2.187   -6.505  0.42 13.79 ?  131 ILE   A C    1 
ATOM   3176 C C    B ILE   A 1 131 ? 9.403  -1.972  -6.252  0.29 25.71 ?  131 ILE   A C    1 
ATOM   3177 C C    C ILE   A 1 131 ? 18.171 2.388   -6.719  0.29 17.23 ?  131 ILE   A C    1 
ATOM   3178 O O    A ILE   A 1 131 ? 18.177 2.693   -7.559  0.42 14.07 ?  131 ILE   A O    1 
ATOM   3179 O O    B ILE   A 1 131 ? 8.879  -1.077  -6.925  0.29 26.15 ?  131 ILE   A O    1 
ATOM   3180 O O    C ILE   A 1 131 ? 18.415 2.988   -7.773  0.29 16.88 ?  131 ILE   A O    1 
ATOM   3181 C CB   A ILE   A 1 131 ? 17.359 4.329   -5.183  0.42 14.96 ?  131 ILE   A CB   1 
ATOM   3182 C CB   B ILE   A 1 131 ? 8.639  -1.059  -3.953  0.29 24.58 ?  131 ILE   A CB   1 
ATOM   3183 C CB   C ILE   A 1 131 ? 17.906 4.362   -5.127  0.29 17.29 ?  131 ILE   A CB   1 
ATOM   3184 C CG1  A ILE   A 1 131 ? 18.588 4.147   -4.288  0.42 15.51 ?  131 ILE   A CG1  1 
ATOM   3185 C CG1  B ILE   A 1 131 ? 7.260  -1.676  -4.228  0.29 24.20 ?  131 ILE   A CG1  1 
ATOM   3186 C CG1  C ILE   A 1 131 ? 19.182 4.084   -4.330  0.29 17.13 ?  131 ILE   A CG1  1 
ATOM   3187 C CG2  A ILE   A 1 131 ? 16.290 5.120   -4.442  0.42 14.97 ?  131 ILE   A CG2  1 
ATOM   3188 C CG2  B ILE   A 1 131 ? 8.678  0.448   -4.172  0.29 24.85 ?  131 ILE   A CG2  1 
ATOM   3189 C CG2  C ILE   A 1 131 ? 16.892 5.100   -4.261  0.29 17.12 ?  131 ILE   A CG2  1 
ATOM   3190 C CD1  A ILE   A 1 131 ? 19.223 5.463   -3.860  0.42 16.18 ?  131 ILE   A CD1  1 
ATOM   3191 C CD1  B ILE   A 1 131 ? 6.241  -1.420  -3.122  0.29 23.93 ?  131 ILE   A CD1  1 
ATOM   3192 C CD1  C ILE   A 1 131 ? 19.863 5.338   -3.811  0.29 17.12 ?  131 ILE   A CD1  1 
ATOM   3193 H H    A ILE   A 1 131 ? 16.530 2.463   -3.747  0.42 18.51 ?  131 ILE   A H    1 
ATOM   3194 H H    B ILE   A 1 131 ? 11.174 -0.547  -5.345  0.29 27.72 ?  131 ILE   A H    1 
ATOM   3195 H H    C ILE   A 1 131 ? 17.365 2.254   -3.856  0.29 22.16 ?  131 ILE   A H    1 
ATOM   3196 H HA   A ILE   A 1 131 ? 16.040 3.176   -6.218  0.42 17.12 ?  131 ILE   A HA   1 
ATOM   3197 H HA   B ILE   A 1 131 ? 9.842  -2.647  -4.385  0.29 29.37 ?  131 ILE   A HA   1 
ATOM   3198 H HA   C ILE   A 1 131 ? 16.485 3.305   -6.123  0.29 21.06 ?  131 ILE   A HA   1 
ATOM   3199 H HB   A ILE   A 1 131 ? 17.619 4.833   -5.970  0.42 17.98 ?  131 ILE   A HB   1 
ATOM   3200 H HB   B ILE   A 1 131 ? 8.835  -1.216  -3.018  0.29 29.52 ?  131 ILE   A HB   1 
ATOM   3201 H HB   C ILE   A 1 131 ? 18.135 4.933   -5.879  0.29 20.77 ?  131 ILE   A HB   1 
ATOM   3202 H HG12 A ILE   A 1 131 ? 18.321 3.670   -3.487  0.42 18.64 ?  131 ILE   A HG12 1 
ATOM   3203 H HG12 B ILE   A 1 131 ? 6.901  -1.302  -5.046  0.29 29.07 ?  131 ILE   A HG12 1 
ATOM   3204 H HG12 C ILE   A 1 131 ? 18.963 3.532   -3.564  0.29 20.58 ?  131 ILE   A HG12 1 
ATOM   3205 H HG13 A ILE   A 1 131 ? 19.254 3.640   -4.772  0.42 18.64 ?  131 ILE   A HG13 1 
ATOM   3206 H HG13 B ILE   A 1 131 ? 7.357  -2.637  -4.319  0.29 29.07 ?  131 ILE   A HG13 1 
ATOM   3207 H HG13 C ILE   A 1 131 ? 19.816 3.622   -4.900  0.29 20.58 ?  131 ILE   A HG13 1 
ATOM   3208 H HG21 A ILE   A 1 131 ? 16.589 6.037   -4.333  0.42 17.99 ?  131 ILE   A HG21 1 
ATOM   3209 H HG21 B ILE   A 1 131 ? 7.926  0.852   -3.711  0.29 29.84 ?  131 ILE   A HG21 1 
ATOM   3210 H HG21 C ILE   A 1 131 ? 17.222 5.993   -4.072  0.29 20.57 ?  131 ILE   A HG21 1 
ATOM   3211 H HG22 A ILE   A 1 131 ? 15.468 5.105   -4.961  0.42 17.99 ?  131 ILE   A HG22 1 
ATOM   3212 H HG22 B ILE   A 1 131 ? 9.509  0.795   -3.805  0.29 29.84 ?  131 ILE   A HG22 1 
ATOM   3213 H HG22 C ILE   A 1 131 ? 16.051 5.152   -4.739  0.29 20.57 ?  131 ILE   A HG22 1 
ATOM   3214 H HG23 A ILE   A 1 131 ? 16.138 4.715   -3.575  0.42 17.99 ?  131 ILE   A HG23 1 
ATOM   3215 H HG23 B ILE   A 1 131 ? 8.628  0.634   -5.118  0.29 29.84 ?  131 ILE   A HG23 1 
ATOM   3216 H HG23 C ILE   A 1 131 ? 16.771 4.610   -3.432  0.29 20.57 ?  131 ILE   A HG23 1 
ATOM   3217 H HD11 A ILE   A 1 131 ? 20.068 5.277   -3.426  0.42 19.45 ?  131 ILE   A HD11 1 
ATOM   3218 H HD11 B ILE   A 1 131 ? 5.556  -2.108  -3.152  0.29 28.75 ?  131 ILE   A HD11 1 
ATOM   3219 H HD11 C ILE   A 1 131 ? 20.730 5.099   -3.446  0.29 20.57 ?  131 ILE   A HD11 1 
ATOM   3220 H HD12 A ILE   A 1 131 ? 19.366 6.015   -4.645  0.42 19.45 ?  131 ILE   A HD12 1 
ATOM   3221 H HD12 B ILE   A 1 131 ? 6.692  -1.444  -2.262  0.29 28.75 ?  131 ILE   A HD12 1 
ATOM   3222 H HD12 C ILE   A 1 131 ? 19.975 5.964   -4.544  0.29 20.57 ?  131 ILE   A HD12 1 
ATOM   3223 H HD13 A ILE   A 1 131 ? 18.627 5.918   -3.242  0.42 19.45 ?  131 ILE   A HD13 1 
ATOM   3224 H HD13 B ILE   A 1 131 ? 5.841  -0.547  -3.255  0.29 28.75 ?  131 ILE   A HD13 1 
ATOM   3225 H HD13 C ILE   A 1 131 ? 19.312 5.736   -3.118  0.29 20.57 ?  131 ILE   A HD13 1 
ATOM   3226 N N    A PHE   A 1 132 ? 18.140 0.963   -6.106  0.42 13.57 ?  132 PHE   A N    1 
ATOM   3227 N N    B PHE   A 1 132 ? 9.710  -3.174  -6.746  0.29 26.70 ?  132 PHE   A N    1 
ATOM   3228 N N    C PHE   A 1 132 ? 18.636 1.162   -6.466  0.29 17.14 ?  132 PHE   A N    1 
ATOM   3229 C CA   A PHE   A 1 132 ? 19.027 0.119   -6.904  0.42 13.56 ?  132 PHE   A CA   1 
ATOM   3230 C CA   B PHE   A 1 132 ? 9.862  -3.513  -8.161  0.29 27.35 ?  132 PHE   A CA   1 
ATOM   3231 C CA   C PHE   A 1 132 ? 19.372 0.380   -7.453  0.29 17.34 ?  132 PHE   A CA   1 
ATOM   3232 C C    A PHE   A 1 132 ? 18.297 -0.642  -8.015  0.42 13.41 ?  132 PHE   A C    1 
ATOM   3233 C C    B PHE   A 1 132 ? 11.068 -2.813  -8.784  0.29 27.25 ?  132 PHE   A C    1 
ATOM   3234 C C    C PHE   A 1 132 ? 18.455 -0.248  -8.497  0.29 18.64 ?  132 PHE   A C    1 
ATOM   3235 O O    A PHE   A 1 132 ? 18.954 -1.263  -8.859  0.42 14.08 ?  132 PHE   A O    1 
ATOM   3236 O O    B PHE   A 1 132 ? 11.930 -2.294  -8.066  0.29 27.25 ?  132 PHE   A O    1 
ATOM   3237 O O    C PHE   A 1 132 ? 18.946 -0.939  -9.397  0.29 18.34 ?  132 PHE   A O    1 
ATOM   3238 C CB   A PHE   A 1 132 ? 19.793 -0.857  -6.002  0.42 12.90 ?  132 PHE   A CB   1 
ATOM   3239 C CB   B PHE   A 1 132 ? 8.589  -3.287  -8.978  0.29 28.53 ?  132 PHE   A CB   1 
ATOM   3240 C CB   C PHE   A 1 132 ? 20.186 -0.723  -6.762  0.29 16.34 ?  132 PHE   A CB   1 
ATOM   3241 C CG   A PHE   A 1 132 ? 20.991 -0.247  -5.300  0.42 12.29 ?  132 PHE   A CG   1 
ATOM   3242 C CG   B PHE   A 1 132 ? 8.198  -4.483  -9.807  0.29 29.51 ?  132 PHE   A CG   1 
ATOM   3243 C CG   C PHE   A 1 132 ? 21.431 -0.229  -6.065  0.29 16.15 ?  132 PHE   A CG   1 
ATOM   3244 C CD1  A PHE   A 1 132 ? 20.832 0.767   -4.368  0.42 12.80 ?  132 PHE   A CD1  1 
ATOM   3245 C CD1  B PHE   A 1 132 ? 8.766  -4.705  -11.054 0.29 29.97 ?  132 PHE   A CD1  1 
ATOM   3246 C CD1  C PHE   A 1 132 ? 21.398 0.897   -5.256  0.29 16.47 ?  132 PHE   A CD1  1 
ATOM   3247 C CD2  A PHE   A 1 132 ? 22.273 -0.719  -5.555  0.42 12.21 ?  132 PHE   A CD2  1 
ATOM   3248 C CD2  B PHE   A 1 132 ? 7.283  -5.402  -9.324  0.29 29.96 ?  132 PHE   A CD2  1 
ATOM   3249 C CD2  C PHE   A 1 132 ? 22.631 -0.908  -6.205  0.29 16.02 ?  132 PHE   A CD2  1 
ATOM   3250 C CE1  A PHE   A 1 132 ? 21.931 1.310   -3.718  0.42 12.55 ?  132 PHE   A CE1  1 
ATOM   3251 C CE1  B PHE   A 1 132 ? 8.416  -5.812  -11.806 0.29 30.28 ?  132 PHE   A CE1  1 
ATOM   3252 C CE1  C PHE   A 1 132 ? 22.538 1.344   -4.617  0.29 16.65 ?  132 PHE   A CE1  1 
ATOM   3253 C CE2  A PHE   A 1 132 ? 23.373 -0.181  -4.908  0.42 12.30 ?  132 PHE   A CE2  1 
ATOM   3254 C CE2  B PHE   A 1 132 ? 6.928  -6.509  -10.072 0.29 30.33 ?  132 PHE   A CE2  1 
ATOM   3255 C CE2  C PHE   A 1 132 ? 23.774 -0.467  -5.566  0.29 16.22 ?  132 PHE   A CE2  1 
ATOM   3256 C CZ   A PHE   A 1 132 ? 23.202 0.834   -3.990  0.42 11.86 ?  132 PHE   A CZ   1 
ATOM   3257 C CZ   B PHE   A 1 132 ? 7.496  -6.714  -11.314 0.29 30.38 ?  132 PHE   A CZ   1 
ATOM   3258 C CZ   C PHE   A 1 132 ? 23.727 0.660   -4.771  0.29 16.44 ?  132 PHE   A CZ   1 
ATOM   3259 H H    A PHE   A 1 132 ? 17.884 0.598   -5.364  0.42 16.31 ?  132 PHE   A H    1 
ATOM   3260 H H    B PHE   A 1 132 ? 9.838  -3.852  -6.244  0.29 32.07 ?  132 PHE   A H    1 
ATOM   3261 H H    C PHE   A 1 132 ? 18.529 0.754   -5.717  0.29 20.59 ?  132 PHE   A H    1 
ATOM   3262 H HA   A PHE   A 1 132 ? 19.678 0.691   -7.326  0.42 16.29 ?  132 PHE   A HA   1 
ATOM   3263 H HA   B PHE   A 1 132 ? 10.030 -4.469  -8.200  0.29 32.85 ?  132 PHE   A HA   1 
ATOM   3264 H HA   C PHE   A 1 132 ? 19.999 0.970   -7.903  0.29 20.84 ?  132 PHE   A HA   1 
ATOM   3265 H HB2  A PHE   A 1 132 ? 19.189 -1.187  -5.317  0.42 15.51 ?  132 PHE   A HB2  1 
ATOM   3266 H HB2  B PHE   A 1 132 ? 7.861  -3.102  -8.372  0.29 34.27 ?  132 PHE   A HB2  1 
ATOM   3267 H HB2  C PHE   A 1 132 ? 19.628 -1.153  -6.099  0.29 19.64 ?  132 PHE   A HB2  1 
ATOM   3268 H HB3  A PHE   A 1 132 ? 20.111 -1.597  -6.542  0.42 15.51 ?  132 PHE   A HB3  1 
ATOM   3269 H HB3  B PHE   A 1 132 ? 8.719  -2.536  -9.578  0.29 34.27 ?  132 PHE   A HB3  1 
ATOM   3270 H HB3  C PHE   A 1 132 ? 20.460 -1.370  -7.432  0.29 19.64 ?  132 PHE   A HB3  1 
ATOM   3271 H HD1  A PHE   A 1 132 ? 19.979 1.088   -4.177  0.42 15.39 ?  132 PHE   A HD1  1 
ATOM   3272 H HD1  B PHE   A 1 132 ? 9.389  -4.103  -11.394 0.29 35.99 ?  132 PHE   A HD1  1 
ATOM   3273 H HD1  C PHE   A 1 132 ? 20.604 1.366   -5.151  0.29 19.79 ?  132 PHE   A HD1  1 
ATOM   3274 H HD2  A PHE   A 1 132 ? 22.396 -1.402  -6.173  0.42 14.68 ?  132 PHE   A HD2  1 
ATOM   3275 H HD2  B PHE   A 1 132 ? 6.900  -5.268  -8.489  0.29 35.97 ?  132 PHE   A HD2  1 
ATOM   3276 H HD2  C PHE   A 1 132 ? 22.671 -1.666  -6.741  0.29 19.26 ?  132 PHE   A HD2  1 
ATOM   3277 H HE1  A PHE   A 1 132 ? 21.814 1.992   -3.095  0.42 15.09 ?  132 PHE   A HE1  1 
ATOM   3278 H HE1  B PHE   A 1 132 ? 8.802  -5.947  -12.643 0.29 36.36 ?  132 PHE   A HE1  1 
ATOM   3279 H HE1  C PHE   A 1 132 ? 22.505 2.103   -4.082  0.29 20.01 ?  132 PHE   A HE1  1 
ATOM   3280 H HE2  A PHE   A 1 132 ? 24.226 -0.502  -5.095  0.42 14.78 ?  132 PHE   A HE2  1 
ATOM   3281 H HE2  B PHE   A 1 132 ? 6.309  -7.116  -9.737  0.29 36.43 ?  132 PHE   A HE2  1 
ATOM   3282 H HE2  C PHE   A 1 132 ? 24.575 -0.928  -5.670  0.29 19.50 ?  132 PHE   A HE2  1 
ATOM   3283 H HZ   A PHE   A 1 132 ? 23.939 1.198   -3.554  0.42 14.26 ?  132 PHE   A HZ   1 
ATOM   3284 H HZ   B PHE   A 1 132 ? 7.259  -7.459  -11.817 0.29 36.48 ?  132 PHE   A HZ   1 
ATOM   3285 H HZ   C PHE   A 1 132 ? 24.497 0.958   -4.339  0.29 19.76 ?  132 PHE   A HZ   1 
ATOM   3286 N N    A GLY   A 1 133 ? 16.965 -0.627  -8.034  0.42 12.51 ?  133 GLY   A N    1 
ATOM   3287 N N    B GLY   A 1 133 ? 11.134 -2.791  -10.115 0.29 27.27 ?  133 GLY   A N    1 
ATOM   3288 N N    C GLY   A 1 133 ? 17.143 -0.052  -8.377  0.29 20.13 ?  133 GLY   A N    1 
ATOM   3289 C CA   A GLY   A 1 133 ? 16.206 -1.027  -9.204  0.42 12.49 ?  133 GLY   A CA   1 
ATOM   3290 C CA   B GLY   A 1 133 ? 12.352 -2.432  -10.815 0.29 27.20 ?  133 GLY   A CA   1 
ATOM   3291 C CA   C GLY   A 1 133 ? 16.195 -0.425  -9.410  0.29 21.58 ?  133 GLY   A CA   1 
ATOM   3292 C C    A GLY   A 1 133 ? 15.764 -2.474  -9.279  0.42 12.19 ?  133 GLY   A C    1 
ATOM   3293 C C    B GLY   A 1 133 ? 13.285 -3.620  -10.929 0.29 27.25 ?  133 GLY   A C    1 
ATOM   3294 C C    C GLY   A 1 133 ? 16.096 -1.918  -9.651  0.29 22.88 ?  133 GLY   A C    1 
ATOM   3295 O O    A GLY   A 1 133 ? 15.004 -2.815  -10.196 0.42 12.58 ?  133 GLY   A O    1 
ATOM   3296 O O    B GLY   A 1 133 ? 13.156 -4.429  -11.852 0.29 27.49 ?  133 GLY   A O    1 
ATOM   3297 O O    C GLY   A 1 133 ? 16.764 -2.453  -10.541 0.29 23.48 ?  133 GLY   A O    1 
ATOM   3298 H H    A GLY   A 1 133 ? 16.473 -0.396  -7.365  0.42 15.04 ?  133 GLY   A H    1 
ATOM   3299 H H    B GLY   A 1 133 ? 10.476 -2.960  -10.639 0.29 32.75 ?  133 GLY   A H    1 
ATOM   3300 H H    C GLY   A 1 133 ? 16.774 0.296   -7.685  0.29 24.18 ?  133 GLY   A H    1 
ATOM   3301 H HA2  A GLY   A 1 133 ? 15.409 -0.485  -9.255  0.42 15.01 ?  133 GLY   A HA2  1 
ATOM   3302 H HA2  B GLY   A 1 133 ? 12.137 -2.122  -11.710 0.29 32.66 ?  133 GLY   A HA2  1 
ATOM   3303 H HA2  C GLY   A 1 133 ? 15.315 -0.093  -9.162  0.29 25.92 ?  133 GLY   A HA2  1 
ATOM   3304 H HA3  A GLY   A 1 133 ? 16.739 -0.860  -9.990  0.42 15.01 ?  133 GLY   A HA3  1 
ATOM   3305 H HA3  B GLY   A 1 133 ? 12.805 -1.725  -10.337 0.29 32.66 ?  133 GLY   A HA3  1 
ATOM   3306 H HA3  C GLY   A 1 133 ? 16.446 0.005   -10.245 0.29 25.92 ?  133 GLY   A HA3  1 
ATOM   3307 N N    A ALA   A 1 134 ? 16.195 -3.337  -8.363  0.42 11.28 ?  134 ALA   A N    1 
ATOM   3308 N N    B ALA   A 1 134 ? 14.235 -3.737  -9.997  0.29 27.17 ?  134 ALA   A N    1 
ATOM   3309 N N    C ALA   A 1 134 ? 15.268 -2.602  -8.868  0.29 23.63 ?  134 ALA   A N    1 
ATOM   3310 C CA   A ALA   A 1 134 ? 15.849 -4.744  -8.473  0.42 11.80 ?  134 ALA   A CA   1 
ATOM   3311 C CA   B ALA   A 1 134 ? 15.023 -4.959  -9.884  0.29 26.81 ?  134 ALA   A CA   1 
ATOM   3312 C CA   C ALA   A 1 134 ? 15.038 -4.029  -9.065  0.29 24.10 ?  134 ALA   A CA   1 
ATOM   3313 C C    A ALA   A 1 134 ? 14.508 -5.040  -7.813  0.42 11.64 ?  134 ALA   A C    1 
ATOM   3314 C C    B ALA   A 1 134 ? 14.260 -6.054  -9.144  0.29 26.34 ?  134 ALA   A C    1 
ATOM   3315 C C    C ALA   A 1 134 ? 13.723 -4.408  -8.387  0.29 24.15 ?  134 ALA   A C    1 
ATOM   3316 O O    A ALA   A 1 134 ? 13.956 -4.232  -7.061  0.42 12.45 ?  134 ALA   A O    1 
ATOM   3317 O O    B ALA   A 1 134 ? 14.544 -7.240  -9.340  0.29 26.97 ?  134 ALA   A O    1 
ATOM   3318 O O    C ALA   A 1 134 ? 12.866 -3.548  -8.152  0.29 24.72 ?  134 ALA   A O    1 
ATOM   3319 C CB   A ALA   A 1 134 ? 16.944 -5.625  -7.872  0.42 11.90 ?  134 ALA   A CB   1 
ATOM   3320 C CB   B ALA   A 1 134 ? 16.356 -4.662  -9.187  0.29 26.84 ?  134 ALA   A CB   1 
ATOM   3321 C CB   C ALA   A 1 134 ? 16.234 -4.845  -8.549  0.29 24.24 ?  134 ALA   A CB   1 
ATOM   3322 H H    A ALA   A 1 134 ? 16.674 -3.133  -7.669  0.42 13.56 ?  134 ALA   A H    1 
ATOM   3323 H H    B ALA   A 1 134 ? 14.433 -3.127  -9.420  0.29 32.63 ?  134 ALA   A H    1 
ATOM   3324 H H    C ALA   A 1 134 ? 14.829 -2.259  -8.212  0.29 28.39 ?  134 ALA   A H    1 
ATOM   3325 H HA   A ALA   A 1 134 ? 15.773 -4.968  -9.407  0.42 14.18 ?  134 ALA   A HA   1 
ATOM   3326 H HA   B ALA   A 1 134 ? 15.231 -5.276  -10.778 0.29 32.20 ?  134 ALA   A HA   1 
ATOM   3327 H HA   C ALA   A 1 134 ? 14.954 -4.200  -10.018 0.29 28.94 ?  134 ALA   A HA   1 
ATOM   3328 H HB1  A ALA   A 1 134 ? 16.690 -6.555  -7.971  0.42 14.30 ?  134 ALA   A HB1  1 
ATOM   3329 H HB1  B ALA   A 1 134 ? 16.871 -5.482  -9.126  0.29 32.24 ?  134 ALA   A HB1  1 
ATOM   3330 H HB1  C ALA   A 1 134 ? 16.096 -5.779  -8.771  0.29 29.12 ?  134 ALA   A HB1  1 
ATOM   3331 H HB2  A ALA   A 1 134 ? 17.775 -5.456  -8.344  0.42 14.30 ?  134 ALA   A HB2  1 
ATOM   3332 H HB2  B ALA   A 1 134 ? 16.851 -4.003  -9.706  0.29 32.24 ?  134 ALA   A HB2  1 
ATOM   3333 H HB2  C ALA   A 1 134 ? 17.040 -4.518  -8.972  0.29 29.12 ?  134 ALA   A HB2  1 
ATOM   3334 H HB3  A ALA   A 1 134 ? 17.049 -5.407  -6.932  0.42 14.30 ?  134 ALA   A HB3  1 
ATOM   3335 H HB3  B ALA   A 1 134 ? 16.180 -4.314  -8.300  0.29 32.24 ?  134 ALA   A HB3  1 
ATOM   3336 H HB3  C ALA   A 1 134 ? 16.294 -4.735  -7.588  0.29 29.12 ?  134 ALA   A HB3  1 
ATOM   3337 N N    A ASP   A 1 135 ? 14.001 -6.239  -8.104  0.42 12.32 ?  135 ASP   A N    1 
ATOM   3338 N N    B ASP   A 1 135 ? 13.303 -5.663  -8.301  0.29 25.13 ?  135 ASP   A N    1 
ATOM   3339 N N    C ASP   A 1 135 ? 13.569 -5.691  -8.065  0.29 23.33 ?  135 ASP   A N    1 
ATOM   3340 C CA   A ASP   A 1 135 ? 12.736 -6.717  -7.560  0.42 13.66 ?  135 ASP   A CA   1 
ATOM   3341 C CA   B ASP   A 1 135 ? 12.293 -6.488  -7.636  0.29 23.78 ?  135 ASP   A CA   1 
ATOM   3342 C CA   C ASP   A 1 135 ? 12.343 -6.224  -7.483  0.29 22.55 ?  135 ASP   A CA   1 
ATOM   3343 C C    A ASP   A 1 135 ? 12.933 -7.187  -6.124  0.42 12.99 ?  135 ASP   A C    1 
ATOM   3344 C C    B ASP   A 1 135 ? 12.738 -7.017  -6.276  0.29 21.89 ?  135 ASP   A C    1 
ATOM   3345 C C    C ASP   A 1 135 ? 12.641 -6.783  -6.098  0.29 21.11 ?  135 ASP   A C    1 
ATOM   3346 O O    A ASP   A 1 135 ? 13.705 -8.126  -5.893  0.42 11.45 ?  135 ASP   A O    1 
ATOM   3347 O O    B ASP   A 1 135 ? 13.590 -7.912  -6.195  0.29 21.34 ?  135 ASP   A O    1 
ATOM   3348 O O    C ASP   A 1 135 ? 13.413 -7.752  -5.979  0.29 20.91 ?  135 ASP   A O    1 
ATOM   3349 C CB   A ASP   A 1 135 ? 12.228 -7.875  -8.411  0.42 15.86 ?  135 ASP   A CB   1 
ATOM   3350 C CB   B ASP   A 1 135 ? 11.785 -7.628  -8.516  0.29 24.39 ?  135 ASP   A CB   1 
ATOM   3351 C CB   C ASP   A 1 135 ? 11.766 -7.327  -8.370  0.29 23.25 ?  135 ASP   A CB   1 
ATOM   3352 C CG   A ASP   A 1 135 ? 10.983 -8.528  -7.845  0.42 17.88 ?  135 ASP   A CG   1 
ATOM   3353 C CG   B ASP   A 1 135 ? 10.400 -8.101  -8.118  0.29 25.03 ?  135 ASP   A CG   1 
ATOM   3354 C CG   C ASP   A 1 135 ? 10.386 -7.776  -7.923  0.29 24.04 ?  135 ASP   A CG   1 
ATOM   3355 O OD1  A ASP   A 1 135 ? 10.340 -7.940  -6.951  0.42 18.29 ?  135 ASP   A OD1  1 
ATOM   3356 O OD1  B ASP   A 1 135 ? 10.006 -7.880  -6.953  0.29 25.61 ?  135 ASP   A OD1  1 
ATOM   3357 O OD1  C ASP   A 1 135 ? 10.021 -7.525  -6.754  0.29 24.42 ?  135 ASP   A OD1  1 
ATOM   3358 O OD2  A ASP   A 1 135 ? 10.672 -9.653  -8.284  0.42 19.93 -1 135 ASP   A OD2  1 
ATOM   3359 O OD2  B ASP   A 1 135 ? 9.708  -8.701  -8.967  0.29 25.26 -1 135 ASP   A OD2  1 
ATOM   3360 O OD2  C ASP   A 1 135 ? 9.662  -8.380  -8.743  0.29 24.43 -1 135 ASP   A OD2  1 
ATOM   3361 H H    A ASP   A 1 135 ? 14.391 -6.815  -8.613  0.42 14.81 ?  135 ASP   A H    1 
ATOM   3362 H H    B ASP   A 1 135 ? 13.215 -4.835  -8.094  0.29 30.18 ?  135 ASP   A H    1 
ATOM   3363 H H    C ASP   A 1 135 ? 14.178 -6.282  -8.175  0.29 28.02 ?  135 ASP   A H    1 
ATOM   3364 H HA   A ASP   A 1 135 ? 12.091 -6.009  -7.577  0.42 16.42 ?  135 ASP   A HA   1 
ATOM   3365 H HA   B ASP   A 1 135 ? 11.539 -5.915  -7.494  0.29 28.56 ?  135 ASP   A HA   1 
ATOM   3366 H HA   C ASP   A 1 135 ? 11.688 -5.513  -7.422  0.29 27.08 ?  135 ASP   A HA   1 
ATOM   3367 H HB2  A ASP   A 1 135 ? 12.040 -7.544  -9.302  0.42 19.06 ?  135 ASP   A HB2  1 
ATOM   3368 H HB2  B ASP   A 1 135 ? 11.754 -7.323  -9.429  0.29 29.29 ?  135 ASP   A HB2  1 
ATOM   3369 H HB2  C ASP   A 1 135 ? 11.692 -6.995  -9.275  0.29 27.93 ?  135 ASP   A HB2  1 
ATOM   3370 H HB3  A ASP   A 1 135 ? 12.900 -8.570  -8.447  0.42 19.06 ?  135 ASP   A HB3  1 
ATOM   3371 H HB3  B ASP   A 1 135 ? 12.360 -8.389  -8.418  0.29 29.29 ?  135 ASP   A HB3  1 
ATOM   3372 H HB3  C ASP   A 1 135 ? 12.362 -8.093  -8.341  0.29 27.93 ?  135 ASP   A HB3  1 
ATOM   3373 N N    A PRO   A 1 136 ? 12.254 -6.585  -5.142  0.42 14.00 ?  136 PRO   A N    1 
ATOM   3374 N N    B PRO   A 1 136 ? 12.155 -6.502  -5.189  0.29 20.90 ?  136 PRO   A N    1 
ATOM   3375 N N    C PRO   A 1 136 ? 12.049 -6.237  -5.034  0.29 20.32 ?  136 PRO   A N    1 
ATOM   3376 C CA   A PRO   A 1 136 ? 12.478 -6.991  -3.742  0.42 13.79 ?  136 PRO   A CA   1 
ATOM   3377 C CA   B PRO   A 1 136 ? 12.507 -7.011  -3.855  0.29 20.13 ?  136 PRO   A CA   1 
ATOM   3378 C CA   C PRO   A 1 136 ? 12.317 -6.776  -3.690  0.29 19.88 ?  136 PRO   A CA   1 
ATOM   3379 C C    A PRO   A 1 136 ? 12.032 -8.406  -3.410  0.42 12.80 ?  136 PRO   A C    1 
ATOM   3380 C C    B PRO   A 1 136 ? 12.090 -8.454  -3.639  0.29 19.23 ?  136 PRO   A C    1 
ATOM   3381 C C    C PRO   A 1 136 ? 11.971 -8.248  -3.534  0.29 19.25 ?  136 PRO   A C    1 
ATOM   3382 O O    A PRO   A 1 136 ? 12.620 -9.017  -2.513  0.42 11.77 ?  136 PRO   A O    1 
ATOM   3383 O O    B PRO   A 1 136 ? 12.693 -9.142  -2.807  0.29 18.75 ?  136 PRO   A O    1 
ATOM   3384 O O    C PRO   A 1 136 ? 12.588 -8.935  -2.710  0.29 18.64 ?  136 PRO   A O    1 
ATOM   3385 C CB   A PRO   A 1 136 ? 11.691 -5.946  -2.938  0.42 14.79 ?  136 PRO   A CB   1 
ATOM   3386 C CB   B PRO   A 1 136 ? 11.768 -6.052  -2.905  0.29 20.51 ?  136 PRO   A CB   1 
ATOM   3387 C CB   C PRO   A 1 136 ? 11.466 -5.880  -2.775  0.29 20.19 ?  136 PRO   A CB   1 
ATOM   3388 C CG   A PRO   A 1 136 ? 10.666 -5.438  -3.893  0.42 15.34 ?  136 PRO   A CG   1 
ATOM   3389 C CG   B PRO   A 1 136 ? 11.350 -4.878  -3.758  0.29 20.70 ?  136 PRO   A CG   1 
ATOM   3390 C CG   C PRO   A 1 136 ? 10.437 -5.264  -3.680  0.29 20.39 ?  136 PRO   A CG   1 
ATOM   3391 C CD   A PRO   A 1 136 ? 11.316 -5.458  -5.240  0.42 15.10 ?  136 PRO   A CD   1 
ATOM   3392 C CD   B PRO   A 1 136 ? 11.160 -5.424  -5.121  0.29 20.94 ?  136 PRO   A CD   1 
ATOM   3393 C CD   C PRO   A 1 136 ? 11.110 -5.104  -5.001  0.29 20.37 ?  136 PRO   A CD   1 
ATOM   3394 H HA   A PRO   A 1 136 ? 13.426 -6.918  -3.514  0.42 16.57 ?  136 PRO   A HA   1 
ATOM   3395 H HA   B PRO   A 1 136 ? 13.459 -6.932  -3.700  0.29 24.19 ?  136 PRO   A HA   1 
ATOM   3396 H HA   C PRO   A 1 136 ? 13.250 -6.656  -3.464  0.29 23.88 ?  136 PRO   A HA   1 
ATOM   3397 H HB2  A PRO   A 1 136 ? 11.278 -6.374  -2.166  0.42 17.78 ?  136 PRO   A HB2  1 
ATOM   3398 H HB2  B PRO   A 1 136 ? 10.990 -6.495  -2.532  0.29 24.64 ?  136 PRO   A HB2  1 
ATOM   3399 H HB2  C PRO   A 1 136 ? 11.042 -6.417  -2.088  0.29 24.26 ?  136 PRO   A HB2  1 
ATOM   3400 H HB3  A PRO   A 1 136 ? 12.294 -5.243  -2.653  0.42 17.78 ?  136 PRO   A HB3  1 
ATOM   3401 H HB3  B PRO   A 1 136 ? 12.365 -5.759  -2.200  0.29 24.64 ?  136 PRO   A HB3  1 
ATOM   3402 H HB3  C PRO   A 1 136 ? 12.028 -5.195  -2.378  0.29 24.26 ?  136 PRO   A HB3  1 
ATOM   3403 H HG2  A PRO   A 1 136 ? 9.896  -6.027  -3.874  0.42 18.43 ?  136 PRO   A HG2  1 
ATOM   3404 H HG2  B PRO   A 1 136 ? 10.518 -4.509  -3.425  0.29 24.87 ?  136 PRO   A HG2  1 
ATOM   3405 H HG2  C PRO   A 1 136 ? 9.673  -5.857  -3.758  0.29 24.49 ?  136 PRO   A HG2  1 
ATOM   3406 H HG3  A PRO   A 1 136 ? 10.425 -4.539  -3.647  0.42 18.43 ?  136 PRO   A HG3  1 
ATOM   3407 H HG3  B PRO   A 1 136 ? 12.045 -4.200  -3.762  0.29 24.87 ?  136 PRO   A HG3  1 
ATOM   3408 H HG3  C PRO   A 1 136 ? 10.168 -4.401  -3.332  0.29 24.49 ?  136 PRO   A HG3  1 
ATOM   3409 H HD2  A PRO   A 1 136 ? 10.665 -5.638  -5.929  0.42 18.15 ?  136 PRO   A HD2  1 
ATOM   3410 H HD2  B PRO   A 1 136 ? 10.258 -5.777  -5.251  0.29 25.15 ?  136 PRO   A HD2  1 
ATOM   3411 H HD2  C PRO   A 1 136 ? 10.461 -5.178  -5.720  0.29 24.47 ?  136 PRO   A HD2  1 
ATOM   3412 H HD3  A PRO   A 1 136 ? 11.811 -4.647  -5.400  0.42 18.15 ?  136 PRO   A HD3  1 
ATOM   3413 H HD3  B PRO   A 1 136 ? 11.384 -4.750  -5.779  0.29 25.15 ?  136 PRO   A HD3  1 
ATOM   3414 H HD3  C PRO   A 1 136 ? 11.599 -4.268  -5.045  0.29 24.47 ?  136 PRO   A HD3  1 
ATOM   3415 N N    A ILE   A 1 137 ? 10.998 -8.941  -4.062  0.42 13.68 ?  137 ILE   A N    1 
ATOM   3416 N N    B ILE   A 1 137 ? 11.073 -8.930  -4.360  0.29 18.89 ?  137 ILE   A N    1 
ATOM   3417 N N    C ILE   A 1 137 ? 11.006 -8.752  -4.293  0.29 19.31 ?  137 ILE   A N    1 
ATOM   3418 C CA   A ILE   A 1 137 ? 10.645 -10.344 -3.847  0.42 13.95 ?  137 ILE   A CA   1 
ATOM   3419 C CA   B ILE   A 1 137 ? 10.648 -10.322 -4.230  0.29 18.65 ?  137 ILE   A CA   1 
ATOM   3420 C CA   C ILE   A 1 137 ? 10.609 -10.153 -4.217  0.29 19.54 ?  137 ILE   A CA   1 
ATOM   3421 C C    A ILE   A 1 137 ? 11.811 -11.238 -4.246  0.42 12.75 ?  137 ILE   A C    1 
ATOM   3422 C C    B ILE   A 1 137 ? 11.802 -11.259 -4.563  0.29 17.81 ?  137 ILE   A C    1 
ATOM   3423 C C    C ILE   A 1 137 ? 11.785 -11.057 -4.579  0.29 19.36 ?  137 ILE   A C    1 
ATOM   3424 O O    A ILE   A 1 137 ? 12.148 -12.204 -3.548  0.42 11.81 ?  137 ILE   A O    1 
ATOM   3425 O O    B ILE   A 1 137 ? 12.099 -12.204 -3.822  0.29 17.54 ?  137 ILE   A O    1 
ATOM   3426 O O    C ILE   A 1 137 ? 12.076 -12.030 -3.880  0.29 19.30 ?  137 ILE   A O    1 
ATOM   3427 C CB   A ILE   A 1 137 ? 9.357  -10.698 -4.615  0.42 15.16 ?  137 ILE   A CB   1 
ATOM   3428 C CB   B ILE   A 1 137 ? 9.422  -10.585 -5.123  0.29 19.40 ?  137 ILE   A CB   1 
ATOM   3429 C CB   C ILE   A 1 137 ? 9.390  -10.427 -5.117  0.29 20.11 ?  137 ILE   A CB   1 
ATOM   3430 C CG1  A ILE   A 1 137 ? 8.187  -9.843  -4.120  0.42 16.95 ?  137 ILE   A CG1  1 
ATOM   3431 C CG1  B ILE   A 1 137 ? 8.294  -9.606  -4.777  0.29 20.02 ?  137 ILE   A CG1  1 
ATOM   3432 C CG1  C ILE   A 1 137 ? 8.236  -9.486  -4.752  0.29 20.67 ?  137 ILE   A CG1  1 
ATOM   3433 C CG2  A ILE   A 1 137 ? 9.037  -12.185 -4.468  0.42 15.47 ?  137 ILE   A CG2  1 
ATOM   3434 C CG2  B ILE   A 1 137 ? 8.953  -12.022 -4.971  0.29 19.65 ?  137 ILE   A CG2  1 
ATOM   3435 C CG2  C ILE   A 1 137 ? 8.957  -11.879 -4.996  0.29 20.26 ?  137 ILE   A CG2  1 
ATOM   3436 C CD1  A ILE   A 1 137 ? 6.904  -10.055 -4.892  0.42 17.90 ?  137 ILE   A CD1  1 
ATOM   3437 C CD1  B ILE   A 1 137 ? 7.121  -9.650  -5.732  0.29 20.44 ?  137 ILE   A CD1  1 
ATOM   3438 C CD1  C ILE   A 1 137 ? 7.039  -9.581  -5.681  0.29 21.06 ?  137 ILE   A CD1  1 
ATOM   3439 H H    A ILE   A 1 137 ? 10.510 -8.529  -4.618  0.42 16.45 ?  137 ILE   A H    1 
ATOM   3440 H H    B ILE   A 1 137 ? 10.618 -8.470  -4.925  0.29 22.70 ?  137 ILE   A H    1 
ATOM   3441 H H    C ILE   A 1 137 ? 10.561 -8.298  -4.864  0.29 23.19 ?  137 ILE   A H    1 
ATOM   3442 H HA   A ILE   A 1 137 ? 10.478 -10.494 -2.903  0.42 16.77 ?  137 ILE   A HA   1 
ATOM   3443 H HA   B ILE   A 1 137 ? 10.387 -10.490 -3.311  0.29 22.41 ?  137 ILE   A HA   1 
ATOM   3444 H HA   C ILE   A 1 137 ? 10.349 -10.355 -3.305  0.29 23.47 ?  137 ILE   A HA   1 
ATOM   3445 H HB   A ILE   A 1 137 ? 9.498  -10.508 -5.552  0.42 18.22 ?  137 ILE   A HB   1 
ATOM   3446 H HB   B ILE   A 1 137 ? 9.680  -10.444 -6.046  0.29 23.31 ?  137 ILE   A HB   1 
ATOM   3447 H HB   C ILE   A 1 137 ? 9.644  -10.260 -6.036  0.29 24.15 ?  137 ILE   A HB   1 
ATOM   3448 H HG12 A ILE   A 1 137 ? 8.015  -10.054 -3.189  0.42 20.36 ?  137 ILE   A HG12 1 
ATOM   3449 H HG12 B ILE   A 1 137 ? 7.964  -9.817  -3.891  0.29 24.05 ?  137 ILE   A HG12 1 
ATOM   3450 H HG12 C ILE   A 1 137 ? 7.933  -9.699  -3.855  0.29 24.83 ?  137 ILE   A HG12 1 
ATOM   3451 H HG13 A ILE   A 1 137 ? 8.431  -8.904  -4.202  0.42 20.36 ?  137 ILE   A HG13 1 
ATOM   3452 H HG13 B ILE   A 1 137 ? 8.641  -8.700  -4.789  0.29 24.05 ?  137 ILE   A HG13 1 
ATOM   3453 H HG13 C ILE   A 1 137 ? 8.553  -8.570  -4.780  0.29 24.83 ?  137 ILE   A HG13 1 
ATOM   3454 H HG21 A ILE   A 1 137 ? 8.293  -12.409 -5.050  0.42 18.59 ?  137 ILE   A HG21 1 
ATOM   3455 H HG21 B ILE   A 1 137 ? 8.115  -12.133 -5.446  0.29 23.61 ?  137 ILE   A HG21 1 
ATOM   3456 H HG21 C ILE   A 1 137 ? 8.147  -12.012 -5.512  0.29 24.34 ?  137 ILE   A HG21 1 
ATOM   3457 H HG22 A ILE   A 1 137 ? 9.804  -12.713 -4.722  0.42 18.59 ?  137 ILE   A HG22 1 
ATOM   3458 H HG22 B ILE   A 1 137 ? 9.623  -12.616 -5.343  0.29 23.61 ?  137 ILE   A HG22 1 
ATOM   3459 H HG22 C ILE   A 1 137 ? 9.660  -12.450 -5.340  0.29 24.34 ?  137 ILE   A HG22 1 
ATOM   3460 H HG23 A ILE   A 1 137 ? 8.798  -12.364 -3.546  0.42 18.59 ?  137 ILE   A HG23 1 
ATOM   3461 H HG23 B ILE   A 1 137 ? 8.825  -12.213 -4.029  0.29 23.61 ?  137 ILE   A HG23 1 
ATOM   3462 H HG23 C ILE   A 1 137 ? 8.791  -12.080 -4.062  0.29 24.34 ?  137 ILE   A HG23 1 
ATOM   3463 H HD11 A ILE   A 1 137 ? 6.178  -9.709  -4.361  0.42 21.51 ?  137 ILE   A HD11 1 
ATOM   3464 H HD11 B ILE   A 1 137 ? 6.852  -8.741  -5.942  0.29 24.55 ?  137 ILE   A HD11 1 
ATOM   3465 H HD11 C ILE   A 1 137 ? 6.447  -8.832  -5.511  0.29 25.30 ?  137 ILE   A HD11 1 
ATOM   3466 H HD12 A ILE   A 1 137 ? 6.961  -9.580  -5.736  0.42 21.51 ?  137 ILE   A HD12 1 
ATOM   3467 H HD12 B ILE   A 1 137 ? 7.389  -10.110 -6.542  0.29 24.55 ?  137 ILE   A HD12 1 
ATOM   3468 H HD12 C ILE   A 1 137 ? 7.350  -9.553  -6.600  0.29 25.30 ?  137 ILE   A HD12 1 
ATOM   3469 H HD13 A ILE   A 1 137 ? 6.763  -10.999 -5.052  0.42 21.51 ?  137 ILE   A HD13 1 
ATOM   3470 H HD13 B ILE   A 1 137 ? 6.387  -10.124 -5.310  0.29 24.55 ?  137 ILE   A HD13 1 
ATOM   3471 H HD13 C ILE   A 1 137 ? 6.573  -10.415 -5.516  0.29 25.30 ?  137 ILE   A HD13 1 
ATOM   3472 N N    A HIS   A 1 138 ? 12.444 -10.929 -5.376  0.42 13.34 ?  138 HIS   A N    1 
ATOM   3473 N N    B HIS   A 1 138 ? 12.472 -11.008 -5.688  0.58 17.49 ?  138 HIS   A N    1 
ATOM   3474 C CA   A HIS   A 1 138 ? 13.645 -11.651 -5.776  0.42 13.31 ?  138 HIS   A CA   1 
ATOM   3475 C CA   B HIS   A 1 138 ? 13.628 -11.815 -6.059  0.58 16.95 ?  138 HIS   A CA   1 
ATOM   3476 C C    A HIS   A 1 138 ? 14.770 -11.451 -4.765  0.42 12.17 ?  138 HIS   A C    1 
ATOM   3477 C C    B HIS   A 1 138 ? 14.743 -11.680 -5.032  0.58 15.22 ?  138 HIS   A C    1 
ATOM   3478 O O    A HIS   A 1 138 ? 15.461 -12.411 -4.400  0.42 12.24 ?  138 HIS   A O    1 
ATOM   3479 O O    B HIS   A 1 138 ? 15.398 -12.669 -4.678  0.58 15.13 ?  138 HIS   A O    1 
ATOM   3480 C CB   A HIS   A 1 138 ? 14.065 -11.213 -7.180  0.42 14.08 ?  138 HIS   A CB   1 
ATOM   3481 C CB   B HIS   A 1 138 ? 14.125 -11.391 -7.438  0.58 17.64 ?  138 HIS   A CB   1 
ATOM   3482 C CG   A HIS   A 1 138 ? 15.324 -11.862 -7.666  0.42 14.76 ?  138 HIS   A CG   1 
ATOM   3483 C CG   B HIS   A 1 138 ? 15.418 -12.031 -7.834  0.58 18.02 ?  138 HIS   A CG   1 
ATOM   3484 N ND1  A HIS   A 1 138 ? 15.416 -13.213 -7.926  0.42 15.36 ?  138 HIS   A ND1  1 
ATOM   3485 N ND1  B HIS   A 1 138 ? 15.521 -13.371 -8.135  0.58 18.55 ?  138 HIS   A ND1  1 
ATOM   3486 C CD2  A HIS   A 1 138 ? 16.544 -11.342 -7.940  0.42 14.85 ?  138 HIS   A CD2  1 
ATOM   3487 C CD2  B HIS   A 1 138 ? 16.663 -11.517 -7.970  0.58 18.10 ?  138 HIS   A CD2  1 
ATOM   3488 C CE1  A HIS   A 1 138 ? 16.639 -13.496 -8.338  0.42 15.49 ?  138 HIS   A CE1  1 
ATOM   3489 C CE1  B HIS   A 1 138 ? 16.774 -13.655 -8.443  0.58 18.62 ?  138 HIS   A CE1  1 
ATOM   3490 N NE2  A HIS   A 1 138 ? 17.344 -12.379 -8.353  0.42 15.17 ?  138 HIS   A NE2  1 
ATOM   3491 N NE2  B HIS   A 1 138 ? 17.488 -12.547 -8.351  0.58 18.18 ?  138 HIS   A NE2  1 
ATOM   3492 H H    A HIS   A 1 138 ? 12.199 -10.312 -5.922  0.42 16.03 ?  138 HIS   A H    1 
ATOM   3493 H H    B HIS   A 1 138 ? 12.287 -10.377 -6.241  0.58 21.02 ?  138 HIS   A H    1 
ATOM   3494 H HA   A HIS   A 1 138 ? 13.448 -12.596 -5.811  0.42 16.00 ?  138 HIS   A HA   1 
ATOM   3495 H HA   B HIS   A 1 138 ? 13.370 -12.746 -6.101  0.58 20.37 ?  138 HIS   A HA   1 
ATOM   3496 H HB2  A HIS   A 1 138 ? 13.357 -11.440 -7.805  0.42 16.92 ?  138 HIS   A HB2  1 
ATOM   3497 H HB2  B HIS   A 1 138 ? 13.459 -11.633 -8.098  0.58 21.19 ?  138 HIS   A HB2  1 
ATOM   3498 H HB3  A HIS   A 1 138 ? 14.209 -10.254 -7.185  0.42 16.92 ?  138 HIS   A HB3  1 
ATOM   3499 H HB3  B HIS   A 1 138 ? 14.257 -10.428 -7.442  0.58 21.19 ?  138 HIS   A HB3  1 
ATOM   3500 H HD1  A HIS   A 1 138 ? 14.778 -13.783 -7.837  0.42 18.46 ?  138 HIS   A HD1  1 
ATOM   3501 H HD2  A HIS   A 1 138 ? 16.794 -10.451 -7.862  0.42 17.85 ?  138 HIS   A HD2  1 
ATOM   3502 H HD2  B HIS   A 1 138 ? 16.914 -10.632 -7.832  0.58 21.75 ?  138 HIS   A HD2  1 
ATOM   3503 H HE1  A HIS   A 1 138 ? 16.951 -14.341 -8.577  0.42 18.61 ?  138 HIS   A HE1  1 
ATOM   3504 H HE1  B HIS   A 1 138 ? 17.094 -14.492 -8.686  0.58 22.37 ?  138 HIS   A HE1  1 
ATOM   3505 H HE2  B HIS   A 1 138 ? 18.330 -12.483 -8.505  0.58 21.84 ?  138 HIS   A HE2  1 
ATOM   3506 N N    A SER   A 1 139 ? 14.965 -10.214 -4.291  0.42 11.46 ?  139 SER   A N    1 
ATOM   3507 N N    B SER   A 1 139 ? 14.975 -10.462 -4.541  0.58 14.05 ?  139 SER   A N    1 
ATOM   3508 C CA   A SER   A 1 139 ? 16.024 -9.962  -3.317  0.42 11.05 ?  139 SER   A CA   1 
ATOM   3509 C CA   B SER   A 1 139 ? 16.073 -10.245 -3.606  0.58 13.13 ?  139 SER   A CA   1 
ATOM   3510 C C    A SER   A 1 139 ? 15.820 -10.797 -2.060  0.42 10.90 ?  139 SER   A C    1 
ATOM   3511 C C    B SER   A 1 139 ? 15.860 -11.015 -2.309  0.58 12.68 ?  139 SER   A C    1 
ATOM   3512 O O    A SER   A 1 139 ? 16.786 -11.323 -1.491  0.42 10.68 ?  139 SER   A O    1 
ATOM   3513 O O    B SER   A 1 139 ? 16.805 -11.604 -1.769  0.58 12.20 ?  139 SER   A O    1 
ATOM   3514 C CB   A SER   A 1 139 ? 16.114 -8.466  -2.991  0.42 11.00 ?  139 SER   A CB   1 
ATOM   3515 C CB   B SER   A 1 139 ? 16.221 -8.754  -3.317  0.58 12.73 ?  139 SER   A CB   1 
ATOM   3516 O OG   A SER   A 1 139 ? 17.135 -8.217  -2.037  0.42 10.59 ?  139 SER   A OG   1 
ATOM   3517 O OG   B SER   A 1 139 ? 17.318 -8.527  -2.456  0.58 12.14 ?  139 SER   A OG   1 
ATOM   3518 H H    A SER   A 1 139 ? 14.506 -9.516  -4.506  0.42 13.78 ?  139 SER   A H    1 
ATOM   3519 H H    B SER   A 1 139 ? 14.523 -9.758  -4.732  0.58 16.89 ?  139 SER   A H    1 
ATOM   3520 H HA   A SER   A 1 139 ? 16.874 -10.222 -3.699  0.42 13.29 ?  139 SER   A HA   1 
ATOM   3521 H HA   B SER   A 1 139 ? 16.902 -10.551 -4.014  0.58 15.78 ?  139 SER   A HA   1 
ATOM   3522 H HB2  A SER   A 1 139 ? 16.317 -7.970  -3.805  0.42 13.22 ?  139 SER   A HB2  1 
ATOM   3523 H HB2  B SER   A 1 139 ? 16.383 -8.281  -4.146  0.58 15.30 ?  139 SER   A HB2  1 
ATOM   3524 H HB3  A SER   A 1 139 ? 15.275 -8.160  -2.620  0.42 13.22 ?  139 SER   A HB3  1 
ATOM   3525 H HB3  B SER   A 1 139 ? 15.407 -8.432  -2.899  0.58 15.30 ?  139 SER   A HB3  1 
ATOM   3526 H HG   A SER   A 1 139 ? 17.194 -7.383  -1.873  0.42 12.73 ?  139 SER   A HG   1 
ATOM   3527 H HG   B SER   A 1 139 ? 17.387 -7.712  -2.280  0.58 14.59 ?  139 SER   A HG   1 
ATOM   3528 N N    A LEU   A 1 140 ? 14.571 -10.951 -1.621  0.42 11.44 ?  140 LEU   A N    1 
ATOM   3529 N N    B LEU   A 1 140 ? 14.634 -11.009 -1.781  0.58 12.83 ?  140 LEU   A N    1 
ATOM   3530 C CA   A LEU   A 1 140 ? 14.319 -11.806 -0.467  0.42 11.48 ?  140 LEU   A CA   1 
ATOM   3531 C CA   B LEU   A 1 140 ? 14.357 -11.771 -0.566  0.58 12.15 ?  140 LEU   A CA   1 
ATOM   3532 C C    A LEU   A 1 140 ? 14.617 -13.269 -0.786  0.42 11.85 ?  140 LEU   A C    1 
ATOM   3533 C C    B LEU   A 1 140 ? 14.628 -13.256 -0.776  0.58 12.20 ?  140 LEU   A C    1 
ATOM   3534 O O    A LEU   A 1 140 ? 15.210 -13.981 0.034   0.42 11.96 ?  140 LEU   A O    1 
ATOM   3535 O O    B LEU   A 1 140 ? 15.185 -13.925 0.104   0.58 12.61 ?  140 LEU   A O    1 
ATOM   3536 C CB   A LEU   A 1 140 ? 12.879 -11.632 0.008   0.42 11.74 ?  140 LEU   A CB   1 
ATOM   3537 C CB   B LEU   A 1 140 ? 12.913 -11.542 -0.112  0.58 12.52 ?  140 LEU   A CB   1 
ATOM   3538 C CG   A LEU   A 1 140 ? 12.478 -12.560 1.154   0.42 12.02 ?  140 LEU   A CG   1 
ATOM   3539 C CG   B LEU   A 1 140 ? 12.440 -12.368 1.092   0.58 13.28 ?  140 LEU   A CG   1 
ATOM   3540 C CD1  A LEU   A 1 140 ? 13.373 -12.342 2.364   0.42 12.15 ?  140 LEU   A CD1  1 
ATOM   3541 C CD1  B LEU   A 1 140 ? 13.283 -12.094 2.326   0.58 13.05 ?  140 LEU   A CD1  1 
ATOM   3542 C CD2  A LEU   A 1 140 ? 11.021 -12.332 1.510   0.42 12.39 ?  140 LEU   A CD2  1 
ATOM   3543 C CD2  B LEU   A 1 140 ? 10.971 -12.089 1.384   0.58 13.86 ?  140 LEU   A CD2  1 
ATOM   3544 H H    A LEU   A 1 140 ? 13.872 -10.579 -1.966  0.42 13.75 ?  140 LEU   A H    1 
ATOM   3545 H H    B LEU   A 1 140 ? 13.967 -10.573 -2.094  0.58 15.43 ?  140 LEU   A H    1 
ATOM   3546 H HA   A LEU   A 1 140 ? 14.905 -11.531 0.253   0.42 13.81 ?  140 LEU   A HA   1 
ATOM   3547 H HA   B LEU   A 1 140 ? 14.944 -11.461 0.140   0.58 14.61 ?  140 LEU   A HA   1 
ATOM   3548 H HB2  A LEU   A 1 140 ? 12.763 -10.718 0.316   0.42 14.12 ?  140 LEU   A HB2  1 
ATOM   3549 H HB2  B LEU   A 1 140 ? 12.815 -10.609 0.126   0.58 15.06 ?  140 LEU   A HB2  1 
ATOM   3550 H HB3  A LEU   A 1 140 ? 12.283 -11.806 -0.735  0.42 14.12 ?  140 LEU   A HB3  1 
ATOM   3551 H HB3  B LEU   A 1 140 ? 12.324 -11.754 -0.850  0.58 15.06 ?  140 LEU   A HB3  1 
ATOM   3552 H HG   A LEU   A 1 140 ? 12.576 -13.481 0.868   0.42 14.46 ?  140 LEU   A HG   1 
ATOM   3553 H HG   B LEU   A 1 140 ? 12.523 -13.312 0.885   0.58 15.96 ?  140 LEU   A HG   1 
ATOM   3554 H HD11 A LEU   A 1 140 ? 13.013 -12.842 3.112   0.42 14.60 ?  140 LEU   A HD11 1 
ATOM   3555 H HD11 B LEU   A 1 140 ? 12.914 -12.588 3.075   0.58 15.68 ?  140 LEU   A HD11 1 
ATOM   3556 H HD12 A LEU   A 1 140 ? 14.269 -12.656 2.158   0.42 14.60 ?  140 LEU   A HD12 1 
ATOM   3557 H HD12 B LEU   A 1 140 ? 14.193 -12.380 2.157   0.58 15.68 ?  140 LEU   A HD12 1 
ATOM   3558 H HD13 A LEU   A 1 140 ? 13.393 -11.397 2.576   0.42 14.60 ?  140 LEU   A HD13 1 
ATOM   3559 H HD13 B LEU   A 1 140 ? 13.262 -11.143 2.515   0.58 15.68 ?  140 LEU   A HD13 1 
ATOM   3560 H HD21 A LEU   A 1 140 ? 10.779 -12.926 2.235   0.42 14.90 ?  140 LEU   A HD21 1 
ATOM   3561 H HD21 B LEU   A 1 140 ? 10.686 -12.643 2.129   0.58 16.66 ?  140 LEU   A HD21 1 
ATOM   3562 H HD22 A LEU   A 1 140 ? 10.906 -11.408 1.783   0.42 14.90 ?  140 LEU   A HD22 1 
ATOM   3563 H HD22 B LEU   A 1 140 ? 10.868 -11.152 1.611   0.58 16.66 ?  140 LEU   A HD22 1 
ATOM   3564 H HD23 A LEU   A 1 140 ? 10.475 -12.517 0.730   0.42 14.90 ?  140 LEU   A HD23 1 
ATOM   3565 H HD23 B LEU   A 1 140 ? 10.448 -12.301 0.596   0.58 16.66 ?  140 LEU   A HD23 1 
ATOM   3566 N N    A ARG   A 1 141 ? 14.220 -13.735 -1.974  0.42 12.53 ?  141 ARG   A N    1 
ATOM   3567 N N    B ARG   A 1 141 ? 14.250 -13.792 -1.941  0.58 12.58 ?  141 ARG   A N    1 
ATOM   3568 C CA   A ARG   A 1 141 ? 14.466 -15.125 -2.352  0.42 13.45 ?  141 ARG   A CA   1 
ATOM   3569 C CA   B ARG   A 1 141 ? 14.511 -15.201 -2.211  0.58 13.37 ?  141 ARG   A CA   1 
ATOM   3570 C C    A ARG   A 1 141 ? 15.957 -15.444 -2.314  0.42 12.74 ?  141 ARG   A C    1 
ATOM   3571 C C    B ARG   A 1 141 ? 16.006 -15.478 -2.295  0.58 12.61 ?  141 ARG   A C    1 
ATOM   3572 O O    A ARG   A 1 141 ? 16.381 -16.437 -1.712  0.42 12.66 ?  141 ARG   A O    1 
ATOM   3573 O O    B ARG   A 1 141 ? 16.481 -16.492 -1.769  0.58 12.71 ?  141 ARG   A O    1 
ATOM   3574 C CB   A ARG   A 1 141 ? 13.884 -15.375 -3.747  0.42 14.64 ?  141 ARG   A CB   1 
ATOM   3575 C CB   B ARG   A 1 141 ? 13.801 -15.643 -3.491  0.58 14.49 ?  141 ARG   A CB   1 
ATOM   3576 C CG   A ARG   A 1 141 ? 13.889 -16.826 -4.202  0.42 16.29 ?  141 ARG   A CG   1 
ATOM   3577 C CG   B ARG   A 1 141 ? 13.933 -17.138 -3.786  0.58 15.74 ?  141 ARG   A CG   1 
ATOM   3578 C CD   A ARG   A 1 141 ? 12.865 -17.643 -3.444  0.42 17.41 ?  141 ARG   A CD   1 
ATOM   3579 C CD   B ARG   A 1 141 ? 13.301 -17.985 -2.694  0.58 16.72 ?  141 ARG   A CD   1 
ATOM   3580 N NE   A ARG   A 1 141 ? 13.478 -18.472 -2.416  0.42 18.22 ?  141 ARG   A NE   1 
ATOM   3581 N NE   B ARG   A 1 141 ? 11.877 -17.710 -2.558  0.58 17.69 ?  141 ARG   A NE   1 
ATOM   3582 C CZ   A ARG   A 1 141 ? 12.808 -19.050 -1.429  0.42 18.70 ?  141 ARG   A CZ   1 
ATOM   3583 C CZ   B ARG   A 1 141 ? 11.097 -18.239 -1.626  0.58 17.90 ?  141 ARG   A CZ   1 
ATOM   3584 N NH1  A ARG   A 1 141 ? 11.505 -18.869 -1.279  0.42 19.18 ?  141 ARG   A NH1  1 
ATOM   3585 N NH1  B ARG   A 1 141 ? 11.572 -19.080 -0.720  0.58 18.27 ?  141 ARG   A NH1  1 
ATOM   3586 N NH2  A ARG   A 1 141 ? 13.460 -19.825 -0.568  0.42 18.84 ?  141 ARG   A NH2  1 
ATOM   3587 N NH2  B ARG   A 1 141 ? 9.806  -17.916 -1.601  0.58 18.25 ?  141 ARG   A NH2  1 
ATOM   3588 H H    A ARG   A 1 141 ? 13.817 -13.268 -2.575  0.42 15.07 ?  141 ARG   A H    1 
ATOM   3589 H H    B ARG   A 1 141 ? 13.855 -13.369 -2.573  0.58 15.13 ?  141 ARG   A H    1 
ATOM   3590 H HA   A ARG   A 1 141 ? 14.019 -15.709 -1.725  0.42 16.16 ?  141 ARG   A HA   1 
ATOM   3591 H HA   B ARG   A 1 141 ? 14.160 -15.723 -1.478  0.58 16.07 ?  141 ARG   A HA   1 
ATOM   3592 H HB2  A ARG   A 1 141 ? 12.962 -15.071 -3.755  0.42 17.60 ?  141 ARG   A HB2  1 
ATOM   3593 H HB2  B ARG   A 1 141 ? 12.855 -15.443 -3.411  0.58 17.42 ?  141 ARG   A HB2  1 
ATOM   3594 H HB3  A ARG   A 1 141 ? 14.397 -14.869 -4.393  0.42 17.60 ?  141 ARG   A HB3  1 
ATOM   3595 H HB3  B ARG   A 1 141 ? 14.176 -15.161 -4.244  0.58 17.42 ?  141 ARG   A HB3  1 
ATOM   3596 H HG2  A ARG   A 1 141 ? 13.672 -16.870 -5.147  0.42 19.58 ?  141 ARG   A HG2  1 
ATOM   3597 H HG2  B ARG   A 1 141 ? 13.485 -17.339 -4.623  0.58 18.92 ?  141 ARG   A HG2  1 
ATOM   3598 H HG3  A ARG   A 1 141 ? 14.764 -17.215 -4.043  0.42 19.58 ?  141 ARG   A HG3  1 
ATOM   3599 H HG3  B ARG   A 1 141 ? 14.874 -17.373 -3.848  0.58 18.92 ?  141 ARG   A HG3  1 
ATOM   3600 H HD2  A ARG   A 1 141 ? 12.237 -17.044 -3.009  0.42 20.92 ?  141 ARG   A HD2  1 
ATOM   3601 H HD2  B ARG   A 1 141 ? 13.407 -18.919 -2.919  0.58 20.09 ?  141 ARG   A HD2  1 
ATOM   3602 H HD3  A ARG   A 1 141 ? 12.394 -18.223 -4.065  0.42 20.92 ?  141 ARG   A HD3  1 
ATOM   3603 H HD3  B ARG   A 1 141 ? 13.730 -17.797 -1.844  0.58 20.09 ?  141 ARG   A HD3  1 
ATOM   3604 H HE   A ARG   A 1 141 ? 14.311 -18.668 -2.503  0.42 21.89 ?  141 ARG   A HE   1 
ATOM   3605 H HE   B ARG   A 1 141 ? 11.511 -17.184 -3.134  0.58 21.26 ?  141 ARG   A HE   1 
ATOM   3606 H HH11 A ARG   A 1 141 ? 11.070 -18.375 -1.832  0.42 23.05 ?  141 ARG   A HH11 1 
ATOM   3607 H HH11 B ARG   A 1 141 ? 12.401 -19.298 -0.729  0.58 21.95 ?  141 ARG   A HH11 1 
ATOM   3608 H HH12 A ARG   A 1 141 ? 11.092 -19.252 -0.629  0.42 23.05 ?  141 ARG   A HH12 1 
ATOM   3609 H HH12 B ARG   A 1 141 ? 11.044 -19.412 -0.128  0.58 21.95 ?  141 ARG   A HH12 1 
ATOM   3610 H HH21 A ARG   A 1 141 ? 14.307 -19.948 -0.657  0.42 22.63 ?  141 ARG   A HH21 1 
ATOM   3611 H HH21 B ARG   A 1 141 ? 9.487  -17.372 -2.187  0.58 21.92 ?  141 ARG   A HH21 1 
ATOM   3612 H HH22 A ARG   A 1 141 ? 13.038 -20.200 0.080   0.42 22.63 ?  141 ARG   A HH22 1 
ATOM   3613 H HH22 B ARG   A 1 141 ? 9.287  -18.254 -1.004  0.58 21.92 ?  141 ARG   A HH22 1 
ATOM   3614 N N    . VAL   A 1 142 ? 16.767 -14.599 -2.952  1.00 12.67 ?  142 VAL   A N    1 
ATOM   3615 C CA   . VAL   A 1 142 ? 18.212 -14.797 -2.983  1.00 12.22 ?  142 VAL   A CA   1 
ATOM   3616 C C    . VAL   A 1 142 ? 18.783 -14.754 -1.573  1.00 11.51 ?  142 VAL   A C    1 
ATOM   3617 O O    . VAL   A 1 142 ? 19.653 -15.557 -1.216  1.00 11.95 ?  142 VAL   A O    1 
ATOM   3618 C CB   . VAL   A 1 142 ? 18.886 -13.773 -3.915  1.00 12.75 ?  142 VAL   A CB   1 
ATOM   3619 C CG1  . VAL   A 1 142 ? 20.395 -13.964 -3.900  1.00 12.77 ?  142 VAL   A CG1  1 
ATOM   3620 C CG2  . VAL   A 1 142 ? 18.369 -13.905 -5.336  1.00 14.47 ?  142 VAL   A CG2  1 
ATOM   3621 H H    A VAL   A 1 142 ? 16.504 -13.898 -3.377  0.42 15.23 ?  142 VAL   A H    1 
ATOM   3622 H H    B VAL   A 1 142 ? 16.484 -13.903 -3.372  0.58 15.23 ?  142 VAL   A H    1 
ATOM   3623 H HA   . VAL   A 1 142 ? 18.401 -15.671 -3.344  1.00 14.69 ?  142 VAL   A HA   1 
ATOM   3624 H HB   . VAL   A 1 142 ? 18.695 -12.868 -3.601  1.00 15.33 ?  142 VAL   A HB   1 
ATOM   3625 H HG11 . VAL   A 1 142 ? 20.782 -13.467 -4.638  1.00 15.35 ?  142 VAL   A HG11 1 
ATOM   3626 H HG12 . VAL   A 1 142 ? 20.750 -13.632 -3.059  1.00 15.35 ?  142 VAL   A HG12 1 
ATOM   3627 H HG13 . VAL   A 1 142 ? 20.590 -14.906 -3.996  1.00 15.35 ?  142 VAL   A HG13 1 
ATOM   3628 H HG21 . VAL   A 1 142 ? 18.768 -13.208 -5.884  1.00 17.39 ?  142 VAL   A HG21 1 
ATOM   3629 H HG22 . VAL   A 1 142 ? 18.613 -14.775 -5.677  1.00 17.39 ?  142 VAL   A HG22 1 
ATOM   3630 H HG23 . VAL   A 1 142 ? 17.405 -13.805 -5.333  1.00 17.39 ?  142 VAL   A HG23 1 
ATOM   3631 N N    . CYS   A 1 143 ? 18.317 -13.813 -0.751  1.00 11.37 ?  143 CYS   A N    1 
ATOM   3632 C CA   . CYS   A 1 143 ? 18.782 -13.741 0.630   1.00 11.31 ?  143 CYS   A CA   1 
ATOM   3633 C C    . CYS   A 1 143 ? 18.547 -15.066 1.347   1.00 11.33 ?  143 CYS   A C    1 
ATOM   3634 O O    . CYS   A 1 143 ? 19.460 -15.646 1.942   1.00 11.18 ?  143 CYS   A O    1 
ATOM   3635 C CB   . CYS   A 1 143 ? 18.051 -12.611 1.348   1.00 12.14 ?  143 CYS   A CB   1 
ATOM   3636 S SG   . CYS   A 1 143 ? 18.544 -12.397 3.075   1.00 12.52 ?  143 CYS   A SG   1 
ATOM   3637 H H    . CYS   A 1 143 ? 17.737 -13.218 -0.962  1.00 13.67 ?  143 CYS   A H    1 
ATOM   3638 H HA   . CYS   A 1 143 ? 19.733 -13.557 0.645   1.00 13.60 ?  143 CYS   A HA   1 
ATOM   3639 H HB2  . CYS   A 1 143 ? 18.224 -11.781 0.882   1.00 14.59 ?  143 CYS   A HB2  1 
ATOM   3640 H HB3  . CYS   A 1 143 ? 17.102 -12.800 1.334   1.00 14.59 ?  143 CYS   A HB3  1 
ATOM   3641 H HG   . CYS   A 1 143 ? 17.942 -11.472 3.541   1.00 15.05 ?  143 CYS   A HG   1 
ATOM   3642 N N    . VAL   A 1 144 ? 17.315 -15.567 1.291   1.00 11.69 ?  144 VAL   A N    1 
ATOM   3643 C CA   . VAL   A 1 144 ? 16.964 -16.799 1.988   1.00 12.55 ?  144 VAL   A CA   1 
ATOM   3644 C C    . VAL   A 1 144 ? 17.796 -17.971 1.491   1.00 12.22 ?  144 VAL   A C    1 
ATOM   3645 O O    . VAL   A 1 144 ? 18.166 -18.857 2.270   1.00 13.09 ?  144 VAL   A O    1 
ATOM   3646 C CB   . VAL   A 1 144 ? 15.454 -17.042 1.816   1.00 14.47 ?  144 VAL   A CB   1 
ATOM   3647 C CG1  . VAL   A 1 144 ? 15.082 -18.483 2.102   1.00 15.84 ?  144 VAL   A CG1  1 
ATOM   3648 C CG2  . VAL   A 1 144 ? 14.671 -16.073 2.698   1.00 14.77 ?  144 VAL   A CG2  1 
ATOM   3649 H H    . VAL   A 1 144 ? 16.663 -15.216 0.851   1.00 14.06 ?  144 VAL   A H    1 
ATOM   3650 H HA   . VAL   A 1 144 ? 17.135 -16.690 2.932   1.00 15.09 ?  144 VAL   A HA   1 
ATOM   3651 H HB   . VAL   A 1 144 ? 15.206 -16.859 0.894   1.00 17.39 ?  144 VAL   A HB   1 
ATOM   3652 H HG11 . VAL   A 1 144 ? 14.120 -18.540 2.245   1.00 19.03 ?  144 VAL   A HG11 1 
ATOM   3653 H HG12 . VAL   A 1 144 ? 15.329 -19.035 1.344   1.00 19.03 ?  144 VAL   A HG12 1 
ATOM   3654 H HG13 . VAL   A 1 144 ? 15.547 -18.777 2.899   1.00 19.03 ?  144 VAL   A HG13 1 
ATOM   3655 H HG21 . VAL   A 1 144 ? 13.719 -16.262 2.623   1.00 17.75 ?  144 VAL   A HG21 1 
ATOM   3656 H HG22 . VAL   A 1 144 ? 14.952 -16.182 3.620   1.00 17.75 ?  144 VAL   A HG22 1 
ATOM   3657 H HG23 . VAL   A 1 144 ? 14.846 -15.163 2.406   1.00 17.75 ?  144 VAL   A HG23 1 
ATOM   3658 N N    . ASP   A 1 145 ? 18.083 -18.010 0.192   1.00 12.64 ?  145 ASP   A N    1 
ATOM   3659 C CA   . ASP   A 1 145 ? 18.796 -19.124 -0.422  1.00 13.22 ?  145 ASP   A CA   1 
ATOM   3660 C C    . ASP   A 1 145 ? 20.314 -18.975 -0.363  1.00 12.92 ?  145 ASP   A C    1 
ATOM   3661 O O    . ASP   A 1 145 ? 21.026 -19.873 -0.823  1.00 15.25 ?  145 ASP   A O    1 
ATOM   3662 C CB   . ASP   A 1 145 ? 18.355 -19.280 -1.880  1.00 14.55 ?  145 ASP   A CB   1 
ATOM   3663 C CG   . ASP   A 1 145 ? 16.926 -19.770 -2.011  1.00 16.52 ?  145 ASP   A CG   1 
ATOM   3664 O OD1  . ASP   A 1 145 ? 16.366 -20.302 -1.022  1.00 17.38 ?  145 ASP   A OD1  1 
ATOM   3665 O OD2  . ASP   A 1 145 ? 16.365 -19.614 -3.116  1.00 18.08 -1 145 ASP   A OD2  1 
ATOM   3666 H H    . ASP   A 1 145 ? 17.860 -17.391 -0.369  1.00 15.19 ?  145 ASP   A H    1 
ATOM   3667 H HA   . ASP   A 1 145 ? 18.560 -19.939 0.043   1.00 15.89 ?  145 ASP   A HA   1 
ATOM   3668 H HB2  . ASP   A 1 145 ? 18.419 -18.417 -2.327  1.00 17.49 ?  145 ASP   A HB2  1 
ATOM   3669 H HB3  . ASP   A 1 145 ? 18.937 -19.919 -2.322  1.00 17.49 ?  145 ASP   A HB3  1 
ATOM   3670 N N    . THR   A 1 146 ? 20.823 -17.874 0.179   1.00 11.83 ?  146 THR   A N    1 
ATOM   3671 C CA   . THR   A 1 146 ? 22.257 -17.602 0.204   1.00 11.26 ?  146 THR   A CA   1 
ATOM   3672 C C    . THR   A 1 146 ? 22.806 -17.407 1.606   1.00 11.10 ?  146 THR   A C    1 
ATOM   3673 O O    . THR   A 1 146 ? 23.888 -17.922 1.922   1.00 11.99 ?  146 THR   A O    1 
ATOM   3674 C CB   . THR   A 1 146 ? 22.568 -16.348 -0.638  1.00 11.37 ?  146 THR   A CB   1 
ATOM   3675 O OG1  . THR   A 1 146 ? 22.060 -16.525 -1.962  1.00 11.78 ?  146 THR   A OG1  1 
ATOM   3676 C CG2  . THR   A 1 146 ? 24.062 -16.091 -0.716  1.00 12.05 ?  146 THR   A CG2  1 
ATOM   3677 H H    . THR   A 1 146 ? 20.350 -17.255 0.544   1.00 14.23 ?  146 THR   A H    1 
ATOM   3678 H HA   . THR   A 1 146 ? 22.732 -18.343 -0.193  1.00 13.54 ?  146 THR   A HA   1 
ATOM   3679 H HB   . THR   A 1 146 ? 22.147 -15.569 -0.238  1.00 13.67 ?  146 THR   A HB   1 
ATOM   3680 H HG1  . THR   A 1 146 ? 21.228 -16.628 -1.940  1.00 14.16 ?  146 THR   A HG1  1 
ATOM   3681 H HG21 . THR   A 1 146 ? 24.246 -15.427 -1.400  1.00 14.49 ?  146 THR   A HG21 1 
ATOM   3682 H HG22 . THR   A 1 146 ? 24.385 -15.758 0.137   1.00 14.49 ?  146 THR   A HG22 1 
ATOM   3683 H HG23 . THR   A 1 146 ? 24.525 -16.909 -0.936  1.00 14.49 ?  146 THR   A HG23 1 
ATOM   3684 N N    . VAL   A 1 147 ? 22.112 -16.634 2.437   1.00 10.79 ?  147 VAL   A N    1 
ATOM   3685 C CA   . VAL   A 1 147 ? 22.588 -16.328 3.777   1.00 10.78 ?  147 VAL   A CA   1 
ATOM   3686 C C    . VAL   A 1 147 ? 22.267 -17.500 4.690   1.00 11.42 ?  147 VAL   A C    1 
ATOM   3687 O O    . VAL   A 1 147 ? 21.124 -17.977 4.727   1.00 11.98 ?  147 VAL   A O    1 
ATOM   3688 C CB   . VAL   A 1 147 ? 21.953 -15.027 4.288   1.00 11.16 ?  147 VAL   A CB   1 
ATOM   3689 C CG1  . VAL   A 1 147 ? 22.456 -14.699 5.664   1.00 12.27 ?  147 VAL   A CG1  1 
ATOM   3690 C CG2  . VAL   A 1 147 ? 22.223 -13.877 3.310   1.00 11.42 ?  147 VAL   A CG2  1 
ATOM   3691 H H    . VAL   A 1 147 ? 21.345 -16.283 2.253   1.00 12.98 ?  147 VAL   A H    1 
ATOM   3692 H HA   . VAL   A 1 147 ? 23.550 -16.208 3.755   1.00 12.97 ?  147 VAL   A HA   1 
ATOM   3693 H HB   . VAL   A 1 147 ? 20.992 -15.148 4.348   1.00 13.42 ?  147 VAL   A HB   1 
ATOM   3694 H HG11 . VAL   A 1 147 ? 22.186 -13.795 5.892   1.00 14.76 ?  147 VAL   A HG11 1 
ATOM   3695 H HG12 . VAL   A 1 147 ? 22.075 -15.326 6.300   1.00 14.76 ?  147 VAL   A HG12 1 
ATOM   3696 H HG13 . VAL   A 1 147 ? 23.423 -14.766 5.671   1.00 14.76 ?  147 VAL   A HG13 1 
ATOM   3697 H HG21 . VAL   A 1 147 ? 21.883 -13.053 3.694   1.00 13.73 ?  147 VAL   A HG21 1 
ATOM   3698 H HG22 . VAL   A 1 147 ? 23.172 -13.810 3.158   1.00 13.73 ?  147 VAL   A HG22 1 
ATOM   3699 H HG23 . VAL   A 1 147 ? 21.761 -14.065 2.475   1.00 13.73 ?  147 VAL   A HG23 1 
ATOM   3700 N N    . ARG   A 1 148 ? 23.283 -17.956 5.428   1.00 11.37 ?  148 ARG   A N    1 
ATOM   3701 C CA   . ARG   A 1 148 ? 23.150 -19.035 6.391   1.00 11.84 ?  148 ARG   A CA   1 
ATOM   3702 C C    . ARG   A 1 148 ? 23.276 -18.568 7.828   1.00 11.70 ?  148 ARG   A C    1 
ATOM   3703 O O    . ARG   A 1 148 ? 22.866 -19.296 8.739   1.00 13.12 ?  148 ARG   A O    1 
ATOM   3704 C CB   . ARG   A 1 148 ? 24.193 -20.128 6.120   1.00 12.38 ?  148 ARG   A CB   1 
ATOM   3705 C CG   . ARG   A 1 148 ? 24.030 -20.777 4.760   1.00 13.57 ?  148 ARG   A CG   1 
ATOM   3706 C CD   . ARG   A 1 148 ? 25.115 -21.806 4.474   1.00 14.36 ?  148 ARG   A CD   1 
ATOM   3707 N NE   . ARG   A 1 148 ? 26.453 -21.225 4.481   1.00 14.25 ?  148 ARG   A NE   1 
ATOM   3708 C CZ   . ARG   A 1 148 ? 26.959 -20.494 3.497   1.00 13.50 ?  148 ARG   A CZ   1 
ATOM   3709 N NH1  . ARG   A 1 148 ? 26.277 -20.255 2.388   1.00 13.96 ?  148 ARG   A NH1  1 
ATOM   3710 N NH2  . ARG   A 1 148 ? 28.180 -19.980 3.632   1.00 13.97 ?  148 ARG   A NH2  1 
ATOM   3711 H H    . ARG   A 1 148 ? 24.087 -17.640 5.375   1.00 13.67 ?  148 ARG   A H    1 
ATOM   3712 H HA   . ARG   A 1 148 ? 22.275 -19.431 6.288   1.00 14.23 ?  148 ARG   A HA   1 
ATOM   3713 H HB2  . ARG   A 1 148 ? 25.079 -19.743 6.165   1.00 14.88 ?  148 ARG   A HB2  1 
ATOM   3714 H HB3  . ARG   A 1 148 ? 24.098 -20.824 6.792   1.00 14.88 ?  148 ARG   A HB3  1 
ATOM   3715 H HG2  . ARG   A 1 148 ? 23.171 -21.222 4.724   1.00 16.31 ?  148 ARG   A HG2  1 
ATOM   3716 H HG3  . ARG   A 1 148 ? 24.080 -20.088 4.079   1.00 16.31 ?  148 ARG   A HG3  1 
ATOM   3717 H HD2  . ARG   A 1 148 ? 25.087 -22.497 5.156   1.00 17.26 ?  148 ARG   A HD2  1 
ATOM   3718 H HD3  . ARG   A 1 148 ? 24.960 -22.198 3.600   1.00 17.26 ?  148 ARG   A HD3  1 
ATOM   3719 H HE   . ARG   A 1 148 ? 26.952 -21.371 5.165   1.00 17.13 ?  148 ARG   A HE   1 
ATOM   3720 H HH11 . ARG   A 1 148 ? 25.487 -20.576 2.288   1.00 16.78 ?  148 ARG   A HH11 1 
ATOM   3721 H HH12 . ARG   A 1 148 ? 26.628 -19.776 1.762   1.00 16.78 ?  148 ARG   A HH12 1 
ATOM   3722 H HH21 . ARG   A 1 148 ? 28.636 -20.132 4.342   1.00 16.79 ?  148 ARG   A HH21 1 
ATOM   3723 H HH22 . ARG   A 1 148 ? 28.523 -19.507 2.996   1.00 16.79 ?  148 ARG   A HH22 1 
ATOM   3724 N N    . THR   A 1 149 ? 23.831 -17.382 8.048   1.00 11.87 ?  149 THR   A N    1 
ATOM   3725 C CA   . THR   A 1 149 ? 23.905 -16.788 9.367   1.00 11.96 ?  149 THR   A CA   1 
ATOM   3726 C C    . THR   A 1 149 ? 22.573 -16.103 9.672   1.00 11.17 ?  149 THR   A C    1 
ATOM   3727 O O    . THR   A 1 149 ? 21.637 -16.104 8.857   1.00 12.15 ?  149 THR   A O    1 
ATOM   3728 C CB   . THR   A 1 149 ? 25.100 -15.842 9.420   1.00 12.12 ?  149 THR   A CB   1 
ATOM   3729 O OG1  . THR   A 1 149 ? 24.964 -14.913 8.342   1.00 12.25 ?  149 THR   A OG1  1 
ATOM   3730 C CG2  . THR   A 1 149 ? 26.406 -16.632 9.287   1.00 12.89 ?  149 THR   A CG2  1 
ATOM   3731 H H    . THR   A 1 149 ? 24.183 -16.893 7.432   1.00 14.27 ?  149 THR   A H    1 
ATOM   3732 H HA   . THR   A 1 149 ? 24.044 -17.493 10.023  1.00 14.38 ?  149 THR   A HA   1 
ATOM   3733 H HB   . THR   A 1 149 ? 25.098 -15.370 10.266  1.00 14.57 ?  149 THR   A HB   1 
ATOM   3734 H HG1  . THR   A 1 149 ? 25.611 -14.376 8.345   1.00 14.73 ?  149 THR   A HG1  1 
ATOM   3735 H HG21 . THR   A 1 149 ? 27.165 -16.032 9.346   1.00 15.50 ?  149 THR   A HG21 1 
ATOM   3736 H HG22 . THR   A 1 149 ? 26.472 -17.294 9.996   1.00 15.50 ?  149 THR   A HG22 1 
ATOM   3737 H HG23 . THR   A 1 149 ? 26.435 -17.092 8.430   1.00 15.50 ?  149 THR   A HG23 1 
ATOM   3738 N N    . ASN   A 1 150 ? 22.445 -15.560 10.877  1.00 11.81 ?  150 ASN   A N    1 
ATOM   3739 C CA   . ASN   A 1 150 ? 21.155 -15.058 11.344  1.00 12.08 ?  150 ASN   A CA   1 
ATOM   3740 C C    . ASN   A 1 150 ? 20.970 -13.625 10.877  1.00 11.69 ?  150 ASN   A C    1 
ATOM   3741 O O    . ASN   A 1 150 ? 21.707 -12.728 11.298  1.00 13.10 ?  150 ASN   A O    1 
ATOM   3742 C CB   . ASN   A 1 150 ? 21.062 -15.173 12.858  1.00 14.15 ?  150 ASN   A CB   1 
ATOM   3743 C CG   . ASN   A 1 150 ? 20.976 -16.609 13.313  1.00 17.68 ?  150 ASN   A CG   1 
ATOM   3744 O OD1  . ASN   A 1 150 ? 20.421 -17.456 12.614  1.00 18.97 ?  150 ASN   A OD1  1 
ATOM   3745 N ND2  . ASN   A 1 150 ? 21.552 -16.902 14.471  1.00 20.06 ?  150 ASN   A ND2  1 
ATOM   3746 H H    . ASN   A 1 150 ? 23.091 -15.466 11.444  1.00 14.19 ?  150 ASN   A H    1 
ATOM   3747 H HA   . ASN   A 1 150 ? 20.449 -15.598 10.960  1.00 14.52 ?  150 ASN   A HA   1 
ATOM   3748 H HB2  . ASN   A 1 150 ? 21.850 -14.776 13.260  1.00 17.00 ?  150 ASN   A HB2  1 
ATOM   3749 H HB3  . ASN   A 1 150 ? 20.264 -14.712 13.164  1.00 17.00 ?  150 ASN   A HB3  1 
ATOM   3750 H HD21 . ASN   A 1 150 ? 21.532 -17.711 14.774  1.00 24.10 ?  150 ASN   A HD21 1 
ATOM   3751 H HD22 . ASN   A 1 150 ? 21.940 -16.287 14.930  1.00 24.10 ?  150 ASN   A HD22 1 
ATOM   3752 N N    . VAL   A 1 151 ? 19.982 -13.408 10.018  1.00 11.25 ?  151 VAL   A N    1 
ATOM   3753 C CA   . VAL   A 1 151 ? 19.766 -12.109 9.408   1.00 11.14 ?  151 VAL   A CA   1 
ATOM   3754 C C    . VAL   A 1 151 ? 18.372 -11.608 9.753   1.00 10.96 ?  151 VAL   A C    1 
ATOM   3755 O O    . VAL   A 1 151 ? 17.373 -12.324 9.592   1.00 12.08 ?  151 VAL   A O    1 
ATOM   3756 C CB   . VAL   A 1 151 ? 20.076 -12.106 7.897   1.00 12.11 ?  151 VAL   A CB   1 
ATOM   3757 C CG1  . VAL   A 1 151 ? 19.252 -13.116 7.136   1.00 13.13 ?  151 VAL   A CG1  1 
ATOM   3758 C CG2  . VAL   A 1 151 ? 19.917 -10.707 7.325   1.00 12.62 ?  151 VAL   A CG2  1 
ATOM   3759 H H    . VAL   A 1 151 ? 19.412 -14.009 9.777   1.00 13.52 ?  151 VAL   A H    1 
ATOM   3760 H HA   . VAL   A 1 151 ? 20.393 -11.487 9.811   1.00 13.40 ?  151 VAL   A HA   1 
ATOM   3761 H HB   . VAL   A 1 151 ? 21.011 -12.353 7.778   1.00 14.56 ?  151 VAL   A HB   1 
ATOM   3762 H HG11 . VAL   A 1 151 ? 19.481 -13.073 6.194   1.00 15.79 ?  151 VAL   A HG11 1 
ATOM   3763 H HG12 . VAL   A 1 151 ? 19.441 -14.004 7.480   1.00 15.79 ?  151 VAL   A HG12 1 
ATOM   3764 H HG13 . VAL   A 1 151 ? 18.310 -12.910 7.256   1.00 15.79 ?  151 VAL   A HG13 1 
ATOM   3765 H HG21 . VAL   A 1 151 ? 20.251 -10.703 6.412   1.00 15.17 ?  151 VAL   A HG21 1 
ATOM   3766 H HG22 . VAL   A 1 151 ? 18.982 -10.466 7.337   1.00 15.17 ?  151 VAL   A HG22 1 
ATOM   3767 H HG23 . VAL   A 1 151 ? 20.433 -10.086 7.864   1.00 15.17 ?  151 VAL   A HG23 1 
ATOM   3768 N N    . TYR   A 1 152 ? 18.336 -10.364 10.230  1.00 10.93 ?  152 TYR   A N    1 
ATOM   3769 C CA   . TYR   A 1 152 ? 17.131 -9.641  10.604  1.00 10.76 ?  152 TYR   A CA   1 
ATOM   3770 C C    . TYR   A 1 152 ? 16.925 -8.551  9.565   1.00 10.21 ?  152 TYR   A C    1 
ATOM   3771 O O    . TYR   A 1 152 ? 17.700 -7.589  9.502   1.00 10.74 ?  152 TYR   A O    1 
ATOM   3772 C CB   . TYR   A 1 152 ? 17.311 -9.080  12.013  1.00 11.61 ?  152 TYR   A CB   1 
ATOM   3773 C CG   . TYR   A 1 152 ? 17.263 -10.185 13.038  1.00 12.21 ?  152 TYR   A CG   1 
ATOM   3774 C CD1  . TYR   A 1 152 ? 18.384 -10.950 13.330  1.00 13.79 ?  152 TYR   A CD1  1 
ATOM   3775 C CD2  . TYR   A 1 152 ? 16.079 -10.509 13.674  1.00 12.68 ?  152 TYR   A CD2  1 
ATOM   3776 C CE1  . TYR   A 1 152 ? 18.334 -11.992 14.243  1.00 15.35 ?  152 TYR   A CE1  1 
ATOM   3777 C CE2  . TYR   A 1 152 ? 16.015 -11.551 14.592  1.00 14.34 ?  152 TYR   A CE2  1 
ATOM   3778 C CZ   . TYR   A 1 152 ? 17.146 -12.289 14.873  1.00 15.58 ?  152 TYR   A CZ   1 
ATOM   3779 O OH   . TYR   A 1 152 ? 17.094 -13.327 15.778  1.00 18.18 ?  152 TYR   A OH   1 
ATOM   3780 H H    . TYR   A 1 152 ? 19.050 -9.888  10.337  1.00 13.14 ?  152 TYR   A H    1 
ATOM   3781 H HA   . TYR   A 1 152 ? 16.370 -10.246 10.596  1.00 12.94 ?  152 TYR   A HA   1 
ATOM   3782 H HB2  . TYR   A 1 152 ? 18.174 -8.646  12.076  1.00 13.96 ?  152 TYR   A HB2  1 
ATOM   3783 H HB3  . TYR   A 1 152 ? 16.599 -8.454  12.203  1.00 13.96 ?  152 TYR   A HB3  1 
ATOM   3784 H HD1  . TYR   A 1 152 ? 19.187 -10.755 12.902  1.00 16.58 ?  152 TYR   A HD1  1 
ATOM   3785 H HD2  . TYR   A 1 152 ? 15.310 -10.017 13.483  1.00 15.24 ?  152 TYR   A HD2  1 
ATOM   3786 H HE1  . TYR   A 1 152 ? 19.100 -12.484 14.431  1.00 18.44 ?  152 TYR   A HE1  1 
ATOM   3787 H HE2  . TYR   A 1 152 ? 15.210 -11.744 15.015  1.00 17.24 ?  152 TYR   A HE2  1 
ATOM   3788 H HH   . TYR   A 1 152 ? 16.316 -13.386 16.092  1.00 21.85 ?  152 TYR   A HH   1 
ATOM   3789 N N    . LEU   A 1 153 ? 15.918 -8.733  8.720   1.00 10.70 ?  153 LEU   A N    1 
ATOM   3790 C CA   . LEU   A 1 153 ? 15.645 -7.835  7.609   1.00 11.00 ?  153 LEU   A CA   1 
ATOM   3791 C C    . LEU   A 1 153 ? 14.638 -6.773  8.012   1.00 10.87 ?  153 LEU   A C    1 
ATOM   3792 O O    . LEU   A 1 153 ? 13.537 -7.087  8.482   1.00 12.38 ?  153 LEU   A O    1 
ATOM   3793 C CB   . LEU   A 1 153 ? 15.096 -8.611  6.412   1.00 11.24 ?  153 LEU   A CB   1 
ATOM   3794 C CG   . LEU   A 1 153 ? 16.061 -9.605  5.770   1.00 11.25 ?  153 LEU   A CG   1 
ATOM   3795 C CD1  . LEU   A 1 153 ? 15.308 -10.496 4.799   1.00 11.96 ?  153 LEU   A CD1  1 
ATOM   3796 C CD2  . LEU   A 1 153 ? 17.205 -8.873  5.077   1.00 12.44 ?  153 LEU   A CD2  1 
ATOM   3797 H H    . LEU   A 1 153 ? 15.359 -9.396  8.770   1.00 12.87 ?  153 LEU   A H    1 
ATOM   3798 H HA   . LEU   A 1 153 ? 16.471 -7.406  7.352   1.00 13.22 ?  153 LEU   A HA   1 
ATOM   3799 H HB2  . LEU   A 1 153 ? 14.319 -9.101  6.703   1.00 13.52 ?  153 LEU   A HB2  1 
ATOM   3800 H HB3  . LEU   A 1 153 ? 14.844 -7.964  5.732   1.00 13.52 ?  153 LEU   A HB3  1 
ATOM   3801 H HG   . LEU   A 1 153 ? 16.451 -10.160 6.467   1.00 13.52 ?  153 LEU   A HG   1 
ATOM   3802 H HD11 . LEU   A 1 153 ? 15.915 -11.173 4.461   1.00 14.38 ?  153 LEU   A HD11 1 
ATOM   3803 H HD12 . LEU   A 1 153 ? 14.573 -10.913 5.269   1.00 14.38 ?  153 LEU   A HD12 1 
ATOM   3804 H HD13 . LEU   A 1 153 ? 14.976 -9.952  4.070   1.00 14.38 ?  153 LEU   A HD13 1 
ATOM   3805 H HD21 . LEU   A 1 153 ? 17.777 -9.526  4.646   1.00 14.95 ?  153 LEU   A HD21 1 
ATOM   3806 H HD22 . LEU   A 1 153 ? 16.833 -8.269  4.418   1.00 14.95 ?  153 LEU   A HD22 1 
ATOM   3807 H HD23 . LEU   A 1 153 ? 17.712 -8.374  5.737   1.00 14.95 ?  153 LEU   A HD23 1 
ATOM   3808 N N    A ALA   A 1 154 ? 15.036 -5.512  7.864   0.42 10.66 ?  154 ALA   A N    1 
ATOM   3809 N N    B ALA   A 1 154 ? 14.993 -5.519  7.763   0.58 10.99 ?  154 ALA   A N    1 
ATOM   3810 C CA   A ALA   A 1 154 ? 14.183 -4.368  8.147   0.42 10.79 ?  154 ALA   A CA   1 
ATOM   3811 C CA   B ALA   A 1 154 ? 14.089 -4.391  7.934   0.58 11.28 ?  154 ALA   A CA   1 
ATOM   3812 C C    A ALA   A 1 154 ? 13.673 -3.820  6.824   0.42 10.76 ?  154 ALA   A C    1 
ATOM   3813 C C    B ALA   A 1 154 ? 13.611 -3.940  6.558   0.58 11.24 ?  154 ALA   A C    1 
ATOM   3814 O O    A ALA   A 1 154 ? 14.466 -3.376  5.988   0.42 10.77 ?  154 ALA   A O    1 
ATOM   3815 O O    B ALA   A 1 154 ? 14.423 -3.533  5.719   0.58 12.04 ?  154 ALA   A O    1 
ATOM   3816 C CB   A ALA   A 1 154 ? 14.954 -3.280  8.893   0.42 11.39 ?  154 ALA   A CB   1 
ATOM   3817 C CB   B ALA   A 1 154 ? 14.797 -3.244  8.649   0.58 11.52 ?  154 ALA   A CB   1 
ATOM   3818 H H    A ALA   A 1 154 ? 15.820 -5.286  7.586   0.42 12.82 ?  154 ALA   A H    1 
ATOM   3819 H H    B ALA   A 1 154 ? 15.773 -5.291  7.479   0.58 13.22 ?  154 ALA   A H    1 
ATOM   3820 H HA   A ALA   A 1 154 ? 13.424 -4.639  8.682   0.42 12.98 ?  154 ALA   A HA   1 
ATOM   3821 H HA   B ALA   A 1 154 ? 13.317 -4.665  8.458   0.58 13.57 ?  154 ALA   A HA   1 
ATOM   3822 H HB1  A ALA   A 1 154 ? 14.358 -2.531  9.064   0.42 13.70 ?  154 ALA   A HB1  1 
ATOM   3823 H HB1  B ALA   A 1 154 ? 14.174 -2.508  8.752   0.58 13.85 ?  154 ALA   A HB1  1 
ATOM   3824 H HB2  A ALA   A 1 154 ? 15.275 -3.644  9.730   0.42 13.70 ?  154 ALA   A HB2  1 
ATOM   3825 H HB2  B ALA   A 1 154 ? 15.092 -3.553  9.520   0.58 13.85 ?  154 ALA   A HB2  1 
ATOM   3826 H HB3  A ALA   A 1 154 ? 15.700 -2.990  8.346   0.42 13.70 ?  154 ALA   A HB3  1 
ATOM   3827 H HB3  B ALA   A 1 154 ? 15.558 -2.966  8.119   0.58 13.85 ?  154 ALA   A HB3  1 
ATOM   3828 N N    A VAL   A 1 155 ? 12.356 -3.851  6.646   0.42 11.38 ?  155 VAL   A N    1 
ATOM   3829 N N    B VAL   A 1 155 ? 12.301 -4.037  6.332   0.58 11.52 ?  155 VAL   A N    1 
ATOM   3830 C CA   A VAL   A 1 155 ? 11.688 -3.389  5.435   0.42 11.85 ?  155 VAL   A CA   1 
ATOM   3831 C CA   B VAL   A 1 155 ? 11.654 -3.652  5.081   0.58 11.76 ?  155 VAL   A CA   1 
ATOM   3832 C C    A VAL   A 1 155 ? 10.988 -2.087  5.782   0.42 12.08 ?  155 VAL   A C    1 
ATOM   3833 C C    B VAL   A 1 155 ? 10.927 -2.332  5.319   0.58 11.41 ?  155 VAL   A C    1 
ATOM   3834 O O    A VAL   A 1 155 ? 10.091 -2.065  6.633   0.42 12.22 ?  155 VAL   A O    1 
ATOM   3835 O O    B VAL   A 1 155 ? 9.960  -2.280  6.089   0.58 11.64 ?  155 VAL   A O    1 
ATOM   3836 C CB   A VAL   A 1 155 ? 10.698 -4.438  4.902   0.42 12.81 ?  155 VAL   A CB   1 
ATOM   3837 C CB   B VAL   A 1 155 ? 10.683 -4.744  4.597   0.58 12.36 ?  155 VAL   A CB   1 
ATOM   3838 C CG1  A VAL   A 1 155 ? 9.886  -3.883  3.740   0.42 13.18 ?  155 VAL   A CG1  1 
ATOM   3839 C CG1  B VAL   A 1 155 ? 9.901  -4.276  3.383   0.58 12.26 ?  155 VAL   A CG1  1 
ATOM   3840 C CG2  A VAL   A 1 155 ? 11.449 -5.686  4.467   0.42 13.49 ?  155 VAL   A CG2  1 
ATOM   3841 C CG2  B VAL   A 1 155 ? 11.440 -6.032  4.274   0.58 13.50 ?  155 VAL   A CG2  1 
ATOM   3842 H H    A VAL   A 1 155 ? 11.804 -4.137  7.239   0.42 13.68 ?  155 VAL   A H    1 
ATOM   3843 H H    B VAL   A 1 155 ? 11.742 -4.351  6.911   0.58 13.85 ?  155 VAL   A H    1 
ATOM   3844 H HA   A VAL   A 1 155 ? 12.343 -3.205  4.746   0.42 14.24 ?  155 VAL   A HA   1 
ATOM   3845 H HA   B VAL   A 1 155 ? 12.325 -3.526  4.391   0.58 14.15 ?  155 VAL   A HA   1 
ATOM   3846 H HB   A VAL   A 1 155 ? 10.081 -4.684  5.609   0.42 15.40 ?  155 VAL   A HB   1 
ATOM   3847 H HB   B VAL   A 1 155 ? 10.050 -4.948  5.302   0.58 14.86 ?  155 VAL   A HB   1 
ATOM   3848 H HG11 A VAL   A 1 155 ? 9.433  -4.616  3.292   0.42 15.85 ?  155 VAL   A HG11 1 
ATOM   3849 H HG11 B VAL   A 1 155 ? 9.482  -5.043  2.958   0.58 14.74 ?  155 VAL   A HG11 1 
ATOM   3850 H HG12 A VAL   A 1 155 ? 9.230  -3.251  4.078   0.42 15.85 ?  155 VAL   A HG12 1 
ATOM   3851 H HG12 B VAL   A 1 155 ? 9.219  -3.650  3.671   0.58 14.74 ?  155 VAL   A HG12 1 
ATOM   3852 H HG13 A VAL   A 1 155 ? 10.484 -3.438  3.118   0.42 15.85 ?  155 VAL   A HG13 1 
ATOM   3853 H HG13 B VAL   A 1 155 ? 10.508 -3.848  2.762   0.58 14.74 ?  155 VAL   A HG13 1 
ATOM   3854 H HG21 A VAL   A 1 155 ? 10.816 -6.335  4.123   0.42 16.22 ?  155 VAL   A HG21 1 
ATOM   3855 H HG21 B VAL   A 1 155 ? 10.842 -6.654  3.826   0.58 16.23 ?  155 VAL   A HG21 1 
ATOM   3856 H HG22 A VAL   A 1 155 ? 12.086 -5.446  3.773   0.42 16.22 ?  155 VAL   A HG22 1 
ATOM   3857 H HG22 B VAL   A 1 155 ? 12.190 -5.824  3.693   0.58 16.23 ?  155 VAL   A HG22 1 
ATOM   3858 H HG23 A VAL   A 1 155 ? 11.920 -6.054  5.231   0.42 16.22 ?  155 VAL   A HG23 1 
ATOM   3859 H HG23 B VAL   A 1 155 ? 11.766 -6.427  5.100   0.58 16.23 ?  155 VAL   A HG23 1 
ATOM   3860 N N    A PHE   A 1 156 ? 11.406 -0.998  5.133   0.42 12.08 ?  156 PHE   A N    1 
ATOM   3861 N N    B PHE   A 1 156 ? 11.372 -1.271  4.635   0.58 11.66 ?  156 PHE   A N    1 
ATOM   3862 C CA   A PHE   A 1 156 ? 10.898 0.324   5.493   0.42 13.64 ?  156 PHE   A CA   1 
ATOM   3863 C CA   B PHE   A 1 156 ? 10.861 0.078   4.897   0.58 12.19 ?  156 PHE   A CA   1 
ATOM   3864 C C    A PHE   A 1 156 ? 9.431  0.497   5.113   0.42 13.27 ?  156 PHE   A C    1 
ATOM   3865 C C    B PHE   A 1 156 ? 9.394  0.230   4.497   0.58 13.30 ?  156 PHE   A C    1 
ATOM   3866 O O    A PHE   A 1 156 ? 8.658  1.086   5.878   0.42 13.75 ?  156 PHE   A O    1 
ATOM   3867 O O    B PHE   A 1 156 ? 8.603  0.822   5.242   0.58 15.11 ?  156 PHE   A O    1 
ATOM   3868 C CB   A PHE   A 1 156 ? 11.756 1.410   4.838   0.42 15.70 ?  156 PHE   A CB   1 
ATOM   3869 C CB   B PHE   A 1 156 ? 11.746 1.096   4.163   0.58 11.62 ?  156 PHE   A CB   1 
ATOM   3870 C CG   A PHE   A 1 156 ? 11.294 2.816   5.130   0.42 18.11 ?  156 PHE   A CG   1 
ATOM   3871 C CG   B PHE   A 1 156 ? 11.391 2.561   4.420   0.58 12.85 ?  156 PHE   A CG   1 
ATOM   3872 C CD1  A PHE   A 1 156 ? 11.272 3.298   6.428   0.42 19.65 ?  156 PHE   A CD1  1 
ATOM   3873 C CD1  B PHE   A 1 156 ? 11.960 3.264   5.480   0.58 13.17 ?  156 PHE   A CD1  1 
ATOM   3874 C CD2  A PHE   A 1 156 ? 10.899 3.657   4.103   0.42 19.09 ?  156 PHE   A CD2  1 
ATOM   3875 C CD2  B PHE   A 1 156 ? 10.527 3.240   3.577   0.58 15.04 ?  156 PHE   A CD2  1 
ATOM   3876 C CE1  A PHE   A 1 156 ? 10.852 4.588   6.699   0.42 20.66 ?  156 PHE   A CE1  1 
ATOM   3877 C CE1  B PHE   A 1 156 ? 11.652 4.602   5.703   0.58 14.66 ?  156 PHE   A CE1  1 
ATOM   3878 C CE2  A PHE   A 1 156 ? 10.481 4.950   4.366   0.42 20.10 ?  156 PHE   A CE2  1 
ATOM   3879 C CE2  B PHE   A 1 156 ? 10.218 4.574   3.796   0.58 16.25 ?  156 PHE   A CE2  1 
ATOM   3880 C CZ   A PHE   A 1 156 ? 10.458 5.416   5.667   0.42 20.68 ?  156 PHE   A CZ   1 
ATOM   3881 C CZ   B PHE   A 1 156 ? 10.784 5.254   4.860   0.58 16.19 ?  156 PHE   A CZ   1 
ATOM   3882 H H    A PHE   A 1 156 ? 11.985 -0.991  4.495   0.42 14.52 ?  156 PHE   A H    1 
ATOM   3883 H H    B PHE   A 1 156 ? 11.969 -1.315  4.017   0.58 14.02 ?  156 PHE   A H    1 
ATOM   3884 H HA   A PHE   A 1 156 ? 10.965 0.439   6.451   0.42 16.40 ?  156 PHE   A HA   1 
ATOM   3885 H HA   B PHE   A 1 156 ? 10.927 0.247   5.844   0.58 14.65 ?  156 PHE   A HA   1 
ATOM   3886 H HB2  A PHE   A 1 156 ? 12.666 1.329   5.162   0.42 18.87 ?  156 PHE   A HB2  1 
ATOM   3887 H HB2  B PHE   A 1 156 ? 12.663 0.955   4.448   0.58 13.97 ?  156 PHE   A HB2  1 
ATOM   3888 H HB3  A PHE   A 1 156 ? 11.737 1.292   3.876   0.42 18.87 ?  156 PHE   A HB3  1 
ATOM   3889 H HB3  B PHE   A 1 156 ? 11.677 0.934   3.207   0.58 13.97 ?  156 PHE   A HB3  1 
ATOM   3890 H HD1  A PHE   A 1 156 ? 11.537 2.744   7.128   0.42 23.60 ?  156 PHE   A HD1  1 
ATOM   3891 H HD1  B PHE   A 1 156 ? 12.554 2.817   6.054   0.58 15.83 ?  156 PHE   A HD1  1 
ATOM   3892 H HD2  A PHE   A 1 156 ? 10.914 3.348   3.227   0.42 22.93 ?  156 PHE   A HD2  1 
ATOM   3893 H HD2  B PHE   A 1 156 ? 10.142 2.785   2.864   0.58 18.08 ?  156 PHE   A HD2  1 
ATOM   3894 H HE1  A PHE   A 1 156 ? 10.840 4.897   7.578   0.42 24.81 ?  156 PHE   A HE1  1 
ATOM   3895 H HE1  B PHE   A 1 156 ? 12.038 5.041   6.424   0.58 17.62 ?  156 PHE   A HE1  1 
ATOM   3896 H HE2  A PHE   A 1 156 ? 10.215 5.504   3.668   0.42 24.15 ?  156 PHE   A HE2  1 
ATOM   3897 H HE2  B PHE   A 1 156 ? 9.625  5.006   3.231   0.58 19.52 ?  156 PHE   A HE2  1 
ATOM   3898 H HZ   A PHE   A 1 156 ? 10.177 6.283   5.848   0.42 24.84 ?  156 PHE   A HZ   1 
ATOM   3899 H HZ   B PHE   A 1 156 ? 10.572 6.141   5.014   0.58 19.45 ?  156 PHE   A HZ   1 
ATOM   3900 N N    A ASP   A 1 157 ? 9.031  0.009   3.942   0.42 13.28 ?  157 ASP   A N    1 
ATOM   3901 N N    B ASP   A 1 157 ? 9.010  -0.290  3.332   0.58 13.73 ?  157 ASP   A N    1 
ATOM   3902 C CA   A ASP   A 1 157 ? 7.702  0.268   3.398   0.42 14.30 ?  157 ASP   A CA   1 
ATOM   3903 C CA   B ASP   A 1 157 ? 7.684  -0.046  2.768   0.58 14.60 ?  157 ASP   A CA   1 
ATOM   3904 C C    A ASP   A 1 157 ? 6.708  -0.766  3.923   0.42 14.46 ?  157 ASP   A C    1 
ATOM   3905 C C    B ASP   A 1 157 ? 6.689  -1.099  3.254   0.58 14.09 ?  157 ASP   A C    1 
ATOM   3906 O O    A ASP   A 1 157 ? 6.894  -1.970  3.715   0.42 14.40 ?  157 ASP   A O    1 
ATOM   3907 O O    B ASP   A 1 157 ? 6.892  -2.295  3.034   0.58 13.39 ?  157 ASP   A O    1 
ATOM   3908 C CB   A ASP   A 1 157 ? 7.761  0.215   1.873   0.42 15.15 ?  157 ASP   A CB   1 
ATOM   3909 C CB   B ASP   A 1 157 ? 7.767  -0.063  1.243   0.58 15.85 ?  157 ASP   A CB   1 
ATOM   3910 C CG   A ASP   A 1 157 ? 6.495  0.734   1.230   0.42 16.69 ?  157 ASP   A CG   1 
ATOM   3911 C CG   B ASP   A 1 157 ? 6.468  0.366   0.582   0.58 17.60 ?  157 ASP   A CG   1 
ATOM   3912 O OD1  A ASP   A 1 157 ? 6.371  1.970   1.094   0.42 18.72 ?  157 ASP   A OD1  1 
ATOM   3913 O OD1  B ASP   A 1 157 ? 6.141  1.570   0.626   0.58 19.06 ?  157 ASP   A OD1  1 
ATOM   3914 O OD2  A ASP   A 1 157 ? 5.616  -0.085  0.882   0.42 16.69 -1 157 ASP   A OD2  1 
ATOM   3915 O OD2  B ASP   A 1 157 ? 5.765  -0.496  0.017   0.58 18.50 -1 157 ASP   A OD2  1 
ATOM   3916 H H    A ASP   A 1 157 ? 9.518  -0.480  3.431   0.42 15.96 ?  157 ASP   A H    1 
ATOM   3917 H H    B ASP   A 1 157 ? 9.506  -0.796  2.839   0.58 16.50 ?  157 ASP   A H    1 
ATOM   3918 H HA   A ASP   A 1 157 ? 7.400  1.154   3.661   0.42 17.19 ?  157 ASP   A HA   1 
ATOM   3919 H HA   B ASP   A 1 157 ? 7.368  0.823   3.051   0.58 17.55 ?  157 ASP   A HA   1 
ATOM   3920 H HB2  A ASP   A 1 157 ? 8.513  0.752   1.567   0.42 18.20 ?  157 ASP   A HB2  1 
ATOM   3921 H HB2  B ASP   A 1 157 ? 8.476  0.534   0.959   0.58 19.05 ?  157 ASP   A HB2  1 
ATOM   3922 H HB3  A ASP   A 1 157 ? 7.885  -0.706  1.593   0.42 18.20 ?  157 ASP   A HB3  1 
ATOM   3923 H HB3  B ASP   A 1 157 ? 7.957  -0.968  0.944   0.58 19.05 ?  157 ASP   A HB3  1 
ATOM   3924 N N    A LYS   A 1 158 ? 5.641  -0.296  4.581   0.42 15.17 ?  158 LYS   A N    1 
ATOM   3925 N N    B LYS   A 1 158 ? 5.595  -0.649  3.879   0.58 14.63 ?  158 LYS   A N    1 
ATOM   3926 C CA   A LYS   A 1 158 ? 4.664  -1.218  5.159   0.42 16.40 ?  158 LYS   A CA   1 
ATOM   3927 C CA   B LYS   A 1 158 ? 4.609  -1.574  4.442   0.58 15.68 ?  158 LYS   A CA   1 
ATOM   3928 C C    A LYS   A 1 158 ? 3.953  -2.026  4.078   0.42 16.63 ?  158 LYS   A C    1 
ATOM   3929 C C    B LYS   A 1 158 ? 3.943  -2.414  3.356   0.58 15.20 ?  158 LYS   A C    1 
ATOM   3930 O O    A LYS   A 1 158 ? 3.778  -3.243  4.220   0.42 16.74 ?  158 LYS   A O    1 
ATOM   3931 O O    B LYS   A 1 158 ? 3.769  -3.627  3.520   0.58 15.19 ?  158 LYS   A O    1 
ATOM   3932 C CB   A LYS   A 1 158 ? 3.661  -0.455  6.030   0.42 17.66 ?  158 LYS   A CB   1 
ATOM   3933 C CB   B LYS   A 1 158 ? 3.560  -0.788  5.235   0.58 17.93 ?  158 LYS   A CB   1 
ATOM   3934 C CG   A LYS   A 1 158 ? 2.466  -1.282  6.503   0.42 19.27 ?  158 LYS   A CG   1 
ATOM   3935 C CG   B LYS   A 1 158 ? 2.331  -1.591  5.669   0.58 20.42 ?  158 LYS   A CG   1 
ATOM   3936 C CD   A LYS   A 1 158 ? 2.878  -2.518  7.295   0.42 21.01 ?  158 LYS   A CD   1 
ATOM   3937 C CD   B LYS   A 1 158 ? 2.642  -2.608  6.760   0.58 22.97 ?  158 LYS   A CD   1 
ATOM   3938 C CE   A LYS   A 1 158 ? 1.655  -3.237  7.846   0.42 22.02 ?  158 LYS   A CE   1 
ATOM   3939 C CE   B LYS   A 1 158 ? 1.367  -3.266  7.280   0.58 24.30 ?  158 LYS   A CE   1 
ATOM   3940 N NZ   A LYS   A 1 158 ? 1.977  -4.585  8.392   0.42 22.52 ?  158 LYS   A NZ   1 
ATOM   3941 N NZ   B LYS   A 1 158 ? 1.634  -4.409  8.196   0.58 24.75 ?  158 LYS   A NZ   1 
ATOM   3942 H H    A LYS   A 1 158 ? 5.464  0.539   4.702   0.42 18.24 ?  158 LYS   A H    1 
ATOM   3943 H H    B LYS   A 1 158 ? 5.400  0.175   3.982   0.58 17.58 ?  158 LYS   A H    1 
ATOM   3944 H HA   A LYS   A 1 158 ? 5.128  -1.841  5.730   0.42 19.71 ?  158 LYS   A HA   1 
ATOM   3945 H HA   B LYS   A 1 158 ? 5.052  -2.179  5.059   0.58 18.84 ?  158 LYS   A HA   1 
ATOM   3946 H HB2  A LYS   A 1 158 ? 4.121  -0.132  6.823   0.42 21.22 ?  158 LYS   A HB2  1 
ATOM   3947 H HB2  B LYS   A 1 158 ? 3.978  -0.442  6.041   0.58 21.55 ?  158 LYS   A HB2  1 
ATOM   3948 H HB3  A LYS   A 1 158 ? 3.315  0.299   5.527   0.42 21.22 ?  158 LYS   A HB3  1 
ATOM   3949 H HB3  B LYS   A 1 158 ? 3.250  -0.049  4.689   0.58 21.55 ?  158 LYS   A HB3  1 
ATOM   3950 H HG2  A LYS   A 1 158 ? 1.912  -0.730  7.079   0.42 23.15 ?  158 LYS   A HG2  1 
ATOM   3951 H HG2  B LYS   A 1 158 ? 1.671  -0.973  6.019   0.58 24.53 ?  158 LYS   A HG2  1 
ATOM   3952 H HG3  A LYS   A 1 158 ? 1.947  -1.570  5.734   0.42 23.15 ?  158 LYS   A HG3  1 
ATOM   3953 H HG3  B LYS   A 1 158 ? 1.956  -2.063  4.908   0.58 24.53 ?  158 LYS   A HG3  1 
ATOM   3954 H HD2  A LYS   A 1 158 ? 3.352  -3.128  6.712   0.42 25.23 ?  158 LYS   A HD2  1 
ATOM   3955 H HD2  B LYS   A 1 158 ? 3.221  -3.295  6.403   0.58 27.59 ?  158 LYS   A HD2  1 
ATOM   3956 H HD3  A LYS   A 1 158 ? 3.441  -2.248  8.037   0.42 25.23 ?  158 LYS   A HD3  1 
ATOM   3957 H HD3  B LYS   A 1 158 ? 3.073  -2.152  7.503   0.58 27.59 ?  158 LYS   A HD3  1 
ATOM   3958 H HE2  A LYS   A 1 158 ? 1.257  -2.704  8.552   0.42 26.45 ?  158 LYS   A HE2  1 
ATOM   3959 H HE2  B LYS   A 1 158 ? 0.878  -2.605  7.788   0.58 29.18 ?  158 LYS   A HE2  1 
ATOM   3960 H HE3  A LYS   A 1 158 ? 1.013  -3.350  7.132   0.42 26.45 ?  158 LYS   A HE3  1 
ATOM   3961 H HE3  B LYS   A 1 158 ? 0.831  -3.580  6.530   0.58 29.18 ?  158 LYS   A HE3  1 
ATOM   3962 H HZ1  A LYS   A 1 158 ? 1.239  -4.970  8.706   0.42 27.05 ?  158 LYS   A HZ1  1 
ATOM   3963 H HZ1  B LYS   A 1 158 ? 0.865  -4.764  8.471   0.58 29.72 ?  158 LYS   A HZ1  1 
ATOM   3964 H HZ2  A LYS   A 1 158 ? 2.318  -5.095  7.747   0.42 27.05 ?  158 LYS   A HZ2  1 
ATOM   3965 H HZ2  B LYS   A 1 158 ? 2.108  -5.031  7.776   0.58 29.72 ?  158 LYS   A HZ2  1 
ATOM   3966 H HZ3  A LYS   A 1 158 ? 2.571  -4.514  9.050   0.42 27.05 ?  158 LYS   A HZ3  1 
ATOM   3967 H HZ3  B LYS   A 1 158 ? 2.090  -4.125  8.906   0.58 29.72 ?  158 LYS   A HZ3  1 
ATOM   3968 N N    A ASN   A 1 159 ? 3.533  -1.370  2.993   0.42 17.48 ?  159 ASN   A N    1 
ATOM   3969 N N    B ASN   A 1 159 ? 3.543  -1.788  2.251   0.58 15.88 ?  159 ASN   A N    1 
ATOM   3970 C CA   A ASN   A 1 159 ? 2.868  -2.090  1.910   0.42 18.24 ?  159 ASN   A CA   1 
ATOM   3971 C CA   B ASN   A 1 159 ? 2.918  -2.536  1.165   0.58 16.95 ?  159 ASN   A CA   1 
ATOM   3972 C C    A ASN   A 1 159 ? 3.767  -3.183  1.346   0.42 17.39 ?  159 ASN   A C    1 
ATOM   3973 C C    B ASN   A 1 159 ? 3.842  -3.645  0.671   0.58 15.78 ?  159 ASN   A C    1 
ATOM   3974 O O    A ASN   A 1 159 ? 3.320  -4.314  1.124   0.42 17.67 ?  159 ASN   A O    1 
ATOM   3975 O O    B ASN   A 1 159 ? 3.412  -4.786  0.458   0.58 16.21 ?  159 ASN   A O    1 
ATOM   3976 C CB   A ASN   A 1 159 ? 2.435  -1.108  0.816   0.42 20.08 ?  159 ASN   A CB   1 
ATOM   3977 C CB   B ASN   A 1 159 ? 2.574  -1.562  0.034   0.58 19.73 ?  159 ASN   A CB   1 
ATOM   3978 C CG   A ASN   A 1 159 ? 1.248  -0.260  1.234   0.42 21.80 ?  159 ASN   A CG   1 
ATOM   3979 C CG   B ASN   A 1 159 ? 1.430  -2.038  -0.835  0.58 22.96 ?  159 ASN   A CG   1 
ATOM   3980 O OD1  A ASN   A 1 159 ? 0.367  -0.735  1.944   0.42 22.42 ?  159 ASN   A OD1  1 
ATOM   3981 O OD1  B ASN   A 1 159 ? 0.709  -2.976  -0.489  0.58 24.28 ?  159 ASN   A OD1  1 
ATOM   3982 N ND2  A ASN   A 1 159 ? 1.220  1.001   0.797   0.42 22.77 ?  159 ASN   A ND2  1 
ATOM   3983 N ND2  B ASN   A 1 159 ? 1.234  -1.363  -1.963  0.58 23.87 ?  159 ASN   A ND2  1 
ATOM   3984 H H    A ASN   A 1 159 ? 3.620  -0.526  2.858   0.42 21.00 ?  159 ASN   A H    1 
ATOM   3985 H H    B ASN   A 1 159 ? 3.619  -0.948  2.116   0.58 19.08 ?  159 ASN   A H    1 
ATOM   3986 H HA   A ASN   A 1 159 ? 2.065  -2.514  2.251   0.42 21.92 ?  159 ASN   A HA   1 
ATOM   3987 H HA   B ASN   A 1 159 ? 2.090  -2.936  1.480   0.58 20.37 ?  159 ASN   A HA   1 
ATOM   3988 H HB2  A ASN   A 1 159 ? 3.166  -0.508  0.610   0.42 24.12 ?  159 ASN   A HB2  1 
ATOM   3989 H HB2  B ASN   A 1 159 ? 2.325  -0.701  0.422   0.58 23.71 ?  159 ASN   A HB2  1 
ATOM   3990 H HB3  A ASN   A 1 159 ? 2.176  -1.601  0.019   0.42 24.12 ?  159 ASN   A HB3  1 
ATOM   3991 H HB3  B ASN   A 1 159 ? 3.353  -1.447  -0.533  0.58 23.71 ?  159 ASN   A HB3  1 
ATOM   3992 H HD21 A ASN   A 1 159 ? 0.568  1.522   1.005   0.42 27.35 ?  159 ASN   A HD21 1 
ATOM   3993 H HD21 B ASN   A 1 159 ? 0.598  -1.583  -2.492  0.58 28.67 ?  159 ASN   A HD21 1 
ATOM   3994 H HD22 A ASN   A 1 159 ? 1.858  1.300   0.309   0.42 27.35 ?  159 ASN   A HD22 1 
ATOM   3995 H HD22 B ASN   A 1 159 ? 1.752  -0.710  -2.172  0.58 28.67 ?  159 ASN   A HD22 1 
ATOM   3996 N N    A LEU   A 1 160 ? 5.044  -2.870  1.125   0.42 16.38 ?  160 LEU   A N    1 
ATOM   3997 N N    B LEU   A 1 160 ? 5.128  -3.334  0.511   0.58 14.78 ?  160 LEU   A N    1 
ATOM   3998 C CA   A LEU   A 1 160 ? 5.964  -3.870  0.593   0.42 15.82 ?  160 LEU   A CA   1 
ATOM   3999 C CA   B LEU   A 1 160 ? 6.085  -4.340  0.062   0.58 14.46 ?  160 LEU   A CA   1 
ATOM   4000 C C    A LEU   A 1 160 ? 6.179  -5.002  1.588   0.42 14.97 ?  160 LEU   A C    1 
ATOM   4001 C C    B LEU   A 1 160 ? 6.229  -5.460  1.088   0.58 14.00 ?  160 LEU   A C    1 
ATOM   4002 O O    A LEU   A 1 160 ? 6.213  -6.178  1.205   0.42 14.97 ?  160 LEU   A O    1 
ATOM   4003 O O    B LEU   A 1 160 ? 6.234  -6.643  0.734   0.58 14.36 ?  160 LEU   A O    1 
ATOM   4004 C CB   A LEU   A 1 160 ? 7.294  -3.212  0.239   0.42 16.02 ?  160 LEU   A CB   1 
ATOM   4005 C CB   B LEU   A 1 160 ? 7.438  -3.688  -0.210  0.58 14.73 ?  160 LEU   A CB   1 
ATOM   4006 C CG   A LEU   A 1 160 ? 8.385  -4.166  -0.238  0.42 16.43 ?  160 LEU   A CG   1 
ATOM   4007 C CG   B LEU   A 1 160 ? 8.548  -4.700  -0.502  0.58 14.88 ?  160 LEU   A CG   1 
ATOM   4008 C CD1  A LEU   A 1 160 ? 7.930  -4.868  -1.501  0.42 16.66 ?  160 LEU   A CD1  1 
ATOM   4009 C CD1  B LEU   A 1 160 ? 8.236  -5.503  -1.759  0.58 15.62 ?  160 LEU   A CD1  1 
ATOM   4010 C CD2  A LEU   A 1 160 ? 9.683  -3.414  -0.466  0.42 16.65 ?  160 LEU   A CD2  1 
ATOM   4011 C CD2  B LEU   A 1 160 ? 9.874  -3.985  -0.612  0.58 15.07 ?  160 LEU   A CD2  1 
ATOM   4012 H H    A LEU   A 1 160 ? 5.399  -2.105  1.287   0.42 19.68 ?  160 LEU   A H    1 
ATOM   4013 H H    B LEU   A 1 160 ? 5.466  -2.563  0.667   0.58 17.77 ?  160 LEU   A H    1 
ATOM   4014 H HA   A LEU   A 1 160 ? 5.588  -4.248  -0.217  0.42 19.01 ?  160 LEU   A HA   1 
ATOM   4015 H HA   B LEU   A 1 160 ? 5.763  -4.729  -0.766  0.58 17.37 ?  160 LEU   A HA   1 
ATOM   4016 H HB2  A LEU   A 1 160 ? 7.140  -2.564  -0.469  0.42 19.25 ?  160 LEU   A HB2  1 
ATOM   4017 H HB2  B LEU   A 1 160 ? 7.353  -3.104  -0.980  0.58 17.70 ?  160 LEU   A HB2  1 
ATOM   4018 H HB3  A LEU   A 1 160 ? 7.629  -2.761  1.026   0.42 19.25 ?  160 LEU   A HB3  1 
ATOM   4019 H HB3  B LEU   A 1 160 ? 7.697  -3.172  0.569   0.58 17.70 ?  160 LEU   A HB3  1 
ATOM   4020 H HG   A LEU   A 1 160 ? 8.546  -4.839  0.444   0.42 19.74 ?  160 LEU   A HG   1 
ATOM   4021 H HG   B LEU   A 1 160 ? 8.619  -5.323  0.237   0.58 17.88 ?  160 LEU   A HG   1 
ATOM   4022 H HD11 A LEU   A 1 160 ? 8.677  -5.359  -1.872  0.42 20.02 ?  160 LEU   A HD11 1 
ATOM   4023 H HD11 B LEU   A 1 160 ? 8.951  -6.136  -1.910  0.58 18.78 ?  160 LEU   A HD11 1 
ATOM   4024 H HD12 A LEU   A 1 160 ? 7.207  -5.476  -1.282  0.42 20.02 ?  160 LEU   A HD12 1 
ATOM   4025 H HD12 B LEU   A 1 160 ? 7.399  -5.978  -1.638  0.58 18.78 ?  160 LEU   A HD12 1 
ATOM   4026 H HD13 A LEU   A 1 160 ? 7.622  -4.201  -2.135  0.42 20.02 ?  160 LEU   A HD13 1 
ATOM   4027 H HD13 B LEU   A 1 160 ? 8.165  -4.894  -2.512  0.58 18.78 ?  160 LEU   A HD13 1 
ATOM   4028 H HD21 A LEU   A 1 160 ? 10.361 -4.040  -0.764  0.42 20.00 ?  160 LEU   A HD21 1 
ATOM   4029 H HD21 B LEU   A 1 160 ? 10.568 -4.639  -0.775  0.58 18.11 ?  160 LEU   A HD21 1 
ATOM   4030 H HD22 A LEU   A 1 160 ? 9.538  -2.735  -1.142  0.42 20.00 ?  160 LEU   A HD22 1 
ATOM   4031 H HD22 B LEU   A 1 160 ? 9.829  -3.352  -1.344  0.58 18.11 ?  160 LEU   A HD22 1 
ATOM   4032 H HD23 A LEU   A 1 160 ? 9.959  -2.999  0.367   0.42 20.00 ?  160 LEU   A HD23 1 
ATOM   4033 H HD23 B LEU   A 1 160 ? 10.046 -3.517  0.221   0.58 18.11 ?  160 LEU   A HD23 1 
ATOM   4034 N N    A TYR   A 1 161 ? 6.325  -4.667  2.869   0.42 15.19 ?  161 TYR   A N    1 
ATOM   4035 N N    B TYR   A 1 161 ? 6.385  -5.104  2.364   0.58 13.45 ?  161 TYR   A N    1 
ATOM   4036 C CA   A TYR   A 1 161 ? 6.450  -5.699  3.889   0.42 15.20 ?  161 TYR   A CA   1 
ATOM   4037 C CA   B TYR   A 1 161 ? 6.477  -6.104  3.428   0.58 13.29 ?  161 TYR   A CA   1 
ATOM   4038 C C    A TYR   A 1 161 ? 5.292  -6.685  3.813   0.42 15.71 ?  161 TYR   A C    1 
ATOM   4039 C C    B TYR   A 1 161 ? 5.308  -7.076  3.374   0.58 14.23 ?  161 TYR   A C    1 
ATOM   4040 O O    A TYR   A 1 161 ? 5.491  -7.903  3.867   0.42 15.57 ?  161 TYR   A O    1 
ATOM   4041 O O    B TYR   A 1 161 ? 5.500  -8.295  3.393   0.58 13.81 ?  161 TYR   A O    1 
ATOM   4042 C CB   A TYR   A 1 161 ? 6.516  -5.069  5.278   0.42 15.60 ?  161 TYR   A CB   1 
ATOM   4043 C CB   B TYR   A 1 161 ? 6.532  -5.389  4.781   0.58 13.73 ?  161 TYR   A CB   1 
ATOM   4044 C CG   A TYR   A 1 161 ? 6.450  -6.124  6.347   0.42 15.56 ?  161 TYR   A CG   1 
ATOM   4045 C CG   B TYR   A 1 161 ? 6.364  -6.246  6.031   0.58 15.08 ?  161 TYR   A CG   1 
ATOM   4046 C CD1  A TYR   A 1 161 ? 7.588  -6.812  6.730   0.42 15.94 ?  161 TYR   A CD1  1 
ATOM   4047 C CD1  B TYR   A 1 161 ? 7.438  -6.931  6.594   0.58 16.02 ?  161 TYR   A CD1  1 
ATOM   4048 C CD2  A TYR   A 1 161 ? 5.241  -6.470  6.938   0.42 15.68 ?  161 TYR   A CD2  1 
ATOM   4049 C CD2  B TYR   A 1 161 ? 5.133  -6.323  6.683   0.58 16.29 ?  161 TYR   A CD2  1 
ATOM   4050 C CE1  A TYR   A 1 161 ? 7.534  -7.795  7.685   0.42 16.25 ?  161 TYR   A CE1  1 
ATOM   4051 C CE1  B TYR   A 1 161 ? 7.278  -7.697  7.752   0.58 16.79 ?  161 TYR   A CE1  1 
ATOM   4052 C CE2  A TYR   A 1 161 ? 5.178  -7.452  7.897   0.42 16.02 ?  161 TYR   A CE2  1 
ATOM   4053 C CE2  B TYR   A 1 161 ? 4.968  -7.076  7.841   0.58 17.00 ?  161 TYR   A CE2  1 
ATOM   4054 C CZ   A TYR   A 1 161 ? 6.330  -8.111  8.267   0.42 16.49 ?  161 TYR   A CZ   1 
ATOM   4055 C CZ   B TYR   A 1 161 ? 6.040  -7.760  8.371   0.58 17.65 ?  161 TYR   A CZ   1 
ATOM   4056 O OH   A TYR   A 1 161 ? 6.273  -9.088  9.225   0.42 16.95 ?  161 TYR   A OH   1 
ATOM   4057 O OH   B TYR   A 1 161 ? 5.880  -8.518  9.518   0.58 18.94 ?  161 TYR   A OH   1 
ATOM   4058 H H    A TYR   A 1 161 ? 6.351  -3.864  3.168   0.42 18.25 ?  161 TYR   A H    1 
ATOM   4059 H H    B TYR   A 1 161 ? 6.439  -4.303  2.639   0.58 16.16 ?  161 TYR   A H    1 
ATOM   4060 H HA   A TYR   A 1 161 ? 7.268  -6.195  3.745   0.42 18.27 ?  161 TYR   A HA   1 
ATOM   4061 H HA   B TYR   A 1 161 ? 7.291  -6.622  3.321   0.58 15.97 ?  161 TYR   A HA   1 
ATOM   4062 H HB2  A TYR   A 1 161 ? 7.353  -4.587  5.375   0.42 18.75 ?  161 TYR   A HB2  1 
ATOM   4063 H HB2  B TYR   A 1 161 ? 7.393  -4.956  4.849   0.58 16.50 ?  161 TYR   A HB2  1 
ATOM   4064 H HB3  A TYR   A 1 161 ? 5.765  -4.464  5.397   0.42 18.75 ?  161 TYR   A HB3  1 
ATOM   4065 H HB3  B TYR   A 1 161 ? 5.829  -4.727  4.796   0.58 16.50 ?  161 TYR   A HB3  1 
ATOM   4066 H HD1  A TYR   A 1 161 ? 8.402  -6.598  6.338   0.42 19.15 ?  161 TYR   A HD1  1 
ATOM   4067 H HD1  B TYR   A 1 161 ? 8.270  -6.896  6.184   0.58 19.25 ?  161 TYR   A HD1  1 
ATOM   4068 H HD2  A TYR   A 1 161 ? 4.461  -6.022  6.687   0.42 18.84 ?  161 TYR   A HD2  1 
ATOM   4069 H HD2  B TYR   A 1 161 ? 4.403  -5.868  6.335   0.58 19.57 ?  161 TYR   A HD2  1 
ATOM   4070 H HE1  A TYR   A 1 161 ? 8.307  -8.244  7.936   0.42 19.53 ?  161 TYR   A HE1  1 
ATOM   4071 H HE1  B TYR   A 1 161 ? 8.004  -8.155  8.117   0.58 20.18 ?  161 TYR   A HE1  1 
ATOM   4072 H HE2  A TYR   A 1 161 ? 4.361  -7.669  8.287   0.42 19.25 ?  161 TYR   A HE2  1 
ATOM   4073 H HE2  B TYR   A 1 161 ? 4.134  -7.122  8.261   0.58 20.43 ?  161 TYR   A HE2  1 
ATOM   4074 H HH   A TYR   A 1 161 ? 7.034  -9.409  9.348   0.42 20.36 ?  161 TYR   A HH   1 
ATOM   4075 H HH   B TYR   A 1 161 ? 5.089  -8.466  9.800   0.58 22.76 ?  161 TYR   A HH   1 
ATOM   4076 N N    A ASP   A 1 162 ? 4.066  -6.170  3.693   0.42 16.91 ?  162 ASP   A N    1 
ATOM   4077 N N    B ASP   A 1 162 ? 4.082  -6.552  3.300   0.58 15.50 ?  162 ASP   A N    1 
ATOM   4078 C CA   A ASP   A 1 162 ? 2.904  -7.050  3.615   0.42 18.09 ?  162 ASP   A CA   1 
ATOM   4079 C CA   B ASP   A 1 162 ? 2.904  -7.414  3.224   0.58 16.48 ?  162 ASP   A CA   1 
ATOM   4080 C C    A ASP   A 1 162 ? 2.940  -7.906  2.355   0.42 19.26 ?  162 ASP   A C    1 
ATOM   4081 C C    B ASP   A 1 162 ? 2.989  -8.356  2.030   0.58 16.93 ?  162 ASP   A C    1 
ATOM   4082 O O    A ASP   A 1 162 ? 2.571  -9.086  2.388   0.42 19.56 ?  162 ASP   A O    1 
ATOM   4083 O O    B ASP   A 1 162 ? 2.641  -9.536  2.134   0.58 17.63 ?  162 ASP   A O    1 
ATOM   4084 C CB   A ASP   A 1 162 ? 1.614  -6.231  3.678   0.42 18.30 ?  162 ASP   A CB   1 
ATOM   4085 C CB   B ASP   A 1 162 ? 1.640  -6.557  3.114   0.58 18.33 ?  162 ASP   A CB   1 
ATOM   4086 C CG   A ASP   A 1 162 ? 1.286  -5.759  5.081   0.42 18.47 ?  162 ASP   A CG   1 
ATOM   4087 C CG   B ASP   A 1 162 ? 1.372  -5.727  4.353   0.58 19.92 ?  162 ASP   A CG   1 
ATOM   4088 O OD1  A ASP   A 1 162 ? 1.948  -6.205  6.041   0.42 18.83 ?  162 ASP   A OD1  1 
ATOM   4089 O OD1  B ASP   A 1 162 ? 1.982  -5.993  5.404   0.58 20.60 ?  162 ASP   A OD1  1 
ATOM   4090 O OD2  A ASP   A 1 162 ? 0.348  -4.947  5.224   0.42 18.48 -1 162 ASP   A OD2  1 
ATOM   4091 O OD2  B ASP   A 1 162 ? 0.523  -4.811  4.275   0.58 20.90 -1 162 ASP   A OD2  1 
ATOM   4092 H H    A ASP   A 1 162 ? 3.880  -5.329  3.656   0.42 20.32 ?  162 ASP   A H    1 
ATOM   4093 H H    B ASP   A 1 162 ? 3.904  -5.724  3.294   0.58 18.63 ?  162 ASP   A H    1 
ATOM   4094 H HA   A ASP   A 1 162 ? 2.907  -7.647  4.375   0.42 21.73 ?  162 ASP   A HA   1 
ATOM   4095 H HA   B ASP   A 1 162 ? 2.828  -7.958  4.026   0.58 19.81 ?  162 ASP   A HA   1 
ATOM   4096 H HB2  A ASP   A 1 162 ? 1.703  -5.446  3.114   0.42 21.99 ?  162 ASP   A HB2  1 
ATOM   4097 H HB2  B ASP   A 1 162 ? 1.727  -5.960  2.355   0.58 22.02 ?  162 ASP   A HB2  1 
ATOM   4098 H HB3  A ASP   A 1 162 ? 0.871  -6.776  3.370   0.42 21.99 ?  162 ASP   A HB3  1 
ATOM   4099 H HB3  B ASP   A 1 162 ? 0.864  -7.127  3.000   0.58 22.02 ?  162 ASP   A HB3  1 
ATOM   4100 N N    A LYS   A 1 163 ? 3.378  -7.330  1.233   0.42 20.32 ?  163 LYS   A N    1 
ATOM   4101 N N    B LYS   A 1 163 ? 3.439  -7.847  0.886   0.58 17.00 ?  163 LYS   A N    1 
ATOM   4102 C CA   A LYS   A 1 163 ? 3.473  -8.105  -0.001  0.42 21.48 ?  163 LYS   A CA   1 
ATOM   4103 C CA   B LYS   A 1 163 ? 3.544  -8.657  -0.321  0.58 18.50 ?  163 LYS   A CA   1 
ATOM   4104 C C    A LYS   A 1 163 ? 4.551  -9.181  0.104   0.42 19.82 ?  163 LYS   A C    1 
ATOM   4105 C C    B LYS   A 1 163 ? 4.618  -9.730  -0.179  0.58 16.69 ?  163 LYS   A C    1 
ATOM   4106 O O    A LYS   A 1 163 ? 4.379  -10.292 -0.411  0.42 20.46 ?  163 LYS   A O    1 
ATOM   4107 O O    B LYS   A 1 163 ? 4.415  -10.880 -0.585  0.58 17.14 ?  163 LYS   A O    1 
ATOM   4108 C CB   A LYS   A 1 163 ? 3.733  -7.173  -1.189  0.42 25.03 ?  163 LYS   A CB   1 
ATOM   4109 C CB   B LYS   A 1 163 ? 3.865  -7.725  -1.482  0.58 22.88 ?  163 LYS   A CB   1 
ATOM   4110 C CG   A LYS   A 1 163 ? 3.806  -7.883  -2.537  0.42 28.68 ?  163 LYS   A CG   1 
ATOM   4111 C CG   B LYS   A 1 163 ? 3.696  -8.292  -2.861  0.58 28.06 ?  163 LYS   A CG   1 
ATOM   4112 C CD   A LYS   A 1 163 ? 4.246  -6.941  -3.650  0.42 32.01 ?  163 LYS   A CD   1 
ATOM   4113 C CD   B LYS   A 1 163 ? 3.777  -7.148  -3.850  0.58 32.65 ?  163 LYS   A CD   1 
ATOM   4114 C CE   A LYS   A 1 163 ? 4.175  -7.619  -5.011  0.42 34.87 ?  163 LYS   A CE   1 
ATOM   4115 C CE   B LYS   A 1 163 ? 4.090  -7.626  -5.247  0.58 36.47 ?  163 LYS   A CE   1 
ATOM   4116 N NZ   A LYS   A 1 163 ? 4.820  -6.806  -6.079  0.42 36.32 ?  163 LYS   A NZ   1 
ATOM   4117 N NZ   B LYS   A 1 163 ? 4.553  -6.501  -6.102  0.58 38.51 ?  163 LYS   A NZ   1 
ATOM   4118 H H    A LYS   A 1 163 ? 3.615  -6.506  1.162   0.42 24.41 ?  163 LYS   A H    1 
ATOM   4119 H H    B LYS   A 1 163 ? 3.701  -7.042  0.788   0.58 20.42 ?  163 LYS   A H    1 
ATOM   4120 H HA   A LYS   A 1 163 ? 2.626  -8.548  -0.160  0.42 25.81 ?  163 LYS   A HA   1 
ATOM   4121 H HA   B LYS   A 1 163 ? 2.697  -9.095  -0.501  0.58 22.22 ?  163 LYS   A HA   1 
ATOM   4122 H HB2  A LYS   A 1 163 ? 3.010  -6.521  -1.241  0.42 30.07 ?  163 LYS   A HB2  1 
ATOM   4123 H HB2  B LYS   A 1 163 ? 3.284  -6.953  -1.414  0.58 27.48 ?  163 LYS   A HB2  1 
ATOM   4124 H HB3  A LYS   A 1 163 ? 4.574  -6.712  -1.052  0.42 30.07 ?  163 LYS   A HB3  1 
ATOM   4125 H HB3  B LYS   A 1 163 ? 4.789  -7.443  -1.397  0.58 27.48 ?  163 LYS   A HB3  1 
ATOM   4126 H HG2  A LYS   A 1 163 ? 4.450  -8.605  -2.488  0.42 34.44 ?  163 LYS   A HG2  1 
ATOM   4127 H HG2  B LYS   A 1 163 ? 4.409  -8.923  -3.048  0.58 33.70 ?  163 LYS   A HG2  1 
ATOM   4128 H HG3  A LYS   A 1 163 ? 2.929  -8.230  -2.765  0.42 34.44 ?  163 LYS   A HG3  1 
ATOM   4129 H HG3  B LYS   A 1 163 ? 2.827  -8.717  -2.940  0.58 33.70 ?  163 LYS   A HG3  1 
ATOM   4130 H HD2  A LYS   A 1 163 ? 3.661  -6.167  -3.667  0.42 38.44 ?  163 LYS   A HD2  1 
ATOM   4131 H HD2  B LYS   A 1 163 ? 2.923  -6.686  -3.869  0.58 39.21 ?  163 LYS   A HD2  1 
ATOM   4132 H HD3  A LYS   A 1 163 ? 5.163  -6.666  -3.495  0.42 38.44 ?  163 LYS   A HD3  1 
ATOM   4133 H HD3  B LYS   A 1 163 ? 4.478  -6.537  -3.570  0.58 39.21 ?  163 LYS   A HD3  1 
ATOM   4134 H HE2  A LYS   A 1 163 ? 4.621  -8.478  -4.970  0.42 41.87 ?  163 LYS   A HE2  1 
ATOM   4135 H HE2  B LYS   A 1 163 ? 4.792  -8.293  -5.205  0.58 43.79 ?  163 LYS   A HE2  1 
ATOM   4136 H HE3  A LYS   A 1 163 ? 3.245  -7.745  -5.252  0.42 41.87 ?  163 LYS   A HE3  1 
ATOM   4137 H HE3  B LYS   A 1 163 ? 3.289  -8.002  -5.641  0.58 43.79 ?  163 LYS   A HE3  1 
ATOM   4138 H HZ1  A LYS   A 1 163 ? 4.763  -7.229  -6.860  0.42 43.62 ?  163 LYS   A HZ1  1 
ATOM   4139 H HZ1  B LYS   A 1 163 ? 4.735  -6.798  -6.919  0.58 46.24 ?  163 LYS   A HZ1  1 
ATOM   4140 H HZ2  A LYS   A 1 163 ? 4.413  -6.017  -6.147  0.42 43.62 ?  163 LYS   A HZ2  1 
ATOM   4141 H HZ2  B LYS   A 1 163 ? 3.921  -5.877  -6.152  0.58 46.24 ?  163 LYS   A HZ2  1 
ATOM   4142 H HZ3  A LYS   A 1 163 ? 5.678  -6.673  -5.884  0.42 43.62 ?  163 LYS   A HZ3  1 
ATOM   4143 H HZ3  B LYS   A 1 163 ? 5.290  -6.139  -5.754  0.58 46.24 ?  163 LYS   A HZ3  1 
ATOM   4144 N N    A LEU   A 1 164 ? 5.665  -8.874  0.775   0.42 17.52 ?  164 LEU   A N    1 
ATOM   4145 N N    B LEU   A 1 164 ? 5.774  -9.373  0.382   0.58 15.05 ?  164 LEU   A N    1 
ATOM   4146 C CA   A LEU   A 1 164 ? 6.756  -9.841  0.884   0.42 16.13 ?  164 LEU   A CA   1 
ATOM   4147 C CA   B LEU   A 1 164 ? 6.840  -10.352 0.573   0.58 14.44 ?  164 LEU   A CA   1 
ATOM   4148 C C    A LEU   A 1 164 ? 6.326  -11.065 1.677   0.42 16.58 ?  164 LEU   A C    1 
ATOM   4149 C C    B LEU   A 1 164 ? 6.406  -11.464 1.516   0.58 14.71 ?  164 LEU   A C    1 
ATOM   4150 O O    A LEU   A 1 164 ? 6.649  -12.201 1.312   0.42 17.13 ?  164 LEU   A O    1 
ATOM   4151 O O    B LEU   A 1 164 ? 6.688  -12.642 1.269   0.58 15.27 ?  164 LEU   A O    1 
ATOM   4152 C CB   A LEU   A 1 164 ? 7.964  -9.187  1.552   0.42 14.80 ?  164 LEU   A CB   1 
ATOM   4153 C CB   B LEU   A 1 164 ? 8.079  -9.667  1.142   0.58 14.04 ?  164 LEU   A CB   1 
ATOM   4154 C CG   A LEU   A 1 164 ? 8.750  -8.197  0.694   0.42 14.49 ?  164 LEU   A CG   1 
ATOM   4155 C CG   B LEU   A 1 164 ? 8.787  -8.659  0.245   0.58 14.45 ?  164 LEU   A CG   1 
ATOM   4156 C CD1  A LEU   A 1 164 ? 9.686  -7.367  1.554   0.42 14.11 ?  164 LEU   A CD1  1 
ATOM   4157 C CD1  B LEU   A 1 164 ? 9.827  -7.904  1.047   0.58 14.08 ?  164 LEU   A CD1  1 
ATOM   4158 C CD2  A LEU   A 1 164 ? 9.528  -8.936  -0.385  0.42 14.44 ?  164 LEU   A CD2  1 
ATOM   4159 C CD2  B LEU   A 1 164 ? 9.421  -9.372  -0.930  0.58 15.42 ?  164 LEU   A CD2  1 
ATOM   4160 H H    A LEU   A 1 164 ? 5.805  -8.127  1.179   0.42 21.05 ?  164 LEU   A H    1 
ATOM   4161 H H    B LEU   A 1 164 ? 5.969  -8.594  0.652   0.58 18.08 ?  164 LEU   A H    1 
ATOM   4162 H HA   A LEU   A 1 164 ? 7.015  -10.130 -0.002  0.42 19.38 ?  164 LEU   A HA   1 
ATOM   4163 H HA   B LEU   A 1 164 ? 7.073  -10.765 -0.276  0.58 17.35 ?  164 LEU   A HA   1 
ATOM   4164 H HB2  A LEU   A 1 164 ? 7.657  -8.707  2.338   0.42 17.79 ?  164 LEU   A HB2  1 
ATOM   4165 H HB2  B LEU   A 1 164 ? 7.819  -9.209  1.951   0.58 16.87 ?  164 LEU   A HB2  1 
ATOM   4166 H HB3  A LEU   A 1 164 ? 8.579  -9.886  1.822   0.42 17.79 ?  164 LEU   A HB3  1 
ATOM   4167 H HB3  B LEU   A 1 164 ? 8.729  -10.360 1.363   0.58 16.87 ?  164 LEU   A HB3  1 
ATOM   4168 H HG   A LEU   A 1 164 ? 8.128  -7.592  0.258   0.42 17.42 ?  164 LEU   A HG   1 
ATOM   4169 H HG   B LEU   A 1 164 ? 8.137  -8.024  -0.094  0.58 17.37 ?  164 LEU   A HG   1 
ATOM   4170 H HD11 A LEU   A 1 164 ? 10.174 -6.751  0.985   0.42 16.96 ?  164 LEU   A HD11 1 
ATOM   4171 H HD11 B LEU   A 1 164 ? 10.271 -7.270  0.467   0.58 16.93 ?  164 LEU   A HD11 1 
ATOM   4172 H HD12 A LEU   A 1 164 ? 9.163  -6.873  2.205   0.42 16.96 ?  164 LEU   A HD12 1 
ATOM   4173 H HD12 B LEU   A 1 164 ? 9.388  -7.441  1.777   0.58 16.93 ?  164 LEU   A HD12 1 
ATOM   4174 H HD13 A LEU   A 1 164 ? 10.305 -7.960  2.008   0.42 16.96 ?  164 LEU   A HD13 1 
ATOM   4175 H HD13 B LEU   A 1 164 ? 10.472 -8.540  1.400   0.58 16.93 ?  164 LEU   A HD13 1 
ATOM   4176 H HD21 A LEU   A 1 164 ? 10.079 -8.300  -0.869  0.42 17.35 ?  164 LEU   A HD21 1 
ATOM   4177 H HD21 B LEU   A 1 164 ? 9.933  -8.731  -1.444  0.58 18.53 ?  164 LEU   A HD21 1 
ATOM   4178 H HD22 A LEU   A 1 164 ? 10.088 -9.608  0.033   0.42 17.35 ?  164 LEU   A HD22 1 
ATOM   4179 H HD22 B LEU   A 1 164 ? 10.002 -10.072 -0.595  0.58 18.53 ?  164 LEU   A HD22 1 
ATOM   4180 H HD23 A LEU   A 1 164 ? 8.902  -9.360  -0.994  0.42 17.35 ?  164 LEU   A HD23 1 
ATOM   4181 H HD23 B LEU   A 1 164 ? 8.721  -9.757  -1.480  0.58 18.53 ?  164 LEU   A HD23 1 
ATOM   4182 N N    A VAL   A 1 165 ? 5.606  -10.847 2.774   0.42 16.94 ?  165 VAL   A N    1 
ATOM   4183 N N    B VAL   A 1 165 ? 5.741  -11.110 2.616   0.58 15.36 ?  165 VAL   A N    1 
ATOM   4184 C CA   A VAL   A 1 165 ? 5.147  -11.953 3.602   0.42 17.46 ?  165 VAL   A CA   1 
ATOM   4185 C CA   B VAL   A 1 165 ? 5.347  -12.107 3.609   0.58 16.61 ?  165 VAL   A CA   1 
ATOM   4186 C C    A VAL   A 1 165 ? 4.113  -12.784 2.852   0.42 18.23 ?  165 VAL   A C    1 
ATOM   4187 C C    B VAL   A 1 165 ? 4.262  -13.016 3.049   0.58 16.96 ?  165 VAL   A C    1 
ATOM   4188 O O    A VAL   A 1 165 ? 4.228  -14.011 2.749   0.42 17.90 ?  165 VAL   A O    1 
ATOM   4189 O O    B VAL   A 1 165 ? 4.316  -14.244 3.196   0.58 17.56 ?  165 VAL   A O    1 
ATOM   4190 C CB   A VAL   A 1 165 ? 4.590  -11.402 4.927   0.42 17.60 ?  165 VAL   A CB   1 
ATOM   4191 C CB   B VAL   A 1 165 ? 4.903  -11.402 4.906   0.58 18.27 ?  165 VAL   A CB   1 
ATOM   4192 C CG1  A VAL   A 1 165 ? 3.938  -12.507 5.729   0.42 17.96 ?  165 VAL   A CG1  1 
ATOM   4193 C CG1  B VAL   A 1 165 ? 4.275  -12.391 5.872   0.58 19.25 ?  165 VAL   A CG1  1 
ATOM   4194 C CG2  A VAL   A 1 165 ? 5.699  -10.717 5.720   0.42 17.66 ?  165 VAL   A CG2  1 
ATOM   4195 C CG2  B VAL   A 1 165 ? 6.083  -10.692 5.561   0.58 18.53 ?  165 VAL   A CG2  1 
ATOM   4196 H H    A VAL   A 1 165 ? 5.374  -10.070 3.060   0.42 20.35 ?  165 VAL   A H    1 
ATOM   4197 H H    B VAL   A 1 165 ? 5.513  -10.312 2.811   0.58 18.46 ?  165 VAL   A H    1 
ATOM   4198 H HA   A VAL   A 1 165 ? 5.902  -12.526 3.812   0.42 20.98 ?  165 VAL   A HA   1 
ATOM   4199 H HA   B VAL   A 1 165 ? 6.111  -12.662 3.829   0.58 19.96 ?  165 VAL   A HA   1 
ATOM   4200 H HB   A VAL   A 1 165 ? 3.915  -10.736 4.731   0.42 21.14 ?  165 VAL   A HB   1 
ATOM   4201 H HB   B VAL   A 1 165 ? 4.234  -10.733 4.693   0.58 21.95 ?  165 VAL   A HB   1 
ATOM   4202 H HG11 A VAL   A 1 165 ? 3.838  -12.211 6.646   0.42 21.58 ?  165 VAL   A HG11 1 
ATOM   4203 H HG11 B VAL   A 1 165 ? 4.252  -11.994 6.757   0.58 23.13 ?  165 VAL   A HG11 1 
ATOM   4204 H HG12 A VAL   A 1 165 ? 3.069  -12.702 5.346   0.42 21.58 ?  165 VAL   A HG12 1 
ATOM   4205 H HG12 B VAL   A 1 165 ? 3.374  -12.593 5.578   0.58 23.13 ?  165 VAL   A HG12 1 
ATOM   4206 H HG13 A VAL   A 1 165 ? 4.503  -13.295 5.695   0.42 21.58 ?  165 VAL   A HG13 1 
ATOM   4207 H HG13 B VAL   A 1 165 ? 4.812  -13.198 5.887   0.58 23.13 ?  165 VAL   A HG13 1 
ATOM   4208 H HG21 A VAL   A 1 165 ? 5.338  -10.396 6.561   0.42 21.22 ?  165 VAL   A HG21 1 
ATOM   4209 H HG21 B VAL   A 1 165 ? 5.777  -10.249 6.370   0.58 22.27 ?  165 VAL   A HG21 1 
ATOM   4210 H HG22 A VAL   A 1 165 ? 6.411  -11.355 5.888   0.42 21.22 ?  165 VAL   A HG22 1 
ATOM   4211 H HG22 B VAL   A 1 165 ? 6.763  -11.346 5.780   0.58 22.27 ?  165 VAL   A HG22 1 
ATOM   4212 H HG23 A VAL   A 1 165 ? 6.045  -9.969  5.203   0.42 21.22 ?  165 VAL   A HG23 1 
ATOM   4213 H HG23 B VAL   A 1 165 ? 6.438  -10.037 4.941   0.58 22.27 ?  165 VAL   A HG23 1 
ATOM   4214 N N    A SER   A 1 166 ? 3.098  -12.122 2.297   0.42 19.64 ?  166 SER   A N    1 
ATOM   4215 N N    B SER   A 1 166 ? 3.270  -12.434 2.382   0.58 17.80 ?  166 SER   A N    1 
ATOM   4216 C CA   A SER   A 1 166 ? 1.993  -12.833 1.667   0.42 21.16 ?  166 SER   A CA   1 
ATOM   4217 C CA   B SER   A 1 166 ? 2.136  -13.229 1.933   0.58 19.10 ?  166 SER   A CA   1 
ATOM   4218 C C    A SER   A 1 166 ? 2.441  -13.644 0.462   0.42 21.13 ?  166 SER   A C    1 
ATOM   4219 C C    B SER   A 1 166 ? 2.523  -14.187 0.815   0.58 19.38 ?  166 SER   A C    1 
ATOM   4220 O O    A SER   A 1 166 ? 1.760  -14.606 0.087   0.42 21.40 ?  166 SER   A O    1 
ATOM   4221 O O    B SER   A 1 166 ? 1.943  -15.273 0.707   0.58 20.10 ?  166 SER   A O    1 
ATOM   4222 C CB   A SER   A 1 166 ? 0.922  -11.834 1.226   0.42 23.23 ?  166 SER   A CB   1 
ATOM   4223 C CB   B SER   A 1 166 ? 1.005  -12.301 1.499   0.58 21.65 ?  166 SER   A CB   1 
ATOM   4224 O OG   A SER   A 1 166 ? 0.441  -11.067 2.319   0.42 25.14 ?  166 SER   A OG   1 
ATOM   4225 O OG   B SER   A 1 166 ? 0.688  -11.408 2.552   0.58 24.77 ?  166 SER   A OG   1 
ATOM   4226 H H    A SER   A 1 166 ? 3.033  -11.268 2.272   0.42 23.59 ?  166 SER   A H    1 
ATOM   4227 H H    B SER   A 1 166 ? 3.226  -11.604 2.187   0.58 21.39 ?  166 SER   A H    1 
ATOM   4228 H HA   A SER   A 1 166 ? 1.593  -13.436 2.313   0.42 25.42 ?  166 SER   A HA   1 
ATOM   4229 H HA   B SER   A 1 166 ? 1.800  -13.757 2.680   0.58 22.94 ?  166 SER   A HA   1 
ATOM   4230 H HB2  A SER   A 1 166 ? 1.306  -11.234 0.569   0.42 27.91 ?  166 SER   A HB2  1 
ATOM   4231 H HB2  B SER   A 1 166 ? 1.281  -11.799 0.718   0.58 26.01 ?  166 SER   A HB2  1 
ATOM   4232 H HB3  A SER   A 1 166 ? 0.181  -12.323 0.834   0.42 27.91 ?  166 SER   A HB3  1 
ATOM   4233 H HB3  B SER   A 1 166 ? 0.213  -12.826 1.290   0.58 26.01 ?  166 SER   A HB3  1 
ATOM   4234 H HG   A SER   A 1 166 ? 1.077  -10.644 2.671   0.42 30.20 ?  166 SER   A HG   1 
ATOM   4235 H HG   B SER   A 1 166 ? 1.340  -10.902 2.715   0.58 29.75 ?  166 SER   A HG   1 
ATOM   4236 N N    A SER   A 1 167 ? 3.559  -13.273 -0.159  0.42 21.56 ?  167 SER   A N    1 
ATOM   4237 N N    B SER   A 1 167 ? 3.501  -13.820 -0.009  0.58 19.57 ?  167 SER   A N    1 
ATOM   4238 C CA   A SER   A 1 167 ? 4.054  -13.958 -1.343  0.42 21.97 ?  167 SER   A CA   1 
ATOM   4239 C CA   B SER   A 1 167 ? 3.913  -14.652 -1.130  0.58 20.23 ?  167 SER   A CA   1 
ATOM   4240 C C    A SER   A 1 167 ? 5.255  -14.853 -1.066  0.42 22.27 ?  167 SER   A C    1 
ATOM   4241 C C    B SER   A 1 167 ? 5.057  -15.591 -0.780  0.58 20.58 ?  167 SER   A C    1 
ATOM   4242 O O    A SER   A 1 167 ? 5.770  -15.471 -2.002  0.42 22.06 ?  167 SER   A O    1 
ATOM   4243 O O    B SER   A 1 167 ? 5.546  -16.304 -1.663  0.58 20.31 ?  167 SER   A O    1 
ATOM   4244 C CB   A SER   A 1 167 ? 4.409  -12.939 -2.431  0.42 22.14 ?  167 SER   A CB   1 
ATOM   4245 C CB   B SER   A 1 167 ? 4.311  -13.778 -2.324  0.58 20.80 ?  167 SER   A CB   1 
ATOM   4246 O OG   A SER   A 1 167 ? 5.455  -12.086 -2.003  0.42 22.34 ?  167 SER   A OG   1 
ATOM   4247 O OG   B SER   A 1 167 ? 5.455  -12.991 -2.035  0.58 21.11 ?  167 SER   A OG   1 
ATOM   4248 H H    A SER   A 1 167 ? 4.044  -12.604 0.087   0.42 25.90 ?  167 SER   A H    1 
ATOM   4249 H H    B SER   A 1 167 ? 3.932  -13.086 0.066   0.58 23.51 ?  167 SER   A H    1 
ATOM   4250 H HA   A SER   A 1 167 ? 3.347  -14.518 -1.691  0.42 26.39 ?  167 SER   A HA   1 
ATOM   4251 H HA   B SER   A 1 167 ? 3.154  -15.191 -1.403  0.58 24.31 ?  167 SER   A HA   1 
ATOM   4252 H HB2  A SER   A 1 167 ? 4.694  -13.415 -3.226  0.42 26.60 ?  167 SER   A HB2  1 
ATOM   4253 H HB2  B SER   A 1 167 ? 4.505  -14.356 -3.078  0.58 24.98 ?  167 SER   A HB2  1 
ATOM   4254 H HB3  A SER   A 1 167 ? 3.622  -12.404 -2.631  0.42 26.60 ?  167 SER   A HB3  1 
ATOM   4255 H HB3  B SER   A 1 167 ? 3.568  -13.192 -2.543  0.58 24.98 ?  167 SER   A HB3  1 
ATOM   4256 H HG   A SER   A 1 167 ? 5.216  -11.661 -1.318  0.42 26.83 ?  167 SER   A HG   1 
ATOM   4257 H HG   B SER   A 1 167 ? 5.294  -12.484 -1.385  0.58 25.36 ?  167 SER   A HG   1 
ATOM   4258 N N    A PHE   A 1 168 ? 5.715  -14.943 0.182   0.42 22.70 ?  168 PHE   A N    1 
ATOM   4259 N N    B PHE   A 1 168 ? 5.488  -15.623 0.481   0.58 22.23 ?  168 PHE   A N    1 
ATOM   4260 C CA   A PHE   A 1 168 ? 6.894  -15.750 0.469   0.42 23.74 ?  168 PHE   A CA   1 
ATOM   4261 C CA   B PHE   A 1 168 ? 6.640  -16.434 0.847   0.58 24.62 ?  168 PHE   A CA   1 
ATOM   4262 C C    A PHE   A 1 168 ? 6.561  -17.233 0.388   0.42 26.36 ?  168 PHE   A C    1 
ATOM   4263 C C    B PHE   A 1 168 ? 6.282  -17.894 1.104   0.58 29.80 ?  168 PHE   A C    1 
ATOM   4264 O O    A PHE   A 1 168 ? 5.570  -17.694 0.964   0.42 27.43 ?  168 PHE   A O    1 
ATOM   4265 O O    B PHE   A 1 168 ? 7.177  -18.745 1.075   0.58 31.24 ?  168 PHE   A O    1 
ATOM   4266 C CB   A PHE   A 1 168 ? 7.468  -15.427 1.847   0.42 22.43 ?  168 PHE   A CB   1 
ATOM   4267 C CB   B PHE   A 1 168 ? 7.310  -15.863 2.094   0.58 22.65 ?  168 PHE   A CB   1 
ATOM   4268 C CG   A PHE   A 1 168 ? 8.703  -16.225 2.177   0.42 21.26 ?  168 PHE   A CG   1 
ATOM   4269 C CG   B PHE   A 1 168 ? 8.650  -16.465 2.372   0.58 20.75 ?  168 PHE   A CG   1 
ATOM   4270 C CD1  A PHE   A 1 168 ? 9.925  -15.887 1.621   0.42 20.89 ?  168 PHE   A CD1  1 
ATOM   4271 C CD1  B PHE   A 1 168 ? 9.756  -16.066 1.645   0.58 20.07 ?  168 PHE   A CD1  1 
ATOM   4272 C CD2  A PHE   A 1 168 ? 8.642  -17.321 3.023   0.42 20.31 ?  168 PHE   A CD2  1 
ATOM   4273 C CD2  B PHE   A 1 168 ? 8.807  -17.440 3.342   0.58 19.33 ?  168 PHE   A CD2  1 
ATOM   4274 C CE1  A PHE   A 1 168 ? 11.062 -16.618 1.907   0.42 20.39 ?  168 PHE   A CE1  1 
ATOM   4275 C CE1  B PHE   A 1 168 ? 10.995 -16.619 1.882   0.58 19.39 ?  168 PHE   A CE1  1 
ATOM   4276 C CE2  A PHE   A 1 168 ? 9.783  -18.057 3.318   0.42 19.84 ?  168 PHE   A CE2  1 
ATOM   4277 C CE2  B PHE   A 1 168 ? 10.047 -17.999 3.587   0.58 18.19 ?  168 PHE   A CE2  1 
ATOM   4278 C CZ   A PHE   A 1 168 ? 10.993 -17.703 2.756   0.42 20.02 ?  168 PHE   A CZ   1 
ATOM   4279 C CZ   B PHE   A 1 168 ? 11.144 -17.586 2.855   0.58 18.75 ?  168 PHE   A CZ   1 
ATOM   4280 H H    A PHE   A 1 168 ? 5.369  -14.550 0.867   0.42 27.27 ?  168 PHE   A H    1 
ATOM   4281 H H    B PHE   A 1 168 ? 5.132  -15.185 1.137   0.58 26.70 ?  168 PHE   A H    1 
ATOM   4282 H HA   A PHE   A 1 168 ? 7.576  -15.555 -0.193  0.42 28.51 ?  168 PHE   A HA   1 
ATOM   4283 H HA   B PHE   A 1 168 ? 7.282  -16.399 0.123   0.58 29.57 ?  168 PHE   A HA   1 
ATOM   4284 H HB2  A PHE   A 1 168 ? 7.704  -14.486 1.878   0.42 26.94 ?  168 PHE   A HB2  1 
ATOM   4285 H HB2  B PHE   A 1 168 ? 7.433  -14.906 1.978   0.58 27.21 ?  168 PHE   A HB2  1 
ATOM   4286 H HB3  A PHE   A 1 168 ? 6.798  -15.621 2.521   0.42 26.94 ?  168 PHE   A HB3  1 
ATOM   4287 H HB3  B PHE   A 1 168 ? 6.744  -16.031 2.862   0.58 27.21 ?  168 PHE   A HB3  1 
ATOM   4288 H HD1  A PHE   A 1 168 ? 9.982  -15.157 1.047   0.42 25.10 ?  168 PHE   A HD1  1 
ATOM   4289 H HD1  B PHE   A 1 168 ? 9.664  -15.412 0.987   0.58 24.12 ?  168 PHE   A HD1  1 
ATOM   4290 H HD2  A PHE   A 1 168 ? 7.829  -17.564 3.404   0.42 24.40 ?  168 PHE   A HD2  1 
ATOM   4291 H HD2  B PHE   A 1 168 ? 8.072  -17.719 3.836   0.58 23.22 ?  168 PHE   A HD2  1 
ATOM   4292 H HE1  A PHE   A 1 168 ? 11.877 -16.375 1.528   0.42 24.50 ?  168 PHE   A HE1  1 
ATOM   4293 H HE1  B PHE   A 1 168 ? 11.734 -16.336 1.388   0.58 23.30 ?  168 PHE   A HE1  1 
ATOM   4294 H HE2  A PHE   A 1 168 ? 9.733  -18.791 3.889   0.42 23.83 ?  168 PHE   A HE2  1 
ATOM   4295 H HE2  B PHE   A 1 168 ? 10.146 -18.651 4.243   0.58 21.86 ?  168 PHE   A HE2  1 
ATOM   4296 H HZ   A PHE   A 1 168 ? 11.760 -18.194 2.950   0.42 24.05 ?  168 PHE   A HZ   1 
ATOM   4297 H HZ   B PHE   A 1 168 ? 11.981 -17.958 3.017   0.58 22.52 ?  168 PHE   A HZ   1 
ATOM   4298 N N    A LEU   A 1 169 ? 7.400  -17.978 -0.323  0.42 27.73 ?  169 LEU   A N    1 
ATOM   4299 N N    B LEU   A 1 169 ? 5.003  -18.184 1.340   0.58 33.00 ?  169 LEU   A N    1 
ATOM   4300 C CA   A LEU   A 1 169 ? 7.216  -19.412 -0.462  0.42 29.11 ?  169 LEU   A CA   1 
ATOM   4301 C CA   B LEU   A 1 169 ? 4.484  -19.493 1.765   0.58 35.38 ?  169 LEU   A CA   1 
ATOM   4302 C C    A LEU   A 1 169 ? 8.097  -20.154 0.538   0.42 29.25 ?  169 LEU   A C    1 
ATOM   4303 C C    B LEU   A 1 169 ? 4.591  -19.650 3.279   0.58 37.26 ?  169 LEU   A C    1 
ATOM   4304 O O    A LEU   A 1 169 ? 7.618  -20.602 1.580   0.42 29.43 ?  169 LEU   A O    1 
ATOM   4305 O O    B LEU   A 1 169 ? 4.378  -18.705 4.037   0.58 38.05 ?  169 LEU   A O    1 
ATOM   4306 C CB   A LEU   A 1 169 ? 7.544  -19.846 -1.893  0.42 30.03 ?  169 LEU   A CB   1 
ATOM   4307 C CB   B LEU   A 1 169 ? 5.174  -20.690 1.095   0.58 35.37 ?  169 LEU   A CB   1 
ATOM   4308 C CG   A LEU   A 1 169 ? 7.156  -21.273 -2.279  0.42 30.87 ?  169 LEU   A CG   1 
ATOM   4309 C CG   B LEU   A 1 169 ? 5.062  -20.837 -0.421  0.58 35.06 ?  169 LEU   A CG   1 
ATOM   4310 C CD1  A LEU   A 1 169 ? 5.711  -21.552 -1.900  0.42 31.24 ?  169 LEU   A CD1  1 
ATOM   4311 C CD1  B LEU   A 1 169 ? 5.184  -22.302 -0.820  0.58 34.91 ?  169 LEU   A CD1  1 
ATOM   4312 C CD2  A LEU   A 1 169 ? 7.369  -21.488 -3.769  0.42 31.05 ?  169 LEU   A CD2  1 
ATOM   4313 C CD2  B LEU   A 1 169 ? 3.763  -20.246 -0.924  0.58 34.93 ?  169 LEU   A CD2  1 
ATOM   4314 O OXT  A LEU   A 1 169 ? 9.302  -20.312 0.342   0.42 28.90 -1 169 LEU   A OXT  1 
ATOM   4315 O OXT  B LEU   A 1 169 ? 4.895  -20.736 3.776   0.58 38.02 -1 169 LEU   A OXT  1 
ATOM   4316 H H    A LEU   A 1 169 ? 8.084  -17.668 -0.744  0.42 33.30 ?  169 LEU   A H    1 
ATOM   4317 H H    B LEU   A 1 169 ? 4.380  -17.599 1.270   0.58 39.63 ?  169 LEU   A H    1 
ATOM   4318 H HA   A LEU   A 1 169 ? 6.292  -19.629 -0.271  0.42 34.96 ?  169 LEU   A HA   1 
ATOM   4319 H HA   B LEU   A 1 169 ? 3.544  -19.518 1.513   0.58 42.49 ?  169 LEU   A HA   1 
ATOM   4320 H HB2  A LEU   A 1 169 ? 7.086  -19.249 -2.505  0.42 36.06 ?  169 LEU   A HB2  1 
ATOM   4321 H HB2  B LEU   A 1 169 ? 6.113  -20.677 1.321   0.58 42.47 ?  169 LEU   A HB2  1 
ATOM   4322 H HB3  A LEU   A 1 169 ? 8.502  -19.764 -2.022  0.42 36.06 ?  169 LEU   A HB3  1 
ATOM   4323 H HB3  B LEU   A 1 169 ? 4.781  -21.496 1.477   0.58 42.47 ?  169 LEU   A HB3  1 
ATOM   4324 H HG   A LEU   A 1 169 ? 7.722  -21.898 -1.800  0.42 37.07 ?  169 LEU   A HG   1 
ATOM   4325 H HG   B LEU   A 1 169 ? 5.792  -20.355 -0.838  0.58 42.10 ?  169 LEU   A HG   1 
ATOM   4326 H HD11 A LEU   A 1 169 ? 5.413  -22.349 -2.361  0.42 37.52 ?  169 LEU   A HD11 1 
ATOM   4327 H HD11 B LEU   A 1 169 ? 4.995  -22.392 -1.768  0.58 41.92 ?  169 LEU   A HD11 1 
ATOM   4328 H HD12 A LEU   A 1 169 ? 5.657  -21.684 -0.940  0.42 37.52 ?  169 LEU   A HD12 1 
ATOM   4329 H HD12 B LEU   A 1 169 ? 6.084  -22.609 -0.631  0.58 41.92 ?  169 LEU   A HD12 1 
ATOM   4330 H HD13 A LEU   A 1 169 ? 5.166  -20.793 -2.162  0.42 37.52 ?  169 LEU   A HD13 1 
ATOM   4331 H HD13 B LEU   A 1 169 ? 4.545  -22.820 -0.306  0.58 41.92 ?  169 LEU   A HD13 1 
ATOM   4332 H HD21 A LEU   A 1 169 ? 7.125  -22.399 -3.994  0.42 37.29 ?  169 LEU   A HD21 1 
ATOM   4333 H HD21 B LEU   A 1 169 ? 3.554  -20.642 -1.780  0.58 41.94 ?  169 LEU   A HD21 1 
ATOM   4334 H HD22 A LEU   A 1 169 ? 6.809  -20.865 -4.259  0.42 37.29 ?  169 LEU   A HD22 1 
ATOM   4335 H HD22 B LEU   A 1 169 ? 3.048  -20.430 -0.295  0.58 41.94 ?  169 LEU   A HD22 1 
ATOM   4336 H HD23 A LEU   A 1 169 ? 8.302  -21.331 -3.981  0.42 37.29 ?  169 LEU   A HD23 1 
ATOM   4337 H HD23 B LEU   A 1 169 ? 3.875  -19.290 -1.013  0.58 41.94 ?  169 LEU   A HD23 1 
ATOM   4338 N N    A SER   B 1 1   ? 50.873 -9.228  -23.680 0.42 28.14 ?  1   SER   B N    1 
ATOM   4339 N N    B SER   B 1 1   ? 50.900 -9.328  -23.729 0.58 26.95 ?  1   SER   B N    1 
ATOM   4340 C CA   A SER   B 1 1   ? 51.418 -10.309 -22.833 0.42 28.03 ?  1   SER   B CA   1 
ATOM   4341 C CA   B SER   B 1 1   ? 51.380 -10.308 -22.732 0.58 26.97 ?  1   SER   B CA   1 
ATOM   4342 C C    A SER   B 1 1   ? 50.359 -11.372 -22.578 0.42 26.94 ?  1   SER   B C    1 
ATOM   4343 C C    B SER   B 1 1   ? 50.334 -11.385 -22.490 0.58 25.57 ?  1   SER   B C    1 
ATOM   4344 O O    A SER   B 1 1   ? 49.177 -11.187 -22.884 0.42 26.62 ?  1   SER   B O    1 
ATOM   4345 O O    B SER   B 1 1   ? 49.135 -11.197 -22.741 0.58 25.32 ?  1   SER   B O    1 
ATOM   4346 C CB   A SER   B 1 1   ? 51.927 -9.749  -21.508 0.42 28.59 ?  1   SER   B CB   1 
ATOM   4347 C CB   B SER   B 1 1   ? 51.725 -9.621  -21.415 0.58 27.81 ?  1   SER   B CB   1 
ATOM   4348 O OG   A SER   B 1 1   ? 50.853 -9.433  -20.644 0.42 29.68 ?  1   SER   B OG   1 
ATOM   4349 O OG   B SER   B 1 1   ? 50.569 -9.456  -20.615 0.58 29.29 ?  1   SER   B OG   1 
ATOM   4350 H H1   A SER   B 1 1   ? 50.711 -9.551  -24.491 0.42 33.79 ?  1   SER   B H1   1 
ATOM   4351 H H1   B SER   B 1 1   ? 50.825 -9.731  -24.517 0.58 32.36 ?  1   SER   B H1   1 
ATOM   4352 H H2   A SER   B 1 1   ? 50.123 -8.928  -23.317 0.42 33.79 ?  1   SER   B H2   1 
ATOM   4353 H H2   B SER   B 1 1   ? 50.111 -9.017  -23.472 0.58 32.36 ?  1   SER   B H2   1 
ATOM   4354 H H3   A SER   B 1 1   ? 51.471 -8.574  -23.730 0.42 33.79 ?  1   SER   B H3   1 
ATOM   4355 H H3   B SER   B 1 1   ? 51.486 -8.665  -23.783 0.58 32.36 ?  1   SER   B H3   1 
ATOM   4356 H HA   A SER   B 1 1   ? 52.158 -10.717 -23.301 0.42 33.66 ?  1   SER   B HA   1 
ATOM   4357 H HA   B SER   B 1 1   ? 52.177 -10.728 -23.080 0.58 32.39 ?  1   SER   B HA   1 
ATOM   4358 H HB2  A SER   B 1 1   ? 52.489 -10.416 -21.089 0.42 34.34 ?  1   SER   B HB2  1 
ATOM   4359 H HB2  B SER   B 1 1   ? 52.371 -10.168 -20.944 0.58 33.40 ?  1   SER   B HB2  1 
ATOM   4360 H HB3  A SER   B 1 1   ? 52.439 -8.943  -21.682 0.42 34.34 ?  1   SER   B HB3  1 
ATOM   4361 H HB3  B SER   B 1 1   ? 52.103 -8.749  -21.604 0.58 33.40 ?  1   SER   B HB3  1 
ATOM   4362 H HG   A SER   B 1 1   ? 51.143 -9.027  -19.969 0.42 35.65 ?  1   SER   B HG   1 
ATOM   4363 H HG   B SER   B 1 1   ? 50.746 -8.951  -19.966 0.58 35.17 ?  1   SER   B HG   1 
ATOM   4364 N N    A MET   B 1 2   ? 50.797 -12.486 -22.003 0.42 26.07 ?  2   MET   B N    1 
ATOM   4365 N N    B MET   B 1 2   ? 50.807 -12.519 -21.993 0.58 24.28 ?  2   MET   B N    1 
ATOM   4366 C CA   A MET   B 1 2   ? 49.972 -13.675 -21.836 0.42 25.65 ?  2   MET   B CA   1 
ATOM   4367 C CA   B MET   B 1 2   ? 49.994 -13.713 -21.814 0.58 23.77 ?  2   MET   B CA   1 
ATOM   4368 C C    A MET   B 1 2   ? 49.723 -13.886 -20.349 0.42 23.05 ?  2   MET   B C    1 
ATOM   4369 C C    B MET   B 1 2   ? 49.727 -13.878 -20.328 0.58 22.03 ?  2   MET   B C    1 
ATOM   4370 O O    A MET   B 1 2   ? 50.652 -14.187 -19.594 0.42 23.32 ?  2   MET   B O    1 
ATOM   4371 O O    B MET   B 1 2   ? 50.651 -14.129 -19.551 0.58 22.31 ?  2   MET   B O    1 
ATOM   4372 C CB   A MET   B 1 2   ? 50.680 -14.876 -22.454 0.42 28.68 ?  2   MET   B CB   1 
ATOM   4373 C CB   B MET   B 1 2   ? 50.750 -14.912 -22.360 0.58 26.49 ?  2   MET   B CB   1 
ATOM   4374 C CG   A MET   B 1 2   ? 49.817 -16.119 -22.596 0.42 31.45 ?  2   MET   B CG   1 
ATOM   4375 C CG   B MET   B 1 2   ? 49.886 -16.110 -22.737 0.58 28.79 ?  2   MET   B CG   1 
ATOM   4376 S SD   A MET   B 1 2   ? 50.657 -17.399 -23.547 0.42 34.03 ?  2   MET   B SD   1 
ATOM   4377 S SD   B MET   B 1 2   ? 50.761 -17.142 -23.924 0.58 30.62 ?  2   MET   B SD   1 
ATOM   4378 C CE   A MET   B 1 2   ? 51.239 -16.414 -24.925 0.42 34.49 ?  2   MET   B CE   1 
ATOM   4379 C CE   B MET   B 1 2   ? 51.457 -15.873 -24.957 0.58 31.47 ?  2   MET   B CE   1 
ATOM   4380 H H    A MET   B 1 2   ? 51.593 -12.580 -21.695 0.42 31.31 ?  2   MET   B H    1 
ATOM   4381 H H    B MET   B 1 2   ? 51.624 -12.635 -21.745 0.58 29.17 ?  2   MET   B H    1 
ATOM   4382 H HA   A MET   B 1 2   ? 49.128 -13.557 -22.296 0.42 30.81 ?  2   MET   B HA   1 
ATOM   4383 H HA   B MET   B 1 2   ? 49.161 -13.634 -22.301 0.58 28.55 ?  2   MET   B HA   1 
ATOM   4384 H HB2  A MET   B 1 2   ? 50.981 -14.602 -23.331 0.42 34.44 ?  2   MET   B HB2  1 
ATOM   4385 H HB2  B MET   B 1 2   ? 51.255 -14.577 -23.111 0.58 31.82 ?  2   MET   B HB2  1 
ATOM   4386 H HB3  A MET   B 1 2   ? 51.441 -15.120 -21.909 0.42 34.44 ?  2   MET   B HB3  1 
ATOM   4387 H HB3  B MET   B 1 2   ? 51.364 -15.240 -21.702 0.58 31.82 ?  2   MET   B HB3  1 
ATOM   4388 H HG2  A MET   B 1 2   ? 49.618 -16.473 -21.714 0.42 37.77 ?  2   MET   B HG2  1 
ATOM   4389 H HG2  B MET   B 1 2   ? 49.699 -16.642 -21.937 0.58 34.57 ?  2   MET   B HG2  1 
ATOM   4390 H HG3  A MET   B 1 2   ? 48.997 -15.893 -23.061 0.42 37.77 ?  2   MET   B HG3  1 
ATOM   4391 H HG3  B MET   B 1 2   ? 49.055 -15.817 -23.141 0.58 34.57 ?  2   MET   B HG3  1 
ATOM   4392 H HE1  A MET   B 1 2   ? 51.417 -16.995 -25.669 0.42 41.41 ?  2   MET   B HE1  1 
ATOM   4393 H HE1  B MET   B 1 2   ? 51.558 -16.247 -25.818 0.58 37.80 ?  2   MET   B HE1  1 
ATOM   4394 H HE2  A MET   B 1 2   ? 50.549 -15.768 -25.160 0.42 41.41 ?  2   MET   B HE2  1 
ATOM   4395 H HE2  B MET   B 1 2   ? 50.842 -15.118 -25.002 0.58 37.80 ?  2   MET   B HE2  1 
ATOM   4396 H HE3  A MET   B 1 2   ? 52.051 -15.943 -24.664 0.42 41.41 ?  2   MET   B HE3  1 
ATOM   4397 H HE3  B MET   B 1 2   ? 52.319 -15.590 -24.590 0.58 37.80 ?  2   MET   B HE3  1 
ATOM   4398 N N    . VAL   B 1 3   ? 48.469 -13.721 -19.933 1.00 20.63 ?  3   VAL   B N    1 
ATOM   4399 C CA   . VAL   B 1 3   ? 48.049 -13.951 -18.559 1.00 19.64 ?  3   VAL   B CA   1 
ATOM   4400 C C    . VAL   B 1 3   ? 46.817 -14.844 -18.582 1.00 17.84 ?  3   VAL   B C    1 
ATOM   4401 O O    . VAL   B 1 3   ? 46.088 -14.920 -19.573 1.00 18.57 ?  3   VAL   B O    1 
ATOM   4402 C CB   . VAL   B 1 3   ? 47.754 -12.638 -17.800 1.00 21.52 ?  3   VAL   B CB   1 
ATOM   4403 C CG1  . VAL   B 1 3   ? 49.004 -11.767 -17.708 1.00 22.17 ?  3   VAL   B CG1  1 
ATOM   4404 C CG2  . VAL   B 1 3   ? 46.603 -11.889 -18.463 1.00 22.15 ?  3   VAL   B CG2  1 
ATOM   4405 H H    A VAL   B 1 3   ? 47.828 -13.478 -20.453 0.42 24.78 ?  3   VAL   B H    1 
ATOM   4406 H H    B VAL   B 1 3   ? 47.833 -13.475 -20.457 0.58 24.78 ?  3   VAL   B H    1 
ATOM   4407 H HA   . VAL   B 1 3   ? 48.752 -14.423 -18.084 1.00 23.60 ?  3   VAL   B HA   1 
ATOM   4408 H HB   . VAL   B 1 3   ? 47.481 -12.862 -16.895 1.00 25.85 ?  3   VAL   B HB   1 
ATOM   4409 H HG11 . VAL   B 1 3   ? 48.787 -10.959 -17.218 1.00 26.63 ?  3   VAL   B HG11 1 
ATOM   4410 H HG12 . VAL   B 1 3   ? 49.698 -12.260 -17.243 1.00 26.63 ?  3   VAL   B HG12 1 
ATOM   4411 H HG13 . VAL   B 1 3   ? 49.298 -11.544 -18.603 1.00 26.63 ?  3   VAL   B HG13 1 
ATOM   4412 H HG21 . VAL   B 1 3   ? 46.546 -11.002 -18.085 1.00 26.61 ?  3   VAL   B HG21 1 
ATOM   4413 H HG22 . VAL   B 1 3   ? 46.765 -11.839 -19.416 1.00 26.61 ?  3   VAL   B HG22 1 
ATOM   4414 H HG23 . VAL   B 1 3   ? 45.773 -12.373 -18.296 1.00 26.61 ?  3   VAL   B HG23 1 
ATOM   4415 N N    . ASN   B 1 4   ? 46.596 -15.537 -17.468 1.00 15.87 ?  4   ASN   B N    1 
ATOM   4416 C CA   . ASN   B 1 4   ? 45.461 -16.450 -17.344 1.00 14.68 ?  4   ASN   B CA   1 
ATOM   4417 C C    . ASN   B 1 4   ? 45.402 -17.422 -18.525 1.00 14.93 ?  4   ASN   B C    1 
ATOM   4418 O O    . ASN   B 1 4   ? 44.341 -17.677 -19.093 1.00 15.52 ?  4   ASN   B O    1 
ATOM   4419 C CB   . ASN   B 1 4   ? 44.142 -15.686 -17.184 1.00 13.80 ?  4   ASN   B CB   1 
ATOM   4420 C CG   . ASN   B 1 4   ? 44.086 -14.878 -15.898 1.00 13.50 ?  4   ASN   B CG   1 
ATOM   4421 O OD1  . ASN   B 1 4   ? 44.378 -15.388 -14.820 1.00 13.24 ?  4   ASN   B OD1  1 
ATOM   4422 N ND2  . ASN   B 1 4   ? 43.728 -13.604 -16.011 1.00 14.24 ?  4   ASN   B ND2  1 
ATOM   4423 H H    . ASN   B 1 4   ? 47.098 -15.509 -16.772 1.00 19.07 ?  4   ASN   B H    1 
ATOM   4424 H HA   . ASN   B 1 4   ? 45.585 -16.976 -16.538 1.00 17.64 ?  4   ASN   B HA   1 
ATOM   4425 H HB2  . ASN   B 1 4   ? 44.038 -15.072 -17.929 1.00 16.59 ?  4   ASN   B HB2  1 
ATOM   4426 H HB3  . ASN   B 1 4   ? 43.406 -16.321 -17.174 1.00 16.59 ?  4   ASN   B HB3  1 
ATOM   4427 H HD21 . ASN   B 1 4   ? 43.683 -13.103 -15.309 1.00 17.11 ?  4   ASN   B HD21 1 
ATOM   4428 H HD22 . ASN   B 1 4   ? 43.536 -13.275 -16.781 1.00 17.11 ?  4   ASN   B HD22 1 
ATOM   4429 N N    . SER   B 1 5   ? 46.562 -17.963 -18.903 1.00 15.73 ?  5   SER   B N    1 
ATOM   4430 C CA   . SER   B 1 5   ? 46.653 -18.884 -20.036 1.00 17.43 ?  5   SER   B CA   1 
ATOM   4431 C C    . SER   B 1 5   ? 46.625 -20.316 -19.513 1.00 19.02 ?  5   SER   B C    1 
ATOM   4432 O O    . SER   B 1 5   ? 47.629 -21.020 -19.468 1.00 21.76 ?  5   SER   B O    1 
ATOM   4433 C CB   . SER   B 1 5   ? 47.915 -18.608 -20.850 1.00 19.10 ?  5   SER   B CB   1 
ATOM   4434 O OG   . SER   B 1 5   ? 49.092 -18.815 -20.083 1.00 21.98 ?  5   SER   B OG   1 
ATOM   4435 H H    . SER   B 1 5   ? 47.315 -17.810 -18.515 1.00 18.91 ?  5   SER   B H    1 
ATOM   4436 H HA   . SER   B 1 5   ? 45.880 -18.760 -20.610 1.00 20.95 ?  5   SER   B HA   1 
ATOM   4437 H HB2  . SER   B 1 5   ? 47.920 -19.206 -21.615 1.00 22.95 ?  5   SER   B HB2  1 
ATOM   4438 H HB3  . SER   B 1 5   ? 47.881 -17.689 -21.150 1.00 22.95 ?  5   SER   B HB3  1 
ATOM   4439 H HG   . SER   B 1 5   ? 49.128 -19.617 -19.842 1.00 26.41 ?  5   SER   B HG   1 
ATOM   4440 N N    . PHE   B 1 6   ? 45.439 -20.717 -19.076 1.00 19.42 ?  6   PHE   B N    1 
ATOM   4441 C CA   . PHE   B 1 6   ? 45.222 -22.062 -18.569 1.00 19.30 ?  6   PHE   B CA   1 
ATOM   4442 C C    . PHE   B 1 6   ? 45.120 -23.022 -19.742 1.00 22.68 ?  6   PHE   B C    1 
ATOM   4443 O O    . PHE   B 1 6   ? 44.441 -22.731 -20.732 1.00 25.04 ?  6   PHE   B O    1 
ATOM   4444 C CB   . PHE   B 1 6   ? 43.933 -22.102 -17.750 1.00 17.74 ?  6   PHE   B CB   1 
ATOM   4445 C CG   . PHE   B 1 6   ? 43.969 -21.242 -16.517 1.00 16.09 ?  6   PHE   B CG   1 
ATOM   4446 C CD1  . PHE   B 1 6   ? 44.471 -21.738 -15.329 1.00 14.98 ?  6   PHE   B CD1  1 
ATOM   4447 C CD2  . PHE   B 1 6   ? 43.491 -19.940 -16.545 1.00 15.64 ?  6   PHE   B CD2  1 
ATOM   4448 C CE1  . PHE   B 1 6   ? 44.496 -20.951 -14.189 1.00 14.50 ?  6   PHE   B CE1  1 
ATOM   4449 C CE2  . PHE   B 1 6   ? 43.519 -19.148 -15.411 1.00 15.78 ?  6   PHE   B CE2  1 
ATOM   4450 C CZ   . PHE   B 1 6   ? 44.021 -19.650 -14.235 1.00 14.66 ?  6   PHE   B CZ   1 
ATOM   4451 H H    . PHE   B 1 6   ? 44.733 -20.230 -19.073 1.00 23.34 ?  6   PHE   B H    1 
ATOM   4452 H HA   . PHE   B 1 6   ? 45.958 -22.335 -18.003 1.00 23.18 ?  6   PHE   B HA   1 
ATOM   4453 H HB2  . PHE   B 1 6   ? 43.195 -21.793 -18.302 1.00 21.32 ?  6   PHE   B HB2  1 
ATOM   4454 H HB3  . PHE   B 1 6   ? 43.762 -23.016 -17.465 1.00 21.32 ?  6   PHE   B HB3  1 
ATOM   4455 H HD1  . PHE   B 1 6   ? 44.794 -22.611 -15.293 1.00 18.00 ?  6   PHE   B HD1  1 
ATOM   4456 H HD2  . PHE   B 1 6   ? 43.145 -19.597 -17.335 1.00 18.80 ?  6   PHE   B HD2  1 
ATOM   4457 H HE1  . PHE   B 1 6   ? 44.842 -21.292 -13.394 1.00 17.43 ?  6   PHE   B HE1  1 
ATOM   4458 H HE2  . PHE   B 1 6   ? 43.191 -18.278 -15.444 1.00 18.96 ?  6   PHE   B HE2  1 
ATOM   4459 H HZ   . PHE   B 1 6   ? 44.039 -19.122 -13.471 1.00 17.62 ?  6   PHE   B HZ   1 
ATOM   4460 N N    . SER   B 1 7   ? 45.813 -24.154 -19.637 1.00 24.08 ?  7   SER   B N    1 
ATOM   4461 C CA   . SER   B 1 7   ? 45.855 -25.137 -20.708 1.00 26.86 ?  7   SER   B CA   1 
ATOM   4462 C C    . SER   B 1 7   ? 45.811 -26.538 -20.120 1.00 26.03 ?  7   SER   B C    1 
ATOM   4463 O O    . SER   B 1 7   ? 46.421 -26.811 -19.083 1.00 27.30 ?  7   SER   B O    1 
ATOM   4464 C CB   . SER   B 1 7   ? 47.124 -24.965 -21.555 1.00 29.80 ?  7   SER   B CB   1 
ATOM   4465 O OG   . SER   B 1 7   ? 47.072 -25.771 -22.719 1.00 32.04 ?  7   SER   B OG   1 
ATOM   4466 H H    . SER   B 1 7   ? 46.282 -24.373 -18.946 1.00 28.92 ?  7   SER   B H    1 
ATOM   4467 H HA   . SER   B 1 7   ? 45.088 -25.024 -21.284 1.00 32.25 ?  7   SER   B HA   1 
ATOM   4468 H HB2  . SER   B 1 7   ? 47.209 -24.031 -21.814 1.00 35.79 ?  7   SER   B HB2  1 
ATOM   4469 H HB3  . SER   B 1 7   ? 47.896 -25.231 -21.032 1.00 35.79 ?  7   SER   B HB3  1 
ATOM   4470 H HG   . SER   B 1 7   ? 47.765 -25.655 -23.181 1.00 38.48 ?  7   SER   B HG   1 
ATOM   4471 N N    . GLY   B 1 8   ? 45.078 -27.423 -20.791 1.00 25.88 ?  8   GLY   B N    1 
ATOM   4472 C CA   . GLY   B 1 8   ? 45.049 -28.814 -20.401 1.00 25.00 ?  8   GLY   B CA   1 
ATOM   4473 C C    . GLY   B 1 8   ? 44.108 -29.142 -19.272 1.00 23.59 ?  8   GLY   B C    1 
ATOM   4474 O O    . GLY   B 1 8   ? 44.248 -30.210 -18.661 1.00 25.20 ?  8   GLY   B O    1 
ATOM   4475 H H    . GLY   B 1 8   ? 44.597 -27.232 -21.472 1.00 31.08 ?  8   GLY   B H    1 
ATOM   4476 H HA2  . GLY   B 1 8   ? 44.784 -29.347 -21.164 1.00 30.03 ?  8   GLY   B HA2  1 
ATOM   4477 H HA3  . GLY   B 1 8   ? 45.937 -29.089 -20.132 1.00 30.03 ?  8   GLY   B HA3  1 
ATOM   4478 N N    . TYR   B 1 9   ? 43.127 -28.287 -18.995 1.00 21.57 ?  9   TYR   B N    1 
ATOM   4479 C CA   . TYR   B 1 9   ? 42.177 -28.554 -17.928 1.00 19.26 ?  9   TYR   B CA   1 
ATOM   4480 C C    . TYR   B 1 9   ? 40.988 -29.343 -18.441 1.00 18.58 ?  9   TYR   B C    1 
ATOM   4481 O O    . TYR   B 1 9   ? 40.554 -29.191 -19.586 1.00 20.41 ?  9   TYR   B O    1 
ATOM   4482 C CB   . TYR   B 1 9   ? 41.678 -27.259 -17.283 1.00 18.65 ?  9   TYR   B CB   1 
ATOM   4483 C CG   . TYR   B 1 9   ? 42.710 -26.637 -16.372 1.00 17.91 ?  9   TYR   B CG   1 
ATOM   4484 C CD1  . TYR   B 1 9   ? 43.797 -25.957 -16.897 1.00 18.13 ?  9   TYR   B CD1  1 
ATOM   4485 C CD2  . TYR   B 1 9   ? 42.613 -26.752 -14.994 1.00 16.78 ?  9   TYR   B CD2  1 
ATOM   4486 C CE1  . TYR   B 1 9   ? 44.759 -25.407 -16.075 1.00 18.29 ?  9   TYR   B CE1  1 
ATOM   4487 C CE2  . TYR   B 1 9   ? 43.569 -26.202 -14.162 1.00 17.20 ?  9   TYR   B CE2  1 
ATOM   4488 C CZ   . TYR   B 1 9   ? 44.644 -25.526 -14.709 1.00 17.98 ?  9   TYR   B CZ   1 
ATOM   4489 O OH   . TYR   B 1 9   ? 45.604 -24.985 -13.892 1.00 18.89 ?  9   TYR   B OH   1 
ATOM   4490 H H    . TYR   B 1 9   ? 42.962 -27.566 -19.435 1.00 25.91 ?  9   TYR   B H    1 
ATOM   4491 H HA   . TYR   B 1 9   ? 42.603 -29.083 -17.242 1.00 23.14 ?  9   TYR   B HA   1 
ATOM   4492 H HB2  . TYR   B 1 9   ? 41.446 -26.618 -17.976 1.00 22.41 ?  9   TYR   B HB2  1 
ATOM   4493 H HB3  . TYR   B 1 9   ? 40.897 -27.471 -16.751 1.00 22.41 ?  9   TYR   B HB3  1 
ATOM   4494 H HD1  . TYR   B 1 9   ? 43.877 -25.878 -17.824 1.00 21.79 ?  9   TYR   B HD1  1 
ATOM   4495 H HD2  . TYR   B 1 9   ? 41.885 -27.217 -14.629 1.00 20.17 ?  9   TYR   B HD2  1 
ATOM   4496 H HE1  . TYR   B 1 9   ? 45.475 -24.953 -16.447 1.00 21.97 ?  9   TYR   B HE1  1 
ATOM   4497 H HE2  . TYR   B 1 9   ? 43.478 -26.295 -13.244 1.00 20.66 ?  9   TYR   B HE2  1 
ATOM   4498 H HH   . TYR   B 1 9   ? 46.178 -24.608 -14.366 1.00 22.69 ?  9   TYR   B HH   1 
ATOM   4499 N N    . LEU   B 1 10  ? 40.470 -30.195 -17.566 1.00 17.11 ?  10  LEU   B N    1 
ATOM   4500 C CA   . LEU   B 1 10  ? 39.263 -30.956 -17.824 1.00 17.11 ?  10  LEU   B CA   1 
ATOM   4501 C C    . LEU   B 1 10  ? 38.083 -30.182 -17.252 1.00 16.83 ?  10  LEU   B C    1 
ATOM   4502 O O    . LEU   B 1 10  ? 38.116 -29.756 -16.093 1.00 16.47 ?  10  LEU   B O    1 
ATOM   4503 C CB   . LEU   B 1 10  ? 39.372 -32.321 -17.144 1.00 17.99 ?  10  LEU   B CB   1 
ATOM   4504 C CG   . LEU   B 1 10  ? 38.236 -33.289 -17.458 1.00 19.66 ?  10  LEU   B CG   1 
ATOM   4505 C CD1  . LEU   B 1 10  ? 38.393 -33.852 -18.864 1.00 20.68 ?  10  LEU   B CD1  1 
ATOM   4506 C CD2  . LEU   B 1 10  ? 38.152 -34.406 -16.430 1.00 20.64 ?  10  LEU   B CD2  1 
ATOM   4507 H H    . LEU   B 1 10  ? 40.796 -30.347 -16.784 1.00 20.56 ?  10  LEU   B H    1 
ATOM   4508 H HA   . LEU   B 1 10  ? 39.130 -31.082 -18.775 1.00 20.56 ?  10  LEU   B HA   1 
ATOM   4509 H HB2  . LEU   B 1 10  ? 40.201 -32.738 -17.429 1.00 21.62 ?  10  LEU   B HB2  1 
ATOM   4510 H HB3  . LEU   B 1 10  ? 39.389 -32.190 -16.182 1.00 21.62 ?  10  LEU   B HB3  1 
ATOM   4511 H HG   . LEU   B 1 10  ? 37.397 -32.805 -17.430 1.00 23.62 ?  10  LEU   B HG   1 
ATOM   4512 H HD11 . LEU   B 1 10  ? 37.679 -34.485 -19.031 1.00 24.84 ?  10  LEU   B HD11 1 
ATOM   4513 H HD12 . LEU   B 1 10  ? 38.345 -33.121 -19.501 1.00 24.84 ?  10  LEU   B HD12 1 
ATOM   4514 H HD13 . LEU   B 1 10  ? 39.253 -34.294 -18.931 1.00 24.84 ?  10  LEU   B HD13 1 
ATOM   4515 H HD21 . LEU   B 1 10  ? 37.421 -34.995 -16.668 1.00 24.79 ?  10  LEU   B HD21 1 
ATOM   4516 H HD22 . LEU   B 1 10  ? 38.988 -34.892 -16.427 1.00 24.79 ?  10  LEU   B HD22 1 
ATOM   4517 H HD23 . LEU   B 1 10  ? 37.990 -34.013 -15.557 1.00 24.79 ?  10  LEU   B HD23 1 
ATOM   4518 N N    . LYS   B 1 11  ? 37.050 -30.005 -18.067 1.00 18.13 ?  11  LYS   B N    1 
ATOM   4519 C CA   . LYS   B 1 11  ? 35.858 -29.282 -17.650 1.00 20.58 ?  11  LYS   B CA   1 
ATOM   4520 C C    . LYS   B 1 11  ? 34.990 -30.201 -16.799 1.00 19.70 ?  11  LYS   B C    1 
ATOM   4521 O O    . LYS   B 1 11  ? 34.617 -31.294 -17.239 1.00 21.53 ?  11  LYS   B O    1 
ATOM   4522 C CB   . LYS   B 1 11  ? 35.104 -28.823 -18.897 1.00 24.98 ?  11  LYS   B CB   1 
ATOM   4523 C CG   . LYS   B 1 11  ? 33.983 -27.835 -18.653 1.00 28.73 ?  11  LYS   B CG   1 
ATOM   4524 C CD   . LYS   B 1 11  ? 33.252 -27.532 -19.956 1.00 31.75 ?  11  LYS   B CD   1 
ATOM   4525 C CE   . LYS   B 1 11  ? 32.237 -26.415 -19.786 1.00 33.97 ?  11  LYS   B CE   1 
ATOM   4526 N NZ   . LYS   B 1 11  ? 32.891 -25.094 -19.585 1.00 35.21 ?  11  LYS   B NZ   1 
ATOM   4527 H H    . LYS   B 1 11  ? 37.001 -30.310 -18.874 1.00 21.78 ?  11  LYS   B H    1 
ATOM   4528 H HA   . LYS   B 1 11  ? 36.102 -28.505 -17.128 1.00 24.72 ?  11  LYS   B HA   1 
ATOM   4529 H HB2  . LYS   B 1 11  ? 35.735 -28.396 -19.500 1.00 30.01 ?  11  LYS   B HB2  1 
ATOM   4530 H HB3  . LYS   B 1 11  ? 34.715 -29.597 -19.333 1.00 30.01 ?  11  LYS   B HB3  1 
ATOM   4531 H HG2  . LYS   B 1 11  ? 33.347 -28.215 -18.028 1.00 34.50 ?  11  LYS   B HG2  1 
ATOM   4532 H HG3  . LYS   B 1 11  ? 34.349 -27.007 -18.308 1.00 34.50 ?  11  LYS   B HG3  1 
ATOM   4533 H HD2  . LYS   B 1 11  ? 33.897 -27.257 -20.627 1.00 38.12 ?  11  LYS   B HD2  1 
ATOM   4534 H HD3  . LYS   B 1 11  ? 32.783 -28.329 -20.250 1.00 38.12 ?  11  LYS   B HD3  1 
ATOM   4535 H HE2  . LYS   B 1 11  ? 31.686 -26.363 -20.582 1.00 40.79 ?  11  LYS   B HE2  1 
ATOM   4536 H HE3  . LYS   B 1 11  ? 31.687 -26.604 -19.010 1.00 40.79 ?  11  LYS   B HE3  1 
ATOM   4537 H HZ1  . LYS   B 1 11  ? 32.273 -24.460 -19.496 1.00 42.27 ?  11  LYS   B HZ1  1 
ATOM   4538 H HZ2  . LYS   B 1 11  ? 33.396 -25.112 -18.853 1.00 42.27 ?  11  LYS   B HZ2  1 
ATOM   4539 H HZ3  . LYS   B 1 11  ? 33.405 -24.900 -20.286 1.00 42.27 ?  11  LYS   B HZ3  1 
ATOM   4540 N N    . LEU   B 1 12  ? 34.671 -29.768 -15.580 1.00 17.81 ?  12  LEU   B N    1 
ATOM   4541 C CA   . LEU   B 1 12  ? 33.714 -30.477 -14.736 1.00 16.94 ?  12  LEU   B CA   1 
ATOM   4542 C C    . LEU   B 1 12  ? 32.325 -29.865 -14.819 1.00 16.70 ?  12  LEU   B C    1 
ATOM   4543 O O    . LEU   B 1 12  ? 31.335 -30.581 -14.982 1.00 17.31 ?  12  LEU   B O    1 
ATOM   4544 C CB   . LEU   B 1 12  ? 34.184 -30.500 -13.276 1.00 16.53 ?  12  LEU   B CB   1 
ATOM   4545 C CG   . LEU   B 1 12  ? 35.530 -31.176 -13.027 1.00 16.32 ?  12  LEU   B CG   1 
ATOM   4546 C CD1  . LEU   B 1 12  ? 35.899 -31.134 -11.553 1.00 16.67 ?  12  LEU   B CD1  1 
ATOM   4547 C CD2  . LEU   B 1 12  ? 35.507 -32.610 -13.534 1.00 16.75 ?  12  LEU   B CD2  1 
ATOM   4548 H H    . LEU   B 1 12  ? 34.992 -29.059 -15.219 1.00 21.40 ?  12  LEU   B H    1 
ATOM   4549 H HA   . LEU   B 1 12  ? 33.638 -31.392 -15.042 1.00 20.36 ?  12  LEU   B HA   1 
ATOM   4550 H HB2  . LEU   B 1 12  ? 34.248 -29.591 -12.958 1.00 19.86 ?  12  LEU   B HB2  1 
ATOM   4551 H HB3  . LEU   B 1 12  ? 33.517 -30.981 -12.750 1.00 19.86 ?  12  LEU   B HB3  1 
ATOM   4552 H HG   . LEU   B 1 12  ? 36.212 -30.698 -13.521 1.00 19.61 ?  12  LEU   B HG   1 
ATOM   4553 H HD11 . LEU   B 1 12  ? 36.762 -31.567 -11.430 1.00 20.03 ?  12  LEU   B HD11 1 
ATOM   4554 H HD12 . LEU   B 1 12  ? 35.953 -30.210 -11.264 1.00 20.03 ?  12  LEU   B HD12 1 
ATOM   4555 H HD13 . LEU   B 1 12  ? 35.223 -31.603 -11.039 1.00 20.03 ?  12  LEU   B HD13 1 
ATOM   4556 H HD21 . LEU   B 1 12  ? 36.297 -33.072 -13.221 1.00 20.13 ?  12  LEU   B HD21 1 
ATOM   4557 H HD22 . LEU   B 1 12  ? 34.709 -33.053 -13.196 1.00 20.13 ?  12  LEU   B HD22 1 
ATOM   4558 H HD23 . LEU   B 1 12  ? 35.488 -32.604 -14.506 1.00 20.13 ?  12  LEU   B HD23 1 
ATOM   4559 N N    . THR   B 1 13  ? 32.245 -28.547 -14.717 1.00 16.71 ?  13  THR   B N    1 
ATOM   4560 C CA   . THR   B 1 13  ? 31.021 -27.797 -14.911 1.00 16.30 ?  13  THR   B CA   1 
ATOM   4561 C C    . THR   B 1 13  ? 31.353 -26.602 -15.796 1.00 17.67 ?  13  THR   B C    1 
ATOM   4562 O O    . THR   B 1 13  ? 32.500 -26.405 -16.217 1.00 19.01 ?  13  THR   B O    1 
ATOM   4563 C CB   . THR   B 1 13  ? 30.438 -27.320 -13.576 1.00 16.20 ?  13  THR   B CB   1 
ATOM   4564 O OG1  . THR   B 1 13  ? 31.293 -26.299 -13.040 1.00 16.10 ?  13  THR   B OG1  1 
ATOM   4565 C CG2  . THR   B 1 13  ? 30.314 -28.469 -12.582 1.00 16.90 ?  13  THR   B CG2  1 
ATOM   4566 H H    . THR   B 1 13  ? 32.913 -28.045 -14.526 1.00 20.08 ?  13  THR   B H    1 
ATOM   4567 H HA   . THR   B 1 13  ? 30.357 -28.355 -15.355 1.00 19.59 ?  13  THR   B HA   1 
ATOM   4568 H HB   . THR   B 1 13  ? 29.547 -26.951 -13.725 1.00 19.47 ?  13  THR   B HB   1 
ATOM   4569 H HG1  . THR   B 1 13  ? 31.010 -25.540 -13.281 1.00 19.35 ?  13  THR   B HG1  1 
ATOM   4570 H HG21 . THR   B 1 13  ? 29.823 -28.179 -11.796 1.00 20.31 ?  13  THR   B HG21 1 
ATOM   4571 H HG22 . THR   B 1 13  ? 29.841 -29.212 -12.990 1.00 20.31 ?  13  THR   B HG22 1 
ATOM   4572 H HG23 . THR   B 1 13  ? 31.195 -28.767 -12.310 1.00 20.31 ?  13  THR   B HG23 1 
ATOM   4573 N N    . ASP   B 1 14  ? 30.345 -25.776 -16.064 1.00 19.49 ?  14  ASP   B N    1 
ATOM   4574 C CA   . ASP   B 1 14  ? 30.574 -24.619 -16.916 1.00 21.29 ?  14  ASP   B CA   1 
ATOM   4575 C C    . ASP   B 1 14  ? 31.644 -23.685 -16.365 1.00 19.22 ?  14  ASP   B C    1 
ATOM   4576 O O    . ASP   B 1 14  ? 32.229 -22.925 -17.143 1.00 20.74 ?  14  ASP   B O    1 
ATOM   4577 C CB   . ASP   B 1 14  ? 29.275 -23.848 -17.142 1.00 25.68 ?  14  ASP   B CB   1 
ATOM   4578 C CG   . ASP   B 1 14  ? 28.338 -24.549 -18.105 1.00 29.97 ?  14  ASP   B CG   1 
ATOM   4579 O OD1  . ASP   B 1 14  ? 28.789 -25.443 -18.854 1.00 30.83 ?  14  ASP   B OD1  1 
ATOM   4580 O OD2  . ASP   B 1 14  ? 27.140 -24.203 -18.113 1.00 31.70 -1 14  ASP   B OD2  1 
ATOM   4581 H H    . ASP   B 1 14  ? 29.542 -25.857 -15.768 1.00 23.41 ?  14  ASP   B H    1 
ATOM   4582 H HA   . ASP   B 1 14  ? 30.886 -24.923 -17.780 1.00 25.58 ?  14  ASP   B HA   1 
ATOM   4583 H HB2  . ASP   B 1 14  ? 28.804 -23.763 -16.302 1.00 30.84 ?  14  ASP   B HB2  1 
ATOM   4584 H HB3  . ASP   B 1 14  ? 29.484 -22.969 -17.499 1.00 30.84 ?  14  ASP   B HB3  1 
ATOM   4585 N N    . ASN   B 1 15  ? 31.915 -23.715 -15.051 1.00 16.44 ?  15  ASN   B N    1 
ATOM   4586 C CA   . ASN   B 1 15  ? 32.879 -22.790 -14.461 1.00 14.72 ?  15  ASN   B CA   1 
ATOM   4587 C C    . ASN   B 1 15  ? 33.973 -23.446 -13.626 1.00 13.43 ?  15  ASN   B C    1 
ATOM   4588 O O    . ASN   B 1 15  ? 34.833 -22.725 -13.100 1.00 13.55 ?  15  ASN   B O    1 
ATOM   4589 C CB   . ASN   B 1 15  ? 32.176 -21.730 -13.597 1.00 14.30 ?  15  ASN   B CB   1 
ATOM   4590 C CG   . ASN   B 1 15  ? 31.546 -22.326 -12.355 1.00 14.37 ?  15  ASN   B CG   1 
ATOM   4591 O OD1  . ASN   B 1 15  ? 30.597 -23.115 -12.443 1.00 16.43 ?  15  ASN   B OD1  1 
ATOM   4592 N ND2  . ASN   B 1 15  ? 32.083 -21.993 -11.195 1.00 13.56 ?  15  ASN   B ND2  1 
ATOM   4593 H H    . ASN   B 1 15  ? 31.533 -24.245 -14.484 1.00 19.76 ?  15  ASN   B H    1 
ATOM   4594 H HA   . ASN   B 1 15  ? 33.314 -22.315 -15.178 1.00 17.69 ?  15  ASN   B HA   1 
ATOM   4595 H HB2  . ASN   B 1 15  ? 32.830 -21.062 -13.318 1.00 17.19 ?  15  ASN   B HB2  1 
ATOM   4596 H HB3  . ASN   B 1 15  ? 31.475 -21.297 -14.117 1.00 17.19 ?  15  ASN   B HB3  1 
ATOM   4597 H HD21 . ASN   B 1 15  ? 31.758 -22.304 -10.461 1.00 16.30 ?  15  ASN   B HD21 1 
ATOM   4598 H HD22 . ASN   B 1 15  ? 32.754 -21.448 -11.162 1.00 16.30 ?  15  ASN   B HD22 1 
ATOM   4599 N N    . VAL   B 1 16  ? 33.969 -24.768 -13.473 1.00 13.38 ?  16  VAL   B N    1 
ATOM   4600 C CA   . VAL   B 1 16  ? 34.965 -25.465 -12.666 1.00 12.73 ?  16  VAL   B CA   1 
ATOM   4601 C C    . VAL   B 1 16  ? 35.755 -26.402 -13.564 1.00 13.30 ?  16  VAL   B C    1 
ATOM   4602 O O    . VAL   B 1 16  ? 35.178 -27.278 -14.225 1.00 14.22 ?  16  VAL   B O    1 
ATOM   4603 C CB   . VAL   B 1 16  ? 34.341 -26.228 -11.488 1.00 13.28 ?  16  VAL   B CB   1 
ATOM   4604 C CG1  . VAL   B 1 16  ? 35.423 -26.958 -10.695 1.00 13.56 ?  16  VAL   B CG1  1 
ATOM   4605 C CG2  . VAL   B 1 16  ? 33.546 -25.279 -10.601 1.00 13.95 ?  16  VAL   B CG2  1 
ATOM   4606 H H    . VAL   B 1 16  ? 33.377 -25.291 -13.826 1.00 16.08 ?  16  VAL   B H    1 
ATOM   4607 H HA   . VAL   B 1 16  ? 35.578 -24.811 -12.300 1.00 15.30 ?  16  VAL   B HA   1 
ATOM   4608 H HB   . VAL   B 1 16  ? 33.723 -26.895 -11.835 1.00 15.97 ?  16  VAL   B HB   1 
ATOM   4609 H HG11 . VAL   B 1 16  ? 35.045 -27.252 -9.851  1.00 16.30 ?  16  VAL   B HG11 1 
ATOM   4610 H HG12 . VAL   B 1 16  ? 35.732 -27.717 -11.204 1.00 16.30 ?  16  VAL   B HG12 1 
ATOM   4611 H HG13 . VAL   B 1 16  ? 36.154 -26.340 -10.529 1.00 16.30 ?  16  VAL   B HG13 1 
ATOM   4612 H HG21 . VAL   B 1 16  ? 33.210 -25.770 -9.834  1.00 16.76 ?  16  VAL   B HG21 1 
ATOM   4613 H HG22 . VAL   B 1 16  ? 34.125 -24.562 -10.309 1.00 16.76 ?  16  VAL   B HG22 1 
ATOM   4614 H HG23 . VAL   B 1 16  ? 32.801 -24.918 -11.111 1.00 16.76 ?  16  VAL   B HG23 1 
ATOM   4615 N N    . TYR   B 1 17  ? 37.077 -26.239 -13.545 1.00 13.27 ?  17  TYR   B N    1 
ATOM   4616 C CA   . TYR   B 1 17  ? 38.018 -26.984 -14.364 1.00 14.12 ?  17  TYR   B CA   1 
ATOM   4617 C C    . TYR   B 1 17  ? 39.069 -27.599 -13.451 1.00 13.22 ?  17  TYR   B C    1 
ATOM   4618 O O    . TYR   B 1 17  ? 39.357 -27.066 -12.376 1.00 13.34 ?  17  TYR   B O    1 
ATOM   4619 C CB   . TYR   B 1 17  ? 38.736 -26.046 -15.344 1.00 17.04 ?  17  TYR   B CB   1 
ATOM   4620 C CG   . TYR   B 1 17  ? 37.819 -25.276 -16.261 1.00 19.79 ?  17  TYR   B CG   1 
ATOM   4621 C CD1  . TYR   B 1 17  ? 37.255 -24.071 -15.864 1.00 21.47 ?  17  TYR   B CD1  1 
ATOM   4622 C CD2  . TYR   B 1 17  ? 37.519 -25.754 -17.528 1.00 21.84 ?  17  TYR   B CD2  1 
ATOM   4623 C CE1  . TYR   B 1 17  ? 36.416 -23.360 -16.704 1.00 23.12 ?  17  TYR   B CE1  1 
ATOM   4624 C CE2  . TYR   B 1 17  ? 36.682 -25.051 -18.378 1.00 23.45 ?  17  TYR   B CE2  1 
ATOM   4625 C CZ   . TYR   B 1 17  ? 36.131 -23.856 -17.959 1.00 24.27 ?  17  TYR   B CZ   1 
ATOM   4626 O OH   . TYR   B 1 17  ? 35.299 -23.153 -18.798 1.00 25.74 ?  17  TYR   B OH   1 
ATOM   4627 H H    . TYR   B 1 17  ? 37.470 -25.666 -13.032 1.00 15.95 ?  17  TYR   B H    1 
ATOM   4628 H HA   . TYR   B 1 17  ? 37.559 -27.684 -14.857 1.00 16.97 ?  17  TYR   B HA   1 
ATOM   4629 H HB2  . TYR   B 1 17  ? 39.263 -25.407 -14.842 1.00 20.47 ?  17  TYR   B HB2  1 
ATOM   4630 H HB3  . TYR   B 1 17  ? 39.314 -26.580 -15.904 1.00 20.47 ?  17  TYR   B HB3  1 
ATOM   4631 H HD1  . TYR   B 1 17  ? 37.448 -23.735 -15.020 1.00 25.80 ?  17  TYR   B HD1  1 
ATOM   4632 H HD2  . TYR   B 1 17  ? 37.883 -26.559 -17.816 1.00 26.24 ?  17  TYR   B HD2  1 
ATOM   4633 H HE1  . TYR   B 1 17  ? 36.047 -22.554 -16.425 1.00 27.78 ?  17  TYR   B HE1  1 
ATOM   4634 H HE2  . TYR   B 1 17  ? 36.484 -25.384 -19.226 1.00 28.17 ?  17  TYR   B HE2  1 
ATOM   4635 H HH   . TYR   B 1 17  ? 35.208 -23.562 -19.525 1.00 30.92 ?  17  TYR   B HH   1 
ATOM   4636 N N    . ILE   B 1 18  ? 39.673 -28.705 -13.885 1.00 13.20 ?  18  ILE   B N    1 
ATOM   4637 C CA   . ILE   B 1 18  ? 40.602 -29.431 -13.025 1.00 13.41 ?  18  ILE   B CA   1 
ATOM   4638 C C    . ILE   B 1 18  ? 41.761 -29.991 -13.842 1.00 13.84 ?  18  ILE   B C    1 
ATOM   4639 O O    . ILE   B 1 18  ? 41.598 -30.405 -14.995 1.00 14.75 ?  18  ILE   B O    1 
ATOM   4640 C CB   . ILE   B 1 18  ? 39.851 -30.534 -12.239 1.00 13.75 ?  18  ILE   B CB   1 
ATOM   4641 C CG1  . ILE   B 1 18  ? 40.699 -31.068 -11.083 1.00 14.26 ?  18  ILE   B CG1  1 
ATOM   4642 C CG2  . ILE   B 1 18  ? 39.374 -31.650 -13.182 1.00 14.35 ?  18  ILE   B CG2  1 
ATOM   4643 C CD1  . ILE   B 1 18  ? 39.898 -31.884 -10.092 1.00 15.96 ?  18  ILE   B CD1  1 
ATOM   4644 H H    . ILE   B 1 18  ? 39.566 -29.053 -14.665 1.00 15.87 ?  18  ILE   B H    1 
ATOM   4645 H HA   . ILE   B 1 18  ? 40.959 -28.823 -12.364 1.00 16.12 ?  18  ILE   B HA   1 
ATOM   4646 H HB   . ILE   B 1 18  ? 39.050 -30.141 -11.855 1.00 16.52 ?  18  ILE   B HB   1 
ATOM   4647 H HG12 . ILE   B 1 18  ? 41.400 -31.627 -11.436 1.00 17.14 ?  18  ILE   B HG12 1 
ATOM   4648 H HG13 . ILE   B 1 18  ? 41.075 -30.311 -10.607 1.00 17.14 ?  18  ILE   B HG13 1 
ATOM   4649 H HG21 . ILE   B 1 18  ? 38.763 -32.235 -12.703 1.00 17.25 ?  18  ILE   B HG21 1 
ATOM   4650 H HG22 . ILE   B 1 18  ? 38.918 -31.250 -13.939 1.00 17.25 ?  18  ILE   B HG22 1 
ATOM   4651 H HG23 . ILE   B 1 18  ? 40.141 -32.157 -13.488 1.00 17.25 ?  18  ILE   B HG23 1 
ATOM   4652 H HD11 . ILE   B 1 18  ? 40.478 -32.159 -9.367  1.00 19.18 ?  18  ILE   B HD11 1 
ATOM   4653 H HD12 . ILE   B 1 18  ? 39.169 -31.342 -9.746  1.00 19.18 ?  18  ILE   B HD12 1 
ATOM   4654 H HD13 . ILE   B 1 18  ? 39.538 -32.666 -10.543 1.00 19.18 ?  18  ILE   B HD13 1 
ATOM   4655 N N    . LYS   B 1 19  ? 42.943 -30.021 -13.226 1.00 14.06 ?  19  LYS   B N    1 
ATOM   4656 C CA   . LYS   B 1 19  ? 44.143 -30.504 -13.893 1.00 15.10 ?  19  LYS   B CA   1 
ATOM   4657 C C    . LYS   B 1 19  ? 45.048 -31.180 -12.875 1.00 14.87 ?  19  LYS   B C    1 
ATOM   4658 O O    . LYS   B 1 19  ? 45.142 -30.735 -11.728 1.00 14.65 ?  19  LYS   B O    1 
ATOM   4659 C CB   . LYS   B 1 19  ? 44.899 -29.345 -14.555 1.00 16.06 ?  19  LYS   B CB   1 
ATOM   4660 C CG   . LYS   B 1 19  ? 46.127 -29.758 -15.345 1.00 18.06 ?  19  LYS   B CG   1 
ATOM   4661 C CD   . LYS   B 1 19  ? 46.822 -28.527 -15.901 1.00 20.00 ?  19  LYS   B CD   1 
ATOM   4662 C CE   . LYS   B 1 19  ? 47.984 -28.882 -16.806 1.00 21.96 ?  19  LYS   B CE   1 
ATOM   4663 N NZ   . LYS   B 1 19  ? 48.632 -27.657 -17.342 1.00 22.72 ?  19  LYS   B NZ   1 
ATOM   4664 H H    . LYS   B 1 19  ? 43.067 -29.758 -12.414 1.00 16.89 ?  19  LYS   B H    1 
ATOM   4665 H HA   . LYS   B 1 19  ? 43.892 -31.150 -14.573 1.00 18.15 ?  19  LYS   B HA   1 
ATOM   4666 H HB2  . LYS   B 1 19  ? 44.290 -28.896 -15.164 1.00 19.30 ?  19  LYS   B HB2  1 
ATOM   4667 H HB3  . LYS   B 1 19  ? 45.177 -28.728 -13.859 1.00 19.30 ?  19  LYS   B HB3  1 
ATOM   4668 H HG2  . LYS   B 1 19  ? 46.739 -30.228 -14.760 1.00 21.70 ?  19  LYS   B HG2  1 
ATOM   4669 H HG3  . LYS   B 1 19  ? 45.853 -30.326 -16.082 1.00 21.70 ?  19  LYS   B HG3  1 
ATOM   4670 H HD2  . LYS   B 1 19  ? 46.183 -28.006 -16.415 1.00 24.03 ?  19  LYS   B HD2  1 
ATOM   4671 H HD3  . LYS   B 1 19  ? 47.163 -27.996 -15.162 1.00 24.03 ?  19  LYS   B HD3  1 
ATOM   4672 H HE2  . LYS   B 1 19  ? 48.641 -29.386 -16.299 1.00 26.37 ?  19  LYS   B HE2  1 
ATOM   4673 H HE3  . LYS   B 1 19  ? 47.656 -29.413 -17.551 1.00 26.37 ?  19  LYS   B HE3  1 
ATOM   4674 H HZ1  . LYS   B 1 19  ? 49.295 -27.881 -17.891 1.00 27.29 ?  19  LYS   B HZ1  1 
ATOM   4675 H HZ2  . LYS   B 1 19  ? 48.036 -27.171 -17.791 1.00 27.29 ?  19  LYS   B HZ2  1 
ATOM   4676 H HZ3  . LYS   B 1 19  ? 48.959 -27.170 -16.674 1.00 27.29 ?  19  LYS   B HZ3  1 
ATOM   4677 N N    . ASN   B 1 20  ? 45.733 -32.238 -13.308 1.00 15.76 ?  20  ASN   B N    1 
ATOM   4678 C CA   . ASN   B 1 20  ? 46.775 -32.865 -12.499 1.00 16.77 ?  20  ASN   B CA   1 
ATOM   4679 C C    . ASN   B 1 20  ? 48.049 -32.046 -12.683 1.00 17.13 ?  20  ASN   B C    1 
ATOM   4680 O O    . ASN   B 1 20  ? 48.678 -32.096 -13.748 1.00 18.93 ?  20  ASN   B O    1 
ATOM   4681 C CB   . ASN   B 1 20  ? 46.958 -34.318 -12.939 1.00 18.35 ?  20  ASN   B CB   1 
ATOM   4682 C CG   . ASN   B 1 20  ? 48.127 -35.016 -12.253 1.00 19.70 ?  20  ASN   B CG   1 
ATOM   4683 O OD1  . ASN   B 1 20  ? 48.823 -35.832 -12.871 1.00 21.71 ?  20  ASN   B OD1  1 
ATOM   4684 N ND2  . ASN   B 1 20  ? 48.342 -34.713 -10.978 1.00 19.42 ?  20  ASN   B ND2  1 
ATOM   4685 H H    . ASN   B 1 20  ? 45.611 -32.608 -14.074 1.00 18.94 ?  20  ASN   B H    1 
ATOM   4686 H HA   . ASN   B 1 20  ? 46.507 -32.854 -11.563 1.00 20.16 ?  20  ASN   B HA   1 
ATOM   4687 H HB2  . ASN   B 1 20  ? 46.149 -34.817 -12.730 1.00 22.04 ?  20  ASN   B HB2  1 
ATOM   4688 H HB3  . ASN   B 1 20  ? 47.114 -34.335 -13.896 1.00 22.04 ?  20  ASN   B HB3  1 
ATOM   4689 H HD21 . ASN   B 1 20  ? 48.992 -35.073 -10.552 1.00 23.33 ?  20  ASN   B HD21 1 
ATOM   4690 H HD22 . ASN   B 1 20  ? 47.829 -34.144 -10.572 1.00 23.33 ?  20  ASN   B HD22 1 
ATOM   4691 N N    . ALA   B 1 21  ? 48.423 -31.271 -11.664 1.00 16.53 ?  21  ALA   B N    1 
ATOM   4692 C CA   . ALA   B 1 21  ? 49.533 -30.345 -11.822 1.00 16.95 ?  21  ALA   B CA   1 
ATOM   4693 C C    . ALA   B 1 21  ? 49.990 -29.846 -10.460 1.00 15.92 ?  21  ALA   B C    1 
ATOM   4694 O O    . ALA   B 1 21  ? 49.242 -29.873 -9.476  1.00 15.54 ?  21  ALA   B O    1 
ATOM   4695 C CB   . ALA   B 1 21  ? 49.133 -29.175 -12.714 1.00 18.67 ?  21  ALA   B CB   1 
ATOM   4696 H H    . ALA   B 1 21  ? 48.052 -31.270 -10.883 1.00 19.86 ?  21  ALA   B H    1 
ATOM   4697 H HA   . ALA   B 1 21  ? 50.274 -30.818 -12.236 1.00 20.37 ?  21  ALA   B HA   1 
ATOM   4698 H HB1  . ALA   B 1 21  ? 49.922 -28.645 -12.881 1.00 22.43 ?  21  ALA   B HB1  1 
ATOM   4699 H HB2  . ALA   B 1 21  ? 48.786 -29.530 -13.546 1.00 22.43 ?  21  ALA   B HB2  1 
ATOM   4700 H HB3  . ALA   B 1 21  ? 48.457 -28.657 -12.261 1.00 22.43 ?  21  ALA   B HB3  1 
ATOM   4701 N N    . ASP   B 1 22  ? 51.244 -29.390 -10.440 1.00 15.44 ?  22  ASP   B N    1 
ATOM   4702 C CA   . ASP   B 1 22  ? 51.868 -28.704 -9.312  1.00 14.65 ?  22  ASP   B CA   1 
ATOM   4703 C C    . ASP   B 1 22  ? 51.469 -27.233 -9.384  1.00 13.19 ?  22  ASP   B C    1 
ATOM   4704 O O    . ASP   B 1 22  ? 51.770 -26.558 -10.374 1.00 13.70 ?  22  ASP   B O    1 
ATOM   4705 C CB   . ASP   B 1 22  ? 53.385 -28.885 -9.469  1.00 16.07 ?  22  ASP   B CB   1 
ATOM   4706 C CG   . ASP   B 1 22  ? 54.216 -28.141 -8.426  1.00 17.54 ?  22  ASP   B CG   1 
ATOM   4707 O OD1  . ASP   B 1 22  ? 53.864 -27.016 -8.038  1.00 17.53 ?  22  ASP   B OD1  1 
ATOM   4708 O OD2  . ASP   B 1 22  ? 55.268 -28.688 -8.023  1.00 20.10 -1 22  ASP   B OD2  1 
ATOM   4709 H H    . ASP   B 1 22  ? 51.778 -29.462 -11.115 1.00 18.55 ?  22  ASP   B H    1 
ATOM   4710 H HA   . ASP   B 1 22  ? 51.575 -29.092 -8.471  1.00 17.61 ?  22  ASP   B HA   1 
ATOM   4711 H HB2  . ASP   B 1 22  ? 53.597 -29.824 -9.401  1.00 19.31 ?  22  ASP   B HB2  1 
ATOM   4712 H HB3  . ASP   B 1 22  ? 53.647 -28.545 -10.339 1.00 19.31 ?  22  ASP   B HB3  1 
ATOM   4713 N N    . ILE   B 1 23  ? 50.763 -26.743 -8.356  1.00 12.91 ?  23  ILE   B N    1 
ATOM   4714 C CA   . ILE   B 1 23  ? 50.174 -25.403 -8.422  1.00 12.21 ?  23  ILE   B CA   1 
ATOM   4715 C C    . ILE   B 1 23  ? 51.234 -24.315 -8.566  1.00 12.04 ?  23  ILE   B C    1 
ATOM   4716 O O    . ILE   B 1 23  ? 50.973 -23.277 -9.179  1.00 11.66 ?  23  ILE   B O    1 
ATOM   4717 C CB   . ILE   B 1 23  ? 49.234 -25.154 -7.223  1.00 12.37 ?  23  ILE   B CB   1 
ATOM   4718 C CG1  . ILE   B 1 23  ? 48.404 -23.883 -7.430  1.00 12.86 ?  23  ILE   B CG1  1 
ATOM   4719 C CG2  . ILE   B 1 23  ? 50.008 -25.119 -5.912  1.00 13.28 ?  23  ILE   B CG2  1 
ATOM   4720 C CD1  . ILE   B 1 23  ? 47.292 -23.709 -6.401  1.00 13.72 ?  23  ILE   B CD1  1 
ATOM   4721 H H    . ILE   B 1 23  ? 50.608 -27.169 -7.620  1.00 15.52 ?  23  ILE   B H    1 
ATOM   4722 H HA   . ILE   B 1 23  ? 49.626 -25.365 -9.216  1.00 14.67 ?  23  ILE   B HA   1 
ATOM   4723 H HB   . ILE   B 1 23  ? 48.615 -25.902 -7.179  1.00 14.88 ?  23  ILE   B HB   1 
ATOM   4724 H HG12 . ILE   B 1 23  ? 48.990 -23.110 -7.372  1.00 15.45 ?  23  ILE   B HG12 1 
ATOM   4725 H HG13 . ILE   B 1 23  ? 47.993 -23.913 -8.312  1.00 15.45 ?  23  ILE   B HG13 1 
ATOM   4726 H HG21 . ILE   B 1 23  ? 49.376 -25.112 -5.177  1.00 15.96 ?  23  ILE   B HG21 1 
ATOM   4727 H HG22 . ILE   B 1 23  ? 50.568 -25.909 -5.859  1.00 15.96 ?  23  ILE   B HG22 1 
ATOM   4728 H HG23 . ILE   B 1 23  ? 50.553 -24.321 -5.892  1.00 15.96 ?  23  ILE   B HG23 1 
ATOM   4729 H HD11 . ILE   B 1 23  ? 46.760 -22.933 -6.637  1.00 16.49 ?  23  ILE   B HD11 1 
ATOM   4730 H HD12 . ILE   B 1 23  ? 46.738 -24.504 -6.401  1.00 16.49 ?  23  ILE   B HD12 1 
ATOM   4731 H HD13 . ILE   B 1 23  ? 47.691 -23.584 -5.526  1.00 16.49 ?  23  ILE   B HD13 1 
ATOM   4732 N N    . VAL   B 1 24  ? 52.429 -24.521 -8.007  1.00 12.16 ?  24  VAL   B N    1 
ATOM   4733 C CA   . VAL   B 1 24  ? 53.509 -23.545 -8.174  1.00 12.66 ?  24  VAL   B CA   1 
ATOM   4734 C C    . VAL   B 1 24  ? 53.967 -23.500 -9.625  1.00 12.78 ?  24  VAL   B C    1 
ATOM   4735 O O    . VAL   B 1 24  ? 54.096 -22.425 -10.223 1.00 13.42 ?  24  VAL   B O    1 
ATOM   4736 C CB   . VAL   B 1 24  ? 54.685 -23.857 -7.227  1.00 13.50 ?  24  VAL   B CB   1 
ATOM   4737 C CG1  . VAL   B 1 24  ? 55.897 -22.975 -7.552  1.00 14.42 ?  24  VAL   B CG1  1 
ATOM   4738 C CG2  . VAL   B 1 24  ? 54.261 -23.688 -5.786  1.00 14.96 ?  24  VAL   B CG2  1 
ATOM   4739 H H    . VAL   B 1 24  ? 52.642 -25.208 -7.535  1.00 14.62 ?  24  VAL   B H    1 
ATOM   4740 H HA   . VAL   B 1 24  ? 53.173 -22.666 -7.943  1.00 15.22 ?  24  VAL   B HA   1 
ATOM   4741 H HB   . VAL   B 1 24  ? 54.950 -24.783 -7.350  1.00 16.23 ?  24  VAL   B HB   1 
ATOM   4742 H HG11 . VAL   B 1 24  ? 56.487 -22.960 -6.781  1.00 17.33 ?  24  VAL   B HG11 1 
ATOM   4743 H HG12 . VAL   B 1 24  ? 56.363 -23.355 -8.313  1.00 17.33 ?  24  VAL   B HG12 1 
ATOM   4744 H HG13 . VAL   B 1 24  ? 55.591 -22.081 -7.755  1.00 17.33 ?  24  VAL   B HG13 1 
ATOM   4745 H HG21 . VAL   B 1 24  ? 55.000 -23.931 -5.207  1.00 17.98 ?  24  VAL   B HG21 1 
ATOM   4746 H HG22 . VAL   B 1 24  ? 54.011 -22.764 -5.637  1.00 17.98 ?  24  VAL   B HG22 1 
ATOM   4747 H HG23 . VAL   B 1 24  ? 53.501 -24.269 -5.610  1.00 17.98 ?  24  VAL   B HG23 1 
ATOM   4748 N N    . GLU   B 1 25  ? 54.232 -24.670 -10.212 1.00 13.86 ?  25  GLU   B N    1 
ATOM   4749 C CA   . GLU   B 1 25  ? 54.621 -24.711 -11.616 1.00 14.84 ?  25  GLU   B CA   1 
ATOM   4750 C C    . GLU   B 1 25  ? 53.512 -24.162 -12.504 1.00 13.90 ?  25  GLU   B C    1 
ATOM   4751 O O    . GLU   B 1 25  ? 53.779 -23.455 -13.485 1.00 15.05 ?  25  GLU   B O    1 
ATOM   4752 C CB   . GLU   B 1 25  ? 55.000 -26.137 -12.008 1.00 19.16 ?  25  GLU   B CB   1 
ATOM   4753 C CG   . GLU   B 1 25  ? 56.309 -26.595 -11.378 1.00 25.22 ?  25  GLU   B CG   1 
ATOM   4754 C CD   . GLU   B 1 25  ? 57.423 -25.564 -11.488 1.00 30.59 ?  25  GLU   B CD   1 
ATOM   4755 O OE1  . GLU   B 1 25  ? 57.738 -25.132 -12.618 1.00 32.71 ?  25  GLU   B OE1  1 
ATOM   4756 O OE2  . GLU   B 1 25  ? 57.973 -25.169 -10.435 1.00 32.51 -1 25  GLU   B OE2  1 
ATOM   4757 H H    . GLU   B 1 25  ? 54.199 -25.437 -9.822  1.00 16.66 ?  25  GLU   B H    1 
ATOM   4758 H HA   . GLU   B 1 25  ? 55.386 -24.134 -11.745 1.00 17.84 ?  25  GLU   B HA   1 
ATOM   4759 H HB2  . GLU   B 1 25  ? 54.301 -26.746 -11.712 1.00 23.02 ?  25  GLU   B HB2  1 
ATOM   4760 H HB3  . GLU   B 1 25  ? 55.093 -26.189 -12.972 1.00 23.02 ?  25  GLU   B HB3  1 
ATOM   4761 H HG2  . GLU   B 1 25  ? 56.172 -26.746 -10.436 1.00 30.29 ?  25  GLU   B HG2  1 
ATOM   4762 H HG3  . GLU   B 1 25  ? 56.603 -27.407 -11.817 1.00 30.29 ?  25  GLU   B HG3  1 
ATOM   4763 N N    A GLU   B 1 26  ? 52.257 -24.466 -12.168 0.42 12.99 ?  26  GLU   B N    1 
ATOM   4764 N N    B GLU   B 1 26  ? 52.256 -24.475 -12.170 0.58 13.15 ?  26  GLU   B N    1 
ATOM   4765 C CA   A GLU   B 1 26  ? 51.135 -23.940 -12.938 0.42 13.39 ?  26  GLU   B CA   1 
ATOM   4766 C CA   B GLU   B 1 26  ? 51.123 -23.951 -12.928 0.58 14.25 ?  26  GLU   B CA   1 
ATOM   4767 C C    A GLU   B 1 26  ? 51.084 -22.422 -12.863 0.42 12.96 ?  26  GLU   B C    1 
ATOM   4768 C C    B GLU   B 1 26  ? 51.074 -22.430 -12.860 0.58 13.26 ?  26  GLU   B C    1 
ATOM   4769 O O    A GLU   B 1 26  ? 50.897 -21.744 -13.879 0.42 14.02 ?  26  GLU   B O    1 
ATOM   4770 O O    B GLU   B 1 26  ? 50.871 -21.759 -13.878 0.58 14.44 ?  26  GLU   B O    1 
ATOM   4771 C CB   A GLU   B 1 26  ? 49.824 -24.528 -12.423 0.42 14.18 ?  26  GLU   B CB   1 
ATOM   4772 C CB   B GLU   B 1 26  ? 49.812 -24.527 -12.388 0.58 16.33 ?  26  GLU   B CB   1 
ATOM   4773 C CG   A GLU   B 1 26  ? 49.517 -25.898 -12.960 0.42 16.10 ?  26  GLU   B CG   1 
ATOM   4774 C CG   B GLU   B 1 26  ? 49.251 -25.718 -13.149 0.58 19.38 ?  26  GLU   B CG   1 
ATOM   4775 C CD   A GLU   B 1 26  ? 49.320 -25.917 -14.462 0.42 16.26 ?  26  GLU   B CD   1 
ATOM   4776 C CD   B GLU   B 1 26  ? 48.926 -25.407 -14.605 0.58 20.05 ?  26  GLU   B CD   1 
ATOM   4777 O OE1  A GLU   B 1 26  ? 48.481 -25.142 -14.970 0.42 15.40 ?  26  GLU   B OE1  1 
ATOM   4778 O OE1  B GLU   B 1 26  ? 47.880 -24.782 -14.897 0.58 21.18 ?  26  GLU   B OE1  1 
ATOM   4779 O OE2  A GLU   B 1 26  ? 50.009 -26.709 -15.132 0.42 17.34 -1 26  GLU   B OE2  1 
ATOM   4780 O OE2  B GLU   B 1 26  ? 49.726 -25.810 -15.465 0.58 19.89 -1 26  GLU   B OE2  1 
ATOM   4781 H H    A GLU   B 1 26  ? 52.031 -24.963 -11.501 0.42 15.61 ?  26  GLU   B H    1 
ATOM   4782 H H    B GLU   B 1 26  ? 52.036 -24.979 -11.505 0.58 15.81 ?  26  GLU   B H    1 
ATOM   4783 H HA   A GLU   B 1 26  ? 51.243 -24.190 -13.865 0.42 16.09 ?  26  GLU   B HA   1 
ATOM   4784 H HA   B GLU   B 1 26  ? 51.219 -24.208 -13.855 0.58 17.13 ?  26  GLU   B HA   1 
ATOM   4785 H HB2  A GLU   B 1 26  ? 49.872 -24.591 -11.454 0.42 17.04 ?  26  GLU   B HB2  1 
ATOM   4786 H HB2  B GLU   B 1 26  ? 49.955 -24.805 -11.470 0.58 19.62 ?  26  GLU   B HB2  1 
ATOM   4787 H HB3  A GLU   B 1 26  ? 49.098 -23.932 -12.673 0.42 17.04 ?  26  GLU   B HB3  1 
ATOM   4788 H HB3  B GLU   B 1 26  ? 49.142 -23.825 -12.410 0.58 19.62 ?  26  GLU   B HB3  1 
ATOM   4789 H HG2  A GLU   B 1 26  ? 50.257 -26.476 -12.755 0.42 19.35 ?  26  GLU   B HG2  1 
ATOM   4790 H HG2  B GLU   B 1 26  ? 49.903 -26.435 -13.118 0.58 23.28 ?  26  GLU   B HG2  1 
ATOM   4791 H HG3  A GLU   B 1 26  ? 48.704 -26.215 -12.544 0.42 19.35 ?  26  GLU   B HG3  1 
ATOM   4792 H HG3  B GLU   B 1 26  ? 48.428 -25.999 -12.725 0.58 23.28 ?  26  GLU   B HG3  1 
ATOM   4793 N N    . ALA   B 1 27  ? 51.224 -21.870 -11.656 1.00 12.36 ?  27  ALA   B N    1 
ATOM   4794 C CA   . ALA   B 1 27  ? 51.184 -20.422 -11.509 1.00 12.73 ?  27  ALA   B CA   1 
ATOM   4795 C C    . ALA   B 1 27  ? 52.250 -19.765 -12.373 1.00 13.77 ?  27  ALA   B C    1 
ATOM   4796 O O    . ALA   B 1 27  ? 51.987 -18.774 -13.066 1.00 14.32 ?  27  ALA   B O    1 
ATOM   4797 C CB   . ALA   B 1 27  ? 51.357 -20.043 -10.036 1.00 12.66 ?  27  ALA   B CB   1 
ATOM   4798 H H    A ALA   B 1 27  ? 51.340 -22.303 -10.923 0.42 14.86 ?  27  ALA   B H    1 
ATOM   4799 H H    B ALA   B 1 27  ? 51.342 -22.301 -10.922 0.58 14.86 ?  27  ALA   B H    1 
ATOM   4800 H HA   . ALA   B 1 27  ? 50.321 -20.091 -11.797 1.00 15.31 ?  27  ALA   B HA   1 
ATOM   4801 H HB1  . ALA   B 1 27  ? 51.324 -19.076 -9.948  1.00 15.22 ?  27  ALA   B HB1  1 
ATOM   4802 H HB2  . ALA   B 1 27  ? 50.639 -20.443 -9.519  1.00 15.22 ?  27  ALA   B HB2  1 
ATOM   4803 H HB3  . ALA   B 1 27  ? 52.214 -20.372 -9.721  1.00 15.22 ?  27  ALA   B HB3  1 
ATOM   4804 N N    . LYS   B 1 28  ? 53.463 -20.316 -12.366 1.00 15.05 ?  28  LYS   B N    1 
ATOM   4805 C CA   . LYS   B 1 28  ? 54.538 -19.702 -13.134 1.00 17.45 ?  28  LYS   B CA   1 
ATOM   4806 C C    . LYS   B 1 28  ? 54.283 -19.787 -14.633 1.00 18.00 ?  28  LYS   B C    1 
ATOM   4807 O O    . LYS   B 1 28  ? 54.698 -18.891 -15.377 1.00 19.13 ?  28  LYS   B O    1 
ATOM   4808 C CB   . LYS   B 1 28  ? 55.893 -20.300 -12.743 1.00 20.84 ?  28  LYS   B CB   1 
ATOM   4809 C CG   . LYS   B 1 28  ? 56.310 -19.937 -11.319 1.00 24.28 ?  28  LYS   B CG   1 
ATOM   4810 C CD   . LYS   B 1 28  ? 57.718 -20.405 -10.970 1.00 28.96 ?  28  LYS   B CD   1 
ATOM   4811 C CE   . LYS   B 1 28  ? 57.761 -21.889 -10.680 1.00 33.39 ?  28  LYS   B CE   1 
ATOM   4812 N NZ   . LYS   B 1 28  ? 59.100 -22.318 -10.180 1.00 35.60 ?  28  LYS   B NZ   1 
ATOM   4813 H H    . LYS   B 1 28  ? 53.683 -21.023 -11.929 1.00 18.08 ?  28  LYS   B H    1 
ATOM   4814 H HA   . LYS   B 1 28  ? 54.570 -18.764 -12.915 1.00 20.97 ?  28  LYS   B HA   1 
ATOM   4815 H HB2  . LYS   B 1 28  ? 55.846 -21.263 -12.804 1.00 25.04 ?  28  LYS   B HB2  1 
ATOM   4816 H HB3  . LYS   B 1 28  ? 56.572 -19.959 -13.348 1.00 25.04 ?  28  LYS   B HB3  1 
ATOM   4817 H HG2  . LYS   B 1 28  ? 56.281 -18.970 -11.222 1.00 29.17 ?  28  LYS   B HG2  1 
ATOM   4818 H HG3  . LYS   B 1 28  ? 55.692 -20.348 -10.698 1.00 29.17 ?  28  LYS   B HG3  1 
ATOM   4819 H HD2  . LYS   B 1 28  ? 58.307 -20.221 -11.718 1.00 34.78 ?  28  LYS   B HD2  1 
ATOM   4820 H HD3  . LYS   B 1 28  ? 58.020 -19.928 -10.181 1.00 34.78 ?  28  LYS   B HD3  1 
ATOM   4821 H HE2  . LYS   B 1 28  ? 57.101 -22.099 -10.000 1.00 40.09 ?  28  LYS   B HE2  1 
ATOM   4822 H HE3  . LYS   B 1 28  ? 57.569 -22.380 -11.494 1.00 40.09 ?  28  LYS   B HE3  1 
ATOM   4823 H HZ1  . LYS   B 1 28  ? 59.098 -23.193 -10.017 1.00 42.74 ?  28  LYS   B HZ1  1 
ATOM   4824 H HZ2  . LYS   B 1 28  ? 59.723 -22.139 -10.790 1.00 42.74 ?  28  LYS   B HZ2  1 
ATOM   4825 H HZ3  . LYS   B 1 28  ? 59.298 -21.884 -9.428  1.00 42.74 ?  28  LYS   B HZ3  1 
ATOM   4826 N N    . LYS   B 1 29  ? 53.578 -20.823 -15.092 1.00 18.90 ?  29  LYS   B N    1 
ATOM   4827 C CA   . LYS   B 1 29  ? 53.316 -20.975 -16.519 1.00 21.44 ?  29  LYS   B CA   1 
ATOM   4828 C C    . LYS   B 1 29  ? 52.065 -20.232 -16.976 1.00 20.32 ?  29  LYS   B C    1 
ATOM   4829 O O    . LYS   B 1 29  ? 52.067 -19.624 -18.051 1.00 21.75 ?  29  LYS   B O    1 
ATOM   4830 C CB   . LYS   B 1 29  ? 53.200 -22.458 -16.878 1.00 26.39 ?  29  LYS   B CB   1 
ATOM   4831 C CG   . LYS   B 1 29  ? 52.927 -22.717 -18.350 1.00 31.18 ?  29  LYS   B CG   1 
ATOM   4832 C CD   . LYS   B 1 29  ? 53.103 -24.188 -18.702 1.00 34.95 ?  29  LYS   B CD   1 
ATOM   4833 C CE   . LYS   B 1 29  ? 52.016 -25.056 -18.088 1.00 37.70 ?  29  LYS   B CE   1 
ATOM   4834 N NZ   . LYS   B 1 29  ? 52.199 -26.494 -18.440 1.00 39.31 ?  29  LYS   B NZ   1 
ATOM   4835 H H    . LYS   B 1 29  ? 53.230 -21.443 -14.597 1.00 22.70 ?  29  LYS   B H    1 
ATOM   4836 H HA   . LYS   B 1 29  ? 54.066 -20.613 -17.008 1.00 25.76 ?  29  LYS   B HA   1 
ATOM   4837 H HB2  . LYS   B 1 29  ? 54.036 -22.897 -16.654 1.00 31.70 ?  29  LYS   B HB2  1 
ATOM   4838 H HB3  . LYS   B 1 29  ? 52.476 -22.849 -16.371 1.00 31.70 ?  29  LYS   B HB3  1 
ATOM   4839 H HG2  . LYS   B 1 29  ? 52.015 -22.461 -18.555 1.00 37.44 ?  29  LYS   B HG2  1 
ATOM   4840 H HG3  . LYS   B 1 29  ? 53.549 -22.199 -18.887 1.00 37.44 ?  29  LYS   B HG3  1 
ATOM   4841 H HD2  . LYS   B 1 29  ? 53.065 -24.293 -19.665 1.00 41.96 ?  29  LYS   B HD2  1 
ATOM   4842 H HD3  . LYS   B 1 29  ? 53.960 -24.497 -18.366 1.00 41.96 ?  29  LYS   B HD3  1 
ATOM   4843 H HE2  . LYS   B 1 29  ? 52.045 -24.975 -17.122 1.00 45.27 ?  29  LYS   B HE2  1 
ATOM   4844 H HE3  . LYS   B 1 29  ? 51.151 -24.769 -18.422 1.00 45.27 ?  29  LYS   B HE3  1 
ATOM   4845 H HZ1  . LYS   B 1 29  ? 51.552 -26.983 -18.071 1.00 47.20 ?  29  LYS   B HZ1  1 
ATOM   4846 H HZ2  . LYS   B 1 29  ? 52.171 -26.598 -19.324 1.00 47.20 ?  29  LYS   B HZ2  1 
ATOM   4847 H HZ3  . LYS   B 1 29  ? 52.986 -26.783 -18.140 1.00 47.20 ?  29  LYS   B HZ3  1 
ATOM   4848 N N    . VAL   B 1 30  ? 50.994 -20.285 -16.182 1.00 18.15 ?  30  VAL   B N    1 
ATOM   4849 C CA   . VAL   B 1 30  ? 49.706 -19.702 -16.564 1.00 18.46 ?  30  VAL   B CA   1 
ATOM   4850 C C    . VAL   B 1 30  ? 49.700 -18.193 -16.394 1.00 17.03 ?  30  VAL   B C    1 
ATOM   4851 O O    . VAL   B 1 30  ? 48.951 -17.482 -17.084 1.00 17.75 ?  30  VAL   B O    1 
ATOM   4852 C CB   . VAL   B 1 30  ? 48.607 -20.328 -15.683 1.00 20.48 ?  30  VAL   B CB   1 
ATOM   4853 C CG1  . VAL   B 1 30  ? 47.316 -19.518 -15.746 1.00 21.16 ?  30  VAL   B CG1  1 
ATOM   4854 C CG2  . VAL   B 1 30  ? 48.369 -21.784 -16.073 1.00 21.70 ?  30  VAL   B CG2  1 
ATOM   4855 H H    . VAL   B 1 30  ? 50.983 -20.682 -15.411 1.00 21.81 ?  30  VAL   B H    1 
ATOM   4856 H HA   . VAL   B 1 30  ? 49.513 -19.932 -17.488 1.00 22.17 ?  30  VAL   B HA   1 
ATOM   4857 H HB   . VAL   B 1 30  ? 48.905 -20.326 -14.760 1.00 24.60 ?  30  VAL   B HB   1 
ATOM   4858 H HG11 . VAL   B 1 30  ? 46.579 -20.094 -15.486 1.00 25.42 ?  30  VAL   B HG11 1 
ATOM   4859 H HG12 . VAL   B 1 30  ? 47.376 -18.772 -15.131 1.00 25.42 ?  30  VAL   B HG12 1 
ATOM   4860 H HG13 . VAL   B 1 30  ? 47.179 -19.207 -16.649 1.00 25.42 ?  30  VAL   B HG13 1 
ATOM   4861 H HG21 . VAL   B 1 30  ? 47.678 -22.160 -15.501 1.00 26.06 ?  30  VAL   B HG21 1 
ATOM   4862 H HG22 . VAL   B 1 30  ? 48.081 -21.821 -17.000 1.00 26.06 ?  30  VAL   B HG22 1 
ATOM   4863 H HG23 . VAL   B 1 30  ? 49.193 -22.280 -15.962 1.00 26.06 ?  30  VAL   B HG23 1 
ATOM   4864 N N    A LYS   B 1 31  ? 50.506 -17.686 -15.470 0.42 16.95 ?  31  LYS   B N    1 
ATOM   4865 N N    B LYS   B 1 31  ? 50.504 -17.685 -15.469 0.58 16.49 ?  31  LYS   B N    1 
ATOM   4866 C CA   A LYS   B 1 31  ? 50.511 -16.275 -15.107 0.42 17.47 ?  31  LYS   B CA   1 
ATOM   4867 C CA   B LYS   B 1 31  ? 50.513 -16.273 -15.109 0.58 16.95 ?  31  LYS   B CA   1 
ATOM   4868 C C    A LYS   B 1 31  ? 49.111 -15.786 -14.718 0.42 15.62 ?  31  LYS   B C    1 
ATOM   4869 C C    B LYS   B 1 31  ? 49.117 -15.777 -14.713 0.58 15.29 ?  31  LYS   B C    1 
ATOM   4870 O O    A LYS   B 1 31  ? 48.565 -14.878 -15.353 0.42 15.91 ?  31  LYS   B O    1 
ATOM   4871 O O    B LYS   B 1 31  ? 48.581 -14.854 -15.333 0.58 15.82 ?  31  LYS   B O    1 
ATOM   4872 C CB   A LYS   B 1 31  ? 51.114 -15.422 -16.215 0.42 19.99 ?  31  LYS   B CB   1 
ATOM   4873 C CB   B LYS   B 1 31  ? 51.115 -15.430 -16.226 0.58 19.36 ?  31  LYS   B CB   1 
ATOM   4874 C CG   A LYS   B 1 31  ? 52.562 -15.790 -16.523 0.42 22.62 ?  31  LYS   B CG   1 
ATOM   4875 C CG   B LYS   B 1 31  ? 52.526 -15.876 -16.599 0.58 22.27 ?  31  LYS   B CG   1 
ATOM   4876 C CD   A LYS   B 1 31  ? 53.127 -14.961 -17.660 0.42 24.85 ?  31  LYS   B CD   1 
ATOM   4877 C CD   B LYS   B 1 31  ? 53.101 -15.065 -17.742 0.58 24.79 ?  31  LYS   B CD   1 
ATOM   4878 C CE   A LYS   B 1 31  ? 54.600 -15.251 -17.872 0.42 26.61 ?  31  LYS   B CE   1 
ATOM   4879 C CE   B LYS   B 1 31  ? 54.589 -15.306 -17.886 0.58 26.76 ?  31  LYS   B CE   1 
ATOM   4880 N NZ   A LYS   B 1 31  ? 55.403 -14.930 -16.658 0.42 27.56 ?  31  LYS   B NZ   1 
ATOM   4881 N NZ   B LYS   B 1 31  ? 55.323 -14.938 -16.641 0.58 27.80 ?  31  LYS   B NZ   1 
ATOM   4882 H H    A LYS   B 1 31  ? 51.075 -18.160 -15.032 0.42 20.37 ?  31  LYS   B H    1 
ATOM   4883 H H    B LYS   B 1 31  ? 51.071 -18.164 -15.031 0.58 19.82 ?  31  LYS   B H    1 
ATOM   4884 H HA   A LYS   B 1 31  ? 51.070 -16.181 -14.335 0.42 20.99 ?  31  LYS   B HA   1 
ATOM   4885 H HA   B LYS   B 1 31  ? 51.073 -16.180 -14.338 0.58 20.37 ?  31  LYS   B HA   1 
ATOM   4886 H HB2  A LYS   B 1 31  ? 50.600 -15.538 -17.028 0.42 24.01 ?  31  LYS   B HB2  1 
ATOM   4887 H HB2  B LYS   B 1 31  ? 50.558 -15.502 -17.017 0.58 23.26 ?  31  LYS   B HB2  1 
ATOM   4888 H HB3  A LYS   B 1 31  ? 51.096 -14.496 -15.936 0.42 24.01 ?  31  LYS   B HB3  1 
ATOM   4889 H HB3  B LYS   B 1 31  ? 51.157 -14.513 -15.926 0.58 23.26 ?  31  LYS   B HB3  1 
ATOM   4890 H HG2  A LYS   B 1 31  ? 53.101 -15.635 -15.731 0.42 27.17 ?  31  LYS   B HG2  1 
ATOM   4891 H HG2  B LYS   B 1 31  ? 53.098 -15.772 -15.824 0.58 26.76 ?  31  LYS   B HG2  1 
ATOM   4892 H HG3  A LYS   B 1 31  ? 52.606 -16.727 -16.777 0.42 27.17 ?  31  LYS   B HG3  1 
ATOM   4893 H HG3  B LYS   B 1 31  ? 52.502 -16.809 -16.871 0.58 26.76 ?  31  LYS   B HG3  1 
ATOM   4894 H HD2  A LYS   B 1 31  ? 52.651 -15.178 -18.477 0.42 29.85 ?  31  LYS   B HD2  1 
ATOM   4895 H HD2  B LYS   B 1 31  ? 52.665 -15.329 -18.568 0.58 29.78 ?  31  LYS   B HD2  1 
ATOM   4896 H HD3  A LYS   B 1 31  ? 53.026 -14.021 -17.449 0.42 29.85 ?  31  LYS   B HD3  1 
ATOM   4897 H HD3  B LYS   B 1 31  ? 52.956 -14.124 -17.568 0.58 29.78 ?  31  LYS   B HD3  1 
ATOM   4898 H HE2  A LYS   B 1 31  ? 54.717 -16.194 -18.072 0.42 31.96 ?  31  LYS   B HE2  1 
ATOM   4899 H HE2  B LYS   B 1 31  ? 54.748 -16.247 -18.065 0.58 32.14 ?  31  LYS   B HE2  1 
ATOM   4900 H HE3  A LYS   B 1 31  ? 54.930 -14.710 -18.606 0.42 31.96 ?  31  LYS   B HE3  1 
ATOM   4901 H HE3  B LYS   B 1 31  ? 54.932 -14.764 -18.613 0.58 32.14 ?  31  LYS   B HE3  1 
ATOM   4902 H HZ1  A LYS   B 1 31  ? 56.271 -15.024 -16.833 0.42 33.10 ?  31  LYS   B HZ1  1 
ATOM   4903 H HZ1  B LYS   B 1 31  ? 56.200 -14.932 -16.794 0.58 33.39 ?  31  LYS   B HZ1  1 
ATOM   4904 H HZ2  A LYS   B 1 31  ? 55.248 -14.091 -16.405 0.42 33.10 ?  31  LYS   B HZ2  1 
ATOM   4905 H HZ2  B LYS   B 1 31  ? 55.072 -14.128 -16.368 0.58 33.39 ?  31  LYS   B HZ2  1 
ATOM   4906 H HZ3  A LYS   B 1 31  ? 55.182 -15.478 -15.992 0.42 33.10 ?  31  LYS   B HZ3  1 
ATOM   4907 H HZ3  B LYS   B 1 31  ? 55.147 -15.526 -15.996 0.58 33.39 ?  31  LYS   B HZ3  1 
ATOM   4908 N N    . PRO   B 1 32  ? 48.515 -16.360 -13.672 1.00 13.80 ?  32  PRO   B N    1 
ATOM   4909 C CA   . PRO   B 1 32  ? 47.140 -15.993 -13.304 1.00 12.68 ?  32  PRO   B CA   1 
ATOM   4910 C C    . PRO   B 1 32  ? 47.070 -14.648 -12.594 1.00 12.67 ?  32  PRO   B C    1 
ATOM   4911 O O    . PRO   B 1 32  ? 48.001 -14.232 -11.898 1.00 13.76 ?  32  PRO   B O    1 
ATOM   4912 C CB   . PRO   B 1 32  ? 46.742 -17.112 -12.333 1.00 12.76 ?  32  PRO   B CB   1 
ATOM   4913 C CG   . PRO   B 1 32  ? 48.045 -17.437 -11.647 1.00 13.29 ?  32  PRO   B CG   1 
ATOM   4914 C CD   . PRO   B 1 32  ? 49.103 -17.318 -12.712 1.00 13.51 ?  32  PRO   B CD   1 
ATOM   4915 H HA   . PRO   B 1 32  ? 46.553 -16.007 -14.086 1.00 15.24 ?  32  PRO   B HA   1 
ATOM   4916 H HB2  . PRO   B 1 32  ? 46.085 -16.785 -11.700 1.00 15.34 ?  32  PRO   B HB2  1 
ATOM   4917 H HB3  . PRO   B 1 32  ? 46.405 -17.881 -12.822 1.00 15.34 ?  32  PRO   B HB3  1 
ATOM   4918 H HG2  . PRO   B 1 32  ? 48.206 -16.801 -10.932 1.00 15.97 ?  32  PRO   B HG2  1 
ATOM   4919 H HG3  . PRO   B 1 32  ? 48.016 -18.343 -11.298 1.00 15.97 ?  32  PRO   B HG3  1 
ATOM   4920 H HD2  . PRO   B 1 32  ? 49.920 -16.952 -12.339 1.00 16.24 ?  32  PRO   B HD2  1 
ATOM   4921 H HD3  . PRO   B 1 32  ? 49.256 -18.174 -13.136 1.00 16.24 ?  32  PRO   B HD3  1 
ATOM   4922 N N    . THR   B 1 33  ? 45.919 -13.985 -12.752 1.00 12.12 ?  33  THR   B N    1 
ATOM   4923 C CA   . THR   B 1 33  ? 45.642 -12.810 -11.937 1.00 12.33 ?  33  THR   B CA   1 
ATOM   4924 C C    . THR   B 1 33  ? 45.601 -13.166 -10.456 1.00 12.09 ?  33  THR   B C    1 
ATOM   4925 O O    . THR   B 1 33  ? 46.077 -12.389 -9.617  1.00 13.14 ?  33  THR   B O    1 
ATOM   4926 C CB   . THR   B 1 33  ? 44.323 -12.170 -12.376 1.00 12.96 ?  33  THR   B CB   1 
ATOM   4927 O OG1  . THR   B 1 33  ? 44.355 -11.926 -13.783 1.00 13.32 ?  33  THR   B OG1  1 
ATOM   4928 C CG2  . THR   B 1 33  ? 44.086 -10.876 -11.629 1.00 14.32 ?  33  THR   B CG2  1 
ATOM   4929 H H    . THR   B 1 33  ? 45.297 -14.202 -13.313 1.00 14.57 ?  33  THR   B H    1 
ATOM   4930 H HA   . THR   B 1 33  ? 46.350 -12.168 -12.076 1.00 14.82 ?  33  THR   B HA   1 
ATOM   4931 H HB   . THR   B 1 33  ? 43.590 -12.776 -12.178 1.00 15.58 ?  33  THR   B HB   1 
ATOM   4932 H HG1  . THR   B 1 33  ? 43.642 -11.549 -14.026 1.00 16.01 ?  33  THR   B HG1  1 
ATOM   4933 H HG21 . THR   B 1 33  ? 43.329 -10.408 -12.008 1.00 17.22 ?  33  THR   B HG21 1 
ATOM   4934 H HG22 . THR   B 1 33  ? 43.906 -11.060 -10.691 1.00 17.22 ?  33  THR   B HG22 1 
ATOM   4935 H HG23 . THR   B 1 33  ? 44.872 -10.310 -11.690 1.00 17.22 ?  33  THR   B HG23 1 
ATOM   4936 N N    . VAL   B 1 34  ? 45.031 -14.327 -10.112 1.00 11.44 ?  34  VAL   B N    1 
ATOM   4937 C CA   . VAL   B 1 34  ? 44.835 -14.727 -8.723  1.00 11.22 ?  34  VAL   B CA   1 
ATOM   4938 C C    . VAL   B 1 34  ? 45.260 -16.175 -8.555  1.00 10.20 ?  34  VAL   B C    1 
ATOM   4939 O O    . VAL   B 1 34  ? 44.742 -17.063 -9.243  1.00 11.00 ?  34  VAL   B O    1 
ATOM   4940 C CB   . VAL   B 1 34  ? 43.366 -14.573 -8.277  1.00 12.42 ?  34  VAL   B CB   1 
ATOM   4941 C CG1  . VAL   B 1 34  ? 43.205 -15.043 -6.831  1.00 12.53 ?  34  VAL   B CG1  1 
ATOM   4942 C CG2  . VAL   B 1 34  ? 42.890 -13.140 -8.454  1.00 13.45 ?  34  VAL   B CG2  1 
ATOM   4943 H H    . VAL   B 1 34  ? 44.758 -14.913 -10.681 1.00 13.76 ?  34  VAL   B H    1 
ATOM   4944 H HA   . VAL   B 1 34  ? 45.391 -14.176 -8.148  1.00 13.49 ?  34  VAL   B HA   1 
ATOM   4945 H HB   . VAL   B 1 34  ? 42.813 -15.137 -8.841  1.00 14.93 ?  34  VAL   B HB   1 
ATOM   4946 H HG11 . VAL   B 1 34  ? 42.361 -14.708 -6.486  1.00 15.07 ?  34  VAL   B HG11 1 
ATOM   4947 H HG12 . VAL   B 1 34  ? 43.205 -16.013 -6.810  1.00 15.07 ?  34  VAL   B HG12 1 
ATOM   4948 H HG13 . VAL   B 1 34  ? 43.938 -14.696 -6.302  1.00 15.07 ?  34  VAL   B HG13 1 
ATOM   4949 H HG21 . VAL   B 1 34  ? 41.973 -13.072 -8.145  1.00 16.16 ?  34  VAL   B HG21 1 
ATOM   4950 H HG22 . VAL   B 1 34  ? 43.460 -12.550 -7.940  1.00 16.16 ?  34  VAL   B HG22 1 
ATOM   4951 H HG23 . VAL   B 1 34  ? 42.936 -12.904 -9.398  1.00 16.16 ?  34  VAL   B HG23 1 
ATOM   4952 N N    . VAL   B 1 35  ? 46.161 -16.422 -7.606  1.00 9.71  ?  35  VAL   B N    1 
ATOM   4953 C CA   . VAL   B 1 35  ? 46.397 -17.764 -7.088  1.00 9.68  ?  35  VAL   B CA   1 
ATOM   4954 C C    . VAL   B 1 35  ? 45.854 -17.817 -5.670  1.00 9.13  ?  35  VAL   B C    1 
ATOM   4955 O O    . VAL   B 1 35  ? 46.078 -16.895 -4.877  1.00 9.71  ?  35  VAL   B O    1 
ATOM   4956 C CB   . VAL   B 1 35  ? 47.878 -18.202 -7.168  1.00 10.11 ?  35  VAL   B CB   1 
ATOM   4957 C CG1  . VAL   B 1 35  ? 48.788 -17.369 -6.270  1.00 10.73 ?  35  VAL   B CG1  1 
ATOM   4958 C CG2  . VAL   B 1 35  ? 48.006 -19.687 -6.847  1.00 10.76 ?  35  VAL   B CG2  1 
ATOM   4959 H H    . VAL   B 1 35  ? 46.655 -15.818 -7.238  1.00 11.68 ?  35  VAL   B H    1 
ATOM   4960 H HA   . VAL   B 1 35  ? 45.881 -18.393 -7.613  1.00 11.64 ?  35  VAL   B HA   1 
ATOM   4961 H HB   . VAL   B 1 35  ? 48.180 -18.086 -8.084  1.00 12.16 ?  35  VAL   B HB   1 
ATOM   4962 H HG11 . VAL   B 1 35  ? 49.708 -17.619 -6.443  1.00 12.90 ?  35  VAL   B HG11 1 
ATOM   4963 H HG12 . VAL   B 1 35  ? 48.648 -16.436 -6.467  1.00 12.90 ?  35  VAL   B HG12 1 
ATOM   4964 H HG13 . VAL   B 1 35  ? 48.564 -17.556 -5.343  1.00 12.90 ?  35  VAL   B HG13 1 
ATOM   4965 H HG21 . VAL   B 1 35  ? 48.924 -19.966 -6.959  1.00 12.94 ?  35  VAL   B HG21 1 
ATOM   4966 H HG22 . VAL   B 1 35  ? 47.725 -19.839 -5.924  1.00 12.94 ?  35  VAL   B HG22 1 
ATOM   4967 H HG23 . VAL   B 1 35  ? 47.429 -20.198 -7.444  1.00 12.94 ?  35  VAL   B HG23 1 
ATOM   4968 N N    . VAL   B 1 36  ? 45.142 -18.896 -5.352  1.00 9.26  ?  36  VAL   B N    1 
ATOM   4969 C CA   . VAL   B 1 36  ? 44.592 -19.098 -4.020  1.00 9.19  ?  36  VAL   B CA   1 
ATOM   4970 C C    . VAL   B 1 36  ? 45.595 -19.860 -3.165  1.00 8.77  ?  36  VAL   B C    1 
ATOM   4971 O O    . VAL   B 1 36  ? 46.133 -20.894 -3.585  1.00 9.78  ?  36  VAL   B O    1 
ATOM   4972 C CB   . VAL   B 1 36  ? 43.255 -19.852 -4.093  1.00 9.14  ?  36  VAL   B CB   1 
ATOM   4973 C CG1  . VAL   B 1 36  ? 42.744 -20.205 -2.696  1.00 10.07 ?  36  VAL   B CG1  1 
ATOM   4974 C CG2  . VAL   B 1 36  ? 42.232 -19.031 -4.853  1.00 10.05 ?  36  VAL   B CG2  1 
ATOM   4975 H H    . VAL   B 1 36  ? 44.962 -19.533 -5.898  1.00 11.13 ?  36  VAL   B H    1 
ATOM   4976 H HA   . VAL   B 1 36  ? 44.427 -18.244 -3.600  1.00 11.06 ?  36  VAL   B HA   1 
ATOM   4977 H HB   . VAL   B 1 36  ? 43.383 -20.687 -4.573  1.00 11.00 ?  36  VAL   B HB   1 
ATOM   4978 H HG11 . VAL   B 1 36  ? 41.805 -20.445 -2.756  1.00 12.11 ?  36  VAL   B HG11 1 
ATOM   4979 H HG12 . VAL   B 1 36  ? 43.255 -20.944 -2.345  1.00 12.11 ?  36  VAL   B HG12 1 
ATOM   4980 H HG13 . VAL   B 1 36  ? 42.844 -19.424 -2.124  1.00 12.11 ?  36  VAL   B HG13 1 
ATOM   4981 H HG21 . VAL   B 1 36  ? 41.386 -19.506 -4.866  1.00 12.09 ?  36  VAL   B HG21 1 
ATOM   4982 H HG22 . VAL   B 1 36  ? 42.126 -18.174 -4.418  1.00 12.09 ?  36  VAL   B HG22 1 
ATOM   4983 H HG23 . VAL   B 1 36  ? 42.549 -18.902 -5.765  1.00 12.09 ?  36  VAL   B HG23 1 
ATOM   4984 N N    . ASN   B 1 37  ? 45.822 -19.360 -1.954  1.00 9.03  ?  37  ASN   B N    1 
ATOM   4985 C CA   . ASN   B 1 37  ? 46.567 -20.083 -0.940  1.00 9.27  ?  37  ASN   B CA   1 
ATOM   4986 C C    . ASN   B 1 37  ? 45.617 -20.755 0.043   1.00 9.32  ?  37  ASN   B C    1 
ATOM   4987 O O    . ASN   B 1 37  ? 44.609 -20.172 0.453   1.00 10.18 ?  37  ASN   B O    1 
ATOM   4988 C CB   . ASN   B 1 37  ? 47.494 -19.139 -0.183  1.00 9.29  ?  37  ASN   B CB   1 
ATOM   4989 C CG   . ASN   B 1 37  ? 48.341 -19.854 0.836   1.00 9.50  ?  37  ASN   B CG   1 
ATOM   4990 O OD1  . ASN   B 1 37  ? 48.673 -21.034 0.669   1.00 10.53 ?  37  ASN   B OD1  1 
ATOM   4991 N ND2  . ASN   B 1 37  ? 48.696 -19.150 1.901   1.00 10.00 ?  37  ASN   B ND2  1 
ATOM   4992 H H    . ASN   B 1 37  ? 45.550 -18.588 -1.693  1.00 10.86 ?  37  ASN   B H    1 
ATOM   4993 H HA   . ASN   B 1 37  ? 47.101 -20.777 -1.357  1.00 11.15 ?  37  ASN   B HA   1 
ATOM   4994 H HB2  . ASN   B 1 37  ? 48.089 -18.717 -0.815  1.00 11.18 ?  37  ASN   B HB2  1 
ATOM   4995 H HB3  . ASN   B 1 37  ? 46.962 -18.477 0.279   1.00 11.18 ?  37  ASN   B HB3  1 
ATOM   4996 H HD21 . ASN   B 1 37  ? 49.181 -19.517 2.514   1.00 12.03 ?  37  ASN   B HD21 1 
ATOM   4997 H HD22 . ASN   B 1 37  ? 48.446 -18.341 1.987   1.00 12.03 ?  37  ASN   B HD22 1 
ATOM   4998 N N    . ALA   B 1 38  ? 45.966 -21.988 0.420   1.00 9.65  ?  38  ALA   B N    1 
ATOM   4999 C CA   . ALA   B 1 38  ? 45.306 -22.731 1.493   1.00 10.14 ?  38  ALA   B CA   1 
ATOM   5000 C C    . ALA   B 1 38  ? 45.890 -22.248 2.821   1.00 9.54  ?  38  ALA   B C    1 
ATOM   5001 O O    . ALA   B 1 38  ? 46.792 -22.858 3.407   1.00 10.80 ?  38  ALA   B O    1 
ATOM   5002 C CB   . ALA   B 1 38  ? 45.524 -24.227 1.302   1.00 11.27 ?  38  ALA   B CB   1 
ATOM   5003 H H    . ALA   B 1 38  ? 46.615 -22.424 0.065   1.00 11.61 ?  38  ALA   B H    1 
ATOM   5004 H HA   . ALA   B 1 38  ? 44.353 -22.548 1.483   1.00 12.19 ?  38  ALA   B HA   1 
ATOM   5005 H HB1  . ALA   B 1 38  ? 45.076 -24.706 2.023   1.00 13.55 ?  38  ALA   B HB1  1 
ATOM   5006 H HB2  . ALA   B 1 38  ? 45.146 -24.495 0.449   1.00 13.55 ?  38  ALA   B HB2  1 
ATOM   5007 H HB3  . ALA   B 1 38  ? 46.472 -24.416 1.322   1.00 13.55 ?  38  ALA   B HB3  1 
ATOM   5008 N N    . ALA   B 1 39  ? 45.375 -21.107 3.281   1.00 9.58  ?  39  ALA   B N    1 
ATOM   5009 C CA   . ALA   B 1 39  ? 45.929 -20.369 4.405   1.00 10.13 ?  39  ALA   B CA   1 
ATOM   5010 C C    . ALA   B 1 39  ? 45.319 -20.815 5.732   1.00 10.13 ?  39  ALA   B C    1 
ATOM   5011 O O    . ALA   B 1 39  ? 44.290 -21.489 5.788   1.00 10.85 ?  39  ALA   B O    1 
ATOM   5012 C CB   . ALA   B 1 39  ? 45.689 -18.873 4.203   1.00 10.66 ?  39  ALA   B CB   1 
ATOM   5013 H H    . ALA   B 1 39  ? 44.673 -20.738 2.940   1.00 11.53 ?  39  ALA   B H    1 
ATOM   5014 H HA   . ALA   B 1 39  ? 46.881 -20.522 4.442   1.00 12.18 ?  39  ALA   B HA   1 
ATOM   5015 H HB1  . ALA   B 1 39  ? 46.065 -18.389 4.953   1.00 12.82 ?  39  ALA   B HB1  1 
ATOM   5016 H HB2  . ALA   B 1 39  ? 46.124 -18.590 3.378   1.00 12.82 ?  39  ALA   B HB2  1 
ATOM   5017 H HB3  . ALA   B 1 39  ? 44.736 -18.705 4.142   1.00 12.82 ?  39  ALA   B HB3  1 
ATOM   5018 N N    . ASN   B 1 40  ? 45.963 -20.392 6.817   1.00 10.83 ?  40  ASN   B N    1 
ATOM   5019 C CA   . ASN   B 1 40  ? 45.403 -20.435 8.157   1.00 11.53 ?  40  ASN   B CA   1 
ATOM   5020 C C    . ASN   B 1 40  ? 45.223 -19.007 8.680   1.00 11.06 ?  40  ASN   B C    1 
ATOM   5021 O O    . ASN   B 1 40  ? 45.630 -18.030 8.043   1.00 11.07 ?  40  ASN   B O    1 
ATOM   5022 C CB   . ASN   B 1 40  ? 46.254 -21.310 9.090   1.00 12.18 ?  40  ASN   B CB   1 
ATOM   5023 C CG   . ASN   B 1 40  ? 47.705 -20.901 9.116   1.00 13.37 ?  40  ASN   B CG   1 
ATOM   5024 O OD1  . ASN   B 1 40  ? 48.023 -19.720 9.170   1.00 15.36 ?  40  ASN   B OD1  1 
ATOM   5025 N ND2  . ASN   B 1 40  ? 48.601 -21.880 9.073   1.00 13.79 ?  40  ASN   B ND2  1 
ATOM   5026 H H    . ASN   B 1 40  ? 46.754 -20.058 6.793   1.00 13.02 ?  40  ASN   B H    1 
ATOM   5027 H HA   . ASN   B 1 40  ? 44.518 -20.830 8.111   1.00 13.87 ?  40  ASN   B HA   1 
ATOM   5028 H HB2  . ASN   B 1 40  ? 45.901 -21.239 9.992   1.00 14.65 ?  40  ASN   B HB2  1 
ATOM   5029 H HB3  . ASN   B 1 40  ? 46.201 -22.228 8.785   1.00 14.65 ?  40  ASN   B HB3  1 
ATOM   5030 H HD21 . ASN   B 1 40  ? 49.441 -21.700 9.097   1.00 16.57 ?  40  ASN   B HD21 1 
ATOM   5031 H HD22 . ASN   B 1 40  ? 48.340 -22.701 9.035   1.00 16.57 ?  40  ASN   B HD22 1 
ATOM   5032 N N    . VAL   B 1 41  ? 44.567 -18.881 9.838   1.00 11.61 ?  41  VAL   B N    1 
ATOM   5033 C CA   . VAL   B 1 41  ? 44.110 -17.562 10.287  1.00 11.86 ?  41  VAL   B CA   1 
ATOM   5034 C C    . VAL   B 1 41  ? 45.260 -16.605 10.576  1.00 11.58 ?  41  VAL   B C    1 
ATOM   5035 O O    . VAL   B 1 41  ? 45.079 -15.384 10.493  1.00 11.89 ?  41  VAL   B O    1 
ATOM   5036 C CB   . VAL   B 1 41  ? 43.139 -17.641 11.484  1.00 13.49 ?  41  VAL   B CB   1 
ATOM   5037 C CG1  . VAL   B 1 41  ? 41.827 -18.304 11.081  1.00 14.14 ?  41  VAL   B CG1  1 
ATOM   5038 C CG2  . VAL   B 1 41  ? 43.782 -18.348 12.666  1.00 14.34 ?  41  VAL   B CG2  1 
ATOM   5039 H H    . VAL   B 1 41  ? 44.377 -19.526 10.368  1.00 13.96 ?  41  VAL   B H    1 
ATOM   5040 H HA   . VAL   B 1 41  ? 43.603 -17.168 9.557   1.00 14.27 ?  41  VAL   B HA   1 
ATOM   5041 H HB   . VAL   B 1 41  ? 42.923 -16.738 11.769  1.00 16.22 ?  41  VAL   B HB   1 
ATOM   5042 H HG11 . VAL   B 1 41  ? 41.228 -18.314 11.845  1.00 17.00 ?  41  VAL   B HG11 1 
ATOM   5043 H HG12 . VAL   B 1 41  ? 41.426 -17.799 10.355  1.00 17.00 ?  41  VAL   B HG12 1 
ATOM   5044 H HG13 . VAL   B 1 41  ? 42.008 -19.212 10.792  1.00 17.00 ?  41  VAL   B HG13 1 
ATOM   5045 H HG21 . VAL   B 1 41  ? 43.157 -18.357 13.408  1.00 17.24 ?  41  VAL   B HG21 1 
ATOM   5046 H HG22 . VAL   B 1 41  ? 43.996 -19.261 12.408  1.00 17.24 ?  41  VAL   B HG22 1 
ATOM   5047 H HG23 . VAL   B 1 41  ? 44.588 -17.876 12.916  1.00 17.24 ?  41  VAL   B HG23 1 
ATOM   5048 N N    . TYR   B 1 42  ? 46.433 -17.118 10.952  1.00 12.07 ?  42  TYR   B N    1 
ATOM   5049 C CA   . TYR   B 1 42  ? 47.588 -16.271 11.225  1.00 12.39 ?  42  TYR   B CA   1 
ATOM   5050 C C    . TYR   B 1 42  ? 48.550 -16.195 10.043  1.00 12.07 ?  42  TYR   B C    1 
ATOM   5051 O O    . TYR   B 1 42  ? 49.636 -15.620 10.175  1.00 12.80 ?  42  TYR   B O    1 
ATOM   5052 C CB   . TYR   B 1 42  ? 48.282 -16.677 12.533  1.00 14.32 ?  42  TYR   B CB   1 
ATOM   5053 C CG   . TYR   B 1 42  ? 47.686 -15.981 13.759  1.00 14.45 ?  42  TYR   B CG   1 
ATOM   5054 C CD1  . TYR   B 1 42  ? 47.910 -14.627 13.983  1.00 13.47 ?  42  TYR   B CD1  1 
ATOM   5055 C CD2  . TYR   B 1 42  ? 46.901 -16.666 14.674  1.00 15.96 ?  42  TYR   B CD2  1 
ATOM   5056 C CE1  . TYR   B 1 42  ? 47.384 -13.979 15.073  1.00 14.45 ?  42  TYR   B CE1  1 
ATOM   5057 C CE2  . TYR   B 1 42  ? 46.364 -16.019 15.778  1.00 16.29 ?  42  TYR   B CE2  1 
ATOM   5058 C CZ   . TYR   B 1 42  ? 46.611 -14.672 15.971  1.00 16.24 ?  42  TYR   B CZ   1 
ATOM   5059 O OH   . TYR   B 1 42  ? 46.093 -14.019 17.068  1.00 19.38 ?  42  TYR   B OH   1 
ATOM   5060 H H    . TYR   B 1 42  ? 46.581 -17.962 11.048  1.00 14.51 ?  42  TYR   B H    1 
ATOM   5061 H HA   . TYR   B 1 42  ? 47.256 -15.370 11.357  1.00 14.89 ?  42  TYR   B HA   1 
ATOM   5062 H HB2  . TYR   B 1 42  ? 48.187 -17.632 12.654  1.00 17.21 ?  42  TYR   B HB2  1 
ATOM   5063 H HB3  . TYR   B 1 42  ? 49.219 -16.438 12.473  1.00 17.21 ?  42  TYR   B HB3  1 
ATOM   5064 H HD1  . TYR   B 1 42  ? 48.440 -14.149 13.374  1.00 16.19 ?  42  TYR   B HD1  1 
ATOM   5065 H HD2  . TYR   B 1 42  ? 46.730 -17.571 14.538  1.00 19.18 ?  42  TYR   B HD2  1 
ATOM   5066 H HE1  . TYR   B 1 42  ? 47.558 -13.074 15.204  1.00 17.36 ?  42  TYR   B HE1  1 
ATOM   5067 H HE2  . TYR   B 1 42  ? 45.840 -16.493 16.381  1.00 19.57 ?  42  TYR   B HE2  1 
ATOM   5068 H HH   . TYR   B 1 42  ? 46.325 -13.220 17.057  1.00 23.29 ?  42  TYR   B HH   1 
ATOM   5069 N N    . LEU   B 1 43  ? 48.153 -16.717 8.882   1.00 10.87 ?  43  LEU   B N    1 
ATOM   5070 C CA   . LEU   B 1 43  ? 48.966 -16.651 7.670   1.00 10.86 ?  43  LEU   B CA   1 
ATOM   5071 C C    . LEU   B 1 43  ? 50.381 -17.161 7.927   1.00 11.06 ?  43  LEU   B C    1 
ATOM   5072 O O    . LEU   B 1 43  ? 51.363 -16.566 7.483   1.00 11.87 ?  43  LEU   B O    1 
ATOM   5073 C CB   . LEU   B 1 43  ? 48.981 -15.251 7.051   1.00 10.83 ?  43  LEU   B CB   1 
ATOM   5074 C CG   . LEU   B 1 43  ? 47.626 -14.639 6.692   1.00 11.06 ?  43  LEU   B CG   1 
ATOM   5075 C CD1  . LEU   B 1 43  ? 47.843 -13.258 6.121   1.00 12.31 ?  43  LEU   B CD1  1 
ATOM   5076 C CD2  . LEU   B 1 43  ? 46.851 -15.515 5.724   1.00 11.37 ?  43  LEU   B CD2  1 
ATOM   5077 H H    . LEU   B 1 43  ? 47.406 -17.131 8.771   1.00 13.07 ?  43  LEU   B H    1 
ATOM   5078 H HA   . LEU   B 1 43  ? 48.567 -17.247 7.013   1.00 13.06 ?  43  LEU   B HA   1 
ATOM   5079 H HB2  . LEU   B 1 43  ? 49.411 -14.650 7.671   1.00 13.03 ?  43  LEU   B HB2  1 
ATOM   5080 H HB3  . LEU   B 1 43  ? 49.499 -15.295 6.229   1.00 13.03 ?  43  LEU   B HB3  1 
ATOM   5081 H HG   . LEU   B 1 43  ? 47.098 -14.555 7.497   1.00 13.29 ?  43  LEU   B HG   1 
ATOM   5082 H HD11 . LEU   B 1 43  ? 46.983 -12.871 5.894   1.00 14.80 ?  43  LEU   B HD11 1 
ATOM   5083 H HD12 . LEU   B 1 43  ? 48.286 -12.710 6.790   1.00 14.80 ?  43  LEU   B HD12 1 
ATOM   5084 H HD13 . LEU   B 1 43  ? 48.397 -13.324 5.328   1.00 14.80 ?  43  LEU   B HD13 1 
ATOM   5085 H HD21 . LEU   B 1 43  ? 46.041 -15.052 5.456   1.00 13.67 ?  43  LEU   B HD21 1 
ATOM   5086 H HD22 . LEU   B 1 43  ? 47.401 -15.696 4.946   1.00 13.67 ?  43  LEU   B HD22 1 
ATOM   5087 H HD23 . LEU   B 1 43  ? 46.620 -16.351 6.164   1.00 13.67 ?  43  LEU   B HD23 1 
ATOM   5088 N N    . LYS   B 1 44  ? 50.483 -18.285 8.635   1.00 11.03 ?  44  LYS   B N    1 
ATOM   5089 C CA   . LYS   B 1 44  ? 51.753 -18.955 8.880   1.00 11.85 ?  44  LYS   B CA   1 
ATOM   5090 C C    . LYS   B 1 44  ? 51.875 -20.073 7.855   1.00 11.34 ?  44  LYS   B C    1 
ATOM   5091 O O    . LYS   B 1 44  ? 51.171 -21.084 7.938   1.00 12.72 ?  44  LYS   B O    1 
ATOM   5092 C CB   . LYS   B 1 44  ? 51.801 -19.471 10.316  1.00 13.49 ?  44  LYS   B CB   1 
ATOM   5093 C CG   . LYS   B 1 44  ? 52.000 -18.357 11.338  1.00 16.21 ?  44  LYS   B CG   1 
ATOM   5094 C CD   . LYS   B 1 44  ? 53.219 -17.510 10.952  1.00 19.54 ?  44  LYS   B CD   1 
ATOM   5095 C CE   . LYS   B 1 44  ? 53.736 -16.648 12.077  1.00 22.35 ?  44  LYS   B CE   1 
ATOM   5096 N NZ   . LYS   B 1 44  ? 54.872 -15.795 11.651  1.00 23.34 ?  44  LYS   B NZ   1 
ATOM   5097 H H    . LYS   B 1 44  ? 49.812 -18.679 8.997   1.00 13.27 ?  44  LYS   B H    1 
ATOM   5098 H HA   . LYS   B 1 44  ? 52.483 -18.339 8.720   1.00 14.25 ?  44  LYS   B HA   1 
ATOM   5099 H HB2  . LYS   B 1 44  ? 50.953 -19.911 10.515  1.00 16.22 ?  44  LYS   B HB2  1 
ATOM   5100 H HB3  . LYS   B 1 44  ? 52.527 -20.099 10.402  1.00 16.22 ?  44  LYS   B HB3  1 
ATOM   5101 H HG2  . LYS   B 1 44  ? 51.218 -17.789 11.360  1.00 19.48 ?  44  LYS   B HG2  1 
ATOM   5102 H HG3  . LYS   B 1 44  ? 52.163 -18.751 12.212  1.00 19.48 ?  44  LYS   B HG3  1 
ATOM   5103 H HD2  . LYS   B 1 44  ? 53.932 -18.106 10.657  1.00 23.47 ?  44  LYS   B HD2  1 
ATOM   5104 H HD3  . LYS   B 1 44  ? 52.965 -16.920 10.222  1.00 23.47 ?  44  LYS   B HD3  1 
ATOM   5105 H HE2  . LYS   B 1 44  ? 53.034 -16.051 12.345  1.00 26.84 ?  44  LYS   B HE2  1 
ATOM   5106 H HE3  . LYS   B 1 44  ? 54.020 -17.211 12.815  1.00 26.84 ?  44  LYS   B HE3  1 
ATOM   5107 H HZ1  . LYS   B 1 44  ? 55.149 -15.297 12.335  1.00 28.03 ?  44  LYS   B HZ1  1 
ATOM   5108 H HZ2  . LYS   B 1 44  ? 55.546 -16.297 11.366  1.00 28.03 ?  44  LYS   B HZ2  1 
ATOM   5109 H HZ3  . LYS   B 1 44  ? 54.614 -15.254 10.989  1.00 28.03 ?  44  LYS   B HZ3  1 
ATOM   5110 N N    . HIS   B 1 45  ? 52.721 -19.858 6.851   1.00 11.11 ?  45  HIS   B N    1 
ATOM   5111 C CA   . HIS   B 1 45  ? 52.728 -20.691 5.649   1.00 11.39 ?  45  HIS   B CA   1 
ATOM   5112 C C    . HIS   B 1 45  ? 53.739 -21.823 5.802   1.00 13.50 ?  45  HIS   B C    1 
ATOM   5113 O O    . HIS   B 1 45  ? 54.807 -21.837 5.199   1.00 16.16 ?  45  HIS   B O    1 
ATOM   5114 C CB   . HIS   B 1 45  ? 53.042 -19.839 4.432   1.00 11.47 ?  45  HIS   B CB   1 
ATOM   5115 C CG   . HIS   B 1 45  ? 52.177 -18.634 4.326   1.00 11.14 ?  45  HIS   B CG   1 
ATOM   5116 N ND1  . HIS   B 1 45  ? 50.800 -18.706 4.301   1.00 11.19 ?  45  HIS   B ND1  1 
ATOM   5117 C CD2  . HIS   B 1 45  ? 52.500 -17.324 4.249   1.00 11.85 ?  45  HIS   B CD2  1 
ATOM   5118 C CE1  . HIS   B 1 45  ? 50.319 -17.478 4.202   1.00 10.71 ?  45  HIS   B CE1  1 
ATOM   5119 N NE2  . HIS   B 1 45  ? 51.327 -16.622 4.168   1.00 11.37 ?  45  HIS   B NE2  1 
ATOM   5120 H H    . HIS   B 1 45  ? 53.296 -19.220 6.832   1.00 13.36 ?  45  HIS   B H    1 
ATOM   5121 H HA   . HIS   B 1 45  ? 51.848 -21.084 5.520   1.00 13.70 ?  45  HIS   B HA   1 
ATOM   5122 H HB2  . HIS   B 1 45  ? 53.963 -19.549 4.474   1.00 13.79 ?  45  HIS   B HB2  1 
ATOM   5123 H HB3  . HIS   B 1 45  ? 52.905 -20.377 3.626   1.00 13.79 ?  45  HIS   B HB3  1 
ATOM   5124 H HD2  . HIS   B 1 45  ? 53.359 -16.962 4.250   1.00 14.25 ?  45  HIS   B HD2  1 
ATOM   5125 H HE1  . HIS   B 1 45  ? 49.416 -17.246 4.161   1.00 12.87 ?  45  HIS   B HE1  1 
ATOM   5126 H HE2  . HIS   B 1 45  ? 51.257 -15.764 4.118   1.00 13.67 ?  45  HIS   B HE2  1 
ATOM   5127 N N    A GLY   B 1 46  ? 53.360 -22.802 6.615   0.42 14.40 ?  46  GLY   B N    1 
ATOM   5128 N N    B GLY   B 1 46  ? 53.366 -22.794 6.625   0.58 14.26 ?  46  GLY   B N    1 
ATOM   5129 C CA   A GLY   B 1 46  ? 54.282 -23.853 7.000   0.42 16.01 ?  46  GLY   B CA   1 
ATOM   5130 C CA   B GLY   B 1 46  ? 54.287 -23.855 6.983   0.58 15.93 ?  46  GLY   B CA   1 
ATOM   5131 C C    A GLY   B 1 46  ? 54.320 -25.083 6.113   0.42 17.80 ?  46  GLY   B C    1 
ATOM   5132 C C    B GLY   B 1 46  ? 54.316 -25.049 6.048   0.58 17.95 ?  46  GLY   B C    1 
ATOM   5133 O O    A GLY   B 1 46  ? 55.400 -25.532 5.717   0.42 19.94 ?  46  GLY   B O    1 
ATOM   5134 O O    B GLY   B 1 46  ? 55.378 -25.431 5.546   0.58 20.36 ?  46  GLY   B O    1 
ATOM   5135 H H    A GLY   B 1 46  ? 52.576 -22.868 6.966   0.42 17.30 ?  46  GLY   B H    1 
ATOM   5136 H H    B GLY   B 1 46  ? 52.590 -22.847 6.997   0.58 17.14 ?  46  GLY   B H    1 
ATOM   5137 H HA2  A GLY   B 1 46  ? 55.177 -23.479 7.032   0.42 19.23 ?  46  GLY   B HA2  1 
ATOM   5138 H HA2  B GLY   B 1 46  ? 55.183 -23.483 7.029   0.58 19.15 ?  46  GLY   B HA2  1 
ATOM   5139 H HA3  A GLY   B 1 46  ? 54.053 -24.147 7.895   0.42 19.23 ?  46  GLY   B HA3  1 
ATOM   5140 H HA3  B GLY   B 1 46  ? 54.054 -24.179 7.867   0.58 19.15 ?  46  GLY   B HA3  1 
ATOM   5141 N N    . GLY   B 1 47  ? 53.159 -25.661 5.805   1.00 17.63 ?  47  GLY   B N    1 
ATOM   5142 C CA   . GLY   B 1 47  ? 53.098 -26.937 5.119   1.00 15.40 ?  47  GLY   B CA   1 
ATOM   5143 C C    . GLY   B 1 47  ? 52.196 -26.910 3.899   1.00 13.22 ?  47  GLY   B C    1 
ATOM   5144 O O    . GLY   B 1 47  ? 51.560 -25.902 3.597   1.00 13.38 ?  47  GLY   B O    1 
ATOM   5145 H H    A GLY   B 1 47  ? 52.387 -25.333 6.004   0.42 21.18 ?  47  GLY   B H    1 
ATOM   5146 H H    B GLY   B 1 47  ? 52.389 -25.360 6.050   0.58 21.18 ?  47  GLY   B H    1 
ATOM   5147 H HA2  . GLY   B 1 47  ? 53.984 -27.195 4.829   1.00 18.50 ?  47  GLY   B HA2  1 
ATOM   5148 H HA3  . GLY   B 1 47  ? 52.769 -27.611 5.734   1.00 18.50 ?  47  GLY   B HA3  1 
ATOM   5149 N N    . GLY   B 1 48  ? 52.139 -28.054 3.221   1.00 12.40 ?  48  GLY   B N    1 
ATOM   5150 C CA   . GLY   B 1 48  ? 51.226 -28.196 2.103   1.00 12.16 ?  48  GLY   B CA   1 
ATOM   5151 C C    . GLY   B 1 48  ? 51.370 -27.080 1.094   1.00 11.92 ?  48  GLY   B C    1 
ATOM   5152 O O    . GLY   B 1 48  ? 52.476 -26.625 0.776   1.00 12.23 ?  48  GLY   B O    1 
ATOM   5153 H H    . GLY   B 1 48  ? 52.611 -28.750 3.391   1.00 14.90 ?  48  GLY   B H    1 
ATOM   5154 H HA2  . GLY   B 1 48  ? 51.395 -29.042 1.654   1.00 14.61 ?  48  GLY   B HA2  1 
ATOM   5155 H HA3  . GLY   B 1 48  ? 50.311 -28.201 2.424   1.00 14.61 ?  48  GLY   B HA3  1 
ATOM   5156 N N    . VAL   B 1 49  ? 50.226 -26.635 0.574   1.00 11.65 ?  49  VAL   B N    1 
ATOM   5157 C CA   . VAL   B 1 49  ? 50.215 -25.606 -0.463  1.00 11.54 ?  49  VAL   B CA   1 
ATOM   5158 C C    . VAL   B 1 49  ? 50.883 -24.321 0.029   1.00 10.63 ?  49  VAL   B C    1 
ATOM   5159 O O    . VAL   B 1 49  ? 51.682 -23.706 -0.689  1.00 11.60 ?  49  VAL   B O    1 
ATOM   5160 C CB   . VAL   B 1 49  ? 48.771 -25.348 -0.941  1.00 12.78 ?  49  VAL   B CB   1 
ATOM   5161 C CG1  . VAL   B 1 49  ? 48.698 -24.101 -1.812  1.00 13.05 ?  49  VAL   B CG1  1 
ATOM   5162 C CG2  . VAL   B 1 49  ? 48.236 -26.562 -1.688  1.00 13.84 ?  49  VAL   B CG2  1 
ATOM   5163 H H    . VAL   B 1 49  ? 49.440 -26.893 0.813   1.00 14.01 ?  49  VAL   B H    1 
ATOM   5164 H HA   . VAL   B 1 49  ? 50.721 -25.925 -1.224  1.00 13.87 ?  49  VAL   B HA   1 
ATOM   5165 H HB   . VAL   B 1 49  ? 48.205 -25.201 -0.169  1.00 15.36 ?  49  VAL   B HB   1 
ATOM   5166 H HG11 . VAL   B 1 49  ? 47.864 -24.110 -2.310  1.00 15.69 ?  49  VAL   B HG11 1 
ATOM   5167 H HG12 . VAL   B 1 49  ? 48.730 -23.312 -1.246  1.00 15.69 ?  49  VAL   B HG12 1 
ATOM   5168 H HG13 . VAL   B 1 49  ? 49.447 -24.097 -2.428  1.00 15.69 ?  49  VAL   B HG13 1 
ATOM   5169 H HG21 . VAL   B 1 49  ? 47.329 -26.379 -1.980  1.00 16.63 ?  49  VAL   B HG21 1 
ATOM   5170 H HG22 . VAL   B 1 49  ? 48.802 -26.733 -2.458  1.00 16.63 ?  49  VAL   B HG22 1 
ATOM   5171 H HG23 . VAL   B 1 49  ? 48.245 -27.326 -1.093  1.00 16.63 ?  49  VAL   B HG23 1 
ATOM   5172 N N    . ALA   B 1 50  ? 50.545 -23.882 1.244   1.00 10.51 ?  50  ALA   B N    1 
ATOM   5173 C CA   . ALA   B 1 50  ? 51.061 -22.605 1.733   1.00 10.36 ?  50  ALA   B CA   1 
ATOM   5174 C C    . ALA   B 1 50  ? 52.577 -22.636 1.838   1.00 10.52 ?  50  ALA   B C    1 
ATOM   5175 O O    . ALA   B 1 50  ? 53.261 -21.671 1.466   1.00 10.68 ?  50  ALA   B O    1 
ATOM   5176 C CB   . ALA   B 1 50  ? 50.433 -22.262 3.083   1.00 10.88 ?  50  ALA   B CB   1 
ATOM   5177 H H    . ALA   B 1 50  ? 50.037 -24.299 1.796   1.00 12.64 ?  50  ALA   B H    1 
ATOM   5178 H HA   . ALA   B 1 50  ? 50.827 -21.907 1.110   1.00 12.45 ?  50  ALA   B HA   1 
ATOM   5179 H HB1  . ALA   B 1 50  ? 50.784 -21.412 3.393   1.00 13.08 ?  50  ALA   B HB1  1 
ATOM   5180 H HB2  . ALA   B 1 50  ? 49.469 -22.201 2.978   1.00 13.08 ?  50  ALA   B HB2  1 
ATOM   5181 H HB3  . ALA   B 1 50  ? 50.648 -22.960 3.724   1.00 13.08 ?  50  ALA   B HB3  1 
ATOM   5182 N N    . GLY   B 1 51  ? 53.128 -23.740 2.340   1.00 11.31 ?  51  GLY   B N    1 
ATOM   5183 C CA   . GLY   B 1 51  ? 54.571 -23.853 2.407   1.00 12.34 ?  51  GLY   B CA   1 
ATOM   5184 C C    . GLY   B 1 51  ? 55.216 -23.793 1.037   1.00 11.82 ?  51  GLY   B C    1 
ATOM   5185 O O    . GLY   B 1 51  ? 56.260 -23.161 0.860   1.00 12.53 ?  51  GLY   B O    1 
ATOM   5186 H H    . GLY   B 1 51  ? 52.695 -24.422 2.645   1.00 13.60 ?  51  GLY   B H    1 
ATOM   5187 H HA2  . GLY   B 1 51  ? 54.928 -23.129 2.948   1.00 14.84 ?  51  GLY   B HA2  1 
ATOM   5188 H HA3  . GLY   B 1 51  ? 54.812 -24.695 2.830   1.00 14.84 ?  51  GLY   B HA3  1 
ATOM   5189 N N    . ALA   B 1 52  ? 54.609 -24.457 0.052   1.00 11.29 ?  52  ALA   B N    1 
ATOM   5190 C CA   . ALA   B 1 52  ? 55.176 -24.467 -1.289  1.00 11.54 ?  52  ALA   B CA   1 
ATOM   5191 C C    . ALA   B 1 52  ? 55.097 -23.086 -1.938  1.00 11.19 ?  52  ALA   B C    1 
ATOM   5192 O O    . ALA   B 1 52  ? 56.065 -22.630 -2.565  1.00 11.81 ?  52  ALA   B O    1 
ATOM   5193 C CB   . ALA   B 1 52  ? 54.461 -25.509 -2.140  1.00 12.32 ?  52  ALA   B CB   1 
ATOM   5194 H H    . ALA   B 1 52  ? 53.870 -24.897 0.137   1.00 13.57 ?  52  ALA   B H    1 
ATOM   5195 H HA   . ALA   B 1 52  ? 56.110 -24.720 -1.227  1.00 13.88 ?  52  ALA   B HA   1 
ATOM   5196 H HB1  . ALA   B 1 52  ? 54.852 -25.509 -3.028  1.00 14.81 ?  52  ALA   B HB1  1 
ATOM   5197 H HB2  . ALA   B 1 52  ? 54.576 -26.383 -1.730  1.00 14.81 ?  52  ALA   B HB2  1 
ATOM   5198 H HB3  . ALA   B 1 52  ? 53.521 -25.288 -2.189  1.00 14.81 ?  52  ALA   B HB3  1 
ATOM   5199 N N    . LEU   B 1 53  ? 53.956 -22.406 -1.812  1.00 10.81 ?  53  LEU   B N    1 
ATOM   5200 C CA   . LEU   B 1 53  ? 53.853 -21.063 -2.377  1.00 11.23 ?  53  LEU   B CA   1 
ATOM   5201 C C    . LEU   B 1 53  ? 54.865 -20.125 -1.728  1.00 10.97 ?  53  LEU   B C    1 
ATOM   5202 O O    . LEU   B 1 53  ? 55.573 -19.376 -2.414  1.00 11.63 ?  53  LEU   B O    1 
ATOM   5203 C CB   . LEU   B 1 53  ? 52.432 -20.515 -2.207  1.00 11.65 ?  53  LEU   B CB   1 
ATOM   5204 C CG   . LEU   B 1 53  ? 51.299 -21.231 -2.953  1.00 11.78 ?  53  LEU   B CG   1 
ATOM   5205 C CD1  . LEU   B 1 53  ? 49.950 -20.632 -2.582  1.00 12.86 ?  53  LEU   B CD1  1 
ATOM   5206 C CD2  . LEU   B 1 53  ? 51.497 -21.179 -4.463  1.00 13.52 ?  53  LEU   B CD2  1 
ATOM   5207 H H    . LEU   B 1 53  ? 53.254 -22.691 -1.407  1.00 13.00 ?  53  LEU   B H    1 
ATOM   5208 H HA   . LEU   B 1 53  ? 54.056 -21.111 -3.327  1.00 13.51 ?  53  LEU   B HA   1 
ATOM   5209 H HB2  . LEU   B 1 53  ? 52.216 -20.556 -1.264  1.00 14.01 ?  53  LEU   B HB2  1 
ATOM   5210 H HB3  . LEU   B 1 53  ? 52.432 -19.602 -2.505  1.00 14.01 ?  53  LEU   B HB3  1 
ATOM   5211 H HG   . LEU   B 1 53  ? 51.283 -22.168 -2.691  1.00 14.16 ?  53  LEU   B HG   1 
ATOM   5212 H HD11 . LEU   B 1 53  ? 49.247 -21.104 -3.063  1.00 15.46 ?  53  LEU   B HD11 1 
ATOM   5213 H HD12 . LEU   B 1 53  ? 49.809 -20.736 -1.624  1.00 15.46 ?  53  LEU   B HD12 1 
ATOM   5214 H HD13 . LEU   B 1 53  ? 49.940 -19.696 -2.818  1.00 15.46 ?  53  LEU   B HD13 1 
ATOM   5215 H HD21 . LEU   B 1 53  ? 50.836 -21.743 -4.892  1.00 16.26 ?  53  LEU   B HD21 1 
ATOM   5216 H HD22 . LEU   B 1 53  ? 51.387 -20.261 -4.762  1.00 16.26 ?  53  LEU   B HD22 1 
ATOM   5217 H HD23 . LEU   B 1 53  ? 52.388 -21.494 -4.681  1.00 16.26 ?  53  LEU   B HD23 1 
ATOM   5218 N N    . ASN   B 1 54  ? 54.953 -20.154 -0.401  1.00 10.80 ?  54  ASN   B N    1 
ATOM   5219 C CA   . ASN   B 1 54  ? 55.873 -19.243 0.268   1.00 11.22 ?  54  ASN   B CA   1 
ATOM   5220 C C    . ASN   B 1 54  ? 57.317 -19.528 -0.130  1.00 11.60 ?  54  ASN   B C    1 
ATOM   5221 O O    . ASN   B 1 54  ? 58.095 -18.595 -0.369  1.00 11.87 ?  54  ASN   B O    1 
ATOM   5222 C CB   . ASN   B 1 54  ? 55.708 -19.314 1.778   1.00 11.81 ?  54  ASN   B CB   1 
ATOM   5223 C CG   . ASN   B 1 54  ? 56.678 -18.399 2.487   1.00 11.92 ?  54  ASN   B CG   1 
ATOM   5224 O OD1  . ASN   B 1 54  ? 56.689 -17.196 2.238   1.00 12.12 ?  54  ASN   B OD1  1 
ATOM   5225 N ND2  . ASN   B 1 54  ? 57.523 -18.961 3.343   1.00 13.76 ?  54  ASN   B ND2  1 
ATOM   5226 H H    . ASN   B 1 54  ? 54.502 -20.668 0.119   1.00 12.98 ?  54  ASN   B H    1 
ATOM   5227 H HA   . ASN   B 1 54  ? 55.666 -18.335 -0.011  1.00 13.49 ?  54  ASN   B HA   1 
ATOM   5228 H HB2  . ASN   B 1 54  ? 54.807 -19.037 2.012   1.00 14.20 ?  54  ASN   B HB2  1 
ATOM   5229 H HB3  . ASN   B 1 54  ? 55.871 -20.218 2.076   1.00 14.20 ?  54  ASN   B HB3  1 
ATOM   5230 H HD21 . ASN   B 1 54  ? 58.097 -18.477 3.761   1.00 16.54 ?  54  ASN   B HD21 1 
ATOM   5231 H HD22 . ASN   B 1 54  ? 57.495 -19.810 3.480   1.00 16.54 ?  54  ASN   B HD22 1 
ATOM   5232 N N    . LYS   B 1 55  ? 57.696 -20.807 -0.196  1.00 12.33 ?  55  LYS   B N    1 
ATOM   5233 C CA   . LYS   B 1 55  ? 59.047 -21.158 -0.618  1.00 12.93 ?  55  LYS   B CA   1 
ATOM   5234 C C    . LYS   B 1 55  ? 59.346 -20.609 -2.007  1.00 12.96 ?  55  LYS   B C    1 
ATOM   5235 O O    . LYS   B 1 55  ? 60.450 -20.109 -2.259  1.00 13.49 ?  55  LYS   B O    1 
ATOM   5236 C CB   . LYS   B 1 55  ? 59.223 -22.678 -0.569  1.00 14.18 ?  55  LYS   B CB   1 
ATOM   5237 C CG   . LYS   B 1 55  ? 60.593 -23.160 -0.997  1.00 18.47 ?  55  LYS   B CG   1 
ATOM   5238 C CD   . LYS   B 1 55  ? 60.754 -24.659 -0.789  1.00 22.09 ?  55  LYS   B CD   1 
ATOM   5239 C CE   . LYS   B 1 55  ? 60.806 -25.024 0.695   1.00 25.09 ?  55  LYS   B CE   1 
ATOM   5240 N NZ   . LYS   B 1 55  ? 61.173 -26.443 0.920   1.00 26.63 ?  55  LYS   B NZ   1 
ATOM   5241 H H    . LYS   B 1 55  ? 57.194 -21.477 -0.003  1.00 14.83 ?  55  LYS   B H    1 
ATOM   5242 H HA   . LYS   B 1 55  ? 59.683 -20.766 -0.003  1.00 15.54 ?  55  LYS   B HA   1 
ATOM   5243 H HB2  . LYS   B 1 55  ? 59.071 -22.973 0.343   1.00 17.05 ?  55  LYS   B HB2  1 
ATOM   5244 H HB3  . LYS   B 1 55  ? 58.567 -23.086 -1.157  1.00 17.05 ?  55  LYS   B HB3  1 
ATOM   5245 H HG2  . LYS   B 1 55  ? 60.718 -22.970 -1.941  1.00 22.20 ?  55  LYS   B HG2  1 
ATOM   5246 H HG3  . LYS   B 1 55  ? 61.270 -22.703 -0.473  1.00 22.20 ?  55  LYS   B HG3  1 
ATOM   5247 H HD2  . LYS   B 1 55  ? 60.001 -25.121 -1.189  1.00 26.53 ?  55  LYS   B HD2  1 
ATOM   5248 H HD3  . LYS   B 1 55  ? 61.584 -24.952 -1.199  1.00 26.53 ?  55  LYS   B HD3  1 
ATOM   5249 H HE2  . LYS   B 1 55  ? 61.465 -24.459 1.133   1.00 30.13 ?  55  LYS   B HE2  1 
ATOM   5250 H HE3  . LYS   B 1 55  ? 59.929 -24.869 1.086   1.00 30.13 ?  55  LYS   B HE3  1 
ATOM   5251 H HZ1  . LYS   B 1 55  ? 61.180 -26.617 1.793   1.00 31.98 ?  55  LYS   B HZ1  1 
ATOM   5252 H HZ2  . LYS   B 1 55  ? 60.579 -26.975 0.524   1.00 31.98 ?  55  LYS   B HZ2  1 
ATOM   5253 H HZ3  . LYS   B 1 55  ? 61.979 -26.604 0.585   1.00 31.98 ?  55  LYS   B HZ3  1 
ATOM   5254 N N    . ALA   B 1 56  ? 58.371 -20.684 -2.922  1.00 12.87 ?  56  ALA   B N    1 
ATOM   5255 C CA   . ALA   B 1 56  ? 58.596 -20.187 -4.274  1.00 13.33 ?  56  ALA   B CA   1 
ATOM   5256 C C    . ALA   B 1 56  ? 58.877 -18.691 -4.275  1.00 12.72 ?  56  ALA   B C    1 
ATOM   5257 O O    . ALA   B 1 56  ? 59.607 -18.194 -5.146  1.00 13.89 ?  56  ALA   B O    1 
ATOM   5258 C CB   . ALA   B 1 56  ? 57.398 -20.527 -5.161  1.00 14.29 ?  56  ALA   B CB   1 
ATOM   5259 H H    . ALA   B 1 56  ? 57.581 -21.008 -2.781  1.00 15.48 ?  56  ALA   B H    1 
ATOM   5260 H HA   . ALA   B 1 56  ? 59.371 -20.628 -4.642  1.00 16.02 ?  56  ALA   B HA   1 
ATOM   5261 H HB1  . ALA   B 1 56  ? 57.565 -20.197 -6.059  1.00 17.18 ?  56  ALA   B HB1  1 
ATOM   5262 H HB2  . ALA   B 1 56  ? 57.287 -21.493 -5.184  1.00 17.18 ?  56  ALA   B HB2  1 
ATOM   5263 H HB3  . ALA   B 1 56  ? 56.601 -20.113 -4.799  1.00 17.18 ?  56  ALA   B HB3  1 
ATOM   5264 N N    . THR   B 1 57  ? 58.303 -17.959 -3.314  1.00 12.74 ?  57  THR   B N    1 
ATOM   5265 C CA   . THR   B 1 57  ? 58.546 -16.526 -3.177  1.00 12.70 ?  57  THR   B CA   1 
ATOM   5266 C C    . THR   B 1 57  ? 59.800 -16.202 -2.374  1.00 13.59 ?  57  THR   B C    1 
ATOM   5267 O O    . THR   B 1 57  ? 60.040 -15.028 -2.081  1.00 14.00 ?  57  THR   B O    1 
ATOM   5268 C CB   . THR   B 1 57  ? 57.345 -15.802 -2.536  1.00 12.40 ?  57  THR   B CB   1 
ATOM   5269 O OG1  . THR   B 1 57  ? 57.324 -16.009 -1.114  1.00 11.96 ?  57  THR   B OG1  1 
ATOM   5270 C CG2  . THR   B 1 57  ? 56.028 -16.233 -3.171  1.00 12.52 ?  57  THR   B CG2  1 
ATOM   5271 H H    . THR   B 1 57  ? 57.757 -18.275 -2.720  1.00 15.31 ?  57  THR   B H    1 
ATOM   5272 H HA   . THR   B 1 57  ? 58.660 -16.153 -4.063  1.00 15.27 ?  57  THR   B HA   1 
ATOM   5273 H HB   . THR   B 1 57  ? 57.441 -14.850 -2.703  1.00 14.91 ?  57  THR   B HB   1 
ATOM   5274 H HG1  . THR   B 1 57  ? 57.264 -16.829 -0.944  1.00 14.38 ?  57  THR   B HG1  1 
ATOM   5275 H HG21 . THR   B 1 57  ? 55.309 -15.652 -2.883  1.00 15.05 ?  57  THR   B HG21 1 
ATOM   5276 H HG22 . THR   B 1 57  ? 56.095 -16.198 -4.139  1.00 15.05 ?  57  THR   B HG22 1 
ATOM   5277 H HG23 . THR   B 1 57  ? 55.816 -17.145 -2.910  1.00 15.05 ?  57  THR   B HG23 1 
ATOM   5278 N N    . ASN   B 1 58  ? 60.596 -17.204 -2.007  1.00 14.72 ?  58  ASN   B N    1 
ATOM   5279 C CA   . ASN   B 1 58  ? 61.794 -16.987 -1.197  1.00 16.73 ?  58  ASN   B CA   1 
ATOM   5280 C C    . ASN   B 1 58  ? 61.456 -16.270 0.109   1.00 14.49 ?  58  ASN   B C    1 
ATOM   5281 O O    . ASN   B 1 58  ? 62.185 -15.384 0.565   1.00 15.04 ?  58  ASN   B O    1 
ATOM   5282 C CB   . ASN   B 1 58  ? 62.879 -16.238 -1.975  1.00 23.61 ?  58  ASN   B CB   1 
ATOM   5283 C CG   . ASN   B 1 58  ? 64.245 -16.355 -1.324  1.00 32.80 ?  58  ASN   B CG   1 
ATOM   5284 O OD1  . ASN   B 1 58  ? 64.569 -17.375 -0.715  1.00 36.44 ?  58  ASN   B OD1  1 
ATOM   5285 N ND2  . ASN   B 1 58  ? 65.050 -15.306 -1.444  1.00 35.26 ?  58  ASN   B ND2  1 
ATOM   5286 H H    . ASN   B 1 58  ? 60.456 -18.029 -2.205  1.00 17.70 ?  58  ASN   B H    1 
ATOM   5287 H HA   . ASN   B 1 58  ? 62.156 -17.854 -0.964  1.00 20.11 ?  58  ASN   B HA   1 
ATOM   5288 H HB2  . ASN   B 1 58  ? 62.939 -16.608 -2.870  1.00 28.37 ?  58  ASN   B HB2  1 
ATOM   5289 H HB3  . ASN   B 1 58  ? 62.647 -15.297 -2.019  1.00 28.37 ?  58  ASN   B HB3  1 
ATOM   5290 H HD21 . ASN   B 1 58  ? 65.835 -15.323 -1.091  1.00 42.34 ?  58  ASN   B HD21 1 
ATOM   5291 H HD22 . ASN   B 1 58  ? 64.789 -14.609 -1.875  1.00 42.34 ?  58  ASN   B HD22 1 
ATOM   5292 N N    . ASN   B 1 59  ? 60.336 -16.660 0.717   1.00 13.60 ?  59  ASN   B N    1 
ATOM   5293 C CA   . ASN   B 1 59  ? 59.855 -16.191 2.013   1.00 13.17 ?  59  ASN   B CA   1 
ATOM   5294 C C    . ASN   B 1 59  ? 59.259 -14.784 1.950   1.00 12.55 ?  59  ASN   B C    1 
ATOM   5295 O O    . ASN   B 1 59  ? 58.825 -14.272 2.985   1.00 12.71 ?  59  ASN   B O    1 
ATOM   5296 C CB   . ASN   B 1 59  ? 60.927 -16.258 3.115   1.00 14.52 ?  59  ASN   B CB   1 
ATOM   5297 C CG   . ASN   B 1 59  ? 60.342 -16.417 4.494   1.00 15.17 ?  59  ASN   B CG   1 
ATOM   5298 O OD1  . ASN   B 1 59  ? 59.495 -17.279 4.723   1.00 15.64 ?  59  ASN   B OD1  1 
ATOM   5299 N ND2  . ASN   B 1 59  ? 60.782 -15.583 5.425   1.00 15.67 ?  59  ASN   B ND2  1 
ATOM   5300 H H    . ASN   B 1 59  ? 59.803 -17.243 0.375   1.00 16.35 ?  59  ASN   B H    1 
ATOM   5301 H HA   . ASN   B 1 59  ? 59.142 -16.786 2.296   1.00 15.83 ?  59  ASN   B HA   1 
ATOM   5302 H HB2  . ASN   B 1 59  ? 61.505 -17.023 2.958   1.00 17.46 ?  59  ASN   B HB2  1 
ATOM   5303 H HB3  . ASN   B 1 59  ? 61.446 -15.443 3.113   1.00 17.46 ?  59  ASN   B HB3  1 
ATOM   5304 H HD21 . ASN   B 1 59  ? 60.473 -15.629 6.230   1.00 18.83 ?  59  ASN   B HD21 1 
ATOM   5305 H HD22 . ASN   B 1 59  ? 61.367 -14.986 5.226   1.00 18.83 ?  59  ASN   B HD22 1 
ATOM   5306 N N    . ALA   B 1 60  ? 59.201 -14.146 0.779   1.00 12.54 ?  60  ALA   B N    1 
ATOM   5307 C CA   . ALA   B 1 60  ? 58.613 -12.810 0.702   1.00 12.85 ?  60  ALA   B CA   1 
ATOM   5308 C C    . ALA   B 1 60  ? 57.144 -12.825 1.103   1.00 12.15 ?  60  ALA   B C    1 
ATOM   5309 O O    . ALA   B 1 60  ? 56.640 -11.860 1.694   1.00 12.91 ?  60  ALA   B O    1 
ATOM   5310 C CB   . ALA   B 1 60  ? 58.765 -12.245 -0.708  1.00 14.08 ?  60  ALA   B CB   1 
ATOM   5311 H H    . ALA   B 1 60  ? 59.491 -14.462 0.038   1.00 15.08 ?  60  ALA   B H    1 
ATOM   5312 H HA   . ALA   B 1 60  ? 59.087 -12.225 1.314   1.00 15.45 ?  60  ALA   B HA   1 
ATOM   5313 H HB1  . ALA   B 1 60  ? 58.366 -11.364 -0.735  1.00 16.93 ?  60  ALA   B HB1  1 
ATOM   5314 H HB2  . ALA   B 1 60  ? 59.705 -12.197 -0.929  1.00 16.93 ?  60  ALA   B HB2  1 
ATOM   5315 H HB3  . ALA   B 1 60  ? 58.306 -12.836 -1.331  1.00 16.93 ?  60  ALA   B HB3  1 
ATOM   5316 N N    . MET   B 1 61  ? 56.431 -13.897 0.754   1.00 11.78 ?  61  MET   B N    1 
ATOM   5317 C CA   . MET   B 1 61  ? 55.037 -14.025 1.154   1.00 11.01 ?  61  MET   B CA   1 
ATOM   5318 C C    . MET   B 1 61  ? 54.898 -14.032 2.672   1.00 11.05 ?  61  MET   B C    1 
ATOM   5319 O O    . MET   B 1 61  ? 54.003 -13.377 3.218   1.00 10.97 ?  61  MET   B O    1 
ATOM   5320 C CB   . MET   B 1 61  ? 54.447 -15.291 0.528   1.00 10.69 ?  61  MET   B CB   1 
ATOM   5321 C CG   . MET   B 1 61  ? 53.014 -15.587 0.943   1.00 10.85 ?  61  MET   B CG   1 
ATOM   5322 S SD   . MET   B 1 61  ? 52.364 -17.081 0.174   1.00 11.54 ?  61  MET   B SD   1 
ATOM   5323 C CE   . MET   B 1 61  ? 52.126 -16.486 -1.494  1.00 12.91 ?  61  MET   B CE   1 
ATOM   5324 H H    . MET   B 1 61  ? 56.732 -14.558 0.288   1.00 14.16 ?  61  MET   B H    1 
ATOM   5325 H HA   . MET   B 1 61  ? 54.544 -13.271 0.799   1.00 13.24 ?  61  MET   B HA   1 
ATOM   5326 H HB2  . MET   B 1 61  ? 54.453 -15.197 -0.437  1.00 12.86 ?  61  MET   B HB2  1 
ATOM   5327 H HB3  . MET   B 1 61  ? 54.989 -16.052 0.786   1.00 12.86 ?  61  MET   B HB3  1 
ATOM   5328 H HG2  . MET   B 1 61  ? 52.983 -15.715 1.907   1.00 13.04 ?  61  MET   B HG2  1 
ATOM   5329 H HG3  . MET   B 1 61  ? 52.450 -14.845 0.688   1.00 13.04 ?  61  MET   B HG3  1 
ATOM   5330 H HE1  . MET   B 1 61  ? 51.724 -17.188 -2.022  1.00 15.52 ?  61  MET   B HE1  1 
ATOM   5331 H HE2  . MET   B 1 61  ? 51.548 -15.709 -1.469  1.00 15.52 ?  61  MET   B HE2  1 
ATOM   5332 H HE3  . MET   B 1 61  ? 52.991 -16.243 -1.866  1.00 15.52 ?  61  MET   B HE3  1 
ATOM   5333 N N    . GLN   B 1 62  ? 55.771 -14.752 3.378   1.00 11.03 ?  62  GLN   B N    1 
ATOM   5334 C CA   . GLN   B 1 62  ? 55.663 -14.800 4.833   1.00 11.45 ?  62  GLN   B CA   1 
ATOM   5335 C C    . GLN   B 1 62  ? 55.949 -13.442 5.458   1.00 11.26 ?  62  GLN   B C    1 
ATOM   5336 O O    . GLN   B 1 62  ? 55.273 -13.039 6.409   1.00 11.87 ?  62  GLN   B O    1 
ATOM   5337 C CB   . GLN   B 1 62  ? 56.617 -15.847 5.403   1.00 11.92 ?  62  GLN   B CB   1 
ATOM   5338 C CG   . GLN   B 1 62  ? 56.388 -16.123 6.876   1.00 12.06 ?  62  GLN   B CG   1 
ATOM   5339 C CD   . GLN   B 1 62  ? 55.010 -16.710 7.108   1.00 11.48 ?  62  GLN   B CD   1 
ATOM   5340 O OE1  . GLN   B 1 62  ? 54.753 -17.853 6.741   1.00 12.10 ?  62  GLN   B OE1  1 
ATOM   5341 N NE2  . GLN   B 1 62  ? 54.101 -15.918 7.667   1.00 11.82 ?  62  GLN   B NE2  1 
ATOM   5342 H H    . GLN   B 1 62  ? 56.411 -15.215 3.040   1.00 13.27 ?  62  GLN   B H    1 
ATOM   5343 H HA   . GLN   B 1 62  ? 54.758 -15.055 5.069   1.00 13.77 ?  62  GLN   B HA   1 
ATOM   5344 H HB2  . GLN   B 1 62  ? 56.500 -16.680 4.916   1.00 14.33 ?  62  GLN   B HB2  1 
ATOM   5345 H HB3  . GLN   B 1 62  ? 57.529 -15.531 5.297   1.00 14.33 ?  62  GLN   B HB3  1 
ATOM   5346 H HG2  . GLN   B 1 62  ? 57.047 -16.770 7.183   1.00 14.50 ?  62  GLN   B HG2  1 
ATOM   5347 H HG3  . GLN   B 1 62  ? 56.459 -15.303 7.376   1.00 14.50 ?  62  GLN   B HG3  1 
ATOM   5348 H HE21 . GLN   B 1 62  ? 54.311 -15.117 7.896   1.00 14.21 ?  62  GLN   B HE21 1 
ATOM   5349 H HE22 . GLN   B 1 62  ? 53.303 -16.210 7.806   1.00 14.21 ?  62  GLN   B HE22 1 
ATOM   5350 N N    . VAL   B 1 63  ? 56.965 -12.730 4.964   1.00 11.89 ?  63  VAL   B N    1 
ATOM   5351 C CA   . VAL   B 1 63  ? 57.271 -11.410 5.516   1.00 12.81 ?  63  VAL   B CA   1 
ATOM   5352 C C    . VAL   B 1 63  ? 56.076 -10.477 5.335   1.00 12.01 ?  63  VAL   B C    1 
ATOM   5353 O O    . VAL   B 1 63  ? 55.660 -9.774  6.265   1.00 12.46 ?  63  VAL   B O    1 
ATOM   5354 C CB   . VAL   B 1 63  ? 58.556 -10.848 4.885   1.00 13.85 ?  63  VAL   B CB   1 
ATOM   5355 C CG1  . VAL   B 1 63  ? 58.781 -9.412  5.335   1.00 14.54 ?  63  VAL   B CG1  1 
ATOM   5356 C CG2  . VAL   B 1 63  ? 59.747 -11.724 5.261   1.00 14.49 ?  63  VAL   B CG2  1 
ATOM   5357 H H    . VAL   B 1 63  ? 57.484 -12.990 4.322   1.00 14.30 ?  63  VAL   B H    1 
ATOM   5358 H HA   . VAL   B 1 63  ? 57.432 -11.509 6.465   1.00 15.40 ?  63  VAL   B HA   1 
ATOM   5359 H HB   . VAL   B 1 63  ? 58.475 -10.858 3.920   1.00 16.65 ?  63  VAL   B HB   1 
ATOM   5360 H HG11 . VAL   B 1 63  ? 59.696 -9.162  5.146   1.00 17.48 ?  63  VAL   B HG11 1 
ATOM   5361 H HG12 . VAL   B 1 63  ? 58.171 -8.833  4.853   1.00 17.48 ?  63  VAL   B HG12 1 
ATOM   5362 H HG13 . VAL   B 1 63  ? 58.612 -9.353  6.290   1.00 17.48 ?  63  VAL   B HG13 1 
ATOM   5363 H HG21 . VAL   B 1 63  ? 60.555 -11.343 4.879   1.00 17.42 ?  63  VAL   B HG21 1 
ATOM   5364 H HG22 . VAL   B 1 63  ? 59.826 -11.753 6.230   1.00 17.42 ?  63  VAL   B HG22 1 
ATOM   5365 H HG23 . VAL   B 1 63  ? 59.609 -12.618 4.915   1.00 17.42 ?  63  VAL   B HG23 1 
ATOM   5366 N N    . GLU   B 1 64  ? 55.507 -10.463 4.130   1.00 11.56 ?  64  GLU   B N    1 
ATOM   5367 C CA   . GLU   B 1 64  ? 54.338 -9.633  3.856   1.00 11.33 ?  64  GLU   B CA   1 
ATOM   5368 C C    . GLU   B 1 64  ? 53.158 -10.036 4.734   1.00 11.17 ?  64  GLU   B C    1 
ATOM   5369 O O    . GLU   B 1 64  ? 52.416 -9.178  5.236   1.00 11.77 ?  64  GLU   B O    1 
ATOM   5370 C CB   . GLU   B 1 64  ? 53.974 -9.785  2.380   1.00 11.38 ?  64  GLU   B CB   1 
ATOM   5371 C CG   . GLU   B 1 64  ? 52.709 -9.060  1.952   1.00 11.72 ?  64  GLU   B CG   1 
ATOM   5372 C CD   . GLU   B 1 64  ? 52.181 -9.553  0.618   1.00 12.42 ?  64  GLU   B CD   1 
ATOM   5373 O OE1  . GLU   B 1 64  ? 52.364 -10.756 0.296   1.00 12.99 ?  64  GLU   B OE1  1 
ATOM   5374 O OE2  . GLU   B 1 64  ? 51.561 -8.733  -0.099  1.00 13.50 -1 64  GLU   B OE2  1 
ATOM   5375 H H    . GLU   B 1 64  ? 55.786 -10.919 3.452   1.00 13.90 ?  64  GLU   B H    1 
ATOM   5376 H HA   . GLU   B 1 64  ? 54.549 -8.703  4.029   1.00 13.63 ?  64  GLU   B HA   1 
ATOM   5377 H HB2  . GLU   B 1 64  ? 54.703 -9.429  1.841   1.00 13.68 ?  64  GLU   B HB2  1 
ATOM   5378 H HB3  . GLU   B 1 64  ? 53.857 -10.725 2.183   1.00 13.68 ?  64  GLU   B HB3  1 
ATOM   5379 H HG2  . GLU   B 1 64  ? 52.011 -9.205  2.615   1.00 14.09 ?  64  GLU   B HG2  1 
ATOM   5380 H HG3  . GLU   B 1 64  ? 52.897 -8.115  1.874   1.00 14.09 ?  64  GLU   B HG3  1 
ATOM   5381 N N    . SER   B 1 65  ? 52.972 -11.341 4.921   1.00 10.90 ?  65  SER   B N    1 
ATOM   5382 C CA   . SER   B 1 65  ? 51.862 -11.842 5.721   1.00 11.08 ?  65  SER   B CA   1 
ATOM   5383 C C    . SER   B 1 65  ? 51.992 -11.443 7.182   1.00 10.96 ?  65  SER   B C    1 
ATOM   5384 O O    . SER   B 1 65  ? 50.997 -11.074 7.817   1.00 11.54 ?  65  SER   B O    1 
ATOM   5385 C CB   . SER   B 1 65  ? 51.781 -13.365 5.594   1.00 11.53 ?  65  SER   B CB   1 
ATOM   5386 O OG   . SER   B 1 65  ? 51.443 -13.762 4.272   1.00 11.38 ?  65  SER   B OG   1 
ATOM   5387 H H    . SER   B 1 65  ? 53.478 -11.964 4.595   1.00 13.11 ?  65  SER   B H    1 
ATOM   5388 H HA   . SER   B 1 65  ? 51.032 -11.475 5.376   1.00 13.33 ?  65  SER   B HA   1 
ATOM   5389 H HB2  . SER   B 1 65  ? 52.636 -13.751 5.827   1.00 13.87 ?  65  SER   B HB2  1 
ATOM   5390 H HB3  . SER   B 1 65  ? 51.094 -13.696 6.199   1.00 13.87 ?  65  SER   B HB3  1 
ATOM   5391 H HG   . SER   B 1 65  ? 52.029 -13.482 3.730   1.00 13.69 ?  65  SER   B HG   1 
ATOM   5392 N N    . ASP   B 1 66  ? 53.199 -11.542 7.743   1.00 11.66 ?  66  ASP   B N    1 
ATOM   5393 C CA   . ASP   B 1 66  ? 53.391 -11.150 9.135   1.00 12.08 ?  66  ASP   B CA   1 
ATOM   5394 C C    . ASP   B 1 66  ? 53.069 -9.675  9.329   1.00 11.77 ?  66  ASP   B C    1 
ATOM   5395 O O    . ASP   B 1 66  ? 52.492 -9.284  10.350  1.00 12.51 ?  66  ASP   B O    1 
ATOM   5396 C CB   . ASP   B 1 66  ? 54.826 -11.448 9.577   1.00 12.89 ?  66  ASP   B CB   1 
ATOM   5397 C CG   . ASP   B 1 66  ? 55.102 -12.934 9.747   1.00 14.66 ?  66  ASP   B CG   1 
ATOM   5398 O OD1  . ASP   B 1 66  ? 54.150 -13.747 9.677   1.00 15.11 ?  66  ASP   B OD1  1 
ATOM   5399 O OD2  . ASP   B 1 66  ? 56.287 -13.283 9.956   1.00 17.23 -1 66  ASP   B OD2  1 
ATOM   5400 H H    . ASP   B 1 66  ? 53.904 -11.838 7.349   1.00 14.03 ?  66  ASP   B H    1 
ATOM   5401 H HA   . ASP   B 1 66  ? 52.790 -11.660 9.697   1.00 14.52 ?  66  ASP   B HA   1 
ATOM   5402 H HB2  . ASP   B 1 66  ? 55.440 -11.111 8.907   1.00 15.50 ?  66  ASP   B HB2  1 
ATOM   5403 H HB3  . ASP   B 1 66  ? 54.992 -11.010 10.428  1.00 15.50 ?  66  ASP   B HB3  1 
ATOM   5404 N N    . ASP   B 1 67  ? 53.438 -8.833  8.362   1.00 11.65 ?  67  ASP   B N    1 
ATOM   5405 C CA   . ASP   B 1 67  ? 53.091 -7.422  8.446   1.00 12.23 ?  67  ASP   B CA   1 
ATOM   5406 C C    . ASP   B 1 67  ? 51.580 -7.215  8.365   1.00 12.25 ?  67  ASP   B C    1 
ATOM   5407 O O    . ASP   B 1 67  ? 51.019 -6.400  9.111   1.00 12.90 ?  67  ASP   B O    1 
ATOM   5408 C CB   . ASP   B 1 67  ? 53.813 -6.657  7.342   1.00 13.27 ?  67  ASP   B CB   1 
ATOM   5409 C CG   . ASP   B 1 67  ? 53.383 -5.216  7.281   1.00 14.51 ?  67  ASP   B CG   1 
ATOM   5410 O OD1  . ASP   B 1 67  ? 53.898 -4.391  8.067   1.00 15.70 ?  67  ASP   B OD1  1 
ATOM   5411 O OD2  . ASP   B 1 67  ? 52.489 -4.924  6.466   1.00 15.81 -1 67  ASP   B OD2  1 
ATOM   5412 H H    . ASP   B 1 67  ? 53.894 -9.053  7.665   1.00 14.00 ?  67  ASP   B H    1 
ATOM   5413 H HA   . ASP   B 1 67  ? 53.399 -7.069  9.297   1.00 14.70 ?  67  ASP   B HA   1 
ATOM   5414 H HB2  . ASP   B 1 67  ? 54.768 -6.681  7.505   1.00 15.95 ?  67  ASP   B HB2  1 
ATOM   5415 H HB3  . ASP   B 1 67  ? 53.613 -7.072  6.485   1.00 15.95 ?  67  ASP   B HB3  1 
ATOM   5416 N N    . TYR   B 1 68  ? 50.904 -7.950  7.476   1.00 11.98 ?  68  TYR   B N    1 
ATOM   5417 C CA   . TYR   B 1 68  ? 49.446 -7.881  7.400   1.00 12.48 ?  68  TYR   B CA   1 
ATOM   5418 C C    . TYR   B 1 68  ? 48.810 -8.216  8.746   1.00 12.26 ?  68  TYR   B C    1 
ATOM   5419 O O    . TYR   B 1 68  ? 47.882 -7.530  9.196   1.00 12.68 ?  68  TYR   B O    1 
ATOM   5420 C CB   . TYR   B 1 68  ? 48.914 -8.828  6.316   1.00 13.18 ?  68  TYR   B CB   1 
ATOM   5421 C CG   . TYR   B 1 68  ? 47.403 -8.973  6.372   1.00 14.52 ?  68  TYR   B CG   1 
ATOM   5422 C CD1  . TYR   B 1 68  ? 46.811 -9.915  7.208   1.00 14.88 ?  68  TYR   B CD1  1 
ATOM   5423 C CD2  . TYR   B 1 68  ? 46.574 -8.148  5.632   1.00 15.66 ?  68  TYR   B CD2  1 
ATOM   5424 C CE1  . TYR   B 1 68  ? 45.446 -10.034 7.304   1.00 16.04 ?  68  TYR   B CE1  1 
ATOM   5425 C CE2  . TYR   B 1 68  ? 45.191 -8.274  5.711   1.00 15.64 ?  68  TYR   B CE2  1 
ATOM   5426 C CZ   . TYR   B 1 68  ? 44.647 -9.212  6.556   1.00 15.99 ?  68  TYR   B CZ   1 
ATOM   5427 O OH   . TYR   B 1 68  ? 43.278 -9.322  6.652   1.00 16.60 ?  68  TYR   B OH   1 
ATOM   5428 H H    . TYR   B 1 68  ? 51.267 -8.495  6.913   1.00 14.40 ?  68  TYR   B H    1 
ATOM   5429 H HA   . TYR   B 1 68  ? 49.190 -6.979  7.165   1.00 15.01 ?  68  TYR   B HA   1 
ATOM   5430 H HB2  . TYR   B 1 68  ? 49.150 -8.474  5.447   1.00 15.84 ?  68  TYR   B HB2  1 
ATOM   5431 H HB3  . TYR   B 1 68  ? 49.309 -9.705  6.442   1.00 15.84 ?  68  TYR   B HB3  1 
ATOM   5432 H HD1  . TYR   B 1 68  ? 47.350 -10.475 7.722   1.00 17.88 ?  68  TYR   B HD1  1 
ATOM   5433 H HD2  . TYR   B 1 68  ? 46.946 -7.506  5.079   1.00 18.82 ?  68  TYR   B HD2  1 
ATOM   5434 H HE1  . TYR   B 1 68  ? 45.063 -10.683 7.857   1.00 19.27 ?  68  TYR   B HE1  1 
ATOM   5435 H HE2  . TYR   B 1 68  ? 44.633 -7.717  5.214   1.00 18.80 ?  68  TYR   B HE2  1 
ATOM   5436 H HH   . TYR   B 1 68  ? 42.897 -8.778  6.127   1.00 19.94 ?  68  TYR   B HH   1 
ATOM   5437 N N    . ILE   B 1 69  ? 49.291 -9.281  9.395   1.00 11.84 ?  69  ILE   B N    1 
ATOM   5438 C CA   . ILE   B 1 69  ? 48.738 -9.703  10.680  1.00 12.16 ?  69  ILE   B CA   1 
ATOM   5439 C C    . ILE   B 1 69  ? 48.986 -8.649  11.750  1.00 12.19 ?  69  ILE   B C    1 
ATOM   5440 O O    . ILE   B 1 69  ? 48.120 -8.378  12.588  1.00 12.60 ?  69  ILE   B O    1 
ATOM   5441 C CB   . ILE   B 1 69  ? 49.321 -11.071 11.083  1.00 13.03 ?  69  ILE   B CB   1 
ATOM   5442 C CG1  . ILE   B 1 69  ? 48.803 -12.185 10.164  1.00 13.71 ?  69  ILE   B CG1  1 
ATOM   5443 C CG2  . ILE   B 1 69  ? 49.033 -11.383 12.546  1.00 13.91 ?  69  ILE   B CG2  1 
ATOM   5444 C CD1  . ILE   B 1 69  ? 47.320 -12.486 10.312  1.00 13.98 ?  69  ILE   B CD1  1 
ATOM   5445 H H    . ILE   B 1 69  ? 49.944 -9.769  9.114   1.00 14.23 ?  69  ILE   B H    1 
ATOM   5446 H HA   . ILE   B 1 69  ? 47.784 -9.802  10.586  1.00 14.62 ?  69  ILE   B HA   1 
ATOM   5447 H HB   . ILE   B 1 69  ? 50.287 -11.027 10.976  1.00 15.67 ?  69  ILE   B HB   1 
ATOM   5448 H HG12 . ILE   B 1 69  ? 48.964 -11.927 9.243   1.00 16.48 ?  69  ILE   B HG12 1 
ATOM   5449 H HG13 . ILE   B 1 69  ? 49.293 -13.002 10.362  1.00 16.48 ?  69  ILE   B HG13 1 
ATOM   5450 H HG21 . ILE   B 1 69  ? 49.177 -12.332 12.695  1.00 16.72 ?  69  ILE   B HG21 1 
ATOM   5451 H HG22 . ILE   B 1 69  ? 49.634 -10.869 13.106  1.00 16.72 ?  69  ILE   B HG22 1 
ATOM   5452 H HG23 . ILE   B 1 69  ? 48.112 -11.155 12.740  1.00 16.72 ?  69  ILE   B HG23 1 
ATOM   5453 H HD11 . ILE   B 1 69  ? 47.092 -13.215 9.719   1.00 16.80 ?  69  ILE   B HD11 1 
ATOM   5454 H HD12 . ILE   B 1 69  ? 47.139 -12.736 11.231  1.00 16.80 ?  69  ILE   B HD12 1 
ATOM   5455 H HD13 . ILE   B 1 69  ? 46.814 -11.695 10.076  1.00 16.80 ?  69  ILE   B HD13 1 
ATOM   5456 N N    . ALA   B 1 70  ? 50.180 -8.062  11.772  1.00 12.26 ?  70  ALA   B N    1 
ATOM   5457 C CA   . ALA   B 1 70  ? 50.450 -7.020  12.758  1.00 12.20 ?  70  ALA   B CA   1 
ATOM   5458 C C    . ALA   B 1 70  ? 49.450 -5.877  12.640  1.00 12.20 ?  70  ALA   B C    1 
ATOM   5459 O O    . ALA   B 1 70  ? 49.000 -5.334  13.652  1.00 12.85 ?  70  ALA   B O    1 
ATOM   5460 C CB   . ALA   B 1 70  ? 51.882 -6.504  12.606  1.00 12.79 ?  70  ALA   B CB   1 
ATOM   5461 H H    . ALA   B 1 70  ? 50.836 -8.243  11.251  1.00 14.74 ?  70  ALA   B H    1 
ATOM   5462 H HA   . ALA   B 1 70  ? 50.372 -7.398  13.653  1.00 14.66 ?  70  ALA   B HA   1 
ATOM   5463 H HB1  . ALA   B 1 70  ? 52.058 -5.841  13.298  1.00 15.38 ?  70  ALA   B HB1  1 
ATOM   5464 H HB2  . ALA   B 1 70  ? 52.502 -7.245  12.702  1.00 15.38 ?  70  ALA   B HB2  1 
ATOM   5465 H HB3  . ALA   B 1 70  ? 51.983 -6.099  11.732  1.00 15.38 ?  70  ALA   B HB3  1 
ATOM   5466 N N    . THR   B 1 71  ? 49.095 -5.501  11.414  1.00 12.70 ?  71  THR   B N    1 
ATOM   5467 C CA   . THR   B 1 71  ? 48.184 -4.384  11.191  1.00 13.46 ?  71  THR   B CA   1 
ATOM   5468 C C    . THR   B 1 71  ? 46.719 -4.760  11.407  1.00 14.10 ?  71  THR   B C    1 
ATOM   5469 O O    . THR   B 1 71  ? 45.944 -3.946  11.929  1.00 15.48 ?  71  THR   B O    1 
ATOM   5470 C CB   . THR   B 1 71  ? 48.396 -3.835  9.780   1.00 15.34 ?  71  THR   B CB   1 
ATOM   5471 O OG1  . THR   B 1 71  ? 49.717 -3.294  9.675   1.00 17.07 ?  71  THR   B OG1  1 
ATOM   5472 C CG2  . THR   B 1 71  ? 47.376 -2.758  9.448   1.00 16.51 ?  71  THR   B CG2  1 
ATOM   5473 H H    . THR   B 1 71  ? 49.379 -5.883  10.697  1.00 15.26 ?  71  THR   B H    1 
ATOM   5474 H HA   . THR   B 1 71  ? 48.402 -3.681  11.819  1.00 16.18 ?  71  THR   B HA   1 
ATOM   5475 H HB   . THR   B 1 71  ? 48.302 -4.556  9.136   1.00 18.44 ?  71  THR   B HB   1 
ATOM   5476 H HG1  . THR   B 1 71  ? 49.836 -2.974  8.904   1.00 20.51 ?  71  THR   B HG1  1 
ATOM   5477 H HG21 . THR   B 1 71  ? 47.673 -2.251  8.675   1.00 19.84 ?  71  THR   B HG21 1 
ATOM   5478 H HG22 . THR   B 1 71  ? 46.517 -3.157  9.253   1.00 19.84 ?  71  THR   B HG22 1 
ATOM   5479 H HG23 . THR   B 1 71  ? 47.282 -2.150  10.200  1.00 19.84 ?  71  THR   B HG23 1 
ATOM   5480 N N    . ASN   B 1 72  ? 46.322 -5.981  11.025  1.00 13.86 ?  72  ASN   B N    1 
ATOM   5481 C CA   . ASN   B 1 72  ? 44.916 -6.337  10.913  1.00 14.48 ?  72  ASN   B CA   1 
ATOM   5482 C C    . ASN   B 1 72  ? 44.452 -7.434  11.860  1.00 14.59 ?  72  ASN   B C    1 
ATOM   5483 O O    . ASN   B 1 72  ? 43.237 -7.598  12.027  1.00 15.79 ?  72  ASN   B O    1 
ATOM   5484 C CB   . ASN   B 1 72  ? 44.597 -6.773  9.475   1.00 15.31 ?  72  ASN   B CB   1 
ATOM   5485 C CG   . ASN   B 1 72  ? 44.879 -5.681  8.468   1.00 16.56 ?  72  ASN   B CG   1 
ATOM   5486 O OD1  . ASN   B 1 72  ? 45.903 -5.694  7.776   1.00 17.74 ?  72  ASN   B OD1  1 
ATOM   5487 N ND2  . ASN   B 1 72  ? 43.994 -4.706  8.405   1.00 18.14 ?  72  ASN   B ND2  1 
ATOM   5488 H H    . ASN   B 1 72  ? 46.860 -6.629  10.825  1.00 16.66 ?  72  ASN   B H    1 
ATOM   5489 H HA   . ASN   B 1 72  ? 44.384 -5.552  11.105  1.00 17.40 ?  72  ASN   B HA   1 
ATOM   5490 H HB2  . ASN   B 1 72  ? 45.139 -7.543  9.247   1.00 18.40 ?  72  ASN   B HB2  1 
ATOM   5491 H HB3  . ASN   B 1 72  ? 43.654 -7.001  9.415   1.00 18.40 ?  72  ASN   B HB3  1 
ATOM   5492 H HD21 . ASN   B 1 72  ? 44.103 -4.059  7.847   1.00 21.80 ?  72  ASN   B HD21 1 
ATOM   5493 H HD22 . ASN   B 1 72  ? 43.288 -4.727  8.900   1.00 21.80 ?  72  ASN   B HD22 1 
ATOM   5494 N N    . GLY   B 1 73  ? 45.359 -8.184  12.476  1.00 14.28 ?  73  GLY   B N    1 
ATOM   5495 C CA   . GLY   B 1 73  ? 44.968 -9.323  13.268  1.00 13.89 ?  73  GLY   B CA   1 
ATOM   5496 C C    . GLY   B 1 73  ? 44.614 -10.510 12.399  1.00 12.70 ?  73  GLY   B C    1 
ATOM   5497 O O    . GLY   B 1 73  ? 44.600 -10.430 11.167  1.00 12.49 ?  73  GLY   B O    1 
ATOM   5498 H H    . GLY   B 1 73  ? 46.209 -8.046  12.453  1.00 17.17 ?  73  GLY   B H    1 
ATOM   5499 H HA2  . GLY   B 1 73  ? 45.694 -9.574  13.861  1.00 16.69 ?  73  GLY   B HA2  1 
ATOM   5500 H HA3  . GLY   B 1 73  ? 44.194 -9.094  13.811  1.00 16.69 ?  73  GLY   B HA3  1 
ATOM   5501 N N    . PRO   B 1 74  ? 44.324 -11.640 13.038  1.00 12.81 ?  74  PRO   B N    1 
ATOM   5502 C CA   . PRO   B 1 74  ? 44.073 -12.873 12.291  1.00 12.23 ?  74  PRO   B CA   1 
ATOM   5503 C C    . PRO   B 1 74  ? 42.772 -12.810 11.503  1.00 11.91 ?  74  PRO   B C    1 
ATOM   5504 O O    . PRO   B 1 74  ? 41.828 -12.081 11.832  1.00 13.29 ?  74  PRO   B O    1 
ATOM   5505 C CB   . PRO   B 1 74  ? 43.998 -13.938 13.393  1.00 13.09 ?  74  PRO   B CB   1 
ATOM   5506 C CG   . PRO   B 1 74  ? 43.553 -13.189 14.604  1.00 15.00 ?  74  PRO   B CG   1 
ATOM   5507 C CD   . PRO   B 1 74  ? 44.201 -11.839 14.491  1.00 14.27 ?  74  PRO   B CD   1 
ATOM   5508 H HA   . PRO   B 1 74  ? 44.815 -13.067 11.691  1.00 14.70 ?  74  PRO   B HA   1 
ATOM   5509 H HB2  . PRO   B 1 74  ? 43.353 -14.620 13.142  1.00 15.73 ?  74  PRO   B HB2  1 
ATOM   5510 H HB3  . PRO   B 1 74  ? 44.877 -14.331 13.527  1.00 15.73 ?  74  PRO   B HB3  1 
ATOM   5511 H HG2  . PRO   B 1 74  ? 42.584 -13.108 14.598  1.00 18.03 ?  74  PRO   B HG2  1 
ATOM   5512 H HG3  . PRO   B 1 74  ? 43.853 -13.650 15.401  1.00 18.03 ?  74  PRO   B HG3  1 
ATOM   5513 H HD2  . PRO   B 1 74  ? 43.626 -11.158 14.884  1.00 17.15 ?  74  PRO   B HD2  1 
ATOM   5514 H HD3  . PRO   B 1 74  ? 45.074 -11.847 14.908  1.00 17.15 ?  74  PRO   B HD3  1 
ATOM   5515 N N    . LEU   B 1 75  ? 42.737 -13.617 10.450  1.00 11.50 ?  75  LEU   B N    1 
ATOM   5516 C CA   . LEU   B 1 75  ? 41.522 -13.820 9.686   1.00 11.47 ?  75  LEU   B CA   1 
ATOM   5517 C C    . LEU   B 1 75  ? 40.542 -14.675 10.483  1.00 12.29 ?  75  LEU   B C    1 
ATOM   5518 O O    . LEU   B 1 75  ? 40.885 -15.267 11.508  1.00 13.24 ?  75  LEU   B O    1 
ATOM   5519 C CB   . LEU   B 1 75  ? 41.837 -14.531 8.371   1.00 11.38 ?  75  LEU   B CB   1 
ATOM   5520 C CG   . LEU   B 1 75  ? 42.669 -13.789 7.327   1.00 13.26 ?  75  LEU   B CG   1 
ATOM   5521 C CD1  . LEU   B 1 75  ? 42.909 -14.670 6.104   1.00 15.54 ?  75  LEU   B CD1  1 
ATOM   5522 C CD2  . LEU   B 1 75  ? 42.020 -12.496 6.918   1.00 16.81 ?  75  LEU   B CD2  1 
ATOM   5523 H H    . LEU   B 1 75  ? 43.412 -14.070 10.155  1.00 13.83 ?  75  LEU   B H    1 
ATOM   5524 H HA   . LEU   B 1 75  ? 41.110 -12.965 9.488   1.00 13.79 ?  75  LEU   B HA   1 
ATOM   5525 H HB2  . LEU   B 1 75  ? 42.319 -15.349 8.581   1.00 13.68 ?  75  LEU   B HB2  1 
ATOM   5526 H HB3  . LEU   B 1 75  ? 40.997 -14.765 7.945   1.00 13.68 ?  75  LEU   B HB3  1 
ATOM   5527 H HG   . LEU   B 1 75  ? 43.533 -13.578 7.709   1.00 15.94 ?  75  LEU   B HG   1 
ATOM   5528 H HD11 . LEU   B 1 75  ? 43.443 -14.175 5.457   1.00 18.68 ?  75  LEU   B HD11 1 
ATOM   5529 H HD12 . LEU   B 1 75  ? 43.389 -15.469 6.377   1.00 18.68 ?  75  LEU   B HD12 1 
ATOM   5530 H HD13 . LEU   B 1 75  ? 42.058 -14.912 5.711   1.00 18.68 ?  75  LEU   B HD13 1 
ATOM   5531 H HD21 . LEU   B 1 75  ? 42.536 -12.094 6.203   1.00 20.21 ?  75  LEU   B HD21 1 
ATOM   5532 H HD22 . LEU   B 1 75  ? 41.116 -12.677 6.614   1.00 20.21 ?  75  LEU   B HD22 1 
ATOM   5533 H HD23 . LEU   B 1 75  ? 41.997 -11.900 7.684   1.00 20.21 ?  75  LEU   B HD23 1 
ATOM   5534 N N    . LYS   B 1 76  ? 39.306 -14.741 9.993   1.00 13.53 ?  76  LYS   B N    1 
ATOM   5535 C CA   . LYS   B 1 76  ? 38.324 -15.708 10.461  1.00 14.39 ?  76  LYS   B CA   1 
ATOM   5536 C C    . LYS   B 1 76  ? 38.440 -16.991 9.639   1.00 13.54 ?  76  LYS   B C    1 
ATOM   5537 O O    . LYS   B 1 76  ? 38.717 -16.945 8.444   1.00 12.97 ?  76  LYS   B O    1 
ATOM   5538 C CB   . LYS   B 1 76  ? 36.909 -15.146 10.257  1.00 16.96 ?  76  LYS   B CB   1 
ATOM   5539 C CG   . LYS   B 1 76  ? 36.630 -13.760 10.870  1.00 18.93 ?  76  LYS   B CG   1 
ATOM   5540 C CD   . LYS   B 1 76  ? 35.224 -13.234 10.515  1.00 20.12 ?  76  LYS   B CD   1 
ATOM   5541 C CE   . LYS   B 1 76  ? 34.964 -11.853 11.111  1.00 22.19 ?  76  LYS   B CE   1 
ATOM   5542 N NZ   . LYS   B 1 76  ? 33.665 -11.260 10.685  1.00 22.61 ?  76  LYS   B NZ   1 
ATOM   5543 H H    . LYS   B 1 76  ? 39.010 -14.229 9.366   1.00 16.27 ?  76  LYS   B H    1 
ATOM   5544 H HA   . LYS   B 1 76  ? 38.464 -15.915 11.397  1.00 17.30 ?  76  LYS   B HA   1 
ATOM   5545 H HB2  . LYS   B 1 76  ? 36.745 -15.075 9.305   1.00 20.38 ?  76  LYS   B HB2  1 
ATOM   5546 H HB3  . LYS   B 1 76  ? 36.276 -15.764 10.650  1.00 20.38 ?  76  LYS   B HB3  1 
ATOM   5547 H HG2  . LYS   B 1 76  ? 36.697 -13.819 11.837  1.00 22.74 ?  76  LYS   B HG2  1 
ATOM   5548 H HG3  . LYS   B 1 76  ? 37.286 -13.124 10.533  1.00 22.74 ?  76  LYS   B HG3  1 
ATOM   5549 H HD2  . LYS   B 1 76  ? 35.144 -13.170 9.549   1.00 24.17 ?  76  LYS   B HD2  1 
ATOM   5550 H HD3  . LYS   B 1 76  ? 34.559 -13.847 10.864  1.00 24.17 ?  76  LYS   B HD3  1 
ATOM   5551 H HE2  . LYS   B 1 76  ? 34.961 -11.927 12.077  1.00 26.65 ?  76  LYS   B HE2  1 
ATOM   5552 H HE3  . LYS   B 1 76  ? 35.676 -11.254 10.829  1.00 26.65 ?  76  LYS   B HE3  1 
ATOM   5553 H HZ1  . LYS   B 1 76  ? 33.561 -10.458 11.056  1.00 27.16 ?  76  LYS   B HZ1  1 
ATOM   5554 H HZ2  . LYS   B 1 76  ? 33.646 -11.172 9.799   1.00 27.16 ?  76  LYS   B HZ2  1 
ATOM   5555 H HZ3  . LYS   B 1 76  ? 32.993 -11.786 10.937  1.00 27.16 ?  76  LYS   B HZ3  1 
ATOM   5556 N N    . VAL   B 1 77  ? 38.199 -18.143 10.277  1.00 13.95 ?  77  VAL   B N    1 
ATOM   5557 C CA   . VAL   B 1 77  ? 37.983 -19.363 9.501   1.00 14.16 ?  77  VAL   B CA   1 
ATOM   5558 C C    . VAL   B 1 77  ? 36.785 -19.134 8.587   1.00 12.89 ?  77  VAL   B C    1 
ATOM   5559 O O    . VAL   B 1 77  ? 35.720 -18.685 9.032   1.00 13.02 ?  77  VAL   B O    1 
ATOM   5560 C CB   . VAL   B 1 77  ? 37.789 -20.581 10.419  1.00 15.78 ?  77  VAL   B CB   1 
ATOM   5561 C CG1  . VAL   B 1 77  ? 37.502 -21.821 9.582   1.00 17.00 ?  77  VAL   B CG1  1 
ATOM   5562 C CG2  . VAL   B 1 77  ? 39.023 -20.796 11.299  1.00 16.97 ?  77  VAL   B CG2  1 
ATOM   5563 H H    . VAL   B 1 77  ? 38.162 -18.243 11.125  1.00 16.77 ?  77  VAL   B H    1 
ATOM   5564 H HA   . VAL   B 1 77  ? 38.757 -19.528 8.940   1.00 17.02 ?  77  VAL   B HA   1 
ATOM   5565 H HB   . VAL   B 1 77  ? 37.024 -20.424 10.995  1.00 18.97 ?  77  VAL   B HB   1 
ATOM   5566 H HG11 . VAL   B 1 77  ? 37.549 -22.603 10.157  1.00 20.42 ?  77  VAL   B HG11 1 
ATOM   5567 H HG12 . VAL   B 1 77  ? 36.614 -21.753 9.197   1.00 20.42 ?  77  VAL   B HG12 1 
ATOM   5568 H HG13 . VAL   B 1 77  ? 38.165 -21.890 8.879   1.00 20.42 ?  77  VAL   B HG13 1 
ATOM   5569 H HG21 . VAL   B 1 77  ? 38.891 -21.592 11.834  1.00 20.39 ?  77  VAL   B HG21 1 
ATOM   5570 H HG22 . VAL   B 1 77  ? 39.799 -20.899 10.730  1.00 20.39 ?  77  VAL   B HG22 1 
ATOM   5571 H HG23 . VAL   B 1 77  ? 39.133 -20.023 11.875  1.00 20.39 ?  77  VAL   B HG23 1 
ATOM   5572 N N    . GLY   B 1 78  ? 36.960 -19.416 7.296   1.00 12.37 ?  78  GLY   B N    1 
ATOM   5573 C CA   . GLY   B 1 78  ? 35.978 -19.088 6.288   1.00 12.37 ?  78  GLY   B CA   1 
ATOM   5574 C C    . GLY   B 1 78  ? 36.216 -17.768 5.589   1.00 11.46 ?  78  GLY   B C    1 
ATOM   5575 O O    . GLY   B 1 78  ? 35.528 -17.483 4.601   1.00 11.78 ?  78  GLY   B O    1 
ATOM   5576 H H    . GLY   B 1 78  ? 37.659 -19.810 6.975   1.00 14.87 ?  78  GLY   B H    1 
ATOM   5577 H HA2  . GLY   B 1 78  ? 35.965 -19.782 5.615   1.00 14.87 ?  78  GLY   B HA2  1 
ATOM   5578 H HA3  . GLY   B 1 78  ? 35.100 -19.052 6.703   1.00 14.87 ?  78  GLY   B HA3  1 
ATOM   5579 N N    . GLY   B 1 79  ? 37.179 -16.967 6.061   1.00 11.51 ?  79  GLY   B N    1 
ATOM   5580 C CA   . GLY   B 1 79  ? 37.478 -15.674 5.483   1.00 11.09 ?  79  GLY   B CA   1 
ATOM   5581 C C    . GLY   B 1 79  ? 38.714 -15.695 4.594   1.00 10.87 ?  79  GLY   B C    1 
ATOM   5582 O O    . GLY   B 1 79  ? 39.330 -16.732 4.353   1.00 11.21 ?  79  GLY   B O    1 
ATOM   5583 H H    . GLY   B 1 79  ? 37.684 -17.161 6.729   1.00 13.84 ?  79  GLY   B H    1 
ATOM   5584 H HA2  . GLY   B 1 79  ? 36.723 -15.376 4.946   1.00 13.33 ?  79  GLY   B HA2  1 
ATOM   5585 H HA3  . GLY   B 1 79  ? 37.623 -15.027 6.188   1.00 13.33 ?  79  GLY   B HA3  1 
ATOM   5586 N N    . SER   B 1 80  ? 39.079 -14.504 4.114   1.00 10.70 ?  80  SER   B N    1 
ATOM   5587 C CA   . SER   B 1 80  ? 40.190 -14.379 3.182   1.00 10.43 ?  80  SER   B CA   1 
ATOM   5588 C C    . SER   B 1 80  ? 40.769 -12.974 3.231   1.00 10.15 ?  80  SER   B C    1 
ATOM   5589 O O    . SER   B 1 80  ? 40.153 -12.041 3.749   1.00 11.57 ?  80  SER   B O    1 
ATOM   5590 C CB   . SER   B 1 80  ? 39.753 -14.680 1.747   1.00 10.52 ?  80  SER   B CB   1 
ATOM   5591 O OG   . SER   B 1 80  ? 38.916 -13.661 1.235   1.00 11.69 ?  80  SER   B OG   1 
ATOM   5592 H H    . SER   B 1 80  ? 38.702 -13.759 4.315   1.00 12.87 ?  80  SER   B H    1 
ATOM   5593 H HA   . SER   B 1 80  ? 40.880 -15.009 3.433   1.00 12.55 ?  80  SER   B HA   1 
ATOM   5594 H HB2  . SER   B 1 80  ? 40.537 -14.746 1.181   1.00 12.65 ?  80  SER   B HB2  1 
ATOM   5595 H HB3  . SER   B 1 80  ? 39.267 -15.522 1.733   1.00 12.65 ?  80  SER   B HB3  1 
ATOM   5596 H HG   . SER   B 1 80  ? 38.214 -13.595 1.704   1.00 14.05 ?  80  SER   B HG   1 
ATOM   5597 N N    . CYS   B 1 81  ? 41.960 -12.831 2.646   1.00 10.09 ?  81  CYS   B N    1 
ATOM   5598 C CA   . CYS   B 1 81  ? 42.506 -11.518 2.326   1.00 10.68 ?  81  CYS   B CA   1 
ATOM   5599 C C    . CYS   B 1 81  ? 43.276 -11.609 1.017   1.00 9.78  ?  81  CYS   B C    1 
ATOM   5600 O O    . CYS   B 1 81  ? 43.785 -12.672 0.644   1.00 10.69 ?  81  CYS   B O    1 
ATOM   5601 C CB   . CYS   B 1 81  ? 43.397 -10.960 3.446   1.00 11.42 ?  81  CYS   B CB   1 
ATOM   5602 S SG   . CYS   B 1 81  ? 44.919 -11.909 3.691   1.00 11.37 ?  81  CYS   B SG   1 
ATOM   5603 H H    . CYS   B 1 81  ? 42.469 -13.484 2.412   1.00 12.14 ?  81  CYS   B H    1 
ATOM   5604 H HA   . CYS   B 1 81  ? 41.774 -10.896 2.194   1.00 12.85 ?  81  CYS   B HA   1 
ATOM   5605 H HB2  . CYS   B 1 81  ? 43.648 -10.050 3.227   1.00 13.73 ?  81  CYS   B HB2  1 
ATOM   5606 H HB3  . CYS   B 1 81  ? 42.898 -10.972 4.279   1.00 13.73 ?  81  CYS   B HB3  1 
ATOM   5607 H HG   . CYS   B 1 81  ? 45.552 -11.415 4.584   1.00 13.68 ?  81  CYS   B HG   1 
ATOM   5608 N N    . VAL   B 1 82  ? 43.382 -10.470 0.340   1.00 10.47 ?  82  VAL   B N    1 
ATOM   5609 C CA   . VAL   B 1 82  ? 44.139 -10.344 -0.902  1.00 10.29 ?  82  VAL   B CA   1 
ATOM   5610 C C    . VAL   B 1 82  ? 45.479 -9.701  -0.584  1.00 10.51 ?  82  VAL   B C    1 
ATOM   5611 O O    . VAL   B 1 82  ? 45.532 -8.583  -0.053  1.00 11.51 ?  82  VAL   B O    1 
ATOM   5612 C CB   . VAL   B 1 82  ? 43.391 -9.501  -1.945  1.00 11.79 ?  82  VAL   B CB   1 
ATOM   5613 C CG1  . VAL   B 1 82  ? 44.230 -9.351  -3.209  1.00 12.87 ?  82  VAL   B CG1  1 
ATOM   5614 C CG2  . VAL   B 1 82  ? 42.026 -10.089 -2.260  1.00 12.72 ?  82  VAL   B CG2  1 
ATOM   5615 H H    . VAL   B 1 82  ? 43.009 -9.728  0.584   1.00 12.59 ?  82  VAL   B H    1 
ATOM   5616 H HA   . VAL   B 1 82  ? 44.296 -11.222 -1.275  1.00 12.37 ?  82  VAL   B HA   1 
ATOM   5617 H HB   . VAL   B 1 82  ? 43.245 -8.615  -1.588  1.00 14.18 ?  82  VAL   B HB   1 
ATOM   5618 H HG11 . VAL   B 1 82  ? 43.668 -9.029  -3.932  1.00 15.47 ?  82  VAL   B HG11 1 
ATOM   5619 H HG12 . VAL   B 1 82  ? 44.944 -8.709  -3.043  1.00 15.47 ?  82  VAL   B HG12 1 
ATOM   5620 H HG13 . VAL   B 1 82  ? 44.610 -10.211 -3.446  1.00 15.47 ?  82  VAL   B HG13 1 
ATOM   5621 H HG21 . VAL   B 1 82  ? 41.596 -9.552  -2.947  1.00 15.29 ?  82  VAL   B HG21 1 
ATOM   5622 H HG22 . VAL   B 1 82  ? 42.137 -11.000 -2.581  1.00 15.29 ?  82  VAL   B HG22 1 
ATOM   5623 H HG23 . VAL   B 1 82  ? 41.486 -10.087 -1.455  1.00 15.29 ?  82  VAL   B HG23 1 
ATOM   5624 N N    . LEU   B 1 83  ? 46.557 -10.391 -0.944  1.00 10.16 ?  83  LEU   B N    1 
ATOM   5625 C CA   . LEU   B 1 83  ? 47.911 -9.874  -0.826  1.00 10.22 ?  83  LEU   B CA   1 
ATOM   5626 C C    . LEU   B 1 83  ? 48.614 -10.022 -2.177  1.00 10.27 ?  83  LEU   B C    1 
ATOM   5627 O O    . LEU   B 1 83  ? 48.009 -10.445 -3.167  1.00 10.21 ?  83  LEU   B O    1 
ATOM   5628 C CB   . LEU   B 1 83  ? 48.655 -10.558 0.328   1.00 10.53 ?  83  LEU   B CB   1 
ATOM   5629 C CG   . LEU   B 1 83  ? 48.163 -10.192 1.735   1.00 11.91 ?  83  LEU   B CG   1 
ATOM   5630 C CD1  . LEU   B 1 83  ? 48.815 -11.059 2.795   1.00 12.16 ?  83  LEU   B CD1  1 
ATOM   5631 C CD2  . LEU   B 1 83  ? 48.378 -8.713  2.032   1.00 13.42 ?  83  LEU   B CD2  1 
ATOM   5632 H H    . LEU   B 1 83  ? 46.518 -11.190 -1.270  1.00 12.22 ?  83  LEU   B H    1 
ATOM   5633 H HA   . LEU   B 1 83  ? 47.858 -8.927  -0.628  1.00 12.29 ?  83  LEU   B HA   1 
ATOM   5634 H HB2  . LEU   B 1 83  ? 48.567 -11.518 0.226   1.00 12.66 ?  83  LEU   B HB2  1 
ATOM   5635 H HB3  . LEU   B 1 83  ? 49.592 -10.312 0.273   1.00 12.66 ?  83  LEU   B HB3  1 
ATOM   5636 H HG   . LEU   B 1 83  ? 47.211 -10.359 1.773   1.00 14.32 ?  83  LEU   B HG   1 
ATOM   5637 H HD11 . LEU   B 1 83  ? 48.472 -10.802 3.668   1.00 14.62 ?  83  LEU   B HD11 1 
ATOM   5638 H HD12 . LEU   B 1 83  ? 48.601 -11.990 2.621   1.00 14.62 ?  83  LEU   B HD12 1 
ATOM   5639 H HD13 . LEU   B 1 83  ? 49.776 -10.931 2.768   1.00 14.62 ?  83  LEU   B HD13 1 
ATOM   5640 H HD21 . LEU   B 1 83  ? 48.212 -8.555  2.974   1.00 16.13 ?  83  LEU   B HD21 1 
ATOM   5641 H HD22 . LEU   B 1 83  ? 49.295 -8.478  1.815   1.00 16.13 ?  83  LEU   B HD22 1 
ATOM   5642 H HD23 . LEU   B 1 83  ? 47.767 -8.190  1.493   1.00 16.13 ?  83  LEU   B HD23 1 
ATOM   5643 N N    . SER   B 1 84  ? 49.895 -9.666  -2.231  1.00 10.99 ?  84  SER   B N    1 
ATOM   5644 C CA   . SER   B 1 84  ? 50.626 -9.784  -3.484  1.00 11.56 ?  84  SER   B CA   1 
ATOM   5645 C C    . SER   B 1 84  ? 50.786 -11.244 -3.894  1.00 10.72 ?  84  SER   B C    1 
ATOM   5646 O O    . SER   B 1 84  ? 50.910 -12.138 -3.059  1.00 10.84 ?  84  SER   B O    1 
ATOM   5647 C CB   . SER   B 1 84  ? 52.016 -9.172  -3.344  1.00 13.07 ?  84  SER   B CB   1 
ATOM   5648 O OG   . SER   B 1 84  ? 52.759 -9.389  -4.531  1.00 14.52 ?  84  SER   B OG   1 
ATOM   5649 H H    . SER   B 1 84  ? 50.347 -9.347  -1.566  1.00 13.21 ?  84  SER   B H    1 
ATOM   5650 H HA   . SER   B 1 84  ? 50.148 -9.318  -4.180  1.00 13.90 ?  84  SER   B HA   1 
ATOM   5651 H HB2  . SER   B 1 84  ? 51.929 -8.216  -3.192  1.00 15.71 ?  84  SER   B HB2  1 
ATOM   5652 H HB3  . SER   B 1 84  ? 52.474 -9.585  -2.593  1.00 15.71 ?  84  SER   B HB3  1 
ATOM   5653 H HG   . SER   B 1 84  ? 53.532 -9.052  -4.448  1.00 17.46 ?  84  SER   B HG   1 
ATOM   5654 N N    . GLY   B 1 85  ? 50.842 -11.476 -5.198  1.00 11.88 ?  85  GLY   B N    1 
ATOM   5655 C CA   . GLY   B 1 85  ? 51.198 -12.774 -5.719  1.00 12.47 ?  85  GLY   B CA   1 
ATOM   5656 C C    . GLY   B 1 85  ? 52.665 -12.956 -6.028  1.00 11.63 ?  85  GLY   B C    1 
ATOM   5657 O O    . GLY   B 1 85  ? 53.056 -14.031 -6.482  1.00 12.41 ?  85  GLY   B O    1 
ATOM   5658 H H    . GLY   B 1 85  ? 50.667 -10.895 -5.800  1.00 14.28 ?  85  GLY   B H    1 
ATOM   5659 H HA2  . GLY   B 1 85  ? 50.943 -13.460 -5.075  1.00 14.99 ?  85  GLY   B HA2  1 
ATOM   5660 H HA3  . GLY   B 1 85  ? 50.705 -12.938 -6.533  1.00 14.99 ?  85  GLY   B HA3  1 
ATOM   5661 N N    . HIS   B 1 86  ? 53.504 -11.946 -5.813  1.00 11.35 ?  86  HIS   B N    1 
ATOM   5662 C CA   . HIS   B 1 86  ? 54.969 -12.105 -5.907  1.00 11.50 ?  86  HIS   B CA   1 
ATOM   5663 C C    . HIS   B 1 86  ? 55.345 -12.615 -7.296  1.00 11.77 ?  86  HIS   B C    1 
ATOM   5664 O O    . HIS   B 1 86  ? 54.964 -11.999 -8.304  1.00 12.66 ?  86  HIS   B O    1 
ATOM   5665 C CB   . HIS   B 1 86  ? 55.478 -12.943 -4.733  1.00 12.08 ?  86  HIS   B CB   1 
ATOM   5666 C CG   . HIS   B 1 86  ? 55.167 -12.333 -3.408  1.00 12.08 ?  86  HIS   B CG   1 
ATOM   5667 N ND1  . HIS   B 1 86  ? 55.987 -11.408 -2.800  1.00 13.35 ?  86  HIS   B ND1  1 
ATOM   5668 C CD2  . HIS   B 1 86  ? 54.094 -12.483 -2.596  1.00 12.23 ?  86  HIS   B CD2  1 
ATOM   5669 C CE1  . HIS   B 1 86  ? 55.429 -11.017 -1.668  1.00 13.27 ?  86  HIS   B CE1  1 
ATOM   5670 N NE2  . HIS   B 1 86  ? 54.280 -11.652 -1.522  1.00 12.58 ?  86  HIS   B NE2  1 
ATOM   5671 H H    . HIS   B 1 86  ? 53.259 -11.148 -5.619  1.00 13.65 ?  86  HIS   B H    1 
ATOM   5672 H HA   . HIS   B 1 86  ? 55.372 -11.230 -5.812  1.00 13.82 ?  86  HIS   B HA   1 
ATOM   5673 H HB2  . HIS   B 1 86  ? 55.067 -13.822 -4.768  1.00 14.52 ?  86  HIS   B HB2  1 
ATOM   5674 H HB3  . HIS   B 1 86  ? 56.446 -13.033 -4.804  1.00 14.52 ?  86  HIS   B HB3  1 
ATOM   5675 H HD2  . HIS   B 1 86  ? 53.360 -13.034 -2.754  1.00 14.70 ?  86  HIS   B HD2  1 
ATOM   5676 H HE1  . HIS   B 1 86  ? 55.798 -10.417 -1.063  1.00 15.95 ?  86  HIS   B HE1  1 
ATOM   5677 H HE2  . HIS   B 1 86  ? 53.744 -11.574 -0.857  1.00 15.13 ?  86  HIS   B HE2  1 
ATOM   5678 N N    . ASN   B 1 87  ? 56.109 -13.699 -7.402  1.00 12.13 ?  87  ASN   B N    1 
ATOM   5679 C CA   . ASN   B 1 87  ? 56.517 -14.274 -8.674  1.00 13.18 ?  87  ASN   B CA   1 
ATOM   5680 C C    . ASN   B 1 87  ? 55.534 -15.312 -9.185  1.00 12.46 ?  87  ASN   B C    1 
ATOM   5681 O O    . ASN   B 1 87  ? 55.841 -16.010 -10.156 1.00 14.27 ?  87  ASN   B O    1 
ATOM   5682 C CB   . ASN   B 1 87  ? 57.912 -14.907 -8.550  1.00 14.90 ?  87  ASN   B CB   1 
ATOM   5683 C CG   . ASN   B 1 87  ? 57.979 -15.995 -7.484  1.00 15.51 ?  87  ASN   B CG   1 
ATOM   5684 O OD1  . ASN   B 1 87  ? 57.324 -15.904 -6.445  1.00 14.60 ?  87  ASN   B OD1  1 
ATOM   5685 N ND2  . ASN   B 1 87  ? 58.768 -17.041 -7.749  1.00 17.87 ?  87  ASN   B ND2  1 
ATOM   5686 H H    . ASN   B 1 87  ? 56.403 -14.137 -6.729  1.00 14.58 ?  87  ASN   B H    1 
ATOM   5687 H HA   . ASN   B 1 87  ? 56.570 -13.575 -9.337  1.00 15.84 ?  87  ASN   B HA   1 
ATOM   5688 H HB2  . ASN   B 1 87  ? 58.158 -15.310 -9.402  1.00 17.90 ?  87  ASN   B HB2  1 
ATOM   5689 H HB3  . ASN   B 1 87  ? 58.551 -14.218 -8.316  1.00 17.90 ?  87  ASN   B HB3  1 
ATOM   5690 H HD21 . ASN   B 1 87  ? 58.848 -17.678 -7.177  1.00 21.47 ?  87  ASN   B HD21 1 
ATOM   5691 H HD22 . ASN   B 1 87  ? 59.214 -17.074 -8.488  1.00 21.47 ?  87  ASN   B HD22 1 
ATOM   5692 N N    . LEU   B 1 88  ? 54.361 -15.425 -8.562  1.00 11.79 ?  88  LEU   B N    1 
ATOM   5693 C CA   . LEU   B 1 88  ? 53.386 -16.454 -8.893  1.00 12.05 ?  88  LEU   B CA   1 
ATOM   5694 C C    . LEU   B 1 88  ? 52.148 -15.933 -9.606  1.00 11.78 ?  88  LEU   B C    1 
ATOM   5695 O O    . LEU   B 1 88  ? 51.548 -16.673 -10.393 1.00 13.24 ?  88  LEU   B O    1 
ATOM   5696 C CB   . LEU   B 1 88  ? 52.926 -17.152 -7.611  1.00 13.56 ?  88  LEU   B CB   1 
ATOM   5697 C CG   . LEU   B 1 88  ? 54.068 -17.771 -6.809  1.00 15.73 ?  88  LEU   B CG   1 
ATOM   5698 C CD1  . LEU   B 1 88  ? 53.583 -18.235 -5.446  1.00 17.42 ?  88  LEU   B CD1  1 
ATOM   5699 C CD2  . LEU   B 1 88  ? 54.691 -18.918 -7.587  1.00 19.24 ?  88  LEU   B CD2  1 
ATOM   5700 H H    . LEU   B 1 88  ? 54.107 -14.907 -7.920  1.00 14.18 ?  88  LEU   B H    1 
ATOM   5701 H HA   . LEU   B 1 88  ? 53.809 -17.117 -9.459  1.00 14.48 ?  88  LEU   B HA   1 
ATOM   5702 H HB2  . LEU   B 1 88  ? 52.479 -16.505 -7.041  1.00 16.30 ?  88  LEU   B HB2  1 
ATOM   5703 H HB3  . LEU   B 1 88  ? 52.307 -17.863 -7.846  1.00 16.30 ?  88  LEU   B HB3  1 
ATOM   5704 H HG   . LEU   B 1 88  ? 54.753 -17.101 -6.667  1.00 18.91 ?  88  LEU   B HG   1 
ATOM   5705 H HD11 . LEU   B 1 88  ? 54.333 -18.597 -4.950  1.00 20.94 ?  88  LEU   B HD11 1 
ATOM   5706 H HD12 . LEU   B 1 88  ? 53.204 -17.478 -4.971  1.00 20.94 ?  88  LEU   B HD12 1 
ATOM   5707 H HD13 . LEU   B 1 88  ? 52.907 -18.919 -5.571  1.00 20.94 ?  88  LEU   B HD13 1 
ATOM   5708 H HD21 . LEU   B 1 88  ? 55.311 -19.389 -7.008  1.00 23.12 ?  88  LEU   B HD21 1 
ATOM   5709 H HD22 . LEU   B 1 88  ? 53.987 -19.520 -7.877  1.00 23.12 ?  88  LEU   B HD22 1 
ATOM   5710 H HD23 . LEU   B 1 88  ? 55.160 -18.562 -8.356  1.00 23.12 ?  88  LEU   B HD23 1 
ATOM   5711 N N    . ALA   B 1 89  ? 51.738 -14.701 -9.334  1.00 11.32 ?  89  ALA   B N    1 
ATOM   5712 C CA   . ALA   B 1 89  ? 50.437 -14.210 -9.767  1.00 10.85 ?  89  ALA   B CA   1 
ATOM   5713 C C    . ALA   B 1 89  ? 50.418 -12.719 -9.487  1.00 11.19 ?  89  ALA   B C    1 
ATOM   5714 O O    . ALA   B 1 89  ? 51.253 -12.209 -8.741  1.00 11.81 ?  89  ALA   B O    1 
ATOM   5715 C CB   . ALA   B 1 89  ? 49.319 -14.892 -8.984  1.00 10.97 ?  89  ALA   B CB   1 
ATOM   5716 H H    . ALA   B 1 89  ? 52.198 -14.123 -8.895  1.00 13.62 ?  89  ALA   B H    1 
ATOM   5717 H HA   . ALA   B 1 89  ? 50.309 -14.370 -10.720 1.00 13.05 ?  89  ALA   B HA   1 
ATOM   5718 H HB1  . ALA   B 1 89  ? 48.468 -14.556 -9.292  1.00 13.20 ?  89  ALA   B HB1  1 
ATOM   5719 H HB2  . ALA   B 1 89  ? 49.374 -15.852 -9.129  1.00 13.20 ?  89  ALA   B HB2  1 
ATOM   5720 H HB3  . ALA   B 1 89  ? 49.439 -14.696 -8.041  1.00 13.20 ?  89  ALA   B HB3  1 
ATOM   5721 N N    . LYS   B 1 90  ? 49.439 -12.020 -10.055 1.00 12.05 ?  90  LYS   B N    1 
ATOM   5722 C CA   . LYS   B 1 90  ? 49.253 -10.634 -9.649  1.00 12.23 ?  90  LYS   B CA   1 
ATOM   5723 C C    . LYS   B 1 90  ? 48.933 -10.560 -8.160  1.00 11.76 ?  90  LYS   B C    1 
ATOM   5724 O O    . LYS   B 1 90  ? 49.579 -9.815  -7.406  1.00 12.60 ?  90  LYS   B O    1 
ATOM   5725 C CB   . LYS   B 1 90  ? 48.173 -9.971  -10.505 1.00 13.34 ?  90  LYS   B CB   1 
ATOM   5726 C CG   . LYS   B 1 90  ? 47.881 -8.534  -10.126 1.00 14.03 ?  90  LYS   B CG   1 
ATOM   5727 C CD   . LYS   B 1 90  ? 49.094 -7.640  -10.173 1.00 16.61 ?  90  LYS   B CD   1 
ATOM   5728 C CE   . LYS   B 1 90  ? 48.629 -6.222  -9.940  1.00 18.62 ?  90  LYS   B CE   1 
ATOM   5729 N NZ   . LYS   B 1 90  ? 49.740 -5.253  -9.805  1.00 18.62 ?  90  LYS   B NZ   1 
ATOM   5730 H H    . LYS   B 1 90  ? 48.893 -12.316 -10.650 1.00 14.49 ?  90  LYS   B H    1 
ATOM   5731 H HA   . LYS   B 1 90  ? 50.081 -10.157 -9.796  1.00 14.71 ?  90  LYS   B HA   1 
ATOM   5732 H HB2  . LYS   B 1 90  ? 48.461 -9.980  -11.434 1.00 16.03 ?  90  LYS   B HB2  1 
ATOM   5733 H HB3  . LYS   B 1 90  ? 47.348 -10.473 -10.417 1.00 16.03 ?  90  LYS   B HB3  1 
ATOM   5734 H HG2  . LYS   B 1 90  ? 47.229 -8.171  -10.745 1.00 16.87 ?  90  LYS   B HG2  1 
ATOM   5735 H HG3  . LYS   B 1 90  ? 47.528 -8.507  -9.224  1.00 16.87 ?  90  LYS   B HG3  1 
ATOM   5736 H HD2  . LYS   B 1 90  ? 49.718 -7.883  -9.467  1.00 19.96 ?  90  LYS   B HD2  1 
ATOM   5737 H HD3  . LYS   B 1 90  ? 49.520 -7.693  -11.043 1.00 19.96 ?  90  LYS   B HD3  1 
ATOM   5738 H HE2  . LYS   B 1 90  ? 48.083 -5.940  -10.691 1.00 22.38 ?  90  LYS   B HE2  1 
ATOM   5739 H HE3  . LYS   B 1 90  ? 48.110 -6.187  -9.122  1.00 22.38 ?  90  LYS   B HE3  1 
ATOM   5740 H HZ1  . LYS   B 1 90  ? 49.421 -4.431  -9.673  1.00 22.37 ?  90  LYS   B HZ1  1 
ATOM   5741 H HZ2  . LYS   B 1 90  ? 50.260 -5.473  -9.118  1.00 22.37 ?  90  LYS   B HZ2  1 
ATOM   5742 H HZ3  . LYS   B 1 90  ? 50.236 -5.248  -10.549 1.00 22.37 ?  90  LYS   B HZ3  1 
ATOM   5743 N N    . HIS   B 1 91  ? 47.967 -11.371 -7.716  1.00 10.48 ?  91  HIS   B N    1 
ATOM   5744 C CA   . HIS   B 1 91  ? 47.492 -11.401 -6.344  1.00 10.56 ?  91  HIS   B CA   1 
ATOM   5745 C C    . HIS   B 1 91  ? 47.486 -12.827 -5.823  1.00 9.83  ?  91  HIS   B C    1 
ATOM   5746 O O    . HIS   B 1 91  ? 47.262 -13.782 -6.576  1.00 10.41 ?  91  HIS   B O    1 
ATOM   5747 C CB   . HIS   B 1 91  ? 46.043 -10.913 -6.231  1.00 12.18 ?  91  HIS   B CB   1 
ATOM   5748 C CG   . HIS   B 1 91  ? 45.838 -9.509  -6.669  1.00 15.40 ?  91  HIS   B CG   1 
ATOM   5749 N ND1  . HIS   B 1 91  ? 46.452 -8.436  -6.059  1.00 17.79 ?  91  HIS   B ND1  1 
ATOM   5750 C CD2  . HIS   B 1 91  ? 45.042 -8.990  -7.630  1.00 17.65 ?  91  HIS   B CD2  1 
ATOM   5751 C CE1  . HIS   B 1 91  ? 46.072 -7.317  -6.649  1.00 18.81 ?  91  HIS   B CE1  1 
ATOM   5752 N NE2  . HIS   B 1 91  ? 45.209 -7.627  -7.600  1.00 19.07 ?  91  HIS   B NE2  1 
ATOM   5753 H H    . HIS   B 1 91  ? 47.546 -11.930 -8.223  1.00 12.60 ?  91  HIS   B H    1 
ATOM   5754 H HA   . HIS   B 1 91  ? 48.062 -10.847 -5.781  1.00 12.70 ?  91  HIS   B HA   1 
ATOM   5755 H HB2  . HIS   B 1 91  ? 45.477 -11.475 -6.785  1.00 14.64 ?  91  HIS   B HB2  1 
ATOM   5756 H HB3  . HIS   B 1 91  ? 45.758 -10.975 -5.306  1.00 14.64 ?  91  HIS   B HB3  1 
ATOM   5757 H HD1  . HIS   B 1 91  ? 47.010 -8.484  -5.407  1.00 21.38 ?  91  HIS   B HD1  1 
ATOM   5758 H HD2  . HIS   B 1 91  ? 44.494 -9.455  -8.216  1.00 21.21 ?  91  HIS   B HD2  1 
ATOM   5759 H HE1  . HIS   B 1 91  ? 46.351 -6.452  -6.423  1.00 22.60 ?  91  HIS   B HE1  1 
ATOM   5760 N N    . CYS   B 1 92  ? 47.682 -12.958 -4.518  1.00 9.63  ?  92  CYS   B N    1 
ATOM   5761 C CA   . CYS   B 1 92  ? 47.385 -14.191 -3.801  1.00 9.65  ?  92  CYS   B CA   1 
ATOM   5762 C C    . CYS   B 1 92  ? 46.165 -13.954 -2.922  1.00 9.13  ?  92  CYS   B C    1 
ATOM   5763 O O    . CYS   B 1 92  ? 46.167 -13.049 -2.075  1.00 10.07 ?  92  CYS   B O    1 
ATOM   5764 C CB   . CYS   B 1 92  ? 48.570 -14.653 -2.956  1.00 10.17 ?  92  CYS   B CB   1 
ATOM   5765 S SG   . CYS   B 1 92  ? 48.204 -16.188 -2.053  1.00 10.00 ?  92  CYS   B SG   1 
ATOM   5766 H H    . CYS   B 1 92  ? 48.000 -12.333 -4.013  1.00 11.59 ?  92  CYS   B H    1 
ATOM   5767 H HA   . CYS   B 1 92  ? 47.181 -14.888 -4.448  1.00 11.61 ?  92  CYS   B HA   1 
ATOM   5768 H HB2  . CYS   B 1 92  ? 49.329 -14.814 -3.536  1.00 12.23 ?  92  CYS   B HB2  1 
ATOM   5769 H HB3  . CYS   B 1 92  ? 48.779 -13.962 -2.311  1.00 12.23 ?  92  CYS   B HB3  1 
ATOM   5770 H HG   . CYS   B 1 92  ? 49.179 -16.506 -1.425  1.00 12.03 ?  92  CYS   B HG   1 
ATOM   5771 N N    . LEU   B 1 93  ? 45.131 -14.764 -3.132  1.00 8.97  ?  93  LEU   B N    1 
ATOM   5772 C CA   . LEU   B 1 93  ? 43.956 -14.772 -2.275  1.00 9.26  ?  93  LEU   B CA   1 
ATOM   5773 C C    . LEU   B 1 93  ? 44.182 -15.833 -1.211  1.00 8.83  ?  93  LEU   B C    1 
ATOM   5774 O O    . LEU   B 1 93  ? 44.135 -17.031 -1.504  1.00 9.54  ?  93  LEU   B O    1 
ATOM   5775 C CB   . LEU   B 1 93  ? 42.691 -15.050 -3.081  1.00 9.71  ?  93  LEU   B CB   1 
ATOM   5776 C CG   . LEU   B 1 93  ? 41.396 -15.076 -2.266  1.00 10.28 ?  93  LEU   B CG   1 
ATOM   5777 C CD1  . LEU   B 1 93  ? 41.034 -13.692 -1.764  1.00 10.81 ?  93  LEU   B CD1  1 
ATOM   5778 C CD2  . LEU   B 1 93  ? 40.267 -15.668 -3.101  1.00 11.10 ?  93  LEU   B CD2  1 
ATOM   5779 H H    . LEU   B 1 93  ? 45.088 -15.341 -3.779  1.00 10.79 ?  93  LEU   B H    1 
ATOM   5780 H HA   . LEU   B 1 93  ? 43.866 -13.911 -1.845  1.00 11.14 ?  93  LEU   B HA   1 
ATOM   5781 H HB2  . LEU   B 1 93  ? 42.597 -14.358 -3.754  1.00 11.68 ?  93  LEU   B HB2  1 
ATOM   5782 H HB3  . LEU   B 1 93  ? 42.781 -15.913 -3.512  1.00 11.68 ?  93  LEU   B HB3  1 
ATOM   5783 H HG   . LEU   B 1 93  ? 41.520 -15.646 -1.495  1.00 12.36 ?  93  LEU   B HG   1 
ATOM   5784 H HD11 . LEU   B 1 93  ? 40.186 -13.733 -1.297  1.00 13.00 ?  93  LEU   B HD11 1 
ATOM   5785 H HD12 . LEU   B 1 93  ? 41.728 -13.378 -1.164  1.00 13.00 ?  93  LEU   B HD12 1 
ATOM   5786 H HD13 . LEU   B 1 93  ? 40.961 -13.086 -2.524  1.00 13.00 ?  93  LEU   B HD13 1 
ATOM   5787 H HD21 . LEU   B 1 93  ? 39.451 -15.663 -2.578  1.00 13.35 ?  93  LEU   B HD21 1 
ATOM   5788 H HD22 . LEU   B 1 93  ? 40.151 -15.135 -3.903  1.00 13.35 ?  93  LEU   B HD22 1 
ATOM   5789 H HD23 . LEU   B 1 93  ? 40.498 -16.581 -3.343  1.00 13.35 ?  93  LEU   B HD23 1 
ATOM   5790 N N    . HIS   B 1 94  ? 44.459 -15.393 0.012   1.00 8.94  ?  94  HIS   B N    1 
ATOM   5791 C CA   . HIS   B 1 94  ? 44.670 -16.298 1.138   1.00 9.05  ?  94  HIS   B CA   1 
ATOM   5792 C C    . HIS   B 1 94  ? 43.311 -16.646 1.721   1.00 9.17  ?  94  HIS   B C    1 
ATOM   5793 O O    . HIS   B 1 94  ? 42.642 -15.768 2.271   1.00 10.54 ?  94  HIS   B O    1 
ATOM   5794 C CB   . HIS   B 1 94  ? 45.540 -15.621 2.195   1.00 9.54  ?  94  HIS   B CB   1 
ATOM   5795 C CG   . HIS   B 1 94  ? 46.921 -15.326 1.722   1.00 9.31  ?  94  HIS   B CG   1 
ATOM   5796 N ND1  . HIS   B 1 94  ? 47.949 -16.240 1.813   1.00 9.63  ?  94  HIS   B ND1  1 
ATOM   5797 C CD2  . HIS   B 1 94  ? 47.426 -14.224 1.115   1.00 10.06 ?  94  HIS   B CD2  1 
ATOM   5798 C CE1  . HIS   B 1 94  ? 49.035 -15.692 1.296   1.00 9.72  ?  94  HIS   B CE1  1 
ATOM   5799 N NE2  . HIS   B 1 94  ? 48.748 -14.472 0.868   1.00 10.00 ?  94  HIS   B NE2  1 
ATOM   5800 H H    . HIS   B 1 94  ? 44.529 -14.559 0.219   1.00 10.76 ?  94  HIS   B H    1 
ATOM   5801 H HA   . HIS   B 1 94  ? 45.107 -17.110 0.837   1.00 10.89 ?  94  HIS   B HA   1 
ATOM   5802 H HB2  . HIS   B 1 94  ? 45.124 -14.784 2.454   1.00 11.48 ?  94  HIS   B HB2  1 
ATOM   5803 H HB3  . HIS   B 1 94  ? 45.608 -16.207 2.966   1.00 11.48 ?  94  HIS   B HB3  1 
ATOM   5804 H HD2  . HIS   B 1 94  ? 46.973 -13.439 0.913   1.00 12.10 ?  94  HIS   B HD2  1 
ATOM   5805 H HE1  . HIS   B 1 94  ? 49.870 -16.112 1.246   1.00 11.69 ?  94  HIS   B HE1  1 
ATOM   5806 H HE2  . HIS   B 1 94  ? 49.309 -13.939 0.496   1.00 12.03 ?  94  HIS   B HE2  1 
ATOM   5807 N N    . VAL   B 1 95  ? 42.875 -17.897 1.566   1.00 9.26  ?  95  VAL   B N    1 
ATOM   5808 C CA   . VAL   B 1 95  ? 41.548 -18.331 2.000   1.00 9.60  ?  95  VAL   B CA   1 
ATOM   5809 C C    . VAL   B 1 95  ? 41.712 -19.365 3.094   1.00 9.68  ?  95  VAL   B C    1 
ATOM   5810 O O    . VAL   B 1 95  ? 42.479 -20.321 2.934   1.00 10.22 ?  95  VAL   B O    1 
ATOM   5811 C CB   . VAL   B 1 95  ? 40.731 -18.940 0.846   1.00 9.75  ?  95  VAL   B CB   1 
ATOM   5812 C CG1  . VAL   B 1 95  ? 39.368 -19.392 1.344   1.00 10.67 ?  95  VAL   B CG1  1 
ATOM   5813 C CG2  . VAL   B 1 95  ? 40.589 -17.960 -0.282  1.00 9.91  ?  95  VAL   B CG2  1 
ATOM   5814 H H    . VAL   B 1 95  ? 43.336 -18.525 1.197   1.00 11.14 ?  95  VAL   B H    1 
ATOM   5815 H HA   . VAL   B 1 95  ? 41.055 -17.573 2.358   1.00 11.55 ?  95  VAL   B HA   1 
ATOM   5816 H HB   . VAL   B 1 95  ? 41.191 -19.717 0.506   1.00 11.73 ?  95  VAL   B HB   1 
ATOM   5817 H HG11 . VAL   B 1 95  ? 38.786 -19.556 0.583   1.00 12.83 ?  95  VAL   B HG11 1 
ATOM   5818 H HG12 . VAL   B 1 95  ? 39.466 -20.206 1.861   1.00 12.83 ?  95  VAL   B HG12 1 
ATOM   5819 H HG13 . VAL   B 1 95  ? 38.981 -18.693 1.901   1.00 12.83 ?  95  VAL   B HG13 1 
ATOM   5820 H HG21 . VAL   B 1 95  ? 40.011 -18.349 -0.960  1.00 11.92 ?  95  VAL   B HG21 1 
ATOM   5821 H HG22 . VAL   B 1 95  ? 40.186 -17.145 0.062   1.00 11.92 ?  95  VAL   B HG22 1 
ATOM   5822 H HG23 . VAL   B 1 95  ? 41.460 -17.778 -0.647  1.00 11.92 ?  95  VAL   B HG23 1 
ATOM   5823 N N    . VAL   B 1 96  ? 40.980 -19.191 4.187   1.00 10.14 ?  96  VAL   B N    1 
ATOM   5824 C CA   . VAL   B 1 96  ? 41.060 -20.104 5.327   1.00 10.46 ?  96  VAL   B CA   1 
ATOM   5825 C C    . VAL   B 1 96  ? 39.873 -21.066 5.284   1.00 10.94 ?  96  VAL   B C    1 
ATOM   5826 O O    . VAL   B 1 96  ? 38.755 -20.714 5.671   1.00 11.64 ?  96  VAL   B O    1 
ATOM   5827 C CB   . VAL   B 1 96  ? 41.123 -19.355 6.660   1.00 11.24 ?  96  VAL   B CB   1 
ATOM   5828 C CG1  . VAL   B 1 96  ? 41.270 -20.355 7.802   1.00 11.85 ?  96  VAL   B CG1  1 
ATOM   5829 C CG2  . VAL   B 1 96  ? 42.257 -18.336 6.662   1.00 12.18 ?  96  VAL   B CG2  1 
ATOM   5830 H H    . VAL   B 1 96  ? 40.415 -18.552 4.296   1.00 12.20 ?  96  VAL   B H    1 
ATOM   5831 H HA   . VAL   B 1 96  ? 41.870 -20.632 5.246   1.00 12.57 ?  96  VAL   B HA   1 
ATOM   5832 H HB   . VAL   B 1 96  ? 40.288 -18.875 6.788   1.00 13.51 ?  96  VAL   B HB   1 
ATOM   5833 H HG11 . VAL   B 1 96  ? 41.481 -19.870 8.616   1.00 14.25 ?  96  VAL   B HG11 1 
ATOM   5834 H HG12 . VAL   B 1 96  ? 40.434 -20.836 7.915   1.00 14.25 ?  96  VAL   B HG12 1 
ATOM   5835 H HG13 . VAL   B 1 96  ? 41.984 -20.973 7.591   1.00 14.25 ?  96  VAL   B HG13 1 
ATOM   5836 H HG21 . VAL   B 1 96  ? 42.311 -17.928 7.539   1.00 14.65 ?  96  VAL   B HG21 1 
ATOM   5837 H HG22 . VAL   B 1 96  ? 43.088 -18.790 6.454   1.00 14.65 ?  96  VAL   B HG22 1 
ATOM   5838 H HG23 . VAL   B 1 96  ? 42.074 -17.658 5.992   1.00 14.65 ?  96  VAL   B HG23 1 
ATOM   5839 N N    . GLY   B 1 97  ? 40.111 -22.295 4.837   1.00 11.06 ?  97  GLY   B N    1 
ATOM   5840 C CA   . GLY   B 1 97  ? 39.144 -23.357 5.005   1.00 11.83 ?  97  GLY   B CA   1 
ATOM   5841 C C    . GLY   B 1 97  ? 39.268 -23.973 6.384   1.00 12.71 ?  97  GLY   B C    1 
ATOM   5842 O O    . GLY   B 1 97  ? 40.312 -23.860 7.039   1.00 13.16 ?  97  GLY   B O    1 
ATOM   5843 H H    . GLY   B 1 97  ? 40.833 -22.533 4.427   1.00 13.30 ?  97  GLY   B H    1 
ATOM   5844 H HA2  . GLY   B 1 97  ? 38.247 -22.996 4.887   1.00 14.22 ?  97  GLY   B HA2  1 
ATOM   5845 H HA3  . GLY   B 1 97  ? 39.288 -24.043 4.333   1.00 14.22 ?  97  GLY   B HA3  1 
ATOM   5846 N N    . PRO   B 1 98  ? 38.216 -24.649 6.851   1.00 13.74 ?  98  PRO   B N    1 
ATOM   5847 C CA   . PRO   B 1 98  ? 38.309 -25.342 8.140   1.00 15.06 ?  98  PRO   B CA   1 
ATOM   5848 C C    . PRO   B 1 98  ? 39.337 -26.461 8.095   1.00 14.68 ?  98  PRO   B C    1 
ATOM   5849 O O    . PRO   B 1 98  ? 39.445 -27.197 7.115   1.00 14.71 ?  98  PRO   B O    1 
ATOM   5850 C CB   . PRO   B 1 98  ? 36.892 -25.890 8.346   1.00 15.77 ?  98  PRO   B CB   1 
ATOM   5851 C CG   . PRO   B 1 98  ? 36.320 -26.017 6.985   1.00 15.11 ?  98  PRO   B CG   1 
ATOM   5852 C CD   . PRO   B 1 98  ? 36.892 -24.845 6.223   1.00 14.10 ?  98  PRO   B CD   1 
ATOM   5853 H HA   . PRO   B 1 98  ? 38.526 -24.720 8.843   1.00 18.10 ?  98  PRO   B HA   1 
ATOM   5854 H HB2  . PRO   B 1 98  ? 36.937 -26.760 8.777   1.00 18.95 ?  98  PRO   B HB2  1 
ATOM   5855 H HB3  . PRO   B 1 98  ? 36.371 -25.270 8.874   1.00 18.95 ?  98  PRO   B HB3  1 
ATOM   5856 H HG2  . PRO   B 1 98  ? 36.604 -26.861 6.587   1.00 18.16 ?  98  PRO   B HG2  1 
ATOM   5857 H HG3  . PRO   B 1 98  ? 35.353 -25.970 7.026   1.00 18.16 ?  98  PRO   B HG3  1 
ATOM   5858 H HD2  . PRO   B 1 98  ? 36.984 -25.070 5.276   1.00 16.94 ?  98  PRO   B HD2  1 
ATOM   5859 H HD3  . PRO   B 1 98  ? 36.336 -24.060 6.341   1.00 16.94 ?  98  PRO   B HD3  1 
ATOM   5860 N N    . ASN   B 1 99  ? 40.085 -26.593 9.179   1.00 15.92 ?  99  ASN   B N    1 
ATOM   5861 C CA   . ASN   B 1 99  ? 41.061 -27.668 9.336   1.00 17.09 ?  99  ASN   B CA   1 
ATOM   5862 C C    . ASN   B 1 99  ? 40.433 -28.746 10.217  1.00 19.35 ?  99  ASN   B C    1 
ATOM   5863 O O    . ASN   B 1 99  ? 40.356 -28.596 11.440  1.00 20.09 ?  99  ASN   B O    1 
ATOM   5864 C CB   . ASN   B 1 99  ? 42.342 -27.113 9.943   1.00 17.18 ?  99  ASN   B CB   1 
ATOM   5865 C CG   . ASN   B 1 99  ? 43.469 -28.121 9.941   1.00 18.03 ?  99  ASN   B CG   1 
ATOM   5866 O OD1  . ASN   B 1 99  ? 43.242 -29.312 10.109  1.00 18.75 ?  99  ASN   B OD1  1 
ATOM   5867 N ND2  . ASN   B 1 99  ? 44.687 -27.652 9.741   1.00 18.28 ?  99  ASN   B ND2  1 
ATOM   5868 H H    . ASN   B 1 99  ? 40.045 -26.058 9.845   1.00 19.13 ?  99  ASN   B H    1 
ATOM   5869 H HA   . ASN   B 1 99  ? 41.263 -28.058 8.470   1.00 20.54 ?  99  ASN   B HA   1 
ATOM   5870 H HB2  . ASN   B 1 99  ? 42.622 -26.345 9.435   1.00 20.64 ?  99  ASN   B HB2  1 
ATOM   5871 H HB3  . ASN   B 1 99  ? 42.163 -26.866 10.865  1.00 20.64 ?  99  ASN   B HB3  1 
ATOM   5872 H HD21 . ASN   B 1 99  ? 45.356 -28.189 9.731   1.00 21.97 ?  99  ASN   B HD21 1 
ATOM   5873 H HD22 . ASN   B 1 99  ? 44.801 -26.810 9.636   1.00 21.97 ?  99  ASN   B HD22 1 
ATOM   5874 N N    A VAL   B 1 100 ? 39.965 -29.828 9.588   0.42 21.63 ?  100 VAL   B N    1 
ATOM   5875 N N    B VAL   B 1 100 ? 39.981 -29.832 9.582   0.58 21.55 ?  100 VAL   B N    1 
ATOM   5876 C CA   A VAL   B 1 100 ? 39.355 -30.919 10.346  0.42 24.08 ?  100 VAL   B CA   1 
ATOM   5877 C CA   B VAL   B 1 100 ? 39.359 -30.932 10.315  0.58 24.04 ?  100 VAL   B CA   1 
ATOM   5878 C C    A VAL   B 1 100 ? 40.371 -31.577 11.273  0.42 24.63 ?  100 VAL   B C    1 
ATOM   5879 C C    B VAL   B 1 100 ? 40.362 -31.609 11.244  0.58 24.37 ?  100 VAL   B C    1 
ATOM   5880 O O    A VAL   B 1 100 ? 40.015 -32.046 12.361  0.42 25.23 ?  100 VAL   B O    1 
ATOM   5881 O O    B VAL   B 1 100 ? 39.986 -32.129 12.302  0.58 24.89 ?  100 VAL   B O    1 
ATOM   5882 C CB   A VAL   B 1 100 ? 38.684 -31.929 9.392   0.42 26.14 ?  100 VAL   B CB   1 
ATOM   5883 C CB   B VAL   B 1 100 ? 38.712 -31.922 9.327   0.58 26.41 ?  100 VAL   B CB   1 
ATOM   5884 C CG1  A VAL   B 1 100 ? 38.202 -33.154 10.155  0.42 26.88 ?  100 VAL   B CG1  1 
ATOM   5885 C CG1  B VAL   B 1 100 ? 38.215 -33.161 10.052  0.58 27.33 ?  100 VAL   B CG1  1 
ATOM   5886 C CG2  A VAL   B 1 100 ? 37.522 -31.267 8.664   0.42 26.74 ?  100 VAL   B CG2  1 
ATOM   5887 C CG2  B VAL   B 1 100 ? 37.569 -31.248 8.580   0.58 26.99 ?  100 VAL   B CG2  1 
ATOM   5888 H H    A VAL   B 1 100 ? 39.980 -29.947 8.732   0.42 25.98 ?  100 VAL   B H    1 
ATOM   5889 H H    B VAL   B 1 100 ? 40.021 -29.952 8.728   0.58 25.89 ?  100 VAL   B H    1 
ATOM   5890 H HA   A VAL   B 1 100 ? 38.652 -30.545 10.900  0.42 28.92 ?  100 VAL   B HA   1 
ATOM   5891 H HA   B VAL   B 1 100 ? 38.648 -30.571 10.862  0.58 28.87 ?  100 VAL   B HA   1 
ATOM   5892 H HB   A VAL   B 1 100 ? 39.329 -32.224 8.730   0.42 31.39 ?  100 VAL   B HB   1 
ATOM   5893 H HB   B VAL   B 1 100 ? 39.373 -32.205 8.674   0.58 31.72 ?  100 VAL   B HB   1 
ATOM   5894 H HG11 A VAL   B 1 100 ? 37.598 -33.661 9.588   0.42 32.29 ?  100 VAL   B HG11 1 
ATOM   5895 H HG11 B VAL   B 1 100 ? 37.624 -33.656 9.462   0.58 32.82 ?  100 VAL   B HG11 1 
ATOM   5896 H HG12 A VAL   B 1 100 ? 38.965 -33.702 10.395  0.42 32.29 ?  100 VAL   B HG12 1 
ATOM   5897 H HG12 B VAL   B 1 100 ? 38.974 -33.714 10.296  0.58 32.82 ?  100 VAL   B HG12 1 
ATOM   5898 H HG13 A VAL   B 1 100 ? 37.735 -32.864 10.954  0.42 32.29 ?  100 VAL   B HG13 1 
ATOM   5899 H HG13 B VAL   B 1 100 ? 37.732 -32.888 10.848  0.58 32.82 ?  100 VAL   B HG13 1 
ATOM   5900 H HG21 A VAL   B 1 100 ? 37.100 -31.919 8.082   0.42 32.12 ?  100 VAL   B HG21 1 
ATOM   5901 H HG21 B VAL   B 1 100 ? 37.157 -31.892 7.983   0.58 32.41 ?  100 VAL   B HG21 1 
ATOM   5902 H HG22 A VAL   B 1 100 ? 36.881 -30.946 9.319   0.42 32.12 ?  100 VAL   B HG22 1 
ATOM   5903 H HG22 B VAL   B 1 100 ? 36.917 -30.931 9.225   0.58 32.41 ?  100 VAL   B HG22 1 
ATOM   5904 H HG23 A VAL   B 1 100 ? 37.860 -30.526 8.140   0.42 32.12 ?  100 VAL   B HG23 1 
ATOM   5905 H HG23 B VAL   B 1 100 ? 37.922 -30.503 8.072   0.58 32.41 ?  100 VAL   B HG23 1 
ATOM   5906 N N    . ASN   B 1 101 ? 41.644 -31.626 10.867  1.00 25.10 ?  101 ASN   B N    1 
ATOM   5907 C CA   . ASN   B 1 101 ? 42.682 -32.161 11.747  1.00 26.79 ?  101 ASN   B CA   1 
ATOM   5908 C C    . ASN   B 1 101 ? 42.863 -31.319 13.004  1.00 29.99 ?  101 ASN   B C    1 
ATOM   5909 O O    . ASN   B 1 101 ? 43.477 -31.791 13.971  1.00 30.67 ?  101 ASN   B O    1 
ATOM   5910 C CB   . ASN   B 1 101 ? 44.004 -32.305 10.988  1.00 26.39 ?  101 ASN   B CB   1 
ATOM   5911 C CG   . ASN   B 1 101 ? 43.981 -33.454 9.993   1.00 25.72 ?  101 ASN   B CG   1 
ATOM   5912 O OD1  . ASN   B 1 101 ? 43.255 -34.430 10.174  1.00 26.29 ?  101 ASN   B OD1  1 
ATOM   5913 N ND2  . ASN   B 1 101 ? 44.772 -33.337 8.932   1.00 25.51 ?  101 ASN   B ND2  1 
ATOM   5914 H H    A ASN   B 1 101 ? 41.921 -31.369 10.093  0.42 30.14 ?  101 ASN   B H    1 
ATOM   5915 H H    B ASN   B 1 101 ? 41.929 -31.345 10.105  0.58 30.14 ?  101 ASN   B H    1 
ATOM   5916 H HA   . ASN   B 1 101 ? 42.413 -33.043 12.031  1.00 32.17 ?  101 ASN   B HA   1 
ATOM   5917 H HB2  . ASN   B 1 101 ? 44.185 -31.486 10.498  1.00 31.70 ?  101 ASN   B HB2  1 
ATOM   5918 H HB3  . ASN   B 1 101 ? 44.716 -32.476 11.621  1.00 31.70 ?  101 ASN   B HB3  1 
ATOM   5919 H HD21 . ASN   B 1 101 ? 44.793 -33.961 8.340   1.00 30.64 ?  101 ASN   B HD21 1 
ATOM   5920 H HD22 . ASN   B 1 101 ? 45.271 -32.641 8.840   1.00 30.64 ?  101 ASN   B HD22 1 
ATOM   5921 N N    A LYS   B 1 102 ? 42.350 -30.087 13.010  0.42 32.09 ?  102 LYS   B N    1 
ATOM   5922 N N    B LYS   B 1 102 ? 42.353 -30.087 13.011  0.58 32.05 ?  102 LYS   B N    1 
ATOM   5923 C CA   A LYS   B 1 102 ? 42.318 -29.241 14.195  0.42 34.11 ?  102 LYS   B CA   1 
ATOM   5924 C CA   B LYS   B 1 102 ? 42.319 -29.249 14.203  0.58 34.14 ?  102 LYS   B CA   1 
ATOM   5925 C C    A LYS   B 1 102 ? 40.945 -29.221 14.857  0.42 33.49 ?  102 LYS   B C    1 
ATOM   5926 C C    B LYS   B 1 102 ? 40.932 -29.192 14.831  0.58 33.34 ?  102 LYS   B C    1 
ATOM   5927 O O    A LYS   B 1 102 ? 40.732 -28.447 15.795  0.42 33.66 ?  102 LYS   B O    1 
ATOM   5928 O O    B LYS   B 1 102 ? 40.696 -28.363 15.714  0.58 33.41 ?  102 LYS   B O    1 
ATOM   5929 C CB   A LYS   B 1 102 ? 42.722 -27.808 13.842  0.42 36.76 ?  102 LYS   B CB   1 
ATOM   5930 C CB   B LYS   B 1 102 ? 42.786 -27.829 13.877  0.58 37.10 ?  102 LYS   B CB   1 
ATOM   5931 C CG   A LYS   B 1 102 ? 44.180 -27.613 13.464  0.42 39.09 ?  102 LYS   B CG   1 
ATOM   5932 C CG   B LYS   B 1 102 ? 44.256 -27.706 13.521  0.58 39.81 ?  102 LYS   B CG   1 
ATOM   5933 C CD   A LYS   B 1 102 ? 44.432 -26.153 13.117  0.42 41.17 ?  102 LYS   B CD   1 
ATOM   5934 C CD   B LYS   B 1 102 ? 44.580 -26.284 13.094  0.58 42.32 ?  102 LYS   B CD   1 
ATOM   5935 C CE   A LYS   B 1 102 ? 45.893 -25.877 12.814  0.42 42.61 ?  102 LYS   B CE   1 
ATOM   5936 C CE   B LYS   B 1 102 ? 46.071 -26.066 12.919  0.58 44.11 ?  102 LYS   B CE   1 
ATOM   5937 N NZ   A LYS   B 1 102 ? 46.113 -24.448 12.448  0.42 43.43 ?  102 LYS   B NZ   1 
ATOM   5938 N NZ   B LYS   B 1 102 ? 46.362 -24.673 12.477  0.58 45.19 ?  102 LYS   B NZ   1 
ATOM   5939 H H    A LYS   B 1 102 ? 42.003 -29.709 12.317  0.42 38.54 ?  102 LYS   B H    1 
ATOM   5940 H H    B LYS   B 1 102 ? 42.007 -29.706 12.319  0.58 38.49 ?  102 LYS   B H    1 
ATOM   5941 H HA   A LYS   B 1 102 ? 42.958 -29.579 14.839  0.42 40.96 ?  102 LYS   B HA   1 
ATOM   5942 H HA   B LYS   B 1 102 ? 42.933 -29.616 14.858  0.58 40.99 ?  102 LYS   B HA   1 
ATOM   5943 H HB2  A LYS   B 1 102 ? 42.186 -27.511 13.092  0.42 44.13 ?  102 LYS   B HB2  1 
ATOM   5944 H HB2  B LYS   B 1 102 ? 42.273 -27.498 13.125  0.58 44.55 ?  102 LYS   B HB2  1 
ATOM   5945 H HB3  A LYS   B 1 102 ? 42.546 -27.241 14.610  0.42 44.13 ?  102 LYS   B HB3  1 
ATOM   5946 H HB3  B LYS   B 1 102 ? 42.627 -27.265 14.653  0.58 44.55 ?  102 LYS   B HB3  1 
ATOM   5947 H HG2  A LYS   B 1 102 ? 44.748 -27.855 14.213  0.42 46.94 ?  102 LYS   B HG2  1 
ATOM   5948 H HG2  B LYS   B 1 102 ? 44.798 -27.924 14.296  0.58 47.79 ?  102 LYS   B HG2  1 
ATOM   5949 H HG3  A LYS   B 1 102 ? 44.391 -28.156 12.688  0.42 46.94 ?  102 LYS   B HG3  1 
ATOM   5950 H HG3  B LYS   B 1 102 ? 44.462 -28.303 12.784  0.58 47.79 ?  102 LYS   B HG3  1 
ATOM   5951 H HD2  A LYS   B 1 102 ? 43.911 -25.919 12.332  0.42 49.43 ?  102 LYS   B HD2  1 
ATOM   5952 H HD2  B LYS   B 1 102 ? 44.146 -26.100 12.245  0.58 50.82 ?  102 LYS   B HD2  1 
ATOM   5953 H HD3  A LYS   B 1 102 ? 44.169 -25.598 13.868  0.42 49.43 ?  102 LYS   B HD3  1 
ATOM   5954 H HD3  B LYS   B 1 102 ? 44.261 -25.667 13.771  0.58 50.82 ?  102 LYS   B HD3  1 
ATOM   5955 H HE2  A LYS   B 1 102 ? 46.426 -26.075 13.600  0.42 51.16 ?  102 LYS   B HE2  1 
ATOM   5956 H HE2  B LYS   B 1 102 ? 46.520 -26.217 13.766  0.58 52.96 ?  102 LYS   B HE2  1 
ATOM   5957 H HE3  A LYS   B 1 102 ? 46.175 -26.429 12.068  0.42 51.16 ?  102 LYS   B HE3  1 
ATOM   5958 H HE3  B LYS   B 1 102 ? 46.409 -26.677 12.245  0.58 52.96 ?  102 LYS   B HE3  1 
ATOM   5959 H HZ1  A LYS   B 1 102 ? 46.974 -24.307 12.275  0.42 52.14 ?  102 LYS   B HZ1  1 
ATOM   5960 H HZ1  B LYS   B 1 102 ? 47.238 -24.560 12.379  0.58 54.25 ?  102 LYS   B HZ1  1 
ATOM   5961 H HZ2  A LYS   B 1 102 ? 45.634 -24.243 11.726  0.42 52.14 ?  102 LYS   B HZ2  1 
ATOM   5962 H HZ2  B LYS   B 1 102 ? 45.960 -24.511 11.699  0.58 54.25 ?  102 LYS   B HZ2  1 
ATOM   5963 H HZ3  A LYS   B 1 102 ? 45.862 -23.920 13.120  0.42 52.14 ?  102 LYS   B HZ3  1 
ATOM   5964 H HZ3  B LYS   B 1 102 ? 46.061 -24.093 13.082  0.58 54.25 ?  102 LYS   B HZ3  1 
ATOM   5965 N N    . GLY   B 1 103 ? 40.006 -30.035 14.380  1.00 32.86 ?  103 GLY   B N    1 
ATOM   5966 C CA   . GLY   B 1 103 ? 38.675 -30.082 14.951  1.00 32.30 ?  103 GLY   B CA   1 
ATOM   5967 C C    . GLY   B 1 103 ? 37.734 -28.993 14.491  1.00 31.16 ?  103 GLY   B C    1 
ATOM   5968 O O    . GLY   B 1 103 ? 36.642 -28.863 15.057  1.00 31.47 ?  103 GLY   B O    1 
ATOM   5969 H H    A GLY   B 1 103 ? 40.120 -30.571 13.719  0.42 39.46 ?  103 GLY   B H    1 
ATOM   5970 H H    B GLY   B 1 103 ? 40.127 -30.585 13.731  0.58 39.46 ?  103 GLY   B H    1 
ATOM   5971 H HA2  . GLY   B 1 103 ? 38.274 -30.939 14.738  1.00 38.79 ?  103 GLY   B HA2  1 
ATOM   5972 H HA3  . GLY   B 1 103 ? 38.745 -30.017 15.916  1.00 38.79 ?  103 GLY   B HA3  1 
ATOM   5973 N N    A GLU   B 1 104 ? 38.125 -28.193 13.503  0.42 30.55 ?  104 GLU   B N    1 
ATOM   5974 N N    B GLU   B 1 104 ? 38.102 -28.220 13.475  0.58 30.02 ?  104 GLU   B N    1 
ATOM   5975 C CA   A GLU   B 1 104 ? 37.288 -27.091 13.055  0.42 29.71 ?  104 GLU   B CA   1 
ATOM   5976 C CA   B GLU   B 1 104 ? 37.246 -27.143 13.003  0.58 28.68 ?  104 GLU   B CA   1 
ATOM   5977 C C    A GLU   B 1 104 ? 36.098 -27.612 12.255  0.42 30.12 ?  104 GLU   B C    1 
ATOM   5978 C C    B GLU   B 1 104 ? 36.081 -27.691 12.184  0.58 29.13 ?  104 GLU   B C    1 
ATOM   5979 O O    A GLU   B 1 104 ? 36.136 -28.701 11.674  0.42 30.49 ?  104 GLU   B O    1 
ATOM   5980 O O    B GLU   B 1 104 ? 36.157 -28.775 11.596  0.58 29.78 ?  104 GLU   B O    1 
ATOM   5981 C CB   A GLU   B 1 104 ? 38.120 -26.105 12.234  0.42 28.82 ?  104 GLU   B CB   1 
ATOM   5982 C CB   B GLU   B 1 104 ? 38.067 -26.130 12.204  0.58 27.49 ?  104 GLU   B CB   1 
ATOM   5983 C CG   A GLU   B 1 104 ? 39.224 -25.446 13.056  0.42 27.98 ?  104 GLU   B CG   1 
ATOM   5984 C CG   B GLU   B 1 104 ? 39.149 -25.475 13.055  0.58 26.25 ?  104 GLU   B CG   1 
ATOM   5985 C CD   A GLU   B 1 104 ? 40.137 -24.552 12.242  0.42 27.32 ?  104 GLU   B CD   1 
ATOM   5986 C CD   B GLU   B 1 104 ? 40.107 -24.601 12.274  0.58 25.10 ?  104 GLU   B CD   1 
ATOM   5987 O OE1  A GLU   B 1 104 ? 40.122 -24.641 10.998  0.42 26.27 ?  104 GLU   B OE1  1 
ATOM   5988 O OE1  B GLU   B 1 104 ? 40.116 -24.660 11.027  0.58 23.31 ?  104 GLU   B OE1  1 
ATOM   5989 O OE2  A GLU   B 1 104 ? 40.880 -23.758 12.857  0.42 27.36 -1 104 GLU   B OE2  1 
ATOM   5990 O OE2  B GLU   B 1 104 ? 40.865 -23.849 12.922  0.58 25.03 -1 104 GLU   B OE2  1 
ATOM   5991 H H    A GLU   B 1 104 ? 38.874 -28.262 13.084  0.42 36.69 ?  104 GLU   B H    1 
ATOM   5992 H H    B GLU   B 1 104 ? 38.847 -28.292 13.048  0.58 36.05 ?  104 GLU   B H    1 
ATOM   5993 H HA   A GLU   B 1 104 ? 36.945 -26.618 13.829  0.42 35.68 ?  104 GLU   B HA   1 
ATOM   5994 H HA   B GLU   B 1 104 ? 36.874 -26.683 13.769  0.58 34.44 ?  104 GLU   B HA   1 
ATOM   5995 H HB2  A GLU   B 1 104 ? 38.540 -26.577 11.497  0.42 34.61 ?  104 GLU   B HB2  1 
ATOM   5996 H HB2  B GLU   B 1 104 ? 38.497 -26.581 11.462  0.58 33.01 ?  104 GLU   B HB2  1 
ATOM   5997 H HB3  A GLU   B 1 104 ? 37.542 -25.404 11.894  0.42 34.61 ?  104 GLU   B HB3  1 
ATOM   5998 H HB3  B GLU   B 1 104 ? 37.478 -25.432 11.875  0.58 33.01 ?  104 GLU   B HB3  1 
ATOM   5999 H HG2  A GLU   B 1 104 ? 38.819 -24.902 13.751  0.42 33.61 ?  104 GLU   B HG2  1 
ATOM   6000 H HG2  B GLU   B 1 104 ? 38.725 -24.919 13.728  0.58 31.52 ?  104 GLU   B HG2  1 
ATOM   6001 H HG3  A GLU   B 1 104 ? 39.776 -26.134 13.457  0.42 33.61 ?  104 GLU   B HG3  1 
ATOM   6002 H HG3  B GLU   B 1 104 ? 39.674 -26.167 13.485  0.58 31.52 ?  104 GLU   B HG3  1 
ATOM   6003 N N    A ASP   B 1 105 ? 35.027 -26.821 12.239  0.42 29.91 ?  105 ASP   B N    1 
ATOM   6004 N N    B ASP   B 1 105 ? 34.987 -26.929 12.163  0.58 28.48 ?  105 ASP   B N    1 
ATOM   6005 C CA   A ASP   B 1 105 ? 33.757 -27.271 11.683  0.42 30.28 ?  105 ASP   B CA   1 
ATOM   6006 C CA   B ASP   B 1 105 ? 33.722 -27.400 11.611  0.58 28.77 ?  105 ASP   B CA   1 
ATOM   6007 C C    A ASP   B 1 105 ? 33.831 -27.328 10.162  0.42 28.57 ?  105 ASP   B C    1 
ATOM   6008 C C    B ASP   B 1 105 ? 33.782 -27.413 10.089  0.58 26.35 ?  105 ASP   B C    1 
ATOM   6009 O O    A ASP   B 1 105 ? 34.047 -26.305 9.503   0.42 28.06 ?  105 ASP   B O    1 
ATOM   6010 O O    B ASP   B 1 105 ? 33.931 -26.361 9.458   0.58 25.39 ?  105 ASP   B O    1 
ATOM   6011 C CB   A ASP   B 1 105 ? 32.641 -26.326 12.125  0.42 32.42 ?  105 ASP   B CB   1 
ATOM   6012 C CB   B ASP   B 1 105 ? 32.581 -26.502 12.086  0.58 31.70 ?  105 ASP   B CB   1 
ATOM   6013 C CG   A ASP   B 1 105 ? 31.268 -26.804 11.699  0.42 34.37 ?  105 ASP   B CG   1 
ATOM   6014 C CG   B ASP   B 1 105 ? 31.214 -27.066 11.745  0.58 34.19 ?  105 ASP   B CG   1 
ATOM   6015 O OD1  A ASP   B 1 105 ? 31.167 -27.917 11.141  0.42 34.74 ?  105 ASP   B OD1  1 
ATOM   6016 O OD1  B ASP   B 1 105 ? 31.148 -28.078 11.017  0.58 34.73 ?  105 ASP   B OD1  1 
ATOM   6017 O OD2  A ASP   B 1 105 ? 30.286 -26.062 11.920  0.42 35.31 -1 105 ASP   B OD2  1 
ATOM   6018 O OD2  B ASP   B 1 105 ? 30.203 -26.501 12.214  0.58 35.20 -1 105 ASP   B OD2  1 
ATOM   6019 H H    A ASP   B 1 105 ? 35.012 -26.018 12.547  0.42 35.92 ?  105 ASP   B H    1 
ATOM   6020 H H    B ASP   B 1 105 ? 34.955 -26.128 12.467  0.58 34.20 ?  105 ASP   B H    1 
ATOM   6021 H HA   A ASP   B 1 105 ? 33.558 -28.160 12.013  0.42 36.37 ?  105 ASP   B HA   1 
ATOM   6022 H HA   B ASP   B 1 105 ? 33.547 -28.303 11.915  0.58 34.55 ?  105 ASP   B HA   1 
ATOM   6023 H HB2  A ASP   B 1 105 ? 32.658 -26.252 13.094  0.42 38.93 ?  105 ASP   B HB2  1 
ATOM   6024 H HB2  B ASP   B 1 105 ? 32.634 -26.405 13.049  0.58 38.07 ?  105 ASP   B HB2  1 
ATOM   6025 H HB3  A ASP   B 1 105 ? 32.784 -25.456 11.724  0.42 38.93 ?  105 ASP   B HB3  1 
ATOM   6026 H HB3  B ASP   B 1 105 ? 32.662 -25.632 11.660  0.58 38.07 ?  105 ASP   B HB3  1 
ATOM   6027 N N    A ILE   B 1 106 ? 33.635 -28.527 9.607   0.42 27.77 ?  106 ILE   B N    1 
ATOM   6028 N N    B ILE   B 1 106 ? 33.631 -28.604 9.503   0.58 25.95 ?  106 ILE   B N    1 
ATOM   6029 C CA   A ILE   B 1 106 ? 33.642 -28.715 8.161   0.42 26.98 ?  106 ILE   B CA   1 
ATOM   6030 C CA   B ILE   B 1 106 ? 33.621 -28.752 8.052   0.58 25.45 ?  106 ILE   B CA   1 
ATOM   6031 C C    A ILE   B 1 106 ? 32.557 -27.890 7.477   0.42 26.02 ?  106 ILE   B C    1 
ATOM   6032 C C    B ILE   B 1 106 ? 32.526 -27.910 7.408   0.58 24.26 ?  106 ILE   B C    1 
ATOM   6033 O O    A ILE   B 1 106 ? 32.679 -27.572 6.290   0.42 25.56 ?  106 ILE   B O    1 
ATOM   6034 O O    B ILE   B 1 106 ? 32.613 -27.586 6.219   0.58 22.98 ?  106 ILE   B O    1 
ATOM   6035 C CB   A ILE   B 1 106 ? 33.522 -30.222 7.830   0.42 27.20 ?  106 ILE   B CB   1 
ATOM   6036 C CB   B ILE   B 1 106 ? 33.500 -30.251 7.687   0.58 26.24 ?  106 ILE   B CB   1 
ATOM   6037 C CG1  A ILE   B 1 106 ? 33.764 -30.477 6.340   0.42 27.07 ?  106 ILE   B CG1  1 
ATOM   6038 C CG1  B ILE   B 1 106 ? 33.780 -30.481 6.199   0.58 26.51 ?  106 ILE   B CG1  1 
ATOM   6039 C CG2  A ILE   B 1 106 ? 32.156 -30.755 8.246   0.42 27.57 ?  106 ILE   B CG2  1 
ATOM   6040 C CG2  B ILE   B 1 106 ? 32.119 -30.786 8.057   0.58 26.84 ?  106 ILE   B CG2  1 
ATOM   6041 C CD1  A ILE   B 1 106 ? 35.119 -30.009 5.855   0.42 26.95 ?  106 ILE   B CD1  1 
ATOM   6042 C CD1  B ILE   B 1 106 ? 35.141 -29.994 5.757   0.58 26.65 ?  106 ILE   B CD1  1 
ATOM   6043 H H    A ILE   B 1 106 ? 33.503 -29.248 10.052  0.42 33.35 ?  106 ILE   B H    1 
ATOM   6044 H H    B ILE   B 1 106 ? 33.531 -29.341 9.927   0.58 31.17 ?  106 ILE   B H    1 
ATOM   6045 H HA   A ILE   B 1 106 ? 34.492 -28.407 7.821   0.42 32.41 ?  106 ILE   B HA   1 
ATOM   6046 H HA   B ILE   B 1 106 ? 34.468 -28.432 7.711   0.58 30.57 ?  106 ILE   B HA   1 
ATOM   6047 H HB   A ILE   B 1 106 ? 34.200 -30.701 8.334   0.42 32.67 ?  106 ILE   B HB   1 
ATOM   6048 H HB   B ILE   B 1 106 ? 34.160 -30.745 8.198   0.58 31.52 ?  106 ILE   B HB   1 
ATOM   6049 H HG12 A ILE   B 1 106 ? 33.707 -31.433 6.172   0.42 32.51 ?  106 ILE   B HG12 1 
ATOM   6050 H HG12 B ILE   B 1 106 ? 33.736 -31.435 6.016   0.58 31.84 ?  106 ILE   B HG12 1 
ATOM   6051 H HG13 A ILE   B 1 106 ? 33.087 -30.015 5.824   0.42 32.51 ?  106 ILE   B HG13 1 
ATOM   6052 H HG13 B ILE   B 1 106 ? 33.112 -30.016 5.675   0.58 31.84 ?  106 ILE   B HG13 1 
ATOM   6053 H HG21 A ILE   B 1 106 ? 32.157 -31.722 8.169   0.42 33.11 ?  106 ILE   B HG21 1 
ATOM   6054 H HG21 B ILE   B 1 106 ? 32.125 -31.753 7.982   0.58 32.24 ?  106 ILE   B HG21 1 
ATOM   6055 H HG22 A ILE   B 1 106 ? 31.983 -30.497 9.165   0.42 33.11 ?  106 ILE   B HG22 1 
ATOM   6056 H HG22 B ILE   B 1 106 ? 31.917 -30.526 8.969   0.58 32.24 ?  106 ILE   B HG22 1 
ATOM   6057 H HG23 A ILE   B 1 106 ? 31.478 -30.379 7.664   0.42 33.11 ?  106 ILE   B HG23 1 
ATOM   6058 H HG23 B ILE   B 1 106 ? 31.461 -30.411 7.452   0.58 32.24 ?  106 ILE   B HG23 1 
ATOM   6059 H HD11 A ILE   B 1 106 ? 35.306 -30.418 4.997   0.42 32.37 ?  106 ILE   B HD11 1 
ATOM   6060 H HD11 B ILE   B 1 106 ? 35.364 -30.408 4.911   0.58 32.00 ?  106 ILE   B HD11 1 
ATOM   6061 H HD12 A ILE   B 1 106 ? 35.106 -29.043 5.764   0.42 32.37 ?  106 ILE   B HD12 1 
ATOM   6062 H HD12 B ILE   B 1 106 ? 35.112 -29.029 5.657   0.58 32.00 ?  106 ILE   B HD12 1 
ATOM   6063 H HD13 A ILE   B 1 106 ? 35.794 -30.272 6.501   0.42 32.37 ?  106 ILE   B HD13 1 
ATOM   6064 H HD13 B ILE   B 1 106 ? 35.797 -30.239 6.429   0.58 32.00 ?  106 ILE   B HD13 1 
ATOM   6065 N N    A GLN   B 1 107 ? 31.495 -27.530 8.201   0.42 25.80 ?  107 GLN   B N    1 
ATOM   6066 N N    B GLN   B 1 107 ? 31.501 -27.525 8.170   0.58 24.57 ?  107 GLN   B N    1 
ATOM   6067 C CA   A GLN   B 1 107 ? 30.423 -26.728 7.619   0.42 25.63 ?  107 GLN   B CA   1 
ATOM   6068 C CA   B GLN   B 1 107 ? 30.416 -26.723 7.616   0.58 24.84 ?  107 GLN   B CA   1 
ATOM   6069 C C    A GLN   B 1 107 ? 30.915 -25.378 7.106   0.42 23.16 ?  107 GLN   B C    1 
ATOM   6070 C C    B GLN   B 1 107 ? 30.890 -25.355 7.138   0.58 22.68 ?  107 GLN   B C    1 
ATOM   6071 O O    A GLN   B 1 107 ? 30.287 -24.807 6.209   0.42 23.42 ?  107 GLN   B O    1 
ATOM   6072 O O    B GLN   B 1 107 ? 30.226 -24.750 6.293   0.58 23.23 ?  107 GLN   B O    1 
ATOM   6073 C CB   A GLN   B 1 107 ? 29.307 -26.527 8.648   0.42 28.50 ?  107 GLN   B CB   1 
ATOM   6074 C CB   B GLN   B 1 107 ? 29.308 -26.565 8.660   0.58 28.32 ?  107 GLN   B CB   1 
ATOM   6075 C CG   A GLN   B 1 107 ? 27.983 -26.033 8.067   0.42 31.17 ?  107 GLN   B CG   1 
ATOM   6076 C CG   B GLN   B 1 107 ? 27.952 -26.158 8.095   0.58 31.63 ?  107 GLN   B CG   1 
ATOM   6077 C CD   A GLN   B 1 107 ? 27.918 -24.521 7.935   0.42 33.29 ?  107 GLN   B CD   1 
ATOM   6078 C CD   B GLN   B 1 107 ? 27.806 -24.656 7.932   0.58 34.23 ?  107 GLN   B CD   1 
ATOM   6079 O OE1  A GLN   B 1 107 ? 28.742 -23.800 8.498   0.42 34.07 ?  107 GLN   B OE1  1 
ATOM   6080 O OE1  B GLN   B 1 107 ? 28.582 -23.879 8.490   0.58 35.22 ?  107 GLN   B OE1  1 
ATOM   6081 N NE2  A GLN   B 1 107 ? 26.930 -24.034 7.188   0.42 34.05 ?  107 GLN   B NE2  1 
ATOM   6082 N NE2  B GLN   B 1 107 ? 26.802 -24.239 7.165   0.58 35.14 ?  107 GLN   B NE2  1 
ATOM   6083 H H    A GLN   B 1 107 ? 31.371 -27.744 9.021   0.42 30.98 ?  107 GLN   B H    1 
ATOM   6084 H H    B GLN   B 1 107 ? 31.419 -27.705 8.998   0.58 29.51 ?  107 GLN   B H    1 
ATOM   6085 H HA   A GLN   B 1 107 ? 30.043 -27.211 6.869   0.42 30.78 ?  107 GLN   B HA   1 
ATOM   6086 H HA   B GLN   B 1 107 ? 30.041 -27.190 6.852   0.58 29.84 ?  107 GLN   B HA   1 
ATOM   6087 H HB2  A GLN   B 1 107 ? 29.136 -27.374 9.084   0.42 34.23 ?  107 GLN   B HB2  1 
ATOM   6088 H HB2  B GLN   B 1 107 ? 29.194 -27.411 9.112   0.58 34.01 ?  107 GLN   B HB2  1 
ATOM   6089 H HB3  A GLN   B 1 107 ? 29.604 -25.877 9.303   0.42 34.23 ?  107 GLN   B HB3  1 
ATOM   6090 H HB3  B GLN   B 1 107 ? 29.579 -25.886 9.297   0.58 34.01 ?  107 GLN   B HB3  1 
ATOM   6091 H HG2  A GLN   B 1 107 ? 27.862 -26.413 7.183   0.42 37.43 ?  107 GLN   B HG2  1 
ATOM   6092 H HG2  B GLN   B 1 107 ? 27.836 -26.566 7.223   0.58 37.98 ?  107 GLN   B HG2  1 
ATOM   6093 H HG3  A GLN   B 1 107 ? 27.259 -26.317 8.649   0.42 37.43 ?  107 GLN   B HG3  1 
ATOM   6094 H HG3  B GLN   B 1 107 ? 27.256 -26.467 8.699   0.58 37.98 ?  107 GLN   B HG3  1 
ATOM   6095 H HE21 A GLN   B 1 107 ? 26.373 -24.569 6.808   0.42 40.89 ?  107 GLN   B HE21 1 
ATOM   6096 H HE21 B GLN   B 1 107 ? 26.281 -24.811 6.789   0.58 42.20 ?  107 GLN   B HE21 1 
ATOM   6097 H HE22 A GLN   B 1 107 ? 26.846 -23.184 7.085   0.42 40.89 ?  107 GLN   B HE22 1 
ATOM   6098 H HE22 B GLN   B 1 107 ? 26.675 -23.397 7.045   0.58 42.20 ?  107 GLN   B HE22 1 
ATOM   6099 N N    . LEU   B 1 108 ? 32.026 -24.862 7.640   1.00 20.78 ?  108 LEU   B N    1 
ATOM   6100 C CA   . LEU   B 1 108 ? 32.566 -23.564 7.229   1.00 17.99 ?  108 LEU   B CA   1 
ATOM   6101 C C    . LEU   B 1 108 ? 33.222 -23.594 5.857   1.00 15.80 ?  108 LEU   B C    1 
ATOM   6102 O O    . LEU   B 1 108 ? 33.654 -22.544 5.364   1.00 14.80 ?  108 LEU   B O    1 
ATOM   6103 C CB   . LEU   B 1 108 ? 33.568 -23.060 8.268   1.00 18.41 ?  108 LEU   B CB   1 
ATOM   6104 C CG   . LEU   B 1 108 ? 32.959 -22.483 9.547   1.00 20.40 ?  108 LEU   B CG   1 
ATOM   6105 C CD1  . LEU   B 1 108 ? 33.952 -22.527 10.691  1.00 20.78 ?  108 LEU   B CD1  1 
ATOM   6106 C CD2  . LEU   B 1 108 ? 32.496 -21.054 9.304   1.00 21.35 ?  108 LEU   B CD2  1 
ATOM   6107 H H    A LEU   B 1 108 ? 32.483 -25.248 8.252   0.42 24.96 ?  108 LEU   B H    1 
ATOM   6108 H H    B LEU   B 1 108 ? 32.495 -25.261 8.234   0.58 24.96 ?  108 LEU   B H    1 
ATOM   6109 H HA   . LEU   B 1 108 ? 31.837 -22.926 7.189   1.00 21.61 ?  108 LEU   B HA   1 
ATOM   6110 H HB2  . LEU   B 1 108 ? 34.135 -23.800 8.531   1.00 22.12 ?  108 LEU   B HB2  1 
ATOM   6111 H HB3  . LEU   B 1 108 ? 34.106 -22.365 7.864   1.00 22.12 ?  108 LEU   B HB3  1 
ATOM   6112 H HG   . LEU   B 1 108 ? 32.183 -23.007 9.799   1.00 24.51 ?  108 LEU   B HG   1 
ATOM   6113 H HD11 . LEU   B 1 108 ? 33.527 -22.181 11.493  1.00 24.97 ?  108 LEU   B HD11 1 
ATOM   6114 H HD12 . LEU   B 1 108 ? 34.227 -23.445 10.834  1.00 24.97 ?  108 LEU   B HD12 1 
ATOM   6115 H HD13 . LEU   B 1 108 ? 34.721 -21.981 10.464  1.00 24.97 ?  108 LEU   B HD13 1 
ATOM   6116 H HD21 . LEU   B 1 108 ? 32.110 -20.702 10.122  1.00 25.64 ?  108 LEU   B HD21 1 
ATOM   6117 H HD22 . LEU   B 1 108 ? 33.259 -20.514 9.042   1.00 25.64 ?  108 LEU   B HD22 1 
ATOM   6118 H HD23 . LEU   B 1 108 ? 31.832 -21.051 8.597   1.00 25.64 ?  108 LEU   B HD23 1 
ATOM   6119 N N    . LEU   B 1 109 ? 33.280 -24.761 5.229   1.00 14.62 ?  109 LEU   B N    1 
ATOM   6120 C CA   . LEU   B 1 109 ? 33.910 -24.874 3.924   1.00 13.70 ?  109 LEU   B CA   1 
ATOM   6121 C C    . LEU   B 1 109 ? 33.144 -24.095 2.862   1.00 12.77 ?  109 LEU   B C    1 
ATOM   6122 O O    . LEU   B 1 109 ? 33.758 -23.514 1.961   1.00 12.46 ?  109 LEU   B O    1 
ATOM   6123 C CB   . LEU   B 1 109 ? 34.024 -26.351 3.553   1.00 13.86 ?  109 LEU   B CB   1 
ATOM   6124 C CG   . LEU   B 1 109 ? 34.814 -26.691 2.293   1.00 13.59 ?  109 LEU   B CG   1 
ATOM   6125 C CD1  . LEU   B 1 109 ? 36.202 -26.046 2.320   1.00 13.23 ?  109 LEU   B CD1  1 
ATOM   6126 C CD2  . LEU   B 1 109 ? 34.912 -28.206 2.133   1.00 14.61 ?  109 LEU   B CD2  1 
ATOM   6127 H H    . LEU   B 1 109 ? 32.978 -25.500 5.537   1.00 17.57 ?  109 LEU   B H    1 
ATOM   6128 H HA   . LEU   B 1 109 ? 34.812 -24.507 3.972   1.00 16.47 ?  109 LEU   B HA   1 
ATOM   6129 H HB2  . LEU   B 1 109 ? 34.450 -26.821 4.287   1.00 16.66 ?  109 LEU   B HB2  1 
ATOM   6130 H HB3  . LEU   B 1 109 ? 33.130 -26.703 3.424   1.00 16.66 ?  109 LEU   B HB3  1 
ATOM   6131 H HG   . LEU   B 1 109 ? 34.344 -26.350 1.519   1.00 16.33 ?  109 LEU   B HG   1 
ATOM   6132 H HD11 . LEU   B 1 109 ? 36.742 -26.419 1.602   1.00 15.90 ?  109 LEU   B HD11 1 
ATOM   6133 H HD12 . LEU   B 1 109 ? 36.109 -25.091 2.199   1.00 15.90 ?  109 LEU   B HD12 1 
ATOM   6134 H HD13 . LEU   B 1 109 ? 36.623 -26.235 3.175   1.00 15.90 ?  109 LEU   B HD13 1 
ATOM   6135 H HD21 . LEU   B 1 109 ? 35.487 -28.409 1.373   1.00 17.55 ?  109 LEU   B HD21 1 
ATOM   6136 H HD22 . LEU   B 1 109 ? 35.293 -28.588 2.939   1.00 17.55 ?  109 LEU   B HD22 1 
ATOM   6137 H HD23 . LEU   B 1 109 ? 34.027 -28.568 1.980   1.00 17.55 ?  109 LEU   B HD23 1 
ATOM   6138 N N    . LYS   B 1 110 ? 31.811 -24.053 2.950   1.00 12.22 ?  110 LYS   B N    1 
ATOM   6139 C CA   . LYS   B 1 110 ? 31.056 -23.295 1.960   1.00 12.14 ?  110 LYS   B CA   1 
ATOM   6140 C C    . LYS   B 1 110 ? 31.396 -21.810 2.045   1.00 12.04 ?  110 LYS   B C    1 
ATOM   6141 O O    . LYS   B 1 110 ? 31.655 -21.162 1.025   1.00 11.85 ?  110 LYS   B O    1 
ATOM   6142 C CB   . LYS   B 1 110 ? 29.553 -23.543 2.110   1.00 12.60 ?  110 LYS   B CB   1 
ATOM   6143 C CG   . LYS   B 1 110 ? 28.746 -22.925 0.959   1.00 13.00 ?  110 LYS   B CG   1 
ATOM   6144 C CD   . LYS   B 1 110 ? 27.278 -23.345 0.985   1.00 13.46 ?  110 LYS   B CD   1 
ATOM   6145 C CE   . LYS   B 1 110 ? 26.515 -22.827 -0.234  1.00 14.43 ?  110 LYS   B CE   1 
ATOM   6146 N NZ   . LYS   B 1 110 ? 26.862 -23.550 -1.488  1.00 14.36 ?  110 LYS   B NZ   1 
ATOM   6147 H H    . LYS   B 1 110 ? 31.343 -24.435 3.558   1.00 14.70 ?  110 LYS   B H    1 
ATOM   6148 H HA   . LYS   B 1 110 ? 31.315 -23.599 1.078   1.00 14.59 ?  110 LYS   B HA   1 
ATOM   6149 H HB2  . LYS   B 1 110 ? 29.390 -24.499 2.117   1.00 15.15 ?  110 LYS   B HB2  1 
ATOM   6150 H HB3  . LYS   B 1 110 ? 29.245 -23.146 2.940   1.00 15.15 ?  110 LYS   B HB3  1 
ATOM   6151 H HG2  . LYS   B 1 110 ? 28.782 -21.962 1.026   1.00 15.63 ?  110 LYS   B HG2  1 
ATOM   6152 H HG3  . LYS   B 1 110 ? 29.125 -23.219 0.115   1.00 15.63 ?  110 LYS   B HG3  1 
ATOM   6153 H HD2  . LYS   B 1 110 ? 27.219 -24.317 0.989   1.00 16.18 ?  110 LYS   B HD2  1 
ATOM   6154 H HD3  . LYS   B 1 110 ? 26.854 -22.987 1.783   1.00 16.18 ?  110 LYS   B HD3  1 
ATOM   6155 H HE2  . LYS   B 1 110 ? 25.562 -22.934 -0.084  1.00 17.34 ?  110 LYS   B HE2  1 
ATOM   6156 H HE3  . LYS   B 1 110 ? 26.727 -21.890 -0.364  1.00 17.34 ?  110 LYS   B HE3  1 
ATOM   6157 H HZ1  . LYS   B 1 110 ? 26.400 -23.222 -2.172  1.00 17.26 ?  110 LYS   B HZ1  1 
ATOM   6158 H HZ2  . LYS   B 1 110 ? 27.732 -23.468 -1.659  1.00 17.26 ?  110 LYS   B HZ2  1 
ATOM   6159 H HZ3  . LYS   B 1 110 ? 26.670 -24.419 -1.403  1.00 17.26 ?  110 LYS   B HZ3  1 
ATOM   6160 N N    . SER   B 1 111 ? 31.417 -21.256 3.261   1.00 12.28 ?  111 SER   B N    1 
ATOM   6161 C CA   . SER   B 1 111 ? 31.816 -19.859 3.433   1.00 12.16 ?  111 SER   B CA   1 
ATOM   6162 C C    . SER   B 1 111 ? 33.196 -19.604 2.840   1.00 11.30 ?  111 SER   B C    1 
ATOM   6163 O O    . SER   B 1 111 ? 33.422 -18.578 2.186   1.00 11.67 ?  111 SER   B O    1 
ATOM   6164 C CB   . SER   B 1 111 ? 31.814 -19.501 4.916   1.00 13.17 ?  111 SER   B CB   1 
ATOM   6165 O OG   . SER   B 1 111 ? 30.502 -19.506 5.436   1.00 14.62 ?  111 SER   B OG   1 
ATOM   6166 H H    . SER   B 1 111 ? 31.216 -21.660 3.989   1.00 14.76 ?  111 SER   B H    1 
ATOM   6167 H HA   . SER   B 1 111 ? 31.185 -19.284 2.978   1.00 14.62 ?  111 SER   B HA   1 
ATOM   6168 H HB2  . SER   B 1 111 ? 32.344 -20.156 5.400   1.00 15.83 ?  111 SER   B HB2  1 
ATOM   6169 H HB3  . SER   B 1 111 ? 32.201 -18.618 5.030   1.00 15.83 ?  111 SER   B HB3  1 
ATOM   6170 H HG   . SER   B 1 111 ? 30.516 -19.300 6.254   1.00 17.58 ?  111 SER   B HG   1 
ATOM   6171 N N    . ALA   B 1 112 ? 34.131 -20.533 3.054   1.00 11.61 ?  112 ALA   B N    1 
ATOM   6172 C CA   . ALA   B 1 112 ? 35.476 -20.364 2.517   1.00 11.49 ?  112 ALA   B CA   1 
ATOM   6173 C C    . ALA   B 1 112 ? 35.446 -20.264 0.996   1.00 11.20 ?  112 ALA   B C    1 
ATOM   6174 O O    . ALA   B 1 112 ? 36.068 -19.374 0.407   1.00 11.25 ?  112 ALA   B O    1 
ATOM   6175 C CB   . ALA   B 1 112 ? 36.369 -21.514 2.986   1.00 11.52 ?  112 ALA   B CB   1 
ATOM   6176 H H    . ALA   B 1 112 ? 34.012 -21.262 3.494   1.00 13.97 ?  112 ALA   B H    1 
ATOM   6177 H HA   . ALA   B 1 112 ? 35.850 -19.540 2.857   1.00 13.81 ?  112 ALA   B HA   1 
ATOM   6178 H HB1  . ALA   B 1 112 ? 37.264 -21.387 2.631   1.00 13.85 ?  112 ALA   B HB1  1 
ATOM   6179 H HB2  . ALA   B 1 112 ? 36.399 -21.511 3.958   1.00 13.85 ?  112 ALA   B HB2  1 
ATOM   6180 H HB3  . ALA   B 1 112 ? 36.003 -22.353 2.670   1.00 13.85 ?  112 ALA   B HB3  1 
ATOM   6181 N N    . TYR   B 1 113 ? 34.715 -21.170 0.338   1.00 10.85 ?  113 TYR   B N    1 
ATOM   6182 C CA   . TYR   B 1 113 ? 34.626 -21.126 -1.118  1.00 10.85 ?  113 TYR   B CA   1 
ATOM   6183 C C    . TYR   B 1 113 ? 33.926 -19.874 -1.636  1.00 10.20 ?  113 TYR   B C    1 
ATOM   6184 O O    . TYR   B 1 113 ? 34.205 -19.446 -2.761  1.00 10.44 ?  113 TYR   B O    1 
ATOM   6185 C CB   . TYR   B 1 113 ? 33.955 -22.386 -1.663  1.00 10.82 ?  113 TYR   B CB   1 
ATOM   6186 C CG   . TYR   B 1 113 ? 34.915 -23.532 -1.915  1.00 11.38 ?  113 TYR   B CG   1 
ATOM   6187 C CD1  . TYR   B 1 113 ? 35.910 -23.437 -2.880  1.00 11.65 ?  113 TYR   B CD1  1 
ATOM   6188 C CD2  . TYR   B 1 113 ? 34.818 -24.717 -1.203  1.00 11.83 ?  113 TYR   B CD2  1 
ATOM   6189 C CE1  . TYR   B 1 113 ? 36.783 -24.472 -3.122  1.00 11.75 ?  113 TYR   B CE1  1 
ATOM   6190 C CE2  . TYR   B 1 113 ? 35.690 -25.773 -1.444  1.00 11.84 ?  113 TYR   B CE2  1 
ATOM   6191 C CZ   . TYR   B 1 113 ? 36.666 -25.641 -2.408  1.00 12.07 ?  113 TYR   B CZ   1 
ATOM   6192 O OH   . TYR   B 1 113 ? 37.548 -26.653 -2.683  1.00 12.96 ?  113 TYR   B OH   1 
ATOM   6193 H H    . TYR   B 1 113 ? 34.262 -21.802 0.709   1.00 13.05 ?  113 TYR   B H    1 
ATOM   6194 H HA   . TYR   B 1 113 ? 35.525 -21.112 -1.468  1.00 13.05 ?  113 TYR   B HA   1 
ATOM   6195 H HB2  . TYR   B 1 113 ? 33.290 -22.697 -1.024  1.00 13.01 ?  113 TYR   B HB2  1 
ATOM   6196 H HB3  . TYR   B 1 113 ? 33.519 -22.177 -2.505  1.00 13.01 ?  113 TYR   B HB3  1 
ATOM   6197 H HD1  . TYR   B 1 113 ? 35.990 -22.649 -3.372  1.00 14.01 ?  113 TYR   B HD1  1 
ATOM   6198 H HD2  . TYR   B 1 113 ? 34.152 -24.810 -0.561  1.00 14.22 ?  113 TYR   B HD2  1 
ATOM   6199 H HE1  . TYR   B 1 113 ? 37.439 -24.386 -3.778  1.00 14.13 ?  113 TYR   B HE1  1 
ATOM   6200 H HE2  . TYR   B 1 113 ? 35.608 -26.566 -0.964  1.00 14.23 ?  113 TYR   B HE2  1 
ATOM   6201 H HH   . TYR   B 1 113 ? 37.380 -27.320 -2.204  1.00 15.58 ?  113 TYR   B HH   1 
ATOM   6202 N N    . GLU   B 1 114 ? 33.005 -19.289 -0.859  1.00 10.41 ?  114 GLU   B N    1 
ATOM   6203 C CA   . GLU   B 1 114 ? 32.321 -18.079 -1.314  1.00 10.34 ?  114 GLU   B CA   1 
ATOM   6204 C C    . GLU   B 1 114 ? 33.307 -16.958 -1.614  1.00 10.06 ?  114 GLU   B C    1 
ATOM   6205 O O    . GLU   B 1 114 ? 33.035 -16.098 -2.456  1.00 10.41 ?  114 GLU   B O    1 
ATOM   6206 C CB   . GLU   B 1 114 ? 31.259 -17.649 -0.293  1.00 10.65 ?  114 GLU   B CB   1 
ATOM   6207 C CG   . GLU   B 1 114 ? 30.041 -18.573 -0.346  1.00 11.23 ?  114 GLU   B CG   1 
ATOM   6208 C CD   . GLU   B 1 114 ? 29.019 -18.384 0.758   1.00 11.23 ?  114 GLU   B CD   1 
ATOM   6209 O OE1  . GLU   B 1 114 ? 29.318 -17.767 1.798   1.00 11.56 ?  114 GLU   B OE1  1 
ATOM   6210 O OE2  . GLU   B 1 114 ? 27.896 -18.911 0.590   1.00 12.33 -1 114 GLU   B OE2  1 
ATOM   6211 H H    . GLU   B 1 114 ? 32.760 -19.575 -0.084  1.00 12.52 ?  114 GLU   B H    1 
ATOM   6212 H HA   . GLU   B 1 114 ? 31.855 -18.286 -2.139  1.00 12.43 ?  114 GLU   B HA   1 
ATOM   6213 H HB2  . GLU   B 1 114 ? 31.637 -17.694 0.603   1.00 12.81 ?  114 GLU   B HB2  1 
ATOM   6214 H HB3  . GLU   B 1 114 ? 30.968 -16.748 -0.489  1.00 12.81 ?  114 GLU   B HB3  1 
ATOM   6215 H HG2  . GLU   B 1 114 ? 29.586 -18.425 -1.185  1.00 13.51 ?  114 GLU   B HG2  1 
ATOM   6216 H HG3  . GLU   B 1 114 ? 30.352 -19.489 -0.298  1.00 13.51 ?  114 GLU   B HG3  1 
ATOM   6217 N N    . ASN   B 1 115 ? 34.475 -16.963 -0.969  1.00 10.09 ?  115 ASN   B N    1 
ATOM   6218 C CA   . ASN   B 1 115 ? 35.472 -15.935 -1.260  1.00 10.14 ?  115 ASN   B CA   1 
ATOM   6219 C C    . ASN   B 1 115 ? 35.886 -15.959 -2.724  1.00 10.08 ?  115 ASN   B C    1 
ATOM   6220 O O    . ASN   B 1 115 ? 36.265 -14.917 -3.284  1.00 10.34 ?  115 ASN   B O    1 
ATOM   6221 C CB   . ASN   B 1 115 ? 36.709 -16.116 -0.370  1.00 10.81 ?  115 ASN   B CB   1 
ATOM   6222 C CG   . ASN   B 1 115 ? 36.434 -15.837 1.089   1.00 11.04 ?  115 ASN   B CG   1 
ATOM   6223 O OD1  . ASN   B 1 115 ? 36.443 -14.690 1.520   1.00 12.96 ?  115 ASN   B OD1  1 
ATOM   6224 N ND2  . ASN   B 1 115 ? 36.250 -16.892 1.874   1.00 11.35 ?  115 ASN   B ND2  1 
ATOM   6225 H H    . ASN   B 1 115 ? 34.704 -17.527 -0.357  1.00 12.14 ?  115 ASN   B H    1 
ATOM   6226 H HA   . ASN   B 1 115 ? 35.094 -15.064 -1.068  1.00 12.19 ?  115 ASN   B HA   1 
ATOM   6227 H HB2  . ASN   B 1 115 ? 37.021 -17.032 -0.444  1.00 13.00 ?  115 ASN   B HB2  1 
ATOM   6228 H HB3  . ASN   B 1 115 ? 37.401 -15.505 -0.664  1.00 13.00 ?  115 ASN   B HB3  1 
ATOM   6229 H HD21 . ASN   B 1 115 ? 36.100 -16.778 2.717   1.00 13.64 ?  115 ASN   B HD21 1 
ATOM   6230 H HD22 . ASN   B 1 115 ? 36.263 -17.682 1.544   1.00 13.64 ?  115 ASN   B HD22 1 
ATOM   6231 N N    . PHE   B 1 116 ? 35.860 -17.138 -3.353  1.00 9.90  ?  116 PHE   B N    1 
ATOM   6232 C CA   . PHE   B 1 116 ? 36.281 -17.237 -4.745  1.00 9.87  ?  116 PHE   B CA   1 
ATOM   6233 C C    . PHE   B 1 116 ? 35.379 -16.411 -5.660  1.00 9.96  ?  116 PHE   B C    1 
ATOM   6234 O O    . PHE   B 1 116 ? 35.817 -15.980 -6.732  1.00 10.57 ?  116 PHE   B O    1 
ATOM   6235 C CB   . PHE   B 1 116 ? 36.242 -18.682 -5.262  1.00 10.01 ?  116 PHE   B CB   1 
ATOM   6236 C CG   . PHE   B 1 116 ? 37.311 -19.635 -4.719  1.00 9.94  ?  116 PHE   B CG   1 
ATOM   6237 C CD1  . PHE   B 1 116 ? 37.968 -19.458 -3.506  1.00 10.80 ?  116 PHE   B CD1  1 
ATOM   6238 C CD2  . PHE   B 1 116 ? 37.610 -20.767 -5.460  1.00 10.03 ?  116 PHE   B CD2  1 
ATOM   6239 C CE1  . PHE   B 1 116 ? 38.899 -20.403 -3.064  1.00 11.06 ?  116 PHE   B CE1  1 
ATOM   6240 C CE2  . PHE   B 1 116 ? 38.535 -21.703 -5.025  1.00 10.26 ?  116 PHE   B CE2  1 
ATOM   6241 C CZ   . PHE   B 1 116 ? 39.170 -21.528 -3.831  1.00 10.29 ?  116 PHE   B CZ   1 
ATOM   6242 H H    . PHE   B 1 116 ? 35.603 -17.886 -3.000  1.00 11.91 ?  116 PHE   B H    1 
ATOM   6243 H HA   . PHE   B 1 116 ? 37.187 -16.910 -4.831  1.00 11.87 ?  116 PHE   B HA   1 
ATOM   6244 H HB2  . PHE   B 1 116 ? 35.373 -19.059 -5.034  1.00 12.04 ?  116 PHE   B HB2  1 
ATOM   6245 H HB3  . PHE   B 1 116 ? 36.335 -18.662 -6.225  1.00 12.04 ?  116 PHE   B HB3  1 
ATOM   6246 H HD1  . PHE   B 1 116 ? 37.774 -18.714 -2.974  1.00 12.98 ?  116 PHE   B HD1  1 
ATOM   6247 H HD2  . PHE   B 1 116 ? 37.171 -20.908 -6.267  1.00 12.07 ?  116 PHE   B HD2  1 
ATOM   6248 H HE1  . PHE   B 1 116 ? 39.340 -20.273 -2.251  1.00 13.30 ?  116 PHE   B HE1  1 
ATOM   6249 H HE2  . PHE   B 1 116 ? 38.724 -22.447 -5.544  1.00 12.34 ?  116 PHE   B HE2  1 
ATOM   6250 H HZ   . PHE   B 1 116 ? 39.810 -22.137 -3.540  1.00 12.37 ?  116 PHE   B HZ   1 
ATOM   6251 N N    . ASN   B 1 117 ? 34.111 -16.205 -5.278  1.00 10.33 ?  117 ASN   B N    1 
ATOM   6252 C CA   . ASN   B 1 117 ? 33.167 -15.498 -6.142  1.00 10.67 ?  117 ASN   B CA   1 
ATOM   6253 C C    . ASN   B 1 117 ? 33.484 -14.020 -6.288  1.00 10.96 ?  117 ASN   B C    1 
ATOM   6254 O O    . ASN   B 1 117 ? 32.883 -13.360 -7.142  1.00 12.00 ?  117 ASN   B O    1 
ATOM   6255 C CB   . ASN   B 1 117 ? 31.742 -15.714 -5.646  1.00 10.60 ?  117 ASN   B CB   1 
ATOM   6256 C CG   . ASN   B 1 117 ? 31.288 -17.125 -5.896  1.00 10.93 ?  117 ASN   B CG   1 
ATOM   6257 O OD1  . ASN   B 1 117 ? 31.651 -17.718 -6.911  1.00 11.68 ?  117 ASN   B OD1  1 
ATOM   6258 N ND2  . ASN   B 1 117 ? 30.550 -17.699 -4.960  1.00 11.13 ?  117 ASN   B ND2  1 
ATOM   6259 H H    . ASN   B 1 117 ? 33.776 -16.473 -4.525  1.00 12.42 ?  117 ASN   B H    1 
ATOM   6260 H HA   . ASN   B 1 117 ? 33.221 -15.888 -7.021  1.00 12.83 ?  117 ASN   B HA   1 
ATOM   6261 H HB2  . ASN   B 1 117 ? 31.701 -15.546 -4.686  1.00 12.75 ?  117 ASN   B HB2  1 
ATOM   6262 H HB3  . ASN   B 1 117 ? 31.142 -15.111 -6.113  1.00 12.75 ?  117 ASN   B HB3  1 
ATOM   6263 H HD21 . ASN   B 1 117 ? 30.269 -18.503 -5.062  1.00 13.38 ?  117 ASN   B HD21 1 
ATOM   6264 H HD22 . ASN   B 1 117 ? 30.316 -17.250 -4.258  1.00 13.38 ?  117 ASN   B HD22 1 
ATOM   6265 N N    . GLN   B 1 118 ? 34.420 -13.494 -5.502  1.00 10.39 ?  118 GLN   B N    1 
ATOM   6266 C CA   . GLN   B 1 118 ? 34.848 -12.109 -5.640  1.00 10.93 ?  118 GLN   B CA   1 
ATOM   6267 C C    . GLN   B 1 118 ? 35.915 -11.918 -6.713  1.00 10.86 ?  118 GLN   B C    1 
ATOM   6268 O O    . GLN   B 1 118 ? 36.395 -10.788 -6.890  1.00 12.37 ?  118 GLN   B O    1 
ATOM   6269 C CB   . GLN   B 1 118 ? 35.334 -11.578 -4.288  1.00 11.51 ?  118 GLN   B CB   1 
ATOM   6270 C CG   . GLN   B 1 118 ? 34.251 -11.624 -3.221  1.00 11.51 ?  118 GLN   B CG   1 
ATOM   6271 C CD   . GLN   B 1 118 ? 33.088 -10.709 -3.547  1.00 11.46 ?  118 GLN   B CD   1 
ATOM   6272 O OE1  . GLN   B 1 118 ? 33.288 -9.572  -3.974  1.00 12.53 ?  118 GLN   B OE1  1 
ATOM   6273 N NE2  . GLN   B 1 118 ? 31.873 -11.199 -3.368  1.00 12.03 ?  118 GLN   B NE2  1 
ATOM   6274 H H    . GLN   B 1 118 ? 34.838 -13.922 -4.877  1.00 12.49 ?  118 GLN   B H    1 
ATOM   6275 H HA   . GLN   B 1 118 ? 34.082 -11.580 -5.904  1.00 13.15 ?  118 GLN   B HA   1 
ATOM   6276 H HB2  . GLN   B 1 118 ? 36.083 -12.110 -3.983  1.00 13.84 ?  118 GLN   B HB2  1 
ATOM   6277 H HB3  . GLN   B 1 118 ? 35.608 -10.648 -4.392  1.00 13.84 ?  118 GLN   B HB3  1 
ATOM   6278 H HG2  . GLN   B 1 118 ? 33.915 -12.533 -3.149  1.00 13.84 ?  118 GLN   B HG2  1 
ATOM   6279 H HG3  . GLN   B 1 118 ? 34.628 -11.342 -2.372  1.00 13.84 ?  118 GLN   B HG3  1 
ATOM   6280 H HE21 . GLN   B 1 118 ? 31.773 -12.001 -3.072  1.00 14.47 ?  118 GLN   B HE21 1 
ATOM   6281 H HE22 . GLN   B 1 118 ? 31.190 -10.717 -3.550  1.00 14.47 ?  118 GLN   B HE22 1 
ATOM   6282 N N    . HIS   B 1 119 ? 36.268 -12.974 -7.452  1.00 10.66 ?  119 HIS   B N    1 
ATOM   6283 C CA   . HIS   B 1 119 ? 37.313 -12.931 -8.468  1.00 11.12 ?  119 HIS   B CA   1 
ATOM   6284 C C    . HIS   B 1 119 ? 36.821 -13.659 -9.708  1.00 11.10 ?  119 HIS   B C    1 
ATOM   6285 O O    . HIS   B 1 119 ? 36.309 -14.773 -9.607  1.00 11.70 ?  119 HIS   B O    1 
ATOM   6286 C CB   . HIS   B 1 119 ? 38.587 -13.579 -7.915  1.00 11.52 ?  119 HIS   B CB   1 
ATOM   6287 C CG   . HIS   B 1 119 ? 39.067 -12.896 -6.684  1.00 12.84 ?  119 HIS   B CG   1 
ATOM   6288 N ND1  . HIS   B 1 119 ? 39.874 -11.780 -6.725  1.00 14.66 ?  119 HIS   B ND1  1 
ATOM   6289 C CD2  . HIS   B 1 119 ? 38.763 -13.098 -5.381  1.00 13.88 ?  119 HIS   B CD2  1 
ATOM   6290 C CE1  . HIS   B 1 119 ? 40.076 -11.347 -5.493  1.00 15.41 ?  119 HIS   B CE1  1 
ATOM   6291 N NE2  . HIS   B 1 119 ? 39.411 -12.126 -4.660  1.00 15.35 ?  119 HIS   B NE2  1 
ATOM   6292 H H    . HIS   B 1 119 ? 35.894 -13.749 -7.390  1.00 12.82 ?  119 HIS   B H    1 
ATOM   6293 H HA   . HIS   B 1 119 ? 37.510 -12.008 -8.701  1.00 13.37 ?  119 HIS   B HA   1 
ATOM   6294 H HB2  . HIS   B 1 119 ? 38.406 -14.506 -7.695  1.00 13.85 ?  119 HIS   B HB2  1 
ATOM   6295 H HB3  . HIS   B 1 119 ? 39.291 -13.525 -8.582  1.00 13.85 ?  119 HIS   B HB3  1 
ATOM   6296 H HD2  . HIS   B 1 119 ? 38.225 -13.774 -5.034  1.00 16.68 ?  119 HIS   B HD2  1 
ATOM   6297 H HE1  . HIS   B 1 119 ? 40.613 -10.627 -5.245  1.00 18.52 ?  119 HIS   B HE1  1 
ATOM   6298 H HE2  . HIS   B 1 119 ? 39.409 -12.056 -3.797  1.00 18.44 ?  119 HIS   B HE2  1 
ATOM   6299 N N    A GLU   B 1 120 ? 36.973 -13.033 -10.877 0.42 12.18 ?  120 GLU   B N    1 
ATOM   6300 N N    B GLU   B 1 120 ? 36.977 -13.039 -10.878 0.58 11.62 ?  120 GLU   B N    1 
ATOM   6301 C CA   A GLU   B 1 120 ? 36.382 -13.603 -12.084 0.42 13.82 ?  120 GLU   B CA   1 
ATOM   6302 C CA   B GLU   B 1 120 ? 36.374 -13.612 -12.078 0.58 12.81 ?  120 GLU   B CA   1 
ATOM   6303 C C    A GLU   B 1 120 ? 37.049 -14.910 -12.495 0.42 12.34 ?  120 GLU   B C    1 
ATOM   6304 C C    B GLU   B 1 120 ? 37.052 -14.905 -12.513 0.58 11.63 ?  120 GLU   B C    1 
ATOM   6305 O O    A GLU   B 1 120 ? 36.381 -15.791 -13.052 0.42 12.42 ?  120 GLU   B O    1 
ATOM   6306 O O    B GLU   B 1 120 ? 36.395 -15.772 -13.104 0.58 11.97 ?  120 GLU   B O    1 
ATOM   6307 C CB   A GLU   B 1 120 ? 36.423 -12.588 -13.225 0.42 17.61 ?  120 GLU   B CB   1 
ATOM   6308 C CB   B GLU   B 1 120 ? 36.369 -12.589 -13.209 0.58 16.25 ?  120 GLU   B CB   1 
ATOM   6309 C CG   A GLU   B 1 120 ? 35.394 -11.480 -13.080 0.42 21.86 ?  120 GLU   B CG   1 
ATOM   6310 C CG   B GLU   B 1 120 ? 35.410 -11.440 -12.951 0.58 20.55 ?  120 GLU   B CG   1 
ATOM   6311 C CD   A GLU   B 1 120 ? 35.288 -10.614 -14.318 0.42 25.62 ?  120 GLU   B CD   1 
ATOM   6312 C CD   B GLU   B 1 120 ? 35.130 -10.599 -14.174 0.58 24.76 ?  120 GLU   B CD   1 
ATOM   6313 O OE1  A GLU   B 1 120 ? 36.310 -10.461 -15.019 0.42 27.09 ?  120 GLU   B OE1  1 
ATOM   6314 O OE1  B GLU   B 1 120 ? 36.092 -10.183 -14.856 0.58 26.63 ?  120 GLU   B OE1  1 
ATOM   6315 O OE2  A GLU   B 1 120 ? 34.186 -10.090 -14.590 0.42 27.40 -1 120 GLU   B OE2  1 
ATOM   6316 O OE2  B GLU   B 1 120 ? 33.937 -10.349 -14.448 0.58 26.91 -1 120 GLU   B OE2  1 
ATOM   6317 H H    A GLU   B 1 120 ? 37.400 -12.294 -10.994 0.42 14.64 ?  120 GLU   B H    1 
ATOM   6318 H H    B GLU   B 1 120 ? 37.409 -12.304 -11.001 0.58 13.97 ?  120 GLU   B H    1 
ATOM   6319 H HA   A GLU   B 1 120 ? 35.452 -13.799 -11.903 0.42 16.61 ?  120 GLU   B HA   1 
ATOM   6320 H HA   B GLU   B 1 120 ? 35.451 -13.826 -11.879 0.58 15.40 ?  120 GLU   B HA   1 
ATOM   6321 H HB2  A GLU   B 1 120 ? 37.300 -12.176 -13.253 0.42 21.16 ?  120 GLU   B HB2  1 
ATOM   6322 H HB2  B GLU   B 1 120 ? 37.257 -12.218 -13.311 0.58 19.53 ?  120 GLU   B HB2  1 
ATOM   6323 H HB3  A GLU   B 1 120 ? 36.248 -13.048 -14.061 0.42 21.16 ?  120 GLU   B HB3  1 
ATOM   6324 H HB3  B GLU   B 1 120 ? 36.095 -13.027 -14.032 0.58 19.53 ?  120 GLU   B HB3  1 
ATOM   6325 H HG2  A GLU   B 1 120 ? 34.524 -11.876 -12.914 0.42 26.26 ?  120 GLU   B HG2  1 
ATOM   6326 H HG2  B GLU   B 1 120 ? 34.556 -11.794 -12.660 0.58 24.68 ?  120 GLU   B HG2  1 
ATOM   6327 H HG3  A GLU   B 1 120 ? 35.646 -10.909 -12.338 0.42 26.26 ?  120 GLU   B HG3  1 
ATOM   6328 H HG3  B GLU   B 1 120 ? 35.781 -10.860 -12.272 0.58 24.68 ?  120 GLU   B HG3  1 
ATOM   6329 N N    . VAL   B 1 121 ? 38.344 -15.060 -12.227 1.00 11.64 ?  121 VAL   B N    1 
ATOM   6330 C CA   . VAL   B 1 121 ? 39.084 -16.270 -12.585 1.00 11.28 ?  121 VAL   B CA   1 
ATOM   6331 C C    . VAL   B 1 121 ? 40.208 -16.481 -11.575 1.00 11.11 ?  121 VAL   B C    1 
ATOM   6332 O O    . VAL   B 1 121 ? 40.896 -15.530 -11.188 1.00 11.77 ?  121 VAL   B O    1 
ATOM   6333 C CB   . VAL   B 1 121 ? 39.583 -16.221 -14.048 1.00 13.39 ?  121 VAL   B CB   1 
ATOM   6334 C CG1  . VAL   B 1 121 ? 40.437 -14.987 -14.304 1.00 14.56 ?  121 VAL   B CG1  1 
ATOM   6335 C CG2  . VAL   B 1 121 ? 40.325 -17.502 -14.408 1.00 14.86 ?  121 VAL   B CG2  1 
ATOM   6336 H H    A VAL   B 1 121 ? 38.824 -14.466 -11.826 0.42 14.00 ?  121 VAL   B H    1 
ATOM   6337 H H    B VAL   B 1 121 ? 38.821 -14.469 -11.818 0.58 14.00 ?  121 VAL   B H    1 
ATOM   6338 H HA   . VAL   B 1 121 ? 38.478 -17.021 -12.506 1.00 13.56 ?  121 VAL   B HA   1 
ATOM   6339 H HB   . VAL   B 1 121 ? 38.803 -16.163 -14.625 1.00 16.09 ?  121 VAL   B HB   1 
ATOM   6340 H HG11 . VAL   B 1 121 ? 40.737 -15.002 -15.224 1.00 17.50 ?  121 VAL   B HG11 1 
ATOM   6341 H HG12 . VAL   B 1 121 ? 39.897 -14.192 -14.146 1.00 17.50 ?  121 VAL   B HG12 1 
ATOM   6342 H HG13 . VAL   B 1 121 ? 41.194 -14.997 -13.702 1.00 17.50 ?  121 VAL   B HG13 1 
ATOM   6343 H HG21 . VAL   B 1 121 ? 40.515 -17.495 -15.359 1.00 17.86 ?  121 VAL   B HG21 1 
ATOM   6344 H HG22 . VAL   B 1 121 ? 41.153 -17.540 -13.905 1.00 17.86 ?  121 VAL   B HG22 1 
ATOM   6345 H HG23 . VAL   B 1 121 ? 39.767 -18.265 -14.189 1.00 17.86 ?  121 VAL   B HG23 1 
ATOM   6346 N N    . LEU   B 1 122 ? 40.393 -17.735 -11.147 1.00 10.58 ?  122 LEU   B N    1 
ATOM   6347 C CA   . LEU   B 1 122 ? 41.368 -18.089 -10.120 1.00 10.29 ?  122 LEU   B CA   1 
ATOM   6348 C C    . LEU   B 1 122 ? 42.021 -19.420 -10.450 1.00 10.13 ?  122 LEU   B C    1 
ATOM   6349 O O    . LEU   B 1 122 ? 41.360 -20.349 -10.943 1.00 11.32 ?  122 LEU   B O    1 
ATOM   6350 C CB   . LEU   B 1 122 ? 40.703 -18.336 -8.752  1.00 12.09 ?  122 LEU   B CB   1 
ATOM   6351 C CG   . LEU   B 1 122 ? 39.683 -17.305 -8.270  1.00 11.87 ?  122 LEU   B CG   1 
ATOM   6352 C CD1  . LEU   B 1 122 ? 38.296 -17.672 -8.741  1.00 12.60 ?  122 LEU   B CD1  1 
ATOM   6353 C CD2  . LEU   B 1 122 ? 39.727 -17.206 -6.764  1.00 11.64 ?  122 LEU   B CD2  1 
ATOM   6354 H H    . LEU   B 1 122 ? 39.960 -18.411 -11.445 1.00 12.72 ?  122 LEU   B H    1 
ATOM   6355 H HA   . LEU   B 1 122 ? 42.047 -17.396 -10.029 1.00 12.37 ?  122 LEU   B HA   1 
ATOM   6356 H HB2  . LEU   B 1 122 ? 40.245 -19.189 -8.792  1.00 14.53 ?  122 LEU   B HB2  1 
ATOM   6357 H HB3  . LEU   B 1 122 ? 41.399 -18.378 -8.079  1.00 14.53 ?  122 LEU   B HB3  1 
ATOM   6358 H HG   . LEU   B 1 122 ? 39.906 -16.436 -8.641  1.00 14.28 ?  122 LEU   B HG   1 
ATOM   6359 H HD11 . LEU   B 1 122 ? 37.665 -17.018 -8.408  1.00 15.15 ?  122 LEU   B HD11 1 
ATOM   6360 H HD12 . LEU   B 1 122 ? 38.281 -17.682 -9.712  1.00 15.15 ?  122 LEU   B HD12 1 
ATOM   6361 H HD13 . LEU   B 1 122 ? 38.070 -18.553 -8.401  1.00 15.15 ?  122 LEU   B HD13 1 
ATOM   6362 H HD21 . LEU   B 1 122 ? 39.047 -16.580 -6.465  1.00 13.99 ?  122 LEU   B HD21 1 
ATOM   6363 H HD22 . LEU   B 1 122 ? 39.560 -18.082 -6.382  1.00 13.99 ?  122 LEU   B HD22 1 
ATOM   6364 H HD23 . LEU   B 1 122 ? 40.605 -16.891 -6.492  1.00 13.99 ?  122 LEU   B HD23 1 
ATOM   6365 N N    . LEU   B 1 123 ? 43.309 -19.524 -10.091 1.00 9.73  ?  123 LEU   B N    1 
ATOM   6366 C CA   . LEU   B 1 123 ? 44.023 -20.796 -9.969  1.00 10.00 ?  123 LEU   B CA   1 
ATOM   6367 C C    . LEU   B 1 123 ? 43.993 -21.196 -8.497  1.00 9.81  ?  123 LEU   B C    1 
ATOM   6368 O O    . LEU   B 1 123 ? 44.348 -20.368 -7.647  1.00 10.29 ?  123 LEU   B O    1 
ATOM   6369 C CB   . LEU   B 1 123 ? 45.475 -20.623 -10.426 1.00 10.62 ?  123 LEU   B CB   1 
ATOM   6370 C CG   . LEU   B 1 123 ? 46.412 -21.810 -10.184 1.00 10.95 ?  123 LEU   B CG   1 
ATOM   6371 C CD1  . LEU   B 1 123 ? 45.969 -23.062 -10.938 1.00 11.40 ?  123 LEU   B CD1  1 
ATOM   6372 C CD2  . LEU   B 1 123 ? 47.824 -21.420 -10.583 1.00 12.05 ?  123 LEU   B CD2  1 
ATOM   6373 H H    . LEU   B 1 123 ? 43.802 -18.848 -9.885  1.00 11.71 ?  123 LEU   B H    1 
ATOM   6374 H HA   . LEU   B 1 123 ? 43.586 -21.484 -10.500 1.00 12.03 ?  123 LEU   B HA   1 
ATOM   6375 H HB2  . LEU   B 1 123 ? 45.471 -20.448 -11.380 1.00 12.77 ?  123 LEU   B HB2  1 
ATOM   6376 H HB3  . LEU   B 1 123 ? 45.848 -19.860 -9.960  1.00 12.77 ?  123 LEU   B HB3  1 
ATOM   6377 H HG   . LEU   B 1 123 ? 46.427 -22.022 -9.237  1.00 13.17 ?  123 LEU   B HG   1 
ATOM   6378 H HD11 . LEU   B 1 123 ? 46.604 -23.776 -10.769 1.00 13.71 ?  123 LEU   B HD11 1 
ATOM   6379 H HD12 . LEU   B 1 123 ? 45.088 -23.324 -10.618 1.00 13.71 ?  123 LEU   B HD12 1 
ATOM   6380 H HD13 . LEU   B 1 123 ? 45.932 -22.865 -11.884 1.00 13.71 ?  123 LEU   B HD13 1 
ATOM   6381 H HD21 . LEU   B 1 123 ? 48.416 -22.171 -10.434 1.00 14.49 ?  123 LEU   B HD21 1 
ATOM   6382 H HD22 . LEU   B 1 123 ? 47.826 -21.178 -11.526 1.00 14.49 ?  123 LEU   B HD22 1 
ATOM   6383 H HD23 . LEU   B 1 123 ? 48.103 -20.662 -10.049 1.00 14.49 ?  123 LEU   B HD23 1 
ATOM   6384 N N    . ALA   B 1 124 ? 43.553 -22.421 -8.182  1.00 9.59  ?  124 ALA   B N    1 
ATOM   6385 C CA   . ALA   B 1 124 ? 43.294 -22.737 -6.784  1.00 9.86  ?  124 ALA   B CA   1 
ATOM   6386 C C    . ALA   B 1 124 ? 43.578 -24.197 -6.466  1.00 9.43  ?  124 ALA   B C    1 
ATOM   6387 O O    . ALA   B 1 124 ? 43.434 -25.076 -7.330  1.00 10.50 ?  124 ALA   B O    1 
ATOM   6388 C CB   . ALA   B 1 124 ? 41.840 -22.441 -6.409  1.00 10.43 ?  124 ALA   B CB   1 
ATOM   6389 H H    . ALA   B 1 124 ? 43.391 -23.056 -8.747  1.00 11.54 ?  124 ALA   B H    1 
ATOM   6390 H HA   . ALA   B 1 124 ? 43.871 -22.192 -6.240  1.00 11.86 ?  124 ALA   B HA   1 
ATOM   6391 H HB1  . ALA   B 1 124 ? 41.701 -22.665 -5.478  1.00 12.54 ?  124 ALA   B HB1  1 
ATOM   6392 H HB2  . ALA   B 1 124 ? 41.670 -21.496 -6.553  1.00 12.54 ?  124 ALA   B HB2  1 
ATOM   6393 H HB3  . ALA   B 1 124 ? 41.251 -22.970 -6.971  1.00 12.54 ?  124 ALA   B HB3  1 
ATOM   6394 N N    . PRO   B 1 125 ? 43.871 -24.495 -5.202  1.00 10.09 ?  125 PRO   B N    1 
ATOM   6395 C CA   . PRO   B 1 125 ? 43.807 -25.861 -4.685  1.00 10.40 ?  125 PRO   B CA   1 
ATOM   6396 C C    . PRO   B 1 125 ? 42.406 -26.132 -4.136  1.00 10.52 ?  125 PRO   B C    1 
ATOM   6397 O O    . PRO   B 1 125 ? 41.613 -25.216 -3.927  1.00 11.10 ?  125 PRO   B O    1 
ATOM   6398 C CB   . PRO   B 1 125 ? 44.796 -25.794 -3.516  1.00 11.63 ?  125 PRO   B CB   1 
ATOM   6399 C CG   . PRO   B 1 125 ? 44.560 -24.409 -2.942  1.00 11.71 ?  125 PRO   B CG   1 
ATOM   6400 C CD   . PRO   B 1 125 ? 44.222 -23.534 -4.138  1.00 10.85 ?  125 PRO   B CD   1 
ATOM   6401 H HA   . PRO   B 1 125 ? 44.081 -26.530 -5.335  1.00 12.50 ?  125 PRO   B HA   1 
ATOM   6402 H HB2  . PRO   B 1 125 ? 44.587 -26.481 -2.857  1.00 13.98 ?  125 PRO   B HB2  1 
ATOM   6403 H HB3  . PRO   B 1 125 ? 45.707 -25.890 -3.835  1.00 13.98 ?  125 PRO   B HB3  1 
ATOM   6404 H HG2  . PRO   B 1 125 ? 43.818 -24.427 -2.316  1.00 14.07 ?  125 PRO   B HG2  1 
ATOM   6405 H HG3  . PRO   B 1 125 ? 45.368 -24.089 -2.499  1.00 14.07 ?  125 PRO   B HG3  1 
ATOM   6406 H HD2  . PRO   B 1 125 ? 43.471 -22.963 -3.942  1.00 13.04 ?  125 PRO   B HD2  1 
ATOM   6407 H HD3  . PRO   B 1 125 ? 45.005 -23.013 -4.401  1.00 13.04 ?  125 PRO   B HD3  1 
ATOM   6408 N N    . LEU   B 1 126 ? 42.132 -27.405 -3.853  1.00 11.26 ?  126 LEU   B N    1 
ATOM   6409 C CA   . LEU   B 1 126 ? 40.915 -27.765 -3.131  1.00 11.65 ?  126 LEU   B CA   1 
ATOM   6410 C C    . LEU   B 1 126 ? 41.040 -27.366 -1.668  1.00 12.23 ?  126 LEU   B C    1 
ATOM   6411 O O    . LEU   B 1 126 ? 41.926 -27.837 -0.951  1.00 14.35 ?  126 LEU   B O    1 
ATOM   6412 C CB   . LEU   B 1 126 ? 40.651 -29.260 -3.250  1.00 13.14 ?  126 LEU   B CB   1 
ATOM   6413 C CG   . LEU   B 1 126 ? 40.128 -29.753 -4.600  1.00 14.31 ?  126 LEU   B CG   1 
ATOM   6414 C CD1  . LEU   B 1 126 ? 40.173 -31.266 -4.643  1.00 15.97 ?  126 LEU   B CD1  1 
ATOM   6415 C CD2  . LEU   B 1 126 ? 38.711 -29.251 -4.869  1.00 15.00 ?  126 LEU   B CD2  1 
ATOM   6416 H H    . LEU   B 1 126 ? 42.634 -28.077 -4.062  1.00 13.54 ?  126 LEU   B H    1 
ATOM   6417 H HA   . LEU   B 1 126 ? 40.168 -27.284 -3.517  1.00 14.00 ?  126 LEU   B HA   1 
ATOM   6418 H HB2  . LEU   B 1 126 ? 41.480 -29.726 -3.076  1.00 15.80 ?  126 LEU   B HB2  1 
ATOM   6419 H HB3  . LEU   B 1 126 ? 39.993 -29.501 -2.585  1.00 15.80 ?  126 LEU   B HB3  1 
ATOM   6420 H HG   . LEU   B 1 126 ? 40.706 -29.417 -5.307  1.00 17.20 ?  126 LEU   B HG   1 
ATOM   6421 H HD11 . LEU   B 1 126 ? 39.834 -31.571 -5.500  1.00 19.19 ?  126 LEU   B HD11 1 
ATOM   6422 H HD12 . LEU   B 1 126 ? 41.089 -31.562 -4.525  1.00 19.19 ?  126 LEU   B HD12 1 
ATOM   6423 H HD13 . LEU   B 1 126 ? 39.619 -31.619 -3.926  1.00 19.19 ?  126 LEU   B HD13 1 
ATOM   6424 H HD21 . LEU   B 1 126 ? 38.383 -29.653 -5.691  1.00 18.03 ?  126 LEU   B HD21 1 
ATOM   6425 H HD22 . LEU   B 1 126 ? 38.140 -29.503 -4.128  1.00 18.03 ?  126 LEU   B HD22 1 
ATOM   6426 H HD23 . LEU   B 1 126 ? 38.727 -28.284 -4.961  1.00 18.03 ?  126 LEU   B HD23 1 
ATOM   6427 N N    . LEU   B 1 127 ? 40.112 -26.537 -1.207  1.00 12.08 ?  127 LEU   B N    1 
ATOM   6428 C CA   . LEU   B 1 127 ? 40.166 -26.050 0.156   1.00 12.69 ?  127 LEU   B CA   1 
ATOM   6429 C C    . LEU   B 1 127 ? 39.885 -27.168 1.151   1.00 12.25 ?  127 LEU   B C    1 
ATOM   6430 O O    . LEU   B 1 127 ? 39.058 -28.057 0.928   1.00 12.52 ?  127 LEU   B O    1 
ATOM   6431 C CB   . LEU   B 1 127 ? 39.150 -24.931 0.363   1.00 12.68 ?  127 LEU   B CB   1 
ATOM   6432 C CG   . LEU   B 1 127 ? 39.338 -23.666 -0.467  1.00 13.11 ?  127 LEU   B CG   1 
ATOM   6433 C CD1  . LEU   B 1 127 ? 38.221 -22.690 -0.122  1.00 13.79 ?  127 LEU   B CD1  1 
ATOM   6434 C CD2  . LEU   B 1 127 ? 40.710 -23.035 -0.249  1.00 14.00 ?  127 LEU   B CD2  1 
ATOM   6435 H H    . LEU   B 1 127 ? 39.444 -26.233 -1.669  1.00 14.52 ?  127 LEU   B H    1 
ATOM   6436 H HA   . LEU   B 1 127 ? 41.050 -25.690 0.335   1.00 15.26 ?  127 LEU   B HA   1 
ATOM   6437 H HB2  . LEU   B 1 127 ? 38.268 -25.282 0.155   1.00 15.24 ?  127 LEU   B HB2  1 
ATOM   6438 H HB3  . LEU   B 1 127 ? 39.173 -24.669 1.298   1.00 15.24 ?  127 LEU   B HB3  1 
ATOM   6439 H HG   . LEU   B 1 127 ? 39.254 -23.886 -1.404  1.00 15.76 ?  127 LEU   B HG   1 
ATOM   6440 H HD11 . LEU   B 1 127 ? 38.340 -21.876 -0.642  1.00 16.57 ?  127 LEU   B HD11 1 
ATOM   6441 H HD12 . LEU   B 1 127 ? 37.367 -23.093 -0.330  1.00 16.57 ?  127 LEU   B HD12 1 
ATOM   6442 H HD13 . LEU   B 1 127 ? 38.267 -22.477 0.826   1.00 16.57 ?  127 LEU   B HD13 1 
ATOM   6443 H HD21 . LEU   B 1 127 ? 40.744 -22.180 -0.705  1.00 16.83 ?  127 LEU   B HD21 1 
ATOM   6444 H HD22 . LEU   B 1 127 ? 40.851 -22.904 0.705   1.00 16.83 ?  127 LEU   B HD22 1 
ATOM   6445 H HD23 . LEU   B 1 127 ? 41.390 -23.628 -0.603  1.00 16.83 ?  127 LEU   B HD23 1 
ATOM   6446 N N    . SER   B 1 128 ? 40.566 -27.081 2.282   1.00 12.19 ?  128 SER   B N    1 
ATOM   6447 C CA   . SER   B 1 128 ? 40.454 -27.997 3.405   1.00 12.80 ?  128 SER   B CA   1 
ATOM   6448 C C    . SER   B 1 128 ? 40.936 -29.409 3.080   1.00 14.12 ?  128 SER   B C    1 
ATOM   6449 O O    . SER   B 1 128 ? 40.838 -30.285 3.937   1.00 15.88 ?  128 SER   B O    1 
ATOM   6450 C CB   . SER   B 1 128 ? 39.054 -27.994 4.049   1.00 12.94 ?  128 SER   B CB   1 
ATOM   6451 O OG   . SER   B 1 128 ? 38.757 -26.712 4.600   1.00 13.52 ?  128 SER   B OG   1 
ATOM   6452 H H    . SER   B 1 128 ? 41.120 -26.445 2.437   1.00 14.65 ?  128 SER   B H    1 
ATOM   6453 H HA   . SER   B 1 128 ? 41.050 -27.664 4.083   1.00 15.38 ?  128 SER   B HA   1 
ATOM   6454 H HB2  . SER   B 1 128 ? 38.389 -28.225 3.385   1.00 15.56 ?  128 SER   B HB2  1 
ATOM   6455 H HB3  . SER   B 1 128 ? 39.040 -28.660 4.769   1.00 15.56 ?  128 SER   B HB3  1 
ATOM   6456 H HG   . SER   B 1 128 ? 39.332 -26.511 5.179   1.00 16.26 ?  128 SER   B HG   1 
ATOM   6457 N N    . ALA   B 1 129 ? 41.509 -29.639 1.892   1.00 15.16 ?  129 ALA   B N    1 
ATOM   6458 C CA   . ALA   B 1 129 ? 42.042 -30.940 1.523   1.00 16.21 ?  129 ALA   B CA   1 
ATOM   6459 C C    . ALA   B 1 129 ? 43.433 -31.130 2.118   1.00 15.18 ?  129 ALA   B C    1 
ATOM   6460 O O    . ALA   B 1 129 ? 43.998 -30.235 2.761   1.00 14.59 ?  129 ALA   B O    1 
ATOM   6461 C CB   . ALA   B 1 129 ? 42.091 -31.086 0.003   1.00 18.07 ?  129 ALA   B CB   1 
ATOM   6462 H H    . ALA   B 1 129 ? 41.589 -29.041 1.270   1.00 18.21 ?  129 ALA   B H    1 
ATOM   6463 H HA   . ALA   B 1 129 ? 41.459 -31.628 1.873   1.00 19.48 ?  129 ALA   B HA   1 
ATOM   6464 H HB1  . ALA   B 1 129 ? 42.439 -31.965 -0.218  1.00 21.71 ?  129 ALA   B HB1  1 
ATOM   6465 H HB2  . ALA   B 1 129 ? 41.195 -30.987 -0.356  1.00 21.71 ?  129 ALA   B HB2  1 
ATOM   6466 H HB3  . ALA   B 1 129 ? 42.671 -30.399 -0.364  1.00 21.71 ?  129 ALA   B HB3  1 
ATOM   6467 N N    . GLY   B 1 130 ? 43.987 -32.318 1.885   1.00 15.27 ?  130 GLY   B N    1 
ATOM   6468 C CA   . GLY   B 1 130 ? 45.376 -32.562 2.230   1.00 15.83 ?  130 GLY   B CA   1 
ATOM   6469 C C    . GLY   B 1 130 ? 45.601 -32.454 3.720   1.00 15.73 ?  130 GLY   B C    1 
ATOM   6470 O O    . GLY   B 1 130 ? 44.902 -33.083 4.527   1.00 16.28 ?  130 GLY   B O    1 
ATOM   6471 H H    . GLY   B 1 130 ? 43.582 -32.987 1.519   1.00 18.35 ?  130 GLY   B H    1 
ATOM   6472 H HA2  . GLY   B 1 130 ? 45.629 -33.457 1.938   1.00 19.02 ?  130 GLY   B HA2  1 
ATOM   6473 H HA3  . GLY   B 1 130 ? 45.944 -31.922 1.779   1.00 19.02 ?  130 GLY   B HA3  1 
ATOM   6474 N N    . ILE   B 1 131 ? 46.578 -31.621 4.097   1.00 15.98 ?  131 ILE   B N    1 
ATOM   6475 C CA   . ILE   B 1 131 ? 46.957 -31.489 5.498   1.00 16.96 ?  131 ILE   B CA   1 
ATOM   6476 C C    . ILE   B 1 131 ? 45.849 -30.893 6.350   1.00 16.10 ?  131 ILE   B C    1 
ATOM   6477 O O    . ILE   B 1 131 ? 45.936 -30.955 7.578   1.00 17.30 ?  131 ILE   B O    1 
ATOM   6478 C CB   . ILE   B 1 131 ? 48.285 -30.717 5.682   1.00 18.72 ?  131 ILE   B CB   1 
ATOM   6479 C CG1  . ILE   B 1 131 ? 48.121 -29.241 5.298   1.00 19.74 ?  131 ILE   B CG1  1 
ATOM   6480 C CG2  . ILE   B 1 131 ? 49.405 -31.363 4.868   1.00 19.65 ?  131 ILE   B CG2  1 
ATOM   6481 C CD1  . ILE   B 1 131 ? 49.347 -28.387 5.585   1.00 21.11 ?  131 ILE   B CD1  1 
ATOM   6482 H H    . ILE   B 1 131 ? 47.028 -31.122 3.559   1.00 19.20 ?  131 ILE   B H    1 
ATOM   6483 H HA   . ILE   B 1 131 ? 47.112 -32.383 5.837   1.00 20.37 ?  131 ILE   B HA   1 
ATOM   6484 H HB   . ILE   B 1 131 ? 48.529 -30.757 6.619   1.00 22.49 ?  131 ILE   B HB   1 
ATOM   6485 H HG12 . ILE   B 1 131 ? 47.933 -29.186 4.347   1.00 23.71 ?  131 ILE   B HG12 1 
ATOM   6486 H HG13 . ILE   B 1 131 ? 47.379 -28.862 5.798   1.00 23.71 ?  131 ILE   B HG13 1 
ATOM   6487 H HG21 . ILE   B 1 131 ? 50.250 -30.956 5.117   1.00 23.60 ?  131 ILE   B HG21 1 
ATOM   6488 H HG22 . ILE   B 1 131 ? 49.423 -32.311 5.059   1.00 23.60 ?  131 ILE   B HG22 1 
ATOM   6489 H HG23 . ILE   B 1 131 ? 49.232 -31.216 3.924   1.00 23.60 ?  131 ILE   B HG23 1 
ATOM   6490 H HD11 . ILE   B 1 131 ? 49.125 -27.457 5.422   1.00 25.35 ?  131 ILE   B HD11 1 
ATOM   6491 H HD12 . ILE   B 1 131 ? 49.602 -28.509 6.512   1.00 25.35 ?  131 ILE   B HD12 1 
ATOM   6492 H HD13 . ILE   B 1 131 ? 50.067 -28.665 5.001   1.00 25.35 ?  131 ILE   B HD13 1 
ATOM   6493 N N    . PHE   B 1 132 ? 44.805 -30.327 5.733   1.00 15.13 ?  132 PHE   B N    1 
ATOM   6494 C CA   . PHE   B 1 132 ? 43.659 -29.803 6.469   1.00 15.42 ?  132 PHE   B CA   1 
ATOM   6495 C C    . PHE   B 1 132 ? 42.619 -30.875 6.795   1.00 16.74 ?  132 PHE   B C    1 
ATOM   6496 O O    . PHE   B 1 132 ? 41.709 -30.606 7.588   1.00 18.18 ?  132 PHE   B O    1 
ATOM   6497 C CB   . PHE   B 1 132 ? 42.991 -28.667 5.682   1.00 14.54 ?  132 PHE   B CB   1 
ATOM   6498 C CG   . PHE   B 1 132 ? 43.690 -27.320 5.791   1.00 14.06 ?  132 PHE   B CG   1 
ATOM   6499 C CD1  . PHE   B 1 132 ? 44.989 -27.145 5.339   1.00 15.38 ?  132 PHE   B CD1  1 
ATOM   6500 C CD2  . PHE   B 1 132 ? 43.009 -26.216 6.290   1.00 13.59 ?  132 PHE   B CD2  1 
ATOM   6501 C CE1  . PHE   B 1 132 ? 45.608 -25.906 5.426   1.00 15.65 ?  132 PHE   B CE1  1 
ATOM   6502 C CE2  . PHE   B 1 132 ? 43.620 -24.975 6.371   1.00 13.74 ?  132 PHE   B CE2  1 
ATOM   6503 C CZ   . PHE   B 1 132 ? 44.918 -24.822 5.938   1.00 15.04 ?  132 PHE   B CZ   1 
ATOM   6504 H H    . PHE   B 1 132 ? 44.735 -30.249 4.884   1.00 18.18 ?  132 PHE   B H    1 
ATOM   6505 H HA   . PHE   B 1 132 ? 43.972 -29.439 7.310   1.00 18.53 ?  132 PHE   B HA   1 
ATOM   6506 H HB2  . PHE   B 1 132 ? 42.980 -28.916 4.745   1.00 17.48 ?  132 PHE   B HB2  1 
ATOM   6507 H HB3  . PHE   B 1 132 ? 42.084 -28.564 6.005   1.00 17.48 ?  132 PHE   B HB3  1 
ATOM   6508 H HD1  . PHE   B 1 132 ? 45.457 -27.878 4.999   1.00 18.48 ?  132 PHE   B HD1  1 
ATOM   6509 H HD2  . PHE   B 1 132 ? 42.129 -26.320 6.587   1.00 16.34 ?  132 PHE   B HD2  1 
ATOM   6510 H HE1  . PHE   B 1 132 ? 46.483 -25.807 5.135   1.00 18.80 ?  132 PHE   B HE1  1 
ATOM   6511 H HE2  . PHE   B 1 132 ? 43.153 -24.251 6.724   1.00 16.52 ?  132 PHE   B HE2  1 
ATOM   6512 H HZ   . PHE   B 1 132 ? 45.330 -23.991 6.001   1.00 18.08 ?  132 PHE   B HZ   1 
ATOM   6513 N N    . GLY   B 1 133 ? 42.714 -32.070 6.198   1.00 16.68 ?  133 GLY   B N    1 
ATOM   6514 C CA   . GLY   B 1 133 ? 41.998 -33.230 6.697   1.00 17.53 ?  133 GLY   B CA   1 
ATOM   6515 C C    . GLY   B 1 133 ? 40.605 -33.494 6.156   1.00 18.17 ?  133 GLY   B C    1 
ATOM   6516 O O    . GLY   B 1 133 ? 40.012 -34.512 6.530   1.00 20.17 ?  133 GLY   B O    1 
ATOM   6517 H H    . GLY   B 1 133 ? 43.196 -32.227 5.500   1.00 20.04 ?  133 GLY   B H    1 
ATOM   6518 H HA2  . GLY   B 1 133 ? 42.533 -34.017 6.519   1.00 21.07 ?  133 GLY   B HA2  1 
ATOM   6519 H HA3  . GLY   B 1 133 ? 41.911 -33.141 7.656   1.00 21.07 ?  133 GLY   B HA3  1 
ATOM   6520 N N    . ALA   B 1 134 ? 40.052 -32.630 5.310   1.00 16.99 ?  134 ALA   B N    1 
ATOM   6521 C CA   . ALA   B 1 134 ? 38.726 -32.904 4.773   1.00 16.80 ?  134 ALA   B CA   1 
ATOM   6522 C C    . ALA   B 1 134 ? 38.808 -33.896 3.618   1.00 16.23 ?  134 ALA   B C    1 
ATOM   6523 O O    . ALA   B 1 134 ? 39.862 -34.087 3.002   1.00 17.16 ?  134 ALA   B O    1 
ATOM   6524 C CB   . ALA   B 1 134 ? 38.049 -31.619 4.300   1.00 17.75 ?  134 ALA   B CB   1 
ATOM   6525 H H    . ALA   B 1 134 ? 40.405 -31.890 5.043   1.00 20.42 ?  134 ALA   B H    1 
ATOM   6526 H HA   . ALA   B 1 134 ? 38.173 -33.296 5.469   1.00 20.18 ?  134 ALA   B HA   1 
ATOM   6527 H HB1  . ALA   B 1 134 ? 37.161 -31.833 3.968   1.00 21.33 ?  134 ALA   B HB1  1 
ATOM   6528 H HB2  . ALA   B 1 134 ? 37.981 -31.006 5.048   1.00 21.33 ?  134 ALA   B HB2  1 
ATOM   6529 H HB3  . ALA   B 1 134 ? 38.580 -31.225 3.593   1.00 21.33 ?  134 ALA   B HB3  1 
ATOM   6530 N N    . ASP   B 1 135 ? 37.674 -34.531 3.332   1.00 16.47 ?  135 ASP   B N    1 
ATOM   6531 C CA   . ASP   B 1 135 ? 37.573 -35.423 2.187   1.00 17.39 ?  135 ASP   B CA   1 
ATOM   6532 C C    . ASP   B 1 135 ? 37.673 -34.583 0.920   1.00 16.21 ?  135 ASP   B C    1 
ATOM   6533 O O    . ASP   B 1 135 ? 36.821 -33.709 0.701   1.00 16.42 ?  135 ASP   B O    1 
ATOM   6534 C CB   . ASP   B 1 135 ? 36.230 -36.148 2.243   1.00 19.29 ?  135 ASP   B CB   1 
ATOM   6535 C CG   . ASP   B 1 135 ? 36.043 -37.137 1.113   1.00 21.34 ?  135 ASP   B CG   1 
ATOM   6536 O OD1  . ASP   B 1 135 ? 36.902 -37.186 0.208   1.00 21.18 ?  135 ASP   B OD1  1 
ATOM   6537 O OD2  . ASP   B 1 135 ? 35.034 -37.878 1.140   1.00 24.11 -1 135 ASP   B OD2  1 
ATOM   6538 H H    . ASP   B 1 135 ? 36.945 -34.463 3.786   1.00 19.80 ?  135 ASP   B H    1 
ATOM   6539 H HA   . ASP   B 1 135 ? 38.285 -36.077 2.211   1.00 20.89 ?  135 ASP   B HA   1 
ATOM   6540 H HB2  . ASP   B 1 135 ? 36.172 -36.633 3.080   1.00 23.18 ?  135 ASP   B HB2  1 
ATOM   6541 H HB3  . ASP   B 1 135 ? 35.517 -35.496 2.184   1.00 23.18 ?  135 ASP   B HB3  1 
ATOM   6542 N N    . PRO   B 1 136 ? 38.687 -34.786 0.075   1.00 16.34 ?  136 PRO   B N    1 
ATOM   6543 C CA   . PRO   B 1 136 ? 38.776 -33.971 -1.147  1.00 15.88 ?  136 PRO   B CA   1 
ATOM   6544 C C    . PRO   B 1 136 ? 37.584 -34.124 -2.065  1.00 15.38 ?  136 PRO   B C    1 
ATOM   6545 O O    . PRO   B 1 136 ? 37.260 -33.178 -2.790  1.00 14.66 ?  136 PRO   B O    1 
ATOM   6546 C CB   . PRO   B 1 136 ? 40.078 -34.451 -1.803  1.00 16.80 ?  136 PRO   B CB   1 
ATOM   6547 C CG   . PRO   B 1 136 ? 40.305 -35.825 -1.234  1.00 18.16 ?  136 PRO   B CG   1 
ATOM   6548 C CD   . PRO   B 1 136 ? 39.783 -35.763 0.167   1.00 17.71 ?  136 PRO   B CD   1 
ATOM   6549 H HA   . PRO   B 1 136 ? 38.862 -33.033 -0.921  1.00 19.08 ?  136 PRO   B HA   1 
ATOM   6550 H HB2  . PRO   B 1 136 ? 39.970 -34.488 -2.769  1.00 20.19 ?  136 PRO   B HB2  1 
ATOM   6551 H HB3  . PRO   B 1 136 ? 40.800 -33.850 -1.564  1.00 20.19 ?  136 PRO   B HB3  1 
ATOM   6552 H HG2  . PRO   B 1 136 ? 39.810 -36.479 -1.752  1.00 21.82 ?  136 PRO   B HG2  1 
ATOM   6553 H HG3  . PRO   B 1 136 ? 41.251 -36.026 -1.235  1.00 21.82 ?  136 PRO   B HG3  1 
ATOM   6554 H HD2  . PRO   B 1 136 ? 39.442 -36.625 0.442   1.00 21.28 ?  136 PRO   B HD2  1 
ATOM   6555 H HD3  . PRO   B 1 136 ? 40.462 -35.432 0.774   1.00 21.28 ?  136 PRO   B HD3  1 
ATOM   6556 N N    . ILE   B 1 137 ? 36.927 -35.286 -2.070  1.00 15.34 ?  137 ILE   B N    1 
ATOM   6557 C CA   . ILE   B 1 137 ? 35.702 -35.450 -2.848  1.00 15.70 ?  137 ILE   B CA   1 
ATOM   6558 C C    . ILE   B 1 137 ? 34.635 -34.473 -2.366  1.00 15.42 ?  137 ILE   B C    1 
ATOM   6559 O O    . ILE   B 1 137 ? 33.917 -33.858 -3.165  1.00 15.08 ?  137 ILE   B O    1 
ATOM   6560 C CB   . ILE   B 1 137 ? 35.229 -36.918 -2.785  1.00 17.77 ?  137 ILE   B CB   1 
ATOM   6561 C CG1  . ILE   B 1 137 ? 36.233 -37.820 -3.503  1.00 20.23 ?  137 ILE   B CG1  1 
ATOM   6562 C CG2  . ILE   B 1 137 ? 33.851 -37.074 -3.405  1.00 18.33 ?  137 ILE   B CG2  1 
ATOM   6563 C CD1  . ILE   B 1 137 ? 35.924 -39.300 -3.381  1.00 22.31 ?  137 ILE   B CD1  1 
ATOM   6564 H H    . ILE   B 1 137 ? 37.170 -35.988 -1.640  1.00 18.44 ?  137 ILE   B H    1 
ATOM   6565 H HA   . ILE   B 1 137 ? 35.889 -35.248 -3.780  1.00 18.86 ?  137 ILE   B HA   1 
ATOM   6566 H HB   . ILE   B 1 137 ? 35.179 -37.189 -1.859  1.00 21.35 ?  137 ILE   B HB   1 
ATOM   6567 H HG12 . ILE   B 1 137 ? 36.238 -37.604 -4.449  1.00 24.30 ?  137 ILE   B HG12 1 
ATOM   6568 H HG13 . ILE   B 1 137 ? 37.114 -37.677 -3.127  1.00 24.30 ?  137 ILE   B HG13 1 
ATOM   6569 H HG21 . ILE   B 1 137 ? 33.597 -38.012 -3.396  1.00 22.02 ?  137 ILE   B HG21 1 
ATOM   6570 H HG22 . ILE   B 1 137 ? 33.208 -36.568 -2.891  1.00 22.02 ?  137 ILE   B HG22 1 
ATOM   6571 H HG23 . ILE   B 1 137 ? 33.878 -36.753 -4.319  1.00 22.02 ?  137 ILE   B HG23 1 
ATOM   6572 H HD11 . ILE   B 1 137 ? 36.630 -39.796 -3.819  1.00 26.80 ?  137 ILE   B HD11 1 
ATOM   6573 H HD12 . ILE   B 1 137 ? 35.881 -39.542 -2.441  1.00 26.80 ?  137 ILE   B HD12 1 
ATOM   6574 H HD13 . ILE   B 1 137 ? 35.077 -39.496 -3.812  1.00 26.80 ?  137 ILE   B HD13 1 
ATOM   6575 N N    . HIS   B 1 138 ? 34.509 -34.326 -1.050  1.00 15.19 ?  138 HIS   B N    1 
ATOM   6576 C CA   . HIS   B 1 138 ? 33.567 -33.357 -0.505  1.00 15.57 ?  138 HIS   B CA   1 
ATOM   6577 C C    . HIS   B 1 138 ? 33.988 -31.930 -0.824  1.00 14.64 ?  138 HIS   B C    1 
ATOM   6578 O O    . HIS   B 1 138 ? 33.141 -31.081 -1.120  1.00 15.15 ?  138 HIS   B O    1 
ATOM   6579 C CB   . HIS   B 1 138 ? 33.460 -33.535 1.001   1.00 17.22 ?  138 HIS   B CB   1 
ATOM   6580 C CG   . HIS   B 1 138 ? 32.536 -32.555 1.647   1.00 18.56 ?  138 HIS   B CG   1 
ATOM   6581 N ND1  . HIS   B 1 138 ? 31.193 -32.491 1.346   1.00 20.06 ?  138 HIS   B ND1  1 
ATOM   6582 C CD2  . HIS   B 1 138 ? 32.766 -31.579 2.556   1.00 19.05 ?  138 HIS   B CD2  1 
ATOM   6583 C CE1  . HIS   B 1 138 ? 30.632 -31.525 2.051   1.00 20.21 ?  138 HIS   B CE1  1 
ATOM   6584 N NE2  . HIS   B 1 138 ? 31.564 -30.955 2.793   1.00 19.47 ?  138 HIS   B NE2  1 
ATOM   6585 H H    . HIS   B 1 138 ? 34.956 -34.769 -0.464  1.00 18.25 ?  138 HIS   B H    1 
ATOM   6586 H HA   . HIS   B 1 138 ? 32.694 -33.515 -0.896  1.00 18.72 ?  138 HIS   B HA   1 
ATOM   6587 H HB2  . HIS   B 1 138 ? 33.124 -34.428 1.186   1.00 20.69 ?  138 HIS   B HB2  1 
ATOM   6588 H HB3  . HIS   B 1 138 ? 34.338 -33.425 1.393   1.00 20.69 ?  138 HIS   B HB3  1 
ATOM   6589 H HD1  . HIS   B 1 138 ? 30.782 -33.009 0.789   1.00 24.10 ?  138 HIS   B HD1  1 
ATOM   6590 H HD2  . HIS   B 1 138 ? 33.578 -31.371 2.951   1.00 22.89 ?  138 HIS   B HD2  1 
ATOM   6591 H HE1  . HIS   B 1 138 ? 29.727 -31.299 2.035   1.00 24.28 ?  138 HIS   B HE1  1 
ATOM   6592 N N    . SER   B 1 139 ? 35.285 -31.636 -0.758  1.00 14.22 ?  139 SER   B N    1 
ATOM   6593 C CA   . SER   B 1 139 ? 35.728 -30.289 -1.076  1.00 13.38 ?  139 SER   B CA   1 
ATOM   6594 C C    . SER   B 1 139 ? 35.396 -29.936 -2.515  1.00 12.70 ?  139 SER   B C    1 
ATOM   6595 O O    . SER   B 1 139 ? 34.959 -28.819 -2.795  1.00 13.13 ?  139 SER   B O    1 
ATOM   6596 C CB   . SER   B 1 139 ? 37.220 -30.150 -0.810  1.00 13.68 ?  139 SER   B CB   1 
ATOM   6597 O OG   . SER   B 1 139 ? 37.630 -28.821 -1.083  1.00 13.94 ?  139 SER   B OG   1 
ATOM   6598 H H    . SER   B 1 139 ? 35.911 -32.182 -0.550  1.00 17.10 ?  139 SER   B H    1 
ATOM   6599 H HA   . SER   B 1 139 ? 35.255 -29.661 -0.507  1.00 16.08 ?  139 SER   B HA   1 
ATOM   6600 H HB2  . SER   B 1 139 ? 37.394 -30.353 0.120   1.00 16.44 ?  139 SER   B HB2  1 
ATOM   6601 H HB3  . SER   B 1 139 ? 37.708 -30.745 -1.390  1.00 16.44 ?  139 SER   B HB3  1 
ATOM   6602 H HG   . SER   B 1 139 ? 38.451 -28.727 -0.922  1.00 16.76 ?  139 SER   B HG   1 
ATOM   6603 N N    . LEU   B 1 140 ? 35.575 -30.881 -3.438  1.00 13.11 ?  140 LEU   B N    1 
ATOM   6604 C CA   . LEU   B 1 140 ? 35.211 -30.633 -4.828  1.00 13.07 ?  140 LEU   B CA   1 
ATOM   6605 C C    . LEU   B 1 140 ? 33.709 -30.397 -4.959  1.00 13.60 ?  140 LEU   B C    1 
ATOM   6606 O O    . LEU   B 1 140 ? 33.274 -29.504 -5.696  1.00 13.28 ?  140 LEU   B O    1 
ATOM   6607 C CB   . LEU   B 1 140 ? 35.672 -31.798 -5.703  1.00 13.23 ?  140 LEU   B CB   1 
ATOM   6608 C CG   . LEU   B 1 140 ? 35.314 -31.686 -7.176  1.00 13.61 ?  140 LEU   B CG   1 
ATOM   6609 C CD1  . LEU   B 1 140 ? 35.903 -30.422 -7.776  1.00 14.60 ?  140 LEU   B CD1  1 
ATOM   6610 C CD2  . LEU   B 1 140 ? 35.776 -32.922 -7.923  1.00 14.31 ?  140 LEU   B CD2  1 
ATOM   6611 H H    . LEU   B 1 140 ? 35.896 -31.655 -3.289  1.00 15.76 ?  140 LEU   B H    1 
ATOM   6612 H HA   . LEU   B 1 140 ? 35.667 -29.833 -5.138  1.00 15.71 ?  140 LEU   B HA   1 
ATOM   6613 H HB2  . LEU   B 1 140 ? 36.638 -31.869 -5.643  1.00 15.91 ?  140 LEU   B HB2  1 
ATOM   6614 H HB3  . LEU   B 1 140 ? 35.266 -32.614 -5.372  1.00 15.91 ?  140 LEU   B HB3  1 
ATOM   6615 H HG   . LEU   B 1 140 ? 34.354 -31.625 -7.263  1.00 16.36 ?  140 LEU   B HG   1 
ATOM   6616 H HD11 . LEU   B 1 140 ? 35.792 -30.449 -8.738  1.00 17.55 ?  140 LEU   B HD11 1 
ATOM   6617 H HD12 . LEU   B 1 140 ? 35.436 -29.651 -7.413  1.00 17.55 ?  140 LEU   B HD12 1 
ATOM   6618 H HD13 . LEU   B 1 140 ? 36.845 -30.373 -7.552  1.00 17.55 ?  140 LEU   B HD13 1 
ATOM   6619 H HD21 . LEU   B 1 140 ? 35.533 -32.830 -8.859  1.00 17.20 ?  140 LEU   B HD21 1 
ATOM   6620 H HD22 . LEU   B 1 140 ? 36.729 -33.015 -7.829  1.00 17.20 ?  140 LEU   B HD22 1 
ATOM   6621 H HD23 . LEU   B 1 140 ? 35.323 -33.696 -7.543  1.00 17.20 ?  140 LEU   B HD23 1 
ATOM   6622 N N    . ARG   B 1 141 ? 32.906 -31.191 -4.245  1.00 13.81 ?  141 ARG   B N    1 
ATOM   6623 C CA   . ARG   B 1 141 ? 31.455 -31.011 -4.216  1.00 14.64 ?  141 ARG   B CA   1 
ATOM   6624 C C    . ARG   B 1 141 ? 31.082 -29.597 -3.788  1.00 13.90 ?  141 ARG   B C    1 
ATOM   6625 O O    . ARG   B 1 141 ? 30.286 -28.916 -4.450  1.00 13.91 ?  141 ARG   B O    1 
ATOM   6626 C CB   . ARG   B 1 141 ? 30.856 -32.043 -3.247  1.00 15.82 ?  141 ARG   B CB   1 
ATOM   6627 C CG   . ARG   B 1 141 ? 29.387 -31.924 -2.945  1.00 17.84 ?  141 ARG   B CG   1 
ATOM   6628 C CD   . ARG   B 1 141 ? 28.602 -32.550 -4.030  1.00 19.59 ?  141 ARG   B CD   1 
ATOM   6629 N NE   . ARG   B 1 141 ? 28.331 -31.627 -5.119  1.00 19.77 ?  141 ARG   B NE   1 
ATOM   6630 C CZ   . ARG   B 1 141 ? 28.286 -31.967 -6.400  1.00 19.39 ?  141 ARG   B CZ   1 
ATOM   6631 N NH1  . ARG   B 1 141 ? 28.683 -33.159 -6.816  1.00 19.26 ?  141 ARG   B NH1  1 
ATOM   6632 N NH2  . ARG   B 1 141 ? 27.827 -31.086 -7.285  1.00 20.58 ?  141 ARG   B NH2  1 
ATOM   6633 H H    . ARG   B 1 141 ? 33.186 -31.847 -3.765  1.00 16.59 ?  141 ARG   B H    1 
ATOM   6634 H HA   . ARG   B 1 141 ? 31.094 -31.169 -5.098  1.00 17.59 ?  141 ARG   B HA   1 
ATOM   6635 H HB2  . ARG   B 1 141 ? 31.019 -32.926 -3.612  1.00 19.01 ?  141 ARG   B HB2  1 
ATOM   6636 H HB3  . ARG   B 1 141 ? 31.329 -31.965 -2.402  1.00 19.01 ?  141 ARG   B HB3  1 
ATOM   6637 H HG2  . ARG   B 1 141 ? 29.199 -32.377 -2.113  1.00 21.44 ?  141 ARG   B HG2  1 
ATOM   6638 H HG3  . ARG   B 1 141 ? 29.138 -30.984 -2.879  1.00 21.44 ?  141 ARG   B HG3  1 
ATOM   6639 H HD2  . ARG   B 1 141 ? 29.097 -33.311 -4.382  1.00 23.53 ?  141 ARG   B HD2  1 
ATOM   6640 H HD3  . ARG   B 1 141 ? 27.760 -32.853 -3.668  1.00 23.53 ?  141 ARG   B HD3  1 
ATOM   6641 H HE   . ARG   B 1 141 ? 28.194 -30.800 -4.915  1.00 23.75 ?  141 ARG   B HE   1 
ATOM   6642 H HH11 . ARG   B 1 141 ? 28.971 -33.743 -6.257  1.00 23.14 ?  141 ARG   B HH11 1 
ATOM   6643 H HH12 . ARG   B 1 141 ? 28.650 -33.349 -7.653  1.00 23.14 ?  141 ARG   B HH12 1 
ATOM   6644 H HH21 . ARG   B 1 141 ? 27.572 -30.303 -7.026  1.00 24.72 ?  141 ARG   B HH21 1 
ATOM   6645 H HH22 . ARG   B 1 141 ? 27.809 -31.284 -8.122  1.00 24.72 ?  141 ARG   B HH22 1 
ATOM   6646 N N    . VAL   B 1 142 ? 31.628 -29.147 -2.660  1.00 13.60 ?  142 VAL   B N    1 
ATOM   6647 C CA   . VAL   B 1 142 ? 31.297 -27.814 -2.176  1.00 13.23 ?  142 VAL   B CA   1 
ATOM   6648 C C    . VAL   B 1 142 ? 31.776 -26.760 -3.167  1.00 12.79 ?  142 VAL   B C    1 
ATOM   6649 O O    . VAL   B 1 142 ? 31.085 -25.768 -3.415  1.00 13.11 ?  142 VAL   B O    1 
ATOM   6650 C CB   . VAL   B 1 142 ? 31.851 -27.591 -0.755  1.00 13.92 ?  142 VAL   B CB   1 
ATOM   6651 C CG1  . VAL   B 1 142 ? 31.533 -26.184 -0.261  1.00 13.88 ?  142 VAL   B CG1  1 
ATOM   6652 C CG2  . VAL   B 1 142 ? 31.276 -28.619 0.194   1.00 14.64 ?  142 VAL   B CG2  1 
ATOM   6653 H H    . VAL   B 1 142 ? 32.182 -29.580 -2.168  1.00 16.35 ?  142 VAL   B H    1 
ATOM   6654 H HA   . VAL   B 1 142 ? 30.338 -27.735 -2.118  1.00 15.91 ?  142 VAL   B HA   1 
ATOM   6655 H HB   . VAL   B 1 142 ? 32.817 -27.691 -0.760  1.00 16.73 ?  142 VAL   B HB   1 
ATOM   6656 H HG11 . VAL   B 1 142 ? 31.738 -26.125 0.687   1.00 16.68 ?  142 VAL   B HG11 1 
ATOM   6657 H HG12 . VAL   B 1 142 ? 32.073 -25.542 -0.752  1.00 16.68 ?  142 VAL   B HG12 1 
ATOM   6658 H HG13 . VAL   B 1 142 ? 30.592 -26.003 -0.406  1.00 16.68 ?  142 VAL   B HG13 1 
ATOM   6659 H HG21 . VAL   B 1 142 ? 31.589 -28.430 1.092   1.00 17.60 ?  142 VAL   B HG21 1 
ATOM   6660 H HG22 . VAL   B 1 142 ? 30.308 -28.564 0.162   1.00 17.60 ?  142 VAL   B HG22 1 
ATOM   6661 H HG23 . VAL   B 1 142 ? 31.569 -29.498 -0.083  1.00 17.60 ?  142 VAL   B HG23 1 
ATOM   6662 N N    . CYS   B 1 143 ? 32.953 -26.965 -3.763  1.00 12.84 ?  143 CYS   B N    1 
ATOM   6663 C CA   . CYS   B 1 143 ? 33.454 -26.026 -4.762  1.00 12.68 ?  143 CYS   B CA   1 
ATOM   6664 C C    . CYS   B 1 143 ? 32.454 -25.878 -5.901  1.00 12.66 ?  143 CYS   B C    1 
ATOM   6665 O O    . CYS   B 1 143 ? 32.046 -24.767 -6.255  1.00 12.63 ?  143 CYS   B O    1 
ATOM   6666 C CB   . CYS   B 1 143 ? 34.805 -26.518 -5.291  1.00 12.39 ?  143 CYS   B CB   1 
ATOM   6667 S SG   . CYS   B 1 143 ? 35.564 -25.420 -6.507  1.00 12.95 ?  143 CYS   B SG   1 
ATOM   6668 H H    . CYS   B 1 143 ? 33.472 -27.624 -3.605  1.00 15.44 ?  143 CYS   B H    1 
ATOM   6669 H HA   . CYS   B 1 143 ? 33.587 -25.150 -4.355  1.00 15.24 ?  143 CYS   B HA   1 
ATOM   6670 H HB2  . CYS   B 1 143 ? 35.424 -26.605 -4.551  1.00 14.90 ?  143 CYS   B HB2  1 
ATOM   6671 H HB3  . CYS   B 1 143 ? 34.677 -27.376 -5.714  1.00 14.90 ?  143 CYS   B HB3  1 
ATOM   6672 H HG   . CYS   B 1 143 ? 36.628 -25.868 -6.836  1.00 15.57 ?  143 CYS   B HG   1 
ATOM   6673 N N    . VAL   B 1 144 ? 32.047 -26.997 -6.494  1.00 12.92 ?  144 VAL   B N    1 
ATOM   6674 C CA   . VAL   B 1 144 ? 31.139 -26.933 -7.632  1.00 14.09 ?  144 VAL   B CA   1 
ATOM   6675 C C    . VAL   B 1 144 ? 29.805 -26.318 -7.250  1.00 14.15 ?  144 VAL   B C    1 
ATOM   6676 O O    . VAL   B 1 144 ? 29.193 -25.601 -8.051  1.00 15.49 ?  144 VAL   B O    1 
ATOM   6677 C CB   . VAL   B 1 144 ? 30.973 -28.345 -8.191  1.00 16.08 ?  144 VAL   B CB   1 
ATOM   6678 C CG1  . VAL   B 1 144 ? 29.694 -28.473 -9.022  1.00 18.24 ?  144 VAL   B CG1  1 
ATOM   6679 C CG2  . VAL   B 1 144 ? 32.215 -28.757 -8.976  1.00 16.81 ?  144 VAL   B CG2  1 
ATOM   6680 H H    . VAL   B 1 144 ? 32.277 -27.789 -6.265  1.00 15.53 ?  144 VAL   B H    1 
ATOM   6681 H HA   . VAL   B 1 144 ? 31.530 -26.386 -8.333  1.00 16.94 ?  144 VAL   B HA   1 
ATOM   6682 H HB   . VAL   B 1 144 ? 30.886 -28.964 -7.447  1.00 19.33 ?  144 VAL   B HB   1 
ATOM   6683 H HG11 . VAL   B 1 144 ? 29.758 -29.269 -9.580  1.00 21.92 ?  144 VAL   B HG11 1 
ATOM   6684 H HG12 . VAL   B 1 144 ? 28.931 -28.559 -8.427  1.00 21.92 ?  144 VAL   B HG12 1 
ATOM   6685 H HG13 . VAL   B 1 144 ? 29.597 -27.691 -9.582  1.00 21.92 ?  144 VAL   B HG13 1 
ATOM   6686 H HG21 . VAL   B 1 144 ? 32.090 -29.661 -9.317  1.00 20.20 ?  144 VAL   B HG21 1 
ATOM   6687 H HG22 . VAL   B 1 144 ? 32.336 -28.143 -9.717  1.00 20.20 ?  144 VAL   B HG22 1 
ATOM   6688 H HG23 . VAL   B 1 144 ? 32.981 -28.729 -8.389  1.00 20.20 ?  144 VAL   B HG23 1 
ATOM   6689 N N    . ASP   B 1 145 ? 29.341 -26.564 -6.029  1.00 14.19 ?  145 ASP   B N    1 
ATOM   6690 C CA   . ASP   B 1 145 ? 28.030 -26.095 -5.602  1.00 14.86 ?  145 ASP   B CA   1 
ATOM   6691 C C    . ASP   B 1 145 ? 28.060 -24.674 -5.058  1.00 14.26 ?  145 ASP   B C    1 
ATOM   6692 O O    . ASP   B 1 145 ? 27.001 -24.140 -4.708  1.00 15.97 ?  145 ASP   B O    1 
ATOM   6693 C CB   . ASP   B 1 145 ? 27.456 -27.019 -4.522  1.00 16.17 ?  145 ASP   B CB   1 
ATOM   6694 C CG   . ASP   B 1 145 ? 27.075 -28.391 -5.042  1.00 18.09 ?  145 ASP   B CG   1 
ATOM   6695 O OD1  . ASP   B 1 145 ? 26.953 -28.564 -6.272  1.00 18.49 ?  145 ASP   B OD1  1 
ATOM   6696 O OD2  . ASP   B 1 145 ? 26.891 -29.295 -4.198  1.00 19.96 -1 145 ASP   B OD2  1 
ATOM   6697 H H    . ASP   B 1 145 ? 29.782 -26.976 -5.421  1.00 17.05 ?  145 ASP   B H    1 
ATOM   6698 H HA   . ASP   B 1 145 ? 27.433 -26.097 -6.366  1.00 17.86 ?  145 ASP   B HA   1 
ATOM   6699 H HB2  . ASP   B 1 145 ? 28.114 -27.143 -3.832  1.00 19.44 ?  145 ASP   B HB2  1 
ATOM   6700 H HB3  . ASP   B 1 145 ? 26.655 -26.608 -4.158  1.00 19.44 ?  145 ASP   B HB3  1 
ATOM   6701 N N    . THR   B 1 146 ? 29.234 -24.058 -4.963  1.00 12.54 ?  146 THR   B N    1 
ATOM   6702 C CA   . THR   B 1 146 ? 29.377 -22.742 -4.351  1.00 12.03 ?  146 THR   B CA   1 
ATOM   6703 C C    . THR   B 1 146 ? 30.012 -21.715 -5.269  1.00 11.69 ?  146 THR   B C    1 
ATOM   6704 O O    . THR   B 1 146 ? 29.558 -20.560 -5.317  1.00 12.26 ?  146 THR   B O    1 
ATOM   6705 C CB   . THR   B 1 146 ? 30.214 -22.848 -3.075  1.00 12.59 ?  146 THR   B CB   1 
ATOM   6706 O OG1  . THR   B 1 146 ? 29.640 -23.838 -2.212  1.00 12.99 ?  146 THR   B OG1  1 
ATOM   6707 C CG2  . THR   B 1 146 ? 30.290 -21.501 -2.359  1.00 12.57 ?  146 THR   B CG2  1 
ATOM   6708 H H    . THR   B 1 146 ? 29.984 -24.377 -5.260  1.00 15.08 ?  146 THR   B H    1 
ATOM   6709 H HA   . THR   B 1 146 ? 28.503 -22.412 -4.104  1.00 14.46 ?  146 THR   B HA   1 
ATOM   6710 H HB   . THR   B 1 146 ? 31.121 -23.107 -3.314  1.00 15.14 ?  146 THR   B HB   1 
ATOM   6711 H HG1  . THR   B 1 146 ? 29.674 -24.596 -2.596  1.00 15.61 ?  146 THR   B HG1  1 
ATOM   6712 H HG21 . THR   B 1 146 ? 30.638 -21.618 -1.465  1.00 15.11 ?  146 THR   B HG21 1 
ATOM   6713 H HG22 . THR   B 1 146 ? 30.874 -20.892 -2.846  1.00 15.11 ?  146 THR   B HG22 1 
ATOM   6714 H HG23 . THR   B 1 146 ? 29.405 -21.104 -2.304  1.00 15.11 ?  146 THR   B HG23 1 
ATOM   6715 N N    . VAL   B 1 147 ? 31.079 -22.089 -5.963  1.00 11.74 ?  147 VAL   B N    1 
ATOM   6716 C CA   . VAL   B 1 147 ? 31.798 -21.148 -6.807  1.00 11.31 ?  147 VAL   B CA   1 
ATOM   6717 C C    . VAL   B 1 147 ? 31.062 -21.015 -8.129  1.00 11.89 ?  147 VAL   B C    1 
ATOM   6718 O O    . VAL   B 1 147 ? 30.692 -22.017 -8.755  1.00 12.88 ?  147 VAL   B O    1 
ATOM   6719 C CB   . VAL   B 1 147 ? 33.250 -21.606 -7.018  1.00 11.48 ?  147 VAL   B CB   1 
ATOM   6720 C CG1  . VAL   B 1 147 ? 34.010 -20.586 -7.841  1.00 11.65 ?  147 VAL   B CG1  1 
ATOM   6721 C CG2  . VAL   B 1 147 ? 33.936 -21.825 -5.680  1.00 11.87 ?  147 VAL   B CG2  1 
ATOM   6722 H H    . VAL   B 1 147 ? 31.411 -22.886 -5.964  1.00 14.11 ?  147 VAL   B H    1 
ATOM   6723 H HA   . VAL   B 1 147 ? 31.817 -20.278 -6.377  1.00 13.61 ?  147 VAL   B HA   1 
ATOM   6724 H HB   . VAL   B 1 147 ? 33.255 -22.447 -7.504  1.00 13.80 ?  147 VAL   B HB   1 
ATOM   6725 H HG11 . VAL   B 1 147 ? 34.953 -20.817 -7.836  1.00 14.01 ?  147 VAL   B HG11 1 
ATOM   6726 H HG12 . VAL   B 1 147 ? 33.674 -20.596 -8.751  1.00 14.01 ?  147 VAL   B HG12 1 
ATOM   6727 H HG13 . VAL   B 1 147 ? 33.884 -19.709 -7.449  1.00 14.01 ?  147 VAL   B HG13 1 
ATOM   6728 H HG21 . VAL   B 1 147 ? 34.874 -22.016 -5.833  1.00 14.28 ?  147 VAL   B HG21 1 
ATOM   6729 H HG22 . VAL   B 1 147 ? 33.843 -21.023 -5.145  1.00 14.28 ?  147 VAL   B HG22 1 
ATOM   6730 H HG23 . VAL   B 1 147 ? 33.514 -22.575 -5.230  1.00 14.28 ?  147 VAL   B HG23 1 
ATOM   6731 N N    . ARG   B 1 148 ? 30.862 -19.766 -8.557  1.00 11.67 ?  148 ARG   B N    1 
ATOM   6732 C CA   . ARG   B 1 148 ? 30.230 -19.442 -9.827  1.00 12.24 ?  148 ARG   B CA   1 
ATOM   6733 C C    . ARG   B 1 148 ? 31.184 -18.770 -10.801 1.00 11.99 ?  148 ARG   B C    1 
ATOM   6734 O O    . ARG   B 1 148 ? 30.898 -18.758 -12.004 1.00 13.33 ?  148 ARG   B O    1 
ATOM   6735 C CB   . ARG   B 1 148 ? 28.998 -18.555 -9.595  1.00 12.79 ?  148 ARG   B CB   1 
ATOM   6736 C CG   . ARG   B 1 148 ? 27.923 -19.283 -8.806  1.00 13.37 ?  148 ARG   B CG   1 
ATOM   6737 C CD   . ARG   B 1 148 ? 26.711 -18.412 -8.479  1.00 14.36 ?  148 ARG   B CD   1 
ATOM   6738 N NE   . ARG   B 1 148 ? 27.075 -17.199 -7.755  1.00 14.09 ?  148 ARG   B NE   1 
ATOM   6739 C CZ   . ARG   B 1 148 ? 27.399 -17.155 -6.471  1.00 13.32 ?  148 ARG   B CZ   1 
ATOM   6740 N NH1  . ARG   B 1 148 ? 27.357 -18.238 -5.707  1.00 13.40 ?  148 ARG   B NH1  1 
ATOM   6741 N NH2  . ARG   B 1 148 ? 27.790 -15.998 -5.944  1.00 13.24 ?  148 ARG   B NH2  1 
ATOM   6742 H H    . ARG   B 1 148 ? 31.098 -19.065 -8.106  1.00 14.03 ?  148 ARG   B H    1 
ATOM   6743 H HA   . ARG   B 1 148 ? 29.931 -20.265 -10.236 1.00 14.71 ?  148 ARG   B HA   1 
ATOM   6744 H HB2  . ARG   B 1 148 ? 29.263 -17.766 -9.095  1.00 15.37 ?  148 ARG   B HB2  1 
ATOM   6745 H HB3  . ARG   B 1 148 ? 28.629 -18.299 -10.454 1.00 15.37 ?  148 ARG   B HB3  1 
ATOM   6746 H HG2  . ARG   B 1 148 ? 27.613 -20.044 -9.327  1.00 16.07 ?  148 ARG   B HG2  1 
ATOM   6747 H HG3  . ARG   B 1 148 ? 28.300 -19.594 -7.969  1.00 16.07 ?  148 ARG   B HG3  1 
ATOM   6748 H HD2  . ARG   B 1 148 ? 26.276 -18.153 -9.308  1.00 17.26 ?  148 ARG   B HD2  1 
ATOM   6749 H HD3  . ARG   B 1 148 ? 26.093 -18.922 -7.929  1.00 17.26 ?  148 ARG   B HD3  1 
ATOM   6750 H HE   . ARG   B 1 148 ? 27.089 -16.464 -8.197  1.00 16.93 ?  148 ARG   B HE   1 
ATOM   6751 H HH11 . ARG   B 1 148 ? 27.108 -18.992 -6.035  1.00 16.11 ?  148 ARG   B HH11 1 
ATOM   6752 H HH12 . ARG   B 1 148 ? 27.568 -18.184 -4.873  1.00 16.11 ?  148 ARG   B HH12 1 
ATOM   6753 H HH21 . ARG   B 1 148 ? 27.822 -15.291 -6.435  1.00 15.92 ?  148 ARG   B HH21 1 
ATOM   6754 H HH22 . ARG   B 1 148 ? 27.999 -15.951 -5.112  1.00 15.92 ?  148 ARG   B HH22 1 
ATOM   6755 N N    . THR   B 1 149 ? 32.297 -18.222 -10.314 1.00 12.06 ?  149 THR   B N    1 
ATOM   6756 C CA   . THR   B 1 149 ? 33.335 -17.666 -11.163 1.00 11.69 ?  149 THR   B CA   1 
ATOM   6757 C C    . THR   B 1 149 ? 34.215 -18.804 -11.678 1.00 11.37 ?  149 THR   B C    1 
ATOM   6758 O O    . THR   B 1 149 ? 34.022 -19.974 -11.336 1.00 12.28 ?  149 THR   B O    1 
ATOM   6759 C CB   . THR   B 1 149 ? 34.102 -16.608 -10.378 1.00 11.87 ?  149 THR   B CB   1 
ATOM   6760 O OG1  . THR   B 1 149 ? 34.564 -17.214 -9.173  1.00 11.72 ?  149 THR   B OG1  1 
ATOM   6761 C CG2  . THR   B 1 149 ? 33.209 -15.406 -10.053 1.00 12.57 ?  149 THR   B CG2  1 
ATOM   6762 H H    . THR   B 1 149 ? 32.464 -18.154 -9.469  1.00 14.50 ?  149 THR   B H    1 
ATOM   6763 H HA   . THR   B 1 149 ? 32.921 -17.230 -11.922 1.00 14.06 ?  149 THR   B HA   1 
ATOM   6764 H HB   . THR   B 1 149 ? 34.858 -16.309 -10.895 1.00 14.28 ?  149 THR   B HB   1 
ATOM   6765 H HG1  . THR   B 1 149 ? 34.994 -16.657 -8.708  1.00 14.10 ?  149 THR   B HG1  1 
ATOM   6766 H HG21 . THR   B 1 149 ? 33.715 -14.738 -9.566  1.00 15.11 ?  149 THR   B HG21 1 
ATOM   6767 H HG22 . THR   B 1 149 ? 32.871 -15.014 -10.871 1.00 15.11 ?  149 THR   B HG22 1 
ATOM   6768 H HG23 . THR   B 1 149 ? 32.454 -15.687 -9.505  1.00 15.11 ?  149 THR   B HG23 1 
ATOM   6769 N N    . ASN   B 1 150 ? 35.174 -18.478 -12.533 1.00 11.32 ?  150 ASN   B N    1 
ATOM   6770 C CA   . ASN   B 1 150 ? 35.941 -19.500 -13.235 1.00 12.22 ?  150 ASN   B CA   1 
ATOM   6771 C C    . ASN   B 1 150 ? 37.102 -19.953 -12.368 1.00 11.66 ?  150 ASN   B C    1 
ATOM   6772 O O    . ASN   B 1 150 ? 38.043 -19.194 -12.133 1.00 12.43 ?  150 ASN   B O    1 
ATOM   6773 C CB   . ASN   B 1 150 ? 36.414 -18.970 -14.578 1.00 14.31 ?  150 ASN   B CB   1 
ATOM   6774 C CG   . ASN   B 1 150 ? 35.269 -18.751 -15.527 1.00 17.00 ?  150 ASN   B CG   1 
ATOM   6775 O OD1  . ASN   B 1 150 ? 34.360 -19.574 -15.608 1.00 17.69 ?  150 ASN   B OD1  1 
ATOM   6776 N ND2  . ASN   B 1 150 ? 35.280 -17.625 -16.223 1.00 18.97 ?  150 ASN   B ND2  1 
ATOM   6777 H H    . ASN   B 1 150 ? 35.401 -17.669 -12.717 1.00 13.61 ?  150 ASN   B H    1 
ATOM   6778 H HA   . ASN   B 1 150 ? 35.364 -20.266 -13.392 1.00 14.70 ?  150 ASN   B HA   1 
ATOM   6779 H HB2  . ASN   B 1 150 ? 36.863 -18.120 -14.438 1.00 17.20 ?  150 ASN   B HB2  1 
ATOM   6780 H HB3  . ASN   B 1 150 ? 37.024 -19.611 -14.969 1.00 17.20 ?  150 ASN   B HB3  1 
ATOM   6781 H HD21 . ASN   B 1 150 ? 34.650 -17.455 -16.783 1.00 22.79 ?  150 ASN   B HD21 1 
ATOM   6782 H HD22 . ASN   B 1 150 ? 35.930 -17.065 -16.130 1.00 22.79 ?  150 ASN   B HD22 1 
ATOM   6783 N N    . VAL   B 1 151 ? 37.051 -21.196 -11.900 1.00 11.56 ?  151 VAL   B N    1 
ATOM   6784 C CA   . VAL   B 1 151 ? 38.068 -21.729 -11.006 1.00 11.59 ?  151 VAL   B CA   1 
ATOM   6785 C C    . VAL   B 1 151 ? 38.772 -22.898 -11.682 1.00 11.28 ?  151 VAL   B C    1 
ATOM   6786 O O    . VAL   B 1 151 ? 38.128 -23.833 -12.182 1.00 12.67 ?  151 VAL   B O    1 
ATOM   6787 C CB   . VAL   B 1 151 ? 37.509 -22.066 -9.608  1.00 12.75 ?  151 VAL   B CB   1 
ATOM   6788 C CG1  . VAL   B 1 151 ? 36.348 -23.057 -9.676  1.00 13.50 ?  151 VAL   B CG1  1 
ATOM   6789 C CG2  . VAL   B 1 151 ? 38.619 -22.572 -8.697  1.00 13.28 ?  151 VAL   B CG2  1 
ATOM   6790 H H    . VAL   B 1 151 ? 36.421 -21.755 -12.073 1.00 13.90 ?  151 VAL   B H    1 
ATOM   6791 H HA   . VAL   B 1 151 ? 38.740 -21.036 -10.866 1.00 13.94 ?  151 VAL   B HA   1 
ATOM   6792 H HB   . VAL   B 1 151 ? 37.171 -21.250 -9.204  1.00 15.33 ?  151 VAL   B HB   1 
ATOM   6793 H HG11 . VAL   B 1 151 ? 36.036 -23.244 -8.775  1.00 16.22 ?  151 VAL   B HG11 1 
ATOM   6794 H HG12 . VAL   B 1 151 ? 35.632 -22.665 -10.197 1.00 16.22 ?  151 VAL   B HG12 1 
ATOM   6795 H HG13 . VAL   B 1 151 ? 36.655 -23.877 -10.094 1.00 16.22 ?  151 VAL   B HG13 1 
ATOM   6796 H HG21 . VAL   B 1 151 ? 38.274 -22.641 -7.789  1.00 15.96 ?  151 VAL   B HG21 1 
ATOM   6797 H HG22 . VAL   B 1 151 ? 38.909 -23.445 -9.002  1.00 15.96 ?  151 VAL   B HG22 1 
ATOM   6798 H HG23 . VAL   B 1 151 ? 39.359 -21.948 -8.718  1.00 15.96 ?  151 VAL   B HG23 1 
ATOM   6799 N N    . TYR   B 1 152 ? 40.103 -22.816 -11.704 1.00 10.80 ?  152 TYR   B N    1 
ATOM   6800 C CA   . TYR   B 1 152 ? 41.000 -23.802 -12.289 1.00 11.41 ?  152 TYR   B CA   1 
ATOM   6801 C C    . TYR   B 1 152 ? 41.726 -24.481 -11.132 1.00 10.54 ?  152 TYR   B C    1 
ATOM   6802 O O    . TYR   B 1 152 ? 42.582 -23.870 -10.480 1.00 10.97 ?  152 TYR   B O    1 
ATOM   6803 C CB   . TYR   B 1 152 ? 41.968 -23.101 -13.244 1.00 12.08 ?  152 TYR   B CB   1 
ATOM   6804 C CG   . TYR   B 1 152 ? 41.285 -22.636 -14.510 1.00 12.59 ?  152 TYR   B CG   1 
ATOM   6805 C CD1  . TYR   B 1 152 ? 40.634 -21.407 -14.582 1.00 13.02 ?  152 TYR   B CD1  1 
ATOM   6806 C CD2  . TYR   B 1 152 ? 41.279 -23.443 -15.633 1.00 14.05 ?  152 TYR   B CD2  1 
ATOM   6807 C CE1  . TYR   B 1 152 ? 39.990 -21.004 -15.746 1.00 14.52 ?  152 TYR   B CE1  1 
ATOM   6808 C CE2  . TYR   B 1 152 ? 40.644 -23.053 -16.793 1.00 14.69 ?  152 TYR   B CE2  1 
ATOM   6809 C CZ   . TYR   B 1 152 ? 40.004 -21.832 -16.849 1.00 14.94 ?  152 TYR   B CZ   1 
ATOM   6810 O OH   . TYR   B 1 152 ? 39.371 -21.450 -18.009 1.00 17.57 ?  152 TYR   B OH   1 
ATOM   6811 H H    . TYR   B 1 152 ? 40.536 -22.145 -11.368 1.00 12.99 ?  152 TYR   B H    1 
ATOM   6812 H HA   . TYR   B 1 152 ? 40.486 -24.464 -12.781 1.00 13.71 ?  152 TYR   B HA   1 
ATOM   6813 H HB2  . TYR   B 1 152 ? 42.341 -22.324 -12.799 1.00 14.52 ?  152 TYR   B HB2  1 
ATOM   6814 H HB3  . TYR   B 1 152 ? 42.676 -23.717 -13.487 1.00 14.52 ?  152 TYR   B HB3  1 
ATOM   6815 H HD1  . TYR   B 1 152 ? 40.619 -20.853 -13.835 1.00 15.66 ?  152 TYR   B HD1  1 
ATOM   6816 H HD2  . TYR   B 1 152 ? 41.704 -24.275 -15.599 1.00 16.89 ?  152 TYR   B HD2  1 
ATOM   6817 H HE1  . TYR   B 1 152 ? 39.556 -20.186 -15.783 1.00 17.45 ?  152 TYR   B HE1  1 
ATOM   6818 H HE2  . TYR   B 1 152 ? 40.652 -23.618 -17.535 1.00 17.65 ?  152 TYR   B HE2  1 
ATOM   6819 H HH   . TYR   B 1 152 ? 39.461 -22.050 -18.590 1.00 21.11 ?  152 TYR   B HH   1 
ATOM   6820 N N    . LEU   B 1 153 ? 41.349 -25.731 -10.862 1.00 10.83 ?  153 LEU   B N    1 
ATOM   6821 C CA   . LEU   B 1 153 ? 41.854 -26.481 -9.721  1.00 10.62 ?  153 LEU   B CA   1 
ATOM   6822 C C    . LEU   B 1 153 ? 43.082 -27.289 -10.109 1.00 11.12 ?  153 LEU   B C    1 
ATOM   6823 O O    . LEU   B 1 153 ? 43.061 -28.012 -11.109 1.00 12.36 ?  153 LEU   B O    1 
ATOM   6824 C CB   . LEU   B 1 153 ? 40.779 -27.442 -9.214  1.00 11.23 ?  153 LEU   B CB   1 
ATOM   6825 C CG   . LEU   B 1 153 ? 39.528 -26.789 -8.637  1.00 11.88 ?  153 LEU   B CG   1 
ATOM   6826 C CD1  . LEU   B 1 153 ? 38.445 -27.838 -8.479  1.00 12.66 ?  153 LEU   B CD1  1 
ATOM   6827 C CD2  . LEU   B 1 153 ? 39.820 -26.116 -7.307  1.00 12.54 ?  153 LEU   B CD2  1 
ATOM   6828 H H    . LEU   B 1 153 ? 40.778 -26.177 -11.338 1.00 13.02 ?  153 LEU   B H    1 
ATOM   6829 H HA   . LEU   B 1 153 ? 42.081 -25.870 -9.009  1.00 12.78 ?  153 LEU   B HA   1 
ATOM   6830 H HB2  . LEU   B 1 153 ? 40.500 -28.010 -9.951  1.00 13.50 ?  153 LEU   B HB2  1 
ATOM   6831 H HB3  . LEU   B 1 153 ? 41.166 -27.994 -8.513  1.00 13.50 ?  153 LEU   B HB3  1 
ATOM   6832 H HG   . LEU   B 1 153 ? 39.201 -26.113 -9.256  1.00 14.29 ?  153 LEU   B HG   1 
ATOM   6833 H HD11 . LEU   B 1 153 ? 37.642 -27.414 -8.138  1.00 15.22 ?  153 LEU   B HD11 1 
ATOM   6834 H HD12 . LEU   B 1 153 ? 38.267 -28.238 -9.343  1.00 15.22 ?  153 LEU   B HD12 1 
ATOM   6835 H HD13 . LEU   B 1 153 ? 38.755 -28.513 -7.857  1.00 15.22 ?  153 LEU   B HD13 1 
ATOM   6836 H HD21 . LEU   B 1 153 ? 38.997 -25.756 -6.945  1.00 15.08 ?  153 LEU   B HD21 1 
ATOM   6837 H HD22 . LEU   B 1 153 ? 40.191 -26.775 -6.699  1.00 15.08 ?  153 LEU   B HD22 1 
ATOM   6838 H HD23 . LEU   B 1 153 ? 40.461 -25.402 -7.452  1.00 15.08 ?  153 LEU   B HD23 1 
ATOM   6839 N N    . ALA   B 1 154 ? 44.134 -27.185 -9.300  1.00 11.32 ?  154 ALA   B N    1 
ATOM   6840 C CA   . ALA   B 1 154 ? 45.361 -27.944 -9.484  1.00 11.97 ?  154 ALA   B CA   1 
ATOM   6841 C C    . ALA   B 1 154 ? 45.420 -29.024 -8.413  1.00 12.28 ?  154 ALA   B C    1 
ATOM   6842 O O    . ALA   B 1 154 ? 45.339 -28.726 -7.212  1.00 13.58 ?  154 ALA   B O    1 
ATOM   6843 C CB   . ALA   B 1 154 ? 46.583 -27.032 -9.400  1.00 12.99 ?  154 ALA   B CB   1 
ATOM   6844 H H    . ALA   B 1 154 ? 44.154 -26.656 -8.612  1.00 13.62 ?  154 ALA   B H    1 
ATOM   6845 H HA   . ALA   B 1 154 ? 45.351 -28.368 -10.352 1.00 14.40 ?  154 ALA   B HA   1 
ATOM   6846 H HB1  . ALA   B 1 154 ? 47.383 -27.565 -9.525  1.00 15.62 ?  154 ALA   B HB1  1 
ATOM   6847 H HB2  . ALA   B 1 154 ? 46.523 -26.356 -10.094 1.00 15.62 ?  154 ALA   B HB2  1 
ATOM   6848 H HB3  . ALA   B 1 154 ? 46.604 -26.606 -8.527  1.00 15.62 ?  154 ALA   B HB3  1 
ATOM   6849 N N    . VAL   B 1 155 ? 45.542 -30.271 -8.849  1.00 12.20 ?  155 VAL   B N    1 
ATOM   6850 C CA   . VAL   B 1 155 ? 45.648 -31.417 -7.959  1.00 12.39 ?  155 VAL   B CA   1 
ATOM   6851 C C    . VAL   B 1 155 ? 46.984 -32.091 -8.244  1.00 12.74 ?  155 VAL   B C    1 
ATOM   6852 O O    . VAL   B 1 155 ? 47.213 -32.580 -9.358  1.00 14.67 ?  155 VAL   B O    1 
ATOM   6853 C CB   . VAL   B 1 155 ? 44.488 -32.407 -8.156  1.00 13.92 ?  155 VAL   B CB   1 
ATOM   6854 C CG1  . VAL   B 1 155 ? 44.663 -33.602 -7.238  1.00 14.08 ?  155 VAL   B CG1  1 
ATOM   6855 C CG2  . VAL   B 1 155 ? 43.147 -31.716 -7.909  1.00 15.03 ?  155 VAL   B CG2  1 
ATOM   6856 H H    . VAL   B 1 155 ? 45.570 -30.484 -9.683  1.00 14.67 ?  155 VAL   B H    1 
ATOM   6857 H HA   . VAL   B 1 155 ? 45.639 -31.121 -7.038  1.00 14.90 ?  155 VAL   B HA   1 
ATOM   6858 H HB   . VAL   B 1 155 ? 44.492 -32.728 -9.074  1.00 16.73 ?  155 VAL   B HB   1 
ATOM   6859 H HG11 . VAL   B 1 155 ? 43.831 -34.103 -7.205  1.00 16.92 ?  155 VAL   B HG11 1 
ATOM   6860 H HG12 . VAL   B 1 155 ? 45.372 -34.170 -7.582  1.00 16.92 ?  155 VAL   B HG12 1 
ATOM   6861 H HG13 . VAL   B 1 155 ? 44.892 -33.288 -6.349  1.00 16.92 ?  155 VAL   B HG13 1 
ATOM   6862 H HG21 . VAL   B 1 155 ? 42.434 -32.367 -7.999  1.00 18.06 ?  155 VAL   B HG21 1 
ATOM   6863 H HG22 . VAL   B 1 155 ? 43.146 -31.344 -7.014  1.00 18.06 ?  155 VAL   B HG22 1 
ATOM   6864 H HG23 . VAL   B 1 155 ? 43.032 -31.008 -8.562  1.00 18.06 ?  155 VAL   B HG23 1 
ATOM   6865 N N    . PHE   B 1 156 ? 47.855 -32.124 -7.236  1.00 13.12 ?  156 PHE   B N    1 
ATOM   6866 C CA   . PHE   B 1 156 ? 49.230 -32.587 -7.433  1.00 14.06 ?  156 PHE   B CA   1 
ATOM   6867 C C    . PHE   B 1 156 ? 49.324 -34.084 -7.725  1.00 15.01 ?  156 PHE   B C    1 
ATOM   6868 O O    . PHE   B 1 156 ? 50.051 -34.505 -8.635  1.00 16.82 ?  156 PHE   B O    1 
ATOM   6869 C CB   . PHE   B 1 156 ? 50.055 -32.231 -6.201  1.00 13.76 ?  156 PHE   B CB   1 
ATOM   6870 C CG   . PHE   B 1 156 ? 51.477 -32.695 -6.262  1.00 14.68 ?  156 PHE   B CG   1 
ATOM   6871 C CD1  . PHE   B 1 156 ? 52.365 -32.142 -7.167  1.00 16.27 ?  156 PHE   B CD1  1 
ATOM   6872 C CD2  . PHE   B 1 156 ? 51.939 -33.669 -5.395  1.00 15.42 ?  156 PHE   B CD2  1 
ATOM   6873 C CE1  . PHE   B 1 156 ? 53.686 -32.562 -7.217  1.00 17.22 ?  156 PHE   B CE1  1 
ATOM   6874 C CE2  . PHE   B 1 156 ? 53.257 -34.089 -5.438  1.00 16.37 ?  156 PHE   B CE2  1 
ATOM   6875 C CZ   . PHE   B 1 156 ? 54.127 -33.535 -6.352  1.00 16.81 ?  156 PHE   B CZ   1 
ATOM   6876 H H    . PHE   B 1 156 ? 47.671 -31.888 -6.426  1.00 15.77 ?  156 PHE   B H    1 
ATOM   6877 H HA   . PHE   B 1 156 ? 49.603 -32.113 -8.186  1.00 16.90 ?  156 PHE   B HA   1 
ATOM   6878 H HB2  . PHE   B 1 156 ? 50.060 -31.265 -6.102  1.00 16.54 ?  156 PHE   B HB2  1 
ATOM   6879 H HB3  . PHE   B 1 156 ? 49.644 -32.636 -5.420  1.00 16.54 ?  156 PHE   B HB3  1 
ATOM   6880 H HD1  . PHE   B 1 156 ? 52.069 -31.480 -7.754  1.00 19.55 ?  156 PHE   B HD1  1 
ATOM   6881 H HD2  . PHE   B 1 156 ? 51.353 -34.046 -4.780  1.00 18.53 ?  156 PHE   B HD2  1 
ATOM   6882 H HE1  . PHE   B 1 156 ? 54.273 -32.182 -7.834  1.00 20.69 ?  156 PHE   B HE1  1 
ATOM   6883 H HE2  . PHE   B 1 156 ? 53.549 -34.751 -4.854  1.00 19.67 ?  156 PHE   B HE2  1 
ATOM   6884 H HZ   . PHE   B 1 156 ? 55.013 -33.819 -6.383  1.00 20.20 ?  156 PHE   B HZ   1 
ATOM   6885 N N    . ASP   B 1 157 ? 48.645 -34.907 -6.938  1.00 15.46 ?  157 ASP   B N    1 
ATOM   6886 C CA   . ASP   B 1 157 ? 48.794 -36.355 -7.043  1.00 16.19 ?  157 ASP   B CA   1 
ATOM   6887 C C    . ASP   B 1 157 ? 47.876 -36.900 -8.132  1.00 16.53 ?  157 ASP   B C    1 
ATOM   6888 O O    . ASP   B 1 157 ? 46.652 -36.759 -8.041  1.00 16.01 ?  157 ASP   B O    1 
ATOM   6889 C CB   . ASP   B 1 157 ? 48.437 -36.977 -5.699  1.00 17.54 ?  157 ASP   B CB   1 
ATOM   6890 C CG   . ASP   B 1 157 ? 48.574 -38.488 -5.689  1.00 19.71 ?  157 ASP   B CG   1 
ATOM   6891 O OD1  . ASP   B 1 157 ? 48.919 -39.095 -6.732  1.00 20.16 ?  157 ASP   B OD1  1 
ATOM   6892 O OD2  . ASP   B 1 157 ? 48.344 -39.076 -4.612  1.00 21.91 -1 157 ASP   B OD2  1 
ATOM   6893 H H    . ASP   B 1 157 ? 48.098 -34.656 -6.329  1.00 18.58 ?  157 ASP   B H    1 
ATOM   6894 H HA   . ASP   B 1 157 ? 49.712 -36.582 -7.265  1.00 19.45 ?  157 ASP   B HA   1 
ATOM   6895 H HB2  . ASP   B 1 157 ? 49.022 -36.611 -5.021  1.00 21.08 ?  157 ASP   B HB2  1 
ATOM   6896 H HB3  . ASP   B 1 157 ? 47.514 -36.766 -5.491  1.00 21.08 ?  157 ASP   B HB3  1 
ATOM   6897 N N    A LYS   B 1 158 ? 48.468 -37.555 -9.136  0.42 17.29 ?  158 LYS   B N    1 
ATOM   6898 N N    B LYS   B 1 158 ? 48.468 -37.517 -9.162  0.58 17.41 ?  158 LYS   B N    1 
ATOM   6899 C CA   A LYS   B 1 158 ? 47.689 -38.168 -10.211 0.42 18.00 ?  158 LYS   B CA   1 
ATOM   6900 C CA   B LYS   B 1 158 ? 47.686 -38.084 -10.261 0.58 18.35 ?  158 LYS   B CA   1 
ATOM   6901 C C    A LYS   B 1 158 ? 46.629 -39.123 -9.669  0.42 17.73 ?  158 LYS   B C    1 
ATOM   6902 C C    B LYS   B 1 158 ? 46.621 -39.054 -9.754  0.58 18.16 ?  158 LYS   B C    1 
ATOM   6903 O O    A LYS   B 1 158 ? 45.515 -39.198 -10.203 0.42 17.59 ?  158 LYS   B O    1 
ATOM   6904 O O    B LYS   B 1 158 ? 45.520 -39.133 -10.313 0.58 18.19 ?  158 LYS   B O    1 
ATOM   6905 C CB   A LYS   B 1 158 ? 48.637 -38.898 -11.169 0.42 19.27 ?  158 LYS   B CB   1 
ATOM   6906 C CB   B LYS   B 1 158 ? 48.629 -38.783 -11.250 0.58 19.79 ?  158 LYS   B CB   1 
ATOM   6907 C CG   A LYS   B 1 158 ? 47.956 -39.796 -12.192 0.42 20.77 ?  158 LYS   B CG   1 
ATOM   6908 C CG   B LYS   B 1 158 ? 47.940 -39.662 -12.287 0.58 21.48 ?  158 LYS   B CG   1 
ATOM   6909 C CD   A LYS   B 1 158 ? 47.085 -39.012 -13.150 0.42 22.31 ?  158 LYS   B CD   1 
ATOM   6910 C CD   B LYS   B 1 158 ? 47.060 -38.860 -13.223 0.58 23.50 ?  158 LYS   B CD   1 
ATOM   6911 C CE   A LYS   B 1 158 ? 46.508 -39.922 -14.219 0.42 23.44 ?  158 LYS   B CE   1 
ATOM   6912 C CE   B LYS   B 1 158 ? 46.477 -39.745 -14.312 0.58 24.91 ?  158 LYS   B CE   1 
ATOM   6913 N NZ   A LYS   B 1 158 ? 45.451 -39.244 -15.018 0.42 23.70 ?  158 LYS   B NZ   1 
ATOM   6914 N NZ   B LYS   B 1 158 ? 45.414 -39.052 -15.092 0.58 25.36 ?  158 LYS   B NZ   1 
ATOM   6915 H H    A LYS   B 1 158 ? 49.320 -37.660 -9.213  0.42 20.77 ?  158 LYS   B H    1 
ATOM   6916 H H    B LYS   B 1 158 ? 49.322 -37.622 -9.244  0.58 20.92 ?  158 LYS   B H    1 
ATOM   6917 H HA   A LYS   B 1 158 ? 47.241 -37.472 -10.714 0.42 21.63 ?  158 LYS   B HA   1 
ATOM   6918 H HA   B LYS   B 1 158 ? 47.244 -37.366 -10.741 0.58 22.05 ?  158 LYS   B HA   1 
ATOM   6919 H HB2  A LYS   B 1 158 ? 49.153 -38.238 -11.664 0.42 23.15 ?  158 LYS   B HB2  1 
ATOM   6920 H HB2  B LYS   B 1 158 ? 49.135 -38.108 -11.737 0.58 23.78 ?  158 LYS   B HB2  1 
ATOM   6921 H HB3  A LYS   B 1 158 ? 49.241 -39.454 -10.651 0.42 23.15 ?  158 LYS   B HB3  1 
ATOM   6922 H HB3  B LYS   B 1 158 ? 49.245 -39.346 -10.753 0.58 23.78 ?  158 LYS   B HB3  1 
ATOM   6923 H HG2  A LYS   B 1 158 ? 48.637 -40.248 -12.715 0.42 24.95 ?  158 LYS   B HG2  1 
ATOM   6924 H HG2  B LYS   B 1 158 ? 48.619 -40.103 -12.824 0.58 25.80 ?  158 LYS   B HG2  1 
ATOM   6925 H HG3  A LYS   B 1 158 ? 47.403 -40.454 -11.742 0.42 24.95 ?  158 LYS   B HG3  1 
ATOM   6926 H HG3  B LYS   B 1 158 ? 47.394 -40.333 -11.846 0.58 25.80 ?  158 LYS   B HG3  1 
ATOM   6927 H HD2  A LYS   B 1 158 ? 46.350 -38.607 -12.663 0.42 26.79 ?  158 LYS   B HD2  1 
ATOM   6928 H HD2  B LYS   B 1 158 ? 46.326 -38.470 -12.722 0.58 28.23 ?  158 LYS   B HD2  1 
ATOM   6929 H HD3  A LYS   B 1 158 ? 47.617 -38.328 -13.587 0.42 26.79 ?  158 LYS   B HD3  1 
ATOM   6930 H HD3  B LYS   B 1 158 ? 47.588 -38.165 -13.646 0.58 28.23 ?  158 LYS   B HD3  1 
ATOM   6931 H HE2  A LYS   B 1 158 ? 47.215 -40.193 -14.824 0.42 28.16 ?  158 LYS   B HE2  1 
ATOM   6932 H HE2  B LYS   B 1 158 ? 47.182 -40.002 -14.927 0.58 29.92 ?  158 LYS   B HE2  1 
ATOM   6933 H HE3  A LYS   B 1 158 ? 46.114 -40.702 -13.797 0.42 28.16 ?  158 LYS   B HE3  1 
ATOM   6934 H HE3  B LYS   B 1 158 ? 46.086 -40.535 -13.906 0.58 29.92 ?  158 LYS   B HE3  1 
ATOM   6935 H HZ1  A LYS   B 1 158 ? 45.131 -39.799 -15.634 0.42 28.47 ?  158 LYS   B HZ1  1 
ATOM   6936 H HZ1  B LYS   B 1 158 ? 45.092 -39.594 -15.720 0.58 30.46 ?  158 LYS   B HZ1  1 
ATOM   6937 H HZ2  A LYS   B 1 158 ? 44.785 -38.987 -14.485 0.42 28.47 ?  158 LYS   B HZ2  1 
ATOM   6938 H HZ2  B LYS   B 1 158 ? 44.749 -38.810 -14.551 0.58 30.46 ?  158 LYS   B HZ2  1 
ATOM   6939 H HZ3  A LYS   B 1 158 ? 45.790 -38.527 -15.422 0.42 28.47 ?  158 LYS   B HZ3  1 
ATOM   6940 H HZ3  B LYS   B 1 158 ? 45.748 -38.324 -15.481 0.58 30.46 ?  158 LYS   B HZ3  1 
ATOM   6941 N N    A ASN   B 1 159 ? 46.960 -39.875 -8.618  0.42 18.06 ?  159 ASN   B N    1 
ATOM   6942 N N    B ASN   B 1 159 ? 46.939 -39.820 -8.710  0.58 18.45 ?  159 ASN   B N    1 
ATOM   6943 C CA   A ASN   B 1 159 ? 46.013 -40.856 -8.097  0.42 18.49 ?  159 ASN   B CA   1 
ATOM   6944 C CA   B ASN   B 1 159 ? 45.982 -40.802 -8.208  0.58 18.73 ?  159 ASN   B CA   1 
ATOM   6945 C C    A ASN   B 1 159 ? 44.818 -40.185 -7.430  0.42 17.77 ?  159 ASN   B C    1 
ATOM   6946 C C    B ASN   B 1 159 ? 44.792 -40.127 -7.526  0.58 17.86 ?  159 ASN   B C    1 
ATOM   6947 O O    A ASN   B 1 159 ? 43.701 -40.712 -7.484  0.42 17.98 ?  159 ASN   B O    1 
ATOM   6948 O O    B ASN   B 1 159 ? 43.649 -40.586 -7.663  0.58 18.09 ?  159 ASN   B O    1 
ATOM   6949 C CB   A ASN   B 1 159 ? 46.718 -41.797 -7.125  0.42 19.92 ?  159 ASN   B CB   1 
ATOM   6950 C CB   B ASN   B 1 159 ? 46.686 -41.782 -7.275  0.58 20.14 ?  159 ASN   B CB   1 
ATOM   6951 C CG   A ASN   B 1 159 ? 47.740 -42.680 -7.812  0.42 21.40 ?  159 ASN   B CG   1 
ATOM   6952 C CG   B ASN   B 1 159 ? 47.696 -42.641 -8.001  0.58 21.77 ?  159 ASN   B CG   1 
ATOM   6953 O OD1  A ASN   B 1 159 ? 47.491 -43.212 -8.897  0.42 22.41 ?  159 ASN   B OD1  1 
ATOM   6954 O OD1  B ASN   B 1 159 ? 47.452 -43.087 -9.127  0.58 22.63 ?  159 ASN   B OD1  1 
ATOM   6955 N ND2  A ASN   B 1 159 ? 48.900 -42.837 -7.185  0.42 21.78 ?  159 ASN   B ND2  1 
ATOM   6956 N ND2  B ASN   B 1 159 ? 48.843 -42.878 -7.366  0.58 22.50 ?  159 ASN   B ND2  1 
ATOM   6957 H H    A ASN   B 1 159 ? 47.703 -39.826 -8.192  0.42 21.70 ?  159 ASN   B H    1 
ATOM   6958 H H    B ASN   B 1 159 ? 47.688 -39.785 -8.289  0.58 22.17 ?  159 ASN   B H    1 
ATOM   6959 H HA   A ASN   B 1 159 ? 45.683 -41.387 -8.837  0.42 22.22 ?  159 ASN   B HA   1 
ATOM   6960 H HA   B ASN   B 1 159 ? 45.647 -41.307 -8.965  0.58 22.50 ?  159 ASN   B HA   1 
ATOM   6961 H HB2  A ASN   B 1 159 ? 47.177 -41.272 -6.452  0.42 23.93 ?  159 ASN   B HB2  1 
ATOM   6962 H HB2  B ASN   B 1 159 ? 47.153 -41.289 -6.586  0.58 24.20 ?  159 ASN   B HB2  1 
ATOM   6963 H HB3  A ASN   B 1 159 ? 46.056 -42.370 -6.709  0.42 23.93 ?  159 ASN   B HB3  1 
ATOM   6964 H HB3  B ASN   B 1 159 ? 46.024 -42.368 -6.880  0.58 24.20 ?  159 ASN   B HB3  1 
ATOM   6965 H HD21 A ASN   B 1 159 ? 49.511 -43.334 -7.533  0.42 26.16 ?  159 ASN   B HD21 1 
ATOM   6966 H HD21 B ASN   B 1 159 ? 49.451 -43.368 -7.733  0.58 27.03 ?  159 ASN   B HD21 1 
ATOM   6967 H HD22 A ASN   B 1 159 ? 49.034 -42.459 -6.426  0.42 26.16 ?  159 ASN   B HD22 1 
ATOM   6968 H HD22 B ASN   B 1 159 ? 48.974 -42.557 -6.578  0.58 27.03 ?  159 ASN   B HD22 1 
ATOM   6969 N N    . LEU   B 1 160 ? 45.025 -39.026 -6.805  1.00 17.40 ?  160 LEU   B N    1 
ATOM   6970 C CA   . LEU   B 1 160 ? 43.899 -38.292 -6.239  1.00 16.14 ?  160 LEU   B CA   1 
ATOM   6971 C C    . LEU   B 1 160 ? 43.099 -37.613 -7.337  1.00 15.40 ?  160 LEU   B C    1 
ATOM   6972 O O    . LEU   B 1 160 ? 41.860 -37.616 -7.301  1.00 15.45 ?  160 LEU   B O    1 
ATOM   6973 C CB   . LEU   B 1 160 ? 44.366 -37.272 -5.204  1.00 15.98 ?  160 LEU   B CB   1 
ATOM   6974 C CG   . LEU   B 1 160 ? 43.237 -36.362 -4.697  1.00 15.89 ?  160 LEU   B CG   1 
ATOM   6975 C CD1  . LEU   B 1 160 ? 42.097 -37.164 -4.067  1.00 16.77 ?  160 LEU   B CD1  1 
ATOM   6976 C CD2  . LEU   B 1 160 ? 43.781 -35.328 -3.717  1.00 15.94 ?  160 LEU   B CD2  1 
ATOM   6977 H H    A LEU   B 1 160 ? 45.792 -38.648 -6.706  0.42 20.91 ?  160 LEU   B H    1 
ATOM   6978 H H    B LEU   B 1 160 ? 45.799 -38.685 -6.649  0.58 20.91 ?  160 LEU   B H    1 
ATOM   6979 H HA   . LEU   B 1 160 ? 43.312 -38.921 -5.799  1.00 19.40 ?  160 LEU   B HA   1 
ATOM   6980 H HB2  . LEU   B 1 160 ? 44.734 -37.749 -4.445  1.00 19.20 ?  160 LEU   B HB2  1 
ATOM   6981 H HB3  . LEU   B 1 160 ? 45.050 -36.711 -5.604  1.00 19.20 ?  160 LEU   B HB3  1 
ATOM   6982 H HG   . LEU   B 1 160 ? 42.869 -35.871 -5.448  1.00 19.09 ?  160 LEU   B HG   1 
ATOM   6983 H HD11 . LEU   B 1 160 ? 41.464 -36.548 -3.669  1.00 20.16 ?  160 LEU   B HD11 1 
ATOM   6984 H HD12 . LEU   B 1 160 ? 41.660 -37.691 -4.755  1.00 20.16 ?  160 LEU   B HD12 1 
ATOM   6985 H HD13 . LEU   B 1 160 ? 42.463 -37.749 -3.384  1.00 20.16 ?  160 LEU   B HD13 1 
ATOM   6986 H HD21 . LEU   B 1 160 ? 43.053 -34.758 -3.426  1.00 19.16 ?  160 LEU   B HD21 1 
ATOM   6987 H HD22 . LEU   B 1 160 ? 44.170 -35.786 -2.958  1.00 19.16 ?  160 LEU   B HD22 1 
ATOM   6988 H HD23 . LEU   B 1 160 ? 44.459 -34.795 -4.166  1.00 19.16 ?  160 LEU   B HD23 1 
ATOM   6989 N N    . TYR   B 1 161 ? 43.791 -37.042 -8.330  1.00 15.64 ?  161 TYR   B N    1 
ATOM   6990 C CA   . TYR   B 1 161 ? 43.111 -36.474 -9.490  1.00 15.53 ?  161 TYR   B CA   1 
ATOM   6991 C C    . TYR   B 1 161 ? 42.165 -37.493 -10.110 1.00 15.52 ?  161 TYR   B C    1 
ATOM   6992 O O    . TYR   B 1 161 ? 40.996 -37.194 -10.375 1.00 15.51 ?  161 TYR   B O    1 
ATOM   6993 C CB   . TYR   B 1 161 ? 44.147 -35.990 -10.516 1.00 16.16 ?  161 TYR   B CB   1 
ATOM   6994 C CG   . TYR   B 1 161 ? 43.563 -35.521 -11.832 1.00 16.58 ?  161 TYR   B CG   1 
ATOM   6995 C CD1  . TYR   B 1 161 ? 43.184 -34.199 -12.008 1.00 16.42 ?  161 TYR   B CD1  1 
ATOM   6996 C CD2  . TYR   B 1 161 ? 43.387 -36.398 -12.898 1.00 17.32 ?  161 TYR   B CD2  1 
ATOM   6997 C CE1  . TYR   B 1 161 ? 42.644 -33.762 -13.197 1.00 17.74 ?  161 TYR   B CE1  1 
ATOM   6998 C CE2  . TYR   B 1 161 ? 42.846 -35.967 -14.091 1.00 18.27 ?  161 TYR   B CE2  1 
ATOM   6999 C CZ   . TYR   B 1 161 ? 42.485 -34.646 -14.237 1.00 18.28 ?  161 TYR   B CZ   1 
ATOM   7000 O OH   . TYR   B 1 161 ? 41.944 -34.214 -15.421 1.00 20.12 ?  161 TYR   B OH   1 
ATOM   7001 H H    . TYR   B 1 161 ? 44.645 -36.976 -8.361  1.00 18.79 ?  161 TYR   B H    1 
ATOM   7002 H HA   . TYR   B 1 161 ? 42.585 -35.707 -9.214  1.00 18.67 ?  161 TYR   B HA   1 
ATOM   7003 H HB2  . TYR   B 1 161 ? 44.636 -35.240 -10.139 1.00 19.42 ?  161 TYR   B HB2  1 
ATOM   7004 H HB3  . TYR   B 1 161 ? 44.758 -36.712 -10.715 1.00 19.42 ?  161 TYR   B HB3  1 
ATOM   7005 H HD1  . TYR   B 1 161 ? 43.296 -33.590 -11.315 1.00 19.74 ?  161 TYR   B HD1  1 
ATOM   7006 H HD2  . TYR   B 1 161 ? 43.626 -37.292 -12.807 1.00 20.81 ?  161 TYR   B HD2  1 
ATOM   7007 H HE1  . TYR   B 1 161 ? 42.402 -32.865 -13.298 1.00 21.32 ?  161 TYR   B HE1  1 
ATOM   7008 H HE2  . TYR   B 1 161 ? 42.729 -36.567 -14.796 1.00 21.95 ?  161 TYR   B HE2  1 
ATOM   7009 H HH   . TYR   B 1 161 ? 41.902 -34.855 -15.964 1.00 24.17 ?  161 TYR   B HH   1 
ATOM   7010 N N    . ASP   B 1 162 ? 42.658 -38.711 -10.338 1.00 15.88 ?  162 ASP   B N    1 
ATOM   7011 C CA   . ASP   B 1 162 ? 41.826 -39.742 -10.948 1.00 16.82 ?  162 ASP   B CA   1 
ATOM   7012 C C    . ASP   B 1 162 ? 40.626 -40.078 -10.069 1.00 16.36 ?  162 ASP   B C    1 
ATOM   7013 O O    . ASP   B 1 162 ? 39.519 -40.293 -10.575 1.00 16.91 ?  162 ASP   B O    1 
ATOM   7014 C CB   . ASP   B 1 162 ? 42.652 -41.004 -11.210 1.00 18.07 ?  162 ASP   B CB   1 
ATOM   7015 C CG   . ASP   B 1 162 ? 43.650 -40.843 -12.344 1.00 19.42 ?  162 ASP   B CG   1 
ATOM   7016 O OD1  . ASP   B 1 162 ? 43.516 -39.902 -13.152 1.00 19.56 ?  162 ASP   B OD1  1 
ATOM   7017 O OD2  . ASP   B 1 162 ? 44.556 -41.701 -12.440 1.00 21.13 -1 162 ASP   B OD2  1 
ATOM   7018 H H    . ASP   B 1 162 ? 43.457 -38.962 -10.150 1.00 19.09 ?  162 ASP   B H    1 
ATOM   7019 H HA   . ASP   B 1 162 ? 41.488 -39.421 -11.797 1.00 20.22 ?  162 ASP   B HA   1 
ATOM   7020 H HB2  . ASP   B 1 162 ? 43.148 -41.226 -10.410 1.00 21.71 ?  162 ASP   B HB2  1 
ATOM   7021 H HB3  . ASP   B 1 162 ? 42.053 -41.728 -11.446 1.00 21.71 ?  162 ASP   B HB3  1 
ATOM   7022 N N    . LYS   B 1 163 ? 40.826 -40.149 -8.751  1.00 15.76 ?  163 LYS   B N    1 
ATOM   7023 C CA   . LYS   B 1 163 ? 39.706 -40.429 -7.855  1.00 16.22 ?  163 LYS   B CA   1 
ATOM   7024 C C    . LYS   B 1 163 ? 38.660 -39.322 -7.913  1.00 15.18 ?  163 LYS   B C    1 
ATOM   7025 O O    . LYS   B 1 163 ? 37.450 -39.592 -7.913  1.00 16.20 ?  163 LYS   B O    1 
ATOM   7026 C CB   . LYS   B 1 163 ? 40.200 -40.602 -6.421  1.00 19.44 ?  163 LYS   B CB   1 
ATOM   7027 C CG   . LYS   B 1 163 ? 39.115 -41.118 -5.497  1.00 25.21 ?  163 LYS   B CG   1 
ATOM   7028 C CD   . LYS   B 1 163 ? 39.581 -41.274 -4.063  1.00 30.61 ?  163 LYS   B CD   1 
ATOM   7029 C CE   . LYS   B 1 163 ? 38.484 -41.916 -3.222  1.00 34.97 ?  163 LYS   B CE   1 
ATOM   7030 N NZ   . LYS   B 1 163 ? 38.616 -41.607 -1.773  1.00 37.37 ?  163 LYS   B NZ   1 
ATOM   7031 H H    . LYS   B 1 163 ? 41.585 -40.051 -8.360  1.00 18.94 ?  163 LYS   B H    1 
ATOM   7032 H HA   . LYS   B 1 163 ? 39.281 -41.256 -8.126  1.00 19.49 ?  163 LYS   B HA   1 
ATOM   7033 H HB2  . LYS   B 1 163 ? 40.932 -41.243 -6.413  1.00 23.36 ?  163 LYS   B HB2  1 
ATOM   7034 H HB3  . LYS   B 1 163 ? 40.504 -39.748 -6.082  1.00 23.36 ?  163 LYS   B HB3  1 
ATOM   7035 H HG2  . LYS   B 1 163 ? 38.371 -40.498 -5.502  1.00 30.28 ?  163 LYS   B HG2  1 
ATOM   7036 H HG3  . LYS   B 1 163 ? 38.821 -41.990 -5.811  1.00 30.28 ?  163 LYS   B HG3  1 
ATOM   7037 H HD2  . LYS   B 1 163 ? 40.364 -41.847 -4.035  1.00 36.76 ?  163 LYS   B HD2  1 
ATOM   7038 H HD3  . LYS   B 1 163 ? 39.784 -40.402 -3.692  1.00 36.76 ?  163 LYS   B HD3  1 
ATOM   7039 H HE2  . LYS   B 1 163 ? 37.618 -41.603 -3.527  1.00 41.99 ?  163 LYS   B HE2  1 
ATOM   7040 H HE3  . LYS   B 1 163 ? 38.535 -42.878 -3.326  1.00 41.99 ?  163 LYS   B HE3  1 
ATOM   7041 H HZ1  . LYS   B 1 163 ? 37.957 -41.997 -1.318  1.00 44.87 ?  163 LYS   B HZ1  1 
ATOM   7042 H HZ2  . LYS   B 1 163 ? 39.395 -41.908 -1.469  1.00 44.87 ?  163 LYS   B HZ2  1 
ATOM   7043 H HZ3  . LYS   B 1 163 ? 38.574 -40.727 -1.644  1.00 44.87 ?  163 LYS   B HZ3  1 
ATOM   7044 N N    . LEU   B 1 164 ? 39.115 -38.071 -7.969  1.00 14.14 ?  164 LEU   B N    1 
ATOM   7045 C CA   . LEU   B 1 164 ? 38.207 -36.930 -8.022  1.00 13.66 ?  164 LEU   B CA   1 
ATOM   7046 C C    . LEU   B 1 164 ? 37.417 -36.908 -9.326  1.00 13.96 ?  164 LEU   B C    1 
ATOM   7047 O O    . LEU   B 1 164 ? 36.195 -36.710 -9.320  1.00 14.94 ?  164 LEU   B O    1 
ATOM   7048 C CB   . LEU   B 1 164 ? 39.009 -35.635 -7.870  1.00 13.61 ?  164 LEU   B CB   1 
ATOM   7049 C CG   . LEU   B 1 164 ? 39.555 -35.373 -6.470  1.00 14.39 ?  164 LEU   B CG   1 
ATOM   7050 C CD1  . LEU   B 1 164 ? 40.636 -34.310 -6.530  1.00 14.50 ?  164 LEU   B CD1  1 
ATOM   7051 C CD2  . LEU   B 1 164 ? 38.461 -34.955 -5.508  1.00 16.30 ?  164 LEU   B CD2  1 
ATOM   7052 H H    . LEU   B 1 164 ? 39.950 -37.850 -7.985  1.00 16.99 ?  164 LEU   B H    1 
ATOM   7053 H HA   . LEU   B 1 164 ? 37.578 -36.988 -7.291  1.00 16.43 ?  164 LEU   B HA   1 
ATOM   7054 H HB2  . LEU   B 1 164 ? 39.765 -35.670 -8.478  1.00 16.37 ?  164 LEU   B HB2  1 
ATOM   7055 H HB3  . LEU   B 1 164 ? 38.438 -34.890 -8.105  1.00 16.37 ?  164 LEU   B HB3  1 
ATOM   7056 H HG   . LEU   B 1 164 ? 39.961 -36.184 -6.131  1.00 17.30 ?  164 LEU   B HG   1 
ATOM   7057 H HD11 . LEU   B 1 164 ? 40.972 -34.145 -5.632  1.00 17.43 ?  164 LEU   B HD11 1 
ATOM   7058 H HD12 . LEU   B 1 164 ? 41.364 -34.624 -7.095  1.00 17.43 ?  164 LEU   B HD12 1 
ATOM   7059 H HD13 . LEU   B 1 164 ? 40.265 -33.493 -6.896  1.00 17.43 ?  164 LEU   B HD13 1 
ATOM   7060 H HD21 . LEU   B 1 164 ? 38.861 -34.718 -4.657  1.00 19.58 ?  164 LEU   B HD21 1 
ATOM   7061 H HD22 . LEU   B 1 164 ? 37.992 -34.191 -5.877  1.00 19.58 ?  164 LEU   B HD22 1 
ATOM   7062 H HD23 . LEU   B 1 164 ? 37.848 -35.697 -5.391  1.00 19.58 ?  164 LEU   B HD23 1 
ATOM   7063 N N    . VAL   B 1 165 ? 38.103 -37.076 -10.457 1.00 15.41 ?  165 VAL   B N    1 
ATOM   7064 C CA   . VAL   B 1 165 ? 37.444 -37.011 -11.757 1.00 16.75 ?  165 VAL   B CA   1 
ATOM   7065 C C    . VAL   B 1 165 ? 36.537 -38.217 -11.953 1.00 18.43 ?  165 VAL   B C    1 
ATOM   7066 O O    . VAL   B 1 165 ? 35.381 -38.085 -12.375 1.00 19.15 ?  165 VAL   B O    1 
ATOM   7067 C CB   . VAL   B 1 165 ? 38.491 -36.920 -12.881 1.00 17.93 ?  165 VAL   B CB   1 
ATOM   7068 C CG1  . VAL   B 1 165 ? 37.826 -37.032 -14.235 1.00 19.09 ?  165 VAL   B CG1  1 
ATOM   7069 C CG2  . VAL   B 1 165 ? 39.287 -35.634 -12.765 1.00 18.07 ?  165 VAL   B CG2  1 
ATOM   7070 H H    . VAL   B 1 165 ? 38.945 -37.231 -10.499 1.00 18.52 ?  165 VAL   B H    1 
ATOM   7071 H HA   . VAL   B 1 165 ? 36.891 -36.214 -11.797 1.00 20.13 ?  165 VAL   B HA   1 
ATOM   7072 H HB   . VAL   B 1 165 ? 39.113 -37.659 -12.788 1.00 21.54 ?  165 VAL   B HB   1 
ATOM   7073 H HG11 . VAL   B 1 165 ? 38.438 -36.713 -14.913 1.00 22.93 ?  165 VAL   B HG11 1 
ATOM   7074 H HG12 . VAL   B 1 165 ? 37.610 -37.965 -14.402 1.00 22.93 ?  165 VAL   B HG12 1 
ATOM   7075 H HG13 . VAL   B 1 165 ? 37.018 -36.500 -14.236 1.00 22.93 ?  165 VAL   B HG13 1 
ATOM   7076 H HG21 . VAL   B 1 165 ? 39.924 -35.589 -13.496 1.00 21.71 ?  165 VAL   B HG21 1 
ATOM   7077 H HG22 . VAL   B 1 165 ? 38.678 -34.879 -12.812 1.00 21.71 ?  165 VAL   B HG22 1 
ATOM   7078 H HG23 . VAL   B 1 165 ? 39.758 -35.625 -11.916 1.00 21.71 ?  165 VAL   B HG23 1 
ATOM   7079 N N    . SER   B 1 166 ? 37.059 -39.417 -11.666 1.00 19.37 ?  166 SER   B N    1 
ATOM   7080 C CA   . SER   B 1 166 ? 36.310 -40.633 -11.955 1.00 20.48 ?  166 SER   B CA   1 
ATOM   7081 C C    . SER   B 1 166 ? 35.044 -40.725 -11.117 1.00 20.49 ?  166 SER   B C    1 
ATOM   7082 O O    . SER   B 1 166 ? 34.075 -41.351 -11.548 1.00 21.75 ?  166 SER   B O    1 
ATOM   7083 C CB   . SER   B 1 166 ? 37.184 -41.883 -11.770 1.00 21.60 ?  166 SER   B CB   1 
ATOM   7084 O OG   . SER   B 1 166 ? 37.513 -42.093 -10.408 1.00 22.07 ?  166 SER   B OG   1 
ATOM   7085 H H    . SER   B 1 166 ? 37.836 -39.543 -11.313 1.00 23.27 ?  166 SER   B H    1 
ATOM   7086 H HA   . SER   B 1 166 ? 36.046 -40.612 -12.886 1.00 24.60 ?  166 SER   B HA   1 
ATOM   7087 H HB2  . SER   B 1 166 ? 36.703 -42.656 -12.098 1.00 25.95 ?  166 SER   B HB2  1 
ATOM   7088 H HB3  . SER   B 1 166 ? 38.008 -41.771 -12.282 1.00 25.95 ?  166 SER   B HB3  1 
ATOM   7089 H HG   . SER   B 1 166 ? 37.951 -41.435 -10.116 1.00 26.52 ?  166 SER   B HG   1 
ATOM   7090 N N    . SER   B 1 167 ? 35.021 -40.106 -9.935  1.00 18.92 ?  167 SER   B N    1 
ATOM   7091 C CA   . SER   B 1 167 ? 33.860 -40.170 -9.053  1.00 18.57 ?  167 SER   B CA   1 
ATOM   7092 C C    . SER   B 1 167 ? 32.942 -38.953 -9.146  1.00 17.96 ?  167 SER   B C    1 
ATOM   7093 O O    . SER   B 1 167 ? 31.867 -38.958 -8.538  1.00 18.18 ?  167 SER   B O    1 
ATOM   7094 C CB   . SER   B 1 167 ? 34.303 -40.353 -7.596  1.00 18.75 ?  167 SER   B CB   1 
ATOM   7095 O OG   . SER   B 1 167 ? 34.975 -39.192 -7.118  1.00 18.70 ?  167 SER   B OG   1 
ATOM   7096 H H    . SER   B 1 167 ? 35.673 -39.644 -9.626  1.00 22.73 ?  167 SER   B H    1 
ATOM   7097 H HA   . SER   B 1 167 ? 33.336 -40.947 -9.301  1.00 22.32 ?  167 SER   B HA   1 
ATOM   7098 H HB2  . SER   B 1 167 ? 33.517 -40.519 -7.053  1.00 22.53 ?  167 SER   B HB2  1 
ATOM   7099 H HB3  . SER   B 1 167 ? 34.897 -41.128 -7.548  1.00 22.53 ?  167 SER   B HB3  1 
ATOM   7100 H HG   . SER   B 1 167 ? 35.670 -39.070 -7.569  1.00 22.47 ?  167 SER   B HG   1 
ATOM   7101 N N    . PHE   B 1 168 ? 33.329 -37.902 -9.872  1.00 18.03 ?  168 PHE   B N    1 
ATOM   7102 C CA   . PHE   B 1 168 ? 32.492 -36.701 -9.916  1.00 17.69 ?  168 PHE   B CA   1 
ATOM   7103 C C    . PHE   B 1 168 ? 31.173 -36.957 -10.644 1.00 15.43 ?  168 PHE   B C    1 
ATOM   7104 O O    . PHE   B 1 168 ? 30.135 -36.353 -10.308 1.00 16.09 ?  168 PHE   B O    1 
ATOM   7105 C CB   . PHE   B 1 168 ? 33.249 -35.551 -10.577 1.00 18.38 ?  168 PHE   B CB   1 
ATOM   7106 C CG   . PHE   B 1 168 ? 32.429 -34.308 -10.726 1.00 18.36 ?  168 PHE   B CG   1 
ATOM   7107 C CD1  . PHE   B 1 168 ? 32.072 -33.564 -9.609  1.00 19.51 ?  168 PHE   B CD1  1 
ATOM   7108 C CD2  . PHE   B 1 168 ? 32.006 -33.888 -11.969 1.00 17.87 ?  168 PHE   B CD2  1 
ATOM   7109 C CE1  . PHE   B 1 168 ? 31.303 -32.425 -9.726  1.00 19.67 ?  168 PHE   B CE1  1 
ATOM   7110 C CE2  . PHE   B 1 168 ? 31.250 -32.731 -12.100 1.00 18.56 ?  168 PHE   B CE2  1 
ATOM   7111 C CZ   . PHE   B 1 168 ? 30.888 -32.002 -10.973 1.00 18.75 ?  168 PHE   B CZ   1 
ATOM   7112 H H    . PHE   B 1 168 ? 34.060 -37.851 -10.330 1.00 21.66 ?  168 PHE   B H    1 
ATOM   7113 H HA   . PHE   B 1 168 ? 32.278 -36.436 -9.013  1.00 21.26 ?  168 PHE   B HA   1 
ATOM   7114 H HB2  . PHE   B 1 168 ? 34.021 -35.330 -10.033 1.00 22.08 ?  168 PHE   B HB2  1 
ATOM   7115 H HB3  . PHE   B 1 168 ? 33.533 -35.821 -11.461 1.00 22.08 ?  168 PHE   B HB3  1 
ATOM   7116 H HD1  . PHE   B 1 168 ? 32.339 -33.850 -8.767  1.00 23.44 ?  168 PHE   B HD1  1 
ATOM   7117 H HD2  . PHE   B 1 168 ? 32.243 -34.363 -12.725 1.00 21.48 ?  168 PHE   B HD2  1 
ATOM   7118 H HE1  . PHE   B 1 168 ? 31.064 -31.940 -8.968  1.00 23.63 ?  168 PHE   B HE1  1 
ATOM   7119 H HE2  . PHE   B 1 168 ? 30.964 -32.446 -12.943 1.00 22.29 ?  168 PHE   B HE2  1 
ATOM   7120 H HZ   . PHE   B 1 168 ? 30.370 -31.228 -11.060 1.00 22.52 ?  168 PHE   B HZ   1 
ATOM   7121 N N    . LEU   B 1 169 ? 31.203 -37.836 -11.644 1.00 15.47 ?  169 LEU   B N    1 
ATOM   7122 C CA   . LEU   B 1 169 ? 30.017 -38.169 -12.426 1.00 17.79 ?  169 LEU   B CA   1 
ATOM   7123 C C    . LEU   B 1 169 ? 30.010 -39.615 -12.896 1.00 20.88 ?  169 LEU   B C    1 
ATOM   7124 O O    . LEU   B 1 169 ? 29.067 -40.076 -13.546 1.00 23.29 ?  169 LEU   B O    1 
ATOM   7125 C CB   . LEU   B 1 169 ? 29.930 -37.261 -13.648 1.00 19.53 ?  169 LEU   B CB   1 
ATOM   7126 C CG   . LEU   B 1 169 ? 28.715 -36.344 -13.735 1.00 22.94 ?  169 LEU   B CG   1 
ATOM   7127 C CD1  . LEU   B 1 169 ? 28.678 -35.677 -15.095 1.00 23.78 ?  169 LEU   B CD1  1 
ATOM   7128 C CD2  . LEU   B 1 169 ? 27.426 -37.102 -13.473 1.00 23.30 ?  169 LEU   B CD2  1 
ATOM   7129 O OXT  . LEU   B 1 169 ? 30.956 -40.351 -12.648 1.00 22.31 -1 169 LEU   B OXT  1 
ATOM   7130 H H    . LEU   B 1 169 ? 31.912 -38.253 -11.904 1.00 18.60 ?  169 LEU   B H    1 
ATOM   7131 H HA   . LEU   B 1 169 ? 29.235 -38.027 -11.873 1.00 21.38 ?  169 LEU   B HA   1 
ATOM   7132 H HB2  . LEU   B 1 169 ? 30.717 -36.696 -13.668 1.00 23.46 ?  169 LEU   B HB2  1 
ATOM   7133 H HB3  . LEU   B 1 169 ? 29.918 -37.822 -14.440 1.00 23.46 ?  169 LEU   B HB3  1 
ATOM   7134 H HG   . LEU   B 1 169 ? 28.793 -35.646 -13.065 1.00 27.56 ?  169 LEU   B HG   1 
ATOM   7135 H HD11 . LEU   B 1 169 ? 27.916 -35.079 -15.133 1.00 28.56 ?  169 LEU   B HD11 1 
ATOM   7136 H HD12 . LEU   B 1 169 ? 29.500 -35.178 -15.222 1.00 28.56 ?  169 LEU   B HD12 1 
ATOM   7137 H HD13 . LEU   B 1 169 ? 28.597 -36.362 -15.777 1.00 28.56 ?  169 LEU   B HD13 1 
ATOM   7138 H HD21 . LEU   B 1 169 ? 26.687 -36.627 -13.881 1.00 27.99 ?  169 LEU   B HD21 1 
ATOM   7139 H HD22 . LEU   B 1 169 ? 27.502 -37.991 -13.858 1.00 27.99 ?  169 LEU   B HD22 1 
ATOM   7140 H HD23 . LEU   B 1 169 ? 27.291 -37.169 -12.516 1.00 27.99 ?  169 LEU   B HD23 1 
HETATM 7141 N N2   B A1A76 C 2 .   ? 14.999 -0.309  3.761   0.58 9.66  ?  201 A1A76 A N2   1 
HETATM 7142 C C3   B A1A76 C 2 .   ? 13.976 -0.026  -0.394  0.58 11.19 ?  201 A1A76 A C3   1 
HETATM 7143 C C6   B A1A76 C 2 .   ? 14.637 3.102   -1.185  0.58 14.22 ?  201 A1A76 A C6   1 
HETATM 7144 C C9   B A1A76 C 2 .   ? 15.035 0.869   3.104   0.58 9.01  ?  201 A1A76 A C9   1 
HETATM 7145 C C12  B A1A76 C 2 .   ? 15.239 2.078   3.810   0.58 9.12  ?  201 A1A76 A C12  1 
HETATM 7146 C C14  B A1A76 C 2 .   ? 15.565 4.124   4.769   0.58 9.90  ?  201 A1A76 A C14  1 
HETATM 7147 C C1   B A1A76 C 2 .   ? 15.953 -1.112  0.700   0.58 9.63  ?  201 A1A76 A C1   1 
HETATM 7148 C C10  B A1A76 C 2 .   ? 15.098 -0.301  5.115   0.58 9.85  ?  201 A1A76 A C10  1 
HETATM 7149 C C11  B A1A76 C 2 .   ? 15.334 1.933   5.212   0.58 9.48  ?  201 A1A76 A C11  1 
HETATM 7150 C C13  B A1A76 C 2 .   ? 15.387 3.484   3.557   0.58 9.71  ?  201 A1A76 A C13  1 
HETATM 7151 C C2   B A1A76 C 2 .   ? 14.585 -0.423  0.985   0.58 9.56  ?  201 A1A76 A C2   1 
HETATM 7152 C C4   B A1A76 C 2 .   ? 13.415 1.340   -0.124  0.58 11.91 ?  201 A1A76 A C4   1 
HETATM 7153 C C5   B A1A76 C 2 .   ? 13.297 2.355   -1.224  0.58 13.81 ?  201 A1A76 A C5   1 
HETATM 7154 C C7   B A1A76 C 2 .   ? 15.381 2.761   0.108   0.58 12.09 ?  201 A1A76 A C7   1 
HETATM 7155 C C8   B A1A76 C 2 .   ? 14.403 1.953   0.906   0.58 10.83 ?  201 A1A76 A C8   1 
HETATM 7156 N N1   B A1A76 C 2 .   ? 14.896 0.843   1.726   0.58 9.30  ?  201 A1A76 A N1   1 
HETATM 7157 N N3   B A1A76 C 2 .   ? 15.259 0.751   5.898   0.58 9.57  ?  201 A1A76 A N3   1 
HETATM 7158 N N4   B A1A76 C 2 .   ? 15.531 3.174   5.803   0.58 9.78  ?  201 A1A76 A N4   1 
HETATM 7159 O O1   B A1A76 C 2 .   ? 15.650 -2.321  0.029   0.58 10.39 ?  201 A1A76 A O1   1 
HETATM 7160 H H8   B A1A76 C 2 .   ? 14.726 0.014   -1.220  0.58 13.45 ?  201 A1A76 A H8   1 
HETATM 7161 H H7   B A1A76 C 2 .   ? 13.253 -0.748  -0.797  0.58 13.45 ?  201 A1A76 A H7   1 
HETATM 7162 H H11  B A1A76 C 2 .   ? 14.465 4.191   -1.248  0.58 17.09 ?  201 A1A76 A H11  1 
HETATM 7163 H H12  B A1A76 C 2 .   ? 15.241 2.861   -2.085  0.58 17.09 ?  201 A1A76 A H12  1 
HETATM 7164 H H17  B A1A76 C 2 .   ? 15.698 5.166   5.025   0.58 11.91 ?  201 A1A76 A H17  1 
HETATM 7165 H H6   B A1A76 C 2 .   ? 16.615 -0.420  0.145   0.58 11.59 ?  201 A1A76 A H6   1 
HETATM 7166 H H5   B A1A76 C 2 .   ? 16.467 -1.334  1.668   0.58 11.59 ?  201 A1A76 A H5   1 
HETATM 7167 H H15  B A1A76 C 2 .   ? 15.038 -1.242  5.682   0.58 11.85 ?  201 A1A76 A H15  1 
HETATM 7168 H H16  B A1A76 C 2 .   ? 15.351 3.994   2.613   0.58 11.68 ?  201 A1A76 A H16  1 
HETATM 7169 H H1   B A1A76 C 2 .   ? 13.869 -1.098  1.512   0.58 11.50 ?  201 A1A76 A H1   1 
HETATM 7170 H H2   B A1A76 C 2 .   ? 12.399 1.177   0.300   0.58 14.33 ?  201 A1A76 A H2   1 
HETATM 7171 H H9   B A1A76 C 2 .   ? 13.092 1.898   -2.205  0.58 16.60 ?  201 A1A76 A H9   1 
HETATM 7172 H H10  B A1A76 C 2 .   ? 12.409 3.004   -1.086  0.58 16.60 ?  201 A1A76 A H10  1 
HETATM 7173 H H14  B A1A76 C 2 .   ? 15.722 3.645   0.654   0.58 14.54 ?  201 A1A76 A H14  1 
HETATM 7174 H H13  B A1A76 C 2 .   ? 16.297 2.176   -0.077  0.58 14.54 ?  201 A1A76 A H13  1 
HETATM 7175 H H3   B A1A76 C 2 .   ? 13.869 2.593   1.661   0.58 13.03 ?  201 A1A76 A H3   1 
HETATM 7176 H H18  B A1A76 C 2 .   ? 15.651 3.341   6.788   0.58 11.76 ?  201 A1A76 A H18  1 
HETATM 7177 H H4   B A1A76 C 2 .   ? 16.461 -2.789  -0.068  0.58 12.49 ?  201 A1A76 A H4   1 
HETATM 7178 O O    . HOH   D 3 .   ? 13.640 -1.473  -6.930  1.00 32.90 ?  301 HOH   A O    1 
HETATM 7179 O O    . HOH   D 3 .   ? 24.604 1.975   -7.409  1.00 30.44 ?  302 HOH   A O    1 
HETATM 7180 O O    A HOH   D 3 .   ? 14.872 -4.657  20.407  0.42 29.50 ?  303 HOH   A O    1 
HETATM 7181 O O    B HOH   D 3 .   ? 10.386 -0.319  -1.115  0.58 17.53 ?  304 HOH   A O    1 
HETATM 7182 O O    . HOH   D 3 .   ? 34.426 -1.813  12.553  1.00 32.67 ?  305 HOH   A O    1 
HETATM 7183 O O    . HOH   D 3 .   ? 28.528 -0.290  -13.464 1.00 36.15 ?  306 HOH   A O    1 
HETATM 7184 O O    . HOH   D 3 .   ? 25.962 -1.080  -7.658  1.00 19.94 ?  307 HOH   A O    1 
HETATM 7185 O O    . HOH   D 3 .   ? 11.893 -10.922 -10.011 1.00 55.20 ?  308 HOH   A O    1 
HETATM 7186 O O    . HOH   D 3 .   ? 29.040 0.330   -9.834  1.00 20.39 ?  309 HOH   A O    1 
HETATM 7187 O O    A HOH   D 3 .   ? 4.767  3.831   0.595   0.42 21.54 ?  310 HOH   A O    1 
HETATM 7188 O O    . HOH   D 3 .   ? 11.028 1.548   12.246  1.00 21.08 ?  311 HOH   A O    1 
HETATM 7189 O O    . HOH   D 3 .   ? 22.318 5.351   18.973  1.00 44.89 ?  312 HOH   A O    1 
HETATM 7190 O O    . HOH   D 3 .   ? 15.189 -12.334 18.616  1.00 44.74 ?  313 HOH   A O    1 
HETATM 7191 O O    A HOH   D 3 .   ? 14.164 -4.664  -11.747 0.42 26.32 ?  314 HOH   A O    1 
HETATM 7192 O O    . HOH   D 3 .   ? 17.322 -18.052 15.092  1.00 27.99 ?  315 HOH   A O    1 
HETATM 7193 O O    B HOH   D 3 .   ? 14.951 -2.813  3.234   0.58 13.05 ?  316 HOH   A O    1 
HETATM 7194 O O    . HOH   D 3 .   ? 14.890 3.877   17.397  1.00 35.82 ?  317 HOH   A O    1 
HETATM 7195 O O    . HOH   D 3 .   ? 7.738  -6.397  -6.445  1.00 43.18 ?  318 HOH   A O    1 
HETATM 7196 O O    . HOH   D 3 .   ? 9.373  -10.213 19.419  1.00 44.40 ?  319 HOH   A O    1 
HETATM 7197 O O    . HOH   D 3 .   ? 3.468  -9.387  9.671   1.00 47.92 ?  320 HOH   A O    1 
HETATM 7198 O O    . HOH   D 3 .   ? 22.632 -12.026 21.924  1.00 59.33 ?  321 HOH   A O    1 
HETATM 7199 O O    . HOH   D 3 .   ? 28.313 -6.287  19.568  1.00 43.22 ?  322 HOH   A O    1 
HETATM 7200 O O    . HOH   D 3 .   ? 12.083 0.321   14.614  1.00 36.91 ?  323 HOH   A O    1 
HETATM 7201 O O    . HOH   D 3 .   ? 5.294  2.226   5.057   1.00 32.93 ?  324 HOH   A O    1 
HETATM 7202 O O    . HOH   D 3 .   ? 19.087 -22.041 6.824   1.00 30.97 ?  325 HOH   A O    1 
HETATM 7203 O O    . HOH   D 3 .   ? 42.374 10.603  5.098   1.00 19.12 ?  326 HOH   A O    1 
HETATM 7204 O O    A HOH   D 3 .   ? 17.580 -1.778  0.428   0.42 26.03 ?  327 HOH   A O    1 
HETATM 7205 O O    . HOH   D 3 .   ? 30.425 -13.332 -8.467  1.00 20.31 ?  328 HOH   A O    1 
HETATM 7206 O O    . HOH   D 3 .   ? 26.815 11.373  1.654   1.00 14.54 ?  329 HOH   A O    1 
HETATM 7207 O O    . HOH   D 3 .   ? 14.722 -13.957 16.762  1.00 24.50 ?  330 HOH   A O    1 
HETATM 7208 O O    . HOH   D 3 .   ? 31.133 -18.116 7.824   1.00 17.95 ?  331 HOH   A O    1 
HETATM 7209 O O    . HOH   D 3 .   ? 10.380 -22.187 -1.197  1.00 58.48 ?  332 HOH   A O    1 
HETATM 7210 O O    B HOH   D 3 .   ? 11.248 6.357   8.828   0.58 22.64 ?  333 HOH   A O    1 
HETATM 7211 O O    A HOH   D 3 .   ? -0.538 -8.590  2.387   0.42 35.44 ?  334 HOH   A O    1 
HETATM 7212 O O    . HOH   D 3 .   ? 44.276 7.196   6.379   1.00 25.64 ?  335 HOH   A O    1 
HETATM 7213 O O    . HOH   D 3 .   ? 37.520 2.833   10.263  1.00 26.57 ?  336 HOH   A O    1 
HETATM 7214 O O    . HOH   D 3 .   ? 24.034 -15.878 -9.187  1.00 38.51 ?  337 HOH   A O    1 
HETATM 7215 O O    . HOH   D 3 .   ? 14.486 -24.715 11.524  1.00 36.90 ?  338 HOH   A O    1 
HETATM 7216 O O    . HOH   D 3 .   ? 27.319 13.755  2.836   1.00 27.47 ?  339 HOH   A O    1 
HETATM 7217 O O    A HOH   D 3 .   ? 20.174 4.479   -7.563  0.42 33.25 ?  340 HOH   A O    1 
HETATM 7218 O O    A HOH   D 3 .   ? 0.823  -4.704  0.226   0.42 23.90 ?  341 HOH   A O    1 
HETATM 7219 O O    A HOH   D 3 .   ? 14.353 0.507   6.783   0.42 28.27 ?  342 HOH   A O    1 
HETATM 7220 O O    . HOH   D 3 .   ? 20.172 -12.737 -8.704  1.00 25.34 ?  343 HOH   A O    1 
HETATM 7221 O O    . HOH   D 3 .   ? 22.762 12.523  1.552   1.00 12.99 ?  344 HOH   A O    1 
HETATM 7222 O O    . HOH   D 3 .   ? 18.815 -19.364 13.629  1.00 28.82 ?  345 HOH   A O    1 
HETATM 7223 O O    B HOH   D 3 .   ? 15.229 6.816   7.165   0.58 18.34 ?  346 HOH   A O    1 
HETATM 7224 O O    . HOH   D 3 .   ? 21.255 10.194  14.941  1.00 33.54 ?  347 HOH   A O    1 
HETATM 7225 O O    . HOH   D 3 .   ? 19.589 -11.184 24.147  1.00 79.54 ?  348 HOH   A O    1 
HETATM 7226 O O    A HOH   D 3 .   ? 9.903  -21.415 5.728   0.42 13.91 ?  349 HOH   A O    1 
HETATM 7227 O O    . HOH   D 3 .   ? 38.261 10.327  7.087   1.00 44.38 ?  350 HOH   A O    1 
HETATM 7228 O O    . HOH   D 3 .   ? 22.359 -19.311 11.392  1.00 29.28 ?  351 HOH   A O    1 
HETATM 7229 O O    . HOH   D 3 .   ? 31.681 8.216   14.795  1.00 23.98 ?  352 HOH   A O    1 
HETATM 7230 O O    . HOH   D 3 .   ? 36.351 -5.092  -0.475  1.00 31.15 ?  353 HOH   A O    1 
HETATM 7231 O O    A HOH   D 3 .   ? 21.332 -2.455  -2.064  0.42 15.92 ?  354 HOH   A O    1 
HETATM 7232 O O    . HOH   D 3 .   ? 38.555 5.015   7.008   1.00 15.27 ?  355 HOH   A O    1 
HETATM 7233 O O    . HOH   D 3 .   ? 34.092 -1.132  -8.922  1.00 23.93 ?  356 HOH   A O    1 
HETATM 7234 O O    . HOH   D 3 .   ? 30.813 6.273   -12.262 1.00 25.61 ?  357 HOH   A O    1 
HETATM 7235 O O    . HOH   D 3 .   ? 30.614 1.932   16.726  1.00 20.31 ?  358 HOH   A O    1 
HETATM 7236 O O    . HOH   D 3 .   ? 15.683 2.142   24.501  1.00 52.93 ?  359 HOH   A O    1 
HETATM 7237 O O    . HOH   D 3 .   ? 20.804 -19.810 -5.083  1.00 27.12 ?  360 HOH   A O    1 
HETATM 7238 O O    . HOH   D 3 .   ? 43.339 7.823   2.705   1.00 28.30 ?  361 HOH   A O    1 
HETATM 7239 O O    . HOH   D 3 .   ? 14.573 -21.298 -4.302  1.00 26.86 ?  362 HOH   A O    1 
HETATM 7240 O O    . HOH   D 3 .   ? 17.205 -19.345 4.876   1.00 13.35 ?  363 HOH   A O    1 
HETATM 7241 O O    A HOH   D 3 .   ? 15.306 -8.067  -9.660  0.42 19.16 ?  364 HOH   A O    1 
HETATM 7242 O O    . HOH   D 3 .   ? 39.804 -1.020  -5.208  1.00 19.14 ?  365 HOH   A O    1 
HETATM 7243 O O    . HOH   D 3 .   ? 37.261 11.999  4.926   1.00 26.64 ?  366 HOH   A O    1 
HETATM 7244 O O    . HOH   D 3 .   ? 14.557 -0.398  -12.196 1.00 46.81 ?  367 HOH   A O    1 
HETATM 7245 O O    . HOH   D 3 .   ? 33.729 -7.137  4.344   1.00 15.06 ?  368 HOH   A O    1 
HETATM 7246 O O    . HOH   D 3 .   ? 8.097  -13.059 -1.051  1.00 26.83 ?  369 HOH   A O    1 
HETATM 7247 O O    . HOH   D 3 .   ? 17.384 -17.955 -5.056  1.00 28.21 ?  370 HOH   A O    1 
HETATM 7248 O O    . HOH   D 3 .   ? 35.919 -12.648 6.866   1.00 15.03 ?  371 HOH   A O    1 
HETATM 7249 O O    . HOH   D 3 .   ? 18.460 9.461   8.763   1.00 19.12 ?  372 HOH   A O    1 
HETATM 7250 O O    . HOH   D 3 .   ? 37.240 -2.981  9.691   1.00 47.97 ?  373 HOH   A O    1 
HETATM 7251 O O    . HOH   D 3 .   ? 30.785 3.108   8.259   1.00 11.23 ?  374 HOH   A O    1 
HETATM 7252 O O    . HOH   D 3 .   ? 31.251 -13.963 -2.415  1.00 12.29 ?  375 HOH   A O    1 
HETATM 7253 O O    B HOH   D 3 .   ? 10.987 -1.239  1.657   0.58 12.94 ?  376 HOH   A O    1 
HETATM 7254 O O    . HOH   D 3 .   ? 27.548 -10.569 14.112  1.00 15.81 ?  377 HOH   A O    1 
HETATM 7255 O O    . HOH   D 3 .   ? 24.154 -2.211  -2.228  1.00 11.10 ?  378 HOH   A O    1 
HETATM 7256 O O    . HOH   D 3 .   ? 22.026 -21.921 8.514   1.00 26.73 ?  379 HOH   A O    1 
HETATM 7257 O O    . HOH   D 3 .   ? 8.348  -21.614 4.058   1.00 58.32 ?  380 HOH   A O    1 
HETATM 7258 O O    . HOH   D 3 .   ? 32.131 -7.345  -9.736  1.00 21.27 ?  381 HOH   A O    1 
HETATM 7259 O O    . HOH   D 3 .   ? 42.509 4.281   5.321   1.00 30.36 ?  382 HOH   A O    1 
HETATM 7260 O O    B HOH   D 3 .   ? 9.260  2.128   7.607   0.58 26.09 ?  383 HOH   A O    1 
HETATM 7261 O O    . HOH   D 3 .   ? 26.990 4.092   -0.721  1.00 11.97 ?  384 HOH   A O    1 
HETATM 7262 O O    . HOH   D 3 .   ? 16.797 -22.138 1.022   1.00 28.12 ?  385 HOH   A O    1 
HETATM 7263 O O    . HOH   D 3 .   ? 43.940 8.532   -3.043  1.00 27.47 ?  386 HOH   A O    1 
HETATM 7264 O O    B HOH   D 3 .   ? 21.313 2.684   -0.072  0.58 14.47 ?  387 HOH   A O    1 
HETATM 7265 O O    A HOH   D 3 .   ? 7.041  -8.237  11.835  0.42 15.75 ?  388 HOH   A O    1 
HETATM 7266 O O    B HOH   D 3 .   ? 13.322 -3.449  -1.013  0.58 13.49 ?  389 HOH   A O    1 
HETATM 7267 O O    . HOH   D 3 .   ? 13.679 -15.390 -7.577  1.00 28.13 ?  390 HOH   A O    1 
HETATM 7268 O O    . HOH   D 3 .   ? 14.303 -23.165 7.393   1.00 18.44 ?  391 HOH   A O    1 
HETATM 7269 O O    . HOH   D 3 .   ? 15.387 -21.640 14.274  1.00 17.18 ?  392 HOH   A O    1 
HETATM 7270 O O    A HOH   D 3 .   ? 6.554  -5.682  11.163  0.42 14.80 ?  393 HOH   A O    1 
HETATM 7271 O O    . HOH   D 3 .   ? 13.922 -4.907  17.380  1.00 27.18 ?  394 HOH   A O    1 
HETATM 7272 O O    A HOH   D 3 .   ? -0.392 -3.185  3.081   0.42 28.01 ?  395 HOH   A O    1 
HETATM 7273 O O    . HOH   D 3 .   ? 24.280 -7.750  14.439  1.00 14.82 ?  396 HOH   A O    1 
HETATM 7274 O O    B HOH   D 3 .   ? 7.876  3.655   1.362   0.58 21.91 ?  397 HOH   A O    1 
HETATM 7275 O O    . HOH   D 3 .   ? 23.467 11.401  3.993   1.00 11.30 ?  398 HOH   A O    1 
HETATM 7276 O O    . HOH   D 3 .   ? 26.941 -3.127  19.568  1.00 38.96 ?  399 HOH   A O    1 
HETATM 7277 O O    . HOH   D 3 .   ? 15.411 11.966  7.692   1.00 31.20 ?  400 HOH   A O    1 
HETATM 7278 O O    . HOH   D 3 .   ? 27.961 0.764   -7.275  1.00 13.95 ?  401 HOH   A O    1 
HETATM 7279 O O    . HOH   D 3 .   ? 27.152 2.418   18.698  1.00 31.45 ?  402 HOH   A O    1 
HETATM 7280 O O    . HOH   D 3 .   ? 32.886 -9.223  6.011   1.00 20.26 ?  403 HOH   A O    1 
HETATM 7281 O O    B HOH   D 3 .   ? 16.277 -8.259  -7.342  0.58 33.35 ?  404 HOH   A O    1 
HETATM 7282 O O    . HOH   D 3 .   ? 20.705 -20.029 2.817   1.00 16.76 ?  405 HOH   A O    1 
HETATM 7283 O O    A HOH   D 3 .   ? 18.662 -2.535  -16.351 0.42 26.28 ?  406 HOH   A O    1 
HETATM 7284 O O    A HOH   D 3 .   ? 21.424 3.098   -0.365  0.42 8.23  ?  407 HOH   A O    1 
HETATM 7285 O O    . HOH   D 3 .   ? 37.583 -1.990  5.827   1.00 25.92 ?  408 HOH   A O    1 
HETATM 7286 O O    . HOH   D 3 .   ? 24.851 -17.568 12.702  1.00 22.58 ?  409 HOH   A O    1 
HETATM 7287 O O    A HOH   D 3 .   ? 15.881 -1.009  5.255   0.42 34.97 ?  410 HOH   A O    1 
HETATM 7288 O O    . HOH   D 3 .   ? 38.093 -1.276  -1.920  1.00 17.75 ?  411 HOH   A O    1 
HETATM 7289 O O    . HOH   D 3 .   ? 24.036 3.991   -4.914  1.00 32.46 ?  412 HOH   A O    1 
HETATM 7290 O O    . HOH   D 3 .   ? 24.447 3.541   -1.855  1.00 15.47 ?  413 HOH   A O    1 
HETATM 7291 O O    A HOH   D 3 .   ? 14.722 -3.722  3.083   0.42 18.03 ?  414 HOH   A O    1 
HETATM 7292 O O    . HOH   D 3 .   ? 10.586 -13.897 -1.852  1.00 18.47 ?  415 HOH   A O    1 
HETATM 7293 O O    . HOH   D 3 .   ? 27.719 -6.395  -14.074 1.00 31.35 ?  416 HOH   A O    1 
HETATM 7294 O O    . HOH   D 3 .   ? 41.077 -8.332  -6.750  1.00 35.13 ?  417 HOH   A O    1 
HETATM 7295 O O    . HOH   D 3 .   ? 30.437 -12.886 13.565  1.00 18.31 ?  418 HOH   A O    1 
HETATM 7296 O O    . HOH   D 3 .   ? 16.266 16.737  8.727   1.00 33.65 ?  419 HOH   A O    1 
HETATM 7297 O O    A HOH   D 3 .   ? 19.041 -0.732  -1.640  0.42 17.61 ?  420 HOH   A O    1 
HETATM 7298 O O    A HOH   D 3 .   ? 9.104  -12.191 17.178  0.42 33.92 ?  421 HOH   A O    1 
HETATM 7299 O O    . HOH   D 3 .   ? 41.667 1.472   4.979   1.00 37.97 ?  422 HOH   A O    1 
HETATM 7300 O O    . HOH   D 3 .   ? 11.833 -10.760 17.063  1.00 24.31 ?  423 HOH   A O    1 
HETATM 7301 O O    . HOH   D 3 .   ? 22.675 8.178   18.390  1.00 44.80 ?  424 HOH   A O    1 
HETATM 7302 O O    . HOH   D 3 .   ? 32.699 -10.649 3.225   1.00 30.74 ?  425 HOH   A O    1 
HETATM 7303 O O    . HOH   D 3 .   ? 35.295 -5.258  -3.050  1.00 17.96 ?  426 HOH   A O    1 
HETATM 7304 O O    . HOH   D 3 .   ? 32.937 -4.549  -9.874  1.00 25.93 ?  427 HOH   A O    1 
HETATM 7305 O O    . HOH   D 3 .   ? 30.169 -10.057 13.107  1.00 21.45 ?  428 HOH   A O    1 
HETATM 7306 O O    . HOH   D 3 .   ? 36.780 -4.934  5.429   1.00 24.26 ?  429 HOH   A O    1 
HETATM 7307 O O    . HOH   D 3 .   ? 24.100 -20.311 -1.290  1.00 15.49 ?  430 HOH   A O    1 
HETATM 7308 O O    . HOH   D 3 .   ? 16.035 6.955   2.703   1.00 14.25 ?  431 HOH   A O    1 
HETATM 7309 O O    . HOH   D 3 .   ? 28.750 -10.556 -14.110 1.00 40.53 ?  432 HOH   A O    1 
HETATM 7310 O O    A HOH   D 3 .   ? -1.342 -5.036  7.627   0.42 21.48 ?  433 HOH   A O    1 
HETATM 7311 O O    . HOH   D 3 .   ? 6.714  -3.582  12.928  1.00 34.27 ?  434 HOH   A O    1 
HETATM 7312 O O    . HOH   D 3 .   ? 16.270 -14.178 20.258  1.00 46.58 ?  435 HOH   A O    1 
HETATM 7313 O O    . HOH   D 3 .   ? 37.914 -8.882  -3.507  1.00 21.96 ?  436 HOH   A O    1 
HETATM 7314 O O    A HOH   D 3 .   ? 11.148 -0.454  1.917   0.42 19.86 ?  437 HOH   A O    1 
HETATM 7315 O O    A HOH   D 3 .   ? 18.941 1.971   -0.767  0.42 12.21 ?  438 HOH   A O    1 
HETATM 7316 O O    . HOH   D 3 .   ? 21.915 -14.137 -8.206  1.00 52.30 ?  439 HOH   A O    1 
HETATM 7317 O O    . HOH   D 3 .   ? 23.564 -7.982  17.069  1.00 20.08 ?  440 HOH   A O    1 
HETATM 7318 O O    . HOH   D 3 .   ? 29.915 -2.130  -12.820 1.00 52.83 ?  441 HOH   A O    1 
HETATM 7319 O O    . HOH   D 3 .   ? 18.484 -15.988 16.234  1.00 35.68 ?  442 HOH   A O    1 
HETATM 7320 O O    . HOH   D 3 .   ? 23.509 -20.986 1.350   1.00 17.07 ?  443 HOH   A O    1 
HETATM 7321 O O    . HOH   D 3 .   ? 20.592 -17.751 24.815  1.00 64.42 ?  444 HOH   A O    1 
HETATM 7322 O O    . HOH   D 3 .   ? 45.173 -0.473  2.991   1.00 39.75 ?  445 HOH   A O    1 
HETATM 7323 O O    B HOH   D 3 .   ? 21.368 -2.084  -3.013  0.58 16.47 ?  446 HOH   A O    1 
HETATM 7324 O O    . HOH   D 3 .   ? 34.547 -8.137  -0.400  1.00 29.00 ?  447 HOH   A O    1 
HETATM 7325 O O    A HOH   D 3 .   ? 9.496  -16.405 -1.992  0.42 39.16 ?  448 HOH   A O    1 
HETATM 7326 O O    B HOH   D 3 .   ? 4.580  4.237   0.986   0.58 37.57 ?  449 HOH   A O    1 
HETATM 7327 O O    . HOH   D 3 .   ? 30.597 14.779  2.761   1.00 18.31 ?  450 HOH   A O    1 
HETATM 7328 O O    . HOH   D 3 .   ? 23.306 7.678   -3.419  1.00 32.49 ?  451 HOH   A O    1 
HETATM 7329 O O    . HOH   D 3 .   ? 31.462 -12.821 0.036   1.00 18.88 ?  452 HOH   A O    1 
HETATM 7330 O O    A HOH   D 3 .   ? 16.334 2.880   -1.458  0.42 27.45 ?  453 HOH   A O    1 
HETATM 7331 O O    . HOH   D 3 .   ? 21.463 -9.126  21.323  1.00 52.13 ?  454 HOH   A O    1 
HETATM 7332 O O    . HOH   D 3 .   ? 16.389 -7.122  -11.891 1.00 51.06 ?  455 HOH   A O    1 
HETATM 7333 O O    . HOH   D 3 .   ? 21.653 -14.817 17.895  1.00 50.88 ?  456 HOH   A O    1 
HETATM 7334 O O    . HOH   D 3 .   ? 18.512 4.951   -14.995 1.00 63.63 ?  457 HOH   A O    1 
HETATM 7335 O O    . HOH   D 3 .   ? 29.919 -15.987 10.749  1.00 32.72 ?  458 HOH   A O    1 
HETATM 7336 O O    A HOH   D 3 .   ? 14.108 -0.407  3.446   0.42 35.60 ?  459 HOH   A O    1 
HETATM 7337 O O    B HOH   D 3 .   ? 19.039 -0.310  -3.059  0.58 29.94 ?  460 HOH   A O    1 
HETATM 7338 O O    . HOH   D 3 .   ? 20.097 -17.496 -4.968  1.00 24.78 ?  461 HOH   A O    1 
HETATM 7339 O O    . HOH   D 3 .   ? 27.781 7.017   -6.595  1.00 37.18 ?  462 HOH   A O    1 
HETATM 7340 O O    . HOH   D 3 .   ? 25.533 8.395   -4.862  1.00 23.94 ?  463 HOH   A O    1 
HETATM 7341 O O    . HOH   D 3 .   ? 32.407 -16.000 10.907  1.00 31.29 ?  464 HOH   A O    1 
HETATM 7342 O O    . HOH   D 3 .   ? 14.116 -10.291 -10.885 1.00 36.71 ?  465 HOH   A O    1 
HETATM 7343 O O    . HOH   D 3 .   ? 24.897 5.581   20.654  1.00 59.62 ?  466 HOH   A O    1 
HETATM 7344 O O    . HOH   D 3 .   ? 24.680 14.578  7.721   1.00 31.49 ?  467 HOH   A O    1 
HETATM 7345 O O    . HOH   D 3 .   ? 23.358 -22.368 -3.262  1.00 35.33 ?  468 HOH   A O    1 
HETATM 7346 O O    B HOH   D 3 .   ? 12.634 -3.409  1.660   0.58 12.07 ?  469 HOH   A O    1 
HETATM 7347 O O    . HOH   D 3 .   ? 12.013 -13.449 16.334  1.00 50.58 ?  470 HOH   A O    1 
HETATM 7348 O O    . HOH   D 3 .   ? 26.980 11.594  -1.189  1.00 30.07 ?  471 HOH   A O    1 
HETATM 7349 O O    . HOH   D 3 .   ? 18.779 10.912  11.083  1.00 29.43 ?  472 HOH   A O    1 
HETATM 7350 O O    B HOH   D 3 .   ? 18.300 1.994   -1.428  0.58 11.31 ?  473 HOH   A O    1 
HETATM 7351 O O    B HOH   D 3 .   ? 21.567 10.431  -3.958  0.58 17.69 ?  474 HOH   A O    1 
HETATM 7352 O O    . HOH   D 3 .   ? 39.853 -7.110  -3.547  1.00 39.67 ?  475 HOH   A O    1 
HETATM 7353 O O    . HOH   D 3 .   ? 23.479 13.696  5.498   1.00 18.21 ?  476 HOH   A O    1 
HETATM 7354 O O    . HOH   D 3 .   ? 16.031 -21.635 3.725   1.00 20.58 ?  477 HOH   A O    1 
HETATM 7355 O O    . HOH   D 3 .   ? 27.578 -11.431 16.531  1.00 36.62 ?  478 HOH   A O    1 
HETATM 7356 O O    . HOH   D 3 .   ? 26.015 10.901  -3.594  1.00 22.32 ?  479 HOH   A O    1 
HETATM 7357 O O    . HOH   D 3 .   ? 11.265 -15.183 -6.230  1.00 34.96 ?  480 HOH   A O    1 
HETATM 7358 O O    . HOH   D 3 .   ? 18.323 -16.367 -8.887  1.00 45.07 ?  481 HOH   A O    1 
HETATM 7359 O O    . HOH   D 3 .   ? 12.272 1.539   17.247  1.00 39.61 ?  482 HOH   A O    1 
HETATM 7360 O O    B HOH   D 3 .   ? 11.833 8.541   7.477   0.58 23.71 ?  483 HOH   A O    1 
HETATM 7361 O O    . HOH   D 3 .   ? 35.135 7.523   12.266  1.00 49.70 ?  484 HOH   A O    1 
HETATM 7362 O O    A HOH   D 3 .   ? 22.038 5.207   -5.852  0.42 28.70 ?  485 HOH   A O    1 
HETATM 7363 O O    A HOH   D 3 .   ? 23.224 11.764  -4.138  0.42 17.34 ?  486 HOH   A O    1 
HETATM 7364 O O    . HOH   D 3 .   ? 28.786 9.016   17.521  1.00 37.08 ?  487 HOH   A O    1 
HETATM 7365 O O    B HOH   D 3 .   ? 16.019 8.433   9.363   0.58 26.32 ?  488 HOH   A O    1 
HETATM 7366 O O    . HOH   D 3 .   ? 16.931 -20.555 16.243  1.00 29.14 ?  489 HOH   A O    1 
HETATM 7367 O O    . HOH   D 3 .   ? 28.820 -4.895  -12.295 1.00 39.71 ?  490 HOH   A O    1 
HETATM 7368 O O    . HOH   D 3 .   ? 15.803 -17.393 -6.994  1.00 33.97 ?  491 HOH   A O    1 
HETATM 7369 O O    . HOH   D 3 .   ? 17.386 -18.791 19.809  1.00 46.07 ?  492 HOH   A O    1 
HETATM 7370 O O    . HOH   D 3 .   ? 30.882 0.694   19.149  1.00 39.29 ?  493 HOH   A O    1 
HETATM 7371 O O    . HOH   D 3 .   ? 41.068 -3.994  -0.308  1.00 35.72 ?  494 HOH   A O    1 
HETATM 7372 O O    . HOH   D 3 .   ? 44.439 10.492  -1.648  1.00 34.83 ?  495 HOH   A O    1 
HETATM 7373 O O    . HOH   D 3 .   ? 23.257 -12.850 19.266  1.00 49.84 ?  496 HOH   A O    1 
HETATM 7374 O O    . HOH   D 3 .   ? 39.225 2.427   7.288   1.00 31.05 ?  497 HOH   A O    1 
HETATM 7375 O O    . HOH   D 3 .   ? 20.719 -16.009 -7.450  1.00 30.50 ?  498 HOH   A O    1 
HETATM 7376 O O    . HOH   D 3 .   ? 41.688 9.465   -3.915  1.00 30.03 ?  499 HOH   A O    1 
HETATM 7377 O O    . HOH   D 3 .   ? 28.955 -8.102  -15.182 1.00 53.36 ?  500 HOH   A O    1 
HETATM 7378 O O    . HOH   D 3 .   ? 31.688 -0.628  -10.496 1.00 24.16 ?  501 HOH   A O    1 
HETATM 7379 O O    . HOH   D 3 .   ? 16.353 -23.432 5.795   1.00 25.87 ?  502 HOH   A O    1 
HETATM 7380 O O    . HOH   D 3 .   ? 14.020 -25.348 8.900   1.00 37.83 ?  503 HOH   A O    1 
HETATM 7381 O O    . HOH   D 3 .   ? 18.652 -23.273 1.954   1.00 42.17 ?  504 HOH   A O    1 
HETATM 7382 O O    . HOH   D 3 .   ? 20.244 -22.358 4.165   1.00 26.26 ?  505 HOH   A O    1 
HETATM 7383 O O    . HOH   D 3 .   ? 40.608 -0.240  -7.810  1.00 31.28 ?  506 HOH   A O    1 
HETATM 7384 O O    . HOH   D 3 .   ? 30.766 5.823   -14.771 1.00 35.41 ?  507 HOH   A O    1 
HETATM 7385 O O    . HOH   D 3 .   ? 23.444 -23.816 1.654   1.00 29.98 ?  508 HOH   A O    1 
HETATM 7386 O O    B HOH   D 3 .   ? 14.805 7.901   4.978   0.58 17.64 ?  509 HOH   A O    1 
HETATM 7387 O O    . HOH   D 3 .   ? 39.562 -0.099  6.584   1.00 31.40 ?  510 HOH   A O    1 
HETATM 7388 O O    . HOH   D 3 .   ? 30.838 -5.867  -11.970 1.00 51.14 ?  511 HOH   A O    1 
HETATM 7389 O O    . HOH   D 3 .   ? 37.515 -6.650  7.527   1.00 21.95 ?  512 HOH   A O    1 
HETATM 7390 O O    B HOH   D 3 .   ? 8.932  4.947   7.884   0.58 27.58 ?  513 HOH   A O    1 
HETATM 7391 O O    . HOH   D 3 .   ? 28.998 14.477  0.860   1.00 47.80 ?  514 HOH   A O    1 
HETATM 7392 O O    . HOH   D 3 .   ? 37.966 14.031  6.678   1.00 34.09 ?  515 HOH   A O    1 
HETATM 7393 O O    A HOH   D 3 .   ? 8.336  -3.159  -5.687  0.42 33.53 ?  516 HOH   A O    1 
HETATM 7394 O O    . HOH   D 3 .   ? 36.637 -6.428  10.222  1.00 42.51 ?  517 HOH   A O    1 
HETATM 7395 O O    . HOH   D 3 .   ? 22.191 -24.081 4.514   1.00 25.36 ?  518 HOH   A O    1 
HETATM 7396 O O    B HOH   D 3 .   ? 7.484  5.882   5.518   0.58 28.08 ?  519 HOH   A O    1 
HETATM 7397 O O    . HOH   D 3 .   ? 17.468 -7.288  -14.165 1.00 46.50 ?  520 HOH   A O    1 
HETATM 7398 O O    B HOH   D 3 .   ? 5.694  6.791   1.534   0.58 34.55 ?  521 HOH   A O    1 
HETATM 7399 O O    A HOH   D 3 .   ? 14.915 8.585   4.868   0.42 23.04 ?  522 HOH   A O    1 
HETATM 7400 O O    . HOH   D 3 .   ? 24.180 9.239   -7.180  1.00 39.71 ?  523 HOH   A O    1 
HETATM 7401 O O    . HOH   D 3 .   ? 16.239 -21.186 18.790  1.00 44.31 ?  524 HOH   A O    1 
HETATM 7402 O O    . HOH   D 3 .   ? 15.991 -12.425 27.446  1.00 47.57 ?  525 HOH   A O    1 
HETATM 7403 O O    B HOH   D 3 .   ? 8.197  7.311   2.295   0.58 24.78 ?  526 HOH   A O    1 
HETATM 7404 O O    . HOH   D 3 .   ? 14.694 -22.736 19.858  1.00 34.58 ?  527 HOH   A O    1 
HETATM 7405 O O    . HOH   E 3 .   ? 30.009 -22.428 5.537   1.00 18.69 ?  201 HOH   B O    1 
HETATM 7406 O O    . HOH   E 3 .   ? 27.803 -29.133 -1.846  1.00 35.54 ?  202 HOH   B O    1 
HETATM 7407 O O    . HOH   E 3 .   ? 41.738 -36.000 -17.201 1.00 32.50 ?  203 HOH   B O    1 
HETATM 7408 O O    . HOH   E 3 .   ? 27.896 -41.688 -15.136 1.00 38.10 ?  204 HOH   B O    1 
HETATM 7409 O O    . HOH   E 3 .   ? 59.285 -18.674 6.856   1.00 33.84 ?  205 HOH   B O    1 
HETATM 7410 O O    . HOH   E 3 .   ? 49.490 -22.762 -19.724 1.00 46.24 ?  206 HOH   B O    1 
HETATM 7411 O O    . HOH   E 3 .   ? 30.105 -26.302 4.130   1.00 26.12 ?  207 HOH   B O    1 
HETATM 7412 O O    . HOH   E 3 .   ? 47.552 -7.502  -3.927  1.00 40.71 ?  208 HOH   B O    1 
HETATM 7413 O O    . HOH   E 3 .   ? 41.497 -7.880  5.463   1.00 37.14 ?  209 HOH   B O    1 
HETATM 7414 O O    . HOH   E 3 .   ? 38.085 -39.464 -0.271  1.00 43.16 ?  210 HOH   B O    1 
HETATM 7415 O O    . HOH   E 3 .   ? 54.635 -9.439  -8.724  1.00 18.84 ?  211 HOH   B O    1 
HETATM 7416 O O    . HOH   E 3 .   ? 48.192 -7.031  15.499  1.00 32.00 ?  212 HOH   B O    1 
HETATM 7417 O O    . HOH   E 3 .   ? 44.710 -7.241  2.062   1.00 36.02 ?  213 HOH   B O    1 
HETATM 7418 O O    . HOH   E 3 .   ? 30.273 -41.013 -8.095  1.00 16.09 ?  214 HOH   B O    1 
HETATM 7419 O O    . HOH   E 3 .   ? 56.874 -30.778 -7.824  1.00 36.31 ?  215 HOH   B O    1 
HETATM 7420 O O    . HOH   E 3 .   ? 58.405 -12.919 8.415   1.00 27.75 ?  216 HOH   B O    1 
HETATM 7421 O O    . HOH   E 3 .   ? 45.032 -43.521 -10.569 1.00 26.52 ?  217 HOH   B O    1 
HETATM 7422 O O    . HOH   E 3 .   ? 34.638 -36.442 -7.175  1.00 17.22 ?  218 HOH   B O    1 
HETATM 7423 O O    . HOH   E 3 .   ? 35.042 -24.680 13.838  1.00 33.40 ?  219 HOH   B O    1 
HETATM 7424 O O    . HOH   E 3 .   ? 50.279 -3.476  7.067   1.00 30.00 ?  220 HOH   B O    1 
HETATM 7425 O O    . HOH   E 3 .   ? 29.842 -34.075 -0.333  1.00 33.60 ?  221 HOH   B O    1 
HETATM 7426 O O    . HOH   E 3 .   ? 26.643 -19.360 -1.732  1.00 13.09 ?  222 HOH   B O    1 
HETATM 7427 O O    . HOH   E 3 .   ? 56.524 -19.799 7.232   1.00 28.41 ?  223 HOH   B O    1 
HETATM 7428 O O    . HOH   E 3 .   ? 53.088 -13.382 -20.370 1.00 32.94 ?  224 HOH   B O    1 
HETATM 7429 O O    . HOH   E 3 .   ? 31.041 -28.749 4.372   1.00 26.81 ?  225 HOH   B O    1 
HETATM 7430 O O    . HOH   E 3 .   ? 57.560 -16.310 -12.205 1.00 18.20 ?  226 HOH   B O    1 
HETATM 7431 O O    . HOH   E 3 .   ? 57.881 -24.537 5.087   1.00 38.43 ?  227 HOH   B O    1 
HETATM 7432 O O    . HOH   E 3 .   ? 32.350 -9.283  -6.489  1.00 21.17 ?  228 HOH   B O    1 
HETATM 7433 O O    . HOH   E 3 .   ? 41.569 -39.188 -14.888 1.00 21.56 ?  229 HOH   B O    1 
HETATM 7434 O O    . HOH   E 3 .   ? 50.824 -6.149  0.224   1.00 25.68 ?  230 HOH   B O    1 
HETATM 7435 O O    . HOH   E 3 .   ? 46.509 -1.614  13.184  1.00 26.35 ?  231 HOH   B O    1 
HETATM 7436 O O    . HOH   E 3 .   ? 55.584 -16.570 -14.298 1.00 34.03 ?  232 HOH   B O    1 
HETATM 7437 O O    . HOH   E 3 .   ? 28.600 -19.670 -13.125 1.00 23.24 ?  233 HOH   B O    1 
HETATM 7438 O O    . HOH   E 3 .   ? 43.171 -43.276 -8.205  1.00 27.69 ?  234 HOH   B O    1 
HETATM 7439 O O    . HOH   E 3 .   ? 51.788 -6.545  4.399   1.00 18.88 ?  235 HOH   B O    1 
HETATM 7440 O O    . HOH   E 3 .   ? 39.449 -10.827 6.081   1.00 23.53 ?  236 HOH   B O    1 
HETATM 7441 O O    . HOH   E 3 .   ? 35.297 -8.046  -2.952  1.00 17.08 ?  237 HOH   B O    1 
HETATM 7442 O O    . HOH   E 3 .   ? 40.693 -16.095 14.094  1.00 22.52 ?  238 HOH   B O    1 
HETATM 7443 O O    . HOH   E 3 .   ? 38.621 -11.108 -2.255  1.00 18.22 ?  239 HOH   B O    1 
HETATM 7444 O O    . HOH   E 3 .   ? 48.673 -36.547 -15.500 1.00 37.23 ?  240 HOH   B O    1 
HETATM 7445 O O    . HOH   E 3 .   ? 44.639 -27.764 -0.629  1.00 20.95 ?  241 HOH   B O    1 
HETATM 7446 O O    . HOH   E 3 .   ? 41.558 -9.646  13.067  1.00 20.23 ?  242 HOH   B O    1 
HETATM 7447 O O    . HOH   E 3 .   ? 39.721 -11.203 0.316   1.00 15.24 ?  243 HOH   B O    1 
HETATM 7448 O O    . HOH   E 3 .   ? 50.905 -13.023 -0.456  1.00 11.03 ?  244 HOH   B O    1 
HETATM 7449 O O    . HOH   E 3 .   ? 45.249 -35.014 6.804   1.00 39.45 ?  245 HOH   B O    1 
HETATM 7450 O O    . HOH   E 3 .   ? 25.517 -25.944 -1.229  1.00 31.32 ?  246 HOH   B O    1 
HETATM 7451 O O    . HOH   E 3 .   ? 42.022 -23.559 9.316   1.00 17.01 ?  247 HOH   B O    1 
HETATM 7452 O O    . HOH   E 3 .   ? 32.867 -43.825 -11.345 1.00 20.62 ?  248 HOH   B O    1 
HETATM 7453 O O    . HOH   E 3 .   ? 42.728 -25.410 2.698   1.00 14.47 ?  249 HOH   B O    1 
HETATM 7454 O O    . HOH   E 3 .   ? 51.081 -39.991 -8.204  1.00 31.30 ?  250 HOH   B O    1 
HETATM 7455 O O    . HOH   E 3 .   ? 57.759 -24.446 -3.781  1.00 21.55 ?  251 HOH   B O    1 
HETATM 7456 O O    . HOH   E 3 .   ? 33.703 -17.020 8.132   1.00 17.81 ?  252 HOH   B O    1 
HETATM 7457 O O    . HOH   E 3 .   ? 40.509 -12.806 -11.500 1.00 14.05 ?  253 HOH   B O    1 
HETATM 7458 O O    . HOH   E 3 .   ? 58.333 -10.625 -4.046  1.00 19.04 ?  254 HOH   B O    1 
HETATM 7459 O O    . HOH   E 3 .   ? 51.720 -13.890 10.999  1.00 24.95 ?  255 HOH   B O    1 
HETATM 7460 O O    . HOH   E 3 .   ? 37.227 -19.696 -18.074 1.00 40.41 ?  256 HOH   B O    1 
HETATM 7461 O O    . HOH   E 3 .   ? 42.801 -22.901 3.897   1.00 11.00 ?  257 HOH   B O    1 
HETATM 7462 O O    . HOH   E 3 .   ? 36.112 -43.383 -8.388  1.00 36.74 ?  258 HOH   B O    1 
HETATM 7463 O O    . HOH   E 3 .   ? 28.576 -30.872 -14.802 1.00 29.99 ?  259 HOH   B O    1 
HETATM 7464 O O    . HOH   E 3 .   ? 57.664 -9.286  1.430   1.00 18.31 ?  260 HOH   B O    1 
HETATM 7465 O O    . HOH   E 3 .   ? 34.421 -18.511 11.487  1.00 25.42 ?  261 HOH   B O    1 
HETATM 7466 O O    . HOH   E 3 .   ? 31.011 -15.740 2.696   1.00 12.41 ?  262 HOH   B O    1 
HETATM 7467 O O    . HOH   E 3 .   ? 29.826 -25.224 -10.742 1.00 16.14 ?  263 HOH   B O    1 
HETATM 7468 O O    . HOH   E 3 .   ? 57.247 -26.762 -7.615  1.00 38.70 ?  264 HOH   B O    1 
HETATM 7469 O O    . HOH   E 3 .   ? 43.251 -32.389 -17.084 1.00 22.65 ?  265 HOH   B O    1 
HETATM 7470 O O    . HOH   E 3 .   ? 49.913 -0.543  10.156  1.00 27.11 ?  266 HOH   B O    1 
HETATM 7471 O O    . HOH   E 3 .   ? 51.749 -5.851  -7.946  1.00 42.22 ?  267 HOH   B O    1 
HETATM 7472 O O    . HOH   E 3 .   ? 28.342 -34.324 -9.344  1.00 20.16 ?  268 HOH   B O    1 
HETATM 7473 O O    . HOH   E 3 .   ? 48.162 -22.804 5.856   1.00 15.47 ?  269 HOH   B O    1 
HETATM 7474 O O    . HOH   E 3 .   ? 31.904 -17.893 -14.486 1.00 27.71 ?  270 HOH   B O    1 
HETATM 7475 O O    . HOH   E 3 .   ? 34.647 -12.841 2.650   1.00 21.23 ?  271 HOH   B O    1 
HETATM 7476 O O    . HOH   E 3 .   ? 35.038 -33.338 -19.128 1.00 29.96 ?  272 HOH   B O    1 
HETATM 7477 O O    . HOH   E 3 .   ? 49.447 -28.773 -6.891  1.00 15.11 ?  273 HOH   B O    1 
HETATM 7478 O O    . HOH   E 3 .   ? 27.216 -31.817 -9.936  1.00 21.18 ?  274 HOH   B O    1 
HETATM 7479 O O    . HOH   E 3 .   ? 46.745 -31.320 -4.773  1.00 18.60 ?  275 HOH   B O    1 
HETATM 7480 O O    . HOH   E 3 .   ? 57.097 -8.642  8.411   1.00 18.50 ?  276 HOH   B O    1 
HETATM 7481 O O    . HOH   E 3 .   ? 57.309 -12.107 12.309  1.00 35.26 ?  277 HOH   B O    1 
HETATM 7482 O O    . HOH   E 3 .   ? 56.326 -23.621 -14.689 1.00 28.70 ?  278 HOH   B O    1 
HETATM 7483 O O    . HOH   E 3 .   ? 42.534 -9.965  9.301   1.00 18.64 ?  279 HOH   B O    1 
HETATM 7484 O O    . HOH   E 3 .   ? 27.729 -26.771 -15.642 1.00 31.77 ?  280 HOH   B O    1 
HETATM 7485 O O    . HOH   E 3 .   ? 43.549 -15.850 -12.153 1.00 13.76 ?  281 HOH   B O    1 
HETATM 7486 O O    . HOH   E 3 .   ? 52.684 -10.411 12.944  1.00 20.73 ?  282 HOH   B O    1 
HETATM 7487 O O    . HOH   E 3 .   ? 30.635 -42.298 -10.601 1.00 29.75 ?  283 HOH   B O    1 
HETATM 7488 O O    . HOH   E 3 .   ? 37.024 -12.802 -1.538  1.00 24.64 ?  284 HOH   B O    1 
HETATM 7489 O O    . HOH   E 3 .   ? 47.182 -34.071 -4.643  1.00 16.73 ?  285 HOH   B O    1 
HETATM 7490 O O    . HOH   E 3 .   ? 41.300 -5.555  11.567  1.00 43.79 ?  286 HOH   B O    1 
HETATM 7491 O O    . HOH   E 3 .   ? 47.079 -29.577 9.799   1.00 31.87 ?  287 HOH   B O    1 
HETATM 7492 O O    . HOH   E 3 .   ? 60.007 -15.332 8.164   1.00 30.67 ?  288 HOH   B O    1 
HETATM 7493 O O    . HOH   E 3 .   ? 39.028 -11.922 12.389  1.00 33.33 ?  289 HOH   B O    1 
HETATM 7494 O O    . HOH   E 3 .   ? 48.557 -25.089 3.096   1.00 12.79 ?  290 HOH   B O    1 
HETATM 7495 O O    . HOH   E 3 .   ? 48.879 -20.044 5.953   1.00 13.08 ?  291 HOH   B O    1 
HETATM 7496 O O    . HOH   E 3 .   ? 33.680 -15.352 -13.919 1.00 20.25 ?  292 HOH   B O    1 
HETATM 7497 O O    . HOH   E 3 .   ? 28.081 -22.884 -7.933  1.00 16.08 ?  293 HOH   B O    1 
HETATM 7498 O O    . HOH   E 3 .   ? 42.916 -20.289 -20.641 1.00 37.38 ?  294 HOH   B O    1 
HETATM 7499 O O    . HOH   E 3 .   ? 42.507 -9.971  -14.832 1.00 31.57 ?  295 HOH   B O    1 
HETATM 7500 O O    . HOH   E 3 .   ? 37.647 -18.117 13.116  1.00 31.41 ?  296 HOH   B O    1 
HETATM 7501 O O    . HOH   E 3 .   ? 45.818 -36.357 -16.081 1.00 36.95 ?  297 HOH   B O    1 
HETATM 7502 O O    . HOH   E 3 .   ? 42.567 -34.740 3.819   1.00 25.64 ?  298 HOH   B O    1 
HETATM 7503 O O    . HOH   E 3 .   ? 51.335 -37.638 -9.612  1.00 25.86 ?  299 HOH   B O    1 
HETATM 7504 O O    . HOH   E 3 .   ? 48.038 -24.604 -17.792 1.00 29.49 ?  300 HOH   B O    1 
HETATM 7505 O O    . HOH   E 3 .   ? 26.120 -21.499 -3.411  1.00 15.77 ?  301 HOH   B O    1 
HETATM 7506 O O    . HOH   E 3 .   ? 53.110 -15.970 -12.745 1.00 23.45 ?  302 HOH   B O    1 
HETATM 7507 O O    . HOH   E 3 .   ? 52.678 -35.757 -8.655  1.00 29.11 ?  303 HOH   B O    1 
HETATM 7508 O O    . HOH   E 3 .   ? 45.411 -33.453 -15.934 1.00 22.78 ?  304 HOH   B O    1 
HETATM 7509 O O    . HOH   E 3 .   ? 35.227 -33.592 4.620   1.00 30.11 ?  305 HOH   B O    1 
HETATM 7510 O O    . HOH   E 3 .   ? 42.900 -12.196 -18.432 1.00 27.50 ?  306 HOH   B O    1 
HETATM 7511 O O    . HOH   E 3 .   ? 40.447 -10.905 -9.458  1.00 16.31 ?  307 HOH   B O    1 
HETATM 7512 O O    . HOH   E 3 .   ? 62.875 -13.640 4.765   1.00 28.02 ?  308 HOH   B O    1 
HETATM 7513 O O    . HOH   E 3 .   ? 44.166 -29.403 -4.609  1.00 21.95 ?  309 HOH   B O    1 
HETATM 7514 O O    . HOH   E 3 .   ? 57.614 -21.890 3.512   1.00 31.10 ?  310 HOH   B O    1 
HETATM 7515 O O    . HOH   E 3 .   ? 44.770 -27.493 2.051   1.00 14.88 ?  311 HOH   B O    1 
HETATM 7516 O O    . HOH   E 3 .   ? 50.035 -24.765 5.838   1.00 33.95 ?  312 HOH   B O    1 
HETATM 7517 O O    . HOH   E 3 .   ? 45.947 -40.455 -3.605  1.00 28.26 ?  313 HOH   B O    1 
HETATM 7518 O O    . HOH   E 3 .   ? 38.022 -10.289 -10.692 1.00 16.44 ?  314 HOH   B O    1 
HETATM 7519 O O    . HOH   E 3 .   ? 41.915 -8.127  1.365   1.00 21.89 ?  315 HOH   B O    1 
HETATM 7520 O O    . HOH   E 3 .   ? 52.639 -29.271 -13.036 1.00 24.12 ?  316 HOH   B O    1 
HETATM 7521 O O    . HOH   E 3 .   ? 43.381 -21.443 10.706  1.00 15.07 ?  317 HOH   B O    1 
HETATM 7522 O O    . HOH   E 3 .   ? 53.537 -30.287 4.558   1.00 17.99 ?  318 HOH   B O    1 
HETATM 7523 O O    . HOH   E 3 .   ? 43.692 -15.408 18.114  1.00 27.99 ?  319 HOH   B O    1 
HETATM 7524 O O    . HOH   E 3 .   ? 37.395 -35.698 7.274   1.00 33.50 ?  320 HOH   B O    1 
HETATM 7525 O O    . HOH   E 3 .   ? 38.495 -12.708 7.984   1.00 17.17 ?  321 HOH   B O    1 
HETATM 7526 O O    . HOH   E 3 .   ? 48.760 -12.101 -14.217 1.00 26.44 ?  322 HOH   B O    1 
HETATM 7527 O O    . HOH   E 3 .   ? 32.901 -34.620 -5.866  1.00 16.29 ?  323 HOH   B O    1 
HETATM 7528 O O    . HOH   E 3 .   ? 38.502 -9.430  -13.264 1.00 26.82 ?  324 HOH   B O    1 
HETATM 7529 O O    . HOH   E 3 .   ? 48.194 -32.740 -16.626 1.00 38.27 ?  325 HOH   B O    1 
HETATM 7530 O O    . HOH   E 3 .   ? 37.139 -30.621 -20.991 1.00 29.32 ?  326 HOH   B O    1 
HETATM 7531 O O    . HOH   E 3 .   ? 53.787 -12.523 -22.252 1.00 35.85 ?  327 HOH   B O    1 
HETATM 7532 O O    . HOH   E 3 .   ? 41.440 -24.561 15.776  1.00 41.85 ?  328 HOH   B O    1 
HETATM 7533 O O    . HOH   E 3 .   ? 44.199 -1.803  7.685   1.00 42.24 ?  329 HOH   B O    1 
HETATM 7534 O O    . HOH   E 3 .   ? 33.756 -31.144 11.092  1.00 34.43 ?  330 HOH   B O    1 
HETATM 7535 O O    . HOH   E 3 .   ? 26.502 -21.075 -6.194  1.00 15.42 ?  331 HOH   B O    1 
HETATM 7536 O O    . HOH   E 3 .   ? 43.257 -34.616 0.081   1.00 21.64 ?  332 HOH   B O    1 
HETATM 7537 O O    . HOH   E 3 .   ? 47.389 -24.506 8.209   1.00 25.35 ?  333 HOH   B O    1 
HETATM 7538 O O    . HOH   E 3 .   ? 44.814 -24.636 9.611   1.00 19.94 ?  334 HOH   B O    1 
HETATM 7539 O O    . HOH   E 3 .   ? 63.104 -20.203 -0.817  1.00 38.23 ?  335 HOH   B O    1 
HETATM 7540 O O    . HOH   E 3 .   ? 36.887 -12.422 4.299   1.00 16.91 ?  336 HOH   B O    1 
HETATM 7541 O O    . HOH   E 3 .   ? 51.549 -33.084 -10.870 1.00 40.36 ?  337 HOH   B O    1 
HETATM 7542 O O    . HOH   E 3 .   ? 43.003 -43.524 -14.332 1.00 42.92 ?  338 HOH   B O    1 
HETATM 7543 O O    . HOH   E 3 .   ? 60.135 -17.305 -10.470 1.00 34.70 ?  339 HOH   B O    1 
HETATM 7544 O O    . HOH   E 3 .   ? 39.587 -23.432 -20.332 1.00 36.08 ?  340 HOH   B O    1 
HETATM 7545 O O    . HOH   E 3 .   ? 28.935 -42.889 -12.304 1.00 35.11 ?  341 HOH   B O    1 
HETATM 7546 O O    . HOH   E 3 .   ? 27.881 -14.771 -9.497  1.00 36.99 ?  342 HOH   B O    1 
HETATM 7547 O O    . HOH   E 3 .   ? 47.622 -27.495 2.020   1.00 14.46 ?  343 HOH   B O    1 
HETATM 7548 O O    . HOH   E 3 .   ? 37.140 -15.137 -16.511 1.00 35.38 ?  344 HOH   B O    1 
HETATM 7549 O O    . HOH   E 3 .   ? 38.572 -12.274 -16.190 1.00 40.55 ?  345 HOH   B O    1 
HETATM 7550 O O    . HOH   E 3 .   ? 47.031 -19.948 12.215  1.00 29.43 ?  346 HOH   B O    1 
HETATM 7551 O O    . HOH   E 3 .   ? 37.111 -45.243 -9.668  1.00 36.45 ?  347 HOH   B O    1 
HETATM 7552 O O    . HOH   E 3 .   ? 33.149 -14.709 1.098   1.00 16.95 ?  348 HOH   B O    1 
HETATM 7553 O O    . HOH   E 3 .   ? 38.750 -22.483 15.093  1.00 41.80 ?  349 HOH   B O    1 
HETATM 7554 O O    . HOH   E 3 .   ? 39.895 -44.300 -11.157 1.00 40.08 ?  350 HOH   B O    1 
HETATM 7555 O O    . HOH   E 3 .   ? 44.255 -37.412 -17.753 1.00 32.43 ?  351 HOH   B O    1 
HETATM 7556 O O    . HOH   E 3 .   ? 34.656 -10.317 7.641   1.00 21.98 ?  352 HOH   B O    1 
HETATM 7557 O O    . HOH   E 3 .   ? 40.488 -43.469 -9.139  1.00 25.64 ?  353 HOH   B O    1 
HETATM 7558 O O    . HOH   E 3 .   ? 23.487 -23.734 6.899   1.00 31.78 ?  354 HOH   B O    1 
HETATM 7559 O O    . HOH   E 3 .   ? 62.698 -20.037 -4.836  1.00 52.69 ?  355 HOH   B O    1 
HETATM 7560 O O    . HOH   E 3 .   ? 55.791 -8.233  10.781  1.00 23.32 ?  356 HOH   B O    1 
HETATM 7561 O O    . HOH   E 3 .   ? 27.980 -26.644 -0.500  1.00 28.21 ?  357 HOH   B O    1 
HETATM 7562 O O    . HOH   E 3 .   ? 34.008 -9.204  -8.824  1.00 28.26 ?  358 HOH   B O    1 
HETATM 7563 O O    . HOH   E 3 .   ? 36.369 -8.536  -9.657  1.00 29.05 ?  359 HOH   B O    1 
HETATM 7564 O O    . HOH   E 3 .   ? 56.751 -7.302  3.023   1.00 25.89 ?  360 HOH   B O    1 
HETATM 7565 O O    . HOH   E 3 .   ? 34.262 -7.770  11.491  1.00 37.31 ?  361 HOH   B O    1 
HETATM 7566 O O    . HOH   E 3 .   ? 57.043 -21.474 -16.424 1.00 42.26 ?  362 HOH   B O    1 
HETATM 7567 O O    . HOH   E 3 .   ? 61.661 -19.918 1.740   1.00 37.74 ?  363 HOH   B O    1 
HETATM 7568 O O    . HOH   E 3 .   ? 27.303 -25.991 -11.305 1.00 34.08 ?  364 HOH   B O    1 
HETATM 7569 O O    . HOH   E 3 .   ? 40.376 -8.855  9.869   1.00 38.42 ?  365 HOH   B O    1 
HETATM 7570 O O    . HOH   E 3 .   ? 43.311 -12.797 -21.198 1.00 41.11 ?  366 HOH   B O    1 
HETATM 7571 O O    . HOH   E 3 .   ? 59.150 -10.585 9.177   1.00 41.43 ?  367 HOH   B O    1 
HETATM 7572 O O    . HOH   E 3 .   ? 32.717 -23.623 14.052  1.00 41.10 ?  368 HOH   B O    1 
HETATM 7573 O O    . HOH   E 3 .   ? 40.338 -11.397 -13.929 1.00 30.97 ?  369 HOH   B O    1 
HETATM 7574 O O    . HOH   E 3 .   ? 48.476 -26.491 8.763   1.00 42.60 ?  370 HOH   B O    1 
HETATM 7575 O O    . HOH   E 3 .   ? 54.405 -5.881  2.948   1.00 36.10 ?  371 HOH   B O    1 
HETATM 7576 O O    . HOH   E 3 .   ? 36.301 -8.600  8.948   1.00 37.23 ?  372 HOH   B O    1 
HETATM 7577 O O    . HOH   E 3 .   ? 39.979 -7.105  7.797   1.00 41.73 ?  373 HOH   B O    1 
HETATM 7578 O O    . HOH   E 3 .   ? 56.206 -7.903  -0.596  1.00 34.42 ?  374 HOH   B O    1 
HETATM 7579 O O    . HOH   E 3 .   ? 52.184 -12.936 13.297  1.00 26.30 ?  375 HOH   B O    1 
HETATM 7580 O O    . HOH   E 3 .   ? 41.938 -10.041 -17.424 1.00 54.06 ?  376 HOH   B O    1 
HETATM 7581 O O    . HOH   E 3 .   ? 41.998 -6.892  -4.910  1.00 41.70 ?  377 HOH   B O    1 
HETATM 7582 O O    . HOH   E 3 .   ? 63.144 -12.324 6.976   1.00 37.98 ?  378 HOH   B O    1 
HETATM 7583 O O    . HOH   E 3 .   ? 40.280 -7.771  3.078   1.00 40.60 ?  379 HOH   B O    1 
HETATM 7584 O O    . HOH   E 3 .   ? 36.671 -22.831 13.337  1.00 29.04 ?  380 HOH   B O    1 
HETATM 7585 O O    . HOH   E 3 .   ? 38.202 -10.526 10.029  1.00 26.64 ?  381 HOH   B O    1 
HETATM 7586 O O    . HOH   E 3 .   ? 42.818 -17.191 -23.203 1.00 41.08 ?  382 HOH   B O    1 
HETATM 7587 O O    . HOH   E 3 .   ? 39.776 -14.044 15.653  1.00 44.84 ?  383 HOH   B O    1 
HETATM 7588 O O    . HOH   E 3 .   ? 60.586 -22.279 2.888   1.00 43.49 ?  384 HOH   B O    1 
HETATM 7589 O O    . HOH   E 3 .   ? 44.166 -5.613  -3.428  1.00 39.08 ?  385 HOH   B O    1 
HETATM 7590 O O    . HOH   E 3 .   ? 52.961 -29.966 7.235   1.00 23.40 ?  386 HOH   B O    1 
HETATM 7591 O O    . HOH   E 3 .   ? 46.838 -5.403  2.920   1.00 39.59 ?  387 HOH   B O    1 
HETATM 7592 O O    . HOH   E 3 .   ? 25.875 -18.943 -11.838 1.00 41.38 ?  388 HOH   B O    1 
HETATM 7593 O O    . HOH   E 3 .   ? 35.532 -33.757 7.335   1.00 43.05 ?  389 HOH   B O    1 
HETATM 7594 O O    . HOH   E 3 .   ? 35.427 -20.414 13.339  1.00 30.80 ?  390 HOH   B O    1 
HETATM 7595 O O    . HOH   E 3 .   ? 24.083 -20.946 -7.662  1.00 26.95 ?  391 HOH   B O    1 
HETATM 7596 O O    . HOH   E 3 .   ? 41.067 -9.747  15.823  1.00 43.50 ?  392 HOH   B O    1 
HETATM 7597 O O    . HOH   E 3 .   ? 40.927 -6.604  -0.766  1.00 23.57 ?  393 HOH   B O    1 
HETATM 7598 O O    . HOH   E 3 .   ? 44.231 -31.843 -3.847  1.00 33.33 ?  394 HOH   B O    1 
HETATM 7599 O O    . HOH   E 3 .   ? 28.182 -27.091 2.335   1.00 31.50 ?  395 HOH   B O    1 
HETATM 7600 O O    . HOH   E 3 .   ? 26.755 -27.990 -13.384 1.00 34.74 ?  396 HOH   B O    1 
HETATM 7601 O O    . HOH   E 3 .   ? 50.723 -30.947 8.740   1.00 28.72 ?  397 HOH   B O    1 
HETATM 7602 O O    . HOH   E 3 .   ? 24.824 -20.606 -10.527 1.00 40.00 ?  398 HOH   B O    1 
HETATM 7603 O O    . HOH   E 3 .   ? 34.523 -33.467 9.705   1.00 34.36 ?  399 HOH   B O    1 
HETATM 7604 O O    . HOH   E 3 .   ? 26.930 -30.630 -12.576 1.00 27.38 ?  400 HOH   B O    1 
HETATM 7605 O O    . HOH   E 3 .   ? 57.738 -6.547  -2.322  1.00 32.54 ?  401 HOH   B O    1 
HETATM 7606 O O    . HOH   E 3 .   ? 45.819 -20.088 15.311  1.00 43.05 ?  402 HOH   B O    1 
HETATM 7607 O O    . HOH   E 3 .   ? 40.936 -11.910 -22.327 1.00 41.23 ?  403 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   ? 0.6576 0.6581 0.7441 0.0104  -0.0202 0.0474  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6707 0.6618 0.7584 0.0138  -0.0251 0.0653  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6541 0.6548 0.7371 0.0091  -0.0190 0.0472  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6673 0.6582 0.7487 0.0124  -0.0240 0.0656  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6356 0.6376 0.6985 0.0038  -0.0192 0.0483  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6490 0.6397 0.7038 0.0057  -0.0255 0.0658  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6386 0.6406 0.7084 0.0049  -0.0206 0.0494  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6519 0.6428 0.7144 0.0070  -0.0273 0.0673  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6654 0.6654 0.7627 0.0120  -0.0174 0.0456  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6787 0.6698 0.7763 0.0163  -0.0212 0.0644  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6691 0.6689 0.7697 0.0132  -0.0170 0.0451  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6822 0.6730 0.7837 0.0178  -0.0204 0.0639  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6694 0.6692 0.7694 0.0127  -0.0169 0.0450  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6827 0.6741 0.7841 0.0175  -0.0202 0.0639  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6108 0.6146 0.6445 -0.0032 -0.0168 0.0472  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6245 0.6150 0.6409 -0.0029 -0.0239 0.0632  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5828 0.5891 0.5834 -0.0105 -0.0135 0.0447  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.5964 0.5877 0.5702 -0.0120 -0.0199 0.0589  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5428 0.5568 0.5454 -0.0216 -0.0031 0.0344  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5565 0.5572 0.5297 -0.0250 -0.0012 0.0463  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5445 0.5585 0.5517 -0.0224 -0.0018 0.0355  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5584 0.5590 0.5330 -0.0260 0.0007  0.0487  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.5919 0.5937 0.5558 -0.0072 -0.0195 0.0522  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6048 0.5886 0.5369 -0.0089 -0.0329 0.0675  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.5981 0.5965 0.5279 -0.0045 -0.0246 0.0590  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6099 0.5879 0.5033 -0.0064 -0.0450 0.0745  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6002 0.5978 0.5180 -0.0043 -0.0262 0.0611  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6115 0.5870 0.4907 -0.0065 -0.0495 0.0769  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6000 0.5969 0.5213 -0.0026 -0.0267 0.0620  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6115 0.5874 0.4957 -0.0042 -0.0498 0.0783  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.4987 0.5207 0.4952 -0.0327 0.0058  0.0230  5   SER   A N   
60   N N   B SER   A 5   ? 0.5122 0.5229 0.4811 -0.0379 0.0164  0.0317  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4528 0.4829 0.4407 -0.0437 0.0176  0.0124  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4659 0.4865 0.4295 -0.0516 0.0387  0.0184  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4023 0.4409 0.3813 -0.0512 0.0295  0.0063  5   SER   A C   
64   C C   B SER   A 5   ? 0.4119 0.4422 0.3665 -0.0626 0.0632  0.0109  5   SER   A C   
65   O O   A SER   A 5   ? 0.4057 0.4429 0.3753 -0.0508 0.0297  0.0009  5   SER   A O   
66   O O   B SER   A 5   ? 0.4176 0.4445 0.3556 -0.0624 0.0643  0.0014  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4559 0.4859 0.4506 -0.0469 0.0172  0.0089  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4716 0.4927 0.4504 -0.0536 0.0365  0.0145  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4576 0.4875 0.4544 -0.0490 0.0164  0.0070  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4748 0.4961 0.4600 -0.0555 0.0340  0.0121  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3465 0.3952 0.3194 -0.0582 0.0429  0.0087  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3496 0.3936 0.3026 -0.0738 0.0886  0.0165  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2930 0.3486 0.2669 -0.0611 0.0533  0.0144  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.2912 0.3420 0.2571 -0.0797 0.1022  0.0276  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2750 0.3361 0.2562 -0.0670 0.0707  0.0152  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.2821 0.3378 0.2710 -0.0801 0.1235  0.0255  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2769 0.3335 0.2633 -0.0747 0.0758  0.0186  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.2910 0.3416 0.3050 -0.0789 0.1228  0.0348  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2618 0.3157 0.2332 -0.0529 0.0433  0.0155  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2501 0.2982 0.2183 -0.0751 0.0774  0.0343  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2361 0.2876 0.2097 -0.0419 0.0326  0.0175  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2156 0.2623 0.1899 -0.0626 0.0509  0.0372  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2251 0.2760 0.1981 -0.0368 0.0259  0.0167  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2003 0.2473 0.1787 -0.0557 0.0382  0.0383  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2296 0.2760 0.2143 -0.0320 0.0296  0.0186  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2091 0.2497 0.2075 -0.0494 0.0372  0.0364  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2215 0.2686 0.1997 -0.0316 0.0260  0.0197  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.1955 0.2384 0.1901 -0.0504 0.0314  0.0422  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2256 0.2695 0.2158 -0.0264 0.0322  0.0215  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2039 0.2419 0.2184 -0.0432 0.0337  0.0360  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2228 0.2667 0.2082 -0.0279 0.0292  0.0205  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.1976 0.2368 0.2036 -0.0466 0.0304  0.0368  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2579 0.3263 0.2450 -0.0618 0.0736  0.0127  7   SER   A N   
122  N N   B SER   A 7   ? 0.2667 0.3298 0.2593 -0.0762 0.1318  0.0151  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2454 0.3181 0.2480 -0.0501 0.0696  -0.0004 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2577 0.3256 0.2801 -0.0642 0.1178  -0.0090 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2221 0.2885 0.2371 -0.0468 0.0732  0.0013  7   SER   A C   
126  C C   B SER   A 7   ? 0.2272 0.2957 0.2527 -0.0632 0.1180  -0.0116 7   SER   A C   
127  O O   A SER   A 7   ? 0.2285 0.2845 0.2392 -0.0467 0.0719  -0.0004 7   SER   A O   
128  O O   B SER   A 7   ? 0.2323 0.2892 0.2571 -0.0705 0.1127  -0.0142 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2573 0.3356 0.2638 -0.0394 0.0588  -0.0089 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2791 0.3464 0.3290 -0.0519 0.0975  -0.0193 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2671 0.3462 0.2726 -0.0326 0.0499  -0.0106 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.2965 0.3597 0.3675 -0.0447 0.0792  -0.0215 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2009 0.2655 0.2396 -0.0426 0.0674  0.0008  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2021 0.2752 0.2484 -0.0544 0.1056  -0.0088 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1839 0.2412 0.2324 -0.0329 0.0685  0.0034  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.1863 0.2517 0.2490 -0.0360 0.0846  -0.0022 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1700 0.2201 0.2273 -0.0212 0.0560  -0.0000 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1640 0.2262 0.2329 -0.0238 0.0682  0.0112  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1700 0.2220 0.2429 -0.0121 0.0509  -0.0111 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1601 0.2186 0.2474 -0.0111 0.0623  0.0028  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1605 0.1976 0.1998 -0.0159 0.0530  0.0158  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1551 0.2096 0.2143 -0.0160 0.0538  0.0360  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1495 0.1806 0.1849 -0.0106 0.0473  0.0215  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1474 0.1962 0.2008 -0.0084 0.0440  0.0499  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1469 0.1687 0.1975 -0.0058 0.0444  0.0322  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1461 0.1805 0.2000 -0.0101 0.0467  0.0647  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1554 0.1761 0.2148 -0.0032 0.0421  0.0322  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1604 0.1874 0.2064 -0.0088 0.0340  0.0729  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1450 0.1794 0.1792 -0.0097 0.0363  0.0096  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1428 0.2003 0.1981 0.0035  0.0343  0.0418  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1458 0.1814 0.1837 -0.0075 0.0329  -0.0041 9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1384 0.2031 0.1905 0.0053  0.0368  0.0268  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1545 0.1899 0.1962 -0.0104 0.0351  -0.0140 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1454 0.2134 0.2027 -0.0035 0.0466  0.0163  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1434 0.1762 0.1865 -0.0086 0.0284  0.0047  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1313 0.1930 0.1847 0.0081  0.0312  0.0332  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1554 0.1931 0.2071 -0.0113 0.0330  -0.0172 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1408 0.2149 0.2092 -0.0054 0.0464  0.0052  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1472 0.1821 0.1966 -0.0103 0.0312  -0.0018 9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1314 0.1985 0.1903 0.0052  0.0356  0.0216  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1520 0.1910 0.2156 -0.0195 0.0380  -0.0091 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1299 0.2089 0.2103 -0.0098 0.0504  0.0112  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1648 0.1984 0.2414 -0.0301 0.0331  -0.0121 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1397 0.2183 0.2366 -0.0261 0.0408  0.0047  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1490 0.1565 0.2029 -0.0041 0.0366  0.0346  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1433 0.1644 0.1927 -0.0084 0.0433  0.0632  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1503 0.1541 0.2034 -0.0160 0.0235  0.0490  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1395 0.1655 0.2045 -0.0215 0.0355  0.0580  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1465 0.1412 0.1926 -0.0169 0.0114  0.0469  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1287 0.1544 0.1858 -0.0225 0.0335  0.0453  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1422 0.1399 0.1898 -0.0189 0.0008  0.0402  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1304 0.1456 0.1713 -0.0247 0.0448  0.0272  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1573 0.1661 0.2246 -0.0133 0.0186  0.0626  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1515 0.1873 0.2415 -0.0182 0.0150  0.0530  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1740 0.1766 0.2407 -0.0122 0.0134  0.0686  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1719 0.2058 0.2739 -0.0103 -0.0087 0.0339  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1839 0.1819 0.2485 -0.0189 0.0122  0.0686  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1953 0.2185 0.2879 -0.0093 -0.0151 0.0333  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1822 0.1884 0.2503 -0.0090 0.0146  0.0636  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1712 0.2063 0.2745 -0.0045 -0.0034 0.0309  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1524 0.1323 0.1948 -0.0154 0.0131  0.0504  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1322 0.1543 0.2238 -0.0263 0.0328  0.0553  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1532 0.1234 0.2014 -0.0197 0.0152  0.0461  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1282 0.1496 0.2280 -0.0323 0.0208  0.0519  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1461 0.1245 0.2018 -0.0149 0.0148  0.0281  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1152 0.1505 0.2331 -0.0357 0.0130  0.0516  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1427 0.1275 0.2184 -0.0192 0.0191  0.0229  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1114 0.1539 0.2692 -0.0376 0.0105  0.0460  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1659 0.1265 0.1973 -0.0192 0.0137  0.0452  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1396 0.1549 0.2127 -0.0266 0.0186  0.0403  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1756 0.1239 0.1828 -0.0273 0.0196  0.0464  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1483 0.1513 0.1971 -0.0257 0.0243  0.0351  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1868 0.1286 0.1834 -0.0244 0.0170  0.0364  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1616 0.1543 0.1911 -0.0135 0.0157  0.0299  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1914 0.1288 0.1813 -0.0188 0.0197  0.0391  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1655 0.1542 0.1821 -0.0019 0.0150  0.0407  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1923 0.1311 0.1869 -0.0152 0.0140  0.0349  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1655 0.1574 0.1859 0.0043  0.0051  0.0444  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1450 0.1202 0.1782 -0.0142 0.0130  0.0219  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1106 0.1538 0.2152 -0.0374 0.0040  0.0441  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1524 0.1376 0.1764 -0.0204 0.0076  0.0285  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1190 0.1686 0.2147 -0.0371 -0.0077 0.0497  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1490 0.1419 0.1758 -0.0246 0.0124  0.0270  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1166 0.1626 0.2040 -0.0339 -0.0016 0.0506  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1516 0.1483 0.1818 -0.0238 0.0114  0.0149  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1169 0.1596 0.1960 -0.0210 0.0001  0.0562  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1599 0.1377 0.1814 -0.0141 0.0057  0.0361  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1265 0.1766 0.2292 -0.0305 -0.0092 0.0569  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1680 0.1456 0.1982 -0.0067 -0.0027 0.0365  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1384 0.1823 0.2445 -0.0215 -0.0080 0.0522  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1713 0.1525 0.2057 -0.0024 -0.0100 0.0446  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1487 0.1931 0.2596 -0.0163 0.0029  0.0498  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1715 0.1458 0.2074 0.0026  -0.0027 0.0314  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1359 0.1766 0.2488 -0.0109 -0.0167 0.0381  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1410 0.1413 0.1673 -0.0170 0.0121  0.0293  13  THR   A N   
320  N N   B THR   A 13  ? 0.1126 0.1589 0.1991 -0.0287 -0.0023 0.0388  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1395 0.1378 0.1606 -0.0172 0.0159  0.0291  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1212 0.1516 0.1970 -0.0285 0.0034  0.0278  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1428 0.1315 0.1701 -0.0095 0.0147  0.0339  13  THR   A C   
324  C C   B THR   A 13  ? 0.1174 0.1443 0.1953 -0.0292 0.0134  0.0221  13  THR   A C   
325  O O   A THR   A 13  ? 0.1462 0.1295 0.1772 -0.0030 0.0112  0.0342  13  THR   A O   
326  O O   B THR   A 13  ? 0.1188 0.1428 0.1992 -0.0138 0.0204  0.0181  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1414 0.1507 0.1618 -0.0194 0.0259  0.0329  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1364 0.1581 0.1986 -0.0196 -0.0061 0.0304  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1353 0.1522 0.1524 -0.0289 0.0359  0.0442  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1385 0.1554 0.2180 -0.0230 -0.0185 0.0191  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1444 0.1646 0.1679 -0.0212 0.0258  0.0205  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1438 0.1756 0.1971 -0.0219 0.0015  0.0259  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1479 0.1270 0.1687 -0.0040 0.0179  0.0413  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1250 0.1462 0.2001 -0.0287 0.0173  0.0281  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1506 0.1266 0.1889 0.0004  0.0120  0.0487  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1299 0.1519 0.1979 -0.0267 0.0077  0.0355  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1450 0.1356 0.1787 -0.0043 0.0081  0.0438  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1349 0.1455 0.1708 -0.0159 0.0030  0.0372  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1533 0.1471 0.2003 -0.0187 0.0087  0.0459  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1490 0.1432 0.1739 -0.0134 0.0052  0.0344  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1670 0.1243 0.2412 -0.0027 0.0076  0.0604  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1405 0.1890 0.2439 -0.0263 0.0118  0.0539  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1878 0.1635 0.3105 -0.0115 0.0001  0.0518  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.1533 0.2409 0.3021 -0.0351 -0.0024 0.0629  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.1968 0.1848 0.3394 -0.0118 -0.0142 0.0529  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.1546 0.2589 0.3245 -0.0400 -0.0131 0.0714  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.1986 0.1790 0.3454 -0.0215 0.0046  0.0388  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.1704 0.2603 0.3458 -0.0279 -0.0020 0.0624  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1371 0.1366 0.1733 -0.0101 0.0064  0.0465  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1259 0.1347 0.1579 -0.0226 0.0062  0.0370  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1336 0.1331 0.1751 -0.0157 0.0036  0.0390  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1237 0.1302 0.1810 -0.0198 0.0082  0.0214  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1232 0.1257 0.1753 -0.0141 0.0099  0.0320  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1141 0.1264 0.2011 -0.0152 0.0117  0.0277  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1198 0.1313 0.1901 -0.0052 0.0109  0.0202  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1129 0.1291 0.2119 -0.0052 0.0117  0.0205  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1373 0.1335 0.1747 -0.0112 0.0049  0.0436  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1213 0.1263 0.1798 -0.0155 0.0068  0.0140  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1274 0.1402 0.1703 -0.0083 0.0177  0.0372  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1181 0.1405 0.1898 -0.0109 0.0114  0.0178  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1287 0.1372 0.1825 -0.0086 0.0330  0.0311  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1214 0.1466 0.1874 -0.0168 0.0213  0.0091  15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1239 0.1497 0.1646 -0.0145 0.0131  0.0296  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1271 0.1455 0.1892 -0.0119 -0.0002 0.0219  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1219 0.1211 0.1759 -0.0155 0.0105  0.0285  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1160 0.1336 0.2181 -0.0139 0.0062  0.0369  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1251 0.1225 0.1739 -0.0120 0.0048  0.0195  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1194 0.1395 0.2040 -0.0159 0.0162  0.0480  16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1184 0.1101 0.1657 -0.0091 0.0006  0.0209  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1160 0.1433 0.2000 -0.0111 0.0132  0.0529  16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1155 0.1122 0.1738 -0.0148 0.0054  0.0176  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1137 0.1481 0.2093 -0.0105 0.0234  0.0462  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1338 0.1373 0.1743 -0.0044 0.0044  0.0145  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1287 0.1442 0.1873 -0.0033 0.0219  0.0487  16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1478 0.1465 0.1757 0.0006  0.0058  0.0115  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1478 0.1548 0.1872 0.0061  0.0192  0.0424  16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1368 0.1509 0.1767 0.0035  0.0077  0.0098  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1323 0.1572 0.1930 0.0052  0.0276  0.0483  16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1146 0.1061 0.1710 -0.0098 0.0113  0.0187  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1143 0.1368 0.2016 -0.0155 0.0151  0.0523  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1193 0.1205 0.1620 -0.0139 0.0115  0.0191  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1189 0.1363 0.1793 -0.0167 0.0149  0.0487  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1136 0.1207 0.1757 -0.0149 0.0106  0.0240  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1169 0.1354 0.1911 -0.0125 0.0127  0.0445  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1063 0.1095 0.1591 -0.0154 0.0045  0.0166  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1095 0.1413 0.1864 -0.0128 0.0075  0.0434  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1272 0.1272 0.1641 -0.0167 0.0101  0.0186  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1252 0.1406 0.1785 -0.0116 0.0030  0.0438  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.1432 0.1394 0.1834 -0.0229 0.0048  0.0288  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1411 0.1526 0.1778 -0.0163 -0.0088 0.0410  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.1514 0.1481 0.1878 -0.0207 -0.0033 0.0326  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1574 0.1645 0.1785 -0.0034 -0.0100 0.0486  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.1516 0.1423 0.1815 -0.0370 0.0035  0.0339  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1530 0.1633 0.1788 -0.0232 -0.0019 0.0421  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.1638 0.1470 0.1896 -0.0260 -0.0138 0.0325  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.1797 0.1722 0.1879 -0.0022 -0.0081 0.0471  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.1668 0.1420 0.1849 -0.0396 0.0000  0.0280  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.1716 0.1688 0.1851 -0.0218 0.0023  0.0350  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.1792 0.1413 0.1906 -0.0348 -0.0120 0.0340  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.1876 0.1704 0.1900 -0.0099 -0.0116 0.0443  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.1975 0.1380 0.2006 -0.0379 -0.0163 0.0420  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.2030 0.1727 0.2139 -0.0078 -0.0117 0.0502  17  TYR   A OH  
473  N N   . ILE   A 18  ? 0.1195 0.1317 0.1959 -0.0166 0.0144  0.0436  18  ILE   A N   
474  C CA  . ILE   A 18  ? 0.1233 0.1382 0.2027 -0.0164 0.0211  0.0457  18  ILE   A CA  
475  C C   . ILE   A 18  ? 0.1189 0.1446 0.2117 -0.0107 0.0255  0.0474  18  ILE   A C   
476  O O   . ILE   A 18  ? 0.1201 0.1508 0.2227 -0.0141 0.0324  0.0499  18  ILE   A O   
477  C CB  . ILE   A 18  ? 0.1297 0.1466 0.1938 -0.0095 0.0118  0.0514  18  ILE   A CB  
478  C CG1 . ILE   A 18  ? 0.1503 0.1569 0.2006 -0.0080 0.0036  0.0559  18  ILE   A CG1 
479  C CG2 . ILE   A 18  ? 0.1313 0.1512 0.2060 -0.0072 0.0030  0.0446  18  ILE   A CG2 
480  C CD1 . ILE   A 18  ? 0.1941 0.1766 0.2299 -0.0122 0.0010  0.0623  18  ILE   A CD1 
493  N N   A LYS   A 19  ? 0.1324 0.1434 0.2056 -0.0071 0.0381  0.0494  19  LYS   A N   
494  N N   B LYS   A 19  ? 0.1226 0.1421 0.2133 -0.0087 0.0365  0.0407  19  LYS   A N   
495  C CA  A LYS   A 19  ? 0.1466 0.1487 0.2161 0.0015  0.0397  0.0482  19  LYS   A CA  
496  C CA  B LYS   A 19  ? 0.1275 0.1490 0.2289 0.0001  0.0317  0.0314  19  LYS   A CA  
497  C C   A LYS   A 19  ? 0.1444 0.1415 0.2168 0.0070  0.0456  0.0593  19  LYS   A C   
498  C C   B LYS   A 19  ? 0.1157 0.1493 0.2393 0.0032  0.0234  0.0302  19  LYS   A C   
499  O O   A LYS   A 19  ? 0.1409 0.1383 0.2186 0.0097  0.0450  0.0689  19  LYS   A O   
500  O O   B LYS   A 19  ? 0.1015 0.1446 0.2370 0.0020  0.0165  0.0300  19  LYS   A O   
501  C CB  A LYS   A 19  ? 0.1589 0.1612 0.2219 -0.0008 0.0441  0.0407  19  LYS   A CB  
502  C CB  B LYS   A 19  ? 0.1419 0.1574 0.2266 -0.0003 0.0368  0.0293  19  LYS   A CB  
503  C CG  A LYS   A 19  ? 0.1744 0.1752 0.2210 0.0016  0.0510  0.0399  19  LYS   A CG  
504  C CG  B LYS   A 19  ? 0.1627 0.1792 0.2450 0.0019  0.0346  0.0055  19  LYS   A CG  
505  C CD  A LYS   A 19  ? 0.1787 0.1842 0.2085 -0.0018 0.0663  0.0446  19  LYS   A CD  
506  C CD  B LYS   A 19  ? 0.1876 0.2023 0.2516 0.0044  0.0355  -0.0103 19  LYS   A CD  
507  C CE  A LYS   A 19  ? 0.1843 0.1854 0.2166 -0.0073 0.0540  0.0436  19  LYS   A CE  
508  C CE  B LYS   A 19  ? 0.2007 0.2147 0.2535 -0.0029 0.0428  -0.0138 19  LYS   A CE  
509  N NZ  A LYS   A 19  ? 0.1893 0.1885 0.2256 -0.0142 0.0564  0.0427  19  LYS   A NZ  
510  N NZ  B LYS   A 19  ? 0.2080 0.2247 0.2496 -0.0056 0.0489  -0.0198 19  LYS   A NZ  
537  N N   A ASN   A 20  ? 0.1442 0.1418 0.2187 0.0066  0.0443  0.0515  20  ASN   A N   
538  N N   B ASN   A 20  ? 0.1207 0.1589 0.2522 0.0012  0.0170  0.0279  20  ASN   A N   
539  C CA  A ASN   A 20  ? 0.1433 0.1478 0.2010 0.0185  0.0385  0.0363  20  ASN   A CA  
540  C CA  B ASN   A 20  ? 0.1246 0.1713 0.2490 0.0105  0.0148  0.0237  20  ASN   A CA  
541  C C   A ASN   A 20  ? 0.1562 0.1504 0.1769 0.0216  0.0350  0.0345  20  ASN   A C   
542  C C   B ASN   A 20  ? 0.1432 0.1713 0.2343 0.0025  0.0335  0.0244  20  ASN   A C   
543  O O   A ASN   A 20  ? 0.1683 0.1592 0.1697 0.0217  0.0380  0.0383  20  ASN   A O   
544  O O   B ASN   A 20  ? 0.1652 0.1866 0.2454 0.0000  0.0338  0.0348  20  ASN   A O   
545  C CB  A ASN   A 20  ? 0.1433 0.1546 0.2064 0.0189  0.0405  0.0369  20  ASN   A CB  
546  C CB  B ASN   A 20  ? 0.1234 0.1865 0.2522 0.0178  0.0049  0.0234  20  ASN   A CB  
547  C CG  A ASN   A 20  ? 0.1553 0.1632 0.2230 0.0175  0.0295  0.0372  20  ASN   A CG  
548  C CG  B ASN   A 20  ? 0.1265 0.2034 0.2759 0.0282  -0.0001 0.0295  20  ASN   A CG  
549  O OD1 A ASN   A 20  ? 0.1667 0.1761 0.2427 0.0228  0.0213  0.0283  20  ASN   A OD1 
550  O OD1 B ASN   A 20  ? 0.1418 0.2179 0.3134 0.0366  0.0100  0.0266  20  ASN   A OD1 
551  N ND2 A ASN   A 20  ? 0.1606 0.1634 0.2374 0.0058  0.0265  0.0432  20  ASN   A ND2 
552  N ND2 B ASN   A 20  ? 0.1334 0.2015 0.2760 0.0285  -0.0013 0.0315  20  ASN   A ND2 
565  N N   A ALA   A 21  ? 0.1635 0.1472 0.1711 0.0171  0.0178  0.0265  21  ALA   A N   
566  N N   B ALA   A 21  ? 0.1436 0.1583 0.2124 -0.0046 0.0337  0.0190  21  ALA   A N   
567  C CA  A ALA   A 21  ? 0.1819 0.1506 0.1750 0.0119  0.0024  0.0193  21  ALA   A CA  
568  C CA  B ALA   A 21  ? 0.1546 0.1525 0.1963 -0.0075 0.0280  0.0172  21  ALA   A CA  
569  C C   A ALA   A 21  ? 0.1872 0.1589 0.1687 0.0131  0.0084  0.0148  21  ALA   A C   
570  C C   B ALA   A 21  ? 0.1362 0.1423 0.1745 -0.0077 0.0238  0.0149  21  ALA   A C   
571  O O   A ALA   A 21  ? 0.1925 0.1694 0.1659 0.0056  0.0157  0.0046  21  ALA   A O   
572  O O   B ALA   A 21  ? 0.1354 0.1449 0.1717 -0.0143 0.0183  -0.0021 21  ALA   A O   
573  C CB  A ALA   A 21  ? 0.1965 0.1607 0.1960 -0.0026 -0.0218 0.0197  21  ALA   A CB  
574  C CB  B ALA   A 21  ? 0.1817 0.1695 0.2048 -0.0204 0.0236  0.0176  21  ALA   A CB  
585  N N   A ASP   A 22  ? 0.1918 0.1627 0.1807 0.0138  -0.0000 0.0175  22  ASP   A N   
586  N N   B ASP   A 22  ? 0.1274 0.1404 0.1714 -0.0031 0.0240  0.0174  22  ASP   A N   
587  C CA  A ASP   A 22  ? 0.1977 0.1740 0.1815 0.0097  -0.0079 0.0234  22  ASP   A CA  
588  C CA  B ASP   A 22  ? 0.1340 0.1345 0.1501 0.0030  0.0123  0.0145  22  ASP   A CA  
589  C C   A ASP   A 22  ? 0.1848 0.1795 0.1562 0.0008  -0.0056 0.0290  22  ASP   A C   
590  C C   B ASP   A 22  ? 0.1282 0.1417 0.1334 -0.0043 0.0182  0.0159  22  ASP   A C   
591  O O   A ASP   A 22  ? 0.1803 0.1927 0.1508 -0.0035 -0.0052 0.0353  22  ASP   A O   
592  O O   B ASP   A 22  ? 0.1253 0.1580 0.1366 -0.0096 0.0204  0.0111  22  ASP   A O   
593  C CB  A ASP   A 22  ? 0.2154 0.1814 0.2020 0.0067  -0.0080 0.0203  22  ASP   A CB  
594  C CB  B ASP   A 22  ? 0.1480 0.1347 0.1732 0.0067  0.0086  0.0099  22  ASP   A CB  
595  C CG  A ASP   A 22  ? 0.2278 0.1853 0.2115 -0.0035 -0.0085 0.0233  22  ASP   A CG  
596  C CG  B ASP   A 22  ? 0.1593 0.1392 0.1955 0.0090  0.0174  0.0122  22  ASP   A CG  
597  O OD1 A ASP   A 22  ? 0.2291 0.1817 0.2172 -0.0164 -0.0121 0.0364  22  ASP   A OD1 
598  O OD1 B ASP   A 22  ? 0.1554 0.1350 0.1761 0.0014  0.0258  0.0156  22  ASP   A OD1 
599  O OD2 A ASP   A 22  ? 0.2375 0.1940 0.2288 -0.0083 -0.0128 0.0110  22  ASP   A OD2 
600  O OD2 B ASP   A 22  ? 0.1769 0.1585 0.2566 0.0075  0.0104  0.0165  22  ASP   A OD2 
609  N N   A ILE   A 23  ? 0.1761 0.1720 0.1412 -0.0027 0.0002  0.0273  23  ILE   A N   
610  N N   B ILE   A 23  ? 0.1302 0.1344 0.1380 -0.0020 0.0141  0.0180  23  ILE   A N   
611  C CA  A ILE   A 23  ? 0.1655 0.1645 0.1314 -0.0053 0.0085  0.0173  23  ILE   A CA  
612  C CA  B ILE   A 23  ? 0.1275 0.1374 0.1311 -0.0071 0.0118  0.0213  23  ILE   A CA  
613  C C   A ILE   A 23  ? 0.1591 0.1694 0.1320 -0.0007 0.0132  0.0180  23  ILE   A C   
614  C C   B ILE   A 23  ? 0.1252 0.1438 0.1354 -0.0118 0.0119  0.0152  23  ILE   A C   
615  O O   A ILE   A 23  ? 0.1616 0.1755 0.1413 0.0011  0.0103  0.0200  23  ILE   A O   
616  O O   B ILE   A 23  ? 0.1244 0.1477 0.1435 -0.0098 0.0060  0.0143  23  ILE   A O   
617  C CB  A ILE   A 23  ? 0.1681 0.1591 0.1277 -0.0087 0.0153  0.0149  23  ILE   A CB  
618  C CB  B ILE   A 23  ? 0.1359 0.1313 0.1290 0.0050  0.0102  0.0156  23  ILE   A CB  
619  C CG1 A ILE   A 23  ? 0.1726 0.1588 0.1412 -0.0044 0.0186  0.0088  23  ILE   A CG1 
620  C CG1 B ILE   A 23  ? 0.1448 0.1332 0.1430 -0.0000 0.0034  0.0054  23  ILE   A CG1 
621  C CG2 A ILE   A 23  ? 0.1669 0.1555 0.1275 -0.0106 0.0196  0.0164  23  ILE   A CG2 
622  C CG2 B ILE   A 23  ? 0.1358 0.1282 0.1355 0.0095  0.0151  0.0192  23  ILE   A CG2 
623  C CD1 A ILE   A 23  ? 0.1698 0.1558 0.1578 -0.0037 0.0134  0.0015  23  ILE   A CD1 
624  C CD1 B ILE   A 23  ? 0.1411 0.1383 0.1445 0.0072  -0.0013 0.0031  23  ILE   A CD1 
647  N N   A VAL   A 24  ? 0.1583 0.1726 0.1437 -0.0032 0.0054  0.0118  24  VAL   A N   
648  N N   B VAL   A 24  ? 0.1365 0.1499 0.1379 -0.0177 0.0081  0.0144  24  VAL   A N   
649  C CA  A VAL   A 24  ? 0.1647 0.1813 0.1529 -0.0052 0.0009  0.0025  24  VAL   A CA  
650  C CA  B VAL   A 24  ? 0.1514 0.1574 0.1556 -0.0160 0.0041  0.0054  24  VAL   A CA  
651  C C   A VAL   A 24  ? 0.1727 0.1960 0.1617 -0.0075 -0.0036 0.0028  24  VAL   A C   
652  C C   B VAL   A 24  ? 0.1557 0.1723 0.1520 -0.0123 0.0071  0.0012  24  VAL   A C   
653  O O   A VAL   A 24  ? 0.1771 0.1979 0.1594 -0.0027 -0.0074 0.0105  24  VAL   A O   
654  O O   B VAL   A 24  ? 0.1666 0.1753 0.1594 -0.0111 0.0063  0.0011  24  VAL   A O   
655  C CB  A VAL   A 24  ? 0.1654 0.1792 0.1555 -0.0092 0.0128  0.0046  24  VAL   A CB  
656  C CB  B VAL   A 24  ? 0.1575 0.1539 0.1729 -0.0242 0.0091  0.0058  24  VAL   A CB  
657  C CG1 A VAL   A 24  ? 0.1651 0.1854 0.1530 -0.0041 0.0258  -0.0060 24  VAL   A CG1 
658  C CG1 B VAL   A 24  ? 0.1782 0.1576 0.1982 -0.0177 -0.0019 0.0003  24  VAL   A CG1 
659  C CG2 A VAL   A 24  ? 0.1713 0.1730 0.1619 -0.0114 0.0164  0.0070  24  VAL   A CG2 
660  C CG2 B VAL   A 24  ? 0.1671 0.1582 0.1903 -0.0339 0.0168  0.0121  24  VAL   A CG2 
679  N N   A GLU   A 25  ? 0.1811 0.2116 0.1662 -0.0120 0.0039  -0.0042 25  GLU   A N   
680  N N   B GLU   A 25  ? 0.1524 0.1969 0.1621 -0.0051 0.0241  -0.0057 25  GLU   A N   
681  C CA  A GLU   A 25  ? 0.1979 0.2314 0.1865 -0.0103 0.0148  -0.0023 25  GLU   A CA  
682  C CA  B GLU   A 25  ? 0.1557 0.2216 0.1581 -0.0043 0.0318  -0.0111 25  GLU   A CA  
683  C C   A GLU   A 25  ? 0.1888 0.2264 0.1608 -0.0152 0.0224  -0.0087 25  GLU   A C   
684  C C   B GLU   A 25  ? 0.1454 0.2355 0.1381 -0.0122 0.0282  -0.0114 25  GLU   A C   
685  O O   A GLU   A 25  ? 0.1865 0.2345 0.1582 -0.0111 0.0178  -0.0118 25  GLU   A O   
686  O O   B GLU   A 25  ? 0.1550 0.2441 0.1490 -0.0087 0.0333  -0.0081 25  GLU   A O   
687  C CB  A GLU   A 25  ? 0.2236 0.2510 0.2369 -0.0087 0.0146  -0.0016 25  GLU   A CB  
688  C CB  B GLU   A 25  ? 0.1766 0.2345 0.1988 0.0030  0.0407  -0.0182 25  GLU   A CB  
689  C CG  A GLU   A 25  ? 0.2447 0.2669 0.2890 -0.0137 0.0013  -0.0072 25  GLU   A CG  
690  C CG  B GLU   A 25  ? 0.2138 0.2537 0.2828 -0.0004 0.0313  -0.0240 25  GLU   A CG  
691  C CD  A GLU   A 25  ? 0.2611 0.2801 0.3337 -0.0164 -0.0091 -0.0134 25  GLU   A CD  
692  C CD  B GLU   A 25  ? 0.2492 0.2756 0.3593 -0.0073 0.0210  -0.0250 25  GLU   A CD  
693  O OE1 A GLU   A 25  ? 0.2687 0.2851 0.3422 -0.0164 -0.0172 -0.0221 25  GLU   A OE1 
694  O OE1 B GLU   A 25  ? 0.2654 0.2876 0.3963 -0.0074 0.0165  -0.0236 25  GLU   A OE1 
695  O OE2 A GLU   A 25  ? 0.2670 0.2867 0.3579 -0.0172 -0.0127 -0.0179 25  GLU   A OE2 
696  O OE2 B GLU   A 25  ? 0.2604 0.2827 0.3895 -0.0131 0.0165  -0.0249 25  GLU   A OE2 
709  N N   A GLU   A 26  ? 0.1865 0.2124 0.1632 -0.0300 0.0337  -0.0078 26  GLU   A N   
710  N N   B GLU   A 26  ? 0.1363 0.2325 0.1542 -0.0246 0.0255  -0.0164 26  GLU   A N   
711  C CA  A GLU   A 26  ? 0.1990 0.2087 0.1501 -0.0459 0.0393  0.0037  26  GLU   A CA  
712  C CA  B GLU   A 26  ? 0.1556 0.2313 0.1620 -0.0323 0.0248  -0.0020 26  GLU   A CA  
713  C C   A GLU   A 26  ? 0.1996 0.2093 0.1410 -0.0413 0.0412  0.0116  26  GLU   A C   
714  C C   B GLU   A 26  ? 0.1498 0.2075 0.1318 -0.0248 0.0174  0.0078  26  GLU   A C   
715  O O   A GLU   A 26  ? 0.2057 0.2113 0.1429 -0.0394 0.0382  0.0084  26  GLU   A O   
716  O O   B GLU   A 26  ? 0.1709 0.2176 0.1293 -0.0287 0.0240  0.0117  26  GLU   A O   
717  C CB  A GLU   A 26  ? 0.2156 0.2064 0.1822 -0.0609 0.0383  0.0144  26  GLU   A CB  
718  C CB  B GLU   A 26  ? 0.1774 0.2462 0.1990 -0.0415 0.0122  -0.0008 26  GLU   A CB  
719  C CG  A GLU   A 26  ? 0.2273 0.2134 0.2406 -0.0666 0.0421  0.0092  26  GLU   A CG  
720  C CG  B GLU   A 26  ? 0.1901 0.2626 0.2335 -0.0407 0.0261  -0.0090 26  GLU   A CG  
721  C CD  A GLU   A 26  ? 0.2345 0.2163 0.2684 -0.0712 0.0591  0.0030  26  GLU   A CD  
722  C CD  B GLU   A 26  ? 0.1992 0.2749 0.2501 -0.0446 0.0436  -0.0170 26  GLU   A CD  
723  O OE1 A GLU   A 26  ? 0.2342 0.2223 0.2737 -0.0623 0.0672  -0.0345 26  GLU   A OE1 
724  O OE1 B GLU   A 26  ? 0.2033 0.2933 0.2428 -0.0271 0.0678  -0.0370 26  GLU   A OE1 
725  O OE2 A GLU   A 26  ? 0.2372 0.2196 0.2668 -0.0727 0.0677  0.0161  26  GLU   A OE2 
726  O OE2 B GLU   A 26  ? 0.2059 0.2714 0.2204 -0.0551 0.0531  -0.0195 26  GLU   A OE2 
739  N N   A ALA   A 27  ? 0.1943 0.2128 0.1516 -0.0411 0.0460  0.0196  27  ALA   A N   
740  N N   B ALA   A 27  ? 0.1263 0.1809 0.1361 -0.0074 0.0153  0.0168  27  ALA   A N   
741  C CA  A ALA   A 27  ? 0.1998 0.2248 0.1536 -0.0406 0.0440  0.0208  27  ALA   A CA  
742  C CA  B ALA   A 27  ? 0.1320 0.1758 0.1275 0.0053  0.0091  0.0123  27  ALA   A CA  
743  C C   A ALA   A 27  ? 0.2152 0.2458 0.1780 -0.0417 0.0415  0.0141  27  ALA   A C   
744  C C   B ALA   A 27  ? 0.1530 0.1863 0.1227 0.0059  -0.0002 0.0049  27  ALA   A C   
745  O O   A ALA   A 27  ? 0.2135 0.2488 0.1755 -0.0470 0.0404  0.0120  27  ALA   A O   
746  O O   B ALA   A 27  ? 0.1520 0.1916 0.1348 0.0043  -0.0017 -0.0000 27  ALA   A O   
747  C CB  A ALA   A 27  ? 0.1945 0.2175 0.1498 -0.0430 0.0388  0.0269  27  ALA   A CB  
748  C CB  B ALA   A 27  ? 0.1273 0.1711 0.1294 -0.0021 0.0034  0.0085  27  ALA   A CB  
759  N N   A LYS   A 28  ? 0.2399 0.2705 0.2101 -0.0298 0.0344  -0.0016 28  LYS   A N   
760  N N   B LYS   A 28  ? 0.1877 0.2014 0.1250 0.0213  -0.0083 -0.0194 28  LYS   A N   
761  C CA  A LYS   A 28  ? 0.2702 0.2996 0.2500 -0.0154 0.0295  -0.0091 28  LYS   A CA  
762  C CA  B LYS   A 28  ? 0.2301 0.2395 0.1563 0.0442  -0.0115 -0.0336 28  LYS   A CA  
763  C C   A LYS   A 28  ? 0.2816 0.3197 0.2480 -0.0153 0.0304  -0.0081 28  LYS   A C   
764  C C   B LYS   A 28  ? 0.2525 0.2648 0.1403 0.0481  -0.0004 -0.0156 28  LYS   A C   
765  O O   A LYS   A 28  ? 0.2845 0.3262 0.2594 -0.0123 0.0153  -0.0120 28  LYS   A O   
766  O O   B LYS   A 28  ? 0.2686 0.2796 0.1517 0.0456  -0.0147 -0.0164 28  LYS   A O   
767  C CB  A LYS   A 28  ? 0.2891 0.3108 0.2981 -0.0017 0.0246  -0.0141 28  LYS   A CB  
768  C CB  B LYS   A 28  ? 0.2584 0.2589 0.2111 0.0587  -0.0227 -0.0541 28  LYS   A CB  
769  C CG  A LYS   A 28  ? 0.3058 0.3230 0.3472 0.0093  0.0195  -0.0139 28  LYS   A CG  
770  C CG  B LYS   A 28  ? 0.2869 0.2847 0.2829 0.0637  -0.0302 -0.0508 28  LYS   A CG  
771  C CD  A LYS   A 28  ? 0.3184 0.3341 0.3922 0.0177  0.0110  -0.0111 28  LYS   A CD  
772  C CD  B LYS   A 28  ? 0.3155 0.3113 0.3661 0.0655  -0.0368 -0.0437 28  LYS   A CD  
773  C CE  A LYS   A 28  ? 0.3269 0.3418 0.4211 0.0223  0.0056  -0.0108 28  LYS   A CE  
774  C CE  B LYS   A 28  ? 0.3355 0.3287 0.4196 0.0658  -0.0420 -0.0456 28  LYS   A CE  
775  N NZ  A LYS   A 28  ? 0.3334 0.3454 0.4415 0.0250  0.0051  -0.0142 28  LYS   A NZ  
776  N NZ  B LYS   A 28  ? 0.3457 0.3362 0.4449 0.0668  -0.0471 -0.0514 28  LYS   A NZ  
803  N N   A LYS   A 29  ? 0.2882 0.3336 0.2507 -0.0183 0.0456  0.0027  29  LYS   A N   
804  N N   B LYS   A 29  ? 0.2529 0.2806 0.1417 0.0512  0.0409  0.0128  29  LYS   A N   
805  C CA  A LYS   A 29  ? 0.2999 0.3472 0.2633 -0.0216 0.0540  0.0094  29  LYS   A CA  
806  C CA  B LYS   A 29  ? 0.2661 0.3037 0.1603 0.0461  0.0719  0.0289  29  LYS   A CA  
807  C C   A LYS   A 29  ? 0.2848 0.3340 0.2297 -0.0338 0.0422  0.0151  29  LYS   A C   
808  C C   B LYS   A 29  ? 0.2544 0.2937 0.1318 0.0359  0.0592  0.0308  29  LYS   A C   
809  O O   A LYS   A 29  ? 0.2913 0.3410 0.2344 -0.0285 0.0374  0.0121  29  LYS   A O   
810  O O   B LYS   A 29  ? 0.2674 0.3067 0.1531 0.0426  0.0481  0.0243  29  LYS   A O   
811  C CB  A LYS   A 29  ? 0.3233 0.3716 0.3139 -0.0130 0.0719  0.0104  29  LYS   A CB  
812  C CB  B LYS   A 29  ? 0.2922 0.3362 0.2180 0.0477  0.1114  0.0373  29  LYS   A CB  
813  C CG  A LYS   A 29  ? 0.3458 0.3931 0.3702 -0.0053 0.0782  0.0109  29  LYS   A CG  
814  C CG  B LYS   A 29  ? 0.3225 0.3656 0.3038 0.0515  0.1245  0.0354  29  LYS   A CG  
815  C CD  A LYS   A 29  ? 0.3650 0.4105 0.4282 0.0008  0.0798  0.0093  29  LYS   A CD  
816  C CD  B LYS   A 29  ? 0.3497 0.3889 0.3914 0.0562  0.1233  0.0284  29  LYS   A CD  
817  C CE  A LYS   A 29  ? 0.3781 0.4220 0.4661 0.0052  0.0825  0.0076  29  LYS   A CE  
818  C CE  B LYS   A 29  ? 0.3682 0.4047 0.4474 0.0589  0.1267  0.0208  29  LYS   A CE  
819  N NZ  A LYS   A 29  ? 0.3844 0.4279 0.4919 0.0081  0.0836  0.0056  29  LYS   A NZ  
820  N NZ  B LYS   A 29  ? 0.3767 0.4124 0.4833 0.0616  0.1284  0.0158  29  LYS   A NZ  
847  N N   A VAL   A 30  ? 0.2628 0.3109 0.2066 -0.0517 0.0321  0.0209  30  VAL   A N   
848  N N   B VAL   A 30  ? 0.2289 0.2685 0.1389 0.0194  0.0459  0.0369  30  VAL   A N   
849  C CA  A VAL   A 30  ? 0.2507 0.2893 0.1815 -0.0624 0.0157  0.0255  30  VAL   A CA  
850  C CA  B VAL   A 30  ? 0.2140 0.2474 0.1383 -0.0016 0.0242  0.0430  30  VAL   A CA  
851  C C   A VAL   A 30  ? 0.2424 0.2688 0.1392 -0.0582 0.0081  0.0365  30  VAL   A C   
852  C C   B VAL   A 30  ? 0.2123 0.2358 0.1229 -0.0033 0.0154  0.0321  30  VAL   A C   
853  O O   A VAL   A 30  ? 0.2455 0.2659 0.1381 -0.0546 0.0069  0.0429  30  VAL   A O   
854  O O   B VAL   A 30  ? 0.2211 0.2389 0.1410 -0.0087 0.0065  0.0292  30  VAL   A O   
855  C CB  A VAL   A 30  ? 0.2487 0.2887 0.2017 -0.0692 0.0018  0.0171  30  VAL   A CB  
856  C CB  B VAL   A 30  ? 0.2103 0.2381 0.1618 -0.0161 0.0077  0.0461  30  VAL   A CB  
857  C CG1 A VAL   A 30  ? 0.2517 0.2868 0.2150 -0.0691 0.0002  0.0149  30  VAL   A CG1 
858  C CG1 B VAL   A 30  ? 0.2150 0.2336 0.1879 -0.0165 -0.0014 0.0431  30  VAL   A CG1 
859  C CG2 A VAL   A 30  ? 0.2471 0.2925 0.2187 -0.0717 -0.0048 0.0128  30  VAL   A CG2 
860  C CG2 B VAL   A 30  ? 0.2089 0.2416 0.1941 -0.0247 0.0083  0.0449  30  VAL   A CG2 
879  N N   A LYS   A 31  ? 0.2307 0.2505 0.1334 -0.0554 0.0022  0.0317  31  LYS   A N   
880  N N   B LYS   A 31  ? 0.2058 0.2237 0.1301 0.0025  0.0051  0.0271  31  LYS   A N   
881  C CA  A LYS   A 31  ? 0.2334 0.2426 0.1458 -0.0433 -0.0124 0.0246  31  LYS   A CA  
882  C CA  B LYS   A 31  ? 0.2151 0.2226 0.1393 0.0117  -0.0107 0.0187  31  LYS   A CA  
883  C C   A LYS   A 31  ? 0.2150 0.2147 0.1030 -0.0337 -0.0161 0.0463  31  LYS   A C   
884  C C   B LYS   A 31  ? 0.1972 0.2121 0.1188 0.0170  -0.0041 0.0310  31  LYS   A C   
885  O O   A LYS   A 31  ? 0.2134 0.2161 0.1123 -0.0216 -0.0258 0.0495  31  LYS   A O   
886  O O   B LYS   A 31  ? 0.2114 0.2198 0.1453 0.0232  -0.0116 0.0162  31  LYS   A O   
887  C CB  A LYS   A 31  ? 0.2601 0.2673 0.2286 -0.0385 -0.0194 0.0029  31  LYS   A CB  
888  C CB  B LYS   A 31  ? 0.2478 0.2396 0.2105 0.0172  -0.0268 -0.0077 31  LYS   A CB  
889  C CG  A LYS   A 31  ? 0.2901 0.2905 0.3194 -0.0257 -0.0279 -0.0092 31  LYS   A CG  
890  C CG  B LYS   A 31  ? 0.2884 0.2709 0.3113 0.0209  -0.0439 -0.0267 31  LYS   A CG  
891  C CD  A LYS   A 31  ? 0.3134 0.3077 0.3859 -0.0156 -0.0357 -0.0164 31  LYS   A CD  
892  C CD  B LYS   A 31  ? 0.3205 0.2977 0.3937 0.0228  -0.0570 -0.0407 31  LYS   A CD  
893  C CE  A LYS   A 31  ? 0.3271 0.3179 0.4305 -0.0077 -0.0427 -0.0216 31  LYS   A CE  
894  C CE  B LYS   A 31  ? 0.3438 0.3195 0.4545 0.0206  -0.0645 -0.0501 31  LYS   A CE  
895  N NZ  A LYS   A 31  ? 0.3325 0.3223 0.4523 -0.0024 -0.0505 -0.0242 31  LYS   A NZ  
896  N NZ  B LYS   A 31  ? 0.3588 0.3329 0.4887 0.0181  -0.0676 -0.0568 31  LYS   A NZ  
923  N N   A PRO   A 32  ? 0.1988 0.1957 0.1111 -0.0345 -0.0131 0.0369  32  PRO   A N   
924  N N   B PRO   A 32  ? 0.1761 0.2026 0.1167 0.0122  0.0125  0.0311  32  PRO   A N   
925  C CA  A PRO   A 32  ? 0.1927 0.1838 0.1332 -0.0364 -0.0143 0.0366  32  PRO   A CA  
926  C CA  B PRO   A 32  ? 0.1755 0.1933 0.1286 0.0082  0.0138  0.0348  32  PRO   A CA  
927  C C   A PRO   A 32  ? 0.1876 0.1760 0.1275 -0.0258 -0.0244 0.0372  32  PRO   A C   
928  C C   B PRO   A 32  ? 0.1806 0.1930 0.1354 0.0087  0.0085  0.0355  32  PRO   A C   
929  O O   A PRO   A 32  ? 0.1836 0.1701 0.1206 -0.0372 -0.0204 0.0270  32  PRO   A O   
930  O O   B PRO   A 32  ? 0.1834 0.1951 0.1546 0.0031  0.0010  0.0311  32  PRO   A O   
931  C CB  A PRO   A 32  ? 0.1944 0.1927 0.1518 -0.0381 -0.0120 0.0251  32  PRO   A CB  
932  C CB  B PRO   A 32  ? 0.1725 0.2015 0.1540 0.0068  0.0114  0.0187  32  PRO   A CB  
933  C CG  A PRO   A 32  ? 0.1962 0.2001 0.1315 -0.0349 -0.0157 0.0234  32  PRO   A CG  
934  C CG  B PRO   A 32  ? 0.1722 0.2093 0.1299 0.0077  0.0090  0.0188  32  PRO   A CG  
935  C CD  A PRO   A 32  ? 0.1947 0.1951 0.1180 -0.0353 -0.0161 0.0358  32  PRO   A CD  
936  C CD  B PRO   A 32  ? 0.1678 0.2056 0.1205 0.0112  0.0130  0.0293  32  PRO   A CD  
951  N N   A THR   A 33  ? 0.1891 0.1751 0.1262 -0.0132 -0.0309 0.0392  33  THR   A N   
952  N N   B THR   A 33  ? 0.1877 0.1883 0.1366 0.0092  0.0069  0.0383  33  THR   A N   
953  C CA  A THR   A 33  ? 0.1930 0.1807 0.1372 -0.0020 -0.0329 0.0333  33  THR   A CA  
954  C CA  B THR   A 33  ? 0.1921 0.1884 0.1347 0.0152  -0.0129 0.0406  33  THR   A CA  
955  C C   A THR   A 33  ? 0.1738 0.1726 0.1386 -0.0069 -0.0311 0.0309  33  THR   A C   
956  C C   B THR   A 33  ? 0.1711 0.1717 0.1414 0.0032  -0.0179 0.0315  33  THR   A C   
957  O O   A THR   A 33  ? 0.1673 0.1634 0.1365 -0.0043 -0.0419 0.0360  33  THR   A O   
958  O O   B THR   A 33  ? 0.1640 0.1656 0.1596 0.0010  -0.0175 0.0244  33  THR   A O   
959  C CB  A THR   A 33  ? 0.2152 0.1949 0.1623 0.0132  -0.0257 0.0349  33  THR   A CB  
960  C CB  B THR   A 33  ? 0.2176 0.2122 0.1537 0.0282  -0.0176 0.0614  33  THR   A CB  
961  O OG1 A THR   A 33  ? 0.2325 0.1989 0.1946 0.0250  -0.0167 0.0400  33  THR   A OG1 
962  O OG1 B THR   A 33  ? 0.2372 0.2291 0.1848 0.0347  -0.0175 0.0803  33  THR   A OG1 
963  C CG2 A THR   A 33  ? 0.2184 0.2000 0.1614 0.0202  -0.0292 0.0335  33  THR   A CG2 
964  C CG2 B THR   A 33  ? 0.2215 0.2191 0.1678 0.0338  -0.0204 0.0551  33  THR   A CG2 
979  N N   . VAL   A 34  ? 0.1586 0.1672 0.1328 -0.0104 -0.0151 0.0319  34  VAL   A N   
980  C CA  . VAL   A 34  ? 0.1451 0.1561 0.1272 -0.0109 -0.0112 0.0288  34  VAL   A CA  
981  C C   . VAL   A 34  ? 0.1366 0.1482 0.1179 -0.0141 -0.0049 0.0226  34  VAL   A C   
982  O O   . VAL   A 34  ? 0.1380 0.1505 0.1438 -0.0211 -0.0070 0.0296  34  VAL   A O   
983  C CB  . VAL   A 34  ? 0.1489 0.1579 0.1394 -0.0162 -0.0035 0.0235  34  VAL   A CB  
984  C CG1 . VAL   A 34  ? 0.1618 0.1656 0.1374 -0.0124 0.0022  0.0121  34  VAL   A CG1 
985  C CG2 . VAL   A 34  ? 0.1569 0.1720 0.1676 -0.0074 -0.0016 0.0226  34  VAL   A CG2 
996  N N   . VAL   A 35  ? 0.1311 0.1387 0.1213 -0.0175 -0.0107 0.0252  35  VAL   A N   
997  C CA  . VAL   A 35  ? 0.1228 0.1386 0.1225 -0.0089 -0.0014 0.0174  35  VAL   A CA  
998  C C   . VAL   A 35  ? 0.1181 0.1263 0.1092 -0.0083 0.0031  0.0210  35  VAL   A C   
999  O O   . VAL   A 35  ? 0.1144 0.1406 0.1301 -0.0159 0.0024  0.0134  35  VAL   A O   
1000 C CB  . VAL   A 35  ? 0.1307 0.1476 0.1268 -0.0066 0.0061  0.0139  35  VAL   A CB  
1001 C CG1 . VAL   A 35  ? 0.1391 0.1456 0.1301 0.0013  0.0037  0.0049  35  VAL   A CG1 
1002 C CG2 . VAL   A 35  ? 0.1335 0.1484 0.1597 -0.0036 0.0147  0.0109  35  VAL   A CG2 
1012 N N   . VAL   A 36  ? 0.1093 0.1270 0.1118 -0.0102 0.0042  0.0227  36  VAL   A N   
1013 C CA  . VAL   A 36  ? 0.1073 0.1190 0.1122 -0.0079 0.0047  0.0179  36  VAL   A CA  
1014 C C   . VAL   A 36  ? 0.1049 0.1225 0.1123 -0.0106 0.0051  0.0155  36  VAL   A C   
1015 O O   . VAL   A 36  ? 0.1044 0.1235 0.1384 -0.0008 0.0107  0.0255  36  VAL   A O   
1016 C CB  . VAL   A 36  ? 0.1054 0.1160 0.1247 -0.0095 0.0048  0.0203  36  VAL   A CB  
1017 C CG1 . VAL   A 36  ? 0.1102 0.1222 0.1273 -0.0112 0.0009  0.0073  36  VAL   A CG1 
1018 C CG2 . VAL   A 36  ? 0.1162 0.1174 0.1345 -0.0043 0.0020  0.0233  36  VAL   A CG2 
1028 N N   A ASN   A 37  ? 0.0951 0.1108 0.1216 -0.0005 -0.0063 0.0163  37  ASN   A N   
1029 N N   B ASN   A 37  ? 0.1075 0.1099 0.1013 -0.0029 0.0007  0.0194  37  ASN   A N   
1030 C CA  A ASN   A 37  ? 0.0976 0.1143 0.1142 0.0036  -0.0010 0.0226  37  ASN   A CA  
1031 C CA  B ASN   A 37  ? 0.1045 0.1059 0.1064 -0.0048 0.0088  0.0156  37  ASN   A CA  
1032 C C   A ASN   A 37  ? 0.0995 0.1169 0.0948 -0.0030 0.0081  0.0239  37  ASN   A C   
1033 C C   B ASN   A 37  ? 0.1082 0.0954 0.1197 -0.0016 0.0096  0.0118  37  ASN   A C   
1034 O O   A ASN   A 37  ? 0.1094 0.1251 0.0935 0.0026  0.0052  0.0086  37  ASN   A O   
1035 O O   B ASN   A 37  ? 0.1205 0.0997 0.1258 0.0064  0.0064  0.0106  37  ASN   A O   
1036 C CB  A ASN   A 37  ? 0.1028 0.1107 0.1039 0.0053  -0.0057 0.0126  37  ASN   A CB  
1037 C CB  B ASN   A 37  ? 0.1096 0.1081 0.1208 -0.0020 0.0035  0.0078  37  ASN   A CB  
1038 C CG  A ASN   A 37  ? 0.1094 0.1055 0.0855 0.0051  -0.0067 -0.0004 37  ASN   A CG  
1039 C CG  B ASN   A 37  ? 0.1099 0.1120 0.1104 -0.0019 0.0083  0.0049  37  ASN   A CG  
1040 O OD1 A ASN   A 37  ? 0.1110 0.1036 0.0891 0.0079  -0.0025 0.0066  37  ASN   A OD1 
1041 O OD1 B ASN   A 37  ? 0.1118 0.1131 0.1139 -0.0055 0.0082  0.0114  37  ASN   A OD1 
1042 N ND2 A ASN   A 37  ? 0.1078 0.0994 0.0891 -0.0006 -0.0134 0.0059  37  ASN   A ND2 
1043 N ND2 B ASN   A 37  ? 0.1083 0.1041 0.1292 -0.0003 0.0069  0.0154  37  ASN   A ND2 
1056 N N   A ALA   A 38  ? 0.1014 0.1180 0.1076 -0.0055 0.0078  0.0156  38  ALA   A N   
1057 N N   B ALA   A 38  ? 0.1118 0.0960 0.1194 0.0054  0.0038  0.0001  38  ALA   A N   
1058 C CA  A ALA   A 38  ? 0.1097 0.1063 0.1090 -0.0037 0.0036  -0.0052 38  ALA   A CA  
1059 C CA  B ALA   A 38  ? 0.1157 0.1112 0.1280 -0.0032 -0.0052 0.0015  38  ALA   A CA  
1060 C C   A ALA   A 38  ? 0.1095 0.1092 0.1159 0.0030  -0.0004 0.0014  38  ALA   A C   
1061 C C   B ALA   A 38  ? 0.1148 0.1136 0.1159 -0.0044 -0.0127 0.0079  38  ALA   A C   
1062 O O   A ALA   A 38  ? 0.1150 0.1008 0.1156 0.0016  -0.0168 -0.0092 38  ALA   A O   
1063 O O   B ALA   A 38  ? 0.1227 0.1150 0.1142 -0.0004 -0.0124 0.0103  38  ALA   A O   
1064 C CB  A ALA   A 38  ? 0.1143 0.1100 0.1142 -0.0068 -0.0016 -0.0095 38  ALA   A CB  
1065 C CB  B ALA   A 38  ? 0.1188 0.1149 0.1222 -0.0062 0.0013  -0.0090 38  ALA   A CB  
1076 N N   A ALA   A 39  ? 0.1119 0.1133 0.1286 0.0032  0.0055  0.0123  39  ALA   A N   
1077 N N   B ALA   A 39  ? 0.1242 0.1230 0.1390 -0.0036 0.0006  0.0197  39  ALA   A N   
1078 C CA  A ALA   A 39  ? 0.1079 0.1163 0.1273 0.0043  0.0148  0.0180  39  ALA   A CA  
1079 C CA  B ALA   A 39  ? 0.1175 0.1214 0.1302 -0.0065 0.0050  0.0107  39  ALA   A CA  
1080 C C   A ALA   A 39  ? 0.1157 0.1200 0.1235 0.0022  0.0071  0.0152  39  ALA   A C   
1081 C C   B ALA   A 39  ? 0.1219 0.1109 0.1312 -0.0043 -0.0051 0.0077  39  ALA   A C   
1082 O O   A ALA   A 39  ? 0.1233 0.1241 0.1257 -0.0049 0.0148  0.0172  39  ALA   A O   
1083 O O   B ALA   A 39  ? 0.1424 0.1099 0.1403 -0.0071 -0.0059 0.0012  39  ALA   A O   
1084 C CB  A ALA   A 39  ? 0.1045 0.1289 0.1324 0.0052  0.0042  0.0177  39  ALA   A CB  
1085 C CB  B ALA   A 39  ? 0.1224 0.1418 0.1293 -0.0121 -0.0022 0.0066  39  ALA   A CB  
1096 N N   A ASN   A 40  ? 0.1129 0.1254 0.1257 -0.0025 0.0090  0.0099  40  ASN   A N   
1097 N N   B ASN   A 40  ? 0.1205 0.1063 0.1128 -0.0047 0.0070  0.0100  40  ASN   A N   
1098 C CA  A ASN   A 40  ? 0.1165 0.1230 0.1164 -0.0068 -0.0043 0.0041  40  ASN   A CA  
1099 C CA  B ASN   A 40  ? 0.1227 0.1040 0.1134 -0.0013 -0.0024 0.0141  40  ASN   A CA  
1100 C C   A ASN   A 40  ? 0.1227 0.1166 0.1121 -0.0040 -0.0049 0.0161  40  ASN   A C   
1101 C C   B ASN   A 40  ? 0.1176 0.0992 0.1039 -0.0042 0.0086  0.0201  40  ASN   A C   
1102 O O   A ASN   A 40  ? 0.1254 0.1196 0.1250 -0.0050 -0.0056 0.0118  40  ASN   A O   
1103 O O   B ASN   A 40  ? 0.1109 0.1043 0.1035 -0.0074 0.0067  0.0158  40  ASN   A O   
1104 C CB  A ASN   A 40  ? 0.1272 0.1394 0.1312 0.0010  -0.0185 0.0047  40  ASN   A CB  
1105 C CB  B ASN   A 40  ? 0.1275 0.1132 0.1177 -0.0003 -0.0080 0.0189  40  ASN   A CB  
1106 C CG  A ASN   A 40  ? 0.1463 0.1429 0.1549 0.0084  -0.0201 0.0066  40  ASN   A CG  
1107 C CG  B ASN   A 40  ? 0.1321 0.1106 0.1273 -0.0005 -0.0073 0.0218  40  ASN   A CG  
1108 O OD1 A ASN   A 40  ? 0.1535 0.1380 0.1468 0.0153  -0.0322 0.0089  40  ASN   A OD1 
1109 O OD1 B ASN   A 40  ? 0.1354 0.1142 0.1451 -0.0081 0.0076  0.0113  40  ASN   A OD1 
1110 N ND2 A ASN   A 40  ? 0.1534 0.1575 0.1833 0.0129  -0.0137 -0.0062 40  ASN   A ND2 
1111 N ND2 B ASN   A 40  ? 0.1337 0.1243 0.1562 0.0003  -0.0059 -0.0043 40  ASN   A ND2 
1124 N N   A VAL   A 41  ? 0.1209 0.1221 0.1038 -0.0054 -0.0073 0.0113  41  VAL   A N   
1125 N N   B VAL   A 41  ? 0.1233 0.1140 0.1069 -0.0043 0.0046  0.0181  41  VAL   A N   
1126 C CA  A VAL   A 41  ? 0.1196 0.1171 0.1156 -0.0029 0.0011  0.0125  41  VAL   A CA  
1127 C CA  B VAL   A 41  ? 0.1240 0.1188 0.1189 -0.0044 0.0084  0.0228  41  VAL   A CA  
1128 C C   A VAL   A 41  ? 0.1185 0.1134 0.1204 -0.0027 0.0001  0.0184  41  VAL   A C   
1129 C C   B VAL   A 41  ? 0.1201 0.1141 0.1167 -0.0042 0.0138  0.0182  41  VAL   A C   
1130 O O   A VAL   A 41  ? 0.1267 0.1147 0.1160 0.0007  -0.0130 0.0156  41  VAL   A O   
1131 O O   B VAL   A 41  ? 0.1324 0.1142 0.0951 -0.0000 0.0109  0.0113  41  VAL   A O   
1132 C CB  A VAL   A 41  ? 0.1199 0.1144 0.0977 -0.0044 0.0016  0.0073  41  VAL   A CB  
1133 C CB  B VAL   A 41  ? 0.1381 0.1413 0.1432 -0.0027 0.0181  0.0210  41  VAL   A CB  
1134 C CG1 A VAL   A 41  ? 0.1254 0.1156 0.1138 -0.0049 -0.0001 0.0087  41  VAL   A CG1 
1135 C CG1 B VAL   A 41  ? 0.1564 0.1503 0.1580 -0.0024 0.0290  0.0087  41  VAL   A CG1 
1136 C CG2 A VAL   A 41  ? 0.1150 0.1126 0.0913 0.0036  0.0044  0.0021  41  VAL   A CG2 
1137 C CG2 B VAL   A 41  ? 0.1480 0.1528 0.1437 -0.0101 0.0099  0.0163  41  VAL   A CG2 
1156 N N   A TYR   A 42  ? 0.1092 0.1103 0.1469 -0.0016 0.0053  0.0216  42  TYR   A N   
1157 N N   B TYR   A 42  ? 0.1107 0.1102 0.1373 0.0007  0.0209  0.0224  42  TYR   A N   
1158 C CA  A TYR   A 42  ? 0.1145 0.1085 0.1481 -0.0100 0.0008  0.0246  42  TYR   A CA  
1159 C CA  B TYR   A 42  ? 0.1089 0.1124 0.1440 -0.0020 0.0255  0.0207  42  TYR   A CA  
1160 C C   A TYR   A 42  ? 0.1140 0.1046 0.1499 -0.0042 0.0034  0.0185  42  TYR   A C   
1161 C C   B TYR   A 42  ? 0.1124 0.1190 0.1375 -0.0014 0.0210  0.0264  42  TYR   A C   
1162 O O   A TYR   A 42  ? 0.1189 0.1040 0.1586 -0.0112 -0.0037 0.0015  42  TYR   A O   
1163 O O   B TYR   A 42  ? 0.1135 0.1243 0.1495 -0.0100 0.0224  0.0166  42  TYR   A O   
1164 C CB  A TYR   A 42  ? 0.1248 0.1276 0.1407 -0.0096 0.0121  0.0318  42  TYR   A CB  
1165 C CB  B TYR   A 42  ? 0.1176 0.1157 0.1504 0.0014  0.0240  0.0284  42  TYR   A CB  
1166 C CG  A TYR   A 42  ? 0.1284 0.1413 0.1330 -0.0108 0.0052  0.0372  42  TYR   A CG  
1167 C CG  B TYR   A 42  ? 0.1277 0.1266 0.1482 0.0055  0.0081  0.0363  42  TYR   A CG  
1168 C CD1 A TYR   A 42  ? 0.1320 0.1503 0.1397 -0.0111 0.0037  0.0308  42  TYR   A CD1 
1169 C CD1 B TYR   A 42  ? 0.1336 0.1346 0.1508 -0.0009 0.0161  0.0390  42  TYR   A CD1 
1170 C CD2 A TYR   A 42  ? 0.1245 0.1531 0.1361 -0.0051 0.0056  0.0347  42  TYR   A CD2 
1171 C CD2 B TYR   A 42  ? 0.1432 0.1497 0.1708 0.0032  0.0004  0.0266  42  TYR   A CD2 
1172 C CE1 A TYR   A 42  ? 0.1339 0.1538 0.1323 -0.0103 0.0017  0.0269  42  TYR   A CE1 
1173 C CE1 B TYR   A 42  ? 0.1396 0.1465 0.1545 -0.0082 0.0185  0.0389  42  TYR   A CE1 
1174 C CE2 A TYR   A 42  ? 0.1281 0.1594 0.1476 -0.0073 0.0024  0.0355  42  TYR   A CE2 
1175 C CE2 B TYR   A 42  ? 0.1560 0.1636 0.1793 0.0030  0.0005  0.0320  42  TYR   A CE2 
1176 C CZ  A TYR   A 42  ? 0.1399 0.1609 0.1336 -0.0061 -0.0035 0.0268  42  TYR   A CZ  
1177 C CZ  B TYR   A 42  ? 0.1589 0.1610 0.1630 -0.0007 0.0105  0.0245  42  TYR   A CZ  
1178 O OH  A TYR   A 42  ? 0.1536 0.1765 0.1494 -0.0032 -0.0008 0.0193  42  TYR   A OH  
1179 O OH  B TYR   A 42  ? 0.1737 0.1816 0.1718 -0.0020 0.0042  0.0197  42  TYR   A OH  
1198 N N   A LEU   A 43  ? 0.1152 0.1058 0.1331 -0.0054 0.0020  0.0039  43  LEU   A N   
1199 N N   B LEU   A 43  ? 0.1119 0.1184 0.1336 -0.0041 0.0163  0.0144  43  LEU   A N   
1200 C CA  A LEU   A 43  ? 0.1118 0.1130 0.1322 -0.0051 0.0030  0.0082  43  LEU   A CA  
1201 C CA  B LEU   A 43  ? 0.1095 0.1180 0.1284 -0.0065 0.0089  0.0176  43  LEU   A CA  
1202 C C   A LEU   A 43  ? 0.1139 0.1161 0.1310 -0.0046 0.0050  0.0042  43  LEU   A C   
1203 C C   B LEU   A 43  ? 0.1131 0.1203 0.1200 -0.0105 -0.0028 0.0085  43  LEU   A C   
1204 O O   A LEU   A 43  ? 0.1298 0.1175 0.1454 0.0013  -0.0015 0.0068  43  LEU   A O   
1205 O O   B LEU   A 43  ? 0.1371 0.1218 0.1239 -0.0052 -0.0125 0.0107  43  LEU   A O   
1206 C CB  A LEU   A 43  ? 0.1161 0.1171 0.1382 -0.0068 0.0011  0.0032  43  LEU   A CB  
1207 C CB  B LEU   A 43  ? 0.1122 0.1092 0.1418 -0.0075 0.0047  0.0103  43  LEU   A CB  
1208 C CG  A LEU   A 43  ? 0.1205 0.1241 0.1383 -0.0088 -0.0019 0.0045  43  LEU   A CG  
1209 C CG  B LEU   A 43  ? 0.1172 0.1105 0.1526 -0.0012 0.0094  0.0105  43  LEU   A CG  
1210 C CD1 A LEU   A 43  ? 0.1223 0.1326 0.1451 -0.0088 -0.0012 0.0156  43  LEU   A CD1 
1211 C CD1 B LEU   A 43  ? 0.1233 0.1174 0.1713 -0.0010 0.0082  0.0133  43  LEU   A CD1 
1212 C CD2 A LEU   A 43  ? 0.1237 0.1255 0.1370 -0.0112 -0.0072 0.0096  43  LEU   A CD2 
1213 C CD2 B LEU   A 43  ? 0.1296 0.1092 0.1550 -0.0061 0.0032  0.0307  43  LEU   A CD2 
1236 N N   A LYS   A 44  ? 0.1237 0.1155 0.1354 -0.0017 0.0152  0.0099  44  LYS   A N   
1237 N N   B LYS   A 44  ? 0.1147 0.1154 0.1223 -0.0018 -0.0009 0.0114  44  LYS   A N   
1238 C CA  A LYS   A 44  ? 0.1318 0.1175 0.1462 -0.0100 0.0180  0.0182  44  LYS   A CA  
1239 C CA  B LYS   A 44  ? 0.1305 0.1133 0.1282 -0.0025 -0.0052 0.0159  44  LYS   A CA  
1240 C C   A LYS   A 44  ? 0.1222 0.1178 0.1359 -0.0035 0.0065  0.0111  44  LYS   A C   
1241 C C   B LYS   A 44  ? 0.1199 0.1103 0.1268 0.0022  -0.0105 0.0143  44  LYS   A C   
1242 O O   A LYS   A 44  ? 0.1288 0.1332 0.1488 -0.0045 0.0002  -0.0031 44  LYS   A O   
1243 O O   B LYS   A 44  ? 0.1227 0.1241 0.1388 0.0003  -0.0076 -0.0075 44  LYS   A O   
1244 C CB  A LYS   A 44  ? 0.1474 0.1245 0.1691 -0.0144 0.0248  0.0399  44  LYS   A CB  
1245 C CB  B LYS   A 44  ? 0.1604 0.1346 0.1681 0.0125  0.0098  0.0232  44  LYS   A CB  
1246 C CG  A LYS   A 44  ? 0.1701 0.1424 0.2027 -0.0164 0.0429  0.0585  44  LYS   A CG  
1247 C CG  B LYS   A 44  ? 0.1809 0.1658 0.2328 0.0205  0.0301  0.0304  44  LYS   A CG  
1248 C CD  A LYS   A 44  ? 0.1994 0.1866 0.2848 -0.0114 0.0417  0.0416  44  LYS   A CD  
1249 C CD  B LYS   A 44  ? 0.1994 0.2107 0.3161 0.0179  0.0325  0.0286  44  LYS   A CD  
1250 C CE  A LYS   A 44  ? 0.2179 0.2162 0.3358 -0.0023 0.0428  0.0257  44  LYS   A CE  
1251 C CE  B LYS   A 44  ? 0.2099 0.2415 0.3714 0.0094  0.0285  0.0287  44  LYS   A CE  
1252 N NZ  A LYS   A 44  ? 0.2250 0.2353 0.3573 0.0044  0.0440  0.0131  44  LYS   A NZ  
1253 N NZ  B LYS   A 44  ? 0.2218 0.2674 0.4066 -0.0033 0.0190  0.0243  44  LYS   A NZ  
1280 N N   A HIS   A 45  ? 0.1103 0.1129 0.1289 -0.0028 0.0118  0.0095  45  HIS   A N   
1281 N N   B HIS   A 45  ? 0.1151 0.1056 0.1323 -0.0022 -0.0143 0.0138  45  HIS   A N   
1282 C CA  A HIS   A 45  ? 0.1057 0.1133 0.1217 0.0003  0.0100  0.0078  45  HIS   A CA  
1283 C CA  B HIS   A 45  ? 0.1189 0.1107 0.1440 0.0004  -0.0094 0.0095  45  HIS   A CA  
1284 C C   A HIS   A 45  ? 0.1019 0.1197 0.1207 -0.0018 0.0089  0.0110  45  HIS   A C   
1285 C C   B HIS   A 45  ? 0.1287 0.1210 0.1452 0.0009  -0.0093 0.0099  45  HIS   A C   
1286 O O   A HIS   A 45  ? 0.1073 0.1195 0.1379 -0.0069 0.0097  0.0024  45  HIS   A O   
1287 O O   B HIS   A 45  ? 0.1424 0.1264 0.1640 0.0084  -0.0058 0.0006  45  HIS   A O   
1288 C CB  A HIS   A 45  ? 0.1114 0.1096 0.1088 -0.0003 0.0072  0.0049  45  HIS   A CB  
1289 C CB  B HIS   A 45  ? 0.1183 0.1099 0.1435 -0.0041 -0.0102 0.0066  45  HIS   A CB  
1290 C CG  A HIS   A 45  ? 0.1136 0.1005 0.0979 -0.0064 0.0044  0.0079  45  HIS   A CG  
1291 C CG  B HIS   A 45  ? 0.1090 0.1134 0.1349 -0.0045 -0.0016 0.0046  45  HIS   A CG  
1292 N ND1 A HIS   A 45  ? 0.1127 0.1058 0.1002 -0.0074 -0.0005 0.0043  45  HIS   A ND1 
1293 N ND1 B HIS   A 45  ? 0.1048 0.1175 0.1445 -0.0008 -0.0055 0.0079  45  HIS   A ND1 
1294 C CD2 A HIS   A 45  ? 0.1207 0.1096 0.1154 -0.0110 -0.0003 0.0128  45  HIS   A CD2 
1295 C CD2 B HIS   A 45  ? 0.1007 0.1094 0.1256 -0.0078 -0.0059 0.0022  45  HIS   A CD2 
1296 C CE1 A HIS   A 45  ? 0.1175 0.1139 0.1188 -0.0071 0.0014  0.0117  45  HIS   A CE1 
1297 C CE1 B HIS   A 45  ? 0.1016 0.1066 0.1135 -0.0045 -0.0069 0.0075  45  HIS   A CE1 
1298 N NE2 A HIS   A 45  ? 0.1247 0.1167 0.1292 -0.0027 0.0046  0.0203  45  HIS   A NE2 
1299 N NE2 B HIS   A 45  ? 0.1022 0.1050 0.1087 -0.0034 -0.0038 0.0032  45  HIS   A NE2 
1314 N N   A GLY   A 46  ? 0.1046 0.1257 0.1321 0.0063  -0.0047 0.0197  46  GLY   A N   
1315 N N   B GLY   A 46  ? 0.1297 0.1228 0.1514 -0.0014 -0.0211 0.0168  46  GLY   A N   
1316 C CA  A GLY   A 46  ? 0.1116 0.1255 0.1418 0.0048  -0.0096 0.0244  46  GLY   A CA  
1317 C CA  B GLY   A 46  ? 0.1354 0.1262 0.1639 -0.0005 -0.0122 0.0178  46  GLY   A CA  
1318 C C   A GLY   A 46  ? 0.1178 0.1180 0.1289 0.0062  -0.0138 0.0330  46  GLY   A C   
1319 C C   B GLY   A 46  ? 0.1315 0.1221 0.1385 0.0063  -0.0102 0.0213  46  GLY   A C   
1320 O O   A GLY   A 46  ? 0.1232 0.1126 0.1267 0.0109  -0.0216 0.0424  46  GLY   A O   
1321 O O   B GLY   A 46  ? 0.1413 0.1297 0.1585 0.0028  -0.0135 0.0121  46  GLY   A O   
1328 N N   A GLY   A 47  ? 0.1149 0.1209 0.1398 0.0044  -0.0049 0.0216  47  GLY   A N   
1329 N N   B GLY   A 47  ? 0.1295 0.1249 0.1407 0.0083  0.0001  0.0111  47  GLY   A N   
1330 C CA  A GLY   A 47  ? 0.1124 0.1224 0.1248 0.0110  0.0011  0.0092  47  GLY   A CA  
1331 C CA  B GLY   A 47  ? 0.1222 0.1225 0.1369 0.0085  -0.0154 0.0176  47  GLY   A CA  
1332 C C   A GLY   A 47  ? 0.1123 0.1193 0.1275 0.0090  0.0045  0.0013  47  GLY   A C   
1333 C C   B GLY   A 47  ? 0.1138 0.1137 0.1277 0.0089  -0.0122 0.0121  47  GLY   A C   
1334 O O   A GLY   A 47  ? 0.1171 0.1185 0.1433 0.0155  0.0094  0.0007  47  GLY   A O   
1335 O O   B GLY   A 47  ? 0.1105 0.1114 0.1457 0.0153  -0.0115 0.0155  47  GLY   A O   
1342 N N   A GLY   A 48  ? 0.1041 0.1191 0.1268 0.0109  0.0046  -0.0039 48  GLY   A N   
1343 N N   B GLY   A 48  ? 0.1136 0.1186 0.1370 0.0073  -0.0071 0.0064  48  GLY   A N   
1344 C CA  A GLY   A 48  ? 0.1014 0.1216 0.1312 0.0043  0.0035  -0.0007 48  GLY   A CA  
1345 C CA  B GLY   A 48  ? 0.1093 0.1125 0.1435 0.0041  -0.0085 -0.0062 48  GLY   A CA  
1346 C C   A GLY   A 48  ? 0.1084 0.1216 0.1133 -0.0040 0.0042  0.0034  48  GLY   A C   
1347 C C   B GLY   A 48  ? 0.1105 0.1127 0.1465 -0.0048 -0.0053 -0.0003 48  GLY   A C   
1348 O O   A GLY   A 48  ? 0.1171 0.1270 0.1014 -0.0085 -0.0032 0.0102  48  GLY   A O   
1349 O O   B GLY   A 48  ? 0.1256 0.1122 0.1410 0.0006  0.0018  -0.0001 48  GLY   A O   
1356 N N   A VAL   A 49  ? 0.1209 0.1153 0.1355 -0.0055 -0.0016 0.0096  49  VAL   A N   
1357 N N   B VAL   A 49  ? 0.1077 0.1112 0.1619 -0.0063 -0.0116 -0.0001 49  VAL   A N   
1358 C CA  A VAL   A 49  ? 0.1308 0.1124 0.1422 -0.0049 0.0071  0.0087  49  VAL   A CA  
1359 C CA  B VAL   A 49  ? 0.1067 0.1160 0.1497 -0.0053 -0.0060 0.0131  49  VAL   A CA  
1360 C C   A VAL   A 49  ? 0.1267 0.1064 0.1255 -0.0035 0.0034  0.0197  49  VAL   A C   
1361 C C   B VAL   A 49  ? 0.1124 0.1091 0.1250 0.0063  -0.0011 0.0147  49  VAL   A C   
1362 O O   A VAL   A 49  ? 0.1289 0.1123 0.1307 -0.0114 0.0071  0.0071  49  VAL   A O   
1363 O O   B VAL   A 49  ? 0.1171 0.1163 0.1194 0.0015  0.0029  0.0097  49  VAL   A O   
1364 C CB  A VAL   A 49  ? 0.1438 0.1162 0.1673 -0.0077 0.0123  0.0042  49  VAL   A CB  
1365 C CB  B VAL   A 49  ? 0.1003 0.1122 0.1544 -0.0011 -0.0054 0.0167  49  VAL   A CB  
1366 C CG1 A VAL   A 49  ? 0.1457 0.1060 0.1817 -0.0011 0.0148  0.0051  49  VAL   A CG1 
1367 C CG1 B VAL   A 49  ? 0.1033 0.1126 0.1390 0.0101  -0.0001 0.0154  49  VAL   A CG1 
1368 C CG2 A VAL   A 49  ? 0.1493 0.1234 0.1898 -0.0089 0.0219  -0.0072 49  VAL   A CG2 
1369 C CG2 B VAL   A 49  ? 0.1032 0.1061 0.1685 0.0061  -0.0027 0.0162  49  VAL   A CG2 
1388 N N   A ALA   A 50  ? 0.1171 0.1019 0.1188 -0.0059 -0.0130 0.0225  50  ALA   A N   
1389 N N   B ALA   A 50  ? 0.1078 0.1054 0.1230 0.0044  -0.0072 0.0092  50  ALA   A N   
1390 C CA  A ALA   A 50  ? 0.1123 0.0993 0.1146 -0.0116 -0.0178 0.0253  50  ALA   A CA  
1391 C CA  B ALA   A 50  ? 0.1100 0.1088 0.1199 0.0002  -0.0007 0.0048  50  ALA   A CA  
1392 C C   A ALA   A 50  ? 0.1081 0.1005 0.1148 -0.0072 -0.0155 0.0210  50  ALA   A C   
1393 C C   B ALA   A 50  ? 0.1090 0.1156 0.1193 -0.0020 0.0007  0.0044  50  ALA   A C   
1394 O O   A ALA   A 50  ? 0.1065 0.1002 0.1176 -0.0074 -0.0153 0.0221  50  ALA   A O   
1395 O O   B ALA   A 50  ? 0.1115 0.1193 0.1315 -0.0053 0.0091  -0.0032 50  ALA   A O   
1396 C CB  A ALA   A 50  ? 0.1098 0.1047 0.1309 -0.0184 -0.0214 0.0228  50  ALA   A CB  
1397 C CB  B ALA   A 50  ? 0.1133 0.1081 0.1294 0.0008  0.0009  -0.0024 50  ALA   A CB  
1408 N N   A GLY   A 51  ? 0.1150 0.0976 0.1234 0.0003  -0.0195 0.0188  51  GLY   A N   
1409 N N   B GLY   A 51  ? 0.1166 0.1104 0.1273 -0.0010 -0.0115 0.0063  51  GLY   A N   
1410 C CA  A GLY   A 51  ? 0.1196 0.0985 0.1415 0.0047  -0.0135 0.0169  51  GLY   A CA  
1411 C CA  B GLY   A 51  ? 0.1181 0.1088 0.1332 -0.0008 -0.0063 0.0056  51  GLY   A CA  
1412 C C   A GLY   A 51  ? 0.1100 0.1054 0.1497 0.0093  -0.0082 0.0090  51  GLY   A C   
1413 C C   B GLY   A 51  ? 0.1045 0.1190 0.1247 0.0026  -0.0089 -0.0017 51  GLY   A C   
1414 O O   A GLY   A 51  ? 0.1194 0.1123 0.1581 0.0025  -0.0105 0.0071  51  GLY   A O   
1415 O O   B GLY   A 51  ? 0.1077 0.1250 0.1256 -0.0049 -0.0094 -0.0088 51  GLY   A O   
1422 N N   A ALA   A 52  ? 0.1061 0.1111 0.1446 0.0054  -0.0040 0.0098  52  ALA   A N   
1423 N N   B ALA   A 52  ? 0.1034 0.1213 0.1176 -0.0054 -0.0065 -0.0048 52  ALA   A N   
1424 C CA  A ALA   A 52  ? 0.1088 0.1183 0.1411 0.0011  0.0005  0.0019  52  ALA   A CA  
1425 C CA  B ALA   A 52  ? 0.1098 0.1274 0.1338 -0.0055 -0.0052 -0.0019 52  ALA   A CA  
1426 C C   A ALA   A 52  ? 0.1077 0.1228 0.1350 -0.0025 0.0050  0.0064  52  ALA   A C   
1427 C C   B ALA   A 52  ? 0.1138 0.1236 0.1212 -0.0095 -0.0013 -0.0037 52  ALA   A C   
1428 O O   A ALA   A 52  ? 0.1166 0.1252 0.1381 0.0010  0.0022  0.0074  52  ALA   A O   
1429 O O   B ALA   A 52  ? 0.1202 0.1314 0.1353 -0.0043 -0.0057 -0.0148 52  ALA   A O   
1430 C CB  A ALA   A 52  ? 0.1122 0.1346 0.1456 -0.0006 -0.0018 0.0052  52  ALA   A CB  
1431 C CB  B ALA   A 52  ? 0.1165 0.1445 0.1555 0.0011  0.0001  0.0051  52  ALA   A CB  
1442 N N   A LEU   A 53  ? 0.1049 0.1280 0.1275 0.0031  0.0040  0.0098  53  LEU   A N   
1443 N N   B LEU   A 53  ? 0.1132 0.1159 0.1141 -0.0106 -0.0043 -0.0022 53  LEU   A N   
1444 C CA  A LEU   A 53  ? 0.1134 0.1313 0.1304 0.0014  0.0024  0.0133  53  LEU   A CA  
1445 C CA  B LEU   A 53  ? 0.1171 0.1197 0.1152 -0.0071 0.0001  0.0020  53  LEU   A CA  
1446 C C   A LEU   A 53  ? 0.1130 0.1327 0.1219 0.0018  0.0031  0.0096  53  LEU   A C   
1447 C C   B LEU   A 53  ? 0.1145 0.1162 0.0985 0.0040  0.0009  0.0052  53  LEU   A C   
1448 O O   A LEU   A 53  ? 0.1175 0.1281 0.1308 -0.0027 0.0049  0.0004  53  LEU   A O   
1449 O O   B LEU   A 53  ? 0.1203 0.1135 0.1065 0.0025  -0.0047 0.0074  53  LEU   A O   
1450 C CB  A LEU   A 53  ? 0.1285 0.1338 0.1345 -0.0023 -0.0029 0.0166  53  LEU   A CB  
1451 C CB  B LEU   A 53  ? 0.1265 0.1192 0.1135 -0.0040 -0.0064 0.0090  53  LEU   A CB  
1452 C CG  A LEU   A 53  ? 0.1415 0.1378 0.1437 -0.0155 -0.0063 0.0206  53  LEU   A CG  
1453 C CG  B LEU   A 53  ? 0.1354 0.1246 0.1232 -0.0111 -0.0084 0.0121  53  LEU   A CG  
1454 C CD1 A LEU   A 53  ? 0.1484 0.1393 0.1492 -0.0103 -0.0062 0.0261  53  LEU   A CD1 
1455 C CD1 B LEU   A 53  ? 0.1516 0.1265 0.1371 -0.0061 -0.0167 0.0108  53  LEU   A CD1 
1456 C CD2 A LEU   A 53  ? 0.1554 0.1523 0.1522 -0.0269 -0.0097 0.0132  53  LEU   A CD2 
1457 C CD2 B LEU   A 53  ? 0.1425 0.1392 0.1306 -0.0200 0.0021  0.0052  53  LEU   A CD2 
1480 N N   A ASN   A 54  ? 0.1100 0.1274 0.1227 -0.0036 -0.0099 0.0120  54  ASN   A N   
1481 N N   B ASN   A 54  ? 0.1087 0.1172 0.1046 -0.0013 -0.0022 0.0042  54  ASN   A N   
1482 C CA  A ASN   A 54  ? 0.1095 0.1215 0.1333 -0.0028 -0.0152 0.0059  54  ASN   A CA  
1483 C CA  B ASN   A 54  ? 0.1059 0.1169 0.1241 0.0012  -0.0056 -0.0018 54  ASN   A CA  
1484 C C   A ASN   A 54  ? 0.1137 0.1240 0.1327 -0.0112 -0.0046 0.0050  54  ASN   A C   
1485 C C   B ASN   A 54  ? 0.1123 0.1219 0.1278 -0.0116 0.0013  -0.0023 54  ASN   A C   
1486 O O   A ASN   A 54  ? 0.1174 0.1295 0.1364 -0.0072 -0.0092 0.0034  54  ASN   A O   
1487 O O   B ASN   A 54  ? 0.1174 0.1285 0.1291 -0.0037 -0.0041 -0.0146 54  ASN   A O   
1488 C CB  A ASN   A 54  ? 0.1082 0.1121 0.1384 -0.0093 -0.0188 0.0041  54  ASN   A CB  
1489 C CB  B ASN   A 54  ? 0.1033 0.1115 0.1284 -0.0010 0.0002  0.0005  54  ASN   A CB  
1490 C CG  A ASN   A 54  ? 0.1133 0.1149 0.1389 -0.0062 -0.0173 0.0029  54  ASN   A CG  
1491 C CG  B ASN   A 54  ? 0.1034 0.1160 0.1183 0.0050  0.0087  -0.0023 54  ASN   A CG  
1492 O OD1 A ASN   A 54  ? 0.1116 0.1098 0.1522 -0.0065 -0.0203 0.0108  54  ASN   A OD1 
1493 O OD1 B ASN   A 54  ? 0.1001 0.1138 0.1176 0.0031  0.0011  -0.0071 54  ASN   A OD1 
1494 N ND2 A ASN   A 54  ? 0.1160 0.1169 0.1445 -0.0088 -0.0275 0.0075  54  ASN   A ND2 
1495 N ND2 B ASN   A 54  ? 0.1113 0.1193 0.1355 0.0010  0.0034  0.0028  54  ASN   A ND2 
1508 N N   . LYS   A 55  ? 0.1133 0.1254 0.1324 -0.0021 -0.0029 -0.0002 55  LYS   A N   
1509 C CA  . LYS   A 55  ? 0.1222 0.1314 0.1336 0.0049  -0.0051 -0.0058 55  LYS   A CA  
1510 C C   . LYS   A 55  ? 0.1140 0.1398 0.1401 -0.0002 -0.0066 -0.0092 55  LYS   A C   
1511 O O   . LYS   A 55  ? 0.1275 0.1458 0.1375 0.0068  -0.0115 -0.0190 55  LYS   A O   
1512 C CB  . LYS   A 55  ? 0.1339 0.1420 0.1511 0.0154  -0.0132 -0.0038 55  LYS   A CB  
1513 C CG  . LYS   A 55  ? 0.1535 0.1618 0.1618 0.0305  -0.0306 -0.0245 55  LYS   A CG  
1514 C CD  . LYS   A 55  ? 0.1668 0.1857 0.1853 0.0343  -0.0315 -0.0240 55  LYS   A CD  
1515 C CE  . LYS   A 55  ? 0.1840 0.2172 0.2044 0.0500  -0.0363 -0.0211 55  LYS   A CE  
1516 N NZ  . LYS   A 55  ? 0.1932 0.2306 0.2079 0.0566  -0.0344 -0.0175 55  LYS   A NZ  
1531 N N   . ALA   A 56  ? 0.1273 0.1423 0.1337 -0.0062 -0.0034 -0.0062 56  ALA   A N   
1532 C CA  . ALA   A 56  ? 0.1311 0.1574 0.1305 -0.0081 0.0073  -0.0080 56  ALA   A CA  
1533 C C   . ALA   A 56  ? 0.1377 0.1708 0.1134 -0.0089 0.0053  -0.0091 56  ALA   A C   
1534 O O   . ALA   A 56  ? 0.1447 0.2064 0.1283 0.0046  0.0040  -0.0053 56  ALA   A O   
1535 C CB  . ALA   A 56  ? 0.1429 0.1757 0.1382 -0.0132 0.0128  0.0056  56  ALA   A CB  
1541 N N   . THR   A 57  ? 0.1231 0.1475 0.1162 -0.0027 0.0025  -0.0064 57  THR   A N   
1542 C CA  . THR   A 57  ? 0.1300 0.1496 0.1237 -0.0056 -0.0048 -0.0069 57  THR   A CA  
1543 C C   . THR   A 57  ? 0.1273 0.1540 0.1279 -0.0034 -0.0062 -0.0167 57  THR   A C   
1544 O O   . THR   A 57  ? 0.1316 0.1642 0.1371 -0.0076 -0.0156 -0.0218 57  THR   A O   
1545 C CB  . THR   A 57  ? 0.1287 0.1508 0.1245 -0.0054 -0.0064 -0.0023 57  THR   A CB  
1546 O OG1 . THR   A 57  ? 0.1155 0.1453 0.1232 -0.0061 -0.0060 -0.0048 57  THR   A OG1 
1547 C CG2 . THR   A 57  ? 0.1346 0.1507 0.1211 -0.0074 -0.0017 0.0051  57  THR   A CG2 
1555 N N   . ASN   A 58  ? 0.1323 0.1464 0.1402 -0.0048 -0.0058 -0.0169 58  ASN   A N   
1556 C CA  . ASN   A 58  ? 0.1562 0.1432 0.1708 -0.0052 0.0042  -0.0336 58  ASN   A CA  
1557 C C   . ASN   A 58  ? 0.1342 0.1306 0.1587 -0.0012 -0.0045 -0.0146 58  ASN   A C   
1558 O O   . ASN   A 58  ? 0.1416 0.1452 0.1746 -0.0127 -0.0055 -0.0226 58  ASN   A O   
1559 C CB  . ASN   A 58  ? 0.2137 0.1668 0.2069 -0.0220 0.0374  -0.0408 58  ASN   A CB  
1560 C CG  . ASN   A 58  ? 0.2749 0.1938 0.2945 -0.0269 0.0475  -0.0407 58  ASN   A CG  
1561 O OD1 . ASN   A 58  ? 0.2958 0.1850 0.3450 0.0093  0.0867  -0.0300 58  ASN   A OD1 
1562 N ND2 . ASN   A 58  ? 0.3013 0.2100 0.3189 -0.0421 0.0311  -0.0560 58  ASN   A ND2 
1569 N N   . ASN   A 59  ? 0.1191 0.1261 0.1442 -0.0047 -0.0096 -0.0116 59  ASN   A N   
1570 C CA  . ASN   A 59  ? 0.1218 0.1179 0.1378 -0.0037 -0.0096 -0.0054 59  ASN   A CA  
1571 C C   . ASN   A 59  ? 0.1187 0.1179 0.1343 -0.0105 -0.0039 -0.0029 59  ASN   A C   
1572 O O   . ASN   A 59  ? 0.1175 0.1272 0.1479 -0.0064 -0.0028 0.0080  59  ASN   A O   
1573 C CB  . ASN   A 59  ? 0.1310 0.1169 0.1483 0.0002  -0.0231 -0.0125 59  ASN   A CB  
1574 C CG  . ASN   A 59  ? 0.1278 0.1229 0.1396 -0.0021 -0.0266 -0.0028 59  ASN   A CG  
1575 O OD1 . ASN   A 59  ? 0.1394 0.1278 0.1421 -0.0126 -0.0204 0.0079  59  ASN   A OD1 
1576 N ND2 . ASN   A 59  ? 0.1387 0.1320 0.1593 -0.0162 -0.0220 0.0101  59  ASN   A ND2 
1583 N N   . ALA   A 60  ? 0.1121 0.1264 0.1374 -0.0041 -0.0118 0.0008  60  ALA   A N   
1584 C CA  . ALA   A 60  ? 0.1199 0.1295 0.1417 -0.0036 -0.0124 -0.0023 60  ALA   A CA  
1585 C C   . ALA   A 60  ? 0.1118 0.1269 0.1434 -0.0000 -0.0065 -0.0030 60  ALA   A C   
1586 O O   . ALA   A 60  ? 0.1124 0.1247 0.1615 -0.0054 -0.0099 -0.0035 60  ALA   A O   
1587 C CB  . ALA   A 60  ? 0.1306 0.1351 0.1533 -0.0056 -0.0150 -0.0013 60  ALA   A CB  
1593 N N   . MET   A 61  ? 0.1086 0.1158 0.1351 -0.0037 -0.0045 -0.0041 61  MET   A N   
1594 C CA  . MET   A 61  ? 0.1088 0.1156 0.1303 -0.0010 -0.0077 0.0058  61  MET   A CA  
1595 C C   . MET   A 61  ? 0.1105 0.1139 0.1372 -0.0104 -0.0029 0.0005  61  MET   A C   
1596 O O   . MET   A 61  ? 0.1117 0.1181 0.1463 -0.0016 0.0048  0.0029  61  MET   A O   
1597 C CB  . MET   A 61  ? 0.1146 0.1165 0.1344 -0.0036 0.0019  0.0109  61  MET   A CB  
1598 C CG  . MET   A 61  ? 0.1176 0.1242 0.1481 -0.0024 -0.0079 0.0011  61  MET   A CG  
1599 S SD  . MET   A 61  ? 0.1192 0.1270 0.1640 -0.0098 -0.0059 -0.0129 61  MET   A SD  
1600 C CE  . MET   A 61  ? 0.1328 0.1390 0.1898 -0.0186 0.0108  -0.0126 61  MET   A CE  
1610 N N   . GLN   A 62  ? 0.1098 0.1127 0.1348 -0.0053 -0.0034 -0.0012 62  GLN   A N   
1611 C CA  . GLN   A 62  ? 0.1145 0.1110 0.1323 -0.0081 0.0013  -0.0000 62  GLN   A CA  
1612 C C   . GLN   A 62  ? 0.1212 0.1074 0.1340 -0.0017 0.0048  0.0028  62  GLN   A C   
1613 O O   . GLN   A 62  ? 0.1177 0.1191 0.1444 -0.0090 0.0034  -0.0005 62  GLN   A O   
1614 C CB  . GLN   A 62  ? 0.1144 0.1105 0.1390 -0.0048 0.0005  0.0022  62  GLN   A CB  
1615 C CG  . GLN   A 62  ? 0.1207 0.1114 0.1388 -0.0063 -0.0041 0.0081  62  GLN   A CG  
1616 C CD  . GLN   A 62  ? 0.1232 0.1134 0.1397 0.0002  0.0020  0.0112  62  GLN   A CD  
1617 O OE1 . GLN   A 62  ? 0.1217 0.1257 0.1487 -0.0073 -0.0061 0.0007  62  GLN   A OE1 
1618 N NE2 . GLN   A 62  ? 0.1292 0.1165 0.1488 -0.0003 0.0002  0.0027  62  GLN   A NE2 
1627 N N   . VAL   A 63  ? 0.1156 0.1133 0.1513 -0.0100 0.0057  -0.0122 63  VAL   A N   
1628 C CA  . VAL   A 63  ? 0.1184 0.1233 0.1689 -0.0129 -0.0003 -0.0101 63  VAL   A CA  
1629 C C   . VAL   A 63  ? 0.1064 0.1278 0.1648 -0.0163 -0.0108 -0.0149 63  VAL   A C   
1630 O O   . VAL   A 63  ? 0.1106 0.1244 0.1804 -0.0151 -0.0061 -0.0097 63  VAL   A O   
1631 C CB  . VAL   A 63  ? 0.1258 0.1363 0.1973 -0.0168 0.0007  -0.0297 63  VAL   A CB  
1632 C CG1 . VAL   A 63  ? 0.1388 0.1612 0.2393 -0.0159 -0.0029 -0.0602 63  VAL   A CG1 
1633 C CG2 . VAL   A 63  ? 0.1345 0.1293 0.2228 -0.0155 0.0100  -0.0351 63  VAL   A CG2 
1643 N N   . GLU   A 64  ? 0.1087 0.1278 0.1542 -0.0053 -0.0072 -0.0105 64  GLU   A N   
1644 C CA  . GLU   A 64  ? 0.1091 0.1243 0.1500 -0.0068 -0.0114 -0.0006 64  GLU   A CA  
1645 C C   . GLU   A 64  ? 0.1047 0.1228 0.1574 -0.0104 -0.0012 0.0073  64  GLU   A C   
1646 O O   . GLU   A 64  ? 0.1127 0.1313 0.1546 0.0002  -0.0006 0.0039  64  GLU   A O   
1647 C CB  . GLU   A 64  ? 0.1206 0.1386 0.1538 -0.0076 -0.0060 0.0015  64  GLU   A CB  
1648 C CG  . GLU   A 64  ? 0.1188 0.1418 0.1679 -0.0115 -0.0031 -0.0029 64  GLU   A CG  
1649 C CD  . GLU   A 64  ? 0.1327 0.1450 0.1810 -0.0141 0.0027  0.0020  64  GLU   A CD  
1650 O OE1 . GLU   A 64  ? 0.1406 0.1531 0.1963 -0.0195 0.0032  0.0016  64  GLU   A OE1 
1651 O OE2 . GLU   A 64  ? 0.1467 0.1445 0.1762 -0.0167 -0.0017 0.0126  64  GLU   A OE2 
1658 N N   . SER   A 65  ? 0.1017 0.1213 0.1467 -0.0017 -0.0005 0.0026  65  SER   A N   
1659 C CA  . SER   A 65  ? 0.1075 0.1130 0.1498 -0.0016 -0.0012 -0.0005 65  SER   A CA  
1660 C C   . SER   A 65  ? 0.1075 0.1219 0.1519 -0.0006 -0.0034 -0.0042 65  SER   A C   
1661 O O   . SER   A 65  ? 0.1142 0.1325 0.1673 -0.0030 0.0110  0.0008  65  SER   A O   
1662 C CB  . SER   A 65  ? 0.1081 0.1189 0.1526 -0.0072 -0.0026 0.0067  65  SER   A CB  
1663 O OG  . SER   A 65  ? 0.1116 0.1238 0.1529 -0.0100 -0.0075 0.0136  65  SER   A OG  
1669 N N   . ASP   A 66  ? 0.1131 0.1204 0.1481 -0.0055 0.0056  0.0079  66  ASP   A N   
1670 C CA  . ASP   A 66  ? 0.1227 0.1298 0.1556 -0.0069 0.0025  0.0182  66  ASP   A CA  
1671 C C   . ASP   A 66  ? 0.1193 0.1273 0.1671 -0.0114 0.0090  0.0145  66  ASP   A C   
1672 O O   . ASP   A 66  ? 0.1245 0.1401 0.1837 -0.0075 0.0209  0.0227  66  ASP   A O   
1673 C CB  . ASP   A 66  ? 0.1323 0.1402 0.1783 0.0011  0.0060  0.0331  66  ASP   A CB  
1674 C CG  . ASP   A 66  ? 0.1553 0.1498 0.2088 -0.0017 0.0056  0.0455  66  ASP   A CG  
1675 O OD1 . ASP   A 66  ? 0.1532 0.1824 0.1828 -0.0123 -0.0032 0.0409  66  ASP   A OD1 
1676 O OD2 . ASP   A 66  ? 0.1718 0.1584 0.2814 0.0181  -0.0069 0.0290  66  ASP   A OD2 
1681 N N   . ASP   A 67  ? 0.1120 0.1293 0.1781 -0.0054 0.0043  0.0141  67  ASP   A N   
1682 C CA  . ASP   A 67  ? 0.1130 0.1450 0.1996 -0.0029 0.0010  0.0255  67  ASP   A CA  
1683 C C   . ASP   A 67  ? 0.1156 0.1485 0.1846 0.0030  0.0047  0.0260  67  ASP   A C   
1684 O O   . ASP   A 67  ? 0.1115 0.1579 0.2058 0.0015  0.0241  0.0339  67  ASP   A O   
1685 C CB  . ASP   A 67  ? 0.1202 0.1556 0.2203 -0.0063 -0.0178 0.0297  67  ASP   A CB  
1686 C CG  . ASP   A 67  ? 0.1194 0.1698 0.2545 -0.0103 -0.0336 0.0384  67  ASP   A CG  
1687 O OD1 . ASP   A 67  ? 0.1267 0.1909 0.3450 -0.0202 -0.0449 0.0595  67  ASP   A OD1 
1688 O OD2 . ASP   A 67  ? 0.1258 0.1677 0.2440 -0.0022 -0.0264 0.0272  67  ASP   A OD2 
1693 N N   . TYR   A 68  ? 0.1162 0.1363 0.1807 0.0006  0.0149  0.0251  68  TYR   A N   
1694 C CA  . TYR   A 68  ? 0.1295 0.1305 0.1832 0.0032  0.0207  0.0276  68  TYR   A CA  
1695 C C   . TYR   A 68  ? 0.1200 0.1338 0.1839 -0.0003 0.0226  0.0217  68  TYR   A C   
1696 O O   . TYR   A 68  ? 0.1230 0.1382 0.1961 0.0062  0.0327  0.0211  68  TYR   A O   
1697 C CB  . TYR   A 68  ? 0.1356 0.1311 0.1903 0.0055  0.0386  0.0313  68  TYR   A CB  
1698 C CG  . TYR   A 68  ? 0.1411 0.1465 0.2137 0.0032  0.0519  0.0407  68  TYR   A CG  
1699 C CD1 . TYR   A 68  ? 0.1451 0.1543 0.2344 -0.0101 0.0399  0.0006  68  TYR   A CD1 
1700 C CD2 . TYR   A 68  ? 0.1607 0.1487 0.2506 0.0081  0.0584  0.0481  68  TYR   A CD2 
1701 C CE1 . TYR   A 68  ? 0.1508 0.1602 0.2552 -0.0083 0.0366  0.0040  68  TYR   A CE1 
1702 C CE2 . TYR   A 68  ? 0.1606 0.1536 0.2595 -0.0019 0.0592  0.0265  68  TYR   A CE2 
1703 C CZ  . TYR   A 68  ? 0.1582 0.1565 0.2702 -0.0131 0.0461  0.0063  68  TYR   A CZ  
1704 O OH  . TYR   A 68  ? 0.1901 0.1543 0.3009 -0.0062 0.0271  -0.0170 68  TYR   A OH  
1714 N N   . ILE   A 69  ? 0.1167 0.1269 0.1734 -0.0010 0.0199  0.0175  69  ILE   A N   
1715 C CA  . ILE   A 69  ? 0.1237 0.1317 0.1681 0.0003  0.0163  0.0078  69  ILE   A CA  
1716 C C   . ILE   A 69  ? 0.1286 0.1310 0.1641 0.0058  0.0111  0.0187  69  ILE   A C   
1717 O O   . ILE   A 69  ? 0.1317 0.1392 0.1628 0.0015  0.0220  0.0142  69  ILE   A O   
1718 C CB  . ILE   A 69  ? 0.1273 0.1483 0.1704 0.0015  0.0138  0.0003  69  ILE   A CB  
1719 C CG1 . ILE   A 69  ? 0.1261 0.1589 0.1790 0.0059  0.0191  -0.0184 69  ILE   A CG1 
1720 C CG2 . ILE   A 69  ? 0.1430 0.1722 0.1828 0.0057  0.0038  -0.0036 69  ILE   A CG2 
1721 C CD1 . ILE   A 69  ? 0.1276 0.1699 0.2092 -0.0010 0.0179  -0.0206 69  ILE   A CD1 
1733 N N   . ALA   A 70  ? 0.1322 0.1297 0.1638 -0.0047 0.0158  0.0153  70  ALA   A N   
1734 C CA  . ALA   A 70  ? 0.1312 0.1475 0.1800 -0.0146 0.0252  0.0239  70  ALA   A CA  
1735 C C   . ALA   A 70  ? 0.1277 0.1641 0.1781 -0.0068 0.0219  0.0288  70  ALA   A C   
1736 O O   . ALA   A 70  ? 0.1430 0.1994 0.1998 0.0104  0.0380  0.0418  70  ALA   A O   
1737 C CB  . ALA   A 70  ? 0.1325 0.1443 0.2093 -0.0184 0.0196  0.0096  70  ALA   A CB  
1743 N N   . THR   A 71  ? 0.1260 0.1591 0.1730 -0.0034 0.0153  0.0228  71  THR   A N   
1744 C CA  . THR   A 71  ? 0.1309 0.1759 0.2094 0.0048  0.0163  0.0278  71  THR   A CA  
1745 C C   . THR   A 71  ? 0.1212 0.1691 0.2326 0.0147  0.0310  0.0195  71  THR   A C   
1746 O O   . THR   A 71  ? 0.1320 0.1910 0.2845 0.0100  0.0456  -0.0068 71  THR   A O   
1747 C CB  . THR   A 71  ? 0.1649 0.1990 0.2328 0.0134  -0.0165 0.0368  71  THR   A CB  
1748 O OG1 . THR   A 71  ? 0.1923 0.2131 0.2300 0.0013  -0.0350 0.0288  71  THR   A OG1 
1749 C CG2 . THR   A 71  ? 0.1797 0.2145 0.2495 0.0167  -0.0197 0.0544  71  THR   A CG2 
1757 N N   . ASN   A 72  ? 0.1264 0.1519 0.2055 0.0119  0.0260  0.0214  72  ASN   A N   
1758 C CA  . ASN   A 72  ? 0.1337 0.1486 0.2102 0.0173  0.0322  0.0176  72  ASN   A CA  
1759 C C   . ASN   A 72  ? 0.1473 0.1469 0.1937 0.0106  0.0430  0.0108  72  ASN   A C   
1760 O O   . ASN   A 72  ? 0.1676 0.1495 0.2167 0.0112  0.0419  0.0031  72  ASN   A O   
1761 C CB  . ASN   A 72  ? 0.1563 0.1553 0.2085 0.0171  0.0412  0.0232  72  ASN   A CB  
1762 C CG  . ASN   A 72  ? 0.1736 0.1682 0.2131 0.0286  0.0362  0.0301  72  ASN   A CG  
1763 O OD1 . ASN   A 72  ? 0.1938 0.1945 0.2375 0.0264  0.0469  0.0329  72  ASN   A OD1 
1764 N ND2 . ASN   A 72  ? 0.1867 0.1736 0.2287 0.0519  0.0156  0.0259  72  ASN   A ND2 
1771 N N   . GLY   A 73  ? 0.1484 0.1425 0.1752 0.0023  0.0412  0.0085  73  GLY   A N   
1772 C CA  . GLY   A 73  ? 0.1518 0.1425 0.1673 -0.0085 0.0339  0.0136  73  GLY   A CA  
1773 C C   . GLY   A 73  ? 0.1523 0.1312 0.1685 -0.0023 0.0436  0.0246  73  GLY   A C   
1774 O O   . GLY   A 73  ? 0.1464 0.1370 0.1856 0.0060  0.0341  0.0274  73  GLY   A O   
1778 N N   . PRO   A 74  ? 0.1581 0.1327 0.1630 -0.0118 0.0432  0.0134  74  PRO   A N   
1779 C CA  . PRO   A 74  ? 0.1549 0.1330 0.1701 -0.0051 0.0344  0.0164  74  PRO   A CA  
1780 C C   . PRO   A 74  ? 0.1455 0.1205 0.1673 -0.0014 0.0298  0.0112  74  PRO   A C   
1781 O O   . PRO   A 74  ? 0.1558 0.1245 0.1964 0.0040  0.0394  0.0063  74  PRO   A O   
1782 C CB  . PRO   A 74  ? 0.1689 0.1626 0.1825 -0.0016 0.0342  0.0310  74  PRO   A CB  
1783 C CG  . PRO   A 74  ? 0.1953 0.1934 0.2235 -0.0140 0.0269  0.0210  74  PRO   A CG  
1784 C CD  . PRO   A 74  ? 0.1781 0.1727 0.1740 -0.0241 0.0294  0.0061  74  PRO   A CD  
1792 N N   . LEU   A 75  ? 0.1457 0.1136 0.1485 -0.0011 0.0288  0.0102  75  LEU   A N   
1793 C CA  . LEU   A 75  ? 0.1473 0.1145 0.1407 -0.0013 0.0087  0.0166  75  LEU   A CA  
1794 C C   . LEU   A 75  ? 0.1625 0.1223 0.1348 -0.0029 0.0157  0.0184  75  LEU   A C   
1795 O O   . LEU   A 75  ? 0.1939 0.1306 0.1463 0.0005  0.0113  0.0162  75  LEU   A O   
1796 C CB  . LEU   A 75  ? 0.1503 0.1165 0.1381 -0.0084 0.0085  0.0249  75  LEU   A CB  
1797 C CG  . LEU   A 75  ? 0.1693 0.1551 0.1514 -0.0420 0.0094  0.0168  75  LEU   A CG  
1798 C CD1 . LEU   A 75  ? 0.1789 0.2047 0.1634 -0.0388 0.0119  -0.0033 75  LEU   A CD1 
1799 C CD2 . LEU   A 75  ? 0.1905 0.1983 0.1958 -0.0163 0.0170  0.0156  75  LEU   A CD2 
1811 N N   . LYS   A 76  ? 0.1623 0.1204 0.1446 -0.0008 0.0097  0.0093  76  LYS   A N   
1812 C CA  . LYS   A 76  ? 0.1572 0.1322 0.1509 -0.0064 0.0037  0.0090  76  LYS   A CA  
1813 C C   . LYS   A 76  ? 0.1614 0.1243 0.1178 -0.0016 0.0083  0.0168  76  LYS   A C   
1814 O O   . LYS   A 76  ? 0.1674 0.1234 0.1287 -0.0029 0.0147  0.0118  76  LYS   A O   
1815 C CB  . LYS   A 76  ? 0.1603 0.1441 0.1755 -0.0012 0.0037  -0.0149 76  LYS   A CB  
1816 C CG  . LYS   A 76  ? 0.1711 0.1470 0.2151 0.0023  0.0002  -0.0200 76  LYS   A CG  
1817 C CD  . LYS   A 76  ? 0.1772 0.1575 0.2494 0.0112  -0.0113 -0.0237 76  LYS   A CD  
1818 C CE  . LYS   A 76  ? 0.1869 0.1711 0.3015 0.0071  -0.0102 -0.0316 76  LYS   A CE  
1819 N NZ  . LYS   A 76  ? 0.1835 0.1682 0.3597 0.0050  -0.0080 -0.0363 76  LYS   A NZ  
1833 N N   A VAL   A 77  ? 0.1656 0.1312 0.1255 -0.0024 0.0185  0.0150  77  VAL   A N   
1834 N N   B VAL   A 77  ? 0.1654 0.1308 0.1289 -0.0070 0.0220  0.0183  77  VAL   A N   
1835 C CA  A VAL   A 77  ? 0.1662 0.1318 0.1272 0.0030  0.0106  0.0114  77  VAL   A CA  
1836 C CA  B VAL   A 77  ? 0.1638 0.1325 0.1337 -0.0054 0.0104  0.0110  77  VAL   A CA  
1837 C C   A VAL   A 77  ? 0.1603 0.1283 0.1216 0.0048  0.0075  0.0077  77  VAL   A C   
1838 C C   B VAL   A 77  ? 0.1553 0.1259 0.1304 -0.0007 0.0135  0.0087  77  VAL   A C   
1839 O O   A VAL   A 77  ? 0.1668 0.1328 0.1212 0.0063  0.0081  0.0052  77  VAL   A O   
1840 O O   B VAL   A 77  ? 0.1565 0.1275 0.1343 0.0002  0.0218  0.0102  77  VAL   A O   
1841 C CB  A VAL   A 77  ? 0.1762 0.1398 0.1407 0.0086  0.0051  0.0178  77  VAL   A CB  
1842 C CB  B VAL   A 77  ? 0.1753 0.1457 0.1532 -0.0058 -0.0075 0.0132  77  VAL   A CB  
1843 C CG1 A VAL   A 77  ? 0.1825 0.1506 0.1567 0.0087  0.0047  0.0167  77  VAL   A CG1 
1844 C CG1 B VAL   A 77  ? 0.1836 0.1588 0.1742 0.0006  -0.0100 0.0142  77  VAL   A CG1 
1845 C CG2 A VAL   A 77  ? 0.1818 0.1430 0.1449 0.0144  0.0019  0.0229  77  VAL   A CG2 
1846 C CG2 B VAL   A 77  ? 0.1796 0.1528 0.1606 -0.0030 -0.0152 0.0111  77  VAL   A CG2 
1865 N N   . GLY   A 78  ? 0.1511 0.1237 0.1228 0.0032  0.0132  0.0108  78  GLY   A N   
1866 C CA  . GLY   A 78  ? 0.1497 0.1200 0.1423 -0.0057 0.0231  0.0119  78  GLY   A CA  
1867 C C   . GLY   A 78  ? 0.1393 0.1174 0.1443 0.0022  0.0229  0.0138  78  GLY   A C   
1868 O O   . GLY   A 78  ? 0.1369 0.1233 0.1529 -0.0024 0.0174  0.0257  78  GLY   A O   
1873 N N   . GLY   A 79  ? 0.1426 0.1166 0.1395 -0.0003 0.0177  0.0156  79  GLY   A N   
1874 C CA  . GLY   A 79  ? 0.1327 0.1212 0.1498 -0.0040 0.0155  0.0144  79  GLY   A CA  
1875 C C   . GLY   A 79  ? 0.1220 0.1135 0.1438 0.0045  0.0129  0.0068  79  GLY   A C   
1876 O O   . GLY   A 79  ? 0.1314 0.1280 0.1465 0.0135  0.0110  0.0111  79  GLY   A O   
1880 N N   . SER   A 80  ? 0.1196 0.1267 0.1655 -0.0000 0.0170  -0.0016 80  SER   A N   
1881 C CA  . SER   A 80  ? 0.1122 0.1197 0.1562 0.0006  0.0088  0.0069  80  SER   A CA  
1882 C C   . SER   A 80  ? 0.1114 0.1246 0.1506 -0.0001 0.0066  0.0127  80  SER   A C   
1883 O O   . SER   A 80  ? 0.1121 0.1460 0.1787 0.0095  0.0107  0.0039  80  SER   A O   
1884 C CB  . SER   A 80  ? 0.1284 0.1175 0.1720 -0.0054 0.0020  0.0112  80  SER   A CB  
1885 O OG  . SER   A 80  ? 0.1525 0.1220 0.2084 0.0020  -0.0003 0.0251  80  SER   A OG  
1891 N N   . CYS   A 81  ? 0.1049 0.1231 0.1440 0.0040  -0.0005 0.0137  81  CYS   A N   
1892 C CA  . CYS   A 81  ? 0.1092 0.1315 0.1413 0.0007  -0.0070 0.0211  81  CYS   A CA  
1893 C C   . CYS   A 81  ? 0.1068 0.1251 0.1427 -0.0076 -0.0035 0.0251  81  CYS   A C   
1894 O O   . CYS   A 81  ? 0.1063 0.1544 0.1512 -0.0009 -0.0022 0.0287  81  CYS   A O   
1895 C CB  . CYS   A 81  ? 0.1158 0.1339 0.1517 -0.0093 -0.0044 0.0261  81  CYS   A CB  
1896 S SG  . CYS   A 81  ? 0.1303 0.1263 0.1518 -0.0119 0.0017  0.0164  81  CYS   A SG  
1902 N N   . VAL   A 82  ? 0.1095 0.1310 0.1440 0.0025  -0.0082 0.0213  82  VAL   A N   
1903 C CA  . VAL   A 82  ? 0.1218 0.1352 0.1433 0.0032  -0.0152 0.0305  82  VAL   A CA  
1904 C C   . VAL   A 82  ? 0.1164 0.1364 0.1475 -0.0007 -0.0098 0.0265  82  VAL   A C   
1905 O O   . VAL   A 82  ? 0.1123 0.1530 0.1819 -0.0032 -0.0112 0.0090  82  VAL   A O   
1906 C CB  . VAL   A 82  ? 0.1482 0.1496 0.1628 0.0055  -0.0034 0.0325  82  VAL   A CB  
1907 C CG1 . VAL   A 82  ? 0.1741 0.1739 0.1733 0.0139  -0.0045 0.0329  82  VAL   A CG1 
1908 C CG2 . VAL   A 82  ? 0.1605 0.1480 0.1804 0.0001  -0.0031 0.0332  82  VAL   A CG2 
1918 N N   . LEU   A 83  ? 0.1141 0.1330 0.1453 -0.0066 -0.0097 0.0178  83  LEU   A N   
1919 C CA  . LEU   A 83  ? 0.1116 0.1355 0.1427 -0.0082 -0.0108 0.0129  83  LEU   A CA  
1920 C C   . LEU   A 83  ? 0.1213 0.1392 0.1311 -0.0040 -0.0145 0.0179  83  LEU   A C   
1921 O O   . LEU   A 83  ? 0.1306 0.1386 0.1464 -0.0112 -0.0102 0.0231  83  LEU   A O   
1922 C CB  . LEU   A 83  ? 0.1177 0.1437 0.1537 -0.0100 -0.0167 0.0153  83  LEU   A CB  
1923 C CG  . LEU   A 83  ? 0.1366 0.1554 0.1613 -0.0146 0.0015  0.0128  83  LEU   A CG  
1924 C CD1 . LEU   A 83  ? 0.1522 0.1587 0.1553 -0.0201 0.0036  0.0265  83  LEU   A CD1 
1925 C CD2 . LEU   A 83  ? 0.1390 0.1668 0.1676 -0.0139 0.0090  0.0178  83  LEU   A CD2 
1937 N N   . SER   A 84  ? 0.1366 0.1459 0.1507 -0.0126 -0.0174 0.0177  84  SER   A N   
1938 C CA  . SER   A 84  ? 0.1430 0.1515 0.1333 -0.0134 -0.0106 0.0197  84  SER   A CA  
1939 C C   . SER   A 84  ? 0.1494 0.1467 0.1312 -0.0142 -0.0018 0.0116  84  SER   A C   
1940 O O   . SER   A 84  ? 0.1398 0.1581 0.1273 -0.0059 -0.0136 0.0101  84  SER   A O   
1941 C CB  . SER   A 84  ? 0.1458 0.1733 0.1480 -0.0094 -0.0150 0.0122  84  SER   A CB  
1942 O OG  . SER   A 84  ? 0.1535 0.1881 0.1561 -0.0101 -0.0248 0.0005  84  SER   A OG  
1948 N N   A GLY   A 85  ? 0.1569 0.1538 0.1347 -0.0200 0.0041  0.0120  85  GLY   A N   
1949 N N   B GLY   A 85  ? 0.1597 0.1604 0.1424 -0.0137 0.0028  0.0121  85  GLY   A N   
1950 C CA  A GLY   A 85  ? 0.1542 0.1552 0.1381 -0.0276 0.0095  0.0081  85  GLY   A CA  
1951 C CA  B GLY   A 85  ? 0.1584 0.1690 0.1473 -0.0172 0.0091  0.0030  85  GLY   A CA  
1952 C C   A GLY   A 85  ? 0.1517 0.1570 0.1193 -0.0230 -0.0028 0.0044  85  GLY   A C   
1953 C C   B GLY   A 85  ? 0.1591 0.1760 0.1320 -0.0068 -0.0054 0.0000  85  GLY   A C   
1954 O O   A GLY   A 85  ? 0.1483 0.1624 0.1125 -0.0265 -0.0038 -0.0080 85  GLY   A O   
1955 O O   B GLY   A 85  ? 0.1586 0.1870 0.1425 -0.0065 0.0036  -0.0080 85  GLY   A O   
1962 N N   A HIS   A 86  ? 0.1541 0.1519 0.1179 -0.0157 -0.0060 0.0089  86  HIS   A N   
1963 N N   B HIS   A 86  ? 0.1627 0.1706 0.1265 0.0030  -0.0180 0.0043  86  HIS   A N   
1964 C CA  A HIS   A 86  ? 0.1652 0.1575 0.1126 -0.0156 -0.0068 0.0115  86  HIS   A CA  
1965 C CA  B HIS   A 86  ? 0.1724 0.1727 0.1179 0.0080  -0.0141 0.0051  86  HIS   A CA  
1966 C C   A HIS   A 86  ? 0.1772 0.1661 0.0980 -0.0128 -0.0068 0.0099  86  HIS   A C   
1967 C C   B HIS   A 86  ? 0.1961 0.1912 0.1214 0.0082  -0.0161 0.0000  86  HIS   A C   
1968 O O   A HIS   A 86  ? 0.1740 0.1798 0.0993 -0.0032 -0.0053 0.0146  86  HIS   A O   
1969 O O   B HIS   A 86  ? 0.2070 0.2122 0.1410 0.0061  -0.0126 0.0052  86  HIS   A O   
1970 C CB  A HIS   A 86  ? 0.1718 0.1620 0.1374 -0.0203 -0.0143 0.0047  86  HIS   A CB  
1971 C CB  B HIS   A 86  ? 0.1647 0.1604 0.1234 0.0106  -0.0082 0.0049  86  HIS   A CB  
1972 C CG  A HIS   A 86  ? 0.1720 0.1667 0.1542 -0.0197 -0.0175 0.0109  86  HIS   A CG  
1973 C CG  B HIS   A 86  ? 0.1592 0.1530 0.1109 0.0162  0.0045  0.0195  86  HIS   A CG  
1974 N ND1 A HIS   A 86  ? 0.1734 0.1700 0.1775 -0.0248 -0.0297 0.0106  86  HIS   A ND1 
1975 N ND1 B HIS   A 86  ? 0.1717 0.1542 0.1504 0.0078  0.0072  0.0150  86  HIS   A ND1 
1976 C CD2 A HIS   A 86  ? 0.1726 0.1660 0.1591 -0.0156 -0.0185 0.0085  86  HIS   A CD2 
1977 C CD2 B HIS   A 86  ? 0.1613 0.1474 0.1171 0.0192  0.0110  0.0179  86  HIS   A CD2 
1978 C CE1 A HIS   A 86  ? 0.1745 0.1699 0.1778 -0.0195 -0.0202 0.0112  86  HIS   A CE1 
1979 C CE1 B HIS   A 86  ? 0.1742 0.1556 0.1519 0.0032  0.0237  0.0176  86  HIS   A CE1 
1980 N NE2 A HIS   A 86  ? 0.1720 0.1667 0.1665 -0.0131 -0.0168 0.0115  86  HIS   A NE2 
1981 N NE2 B HIS   A 86  ? 0.1677 0.1466 0.1334 0.0159  0.0240  0.0244  86  HIS   A NE2 
1996 N N   A ASN   A 87  ? 0.1914 0.1701 0.1026 -0.0047 0.0071  0.0043  87  ASN   A N   
1997 N N   B ASN   A 87  ? 0.2156 0.1959 0.1337 0.0238  -0.0052 -0.0049 87  ASN   A N   
1998 C CA  A ASN   A 87  ? 0.2040 0.1782 0.1129 -0.0018 0.0227  -0.0051 87  ASN   A CA  
1999 C CA  B ASN   A 87  ? 0.2273 0.2032 0.1213 0.0338  0.0067  -0.0033 87  ASN   A CA  
2000 C C   A ASN   A 87  ? 0.2022 0.1820 0.1321 0.0028  0.0318  0.0037  87  ASN   A C   
2001 C C   B ASN   A 87  ? 0.2219 0.2103 0.1404 0.0283  0.0313  0.0144  87  ASN   A C   
2002 O O   A ASN   A 87  ? 0.2065 0.1853 0.1461 0.0113  0.0482  0.0111  87  ASN   A O   
2003 O O   B ASN   A 87  ? 0.2400 0.2211 0.1649 0.0244  0.0567  0.0230  87  ASN   A O   
2004 C CB  A ASN   A 87  ? 0.2140 0.1871 0.1293 0.0003  0.0281  -0.0080 87  ASN   A CB  
2005 C CB  B ASN   A 87  ? 0.2406 0.2043 0.1283 0.0473  0.0044  -0.0080 87  ASN   A CB  
2006 C CG  A ASN   A 87  ? 0.2203 0.1968 0.1329 -0.0026 0.0374  -0.0029 87  ASN   A CG  
2007 C CG  B ASN   A 87  ? 0.2501 0.2095 0.1347 0.0507  -0.0050 -0.0052 87  ASN   A CG  
2008 O OD1 A ASN   A 87  ? 0.2217 0.1983 0.1306 0.0009  0.0406  0.0018  87  ASN   A OD1 
2009 O OD1 B ASN   A 87  ? 0.2499 0.1990 0.1283 0.0619  -0.0069 -0.0064 87  ASN   A OD1 
2010 N ND2 A ASN   A 87  ? 0.2263 0.2098 0.1578 -0.0006 0.0461  0.0008  87  ASN   A ND2 
2011 N ND2 B ASN   A 87  ? 0.2600 0.2302 0.1725 0.0508  -0.0029 0.0042  87  ASN   A ND2 
2024 N N   A LEU   A 88  ? 0.1881 0.1842 0.1386 -0.0024 0.0191  0.0097  88  LEU   A N   
2025 N N   B LEU   A 88  ? 0.1880 0.2067 0.1316 0.0252  0.0159  0.0174  88  LEU   A N   
2026 C CA  A LEU   A 88  ? 0.1790 0.1838 0.1498 -0.0100 0.0152  0.0305  88  LEU   A CA  
2027 C CA  B LEU   A 88  ? 0.1709 0.2084 0.1448 0.0105  0.0184  0.0290  88  LEU   A CA  
2028 C C   A LEU   A 88  ? 0.1787 0.1873 0.1515 -0.0109 0.0153  0.0380  88  LEU   A C   
2029 C C   B LEU   A 88  ? 0.1537 0.2111 0.1375 0.0077  0.0157  0.0433  88  LEU   A C   
2030 O O   A LEU   A 88  ? 0.1802 0.1966 0.1918 -0.0142 0.0245  0.0490  88  LEU   A O   
2031 O O   B LEU   A 88  ? 0.1526 0.2161 0.1825 0.0044  0.0172  0.0720  88  LEU   A O   
2032 C CB  A LEU   A 88  ? 0.1795 0.1863 0.1568 -0.0138 -0.0184 0.0466  88  LEU   A CB  
2033 C CB  B LEU   A 88  ? 0.1753 0.2121 0.1556 0.0053  0.0140  0.0211  88  LEU   A CB  
2034 C CG  A LEU   A 88  ? 0.1936 0.1908 0.1776 -0.0162 -0.0337 0.0589  88  LEU   A CG  
2035 C CG  B LEU   A 88  ? 0.1854 0.2156 0.1768 0.0059  0.0138  0.0126  88  LEU   A CG  
2036 C CD1 A LEU   A 88  ? 0.1985 0.1912 0.1809 -0.0198 -0.0348 0.0574  88  LEU   A CD1 
2037 C CD1 B LEU   A 88  ? 0.1835 0.2139 0.1757 0.0032  0.0233  0.0069  88  LEU   A CD1 
2038 C CD2 A LEU   A 88  ? 0.2088 0.2043 0.2052 -0.0105 -0.0312 0.0486  88  LEU   A CD2 
2039 C CD2 B LEU   A 88  ? 0.2000 0.2257 0.1992 0.0172  0.0139  0.0012  88  LEU   A CD2 
2062 N N   A ALA   A 89  ? 0.1799 0.1800 0.1332 -0.0063 0.0062  0.0246  89  ALA   A N   
2063 N N   B ALA   A 89  ? 0.1493 0.2044 0.1310 0.0020  0.0083  0.0193  89  ALA   A N   
2064 C CA  A ALA   A 89  ? 0.1802 0.1744 0.1137 -0.0001 0.0020  0.0201  89  ALA   A CA  
2065 C CA  B ALA   A 89  ? 0.1511 0.2006 0.1209 -0.0055 0.0035  0.0176  89  ALA   A CA  
2066 C C   A ALA   A 89  ? 0.1812 0.1693 0.1202 0.0050  -0.0221 0.0200  89  ALA   A C   
2067 C C   B ALA   A 89  ? 0.1517 0.2003 0.1350 -0.0050 -0.0047 0.0125  89  ALA   A C   
2068 O O   A ALA   A 89  ? 0.1745 0.1614 0.1472 0.0018  -0.0300 0.0033  89  ALA   A O   
2069 O O   B ALA   A 89  ? 0.1487 0.2030 0.1749 -0.0146 -0.0172 -0.0087 89  ALA   A O   
2070 C CB  A ALA   A 89  ? 0.1771 0.1756 0.1144 0.0041  0.0141  0.0074  89  ALA   A CB  
2071 C CB  B ALA   A 89  ? 0.1526 0.1965 0.1229 -0.0092 0.0061  0.0103  89  ALA   A CB  
2082 N N   A LYS   A 90  ? 0.1906 0.1786 0.1289 0.0068  -0.0266 0.0218  90  LYS   A N   
2083 N N   B LYS   A 90  ? 0.1546 0.1993 0.1342 -0.0083 -0.0009 0.0218  90  LYS   A N   
2084 C CA  A LYS   A 90  ? 0.1977 0.1972 0.1538 0.0070  -0.0363 0.0117  90  LYS   A CA  
2085 C CA  B LYS   A 90  ? 0.1632 0.2028 0.1307 -0.0015 -0.0187 0.0229  90  LYS   A CA  
2086 C C   A LYS   A 90  ? 0.1827 0.1959 0.1641 -0.0014 -0.0362 -0.0020 90  LYS   A C   
2087 C C   B LYS   A 90  ? 0.1397 0.1831 0.1246 -0.0034 -0.0223 0.0180  90  LYS   A C   
2088 O O   A LYS   A 90  ? 0.1825 0.2103 0.1987 -0.0061 -0.0402 -0.0165 90  LYS   A O   
2089 O O   B LYS   A 90  ? 0.1355 0.1819 0.1391 -0.0018 -0.0287 0.0116  90  LYS   A O   
2090 C CB  A LYS   A 90  ? 0.2183 0.2213 0.1950 0.0110  -0.0412 0.0272  90  LYS   A CB  
2091 C CB  B LYS   A 90  ? 0.1886 0.2262 0.1604 0.0022  -0.0360 0.0385  90  LYS   A CB  
2092 C CG  A LYS   A 90  ? 0.2422 0.2491 0.2727 0.0115  -0.0396 0.0297  90  LYS   A CG  
2093 C CG  B LYS   A 90  ? 0.2210 0.2527 0.2471 0.0113  -0.0521 0.0478  90  LYS   A CG  
2094 C CD  A LYS   A 90  ? 0.2622 0.2703 0.3405 0.0116  -0.0327 0.0293  90  LYS   A CD  
2095 C CD  B LYS   A 90  ? 0.2489 0.2777 0.3297 0.0158  -0.0495 0.0437  90  LYS   A CD  
2096 C CE  A LYS   A 90  ? 0.2788 0.2857 0.3900 0.0112  -0.0273 0.0283  90  LYS   A CE  
2097 C CE  B LYS   A 90  ? 0.2724 0.2977 0.3944 0.0160  -0.0423 0.0340  90  LYS   A CE  
2098 N NZ  A LYS   A 90  ? 0.2905 0.2954 0.4232 0.0088  -0.0224 0.0288  90  LYS   A NZ  
2099 N NZ  B LYS   A 90  ? 0.2880 0.3099 0.4353 0.0126  -0.0328 0.0276  90  LYS   A NZ  
2126 N N   A HIS   A 91  ? 0.1732 0.1813 0.1487 -0.0006 -0.0329 0.0030  91  HIS   A N   
2127 N N   B HIS   A 91  ? 0.1372 0.1615 0.1013 -0.0054 -0.0233 0.0224  91  HIS   A N   
2128 C CA  A HIS   A 91  ? 0.1635 0.1725 0.1492 -0.0001 -0.0265 0.0137  91  HIS   A CA  
2129 C CA  B HIS   A 91  ? 0.1350 0.1561 0.1066 -0.0011 -0.0236 0.0171  91  HIS   A CA  
2130 C C   A HIS   A 91  ? 0.1428 0.1540 0.1271 -0.0069 -0.0095 0.0184  91  HIS   A C   
2131 C C   B HIS   A 91  ? 0.1305 0.1479 0.1049 -0.0040 -0.0075 0.0080  91  HIS   A C   
2132 O O   A HIS   A 91  ? 0.1321 0.1432 0.1173 -0.0124 0.0020  0.0271  91  HIS   A O   
2133 O O   B HIS   A 91  ? 0.1211 0.1498 0.1240 -0.0051 -0.0075 0.0067  91  HIS   A O   
2134 C CB  A HIS   A 91  ? 0.1835 0.1931 0.1824 0.0090  -0.0365 0.0073  91  HIS   A CB  
2135 C CB  B HIS   A 91  ? 0.1507 0.1808 0.1469 0.0251  -0.0287 0.0131  91  HIS   A CB  
2136 C CG  A HIS   A 91  ? 0.2117 0.2248 0.2234 0.0124  -0.0530 -0.0026 91  HIS   A CG  
2137 C CG  B HIS   A 91  ? 0.1821 0.2267 0.2070 0.0402  -0.0525 0.0004  91  HIS   A CG  
2138 N ND1 A HIS   A 91  ? 0.2193 0.2432 0.2509 0.0133  -0.0588 -0.0149 91  HIS   A ND1 
2139 N ND1 B HIS   A 91  ? 0.1888 0.2569 0.2506 0.0390  -0.0537 -0.0206 91  HIS   A ND1 
2140 C CD2 A HIS   A 91  ? 0.2303 0.2366 0.2413 0.0166  -0.0601 0.0044  91  HIS   A CD2 
2141 C CD2 B HIS   A 91  ? 0.2132 0.2456 0.2295 0.0417  -0.0592 0.0094  91  HIS   A CD2 
2142 C CE1 A HIS   A 91  ? 0.2286 0.2485 0.2575 0.0195  -0.0603 -0.0058 91  HIS   A CE1 
2143 C CE1 B HIS   A 91  ? 0.2059 0.2660 0.2567 0.0426  -0.0555 -0.0062 91  HIS   A CE1 
2144 N NE2 A HIS   A 91  ? 0.2390 0.2464 0.2579 0.0243  -0.0618 0.0011  91  HIS   A NE2 
2145 N NE2 B HIS   A 91  ? 0.2239 0.2633 0.2530 0.0460  -0.0577 0.0025  91  HIS   A NE2 
2160 N N   . CYS   A 92  ? 0.1260 0.1458 0.1224 -0.0122 -0.0090 0.0143  92  CYS   A N   
2161 C CA  . CYS   A 92  ? 0.1168 0.1365 0.1256 -0.0123 -0.0005 0.0157  92  CYS   A CA  
2162 C C   . CYS   A 92  ? 0.1161 0.1300 0.1159 -0.0092 -0.0003 0.0218  92  CYS   A C   
2163 O O   . CYS   A 92  ? 0.1189 0.1402 0.1438 -0.0129 -0.0050 0.0163  92  CYS   A O   
2164 C CB  . CYS   A 92  ? 0.1209 0.1380 0.1406 -0.0112 -0.0080 0.0058  92  CYS   A CB  
2165 S SG  . CYS   A 92  ? 0.1256 0.1288 0.1284 -0.0088 -0.0030 0.0138  92  CYS   A SG  
2172 N N   . LEU   A 93  ? 0.1103 0.1231 0.1230 -0.0091 0.0065  0.0158  93  LEU   A N   
2173 C CA  . LEU   A 93  ? 0.1052 0.1217 0.1281 -0.0084 -0.0015 0.0179  93  LEU   A CA  
2174 C C   . LEU   A 93  ? 0.1049 0.1110 0.1260 -0.0035 0.0037  0.0134  93  LEU   A C   
2175 O O   . LEU   A 93  ? 0.1011 0.1161 0.1261 0.0001  0.0042  0.0187  93  LEU   A O   
2176 C CB  . LEU   A 93  ? 0.1121 0.1212 0.1357 -0.0034 -0.0016 0.0243  93  LEU   A CB  
2177 C CG  . LEU   A 93  ? 0.1215 0.1228 0.1326 -0.0033 -0.0010 0.0271  93  LEU   A CG  
2178 C CD1 . LEU   A 93  ? 0.1285 0.1246 0.1709 0.0017  0.0077  0.0203  93  LEU   A CD1 
2179 C CD2 . LEU   A 93  ? 0.1339 0.1197 0.1500 -0.0014 0.0039  0.0173  93  LEU   A CD2 
2191 N N   . HIS   A 94  ? 0.1025 0.1062 0.1271 -0.0029 0.0059  0.0190  94  HIS   A N   
2192 C CA  . HIS   A 94  ? 0.1020 0.1108 0.1208 -0.0016 -0.0013 0.0171  94  HIS   A CA  
2193 C C   . HIS   A 94  ? 0.0999 0.1099 0.1283 -0.0010 0.0017  0.0155  94  HIS   A C   
2194 O O   . HIS   A 94  ? 0.1058 0.1276 0.1610 0.0033  0.0001  -0.0015 94  HIS   A O   
2195 C CB  . HIS   A 94  ? 0.1019 0.1091 0.1413 -0.0021 -0.0003 0.0167  94  HIS   A CB  
2196 C CG  . HIS   A 94  ? 0.1074 0.1060 0.1266 -0.0061 -0.0030 0.0139  94  HIS   A CG  
2197 N ND1 . HIS   A 94  ? 0.1092 0.1086 0.1352 -0.0052 -0.0022 0.0212  94  HIS   A ND1 
2198 C CD2 . HIS   A 94  ? 0.1155 0.1203 0.1392 -0.0048 -0.0088 0.0091  94  HIS   A CD2 
2199 C CE1 . HIS   A 94  ? 0.1139 0.1108 0.1337 -0.0042 -0.0050 0.0105  94  HIS   A CE1 
2200 N NE2 . HIS   A 94  ? 0.1208 0.1171 0.1357 -0.0079 -0.0127 0.0116  94  HIS   A NE2 
2208 N N   . VAL   A 95  ? 0.1026 0.1042 0.1233 -0.0003 0.0059  0.0147  95  VAL   A N   
2209 C CA  . VAL   A 95  ? 0.1053 0.1074 0.1226 -0.0031 0.0074  0.0146  95  VAL   A CA  
2210 C C   . VAL   A 95  ? 0.1071 0.1093 0.1119 -0.0073 0.0020  0.0119  95  VAL   A C   
2211 O O   . VAL   A 95  ? 0.1188 0.1191 0.1290 0.0089  0.0021  0.0126  95  VAL   A O   
2212 C CB  . VAL   A 95  ? 0.1099 0.1118 0.1332 -0.0089 0.0034  0.0104  95  VAL   A CB  
2213 C CG1 . VAL   A 95  ? 0.1308 0.1092 0.1534 -0.0142 0.0059  0.0052  95  VAL   A CG1 
2214 C CG2 . VAL   A 95  ? 0.1105 0.1125 0.1409 -0.0077 0.0098  0.0230  95  VAL   A CG2 
2224 N N   . VAL   A 96  ? 0.1125 0.1109 0.1182 -0.0025 -0.0010 0.0194  96  VAL   A N   
2225 C CA  . VAL   A 96  ? 0.1241 0.1125 0.1308 0.0006  0.0071  0.0223  96  VAL   A CA  
2226 C C   . VAL   A 96  ? 0.1302 0.1184 0.1266 -0.0092 0.0063  0.0231  96  VAL   A C   
2227 O O   . VAL   A 96  ? 0.1370 0.1204 0.1465 -0.0081 0.0118  0.0026  96  VAL   A O   
2228 C CB  . VAL   A 96  ? 0.1323 0.1186 0.1341 -0.0065 0.0152  0.0117  96  VAL   A CB  
2229 C CG1 . VAL   A 96  ? 0.1448 0.1220 0.1224 -0.0022 0.0104  0.0188  96  VAL   A CG1 
2230 C CG2 . VAL   A 96  ? 0.1314 0.1298 0.1425 -0.0128 0.0216  0.0090  96  VAL   A CG2 
2240 N N   A GLY   A 97  ? 0.1272 0.1233 0.1302 -0.0095 0.0094  0.0194  97  GLY   A N   
2241 N N   B GLY   A 97  ? 0.1284 0.1193 0.1248 -0.0118 -0.0044 0.0067  97  GLY   A N   
2242 C CA  A GLY   A 97  ? 0.1341 0.1350 0.1339 -0.0051 -0.0027 0.0335  97  GLY   A CA  
2243 C CA  B GLY   A 97  ? 0.1371 0.1291 0.1228 -0.0118 -0.0106 0.0209  97  GLY   A CA  
2244 C C   A GLY   A 97  ? 0.1384 0.1436 0.1312 -0.0014 -0.0014 0.0268  97  GLY   A C   
2245 C C   B GLY   A 97  ? 0.1417 0.1338 0.1172 -0.0094 -0.0055 0.0145  97  GLY   A C   
2246 O O   A GLY   A 97  ? 0.1392 0.1463 0.1403 0.0002  0.0112  0.0264  97  GLY   A O   
2247 O O   B GLY   A 97  ? 0.1515 0.1277 0.1348 -0.0074 0.0023  0.0197  97  GLY   A O   
2254 N N   A PRO   A 98  ? 0.1433 0.1374 0.1185 0.0024  -0.0078 0.0269  98  PRO   A N   
2255 N N   B PRO   A 98  ? 0.1466 0.1381 0.1269 -0.0053 -0.0042 0.0133  98  PRO   A N   
2256 C CA  A PRO   A 98  ? 0.1509 0.1471 0.1151 0.0015  -0.0037 0.0219  98  PRO   A CA  
2257 C CA  B PRO   A 98  ? 0.1511 0.1531 0.1319 0.0014  0.0023  0.0040  98  PRO   A CA  
2258 C C   A PRO   A 98  ? 0.1553 0.1557 0.1013 -0.0028 0.0014  0.0301  98  PRO   A C   
2259 C C   B PRO   A 98  ? 0.1607 0.1517 0.1285 -0.0007 -0.0013 0.0120  98  PRO   A C   
2260 O O   A PRO   A 98  ? 0.1551 0.1516 0.1022 0.0002  0.0044  0.0212  98  PRO   A O   
2261 O O   B PRO   A 98  ? 0.1598 0.1572 0.1484 0.0065  0.0006  0.0168  98  PRO   A O   
2262 C CB  A PRO   A 98  ? 0.1527 0.1458 0.1192 0.0108  -0.0049 0.0050  98  PRO   A CB  
2263 C CB  B PRO   A 98  ? 0.1552 0.1550 0.1383 0.0098  0.0009  0.0050  98  PRO   A CB  
2264 C CG  A PRO   A 98  ? 0.1477 0.1337 0.1170 0.0073  -0.0119 -0.0007 98  PRO   A CG  
2265 C CG  B PRO   A 98  ? 0.1564 0.1523 0.1602 0.0005  -0.0030 0.0062  98  PRO   A CG  
2266 C CD  A PRO   A 98  ? 0.1398 0.1279 0.1156 0.0079  -0.0082 0.0204  98  PRO   A CD  
2267 C CD  B PRO   A 98  ? 0.1454 0.1403 0.1531 -0.0037 -0.0101 0.0150  98  PRO   A CD  
2282 N N   A ASN   A 99  ? 0.1640 0.1779 0.1135 -0.0034 0.0073  0.0415  99  ASN   A N   
2283 N N   B ASN   A 99  ? 0.1905 0.1492 0.1271 0.0038  -0.0123 0.0249  99  ASN   A N   
2284 C CA  A ASN   A 99  ? 0.1865 0.2038 0.1447 -0.0003 -0.0056 0.0440  99  ASN   A CA  
2285 C CA  B ASN   A 99  ? 0.2201 0.1518 0.1438 0.0116  -0.0136 0.0449  99  ASN   A CA  
2286 C C   A ASN   A 99  ? 0.2126 0.2328 0.1575 -0.0031 -0.0044 0.0435  99  ASN   A C   
2287 C C   B ASN   A 99  ? 0.2290 0.1679 0.1353 0.0075  -0.0153 0.0522  99  ASN   A C   
2288 O O   A ASN   A 99  ? 0.2205 0.2439 0.1604 0.0052  0.0016  0.0373  99  ASN   A O   
2289 O O   B ASN   A 99  ? 0.2256 0.1712 0.1254 0.0166  -0.0079 0.0477  99  ASN   A O   
2290 C CB  A ASN   A 99  ? 0.1907 0.2084 0.1781 0.0042  -0.0149 0.0458  99  ASN   A CB  
2291 C CB  B ASN   A 99  ? 0.2443 0.1471 0.1810 0.0159  -0.0210 0.0382  99  ASN   A CB  
2292 C CG  A ASN   A 99  ? 0.2012 0.2194 0.2145 0.0084  -0.0174 0.0421  99  ASN   A CG  
2293 C CG  B ASN   A 99  ? 0.2656 0.1508 0.1892 0.0208  -0.0193 0.0378  99  ASN   A CG  
2294 O OD1 A ASN   A 99  ? 0.2102 0.2281 0.2212 0.0127  -0.0193 0.0298  99  ASN   A OD1 
2295 O OD1 B ASN   A 99  ? 0.2647 0.1606 0.1863 0.0264  -0.0232 0.0440  99  ASN   A OD1 
2296 N ND2 A ASN   A 99  ? 0.2074 0.2188 0.2289 0.0117  -0.0118 0.0550  99  ASN   A ND2 
2297 N ND2 B ASN   A 99  ? 0.2794 0.1534 0.2253 0.0227  -0.0174 0.0154  99  ASN   A ND2 
2310 N N   A VAL   A 100 ? 0.2296 0.2484 0.1702 -0.0061 -0.0195 0.0401  100 VAL   A N   
2311 N N   B VAL   A 100 ? 0.2510 0.2030 0.1585 -0.0015 -0.0316 0.0542  100 VAL   A N   
2312 C CA  A VAL   A 100 ? 0.2511 0.2676 0.1996 -0.0032 -0.0226 0.0403  100 VAL   A CA  
2313 C CA  B VAL   A 100 ? 0.2822 0.2328 0.1984 -0.0044 -0.0399 0.0460  100 VAL   A CA  
2314 C C   A VAL   A 100 ? 0.2704 0.2856 0.2063 0.0041  -0.0344 0.0580  100 VAL   A C   
2315 C C   B VAL   A 100 ? 0.3072 0.2525 0.2055 0.0077  -0.0459 0.0557  100 VAL   A C   
2316 O O   A VAL   A 100 ? 0.2752 0.2916 0.2157 0.0071  -0.0198 0.0553  100 VAL   A O   
2317 O O   B VAL   A 100 ? 0.3151 0.2621 0.2047 0.0041  -0.0561 0.0589  100 VAL   A O   
2318 C CB  A VAL   A 100 ? 0.2566 0.2698 0.2303 -0.0043 -0.0109 0.0227  100 VAL   A CB  
2319 C CB  B VAL   A 100 ? 0.2910 0.2454 0.2502 -0.0127 -0.0368 0.0381  100 VAL   A CB  
2320 C CG1 A VAL   A 100 ? 0.2566 0.2728 0.2448 -0.0059 -0.0030 0.0122  100 VAL   A CG1 
2321 C CG1 B VAL   A 100 ? 0.2947 0.2552 0.2726 -0.0129 -0.0375 0.0363  100 VAL   A CG1 
2322 C CG2 A VAL   A 100 ? 0.2598 0.2699 0.2388 -0.0054 -0.0054 0.0185  100 VAL   A CG2 
2323 C CG2 B VAL   A 100 ? 0.2970 0.2463 0.2670 -0.0155 -0.0350 0.0372  100 VAL   A CG2 
2342 N N   A ASN   A 101 ? 0.2857 0.2916 0.2180 0.0066  -0.0531 0.0734  101 ASN   A N   
2343 N N   B ASN   A 101 ? 0.3249 0.2669 0.2098 0.0266  -0.0428 0.0578  101 ASN   A N   
2344 C CA  A ASN   A 101 ? 0.3068 0.2987 0.2417 0.0090  -0.0592 0.0774  101 ASN   A CA  
2345 C CA  B ASN   A 101 ? 0.3462 0.2793 0.2295 0.0476  -0.0266 0.0638  101 ASN   A CA  
2346 C C   A ASN   A 101 ? 0.3262 0.3175 0.2678 0.0146  -0.0425 0.0769  101 ASN   A C   
2347 C C   B ASN   A 101 ? 0.3574 0.2827 0.2073 0.0501  -0.0181 0.0663  101 ASN   A C   
2348 O O   A ASN   A 101 ? 0.3324 0.3202 0.2841 0.0165  -0.0349 0.0730  101 ASN   A O   
2349 O O   B ASN   A 101 ? 0.3642 0.2819 0.1955 0.0513  -0.0091 0.0738  101 ASN   A O   
2350 C CB  A ASN   A 101 ? 0.3103 0.2832 0.2401 0.0057  -0.0741 0.0711  101 ASN   A CB  
2351 C CB  B ASN   A 101 ? 0.3596 0.2916 0.2896 0.0565  -0.0091 0.0619  101 ASN   A CB  
2352 C CG  A ASN   A 101 ? 0.3113 0.2693 0.2343 0.0004  -0.0866 0.0527  101 ASN   A CG  
2353 C CG  B ASN   A 101 ? 0.3724 0.3019 0.3391 0.0617  0.0054  0.0549  101 ASN   A CG  
2354 O OD1 A ASN   A 101 ? 0.3148 0.2712 0.2378 -0.0045 -0.0792 0.0349  101 ASN   A OD1 
2355 O OD1 B ASN   A 101 ? 0.3753 0.3087 0.3619 0.0607  0.0061  0.0483  101 ASN   A OD1 
2356 N ND2 A ASN   A 101 ? 0.3110 0.2600 0.2199 0.0018  -0.1051 0.0560  101 ASN   A ND2 
2357 N ND2 B ASN   A 101 ? 0.3795 0.3039 0.3615 0.0662  0.0171  0.0525  101 ASN   A ND2 
2370 N N   A LYS   A 102 ? 0.3373 0.3356 0.2855 0.0157  -0.0346 0.0710  102 LYS   A N   
2371 N N   B LYS   A 102 ? 0.3592 0.2888 0.2180 0.0496  -0.0148 0.0570  102 LYS   A N   
2372 C CA  A LYS   A 102 ? 0.3495 0.3534 0.3012 0.0168  -0.0305 0.0571  102 LYS   A CA  
2373 C CA  B LYS   A 102 ? 0.3616 0.3029 0.2199 0.0430  -0.0051 0.0497  102 LYS   A CA  
2374 C C   A LYS   A 102 ? 0.3470 0.3571 0.2702 0.0209  -0.0244 0.0594  102 LYS   A C   
2375 C C   B LYS   A 102 ? 0.3494 0.2971 0.1819 0.0445  -0.0117 0.0616  102 LYS   A C   
2376 O O   A LYS   A 102 ? 0.3486 0.3627 0.2658 0.0244  -0.0259 0.0610  102 LYS   A O   
2377 O O   B LYS   A 102 ? 0.3501 0.3041 0.2051 0.0473  -0.0043 0.0571  102 LYS   A O   
2378 C CB  A LYS   A 102 ? 0.3620 0.3663 0.3489 0.0140  -0.0347 0.0335  102 LYS   A CB  
2379 C CB  B LYS   A 102 ? 0.3755 0.3257 0.2853 0.0353  -0.0048 0.0237  102 LYS   A CB  
2380 C CG  A LYS   A 102 ? 0.3729 0.3762 0.3922 0.0120  -0.0398 0.0108  102 LYS   A CG  
2381 C CG  B LYS   A 102 ? 0.3879 0.3473 0.3547 0.0286  -0.0091 0.0027  102 LYS   A CG  
2382 C CD  A LYS   A 102 ? 0.3828 0.3855 0.4314 0.0113  -0.0438 -0.0107 102 LYS   A CD  
2383 C CD  B LYS   A 102 ? 0.3993 0.3676 0.4181 0.0249  -0.0135 -0.0158 102 LYS   A CD  
2384 C CE  A LYS   A 102 ? 0.3896 0.3916 0.4602 0.0112  -0.0461 -0.0258 102 LYS   A CE  
2385 C CE  B LYS   A 102 ? 0.4074 0.3818 0.4717 0.0239  -0.0161 -0.0243 102 LYS   A CE  
2386 N NZ  A LYS   A 102 ? 0.3934 0.3951 0.4749 0.0111  -0.0463 -0.0352 102 LYS   A NZ  
2387 N NZ  B LYS   A 102 ? 0.4127 0.3891 0.5010 0.0236  -0.0179 -0.0282 102 LYS   A NZ  
2414 N N   A GLY   A 103 ? 0.3424 0.3541 0.2640 0.0224  -0.0201 0.0522  103 GLY   A N   
2415 N N   B GLY   A 103 ? 0.3339 0.2863 0.1318 0.0437  -0.0249 0.0575  103 GLY   A N   
2416 C CA  A GLY   A 103 ? 0.3368 0.3505 0.2611 0.0217  -0.0139 0.0454  103 GLY   A CA  
2417 C CA  B GLY   A 103 ? 0.3171 0.2746 0.1487 0.0415  -0.0299 0.0443  103 GLY   A CA  
2418 C C   A GLY   A 103 ? 0.3298 0.3469 0.2704 0.0190  -0.0042 0.0371  103 GLY   A C   
2419 C C   B GLY   A 103 ? 0.2975 0.2568 0.1517 0.0359  -0.0329 0.0321  103 GLY   A C   
2420 O O   A GLY   A 103 ? 0.3316 0.3507 0.2882 0.0233  -0.0023 0.0288  103 GLY   A O   
2421 O O   B GLY   A 103 ? 0.3128 0.2658 0.1630 0.0395  -0.0261 0.0294  103 GLY   A O   
2428 N N   A GLU   A 104 ? 0.3198 0.3383 0.2543 0.0116  0.0017  0.0335  104 GLU   A N   
2429 N N   B GLU   A 104 ? 0.2600 0.2265 0.1335 0.0224  -0.0420 0.0341  104 GLU   A N   
2430 C CA  A GLU   A 104 ? 0.3110 0.3296 0.2426 0.0010  0.0079  0.0292  104 GLU   A CA  
2431 C CA  B GLU   A 104 ? 0.2288 0.1985 0.1228 0.0088  -0.0361 0.0284  104 GLU   A CA  
2432 C C   A GLU   A 104 ? 0.3146 0.3333 0.2438 -0.0050 0.0034  0.0168  104 GLU   A C   
2433 C C   B GLU   A 104 ? 0.2239 0.1976 0.1367 0.0071  -0.0277 0.0082  104 GLU   A C   
2434 O O   A GLU   A 104 ? 0.3162 0.3348 0.2472 -0.0075 0.0065  0.0123  104 GLU   A O   
2435 O O   B GLU   A 104 ? 0.2158 0.2030 0.1841 0.0074  -0.0255 0.0008  104 GLU   A O   
2436 C CB  A GLU   A 104 ? 0.2994 0.3186 0.2333 -0.0024 0.0183  0.0365  104 GLU   A CB  
2437 C CB  B GLU   A 104 ? 0.2111 0.1807 0.1171 -0.0091 -0.0259 0.0334  104 GLU   A CB  
2438 C CG  A GLU   A 104 ? 0.2913 0.3107 0.2381 -0.0038 0.0273  0.0418  104 GLU   A CG  
2439 C CG  B GLU   A 104 ? 0.1996 0.1810 0.1313 -0.0205 -0.0184 0.0408  104 GLU   A CG  
2440 C CD  A GLU   A 104 ? 0.2867 0.3061 0.2402 -0.0032 0.0330  0.0468  104 GLU   A CD  
2441 C CD  B GLU   A 104 ? 0.1963 0.1876 0.1215 -0.0333 -0.0177 0.0443  104 GLU   A CD  
2442 O OE1 A GLU   A 104 ? 0.2839 0.3043 0.2292 -0.0052 0.0368  0.0539  104 GLU   A OE1 
2443 O OE1 B GLU   A 104 ? 0.1929 0.1950 0.1214 -0.0398 -0.0223 0.0377  104 GLU   A OE1 
2444 O OE2 A GLU   A 104 ? 0.2888 0.3061 0.2591 -0.0003 0.0349  0.0400  104 GLU   A OE2 
2445 O OE2 B GLU   A 104 ? 0.2048 0.1973 0.1304 -0.0407 -0.0007 0.0376  104 GLU   A OE2 
2458 N N   A ASP   A 105 ? 0.3167 0.3355 0.2430 -0.0077 0.0012  0.0095  105 ASP   A N   
2459 N N   B ASP   A 105 ? 0.2350 0.1908 0.1315 0.0004  -0.0194 0.0104  105 ASP   A N   
2460 C CA  A ASP   A 105 ? 0.3182 0.3376 0.2530 -0.0109 -0.0023 -0.0029 105 ASP   A CA  
2461 C CA  B ASP   A 105 ? 0.2509 0.1859 0.1583 0.0009  -0.0169 -0.0062 105 ASP   A CA  
2462 C C   A ASP   A 105 ? 0.3039 0.3330 0.2427 -0.0162 -0.0134 -0.0061 105 ASP   A C   
2463 C C   B ASP   A 105 ? 0.2359 0.1665 0.1303 -0.0014 -0.0160 -0.0091 105 ASP   A C   
2464 O O   A ASP   A 105 ? 0.2996 0.3349 0.2315 -0.0161 -0.0145 -0.0043 105 ASP   A O   
2465 O O   B ASP   A 105 ? 0.2248 0.1530 0.1115 0.0055  -0.0152 -0.0149 105 ASP   A O   
2466 C CB  A ASP   A 105 ? 0.3324 0.3445 0.2814 -0.0100 0.0078  -0.0071 105 ASP   A CB  
2467 C CB  B ASP   A 105 ? 0.2807 0.2029 0.2236 0.0112  -0.0050 -0.0285 105 ASP   A CB  
2468 C CG  A ASP   A 105 ? 0.3438 0.3500 0.3102 -0.0101 0.0124  -0.0081 105 ASP   A CG  
2469 C CG  B ASP   A 105 ? 0.3069 0.2237 0.2848 0.0238  -0.0012 -0.0515 105 ASP   A CG  
2470 O OD1 A ASP   A 105 ? 0.3467 0.3524 0.3177 -0.0106 0.0074  -0.0178 105 ASP   A OD1 
2471 O OD1 B ASP   A 105 ? 0.3178 0.2298 0.2792 0.0117  -0.0160 -0.0615 105 ASP   A OD1 
2472 O OD2 A ASP   A 105 ? 0.3502 0.3515 0.3279 -0.0115 0.0186  0.0038  105 ASP   A OD2 
2473 O OD2 B ASP   A 105 ? 0.3197 0.2410 0.3462 0.0333  -0.0025 -0.0435 105 ASP   A OD2 
2482 N N   A ILE   A 106 ? 0.2936 0.3264 0.2498 -0.0209 -0.0277 -0.0120 106 ILE   A N   
2483 N N   B ILE   A 106 ? 0.2304 0.1801 0.1559 -0.0094 -0.0359 0.0074  106 ILE   A N   
2484 C CA  A ILE   A 106 ? 0.2791 0.3199 0.2560 -0.0258 -0.0377 -0.0201 106 ILE   A CA  
2485 C CA  B ILE   A 106 ? 0.2156 0.1908 0.1674 -0.0232 -0.0564 0.0057  106 ILE   A CA  
2486 C C   A ILE   A 106 ? 0.2676 0.3112 0.2539 -0.0336 -0.0335 -0.0343 106 ILE   A C   
2487 C C   B ILE   A 106 ? 0.2008 0.1776 0.1563 -0.0270 -0.0521 0.0045  106 ILE   A C   
2488 O O   A ILE   A 106 ? 0.2599 0.3095 0.2466 -0.0365 -0.0300 -0.0358 106 ILE   A O   
2489 O O   B ILE   A 106 ? 0.1834 0.1748 0.1656 -0.0334 -0.0348 0.0082  106 ILE   A O   
2490 C CB  A ILE   A 106 ? 0.2781 0.3234 0.2744 -0.0220 -0.0513 -0.0110 106 ILE   A CB  
2491 C CB  B ILE   A 106 ? 0.2236 0.2240 0.2243 -0.0242 -0.0787 0.0105  106 ILE   A CB  
2492 C CG1 A ILE   A 106 ? 0.2732 0.3257 0.2905 -0.0156 -0.0520 0.0010  106 ILE   A CG1 
2493 C CG1 B ILE   A 106 ? 0.2270 0.2448 0.2605 -0.0109 -0.0763 0.0305  106 ILE   A CG1 
2494 C CG2 A ILE   A 106 ? 0.2799 0.3236 0.2759 -0.0220 -0.0577 -0.0121 106 ILE   A CG2 
2495 C CG2 B ILE   A 106 ? 0.2311 0.2355 0.2506 -0.0309 -0.0778 0.0003  106 ILE   A CG2 
2496 C CD1 A ILE   A 106 ? 0.2721 0.3273 0.3033 -0.0121 -0.0479 0.0058  106 ILE   A CD1 
2497 C CD1 B ILE   A 106 ? 0.2322 0.2534 0.2826 -0.0038 -0.0662 0.0387  106 ILE   A CD1 
2520 N N   A GLN   A 107 ? 0.2716 0.3074 0.2726 -0.0358 -0.0263 -0.0430 107 GLN   A N   
2521 N N   B GLN   A 107 ? 0.2230 0.1727 0.1711 -0.0149 -0.0449 0.0030  107 GLN   A N   
2522 C CA  A GLN   A 107 ? 0.2737 0.3030 0.3032 -0.0346 -0.0176 -0.0425 107 GLN   A CA  
2523 C CA  B GLN   A 107 ? 0.2481 0.1767 0.2214 -0.0061 -0.0268 0.0033  107 GLN   A CA  
2524 C C   A GLN   A 107 ? 0.2380 0.2717 0.2742 -0.0362 -0.0037 -0.0350 107 GLN   A C   
2525 C C   B GLN   A 107 ? 0.2210 0.1489 0.1897 0.0081  -0.0136 0.0176  107 GLN   A C   
2526 O O   A GLN   A 107 ? 0.2420 0.2756 0.3006 -0.0348 0.0029  -0.0308 107 GLN   A O   
2527 O O   B GLN   A 107 ? 0.2309 0.1456 0.2102 0.0081  -0.0117 0.0189  107 GLN   A O   
2528 C CB  A GLN   A 107 ? 0.3120 0.3320 0.3786 -0.0326 -0.0213 -0.0423 107 GLN   A CB  
2529 C CB  B GLN   A 107 ? 0.2991 0.2310 0.3155 -0.0140 -0.0270 0.0006  107 GLN   A CB  
2530 C CG  A GLN   A 107 ? 0.3456 0.3599 0.4588 -0.0281 -0.0252 -0.0347 107 GLN   A CG  
2531 C CG  B GLN   A 107 ? 0.3458 0.2906 0.4166 -0.0180 -0.0303 0.0107  107 GLN   A CG  
2532 C CD  A GLN   A 107 ? 0.3722 0.3815 0.5266 -0.0247 -0.0301 -0.0267 107 GLN   A CD  
2533 C CD  B GLN   A 107 ? 0.3853 0.3370 0.5060 -0.0186 -0.0344 0.0224  107 GLN   A CD  
2534 O OE1 A GLN   A 107 ? 0.3824 0.3905 0.5546 -0.0240 -0.0330 -0.0238 107 GLN   A OE1 
2535 O OE1 B GLN   A 107 ? 0.4000 0.3563 0.5309 -0.0169 -0.0339 0.0294  107 GLN   A OE1 
2536 N NE2 A GLN   A 107 ? 0.3802 0.3883 0.5500 -0.0238 -0.0327 -0.0257 107 GLN   A NE2 
2537 N NE2 B GLN   A 107 ? 0.3933 0.3572 0.5357 -0.0197 -0.0389 0.0251  107 GLN   A NE2 
2554 N N   A LEU   A 108 ? 0.2008 0.2380 0.2265 -0.0384 0.0038  -0.0272 108 LEU   A N   
2555 N N   B LEU   A 108 ? 0.1962 0.1409 0.1420 0.0036  -0.0025 0.0093  108 LEU   A N   
2556 C CA  A LEU   A 108 ? 0.1741 0.2119 0.1891 -0.0285 0.0061  -0.0034 108 LEU   A CA  
2557 C CA  B LEU   A 108 ? 0.1827 0.1477 0.1450 0.0007  0.0045  0.0158  108 LEU   A CA  
2558 C C   A LEU   A 108 ? 0.1523 0.1861 0.1670 -0.0257 0.0001  0.0179  108 LEU   A C   
2559 C C   B LEU   A 108 ? 0.1671 0.1375 0.1394 0.0004  0.0028  0.0325  108 LEU   A C   
2560 O O   A LEU   A 108 ? 0.1497 0.1876 0.1693 -0.0248 0.0017  0.0235  108 LEU   A O   
2561 O O   B LEU   A 108 ? 0.1660 0.1482 0.1526 -0.0016 0.0095  0.0371  108 LEU   A O   
2562 C CB  A LEU   A 108 ? 0.1747 0.2136 0.1790 -0.0249 0.0198  -0.0003 108 LEU   A CB  
2563 C CB  B LEU   A 108 ? 0.1858 0.1631 0.1502 -0.0061 0.0059  0.0203  108 LEU   A CB  
2564 C CG  A LEU   A 108 ? 0.1838 0.2203 0.1891 -0.0148 0.0306  0.0048  108 LEU   A CG  
2565 C CG  B LEU   A 108 ? 0.2028 0.1837 0.1810 0.0014  0.0172  0.0265  108 LEU   A CG  
2566 C CD1 A LEU   A 108 ? 0.1888 0.2217 0.1910 -0.0180 0.0422  0.0033  108 LEU   A CD1 
2567 C CD1 B LEU   A 108 ? 0.2099 0.1891 0.1848 -0.0035 0.0309  0.0267  108 LEU   A CD1 
2568 C CD2 A LEU   A 108 ? 0.1871 0.2306 0.2103 -0.0058 0.0294  0.0091  108 LEU   A CD2 
2569 C CD2 B LEU   A 108 ? 0.2082 0.2017 0.2126 0.0118  0.0158  0.0282  108 LEU   A CD2 
2592 N N   A LEU   A 109 ? 0.1402 0.1702 0.1665 -0.0185 -0.0045 0.0254  109 LEU   A N   
2593 N N   B LEU   A 109 ? 0.1590 0.1364 0.1520 0.0071  0.0016  0.0329  109 LEU   A N   
2594 C CA  A LEU   A 109 ? 0.1397 0.1535 0.1562 -0.0142 -0.0112 0.0218  109 LEU   A CA  
2595 C CA  B LEU   A 109 ? 0.1464 0.1364 0.1494 0.0040  -0.0010 0.0252  109 LEU   A CA  
2596 C C   A LEU   A 109 ? 0.1338 0.1397 0.1554 -0.0163 -0.0051 0.0164  109 LEU   A C   
2597 C C   B LEU   A 109 ? 0.1329 0.1290 0.1484 -0.0032 0.0059  0.0160  109 LEU   A C   
2598 O O   A LEU   A 109 ? 0.1338 0.1358 0.1638 -0.0222 -0.0094 0.0129  109 LEU   A O   
2599 O O   B LEU   A 109 ? 0.1328 0.1209 0.1570 0.0006  0.0026  0.0156  109 LEU   A O   
2600 C CB  A LEU   A 109 ? 0.1440 0.1561 0.1738 -0.0072 -0.0185 0.0280  109 LEU   A CB  
2601 C CB  B LEU   A 109 ? 0.1490 0.1459 0.1733 0.0025  -0.0029 0.0380  109 LEU   A CB  
2602 C CG  A LEU   A 109 ? 0.1421 0.1619 0.1884 -0.0049 -0.0160 0.0223  109 LEU   A CG  
2603 C CG  B LEU   A 109 ? 0.1450 0.1595 0.1896 -0.0046 0.0063  0.0356  109 LEU   A CG  
2604 C CD1 A LEU   A 109 ? 0.1416 0.1575 0.1941 -0.0002 -0.0151 0.0204  109 LEU   A CD1 
2605 C CD1 B LEU   A 109 ? 0.1474 0.1558 0.1955 -0.0050 0.0072  0.0327  109 LEU   A CD1 
2606 C CD2 A LEU   A 109 ? 0.1453 0.1708 0.2058 -0.0023 -0.0211 0.0236  109 LEU   A CD2 
2607 C CD2 B LEU   A 109 ? 0.1455 0.1735 0.2127 -0.0074 0.0037  0.0355  109 LEU   A CD2 
2630 N N   . LYS   A 110 ? 0.1356 0.1332 0.1564 -0.0061 -0.0078 0.0125  110 LYS   A N   
2631 C CA  . LYS   A 110 ? 0.1300 0.1214 0.1653 -0.0122 -0.0031 0.0181  110 LYS   A CA  
2632 C C   . LYS   A 110 ? 0.1313 0.1134 0.1565 -0.0128 0.0037  0.0030  110 LYS   A C   
2633 O O   . LYS   A 110 ? 0.1303 0.1174 0.1595 -0.0090 0.0018  0.0081  110 LYS   A O   
2634 C CB  . LYS   A 110 ? 0.1400 0.1351 0.1810 -0.0100 -0.0040 0.0031  110 LYS   A CB  
2635 C CG  . LYS   A 110 ? 0.1378 0.1291 0.1845 -0.0073 0.0064  -0.0014 110 LYS   A CG  
2636 C CD  . LYS   A 110 ? 0.1450 0.1264 0.2006 -0.0057 -0.0017 -0.0050 110 LYS   A CD  
2637 C CE  . LYS   A 110 ? 0.1576 0.1353 0.2115 -0.0038 0.0170  -0.0039 110 LYS   A CE  
2638 N NZ  . LYS   A 110 ? 0.1516 0.1378 0.2327 -0.0179 0.0214  -0.0007 110 LYS   A NZ  
2653 N N   . SER   A 111 ? 0.1360 0.1220 0.1470 -0.0097 -0.0011 0.0082  111 SER   A N   
2654 C CA  . SER   A 111 ? 0.1304 0.1256 0.1472 -0.0028 0.0074  0.0099  111 SER   A CA  
2655 C C   . SER   A 111 ? 0.1209 0.1186 0.1466 -0.0067 0.0025  0.0156  111 SER   A C   
2656 O O   . SER   A 111 ? 0.1277 0.1127 0.1589 -0.0041 0.0054  0.0144  111 SER   A O   
2657 C CB  . SER   A 111 ? 0.1517 0.1486 0.1723 -0.0100 0.0216  -0.0061 111 SER   A CB  
2658 O OG  . SER   A 111 ? 0.1899 0.1706 0.1873 -0.0035 0.0297  -0.0076 111 SER   A OG  
2664 N N   . ALA   A 112 ? 0.1265 0.1145 0.1421 -0.0024 0.0045  0.0131  112 ALA   A N   
2665 C CA  . ALA   A 112 ? 0.1220 0.1112 0.1424 -0.0066 0.0070  0.0108  112 ALA   A CA  
2666 C C   . ALA   A 112 ? 0.1131 0.1044 0.1443 -0.0028 0.0041  0.0127  112 ALA   A C   
2667 O O   . ALA   A 112 ? 0.1210 0.1071 0.1539 -0.0116 0.0086  0.0163  112 ALA   A O   
2668 C CB  . ALA   A 112 ? 0.1361 0.1194 0.1537 -0.0057 0.0024  0.0214  112 ALA   A CB  
2674 N N   A TYR   A 113 ? 0.1110 0.1163 0.1464 -0.0068 0.0024  0.0146  113 TYR   A N   
2675 N N   B TYR   A 113 ? 0.1127 0.1114 0.1504 -0.0052 0.0062  0.0154  113 TYR   A N   
2676 C CA  A TYR   A 113 ? 0.1078 0.1179 0.1456 -0.0073 0.0029  0.0212  113 TYR   A CA  
2677 C CA  B TYR   A 113 ? 0.1127 0.1037 0.1493 -0.0025 0.0100  0.0234  113 TYR   A CA  
2678 C C   A TYR   A 113 ? 0.1068 0.1113 0.1399 -0.0106 0.0058  0.0155  113 TYR   A C   
2679 C C   B TYR   A 113 ? 0.1125 0.1024 0.1425 -0.0078 0.0110  0.0146  113 TYR   A C   
2680 O O   A TYR   A 113 ? 0.1049 0.1163 0.1443 -0.0084 0.0079  0.0118  113 TYR   A O   
2681 O O   B TYR   A 113 ? 0.1168 0.1066 0.1499 -0.0009 0.0139  0.0078  113 TYR   A O   
2682 C CB  A TYR   A 113 ? 0.1087 0.1304 0.1484 -0.0085 -0.0010 0.0197  113 TYR   A CB  
2683 C CB  B TYR   A 113 ? 0.1199 0.1052 0.1514 0.0016  0.0099  0.0216  113 TYR   A CB  
2684 C CG  A TYR   A 113 ? 0.1055 0.1397 0.1445 -0.0144 0.0005  0.0202  113 TYR   A CG  
2685 C CG  B TYR   A 113 ? 0.1239 0.1059 0.1512 -0.0042 0.0076  0.0196  113 TYR   A CG  
2686 C CD1 A TYR   A 113 ? 0.1056 0.1499 0.1453 -0.0096 0.0002  0.0185  113 TYR   A CD1 
2687 C CD1 B TYR   A 113 ? 0.1273 0.1123 0.1534 0.0023  0.0031  0.0164  113 TYR   A CD1 
2688 C CD2 A TYR   A 113 ? 0.1076 0.1502 0.1457 -0.0180 -0.0090 0.0213  113 TYR   A CD2 
2689 C CD2 B TYR   A 113 ? 0.1333 0.1188 0.1581 -0.0040 -0.0018 0.0162  113 TYR   A CD2 
2690 C CE1 A TYR   A 113 ? 0.1064 0.1563 0.1512 -0.0073 -0.0013 0.0204  113 TYR   A CE1 
2691 C CE1 B TYR   A 113 ? 0.1349 0.1167 0.1659 0.0049  0.0012  0.0097  113 TYR   A CE1 
2692 C CE2 A TYR   A 113 ? 0.1047 0.1575 0.1471 -0.0133 -0.0102 0.0297  113 TYR   A CE2 
2693 C CE2 B TYR   A 113 ? 0.1386 0.1264 0.1643 0.0027  -0.0060 0.0180  113 TYR   A CE2 
2694 C CZ  A TYR   A 113 ? 0.0990 0.1558 0.1462 -0.0065 -0.0008 0.0348  113 TYR   A CZ  
2695 C CZ  B TYR   A 113 ? 0.1354 0.1190 0.1742 0.0111  -0.0038 0.0214  113 TYR   A CZ  
2696 O OH  A TYR   A 113 ? 0.0961 0.1628 0.1494 0.0006  -0.0019 0.0348  113 TYR   A OH  
2697 O OH  B TYR   A 113 ? 0.1443 0.1299 0.2081 0.0234  -0.0073 0.0174  113 TYR   A OH  
2716 N N   . GLU   A 114 ? 0.1115 0.1081 0.1468 -0.0051 0.0096  0.0182  114 GLU   A N   
2717 C CA  . GLU   A 114 ? 0.1122 0.1115 0.1587 0.0005  0.0043  0.0169  114 GLU   A CA  
2718 C C   . GLU   A 114 ? 0.1091 0.1080 0.1548 0.0023  0.0132  0.0157  114 GLU   A C   
2719 O O   . GLU   A 114 ? 0.1217 0.1115 0.1518 0.0042  0.0067  0.0192  114 GLU   A O   
2720 C CB  . GLU   A 114 ? 0.1152 0.1119 0.1570 -0.0027 0.0091  0.0101  114 GLU   A CB  
2721 C CG  . GLU   A 114 ? 0.1238 0.1150 0.1660 -0.0012 0.0077  0.0085  114 GLU   A CG  
2722 C CD  . GLU   A 114 ? 0.1292 0.1142 0.1735 -0.0019 0.0096  0.0084  114 GLU   A CD  
2723 O OE1 . GLU   A 114 ? 0.1339 0.1232 0.1761 -0.0080 0.0165  0.0018  114 GLU   A OE1 
2724 O OE2 . GLU   A 114 ? 0.1518 0.1217 0.1928 -0.0113 0.0153  -0.0081 114 GLU   A OE2 
2732 N N   . ASN   A 115 ? 0.1099 0.1086 0.1453 -0.0080 0.0099  0.0067  115 ASN   A N   
2733 C CA  . ASN   A 115 ? 0.1109 0.1142 0.1529 -0.0041 0.0103  0.0159  115 ASN   A CA  
2734 C C   . ASN   A 115 ? 0.1112 0.1055 0.1533 -0.0067 0.0069  0.0117  115 ASN   A C   
2735 O O   . ASN   A 115 ? 0.1170 0.1240 0.1496 -0.0059 0.0052  0.0160  115 ASN   A O   
2736 C CB  . ASN   A 115 ? 0.1218 0.1208 0.1498 -0.0096 0.0123  0.0153  115 ASN   A CB  
2737 C CG  . ASN   A 115 ? 0.1203 0.1344 0.1610 -0.0168 0.0158  0.0223  115 ASN   A CG  
2738 O OD1 . ASN   A 115 ? 0.1250 0.2349 0.1915 -0.0150 0.0201  0.0380  115 ASN   A OD1 
2739 N ND2 . ASN   A 115 ? 0.1314 0.1252 0.1465 -0.0098 0.0208  0.0193  115 ASN   A ND2 
2746 N N   . PHE   A 116 ? 0.1053 0.1137 0.1492 -0.0003 0.0127  0.0195  116 PHE   A N   
2747 C CA  . PHE   A 116 ? 0.1100 0.1202 0.1416 -0.0035 0.0065  0.0198  116 PHE   A CA  
2748 C C   . PHE   A 116 ? 0.1127 0.1222 0.1431 -0.0017 0.0037  0.0183  116 PHE   A C   
2749 O O   . PHE   A 116 ? 0.1175 0.1291 0.1640 0.0063  0.0064  0.0303  116 PHE   A O   
2750 C CB  . PHE   A 116 ? 0.1171 0.1128 0.1537 0.0031  0.0114  0.0194  116 PHE   A CB  
2751 C CG  . PHE   A 116 ? 0.1139 0.1111 0.1450 -0.0053 0.0090  0.0075  116 PHE   A CG  
2752 C CD1 . PHE   A 116 ? 0.1123 0.1138 0.1571 -0.0057 0.0029  0.0176  116 PHE   A CD1 
2753 C CD2 . PHE   A 116 ? 0.1187 0.1118 0.1570 -0.0046 0.0152  0.0201  116 PHE   A CD2 
2754 C CE1 . PHE   A 116 ? 0.1182 0.1159 0.1584 -0.0144 0.0052  0.0210  116 PHE   A CE1 
2755 C CE2 . PHE   A 116 ? 0.1189 0.1124 0.1736 -0.0039 0.0104  0.0154  116 PHE   A CE2 
2756 C CZ  . PHE   A 116 ? 0.1254 0.1066 0.1601 -0.0033 0.0068  0.0255  116 PHE   A CZ  
2766 N N   . ASN   A 117 ? 0.1149 0.1181 0.1471 -0.0011 0.0088  0.0207  117 ASN   A N   
2767 C CA  . ASN   A 117 ? 0.1139 0.1162 0.1582 -0.0011 0.0091  0.0226  117 ASN   A CA  
2768 C C   . ASN   A 117 ? 0.1169 0.1224 0.1686 0.0001  0.0128  0.0211  117 ASN   A C   
2769 O O   . ASN   A 117 ? 0.1278 0.1326 0.1752 0.0002  -0.0037 0.0403  117 ASN   A O   
2770 C CB  . ASN   A 117 ? 0.1129 0.1211 0.1589 -0.0000 0.0140  0.0291  117 ASN   A CB  
2771 C CG  . ASN   A 117 ? 0.1156 0.1196 0.1689 0.0018  0.0181  0.0310  117 ASN   A CG  
2772 O OD1 . ASN   A 117 ? 0.1136 0.1407 0.1805 -0.0062 0.0184  0.0229  117 ASN   A OD1 
2773 N ND2 . ASN   A 117 ? 0.1091 0.1224 0.1763 -0.0003 0.0167  0.0323  117 ASN   A ND2 
2780 N N   . GLN   A 118 ? 0.1083 0.1213 0.1694 -0.0022 0.0051  0.0316  118 GLN   A N   
2781 C CA  . GLN   A 118 ? 0.1190 0.1339 0.1828 -0.0037 0.0037  0.0161  118 GLN   A CA  
2782 C C   . GLN   A 118 ? 0.1196 0.1407 0.1747 -0.0008 0.0013  0.0313  118 GLN   A C   
2783 O O   . GLN   A 118 ? 0.1210 0.1708 0.1954 0.0019  -0.0126 0.0117  118 GLN   A O   
2784 C CB  . GLN   A 118 ? 0.1166 0.1338 0.1881 0.0032  0.0139  0.0234  118 GLN   A CB  
2785 C CG  . GLN   A 118 ? 0.1217 0.1329 0.1977 0.0061  0.0191  0.0336  118 GLN   A CG  
2786 C CD  . GLN   A 118 ? 0.1150 0.1367 0.2066 0.0068  0.0154  0.0240  118 GLN   A CD  
2787 O OE1 . GLN   A 118 ? 0.1189 0.1607 0.2168 0.0135  -0.0008 0.0155  118 GLN   A OE1 
2788 N NE2 . GLN   A 118 ? 0.1200 0.1381 0.2178 0.0080  0.0141  0.0284  118 GLN   A NE2 
2797 N N   . HIS   A 119 ? 0.1251 0.1339 0.1622 0.0023  0.0012  0.0354  119 HIS   A N   
2798 C CA  . HIS   A 119 ? 0.1293 0.1462 0.1645 0.0028  0.0032  0.0293  119 HIS   A CA  
2799 C C   . HIS   A 119 ? 0.1349 0.1538 0.1623 -0.0036 0.0132  0.0351  119 HIS   A C   
2800 O O   . HIS   A 119 ? 0.1373 0.1530 0.1705 -0.0159 0.0091  0.0309  119 HIS   A O   
2801 C CB  . HIS   A 119 ? 0.1307 0.1377 0.1815 0.0051  0.0177  0.0321  119 HIS   A CB  
2802 C CG  . HIS   A 119 ? 0.1400 0.1412 0.2272 0.0101  0.0212  0.0436  119 HIS   A CG  
2803 N ND1 . HIS   A 119 ? 0.1473 0.1559 0.2867 0.0017  0.0102  0.0249  119 HIS   A ND1 
2804 C CD2 . HIS   A 119 ? 0.1525 0.1503 0.2521 0.0205  0.0384  0.0592  119 HIS   A CD2 
2805 C CE1 . HIS   A 119 ? 0.1489 0.1565 0.3006 -0.0022 0.0342  0.0456  119 HIS   A CE1 
2806 N NE2 . HIS   A 119 ? 0.1612 0.1538 0.2921 0.0056  0.0516  0.0578  119 HIS   A NE2 
2814 N N   A GLU   A 120 ? 0.1331 0.1663 0.1603 -0.0025 -0.0002 0.0473  120 GLU   A N   
2815 N N   B GLU   A 120 ? 0.1445 0.1753 0.1605 0.0035  0.0047  0.0532  120 GLU   A N   
2816 C CA  A GLU   A 120 ? 0.1415 0.1830 0.1752 0.0038  -0.0066 0.0674  120 GLU   A CA  
2817 C CA  B GLU   A 120 ? 0.1663 0.2028 0.1831 0.0163  0.0060  0.0788  120 GLU   A CA  
2818 C C   A GLU   A 120 ? 0.1345 0.1783 0.1606 -0.0022 -0.0030 0.0643  120 GLU   A C   
2819 C C   B GLU   A 120 ? 0.1459 0.1869 0.1661 0.0065  0.0034  0.0721  120 GLU   A C   
2820 O O   A GLU   A 120 ? 0.1335 0.1775 0.1670 -0.0071 -0.0043 0.0628  120 GLU   A O   
2821 O O   B GLU   A 120 ? 0.1440 0.1845 0.1764 0.0061  0.0022  0.0739  120 GLU   A O   
2822 C CB  A GLU   A 120 ? 0.1641 0.2133 0.2178 0.0173  -0.0144 0.0933  120 GLU   A CB  
2823 C CB  B GLU   A 120 ? 0.2152 0.2546 0.2362 0.0376  0.0102  0.1143  120 GLU   A CB  
2824 C CG  A GLU   A 120 ? 0.2065 0.2446 0.3001 0.0275  -0.0208 0.0919  120 GLU   A CG  
2825 C CG  B GLU   A 120 ? 0.2827 0.3087 0.3373 0.0553  0.0125  0.1194  120 GLU   A CG  
2826 C CD  A GLU   A 120 ? 0.2552 0.2727 0.3793 0.0359  -0.0152 0.0778  120 GLU   A CD  
2827 C CD  B GLU   A 120 ? 0.3493 0.3601 0.4306 0.0707  0.0256  0.1129  120 GLU   A CD  
2828 O OE1 A GLU   A 120 ? 0.2733 0.2842 0.4044 0.0392  -0.0132 0.0750  120 GLU   A OE1 
2829 O OE1 B GLU   A 120 ? 0.3685 0.3693 0.4571 0.0744  0.0300  0.1097  120 GLU   A OE1 
2830 O OE2 A GLU   A 120 ? 0.2736 0.2815 0.4073 0.0328  -0.0141 0.0727  120 GLU   A OE2 
2831 O OE2 B GLU   A 120 ? 0.3760 0.3800 0.4658 0.0747  0.0275  0.1118  120 GLU   A OE2 
2844 N N   . VAL   A 121 ? 0.1373 0.1785 0.1470 0.0027  0.0039  0.0629  121 VAL   A N   
2845 C CA  . VAL   A 121 ? 0.1406 0.1830 0.1465 0.0011  0.0146  0.0608  121 VAL   A CA  
2846 C C   . VAL   A 121 ? 0.1277 0.1662 0.1428 -0.0085 0.0095  0.0442  121 VAL   A C   
2847 O O   . VAL   A 121 ? 0.1323 0.1727 0.1548 -0.0167 -0.0039 0.0290  121 VAL   A O   
2848 C CB  . VAL   A 121 ? 0.1799 0.2290 0.1865 0.0106  0.0314  0.0712  121 VAL   A CB  
2849 C CG1 . VAL   A 121 ? 0.1816 0.2436 0.1947 0.0216  0.0422  0.0699  121 VAL   A CG1 
2850 C CG2 . VAL   A 121 ? 0.2086 0.2506 0.2288 0.0019  0.0253  0.0660  121 VAL   A CG2 
2861 N N   . LEU   A 122 ? 0.1244 0.1381 0.1455 -0.0087 0.0078  0.0394  122 LEU   A N   
2862 C CA  . LEU   A 122 ? 0.1283 0.1357 0.1472 -0.0128 0.0231  0.0368  122 LEU   A CA  
2863 C C   . LEU   A 122 ? 0.1260 0.1364 0.1372 -0.0112 0.0101  0.0332  122 LEU   A C   
2864 O O   . LEU   A 122 ? 0.1269 0.1402 0.1700 -0.0196 0.0021  0.0353  122 LEU   A O   
2865 C CB  . LEU   A 122 ? 0.1499 0.1445 0.1803 -0.0029 0.0144  0.0373  122 LEU   A CB  
2866 C CG  . LEU   A 122 ? 0.1620 0.1512 0.1649 -0.0056 0.0205  0.0366  122 LEU   A CG  
2867 C CD1 . LEU   A 122 ? 0.1717 0.1564 0.1776 -0.0064 0.0153  0.0421  122 LEU   A CD1 
2868 C CD2 . LEU   A 122 ? 0.1656 0.1369 0.1506 0.0009  0.0356  0.0259  122 LEU   A CD2 
2880 N N   . LEU   A 123 ? 0.1173 0.1346 0.1383 -0.0121 0.0022  0.0301  123 LEU   A N   
2881 C CA  . LEU   A 123 ? 0.1179 0.1319 0.1342 -0.0142 0.0067  0.0296  123 LEU   A CA  
2882 C C   . LEU   A 123 ? 0.1153 0.1276 0.1255 -0.0068 0.0062  0.0291  123 LEU   A C   
2883 O O   . LEU   A 123 ? 0.1181 0.1395 0.1370 -0.0215 0.0029  0.0293  123 LEU   A O   
2884 C CB  . LEU   A 123 ? 0.1279 0.1364 0.1351 -0.0115 0.0142  0.0277  123 LEU   A CB  
2885 C CG  . LEU   A 123 ? 0.1317 0.1502 0.1454 -0.0013 0.0145  0.0218  123 LEU   A CG  
2886 C CD1 . LEU   A 123 ? 0.1377 0.1666 0.1701 0.0024  0.0066  0.0112  123 LEU   A CD1 
2887 C CD2 . LEU   A 123 ? 0.1403 0.1538 0.1650 -0.0017 0.0059  0.0094  123 LEU   A CD2 
2899 N N   A ALA   A 124 ? 0.1115 0.1248 0.1354 -0.0124 0.0076  0.0269  124 ALA   A N   
2900 N N   B ALA   A 124 ? 0.1163 0.1295 0.1259 -0.0079 0.0008  0.0268  124 ALA   A N   
2901 N N   C ALA   A 124 ? 0.1148 0.1222 0.1262 -0.0130 0.0021  0.0295  124 ALA   A N   
2902 C CA  A ALA   A 124 ? 0.1052 0.1209 0.1369 -0.0031 0.0107  0.0251  124 ALA   A CA  
2903 C CA  B ALA   A 124 ? 0.1173 0.1310 0.1289 -0.0061 -0.0024 0.0268  124 ALA   A CA  
2904 C CA  C ALA   A 124 ? 0.1140 0.1160 0.1280 -0.0158 0.0005  0.0320  124 ALA   A CA  
2905 C C   A ALA   A 124 ? 0.0948 0.1160 0.1368 -0.0080 0.0117  0.0286  124 ALA   A C   
2906 C C   B ALA   A 124 ? 0.1186 0.1312 0.1352 -0.0098 -0.0003 0.0247  124 ALA   A C   
2907 C C   C ALA   A 124 ? 0.1116 0.1131 0.1344 -0.0234 -0.0008 0.0299  124 ALA   A C   
2908 O O   A ALA   A 124 ? 0.1012 0.1294 0.1588 -0.0016 0.0187  0.0255  124 ALA   A O   
2909 O O   B ALA   A 124 ? 0.1181 0.1374 0.1460 -0.0069 0.0025  0.0253  124 ALA   A O   
2910 O O   C ALA   A 124 ? 0.1045 0.1124 0.1425 -0.0262 -0.0025 0.0336  124 ALA   A O   
2911 C CB  A ALA   A 124 ? 0.1086 0.1267 0.1522 0.0040  0.0155  0.0274  124 ALA   A CB  
2912 C CB  B ALA   A 124 ? 0.1179 0.1345 0.1340 -0.0010 -0.0049 0.0319  124 ALA   A CB  
2913 C CB  C ALA   A 124 ? 0.1161 0.1159 0.1322 -0.0130 0.0041  0.0415  124 ALA   A CB  
2929 N N   A PRO   A 125 ? 0.0845 0.1091 0.1266 -0.0011 0.0095  0.0371  125 PRO   A N   
2930 N N   B PRO   A 125 ? 0.1253 0.1319 0.1385 -0.0036 -0.0009 0.0224  125 PRO   A N   
2931 N N   C PRO   A 125 ? 0.1222 0.1219 0.1396 -0.0123 0.0018  0.0268  125 PRO   A N   
2932 C CA  A PRO   A 125 ? 0.0918 0.1123 0.1391 -0.0044 0.0044  0.0344  125 PRO   A CA  
2933 C CA  B PRO   A 125 ? 0.1348 0.1324 0.1464 -0.0021 -0.0050 0.0143  125 PRO   A CA  
2934 C CA  C PRO   A 125 ? 0.1339 0.1268 0.1475 -0.0106 -0.0019 0.0194  125 PRO   A CA  
2935 C C   A PRO   A 125 ? 0.0864 0.1126 0.1492 -0.0119 -0.0029 0.0373  125 PRO   A C   
2936 C C   B PRO   A 125 ? 0.1361 0.1328 0.1538 -0.0022 -0.0093 0.0078  125 PRO   A C   
2937 C C   C PRO   A 125 ? 0.1358 0.1311 0.1495 -0.0146 -0.0037 0.0187  125 PRO   A C   
2938 O O   A PRO   A 125 ? 0.0931 0.1096 0.1725 -0.0024 -0.0079 0.0253  125 PRO   A O   
2939 O O   B PRO   A 125 ? 0.1397 0.1304 0.1586 0.0020  -0.0090 0.0040  125 PRO   A O   
2940 O O   C PRO   A 125 ? 0.1394 0.1270 0.1547 -0.0102 -0.0043 0.0180  125 PRO   A O   
2941 C CB  A PRO   A 125 ? 0.0987 0.1035 0.1276 -0.0079 0.0043  0.0316  125 PRO   A CB  
2942 C CB  B PRO   A 125 ? 0.1399 0.1308 0.1420 -0.0031 0.0002  0.0101  125 PRO   A CB  
2943 C CB  C PRO   A 125 ? 0.1400 0.1262 0.1467 -0.0095 0.0024  0.0125  125 PRO   A CB  
2944 C CG  A PRO   A 125 ? 0.0894 0.0915 0.1199 -0.0053 0.0131  0.0228  125 PRO   A CG  
2945 C CG  B PRO   A 125 ? 0.1409 0.1313 0.1484 -0.0067 0.0010  0.0114  125 PRO   A CG  
2946 C CG  C PRO   A 125 ? 0.1419 0.1275 0.1540 -0.0125 0.0035  0.0139  125 PRO   A CG  
2947 C CD  A PRO   A 125 ? 0.0878 0.1010 0.1278 -0.0064 0.0107  0.0307  125 PRO   A CD  
2948 C CD  B PRO   A 125 ? 0.1322 0.1338 0.1474 -0.0068 0.0007  0.0171  125 PRO   A CD  
2949 C CD  C PRO   A 125 ? 0.1316 0.1299 0.1515 -0.0121 0.0036  0.0200  125 PRO   A CD  
2971 N N   A LEU   A 126 ? 0.0926 0.1262 0.1530 -0.0079 0.0013  0.0299  126 LEU   A N   
2972 N N   B LEU   A 126 ? 0.1399 0.1393 0.1619 -0.0006 -0.0069 -0.0004 126 LEU   A N   
2973 N N   C LEU   A 126 ? 0.1409 0.1447 0.1552 -0.0151 0.0017  0.0117  126 LEU   A N   
2974 C CA  A LEU   A 126 ? 0.1069 0.1314 0.1645 -0.0050 -0.0046 0.0292  126 LEU   A CA  
2975 C CA  B LEU   A 126 ? 0.1416 0.1269 0.1630 -0.0085 -0.0039 0.0087  126 LEU   A CA  
2976 C CA  C LEU   A 126 ? 0.1473 0.1439 0.1631 -0.0231 0.0013  0.0165  126 LEU   A CA  
2977 C C   A LEU   A 126 ? 0.1215 0.1334 0.1747 0.0024  -0.0032 0.0122  126 LEU   A C   
2978 C C   B LEU   A 126 ? 0.1425 0.1160 0.1645 -0.0019 0.0027  0.0071  126 LEU   A C   
2979 C C   C LEU   A 126 ? 0.1508 0.1458 0.1731 -0.0185 0.0082  0.0165  126 LEU   A C   
2980 O O   A LEU   A 126 ? 0.1362 0.1307 0.1852 -0.0035 -0.0040 -0.0004 126 LEU   A O   
2981 O O   B LEU   A 126 ? 0.1556 0.1135 0.1837 -0.0083 0.0219  0.0069  126 LEU   A O   
2982 O O   C LEU   A 126 ? 0.1629 0.1478 0.1965 -0.0245 0.0257  0.0153  126 LEU   A O   
2983 C CB  A LEU   A 126 ? 0.1134 0.1466 0.1725 -0.0032 -0.0150 0.0401  126 LEU   A CB  
2984 C CB  B LEU   A 126 ? 0.1457 0.1398 0.1690 -0.0193 -0.0078 0.0174  126 LEU   A CB  
2985 C CB  C LEU   A 126 ? 0.1537 0.1545 0.1702 -0.0296 -0.0046 0.0197  126 LEU   A CB  
2986 C CG  A LEU   A 126 ? 0.1087 0.1689 0.1938 -0.0009 -0.0149 0.0443  126 LEU   A CG  
2987 C CG  B LEU   A 126 ? 0.1461 0.1494 0.1834 -0.0216 -0.0112 0.0285  126 LEU   A CG  
2988 C CG  C LEU   A 126 ? 0.1565 0.1613 0.1843 -0.0277 -0.0091 0.0259  126 LEU   A CG  
2989 C CD1 A LEU   A 126 ? 0.1166 0.1776 0.2038 0.0006  -0.0070 0.0451  126 LEU   A CD1 
2990 C CD1 B LEU   A 126 ? 0.1469 0.1547 0.1941 -0.0163 -0.0185 0.0250  126 LEU   A CD1 
2991 C CD1 C LEU   A 126 ? 0.1578 0.1656 0.1944 -0.0217 -0.0160 0.0223  126 LEU   A CD1 
2992 C CD2 A LEU   A 126 ? 0.1220 0.1683 0.1989 -0.0102 -0.0166 0.0558  126 LEU   A CD2 
2993 C CD2 B LEU   A 126 ? 0.1544 0.1484 0.1942 -0.0282 -0.0067 0.0366  126 LEU   A CD2 
2994 C CD2 C LEU   A 126 ? 0.1646 0.1597 0.1958 -0.0322 -0.0065 0.0314  126 LEU   A CD2 
3028 N N   A LEU   A 127 ? 0.1178 0.1415 0.1815 0.0028  0.0075  0.0208  127 LEU   A N   
3029 N N   B LEU   A 127 ? 0.1306 0.1149 0.1487 0.0072  -0.0049 0.0253  127 LEU   A N   
3030 N N   C LEU   A 127 ? 0.1422 0.1506 0.1631 -0.0096 0.0049  0.0281  127 LEU   A N   
3031 C CA  A LEU   A 127 ? 0.1241 0.1511 0.1726 -0.0046 0.0096  0.0195  127 LEU   A CA  
3032 C CA  B LEU   A 127 ? 0.1279 0.1242 0.1591 0.0036  0.0008  0.0261  127 LEU   A CA  
3033 C CA  C LEU   A 127 ? 0.1407 0.1615 0.1671 -0.0076 0.0119  0.0283  127 LEU   A CA  
3034 C C   A LEU   A 127 ? 0.1313 0.1482 0.1556 -0.0072 0.0163  0.0192  127 LEU   A C   
3035 C C   B LEU   A 127 ? 0.1280 0.1198 0.1664 0.0005  -0.0091 0.0239  127 LEU   A C   
3036 C C   C LEU   A 127 ? 0.1443 0.1680 0.1629 -0.0035 0.0119  0.0243  127 LEU   A C   
3037 O O   A LEU   A 127 ? 0.1367 0.1510 0.1477 -0.0167 0.0237  0.0129  127 LEU   A O   
3038 O O   B LEU   A 127 ? 0.1216 0.1087 0.1656 -0.0034 -0.0214 0.0183  127 LEU   A O   
3039 O O   C LEU   A 127 ? 0.1514 0.1677 0.1607 -0.0068 0.0073  0.0250  127 LEU   A O   
3040 C CB  A LEU   A 127 ? 0.1276 0.1573 0.1665 0.0004  0.0049  0.0200  127 LEU   A CB  
3041 C CB  B LEU   A 127 ? 0.1275 0.1376 0.1636 0.0034  0.0067  0.0223  127 LEU   A CB  
3042 C CB  C LEU   A 127 ? 0.1406 0.1686 0.1704 -0.0078 0.0135  0.0263  127 LEU   A CB  
3043 C CG  A LEU   A 127 ? 0.1370 0.1582 0.1762 0.0038  -0.0074 0.0242  127 LEU   A CG  
3044 C CG  B LEU   A 127 ? 0.1298 0.1491 0.1656 0.0027  0.0056  0.0274  127 LEU   A CG  
3045 C CG  C LEU   A 127 ? 0.1436 0.1748 0.1734 -0.0088 0.0100  0.0298  127 LEU   A CG  
3046 C CD1 A LEU   A 127 ? 0.1389 0.1536 0.1855 -0.0046 -0.0104 0.0223  127 LEU   A CD1 
3047 C CD1 B LEU   A 127 ? 0.1282 0.1558 0.1764 0.0085  0.0025  0.0302  127 LEU   A CD1 
3048 C CD1 C LEU   A 127 ? 0.1425 0.1797 0.1842 -0.0043 0.0072  0.0320  127 LEU   A CD1 
3049 C CD2 A LEU   A 127 ? 0.1487 0.1585 0.1910 0.0138  -0.0185 0.0266  127 LEU   A CD2 
3050 C CD2 B LEU   A 127 ? 0.1449 0.1578 0.1766 -0.0008 -0.0009 0.0224  127 LEU   A CD2 
3051 C CD2 C LEU   A 127 ? 0.1571 0.1802 0.1831 -0.0112 0.0017  0.0248  127 LEU   A CD2 
3085 N N   A SER   A 128 ? 0.1403 0.1453 0.1635 -0.0075 0.0046  0.0292  128 SER   A N   
3086 N N   B SER   A 128 ? 0.1399 0.1318 0.1731 0.0029  -0.0033 0.0194  128 SER   A N   
3087 N N   C SER   A 128 ? 0.1430 0.1747 0.1679 -0.0001 0.0104  0.0244  128 SER   A N   
3088 C CA  A SER   A 128 ? 0.1450 0.1570 0.1579 -0.0094 -0.0219 0.0388  128 SER   A CA  
3089 C CA  B SER   A 128 ? 0.1583 0.1573 0.1879 0.0137  0.0046  0.0258  128 SER   A CA  
3090 C CA  C SER   A 128 ? 0.1421 0.1855 0.1631 -0.0019 0.0005  0.0228  128 SER   A CA  
3091 C C   A SER   A 128 ? 0.1516 0.1556 0.1684 -0.0117 -0.0405 0.0506  128 SER   A C   
3092 C C   B SER   A 128 ? 0.1867 0.1928 0.2189 0.0207  0.0026  0.0248  128 SER   A C   
3093 C C   C SER   A 128 ? 0.1480 0.1875 0.1629 -0.0071 0.0020  0.0350  128 SER   A C   
3094 O O   A SER   A 128 ? 0.1631 0.1720 0.1727 -0.0076 -0.0351 0.0490  128 SER   A O   
3095 O O   B SER   A 128 ? 0.1904 0.2007 0.2256 0.0218  0.0109  0.0324  128 SER   A O   
3096 O O   C SER   A 128 ? 0.1370 0.1829 0.1406 -0.0175 0.0036  0.0382  128 SER   A O   
3097 C CB  A SER   A 128 ? 0.1404 0.1653 0.1504 -0.0142 -0.0210 0.0450  128 SER   A CB  
3098 C CB  B SER   A 128 ? 0.1466 0.1542 0.1698 0.0100  0.0060  0.0259  128 SER   A CB  
3099 C CB  C SER   A 128 ? 0.1328 0.1914 0.1539 -0.0018 -0.0095 0.0189  128 SER   A CB  
3100 O OG  A SER   A 128 ? 0.1231 0.1688 0.1511 -0.0131 -0.0169 0.0475  128 SER   A OG  
3101 O OG  B SER   A 128 ? 0.1379 0.1554 0.1633 0.0006  0.0092  0.0232  128 SER   A OG  
3102 O OG  C SER   A 128 ? 0.1235 0.1952 0.1570 -0.0024 -0.0151 0.0107  128 SER   A OG  
3118 N N   A ALA   A 129 ? 0.1543 0.1608 0.2102 -0.0060 -0.0358 0.0654  129 ALA   A N   
3119 N N   B ALA   A 129 ? 0.2072 0.2201 0.2455 0.0310  -0.0107 0.0216  129 ALA   A N   
3120 N N   C ALA   A 129 ? 0.1677 0.2097 0.1901 0.0111  -0.0052 0.0392  129 ALA   A N   
3121 C CA  A ALA   A 129 ? 0.1636 0.1678 0.2575 -0.0098 -0.0320 0.0632  129 ALA   A CA  
3122 C CA  B ALA   A 129 ? 0.2303 0.2471 0.2749 0.0249  -0.0215 0.0207  129 ALA   A CA  
3123 C CA  C ALA   A 129 ? 0.1928 0.2310 0.2356 0.0053  -0.0031 0.0235  129 ALA   A CA  
3124 C C   A ALA   A 129 ? 0.1763 0.1676 0.2479 -0.0136 -0.0416 0.0639  129 ALA   A C   
3125 C C   B ALA   A 129 ? 0.2588 0.2626 0.2959 0.0149  -0.0246 0.0201  129 ALA   A C   
3126 C C   C ALA   A 129 ? 0.2144 0.2443 0.2693 -0.0052 -0.0039 0.0054  129 ALA   A C   
3127 O O   A ALA   A 129 ? 0.1752 0.1688 0.2749 -0.0318 -0.0437 0.0627  129 ALA   A O   
3128 O O   B ALA   A 129 ? 0.2662 0.2689 0.3103 0.0109  -0.0265 0.0213  129 ALA   A O   
3129 O O   C ALA   A 129 ? 0.2248 0.2528 0.2818 -0.0128 -0.0066 -0.0019 129 ALA   A O   
3130 C CB  A ALA   A 129 ? 0.1688 0.1757 0.2823 0.0059  -0.0256 0.0744  129 ALA   A CB  
3131 C CB  B ALA   A 129 ? 0.2247 0.2517 0.2809 0.0221  -0.0283 0.0168  129 ALA   A CB  
3132 C CB  C ALA   A 129 ? 0.1970 0.2372 0.2519 0.0041  -0.0028 0.0238  129 ALA   A CB  
3148 N N   A GLY   A 130 ? 0.1895 0.1555 0.2380 -0.0054 -0.0312 0.0465  130 GLY   A N   
3149 N N   B GLY   A 130 ? 0.2769 0.2708 0.2969 0.0106  -0.0302 0.0215  130 GLY   A N   
3150 N N   C GLY   A 130 ? 0.2212 0.2480 0.2815 -0.0067 -0.0095 0.0034  130 GLY   A N   
3151 C CA  A GLY   A 130 ? 0.2099 0.1517 0.2375 -0.0074 -0.0214 0.0359  130 GLY   A CA  
3152 C CA  B GLY   A 130 ? 0.2889 0.2718 0.2863 0.0068  -0.0382 0.0252  130 GLY   A CA  
3153 C CA  C GLY   A 130 ? 0.2201 0.2452 0.2798 -0.0086 -0.0080 -0.0011 130 GLY   A CA  
3154 C C   A GLY   A 130 ? 0.2206 0.1365 0.2334 -0.0081 -0.0195 0.0320  130 GLY   A C   
3155 C C   B GLY   A 130 ? 0.2987 0.2709 0.2785 0.0056  -0.0478 0.0271  130 GLY   A C   
3156 C C   C GLY   A 130 ? 0.2162 0.2410 0.2691 -0.0098 -0.0089 -0.0031 130 GLY   A C   
3157 O O   A GLY   A 130 ? 0.2237 0.1176 0.2335 -0.0113 -0.0293 0.0233  130 GLY   A O   
3158 O O   B GLY   A 130 ? 0.2995 0.2593 0.2474 0.0092  -0.0722 0.0434  130 GLY   A O   
3159 O O   C GLY   A 130 ? 0.2201 0.2451 0.2750 -0.0118 -0.0115 -0.0039 130 GLY   A O   
3169 N N   A ILE   A 131 ? 0.2200 0.1323 0.2329 -0.0060 -0.0213 0.0308  131 ILE   A N   
3170 N N   B ILE   A 131 ? 0.3061 0.2772 0.2935 0.0089  -0.0410 0.0329  131 ILE   A N   
3171 N N   C ILE   A 131 ? 0.2114 0.2302 0.2593 -0.0071 -0.0064 0.0004  131 ILE   A N   
3172 C CA  A ILE   A 131 ? 0.2082 0.1266 0.2064 -0.0050 -0.0416 0.0311  131 ILE   A CA  
3173 C CA  B ILE   A 131 ? 0.3190 0.2901 0.3200 0.0108  -0.0289 0.0294  131 ILE   A CA  
3174 C CA  C ILE   A 131 ? 0.2089 0.2202 0.2368 -0.0025 -0.0097 0.0068  131 ILE   A CA  
3175 C C   A ILE   A 131 ? 0.1966 0.1353 0.1923 -0.0092 -0.0444 0.0382  131 ILE   A C   
3176 C C   B ILE   A 131 ? 0.3293 0.3043 0.3433 0.0117  -0.0234 0.0217  131 ILE   A C   
3177 C C   C ILE   A 131 ? 0.2172 0.2174 0.2201 0.0030  -0.0124 0.0236  131 ILE   A C   
3178 O O   A ILE   A 131 ? 0.1968 0.1559 0.1820 -0.0154 -0.0451 0.0371  131 ILE   A O   
3179 O O   B ILE   A 131 ? 0.3307 0.3069 0.3559 0.0122  -0.0201 0.0216  131 ILE   A O   
3180 O O   C ILE   A 131 ? 0.2203 0.2142 0.2070 0.0042  -0.0148 0.0301  131 ILE   A O   
3181 C CB  A ILE   A 131 ? 0.2127 0.1398 0.2159 -0.0007 -0.0464 0.0127  131 ILE   A CB  
3182 C CB  B ILE   A 131 ? 0.3213 0.2909 0.3215 0.0114  -0.0239 0.0286  131 ILE   A CB  
3183 C CB  C ILE   A 131 ? 0.2014 0.2205 0.2348 -0.0060 -0.0097 -0.0061 131 ILE   A CB  
3184 C CG1 A ILE   A 131 ? 0.2139 0.1617 0.2137 0.0010  -0.0575 0.0062  131 ILE   A CG1 
3185 C CG1 B ILE   A 131 ? 0.3211 0.2878 0.3108 0.0124  -0.0236 0.0292  131 ILE   A CG1 
3186 C CG1 C ILE   A 131 ? 0.2001 0.2222 0.2284 -0.0064 -0.0040 -0.0088 131 ILE   A CG1 
3187 C CG2 A ILE   A 131 ? 0.2147 0.1346 0.2196 0.0002  -0.0470 0.0132  131 ILE   A CG2 
3188 C CG2 B ILE   A 131 ? 0.3230 0.2936 0.3274 0.0112  -0.0202 0.0251  131 ILE   A CG2 
3189 C CG2 C ILE   A 131 ? 0.1983 0.2199 0.2322 -0.0065 -0.0136 -0.0087 131 ILE   A CG2 
3190 C CD1 A ILE   A 131 ? 0.2143 0.1717 0.2289 -0.0022 -0.0544 -0.0036 131 ILE   A CD1 
3191 C CD1 B ILE   A 131 ? 0.3204 0.2850 0.3040 0.0134  -0.0230 0.0304  131 ILE   A CD1 
3192 C CD1 C ILE   A 131 ? 0.2007 0.2231 0.2266 -0.0074 0.0004  -0.0132 131 ILE   A CD1 
3226 N N   A PHE   A 132 ? 0.1910 0.1270 0.1977 -0.0028 -0.0434 0.0355  132 PHE   A N   
3227 N N   B PHE   A 132 ? 0.3407 0.3188 0.3551 0.0133  -0.0197 0.0134  132 PHE   A N   
3228 N N   C PHE   A 132 ? 0.2177 0.2200 0.2135 0.0098  -0.0171 0.0387  132 PHE   A N   
3229 C CA  A PHE   A 132 ? 0.1886 0.1362 0.1902 -0.0036 -0.0438 0.0205  132 PHE   A CA  
3230 C CA  B PHE   A 132 ? 0.3508 0.3329 0.3554 0.0130  -0.0180 0.0054  132 PHE   A CA  
3231 C CA  C PHE   A 132 ? 0.2185 0.2309 0.2094 0.0097  -0.0213 0.0439  132 PHE   A CA  
3232 C C   A PHE   A 132 ? 0.1834 0.1355 0.1906 -0.0023 -0.0521 0.0357  132 PHE   A C   
3233 C C   B PHE   A 132 ? 0.3520 0.3379 0.3456 0.0132  -0.0277 0.0001  132 PHE   A C   
3234 C C   C PHE   A 132 ? 0.2385 0.2528 0.2169 0.0112  -0.0213 0.0468  132 PHE   A C   
3235 O O   A PHE   A 132 ? 0.1947 0.1535 0.1868 -0.0087 -0.0524 0.0390  132 PHE   A O   
3236 O O   B PHE   A 132 ? 0.3536 0.3363 0.3455 0.0147  -0.0267 -0.0021 132 PHE   A O   
3237 O O   C PHE   A 132 ? 0.2418 0.2567 0.1982 0.0155  -0.0321 0.0544  132 PHE   A O   
3238 C CB  A PHE   A 132 ? 0.1910 0.1401 0.1591 0.0018  -0.0519 0.0188  132 PHE   A CB  
3239 C CB  B PHE   A 132 ? 0.3607 0.3425 0.3809 0.0120  -0.0034 -0.0001 132 PHE   A CB  
3240 C CB  C PHE   A 132 ? 0.2006 0.2186 0.2017 0.0140  -0.0305 0.0420  132 PHE   A CB  
3241 C CG  A PHE   A 132 ? 0.1907 0.1449 0.1313 0.0098  -0.0469 0.0092  132 PHE   A CG  
3242 C CG  B PHE   A 132 ? 0.3691 0.3511 0.4008 0.0117  0.0099  -0.0061 132 PHE   A CG  
3243 C CG  C PHE   A 132 ? 0.1915 0.2114 0.2107 0.0182  -0.0334 0.0327  132 PHE   A CG  
3244 C CD1 A PHE   A 132 ? 0.1929 0.1526 0.1410 0.0240  -0.0429 0.0024  132 PHE   A CD1 
3245 C CD1 B PHE   A 132 ? 0.3732 0.3552 0.4105 0.0114  0.0161  -0.0078 132 PHE   A CD1 
3246 C CD1 C PHE   A 132 ? 0.1931 0.2110 0.2217 0.0177  -0.0316 0.0265  132 PHE   A CD1 
3247 C CD2 A PHE   A 132 ? 0.1891 0.1568 0.1180 0.0049  -0.0490 0.0007  132 PHE   A CD2 
3248 C CD2 B PHE   A 132 ? 0.3730 0.3547 0.4104 0.0119  0.0159  -0.0083 132 PHE   A CD2 
3249 C CD2 C PHE   A 132 ? 0.1866 0.2121 0.2101 0.0195  -0.0301 0.0217  132 PHE   A CD2 
3250 C CE1 A PHE   A 132 ? 0.1937 0.1600 0.1232 0.0222  -0.0423 -0.0019 132 PHE   A CE1 
3251 C CE1 B PHE   A 132 ? 0.3756 0.3579 0.4170 0.0115  0.0203  -0.0093 132 PHE   A CE1 
3252 C CE1 C PHE   A 132 ? 0.1917 0.2125 0.2286 0.0180  -0.0311 0.0240  132 PHE   A CE1 
3253 C CE2 A PHE   A 132 ? 0.1872 0.1596 0.1204 0.0129  -0.0461 -0.0038 132 PHE   A CE2 
3254 C CE2 B PHE   A 132 ? 0.3758 0.3577 0.4189 0.0117  0.0196  -0.0093 132 PHE   A CE2 
3255 C CE2 C PHE   A 132 ? 0.1871 0.2125 0.2169 0.0175  -0.0307 0.0184  132 PHE   A CE2 
3256 C CZ  A PHE   A 132 ? 0.1869 0.1593 0.1045 0.0172  -0.0510 -0.0015 132 PHE   A CZ  
3257 C CZ  B PHE   A 132 ? 0.3764 0.3587 0.4191 0.0120  0.0216  -0.0096 132 PHE   A CZ  
3258 C CZ  C PHE   A 132 ? 0.1887 0.2121 0.2239 0.0168  -0.0351 0.0194  132 PHE   A CZ  
3286 N N   A GLY   A 133 ? 0.1687 0.1237 0.1828 0.0026  -0.0632 0.0473  133 GLY   A N   
3287 N N   B GLY   A 133 ? 0.3517 0.3432 0.3413 0.0131  -0.0318 -0.0018 133 GLY   A N   
3288 N N   C GLY   A 133 ? 0.2522 0.2686 0.2438 0.0072  -0.0151 0.0421  133 GLY   A N   
3289 C CA  A GLY   A 133 ? 0.1641 0.1332 0.1772 0.0017  -0.0567 0.0357  133 GLY   A CA  
3290 C CA  B GLY   A 133 ? 0.3503 0.3454 0.3377 0.0115  -0.0345 -0.0042 133 GLY   A CA  
3291 C CA  C GLY   A 133 ? 0.2660 0.2817 0.2722 0.0041  -0.0089 0.0322  133 GLY   A CA  
3292 C C   A GLY   A 133 ? 0.1537 0.1493 0.1602 -0.0020 -0.0512 0.0148  133 GLY   A C   
3293 C C   B GLY   A 133 ? 0.3489 0.3465 0.3399 0.0086  -0.0350 -0.0057 133 GLY   A C   
3294 C C   C GLY   A 133 ? 0.2782 0.2936 0.2976 0.0012  -0.0013 0.0210  133 GLY   A C   
3295 O O   A GLY   A 133 ? 0.1599 0.1640 0.1542 -0.0031 -0.0530 -0.0059 133 GLY   A O   
3296 O O   B GLY   A 133 ? 0.3515 0.3499 0.3432 0.0073  -0.0383 -0.0099 133 GLY   A O   
3297 O O   C GLY   A 133 ? 0.2845 0.2974 0.3102 0.0022  -0.0047 0.0170  133 GLY   A O   
3307 N N   A ALA   A 134 ? 0.1388 0.1410 0.1487 -0.0047 -0.0466 0.0088  134 ALA   A N   
3308 N N   B ALA   A 134 ? 0.3441 0.3434 0.3446 0.0057  -0.0297 -0.0009 134 ALA   A N   
3309 N N   C ALA   A 134 ? 0.2852 0.3011 0.3117 -0.0043 0.0078  0.0151  134 ALA   A N   
3310 C CA  A ALA   A 134 ? 0.1384 0.1421 0.1677 -0.0085 -0.0370 0.0122  134 ALA   A CA  
3311 C CA  B ALA   A 134 ? 0.3375 0.3378 0.3433 0.0021  -0.0198 0.0045  134 ALA   A CA  
3312 C CA  C ALA   A 134 ? 0.2903 0.3065 0.3188 -0.0096 0.0138  0.0119  134 ALA   A CA  
3313 C C   A ALA   A 134 ? 0.1425 0.1493 0.1503 -0.0118 -0.0386 0.0222  134 ALA   A C   
3314 C C   B ALA   A 134 ? 0.3284 0.3316 0.3409 -0.0008 -0.0123 0.0092  134 ALA   A C   
3315 C C   C ALA   A 134 ? 0.2901 0.3066 0.3209 -0.0146 0.0098  0.0154  134 ALA   A C   
3316 O O   A ALA   A 134 ? 0.1515 0.1537 0.1680 -0.0180 -0.0282 0.0268  134 ALA   A O   
3317 O O   B ALA   A 134 ? 0.3318 0.3356 0.3574 0.0003  -0.0089 0.0078  134 ALA   A O   
3318 O O   C ALA   A 134 ? 0.2928 0.3102 0.3364 -0.0140 0.0086  0.0124  134 ALA   A O   
3319 C CB  A ALA   A 134 ? 0.1370 0.1397 0.1753 -0.0104 -0.0335 0.0143  134 ALA   A CB  
3320 C CB  B ALA   A 134 ? 0.3388 0.3387 0.3423 0.0021  -0.0199 0.0053  134 ALA   A CB  
3321 C CB  C ALA   A 134 ? 0.2934 0.3086 0.3191 -0.0101 0.0170  0.0084  134 ALA   A CB  
3337 N N   A ASP   A 135 ? 0.1503 0.1595 0.1582 -0.0118 -0.0286 0.0279  135 ASP   A N   
3338 N N   B ASP   A 135 ? 0.3153 0.3222 0.3173 -0.0050 -0.0106 0.0150  135 ASP   A N   
3339 N N   C ASP   A 135 ? 0.2845 0.3032 0.2985 -0.0187 0.0013  0.0237  135 ASP   A N   
3340 C CA  A ASP   A 135 ? 0.1514 0.1852 0.1823 -0.0206 -0.0400 0.0375  135 ASP   A CA  
3341 C CA  B ASP   A 135 ? 0.3006 0.3107 0.2920 -0.0078 -0.0148 0.0186  135 ASP   A CA  
3342 C CA  C ASP   A 135 ? 0.2782 0.2987 0.2798 -0.0237 -0.0112 0.0234  135 ASP   A CA  
3343 C C   A ASP   A 135 ? 0.1379 0.1720 0.1838 -0.0105 -0.0426 0.0569  135 ASP   A C   
3344 C C   B ASP   A 135 ? 0.2801 0.2937 0.2580 -0.0039 -0.0159 0.0303  135 ASP   A C   
3345 C C   C ASP   A 135 ? 0.2640 0.2876 0.2502 -0.0198 -0.0163 0.0400  135 ASP   A C   
3346 O O   A ASP   A 135 ? 0.1269 0.1482 0.1600 -0.0137 -0.0526 0.0545  135 ASP   A O   
3347 O O   B ASP   A 135 ? 0.2773 0.2892 0.2441 -0.0091 -0.0136 0.0276  135 ASP   A O   
3348 O O   C ASP   A 135 ? 0.2640 0.2868 0.2435 -0.0279 -0.0127 0.0407  135 ASP   A O   
3349 C CB  A ASP   A 135 ? 0.1700 0.2177 0.2150 -0.0299 -0.0443 0.0278  135 ASP   A CB  
3350 C CB  B ASP   A 135 ? 0.3063 0.3161 0.3041 -0.0146 -0.0147 0.0109  135 ASP   A CB  
3351 C CB  C ASP   A 135 ? 0.2866 0.3057 0.2911 -0.0306 -0.0152 0.0083  135 ASP   A CB  
3352 C CG  A ASP   A 135 ? 0.1843 0.2420 0.2531 -0.0377 -0.0346 0.0187  135 ASP   A CG  
3353 C CG  B ASP   A 135 ? 0.3120 0.3223 0.3169 -0.0200 -0.0121 0.0062  135 ASP   A CG  
3354 C CG  C ASP   A 135 ? 0.2945 0.3157 0.3034 -0.0356 -0.0179 -0.0016 135 ASP   A CG  
3355 O OD1 A ASP   A 135 ? 0.1786 0.2542 0.2622 -0.0424 -0.0582 0.0284  135 ASP   A OD1 
3356 O OD1 B ASP   A 135 ? 0.3157 0.3278 0.3295 -0.0218 -0.0103 0.0078  135 ASP   A OD1 
3357 O OD1 C ASP   A 135 ? 0.2980 0.3185 0.3113 -0.0364 -0.0185 -0.0056 135 ASP   A OD1 
3358 O OD2 A ASP   A 135 ? 0.2083 0.2529 0.2962 -0.0305 0.0051  0.0189  135 ASP   A OD2 
3359 O OD2 B ASP   A 135 ? 0.3131 0.3224 0.3244 -0.0217 -0.0123 0.0027  135 ASP   A OD2 
3360 O OD2 C ASP   A 135 ? 0.2963 0.3188 0.3132 -0.0376 -0.0223 -0.0068 135 ASP   A OD2 
3373 N N   A PRO   A 136 ? 0.1398 0.1771 0.2151 0.0150  -0.0280 0.0799  136 PRO   A N   
3374 N N   B PRO   A 136 ? 0.2635 0.2823 0.2484 0.0050  -0.0128 0.0410  136 PRO   A N   
3375 N N   C PRO   A 136 ? 0.2510 0.2785 0.2426 -0.0093 -0.0206 0.0528  136 PRO   A N   
3376 C CA  A PRO   A 136 ? 0.1313 0.1679 0.2246 0.0186  -0.0143 0.0771  136 PRO   A CA  
3377 C CA  B PRO   A 136 ? 0.2505 0.2741 0.2404 0.0074  -0.0092 0.0374  136 PRO   A CA  
3378 C CA  C PRO   A 136 ? 0.2410 0.2749 0.2394 -0.0059 -0.0201 0.0523  136 PRO   A CA  
3379 C C   A PRO   A 136 ? 0.1007 0.1641 0.2213 0.0054  -0.0145 0.0740  136 PRO   A C   
3380 C C   B PRO   A 136 ? 0.2316 0.2675 0.2315 0.0087  -0.0168 0.0326  136 PRO   A C   
3381 C C   C PRO   A 136 ? 0.2274 0.2716 0.2323 -0.0084 -0.0324 0.0489  136 PRO   A C   
3382 O O   A PRO   A 136 ? 0.0844 0.1503 0.2123 0.0032  -0.0118 0.0775  136 PRO   A O   
3383 O O   B PRO   A 136 ? 0.2267 0.2637 0.2219 0.0114  -0.0199 0.0317  136 PRO   A O   
3384 O O   C PRO   A 136 ? 0.2217 0.2666 0.2200 -0.0080 -0.0382 0.0515  136 PRO   A O   
3385 C CB  A PRO   A 136 ? 0.1527 0.1700 0.2392 0.0246  -0.0015 0.0693  136 PRO   A CB  
3386 C CB  B PRO   A 136 ? 0.2564 0.2750 0.2479 0.0070  -0.0026 0.0371  136 PRO   A CB  
3387 C CB  C PRO   A 136 ? 0.2458 0.2738 0.2475 -0.0025 -0.0150 0.0531  136 PRO   A CB  
3388 C CG  A PRO   A 136 ? 0.1568 0.1803 0.2456 0.0246  -0.0080 0.0721  136 PRO   A CG  
3389 C CG  B PRO   A 136 ? 0.2588 0.2766 0.2514 0.0068  -0.0048 0.0424  136 PRO   A CG  
3390 C CG  C PRO   A 136 ? 0.2480 0.2747 0.2518 -0.0023 -0.0173 0.0539  136 PRO   A CG  
3391 C CD  A PRO   A 136 ? 0.1531 0.1809 0.2398 0.0279  -0.0210 0.0856  136 PRO   A CD  
3392 C CD  B PRO   A 136 ? 0.2620 0.2795 0.2540 0.0082  -0.0092 0.0446  136 PRO   A CD  
3393 C CD  C PRO   A 136 ? 0.2501 0.2750 0.2488 -0.0041 -0.0200 0.0550  136 PRO   A CD  
3415 N N   A ILE   A 137 ? 0.1074 0.1859 0.2265 -0.0021 -0.0263 0.0696  137 ILE   A N   
3416 N N   B ILE   A 137 ? 0.2219 0.2672 0.2287 0.0074  -0.0252 0.0314  137 ILE   A N   
3417 N N   C ILE   A 137 ? 0.2235 0.2738 0.2362 -0.0116 -0.0381 0.0423  137 ILE   A N   
3418 C CA  A ILE   A 137 ? 0.1129 0.2063 0.2109 -0.0129 -0.0322 0.0667  137 ILE   A CA  
3419 C CA  B ILE   A 137 ? 0.2121 0.2680 0.2288 0.0060  -0.0299 0.0251  137 ILE   A CA  
3420 C CA  C ILE   A 137 ? 0.2208 0.2773 0.2442 -0.0143 -0.0413 0.0320  137 ILE   A CA  
3421 C C   A ILE   A 137 ? 0.1090 0.1939 0.1816 -0.0251 -0.0397 0.0676  137 ILE   A C   
3422 C C   B ILE   A 137 ? 0.2012 0.2608 0.2146 0.0022  -0.0230 0.0179  137 ILE   A C   
3423 C C   C ILE   A 137 ? 0.2164 0.2744 0.2447 -0.0180 -0.0359 0.0276  137 ILE   A C   
3424 O O   A ILE   A 137 ? 0.1063 0.1793 0.1632 -0.0391 -0.0362 0.0569  137 ILE   A O   
3425 O O   B ILE   A 137 ? 0.1990 0.2542 0.2132 0.0011  -0.0136 0.0106  137 ILE   A O   
3426 O O   C ILE   A 137 ? 0.2139 0.2715 0.2480 -0.0204 -0.0290 0.0203  137 ILE   A O   
3427 C CB  A ILE   A 137 ? 0.1122 0.2363 0.2276 -0.0210 -0.0503 0.0647  137 ILE   A CB  
3428 C CB  B ILE   A 137 ? 0.2143 0.2749 0.2481 0.0063  -0.0416 0.0282  137 ILE   A CB  
3429 C CB  C ILE   A 137 ? 0.2237 0.2820 0.2582 -0.0148 -0.0491 0.0309  137 ILE   A CB  
3430 C CG1 A ILE   A 137 ? 0.1331 0.2577 0.2531 -0.0159 -0.0344 0.0615  137 ILE   A CG1 
3431 C CG1 B ILE   A 137 ? 0.2188 0.2803 0.2615 0.0105  -0.0451 0.0338  137 ILE   A CG1 
3432 C CG1 C ILE   A 137 ? 0.2284 0.2863 0.2705 -0.0098 -0.0503 0.0349  137 ILE   A CG1 
3433 C CG2 A ILE   A 137 ? 0.1164 0.2427 0.2286 -0.0227 -0.0666 0.0660  137 ILE   A CG2 
3434 C CG2 B ILE   A 137 ? 0.2184 0.2767 0.2516 0.0053  -0.0434 0.0244  137 ILE   A CG2 
3435 C CG2 C ILE   A 137 ? 0.2273 0.2825 0.2600 -0.0160 -0.0502 0.0270  137 ILE   A CG2 
3436 C CD1 A ILE   A 137 ? 0.1453 0.2680 0.2668 -0.0153 -0.0253 0.0602  137 ILE   A CD1 
3437 C CD1 B ILE   A 137 ? 0.2212 0.2835 0.2718 0.0119  -0.0454 0.0384  137 ILE   A CD1 
3438 C CD1 C ILE   A 137 ? 0.2312 0.2888 0.2800 -0.0071 -0.0487 0.0384  137 ILE   A CD1 
3472 N N   A HIS   A 138 ? 0.1238 0.2016 0.1813 -0.0183 -0.0279 0.0632  138 HIS   A N   
3473 N N   B HIS   A 138 ? 0.1953 0.2611 0.2083 0.0012  -0.0240 0.0114  138 HIS   A N   
3474 C CA  A HIS   A 138 ? 0.1309 0.1951 0.1797 -0.0230 -0.0251 0.0545  138 HIS   A CA  
3475 C CA  B HIS   A 138 ? 0.1883 0.2525 0.2033 -0.0013 -0.0278 0.0060  138 HIS   A CA  
3476 C C   A HIS   A 138 ? 0.1252 0.1727 0.1645 -0.0197 -0.0234 0.0535  138 HIS   A C   
3477 C C   B HIS   A 138 ? 0.1662 0.2285 0.1834 -0.0001 -0.0244 0.0040  138 HIS   A C   
3478 O O   A HIS   A 138 ? 0.1305 0.1669 0.1676 -0.0218 -0.0256 0.0435  138 HIS   A O   
3479 O O   B HIS   A 138 ? 0.1692 0.2279 0.1780 -0.0018 -0.0204 0.0062  138 HIS   A O   
3480 C CB  A HIS   A 138 ? 0.1494 0.2062 0.1793 -0.0258 -0.0268 0.0407  138 HIS   A CB  
3481 C CB  B HIS   A 138 ? 0.2049 0.2596 0.2057 -0.0060 -0.0375 0.0089  138 HIS   A CB  
3482 C CG  A HIS   A 138 ? 0.1630 0.2105 0.1873 -0.0286 -0.0177 0.0331  138 HIS   A CG  
3483 C CG  B HIS   A 138 ? 0.2170 0.2591 0.2086 -0.0102 -0.0363 0.0088  138 HIS   A CG  
3484 N ND1 A HIS   A 138 ? 0.1715 0.2138 0.1983 -0.0256 -0.0108 0.0212  138 HIS   A ND1 
3485 N ND1 B HIS   A 138 ? 0.2240 0.2602 0.2205 -0.0093 -0.0357 0.0014  138 HIS   A ND1 
3486 C CD2 A HIS   A 138 ? 0.1668 0.2148 0.1826 -0.0279 -0.0174 0.0363  138 HIS   A CD2 
3487 C CD2 B HIS   A 138 ? 0.2206 0.2614 0.2057 -0.0101 -0.0411 0.0125  138 HIS   A CD2 
3488 C CE1 A HIS   A 138 ? 0.1755 0.2167 0.1964 -0.0258 -0.0079 0.0189  138 HIS   A CE1 
3489 C CE1 B HIS   A 138 ? 0.2267 0.2627 0.2181 -0.0085 -0.0355 0.0035  138 HIS   A CE1 
3490 N NE2 A HIS   A 138 ? 0.1721 0.2171 0.1874 -0.0251 -0.0122 0.0309  138 HIS   A NE2 
3491 N NE2 B HIS   A 138 ? 0.2227 0.2626 0.2053 -0.0066 -0.0417 0.0123  138 HIS   A NE2 
3506 N N   A SER   A 139 ? 0.1200 0.1540 0.1614 -0.0103 -0.0180 0.0532  139 SER   A N   
3507 N N   B SER   A 139 ? 0.1493 0.2048 0.1798 0.0089  -0.0126 0.0060  139 SER   A N   
3508 C CA  A SER   A 139 ? 0.1186 0.1458 0.1556 -0.0065 -0.0037 0.0434  139 SER   A CA  
3509 C CA  B SER   A 139 ? 0.1381 0.1828 0.1779 0.0065  -0.0056 0.0155  139 SER   A CA  
3510 C C   A SER   A 139 ? 0.1139 0.1428 0.1574 -0.0061 0.0045  0.0355  139 SER   A C   
3511 C C   B SER   A 139 ? 0.1303 0.1686 0.1830 -0.0048 -0.0061 0.0223  139 SER   A C   
3512 O O   A SER   A 139 ? 0.1134 0.1324 0.1601 -0.0040 -0.0026 0.0273  139 SER   A O   
3513 O O   B SER   A 139 ? 0.1257 0.1619 0.1760 -0.0040 -0.0106 0.0148  139 SER   A O   
3514 C CB  A SER   A 139 ? 0.1197 0.1408 0.1573 -0.0035 0.0015  0.0420  139 SER   A CB  
3515 C CB  B SER   A 139 ? 0.1348 0.1709 0.1779 0.0117  0.0042  0.0179  139 SER   A CB  
3516 O OG  A SER   A 139 ? 0.1193 0.1299 0.1530 0.0025  -0.0021 0.0375  139 SER   A OG  
3517 O OG  B SER   A 139 ? 0.1311 0.1578 0.1722 0.0168  -0.0002 0.0098  139 SER   A OG  
3528 N N   A LEU   A 140 ? 0.1121 0.1606 0.1620 -0.0036 0.0022  0.0408  140 LEU   A N   
3529 N N   B LEU   A 140 ? 0.1256 0.1687 0.1933 -0.0023 -0.0156 0.0356  140 LEU   A N   
3530 C CA  A LEU   A 140 ? 0.1140 0.1623 0.1600 -0.0037 -0.0044 0.0364  140 LEU   A CA  
3531 C CA  B LEU   A 140 ? 0.1215 0.1531 0.1872 -0.0093 -0.0124 0.0438  140 LEU   A CA  
3532 C C   A LEU   A 140 ? 0.1157 0.1675 0.1668 -0.0119 -0.0029 0.0290  140 LEU   A C   
3533 C C   B LEU   A 140 ? 0.1180 0.1564 0.1893 -0.0155 -0.0082 0.0409  140 LEU   A C   
3534 O O   A LEU   A 140 ? 0.1210 0.1641 0.1692 -0.0053 -0.0021 0.0250  140 LEU   A O   
3535 O O   B LEU   A 140 ? 0.1259 0.1485 0.2048 -0.0104 -0.0140 0.0420  140 LEU   A O   
3536 C CB  A LEU   A 140 ? 0.1143 0.1706 0.1612 -0.0016 -0.0102 0.0346  140 LEU   A CB  
3537 C CB  B LEU   A 140 ? 0.1252 0.1576 0.1931 -0.0170 -0.0109 0.0461  140 LEU   A CB  
3538 C CG  A LEU   A 140 ? 0.1152 0.1727 0.1690 -0.0036 -0.0041 0.0314  140 LEU   A CG  
3539 C CG  B LEU   A 140 ? 0.1285 0.1628 0.2133 -0.0270 0.0002  0.0469  140 LEU   A CG  
3540 C CD1 A LEU   A 140 ? 0.1204 0.1662 0.1749 0.0007  -0.0013 0.0258  140 LEU   A CD1 
3541 C CD1 B LEU   A 140 ? 0.1324 0.1564 0.2069 -0.0218 -0.0032 0.0530  140 LEU   A CD1 
3542 C CD2 A LEU   A 140 ? 0.1239 0.1794 0.1676 -0.0037 -0.0105 0.0367  140 LEU   A CD2 
3543 C CD2 B LEU   A 140 ? 0.1367 0.1695 0.2205 -0.0263 0.0041  0.0510  140 LEU   A CD2 
3566 N N   A ARG   A 141 ? 0.1218 0.1764 0.1779 -0.0151 -0.0152 0.0192  141 ARG   A N   
3567 N N   B ARG   A 141 ? 0.1205 0.1677 0.1898 -0.0106 -0.0149 0.0296  141 ARG   A N   
3568 C CA  A ARG   A 141 ? 0.1363 0.1834 0.1913 -0.0274 -0.0199 0.0121  141 ARG   A CA  
3569 C CA  B ARG   A 141 ? 0.1344 0.1772 0.1963 -0.0232 -0.0125 0.0266  141 ARG   A CA  
3570 C C   A ARG   A 141 ? 0.1330 0.1717 0.1795 -0.0229 -0.0120 0.0170  141 ARG   A C   
3571 C C   B ARG   A 141 ? 0.1324 0.1651 0.1818 -0.0210 -0.0102 0.0235  141 ARG   A C   
3572 O O   A ARG   A 141 ? 0.1324 0.1678 0.1808 -0.0207 -0.0006 0.0125  141 ARG   A O   
3573 O O   B ARG   A 141 ? 0.1373 0.1561 0.1897 -0.0203 -0.0000 0.0144  141 ARG   A O   
3574 C CB  A ARG   A 141 ? 0.1469 0.2004 0.2090 -0.0369 -0.0230 0.0020  141 ARG   A CB  
3575 C CB  B ARG   A 141 ? 0.1417 0.1980 0.2110 -0.0307 -0.0004 0.0229  141 ARG   A CB  
3576 C CG  A ARG   A 141 ? 0.1699 0.2212 0.2280 -0.0359 -0.0295 -0.0041 141 ARG   A CG  
3577 C CG  B ARG   A 141 ? 0.1606 0.2113 0.2263 -0.0298 -0.0010 0.0281  141 ARG   A CG  
3578 C CD  A ARG   A 141 ? 0.1825 0.2383 0.2408 -0.0424 -0.0272 -0.0055 141 ARG   A CD  
3579 C CD  B ARG   A 141 ? 0.1758 0.2157 0.2438 -0.0301 -0.0101 0.0386  141 ARG   A CD  
3580 N NE  A ARG   A 141 ? 0.1893 0.2533 0.2496 -0.0465 -0.0151 -0.0093 141 ARG   A NE  
3581 N NE  B ARG   A 141 ? 0.1866 0.2282 0.2573 -0.0285 -0.0062 0.0451  141 ARG   A NE  
3582 C CZ  A ARG   A 141 ? 0.1889 0.2698 0.2516 -0.0558 -0.0128 -0.0128 141 ARG   A CZ  
3583 C CZ  B ARG   A 141 ? 0.1929 0.2345 0.2528 -0.0299 0.0072  0.0508  141 ARG   A CZ  
3584 N NH1 A ARG   A 141 ? 0.1927 0.2737 0.2625 -0.0567 -0.0112 -0.0149 141 ARG   A NH1 
3585 N NH1 B ARG   A 141 ? 0.2051 0.2399 0.2490 -0.0329 0.0163  0.0462  141 ARG   A NH1 
3586 N NH2 A ARG   A 141 ? 0.1862 0.2822 0.2472 -0.0573 -0.0148 -0.0182 141 ARG   A NH2 
3587 N NH2 B ARG   A 141 ? 0.1913 0.2395 0.2625 -0.0242 0.0100  0.0476  141 ARG   A NH2 
3614 N N   . VAL   A 142 ? 0.1302 0.1677 0.1834 -0.0150 -0.0101 0.0219  142 VAL   A N   
3615 C CA  . VAL   A 142 ? 0.1225 0.1626 0.1793 -0.0129 0.0091  0.0179  142 VAL   A CA  
3616 C C   . VAL   A 142 ? 0.1171 0.1486 0.1717 -0.0161 0.0037  0.0201  142 VAL   A C   
3617 O O   . VAL   A 142 ? 0.1251 0.1512 0.1778 -0.0040 0.0025  0.0238  142 VAL   A O   
3618 C CB  . VAL   A 142 ? 0.1351 0.1776 0.1718 -0.0073 0.0004  0.0249  142 VAL   A CB  
3619 C CG1 . VAL   A 142 ? 0.1362 0.1646 0.1843 -0.0122 0.0039  0.0259  142 VAL   A CG1 
3620 C CG2 . VAL   A 142 ? 0.1550 0.1954 0.1993 -0.0127 -0.0008 0.0222  142 VAL   A CG2 
3631 N N   . CYS   A 143 ? 0.1153 0.1477 0.1689 -0.0124 0.0003  0.0211  143 CYS   A N   
3632 C CA  . CYS   A 143 ? 0.1143 0.1390 0.1765 -0.0090 -0.0051 0.0238  143 CYS   A CA  
3633 C C   . CYS   A 143 ? 0.1165 0.1340 0.1799 -0.0102 -0.0012 0.0230  143 CYS   A C   
3634 O O   . CYS   A 143 ? 0.1140 0.1318 0.1789 -0.0104 -0.0035 0.0293  143 CYS   A O   
3635 C CB  . CYS   A 143 ? 0.1321 0.1444 0.1847 -0.0077 0.0008  0.0368  143 CYS   A CB  
3636 S SG  . CYS   A 143 ? 0.1450 0.1461 0.1844 0.0068  0.0015  0.0169  143 CYS   A SG  
3642 N N   . VAL   A 144 ? 0.1147 0.1389 0.1907 -0.0111 0.0048  0.0186  144 VAL   A N   
3643 C CA  . VAL   A 144 ? 0.1218 0.1473 0.2079 -0.0139 0.0203  0.0265  144 VAL   A CA  
3644 C C   . VAL   A 144 ? 0.1241 0.1333 0.2068 -0.0176 0.0033  0.0232  144 VAL   A C   
3645 O O   . VAL   A 144 ? 0.1425 0.1403 0.2145 -0.0089 -0.0005 0.0286  144 VAL   A O   
3646 C CB  . VAL   A 144 ? 0.1386 0.1662 0.2451 -0.0085 0.0260  0.0243  144 VAL   A CB  
3647 C CG1 . VAL   A 144 ? 0.1482 0.1794 0.2741 -0.0240 0.0122  0.0167  144 VAL   A CG1 
3648 C CG2 . VAL   A 144 ? 0.1318 0.1715 0.2580 -0.0048 0.0219  0.0332  144 VAL   A CG2 
3658 N N   . ASP   A 145 ? 0.1325 0.1358 0.2120 -0.0179 0.0066  0.0159  145 ASP   A N   
3659 C CA  . ASP   A 145 ? 0.1385 0.1474 0.2165 -0.0212 0.0073  0.0035  145 ASP   A CA  
3660 C C   . ASP   A 145 ? 0.1341 0.1362 0.2206 -0.0185 0.0048  -0.0055 145 ASP   A C   
3661 O O   . ASP   A 145 ? 0.1406 0.1533 0.2857 -0.0159 0.0120  -0.0358 145 ASP   A O   
3662 C CB  . ASP   A 145 ? 0.1445 0.1835 0.2249 -0.0287 0.0023  -0.0109 145 ASP   A CB  
3663 C CG  . ASP   A 145 ? 0.1605 0.2176 0.2496 -0.0450 -0.0062 -0.0105 145 ASP   A CG  
3664 O OD1 . ASP   A 145 ? 0.1607 0.2244 0.2753 -0.0560 -0.0016 -0.0075 145 ASP   A OD1 
3665 O OD2 . ASP   A 145 ? 0.1774 0.2405 0.2690 -0.0494 -0.0265 -0.0033 145 ASP   A OD2 
3670 N N   . THR   A 146 ? 0.1239 0.1259 0.1998 -0.0125 0.0069  0.0106  146 THR   A N   
3671 C CA  . THR   A 146 ? 0.1179 0.1254 0.1846 -0.0087 0.0055  0.0138  146 THR   A CA  
3672 C C   . THR   A 146 ? 0.1136 0.1217 0.1866 -0.0054 0.0056  0.0211  146 THR   A C   
3673 O O   . THR   A 146 ? 0.1249 0.1334 0.1971 0.0028  -0.0026 0.0153  146 THR   A O   
3674 C CB  . THR   A 146 ? 0.1201 0.1274 0.1845 -0.0074 0.0061  0.0187  146 THR   A CB  
3675 O OG1 . THR   A 146 ? 0.1239 0.1453 0.1782 -0.0059 0.0007  0.0139  146 THR   A OG1 
3676 C CG2 . THR   A 146 ? 0.1278 0.1309 0.1992 -0.0103 0.0074  0.0191  146 THR   A CG2 
3684 N N   . VAL   A 147 ? 0.1124 0.1263 0.1712 -0.0043 0.0107  0.0212  147 VAL   A N   
3685 C CA  . VAL   A 147 ? 0.1106 0.1308 0.1683 -0.0097 0.0168  0.0226  147 VAL   A CA  
3686 C C   . VAL   A 147 ? 0.1199 0.1277 0.1864 -0.0086 0.0143  0.0242  147 VAL   A C   
3687 O O   . VAL   A 147 ? 0.1188 0.1317 0.2049 -0.0137 0.0089  0.0349  147 VAL   A O   
3688 C CB  . VAL   A 147 ? 0.1209 0.1237 0.1794 -0.0098 0.0033  0.0292  147 VAL   A CB  
3689 C CG1 . VAL   A 147 ? 0.1482 0.1302 0.1879 -0.0027 0.0072  0.0350  147 VAL   A CG1 
3690 C CG2 . VAL   A 147 ? 0.1246 0.1272 0.1821 -0.0110 0.0076  0.0240  147 VAL   A CG2 
3700 N N   . ARG   A 148 ? 0.1166 0.1228 0.1927 -0.0077 0.0142  0.0420  148 ARG   A N   
3701 C CA  . ARG   A 148 ? 0.1275 0.1257 0.1967 -0.0053 0.0142  0.0417  148 ARG   A CA  
3702 C C   . ARG   A 148 ? 0.1362 0.1217 0.1868 -0.0085 0.0233  0.0494  148 ARG   A C   
3703 O O   . ARG   A 148 ? 0.1639 0.1412 0.1936 -0.0126 0.0232  0.0427  148 ARG   A O   
3704 C CB  . ARG   A 148 ? 0.1328 0.1235 0.2141 -0.0038 0.0217  0.0364  148 ARG   A CB  
3705 C CG  . ARG   A 148 ? 0.1471 0.1249 0.2435 -0.0101 0.0345  0.0280  148 ARG   A CG  
3706 C CD  . ARG   A 148 ? 0.1607 0.1262 0.2589 -0.0070 0.0378  0.0481  148 ARG   A CD  
3707 N NE  . ARG   A 148 ? 0.1552 0.1312 0.2552 0.0092  0.0427  0.0522  148 ARG   A NE  
3708 C CZ  . ARG   A 148 ? 0.1477 0.1289 0.2363 0.0084  0.0420  0.0375  148 ARG   A CZ  
3709 N NH1 . ARG   A 148 ? 0.1622 0.1297 0.2384 -0.0029 0.0403  0.0186  148 ARG   A NH1 
3710 N NH2 . ARG   A 148 ? 0.1426 0.1442 0.2441 0.0149  0.0436  0.0454  148 ARG   A NH2 
3724 N N   . THR   A 149 ? 0.1332 0.1306 0.1872 -0.0134 0.0001  0.0491  149 THR   A N   
3725 C CA  . THR   A 149 ? 0.1329 0.1423 0.1793 -0.0080 -0.0016 0.0421  149 THR   A CA  
3726 C C   . THR   A 149 ? 0.1228 0.1370 0.1645 -0.0121 0.0067  0.0479  149 THR   A C   
3727 O O   . THR   A 149 ? 0.1294 0.1412 0.1910 -0.0132 0.0081  0.0424  149 THR   A O   
3728 C CB  . THR   A 149 ? 0.1294 0.1503 0.1808 -0.0132 0.0034  0.0348  149 THR   A CB  
3729 O OG1 . THR   A 149 ? 0.1381 0.1377 0.1896 -0.0200 0.0005  0.0381  149 THR   A OG1 
3730 C CG2 . THR   A 149 ? 0.1260 0.1681 0.1957 -0.0072 0.0084  0.0375  149 THR   A CG2 
3738 N N   . ASN   A 150 ? 0.1300 0.1423 0.1762 -0.0041 -0.0021 0.0482  150 ASN   A N   
3739 C CA  . ASN   A 150 ? 0.1380 0.1509 0.1700 -0.0065 0.0104  0.0443  150 ASN   A CA  
3740 C C   . ASN   A 150 ? 0.1194 0.1472 0.1777 -0.0095 0.0028  0.0478  150 ASN   A C   
3741 O O   . ASN   A 150 ? 0.1420 0.1517 0.2041 -0.0102 -0.0189 0.0471  150 ASN   A O   
3742 C CB  . ASN   A 150 ? 0.1792 0.1709 0.1874 -0.0116 0.0180  0.0591  150 ASN   A CB  
3743 C CG  . ASN   A 150 ? 0.2367 0.2009 0.2343 -0.0124 0.0091  0.0636  150 ASN   A CG  
3744 O OD1 . ASN   A 150 ? 0.2596 0.2087 0.2523 -0.0214 0.0132  0.0767  150 ASN   A OD1 
3745 N ND2 . ASN   A 150 ? 0.2678 0.2252 0.2691 -0.0075 -0.0060 0.0732  150 ASN   A ND2 
3752 N N   . VAL   A 151 ? 0.1193 0.1321 0.1759 -0.0088 0.0066  0.0416  151 VAL   A N   
3753 C CA  . VAL   A 151 ? 0.1234 0.1323 0.1675 -0.0116 0.0084  0.0376  151 VAL   A CA  
3754 C C   . VAL   A 151 ? 0.1171 0.1306 0.1686 -0.0170 0.0094  0.0442  151 VAL   A C   
3755 O O   . VAL   A 151 ? 0.1222 0.1352 0.2017 -0.0172 0.0130  0.0363  151 VAL   A O   
3756 C CB  . VAL   A 151 ? 0.1410 0.1471 0.1722 -0.0017 0.0065  0.0365  151 VAL   A CB  
3757 C CG1 . VAL   A 151 ? 0.1406 0.1618 0.1965 -0.0063 0.0146  0.0322  151 VAL   A CG1 
3758 C CG2 . VAL   A 151 ? 0.1535 0.1545 0.1715 -0.0041 0.0177  0.0365  151 VAL   A CG2 
3768 N N   . TYR   A 152 ? 0.1128 0.1329 0.1695 -0.0122 0.0063  0.0392  152 TYR   A N   
3769 C CA  . TYR   A 152 ? 0.1149 0.1368 0.1573 -0.0129 0.0054  0.0327  152 TYR   A CA  
3770 C C   . TYR   A 152 ? 0.1124 0.1262 0.1491 -0.0140 0.0177  0.0326  152 TYR   A C   
3771 O O   . TYR   A 152 ? 0.1298 0.1322 0.1462 -0.0202 0.0136  0.0296  152 TYR   A O   
3772 C CB  . TYR   A 152 ? 0.1307 0.1460 0.1646 -0.0082 0.0160  0.0358  152 TYR   A CB  
3773 C CG  . TYR   A 152 ? 0.1476 0.1627 0.1537 -0.0114 0.0180  0.0416  152 TYR   A CG  
3774 C CD1 . TYR   A 152 ? 0.1668 0.1832 0.1741 -0.0012 0.0200  0.0491  152 TYR   A CD1 
3775 C CD2 . TYR   A 152 ? 0.1544 0.1769 0.1505 -0.0198 0.0187  0.0383  152 TYR   A CD2 
3776 C CE1 . TYR   A 152 ? 0.1926 0.1976 0.1928 0.0064  0.0132  0.0667  152 TYR   A CE1 
3777 C CE2 . TYR   A 152 ? 0.1820 0.1950 0.1680 -0.0237 0.0203  0.0502  152 TYR   A CE2 
3778 C CZ  . TYR   A 152 ? 0.2090 0.1989 0.1841 -0.0090 0.0149  0.0757  152 TYR   A CZ  
3779 O OH  . TYR   A 152 ? 0.2445 0.2215 0.2249 -0.0040 0.0229  0.0932  152 TYR   A OH  
3789 N N   . LEU   A 153 ? 0.1115 0.1295 0.1657 -0.0123 0.0140  0.0383  153 LEU   A N   
3790 C CA  . LEU   A 153 ? 0.1091 0.1303 0.1784 -0.0070 0.0138  0.0384  153 LEU   A CA  
3791 C C   . LEU   A 153 ? 0.1065 0.1305 0.1762 -0.0063 0.0175  0.0388  153 LEU   A C   
3792 O O   . LEU   A 153 ? 0.1215 0.1387 0.2102 -0.0065 0.0348  0.0417  153 LEU   A O   
3793 C CB  . LEU   A 153 ? 0.1100 0.1308 0.1863 -0.0080 0.0021  0.0314  153 LEU   A CB  
3794 C CG  . LEU   A 153 ? 0.1202 0.1363 0.1709 -0.0112 0.0039  0.0303  153 LEU   A CG  
3795 C CD1 . LEU   A 153 ? 0.1340 0.1507 0.1698 -0.0205 -0.0030 0.0322  153 LEU   A CD1 
3796 C CD2 . LEU   A 153 ? 0.1283 0.1584 0.1858 -0.0182 0.0287  0.0171  153 LEU   A CD2 
3808 N N   A ALA   A 154 ? 0.1127 0.1306 0.1618 -0.0008 0.0176  0.0456  154 ALA   A N   
3809 N N   B ALA   A 154 ? 0.1121 0.1245 0.1810 -0.0076 0.0174  0.0352  154 ALA   A N   
3810 C CA  A ALA   A 154 ? 0.1202 0.1370 0.1529 0.0017  0.0118  0.0502  154 ALA   A CA  
3811 C CA  B ALA   A 154 ? 0.1217 0.1300 0.1770 -0.0058 0.0121  0.0301  154 ALA   A CA  
3812 C C   A ALA   A 154 ? 0.1229 0.1393 0.1466 -0.0011 0.0162  0.0470  154 ALA   A C   
3813 C C   B ALA   A 154 ? 0.1215 0.1264 0.1791 0.0003  0.0166  0.0228  154 ALA   A C   
3814 O O   A ALA   A 154 ? 0.1260 0.1406 0.1427 -0.0048 0.0197  0.0566  154 ALA   A O   
3815 O O   B ALA   A 154 ? 0.1299 0.1335 0.1942 0.0000  0.0167  0.0242  154 ALA   A O   
3816 C CB  A ALA   A 154 ? 0.1234 0.1438 0.1656 0.0091  0.0046  0.0388  154 ALA   A CB  
3817 C CB  B ALA   A 154 ? 0.1282 0.1388 0.1706 -0.0016 0.0042  0.0253  154 ALA   A CB  
3828 N N   A VAL   A 155 ? 0.1295 0.1493 0.1536 -0.0001 0.0158  0.0454  155 VAL   A N   
3829 N N   B VAL   A 155 ? 0.1204 0.1320 0.1853 0.0027  0.0127  0.0323  155 VAL   A N   
3830 C CA  A VAL   A 155 ? 0.1402 0.1522 0.1577 -0.0024 0.0100  0.0396  155 VAL   A CA  
3831 C CA  B VAL   A 155 ? 0.1180 0.1308 0.1982 -0.0060 0.0037  0.0306  155 VAL   A CA  
3832 C C   A VAL   A 155 ? 0.1493 0.1549 0.1547 0.0054  0.0010  0.0360  155 VAL   A C   
3833 C C   B VAL   A 155 ? 0.1150 0.1259 0.1927 -0.0026 0.0020  0.0307  155 VAL   A C   
3834 O O   A VAL   A 155 ? 0.1502 0.1589 0.1553 0.0090  0.0030  0.0249  155 VAL   A O   
3835 O O   B VAL   A 155 ? 0.1131 0.1300 0.1992 -0.0027 0.0130  0.0324  155 VAL   A O   
3836 C CB  A VAL   A 155 ? 0.1492 0.1540 0.1836 -0.0102 -0.0040 0.0308  155 VAL   A CB  
3837 C CB  B VAL   A 155 ? 0.1257 0.1253 0.2185 -0.0121 -0.0154 0.0245  155 VAL   A CB  
3838 C CG1 A VAL   A 155 ? 0.1545 0.1533 0.1931 -0.0180 -0.0097 0.0250  155 VAL   A CG1 
3839 C CG1 B VAL   A 155 ? 0.1270 0.1195 0.2193 -0.0041 -0.0261 0.0202  155 VAL   A CG1 
3840 C CG2 A VAL   A 155 ? 0.1582 0.1594 0.1950 -0.0039 -0.0166 0.0285  155 VAL   A CG2 
3841 C CG2 B VAL   A 155 ? 0.1420 0.1306 0.2404 0.0024  -0.0236 0.0242  155 VAL   A CG2 
3860 N N   A PHE   A 156 ? 0.1539 0.1536 0.1514 0.0121  -0.0046 0.0447  156 PHE   A N   
3861 N N   B PHE   A 156 ? 0.1205 0.1237 0.1988 -0.0043 0.0050  0.0274  156 PHE   A N   
3862 C CA  A PHE   A 156 ? 0.1758 0.1651 0.1774 0.0213  -0.0142 0.0395  156 PHE   A CA  
3863 C CA  B PHE   A 156 ? 0.1289 0.1290 0.2052 -0.0065 -0.0010 0.0337  156 PHE   A CA  
3864 C C   A PHE   A 156 ? 0.1641 0.1624 0.1777 0.0254  -0.0025 0.0462  156 PHE   A C   
3865 C C   B PHE   A 156 ? 0.1346 0.1466 0.2239 -0.0044 0.0043  0.0345  156 PHE   A C   
3866 O O   A PHE   A 156 ? 0.1658 0.1705 0.1863 0.0298  0.0099  0.0335  156 PHE   A O   
3867 O O   B PHE   A 156 ? 0.1530 0.1741 0.2470 0.0013  0.0110  0.0141  156 PHE   A O   
3868 C CB  A PHE   A 156 ? 0.2104 0.1849 0.2014 0.0254  -0.0424 0.0370  156 PHE   A CB  
3869 C CB  B PHE   A 156 ? 0.1392 0.1181 0.1841 -0.0114 -0.0228 0.0475  156 PHE   A CB  
3870 C CG  A PHE   A 156 ? 0.2439 0.2038 0.2402 0.0355  -0.0634 0.0240  156 PHE   A CG  
3871 C CG  B PHE   A 156 ? 0.1689 0.1303 0.1889 -0.0037 -0.0354 0.0486  156 PHE   A CG  
3872 C CD1 A PHE   A 156 ? 0.2632 0.2149 0.2683 0.0400  -0.0655 0.0153  156 PHE   A CD1 
3873 C CD1 B PHE   A 156 ? 0.1754 0.1340 0.1909 0.0083  -0.0202 0.0513  156 PHE   A CD1 
3874 C CD2 A PHE   A 156 ? 0.2583 0.2119 0.2550 0.0371  -0.0807 0.0178  156 PHE   A CD2 
3875 C CD2 B PHE   A 156 ? 0.2064 0.1421 0.2230 0.0002  -0.0559 0.0409  156 PHE   A CD2 
3876 C CE1 A PHE   A 156 ? 0.2756 0.2226 0.2866 0.0426  -0.0654 0.0058  156 PHE   A CE1 
3877 C CE1 B PHE   A 156 ? 0.1914 0.1467 0.2191 0.0090  -0.0169 0.0405  156 PHE   A CE1 
3878 C CE2 A PHE   A 156 ? 0.2717 0.2200 0.2722 0.0399  -0.0875 0.0078  156 PHE   A CE2 
3879 C CE2 B PHE   A 156 ? 0.2191 0.1560 0.2422 0.0065  -0.0679 0.0322  156 PHE   A CE2 
3880 C CZ  A PHE   A 156 ? 0.2775 0.2249 0.2834 0.0427  -0.0746 0.0007  156 PHE   A CZ  
3881 C CZ  B PHE   A 156 ? 0.2133 0.1569 0.2448 0.0061  -0.0397 0.0335  156 PHE   A CZ  
3900 N N   A ASP   A 157 ? 0.1582 0.1664 0.1799 0.0149  -0.0059 0.0591  157 ASP   A N   
3901 N N   B ASP   A 157 ? 0.1384 0.1526 0.2306 -0.0117 -0.0099 0.0386  157 ASP   A N   
3902 C CA  A ASP   A 157 ? 0.1600 0.1787 0.2048 0.0066  -0.0123 0.0590  157 ASP   A CA  
3903 C CA  B ASP   A 157 ? 0.1464 0.1625 0.2458 -0.0079 -0.0290 0.0285  157 ASP   A CA  
3904 C C   A ASP   A 157 ? 0.1539 0.1832 0.2125 0.0095  0.0011  0.0630  157 ASP   A C   
3905 C C   B ASP   A 157 ? 0.1349 0.1571 0.2431 -0.0049 -0.0209 0.0247  157 ASP   A C   
3906 O O   A ASP   A 157 ? 0.1562 0.1775 0.2132 0.0069  -0.0003 0.0693  157 ASP   A O   
3907 O O   B ASP   A 157 ? 0.1323 0.1494 0.2271 0.0003  -0.0169 0.0290  157 ASP   A O   
3908 C CB  A ASP   A 157 ? 0.1695 0.1827 0.2234 0.0027  -0.0366 0.0594  157 ASP   A CB  
3909 C CB  B ASP   A 157 ? 0.1681 0.1708 0.2634 -0.0077 -0.0468 0.0338  157 ASP   A CB  
3910 C CG  A ASP   A 157 ? 0.1859 0.1899 0.2584 0.0044  -0.0577 0.0500  157 ASP   A CG  
3911 C CG  B ASP   A 157 ? 0.1945 0.1765 0.2979 -0.0111 -0.0680 0.0314  157 ASP   A CG  
3912 O OD1 A ASP   A 157 ? 0.2100 0.2023 0.2989 0.0008  -0.0699 0.0358  157 ASP   A OD1 
3913 O OD1 B ASP   A 157 ? 0.2214 0.1776 0.3250 -0.0041 -0.1005 0.0274  157 ASP   A OD1 
3914 O OD2 A ASP   A 157 ? 0.1818 0.1837 0.2685 0.0011  -0.0577 0.0397  157 ASP   A OD2 
3915 O OD2 B ASP   A 157 ? 0.1987 0.1904 0.3139 -0.0135 -0.0628 0.0215  157 ASP   A OD2 
3924 N N   A LYS   A 158 ? 0.1519 0.1963 0.2284 0.0163  0.0074  0.0603  158 LYS   A N   
3925 N N   B LYS   A 158 ? 0.1316 0.1583 0.2660 -0.0099 -0.0096 0.0163  158 LYS   A N   
3926 C CA  A LYS   A 158 ? 0.1553 0.2095 0.2584 0.0266  0.0194  0.0556  158 LYS   A CA  
3927 C CA  B LYS   A 158 ? 0.1349 0.1751 0.2858 -0.0054 -0.0014 0.0272  158 LYS   A CA  
3928 C C   A LYS   A 158 ? 0.1560 0.2177 0.2581 0.0304  0.0143  0.0439  158 LYS   A C   
3929 C C   B LYS   A 158 ? 0.1328 0.1682 0.2765 -0.0073 -0.0115 0.0275  158 LYS   A C   
3930 O O   A LYS   A 158 ? 0.1530 0.2167 0.2666 0.0280  0.0275  0.0338  158 LYS   A O   
3931 O O   B LYS   A 158 ? 0.1323 0.1606 0.2841 -0.0160 -0.0072 0.0325  158 LYS   A O   
3932 C CB  A LYS   A 158 ? 0.1667 0.2190 0.2852 0.0285  0.0354  0.0618  158 LYS   A CB  
3933 C CB  B LYS   A 158 ? 0.1536 0.2022 0.3256 -0.0048 0.0180  0.0338  158 LYS   A CB  
3934 C CG  A LYS   A 158 ? 0.1801 0.2331 0.3189 0.0262  0.0442  0.0684  158 LYS   A CG  
3935 C CG  B LYS   A 158 ? 0.1784 0.2304 0.3671 -0.0014 0.0390  0.0391  158 LYS   A CG  
3936 C CD  A LYS   A 158 ? 0.1967 0.2467 0.3548 0.0222  0.0543  0.0793  158 LYS   A CD  
3937 C CD  B LYS   A 158 ? 0.2032 0.2582 0.4114 -0.0030 0.0503  0.0512  158 LYS   A CD  
3938 C CE  A LYS   A 158 ? 0.2033 0.2525 0.3809 0.0183  0.0635  0.0911  158 LYS   A CE  
3939 C CE  B LYS   A 158 ? 0.2179 0.2721 0.4332 -0.0014 0.0659  0.0754  158 LYS   A CE  
3940 N NZ  A LYS   A 158 ? 0.2039 0.2557 0.3960 0.0151  0.0780  0.0974  158 LYS   A NZ  
3941 N NZ  B LYS   A 158 ? 0.2192 0.2790 0.4421 -0.0044 0.0813  0.0946  158 LYS   A NZ  
3968 N N   A ASN   A 159 ? 0.1616 0.2331 0.2695 0.0345  -0.0059 0.0418  159 ASN   A N   
3969 N N   B ASN   A 159 ? 0.1460 0.1762 0.2811 -0.0036 -0.0328 0.0173  159 ASN   A N   
3970 C CA  A ASN   A 159 ? 0.1721 0.2445 0.2765 0.0316  -0.0189 0.0441  159 ASN   A CA  
3971 C CA  B ASN   A 159 ? 0.1616 0.1886 0.2939 0.0104  -0.0483 0.0317  159 ASN   A CA  
3972 C C   A ASN   A 159 ? 0.1709 0.2347 0.2553 0.0244  -0.0076 0.0409  159 ASN   A C   
3973 C C   B ASN   A 159 ? 0.1432 0.1779 0.2785 -0.0024 -0.0401 0.0282  159 ASN   A C   
3974 O O   A ASN   A 159 ? 0.1771 0.2425 0.2519 0.0206  -0.0084 0.0316  159 ASN   A O   
3975 O O   B ASN   A 159 ? 0.1432 0.1869 0.2856 -0.0084 -0.0436 0.0173  159 ASN   A O   
3976 C CB  A ASN   A 159 ? 0.1868 0.2605 0.3156 0.0357  -0.0327 0.0517  159 ASN   A CB  
3977 C CB  B ASN   A 159 ? 0.2056 0.2196 0.3245 0.0269  -0.0581 0.0427  159 ASN   A CB  
3978 C CG  A ASN   A 159 ? 0.2029 0.2731 0.3524 0.0270  -0.0374 0.0557  159 ASN   A CG  
3979 C CG  B ASN   A 159 ? 0.2512 0.2522 0.3692 0.0174  -0.0524 0.0417  159 ASN   A CG  
3980 O OD1 A ASN   A 159 ? 0.2061 0.2760 0.3697 0.0188  -0.0342 0.0569  159 ASN   A OD1 
3981 O OD1 B ASN   A 159 ? 0.2662 0.2647 0.3916 0.0132  -0.0483 0.0364  159 ASN   A OD1 
3982 N ND2 A ASN   A 159 ? 0.2129 0.2809 0.3712 0.0186  -0.0340 0.0497  159 ASN   A ND2 
3983 N ND2 B ASN   A 159 ? 0.2641 0.2639 0.3789 0.0143  -0.0565 0.0443  159 ASN   A ND2 
3996 N N   A LEU   A 160 ? 0.1630 0.2168 0.2425 0.0224  -0.0100 0.0514  160 LEU   A N   
3997 N N   B LEU   A 160 ? 0.1332 0.1670 0.2614 -0.0066 -0.0392 0.0376  160 LEU   A N   
3998 C CA  A LEU   A 160 ? 0.1580 0.2054 0.2375 0.0166  -0.0057 0.0537  160 LEU   A CA  
3999 C CA  B LEU   A 160 ? 0.1367 0.1603 0.2523 -0.0081 -0.0269 0.0386  160 LEU   A CA  
4000 C C   A LEU   A 160 ? 0.1417 0.1971 0.2301 0.0138  0.0056  0.0545  160 LEU   A C   
4001 C C   B LEU   A 160 ? 0.1278 0.1557 0.2483 -0.0093 -0.0174 0.0303  160 LEU   A C   
4002 O O   A LEU   A 160 ? 0.1374 0.1962 0.2350 0.0133  0.0096  0.0409  160 LEU   A O   
4003 O O   B LEU   A 160 ? 0.1403 0.1521 0.2532 -0.0156 -0.0148 0.0163  160 LEU   A O   
4004 C CB  A LEU   A 160 ? 0.1673 0.2055 0.2359 0.0065  0.0013  0.0476  160 LEU   A CB  
4005 C CB  B LEU   A 160 ? 0.1482 0.1560 0.2553 -0.0119 -0.0193 0.0500  160 LEU   A CB  
4006 C CG  A LEU   A 160 ? 0.1726 0.2075 0.2441 -0.0004 0.0086  0.0398  160 LEU   A CG  
4007 C CG  B LEU   A 160 ? 0.1519 0.1585 0.2548 -0.0168 -0.0189 0.0541  160 LEU   A CG  
4008 C CD1 A LEU   A 160 ? 0.1750 0.2040 0.2540 -0.0008 0.0151  0.0329  160 LEU   A CD1 
4009 C CD1 B LEU   A 160 ? 0.1538 0.1667 0.2731 -0.0217 -0.0098 0.0569  160 LEU   A CD1 
4010 C CD2 A LEU   A 160 ? 0.1736 0.2087 0.2503 -0.0031 0.0133  0.0312  160 LEU   A CD2 
4011 C CD2 B LEU   A 160 ? 0.1586 0.1573 0.2567 -0.0160 -0.0251 0.0599  160 LEU   A CD2 
4034 N N   A TYR   A 161 ? 0.1395 0.1980 0.2396 0.0079  0.0075  0.0592  161 TYR   A N   
4035 N N   B TYR   A 161 ? 0.1195 0.1512 0.2402 -0.0080 -0.0057 0.0397  161 TYR   A N   
4036 C CA  A TYR   A 161 ? 0.1368 0.1997 0.2412 0.0020  0.0144  0.0678  161 TYR   A CA  
4037 C CA  B TYR   A 161 ? 0.1193 0.1523 0.2332 -0.0092 -0.0010 0.0497  161 TYR   A CA  
4038 C C   A TYR   A 161 ? 0.1349 0.2146 0.2474 0.0040  0.0213  0.0644  161 TYR   A C   
4039 C C   B TYR   A 161 ? 0.1183 0.1620 0.2602 -0.0156 0.0030  0.0389  161 TYR   A C   
4040 O O   A TYR   A 161 ? 0.1317 0.2140 0.2458 0.0016  0.0223  0.0601  161 TYR   A O   
4041 O O   B TYR   A 161 ? 0.1235 0.1561 0.2453 -0.0156 0.0028  0.0354  161 TYR   A O   
4042 C CB  A TYR   A 161 ? 0.1430 0.1883 0.2617 -0.0036 0.0089  0.0667  161 TYR   A CB  
4043 C CB  B TYR   A 161 ? 0.1223 0.1559 0.2434 -0.0041 -0.0018 0.0514  161 TYR   A CB  
4044 C CG  A TYR   A 161 ? 0.1424 0.1817 0.2673 -0.0122 -0.0076 0.0732  161 TYR   A CG  
4045 C CG  B TYR   A 161 ? 0.1324 0.1644 0.2762 -0.0016 -0.0096 0.0598  161 TYR   A CG  
4046 C CD1 A TYR   A 161 ? 0.1446 0.1796 0.2814 -0.0159 -0.0166 0.0665  161 TYR   A CD1 
4047 C CD1 B TYR   A 161 ? 0.1341 0.1727 0.3018 0.0029  -0.0146 0.0535  161 TYR   A CD1 
4048 C CD2 A TYR   A 161 ? 0.1454 0.1897 0.2607 -0.0143 -0.0240 0.0826  161 TYR   A CD2 
4049 C CD2 B TYR   A 161 ? 0.1489 0.1833 0.2866 -0.0003 -0.0178 0.0734  161 TYR   A CD2 
4050 C CE1 A TYR   A 161 ? 0.1533 0.1792 0.2850 -0.0190 -0.0286 0.0729  161 TYR   A CE1 
4051 C CE1 B TYR   A 161 ? 0.1475 0.1762 0.3143 0.0072  -0.0261 0.0660  161 TYR   A CE1 
4052 C CE2 A TYR   A 161 ? 0.1542 0.1879 0.2664 -0.0165 -0.0287 0.0877  161 TYR   A CE2 
4053 C CE2 B TYR   A 161 ? 0.1590 0.1846 0.3024 0.0003  -0.0263 0.0855  161 TYR   A CE2 
4054 C CZ  A TYR   A 161 ? 0.1648 0.1811 0.2806 -0.0146 -0.0365 0.0892  161 TYR   A CZ  
4055 C CZ  B TYR   A 161 ? 0.1696 0.1803 0.3208 -0.0018 -0.0246 0.0818  161 TYR   A CZ  
4056 O OH  A TYR   A 161 ? 0.1816 0.1757 0.2865 0.0015  -0.0465 0.1026  161 TYR   A OH  
4057 O OH  B TYR   A 161 ? 0.1928 0.1836 0.3433 -0.0030 -0.0196 0.0873  161 TYR   A OH  
4076 N N   A ASP   A 162 ? 0.1395 0.2351 0.2680 0.0104  0.0175  0.0640  162 ASP   A N   
4077 N N   B ASP   A 162 ? 0.1138 0.1769 0.2984 -0.0204 0.0084  0.0315  162 ASP   A N   
4078 C CA  A ASP   A 162 ? 0.1491 0.2636 0.2744 0.0128  0.0158  0.0631  162 ASP   A CA  
4079 C CA  B ASP   A 162 ? 0.1129 0.2012 0.3122 -0.0285 0.0050  0.0366  162 ASP   A CA  
4080 C C   A ASP   A 162 ? 0.1652 0.2780 0.2885 0.0175  0.0162  0.0572  162 ASP   A C   
4081 C C   B ASP   A 162 ? 0.1160 0.2046 0.3228 -0.0287 -0.0101 0.0389  162 ASP   A C   
4082 O O   A ASP   A 162 ? 0.1639 0.2759 0.3032 0.0221  0.0298  0.0513  162 ASP   A O   
4083 O O   B ASP   A 162 ? 0.1214 0.1927 0.3559 -0.0371 0.0042  0.0324  162 ASP   A O   
4084 C CB  A ASP   A 162 ? 0.1498 0.2783 0.2671 0.0139  0.0184  0.0661  162 ASP   A CB  
4085 C CB  B ASP   A 162 ? 0.1294 0.2356 0.3313 -0.0146 0.0068  0.0362  162 ASP   A CB  
4086 C CG  A ASP   A 162 ? 0.1532 0.2930 0.2557 0.0130  0.0325  0.0784  162 ASP   A CG  
4087 C CG  B ASP   A 162 ? 0.1513 0.2653 0.3402 -0.0013 0.0164  0.0434  162 ASP   A CG  
4088 O OD1 A ASP   A 162 ? 0.1583 0.2981 0.2591 0.0073  0.0414  0.0805  162 ASP   A OD1 
4089 O OD1 B ASP   A 162 ? 0.1624 0.2730 0.3472 0.0044  0.0211  0.0499  162 ASP   A OD1 
4090 O OD2 A ASP   A 162 ? 0.1556 0.2984 0.2481 0.0208  0.0479  0.0871  162 ASP   A OD2 
4091 O OD2 B ASP   A 162 ? 0.1674 0.2784 0.3483 0.0104  0.0201  0.0440  162 ASP   A OD2 
4100 N N   A LYS   A 163 ? 0.1884 0.2933 0.2905 0.0182  -0.0020 0.0566  163 LYS   A N   
4101 N N   B LYS   A 163 ? 0.1213 0.2198 0.3047 -0.0242 -0.0465 0.0510  163 LYS   A N   
4102 C CA  A LYS   A 163 ? 0.2177 0.3071 0.2915 0.0103  -0.0137 0.0508  163 LYS   A CA  
4103 C CA  B LYS   A 163 ? 0.1497 0.2465 0.3066 -0.0338 -0.0513 0.0505  163 LYS   A CA  
4104 C C   A LYS   A 163 ? 0.2023 0.2867 0.2642 0.0025  -0.0145 0.0450  163 LYS   A C   
4105 C C   B LYS   A 163 ? 0.1363 0.2176 0.2803 -0.0400 -0.0314 0.0346  163 LYS   A C   
4106 O O   A LYS   A 163 ? 0.2060 0.2933 0.2779 0.0011  -0.0213 0.0347  163 LYS   A O   
4107 O O   B LYS   A 163 ? 0.1434 0.2109 0.2969 -0.0403 -0.0347 0.0201  163 LYS   A O   
4108 C CB  A LYS   A 163 ? 0.2679 0.3415 0.3417 0.0087  -0.0139 0.0450  163 LYS   A CB  
4109 C CB  B LYS   A 163 ? 0.2066 0.3008 0.3620 -0.0367 -0.0585 0.0612  163 LYS   A CB  
4110 C CG  A LYS   A 163 ? 0.3152 0.3725 0.4019 0.0051  -0.0082 0.0376  163 LYS   A CG  
4111 C CG  B LYS   A 163 ? 0.2766 0.3517 0.4379 -0.0407 -0.0378 0.0630  163 LYS   A CG  
4112 C CD  A LYS   A 163 ? 0.3578 0.3974 0.4610 0.0032  -0.0037 0.0323  163 LYS   A CD  
4113 C CD  B LYS   A 163 ? 0.3425 0.3944 0.5037 -0.0432 -0.0250 0.0633  163 LYS   A CD  
4114 C CE  A LYS   A 163 ? 0.3956 0.4185 0.5106 0.0021  -0.0005 0.0302  163 LYS   A CE  
4115 C CE  B LYS   A 163 ? 0.3999 0.4299 0.5557 -0.0452 -0.0170 0.0647  163 LYS   A CE  
4116 N NZ  A LYS   A 163 ? 0.4145 0.4267 0.5390 0.0014  0.0010  0.0298  163 LYS   A NZ  
4117 N NZ  B LYS   A 163 ? 0.4307 0.4465 0.5859 -0.0461 -0.0140 0.0662  163 LYS   A NZ  
4144 N N   A LEU   A 164 ? 0.1813 0.2592 0.2249 -0.0039 -0.0138 0.0500  164 LEU   A N   
4145 N N   B LEU   A 164 ? 0.1237 0.2003 0.2477 -0.0289 -0.0254 0.0306  164 LEU   A N   
4146 C CA  A LEU   A 164 ? 0.1708 0.2354 0.2064 -0.0115 0.0039  0.0513  164 LEU   A CA  
4147 C CA  B LEU   A 164 ? 0.1302 0.1858 0.2326 -0.0156 0.0031  0.0362  164 LEU   A CA  
4148 C C   A LEU   A 164 ? 0.1694 0.2324 0.2283 -0.0148 0.0138  0.0611  164 LEU   A C   
4149 C C   B LEU   A 164 ? 0.1367 0.1807 0.2414 -0.0155 0.0119  0.0375  164 LEU   A C   
4150 O O   A LEU   A 164 ? 0.1731 0.2345 0.2433 -0.0160 0.0278  0.0540  164 LEU   A O   
4151 O O   B LEU   A 164 ? 0.1575 0.1784 0.2443 -0.0114 0.0153  0.0394  164 LEU   A O   
4152 C CB  A LEU   A 164 ? 0.1646 0.2216 0.1762 -0.0157 0.0169  0.0403  164 LEU   A CB  
4153 C CB  B LEU   A 164 ? 0.1333 0.1838 0.2162 -0.0177 0.0169  0.0338  164 LEU   A CB  
4154 C CG  A LEU   A 164 ? 0.1674 0.2159 0.1673 -0.0194 0.0146  0.0252  164 LEU   A CG  
4155 C CG  B LEU   A 164 ? 0.1412 0.1908 0.2170 -0.0180 0.0196  0.0238  164 LEU   A CG  
4156 C CD1 A LEU   A 164 ? 0.1629 0.2120 0.1614 -0.0137 0.0137  0.0175  164 LEU   A CD1 
4157 C CD1 B LEU   A 164 ? 0.1332 0.1912 0.2107 -0.0270 0.0065  0.0200  164 LEU   A CD1 
4158 C CD2 A LEU   A 164 ? 0.1750 0.2144 0.1591 -0.0256 0.0166  0.0182  164 LEU   A CD2 
4159 C CD2 B LEU   A 164 ? 0.1675 0.2038 0.2146 -0.0105 0.0223  0.0188  164 LEU   A CD2 
4182 N N   A VAL   A 165 ? 0.1673 0.2358 0.2404 -0.0216 0.0239  0.0693  165 VAL   A N   
4183 N N   B VAL   A 165 ? 0.1388 0.1836 0.2614 -0.0136 0.0245  0.0465  165 VAL   A N   
4184 C CA  A VAL   A 165 ? 0.1724 0.2435 0.2474 -0.0350 0.0368  0.0721  165 VAL   A CA  
4185 C CA  B VAL   A 165 ? 0.1513 0.1988 0.2811 -0.0153 0.0379  0.0546  165 VAL   A CA  
4186 C C   A VAL   A 165 ? 0.1780 0.2522 0.2625 -0.0364 0.0241  0.0742  165 VAL   A C   
4187 C C   B VAL   A 165 ? 0.1416 0.1890 0.3139 -0.0191 0.0232  0.0599  165 VAL   A C   
4188 O O   A VAL   A 165 ? 0.1775 0.2553 0.2473 -0.0336 0.0294  0.0862  165 VAL   A O   
4189 O O   B VAL   A 165 ? 0.1604 0.1852 0.3217 -0.0172 0.0123  0.0722  165 VAL   A O   
4190 C CB  A VAL   A 165 ? 0.1749 0.2455 0.2482 -0.0457 0.0524  0.0709  165 VAL   A CB  
4191 C CB  B VAL   A 165 ? 0.1788 0.2297 0.2857 -0.0169 0.0452  0.0506  165 VAL   A CB  
4192 C CG1 A VAL   A 165 ? 0.1723 0.2532 0.2571 -0.0502 0.0491  0.0599  165 VAL   A CG1 
4193 C CG1 B VAL   A 165 ? 0.1877 0.2440 0.2998 -0.0229 0.0391  0.0492  165 VAL   A CG1 
4194 C CG2 A VAL   A 165 ? 0.1827 0.2389 0.2493 -0.0464 0.0508  0.0814  165 VAL   A CG2 
4195 C CG2 B VAL   A 165 ? 0.1905 0.2373 0.2765 -0.0108 0.0546  0.0509  165 VAL   A CG2 
4214 N N   A SER   A 166 ? 0.1890 0.2609 0.2963 -0.0354 0.0153  0.0695  166 SER   A N   
4215 N N   B SER   A 166 ? 0.1297 0.1996 0.3470 -0.0198 0.0188  0.0524  166 SER   A N   
4216 C CA  A SER   A 166 ? 0.2048 0.2752 0.3242 -0.0389 0.0053  0.0624  166 SER   A CA  
4217 C CA  B SER   A 166 ? 0.1328 0.2270 0.3658 -0.0214 0.0001  0.0564  166 SER   A CA  
4218 C C   A SER   A 166 ? 0.2066 0.2799 0.3165 -0.0507 -0.0076 0.0602  166 SER   A C   
4219 C C   B SER   A 166 ? 0.1468 0.2485 0.3413 -0.0335 -0.0118 0.0513  166 SER   A C   
4220 O O   A SER   A 166 ? 0.2078 0.2780 0.3274 -0.0556 -0.0110 0.0547  166 SER   A O   
4221 O O   B SER   A 166 ? 0.1611 0.2516 0.3510 -0.0397 -0.0109 0.0528  166 SER   A O   
4222 C CB  A SER   A 166 ? 0.2258 0.2904 0.3665 -0.0201 0.0020  0.0481  166 SER   A CB  
4223 C CB  B SER   A 166 ? 0.1567 0.2447 0.4213 -0.0045 -0.0074 0.0613  166 SER   A CB  
4224 O OG  A SER   A 166 ? 0.2454 0.3031 0.4067 -0.0071 0.0014  0.0468  166 SER   A OG  
4225 O OG  B SER   A 166 ? 0.1959 0.2707 0.4746 0.0005  -0.0044 0.0614  166 SER   A OG  
4236 N N   A SER   A 167 ? 0.2196 0.2910 0.3085 -0.0475 -0.0182 0.0528  167 SER   A N   
4237 N N   B SER   A 167 ? 0.1670 0.2625 0.3140 -0.0283 -0.0095 0.0485  167 SER   A N   
4238 C CA  A SER   A 167 ? 0.2387 0.2969 0.2991 -0.0402 -0.0297 0.0514  167 SER   A CA  
4239 C CA  B SER   A 167 ? 0.1934 0.2828 0.2925 -0.0257 -0.0106 0.0489  167 SER   A CA  
4240 C C   A SER   A 167 ? 0.2506 0.3017 0.2939 -0.0358 -0.0243 0.0515  167 SER   A C   
4241 C C   B SER   A 167 ? 0.2094 0.2971 0.2756 -0.0175 -0.0136 0.0435  167 SER   A C   
4242 O O   A SER   A 167 ? 0.2523 0.2991 0.2867 -0.0395 -0.0245 0.0570  167 SER   A O   
4243 O O   B SER   A 167 ? 0.2135 0.2967 0.2615 -0.0181 -0.0173 0.0459  167 SER   A O   
4244 C CB  A SER   A 167 ? 0.2438 0.2958 0.3016 -0.0362 -0.0372 0.0519  167 SER   A CB  
4245 C CB  B SER   A 167 ? 0.2004 0.2903 0.2995 -0.0254 -0.0048 0.0423  167 SER   A CB  
4246 O OG  A SER   A 167 ? 0.2487 0.2948 0.3052 -0.0365 -0.0362 0.0529  167 SER   A OG  
4247 O OG  B SER   A 167 ? 0.2068 0.2947 0.3006 -0.0216 -0.0001 0.0351  167 SER   A OG  
4258 N N   A PHE   A 168 ? 0.2574 0.3090 0.2961 -0.0281 -0.0164 0.0537  168 PHE   A N   
4259 N N   B PHE   A 168 ? 0.2289 0.3148 0.3008 -0.0060 -0.0189 0.0313  168 PHE   A N   
4260 C CA  A PHE   A 168 ? 0.2665 0.3192 0.3162 -0.0216 -0.0090 0.0406  168 PHE   A CA  
4261 C CA  B PHE   A 168 ? 0.2615 0.3344 0.3396 -0.0026 -0.0209 0.0240  168 PHE   A CA  
4262 C C   A PHE   A 168 ? 0.2915 0.3421 0.3680 -0.0198 0.0036  0.0271  168 PHE   A C   
4263 C C   B PHE   A 168 ? 0.3342 0.3674 0.4307 -0.0082 -0.0265 0.0115  168 PHE   A C   
4264 O O   A PHE   A 168 ? 0.2949 0.3487 0.3985 -0.0200 0.0026  0.0310  168 PHE   A O   
4265 O O   B PHE   A 168 ? 0.3468 0.3742 0.4661 -0.0110 -0.0354 -0.0041 168 PHE   A O   
4266 C CB  A PHE   A 168 ? 0.2553 0.3084 0.2886 -0.0189 -0.0166 0.0417  168 PHE   A CB  
4267 C CB  B PHE   A 168 ? 0.2307 0.3250 0.3050 -0.0025 -0.0204 0.0307  168 PHE   A CB  
4268 C CG  A PHE   A 168 ? 0.2427 0.2985 0.2666 -0.0221 -0.0191 0.0372  168 PHE   A CG  
4269 C CG  B PHE   A 168 ? 0.2036 0.3126 0.2723 -0.0076 -0.0228 0.0430  168 PHE   A CG  
4270 C CD1 A PHE   A 168 ? 0.2405 0.2950 0.2583 -0.0256 -0.0233 0.0400  168 PHE   A CD1 
4271 C CD1 B PHE   A 168 ? 0.1937 0.3077 0.2614 -0.0184 -0.0272 0.0520  168 PHE   A CD1 
4272 C CD2 A PHE   A 168 ? 0.2330 0.2908 0.2478 -0.0253 -0.0127 0.0332  168 PHE   A CD2 
4273 C CD2 B PHE   A 168 ? 0.1869 0.3027 0.2449 -0.0073 -0.0190 0.0513  168 PHE   A CD2 
4274 C CE1 A PHE   A 168 ? 0.2345 0.2911 0.2491 -0.0301 -0.0223 0.0430  168 PHE   A CE1 
4275 C CE1 B PHE   A 168 ? 0.1812 0.3035 0.2521 -0.0266 -0.0336 0.0573  168 PHE   A CE1 
4276 C CE2 A PHE   A 168 ? 0.2277 0.2860 0.2401 -0.0304 -0.0126 0.0345  168 PHE   A CE2 
4277 C CE2 B PHE   A 168 ? 0.1721 0.2953 0.2238 -0.0184 -0.0242 0.0588  168 PHE   A CE2 
4278 C CZ  A PHE   A 168 ? 0.2296 0.2882 0.2428 -0.0312 -0.0161 0.0392  168 PHE   A CZ  
4279 C CZ  B PHE   A 168 ? 0.1737 0.2985 0.2401 -0.0258 -0.0247 0.0598  168 PHE   A CZ  
4298 N N   A LEU   A 169 ? 0.3148 0.3534 0.3854 -0.0201 0.0119  0.0074  169 LEU   A N   
4299 N N   B LEU   A 169 ? 0.3889 0.3931 0.4719 -0.0151 -0.0159 0.0093  169 LEU   A N   
4300 C CA  A LEU   A 169 ? 0.3383 0.3653 0.4026 -0.0158 0.0183  -0.0011 169 LEU   A CA  
4301 C CA  B LEU   A 169 ? 0.4348 0.4154 0.4942 -0.0171 -0.0072 -0.0004 169 LEU   A CA  
4302 C C   A LEU   A 169 ? 0.3434 0.3659 0.4023 -0.0156 0.0230  0.0041  169 LEU   A C   
4303 C C   B LEU   A 169 ? 0.4565 0.4253 0.5340 -0.0143 -0.0137 -0.0072 169 LEU   A C   
4304 O O   A LEU   A 169 ? 0.3505 0.3698 0.3978 -0.0123 0.0233  0.0062  169 LEU   A O   
4305 O O   B LEU   A 169 ? 0.4653 0.4304 0.5499 -0.0125 -0.0140 -0.0120 169 LEU   A O   
4306 C CB  A LEU   A 169 ? 0.3534 0.3739 0.4138 -0.0147 0.0190  -0.0143 169 LEU   A CB  
4307 C CB  B LEU   A 169 ? 0.4531 0.4245 0.4661 -0.0206 0.0063  -0.0036 169 LEU   A CB  
4308 C CG  A LEU   A 169 ? 0.3648 0.3817 0.4265 -0.0137 0.0197  -0.0281 169 LEU   A CG  
4309 C CG  B LEU   A 169 ? 0.4659 0.4307 0.4357 -0.0242 0.0198  -0.0020 169 LEU   A CG  
4310 C CD1 A LEU   A 169 ? 0.3682 0.3846 0.4343 -0.0126 0.0199  -0.0313 169 LEU   A CD1 
4311 C CD1 B LEU   A 169 ? 0.4706 0.4317 0.4243 -0.0254 0.0250  0.0003  169 LEU   A CD1 
4312 C CD2 A LEU   A 169 ? 0.3686 0.3838 0.4273 -0.0138 0.0206  -0.0338 169 LEU   A CD2 
4313 C CD2 B LEU   A 169 ? 0.4686 0.4341 0.4243 -0.0257 0.0250  -0.0027 169 LEU   A CD2 
4314 O OXT A LEU   A 169 ? 0.3370 0.3623 0.3989 -0.0190 0.0332  0.0036  169 LEU   A OXT 
4315 O OXT B LEU   A 169 ? 0.4635 0.4283 0.5530 -0.0138 -0.0170 -0.0089 169 LEU   A OXT 
4338 N N   A SER   B 1   ? 0.3584 0.3520 0.3588 -0.0847 -0.0744 0.0167  1   SER   B N   
4339 N N   B SER   B 1   ? 0.3456 0.3347 0.3434 -0.1052 -0.0609 0.0114  1   SER   B N   
4340 C CA  A SER   B 1   ? 0.3527 0.3535 0.3588 -0.0866 -0.0779 0.0177  1   SER   B CA  
4341 C CA  B SER   B 1   ? 0.3370 0.3401 0.3476 -0.1087 -0.0667 0.0108  1   SER   B CA  
4342 C C   A SER   B 1   ? 0.3348 0.3496 0.3391 -0.0908 -0.0820 0.0370  1   SER   B C   
4343 C C   B SER   B 1   ? 0.3101 0.3368 0.3245 -0.1168 -0.0759 0.0324  1   SER   B C   
4344 O O   A SER   B 1   ? 0.3400 0.3490 0.3225 -0.0898 -0.0881 0.0333  1   SER   B O   
4345 O O   B SER   B 1   ? 0.3185 0.3366 0.3068 -0.1141 -0.0739 0.0268  1   SER   B O   
4346 C CB  A SER   B 1   ? 0.3621 0.3558 0.3686 -0.0845 -0.0750 0.0042  1   SER   B CB  
4347 C CB  B SER   B 1   ? 0.3503 0.3433 0.3631 -0.1047 -0.0594 -0.0070 1   SER   B CB  
4348 O OG  A SER   B 1   ? 0.3712 0.3616 0.3950 -0.0824 -0.0716 -0.0013 1   SER   B OG  
4349 O OG  B SER   B 1   ? 0.3624 0.3516 0.3987 -0.1014 -0.0571 -0.0149 1   SER   B OG  
4364 N N   A MET   B 2   ? 0.3131 0.3464 0.3311 -0.0930 -0.0742 0.0682  2   MET   B N   
4365 N N   B MET   B 2   ? 0.2800 0.3339 0.3087 -0.1206 -0.0762 0.0749  2   MET   B N   
4366 C CA  A MET   B 2   ? 0.2958 0.3461 0.3328 -0.0860 -0.0687 0.0888  2   MET   B CA  
4367 C CA  B MET   B 2   ? 0.2615 0.3375 0.3042 -0.1052 -0.0812 0.0991  2   MET   B CA  
4368 C C   A MET   B 2   ? 0.2573 0.3270 0.2914 -0.0873 -0.0839 0.1184  2   MET   B C   
4369 C C   B MET   B 2   ? 0.2352 0.3242 0.2776 -0.0924 -0.0960 0.1262  2   MET   B C   
4370 O O   A MET   B 2   ? 0.2566 0.3368 0.2927 -0.0802 -0.0869 0.1134  2   MET   B O   
4371 O O   B MET   B 2   ? 0.2271 0.3355 0.2849 -0.0806 -0.1051 0.1218  2   MET   B O   
4372 C CB  A MET   B 2   ? 0.3223 0.3697 0.3976 -0.0682 -0.0463 0.0694  2   MET   B CB  
4373 C CB  B MET   B 2   ? 0.2831 0.3639 0.3596 -0.0841 -0.0622 0.0811  2   MET   B CB  
4374 C CG  A MET   B 2   ? 0.3473 0.3911 0.4566 -0.0499 -0.0252 0.0557  2   MET   B CG  
4375 C CG  B MET   B 2   ? 0.3040 0.3875 0.4022 -0.0604 -0.0427 0.0803  2   MET   B CG  
4376 S SD  A MET   B 2   ? 0.3680 0.4098 0.5151 -0.0346 -0.0116 0.0454  2   MET   B SD  
4377 S SD  B MET   B 2   ? 0.3217 0.4100 0.4317 -0.0397 -0.0355 0.0848  2   MET   B SD  
4378 C CE  A MET   B 2   ? 0.3735 0.4154 0.5214 -0.0309 -0.0048 0.0444  2   MET   B CE  
4379 C CE  B MET   B 2   ? 0.3251 0.4160 0.4548 -0.0373 -0.0283 0.0733  2   MET   B CE  
4398 N N   . VAL   B 3   ? 0.2191 0.2933 0.2715 -0.1021 -0.0885 0.1446  3   VAL   B N   
4399 C CA  . VAL   B 3   ? 0.2065 0.2567 0.2830 -0.0849 -0.0776 0.1361  3   VAL   B CA  
4400 C C   . VAL   B 3   ? 0.1880 0.2420 0.2477 -0.0744 -0.0766 0.1202  3   VAL   B C   
4401 O O   . VAL   B 3   ? 0.1913 0.2608 0.2533 -0.0743 -0.0781 0.1276  3   VAL   B O   
4402 C CB  . VAL   B 3   ? 0.2202 0.2513 0.3460 -0.0774 -0.0654 0.1093  3   VAL   B CB  
4403 C CG1 . VAL   B 3   ? 0.2250 0.2467 0.3707 -0.0787 -0.0618 0.1063  3   VAL   B CG1 
4404 C CG2 . VAL   B 3   ? 0.2241 0.2521 0.3654 -0.0697 -0.0517 0.1121  3   VAL   B CG2 
4415 N N   . ASN   B 4   ? 0.1775 0.2139 0.2117 -0.0650 -0.0602 0.0934  4   ASN   B N   
4416 C CA  . ASN   B 4   ? 0.1752 0.2061 0.1764 -0.0556 -0.0511 0.0483  4   ASN   B CA  
4417 C C   . ASN   B 4   ? 0.1810 0.2199 0.1665 -0.0566 -0.0368 0.0330  4   ASN   B C   
4418 O O   . ASN   B 4   ? 0.1826 0.2248 0.1823 -0.0534 -0.0326 0.0052  4   ASN   B O   
4419 C CB  . ASN   B 4   ? 0.1713 0.1926 0.1606 -0.0501 -0.0465 0.0357  4   ASN   B CB  
4420 C CG  . ASN   B 4   ? 0.1778 0.1779 0.1573 -0.0484 -0.0453 0.0329  4   ASN   B CG  
4421 O OD1 . ASN   B 4   ? 0.1744 0.1649 0.1639 -0.0473 -0.0462 0.0358  4   ASN   B OD1 
4422 N ND2 . ASN   B 4   ? 0.1997 0.1826 0.1586 -0.0277 -0.0327 0.0255  4   ASN   B ND2 
4429 N N   . SER   B 5   ? 0.1884 0.2344 0.1749 -0.0547 -0.0272 0.0400  5   SER   B N   
4430 C CA  . SER   B 5   ? 0.2054 0.2696 0.1874 -0.0398 -0.0057 0.0410  5   SER   B CA  
4431 C C   . SER   B 5   ? 0.2263 0.2712 0.2250 -0.0584 0.0243  0.0359  5   SER   B C   
4432 O O   . SER   B 5   ? 0.2465 0.2672 0.3130 -0.0518 0.0530  0.0397  5   SER   B O   
4433 C CB  . SER   B 5   ? 0.2144 0.2928 0.2186 -0.0298 0.0013  0.0460  5   SER   B CB  
4434 O OG  . SER   B 5   ? 0.2377 0.3163 0.2813 -0.0208 0.0016  0.0457  5   SER   B OG  
4440 N N   . PHE   B 6   ? 0.2468 0.2891 0.2022 -0.0647 0.0418  0.0405  6   PHE   B N   
4441 C CA  . PHE   B 6   ? 0.2637 0.2959 0.1737 -0.0873 0.0406  0.0188  6   PHE   B CA  
4442 C C   . PHE   B 6   ? 0.3216 0.3338 0.2063 -0.0945 0.0616  -0.0068 6   PHE   B C   
4443 O O   . PHE   B 6   ? 0.3389 0.3639 0.2485 -0.0882 0.0480  -0.0191 6   PHE   B O   
4444 C CB  . PHE   B 6   ? 0.2333 0.2735 0.1672 -0.0839 0.0162  0.0137  6   PHE   B CB  
4445 C CG  . PHE   B 6   ? 0.2027 0.2441 0.1645 -0.0786 -0.0027 0.0128  6   PHE   B CG  
4446 C CD1 . PHE   B 6   ? 0.2081 0.2126 0.1483 -0.0672 -0.0076 0.0114  6   PHE   B CD1 
4447 C CD2 . PHE   B 6   ? 0.1824 0.2427 0.1693 -0.0659 -0.0022 0.0367  6   PHE   B CD2 
4448 C CE1 . PHE   B 6   ? 0.2016 0.1911 0.1583 -0.0575 -0.0099 0.0138  6   PHE   B CE1 
4449 C CE2 . PHE   B 6   ? 0.1840 0.2210 0.1946 -0.0522 0.0079  0.0379  6   PHE   B CE2 
4450 C CZ  . PHE   B 6   ? 0.1843 0.1969 0.1758 -0.0546 0.0028  0.0197  6   PHE   B CZ  
4460 N N   . SER   B 7   ? 0.3607 0.3255 0.2288 -0.1145 0.1023  -0.0284 7   SER   B N   
4461 C CA  . SER   B 7   ? 0.3953 0.3368 0.2882 -0.1134 0.1279  -0.0432 7   SER   B CA  
4462 C C   . SER   B 7   ? 0.3921 0.3204 0.2766 -0.1214 0.1404  -0.0615 7   SER   B C   
4463 O O   . SER   B 7   ? 0.3977 0.3219 0.3176 -0.1290 0.1352  -0.0574 7   SER   B O   
4464 C CB  . SER   B 7   ? 0.4175 0.3607 0.3541 -0.1093 0.1426  -0.0432 7   SER   B CB  
4465 O OG  . SER   B 7   ? 0.4322 0.3760 0.4094 -0.1049 0.1405  -0.0390 7   SER   B OG  
4471 N N   . GLY   B 8   ? 0.3897 0.3064 0.2871 -0.1115 0.1420  -0.0723 8   GLY   B N   
4472 C CA  . GLY   B 8   ? 0.3729 0.2884 0.2888 -0.1038 0.1473  -0.0730 8   GLY   B CA  
4473 C C   . GLY   B 8   ? 0.3492 0.2622 0.2847 -0.0958 0.1474  -0.0691 8   GLY   B C   
4474 O O   . GLY   B 8   ? 0.3609 0.2697 0.3270 -0.0853 0.1500  -0.0703 8   GLY   B O   
4478 N N   . TYR   B 9   ? 0.3220 0.2379 0.2597 -0.0848 0.1156  -0.0833 9   TYR   B N   
4479 C CA  . TYR   B 9   ? 0.2983 0.2093 0.2242 -0.0715 0.0855  -0.0667 9   TYR   B CA  
4480 C C   . TYR   B 9   ? 0.2937 0.2075 0.2049 -0.0658 0.0579  -0.0505 9   TYR   B C   
4481 O O   . TYR   B 9   ? 0.3083 0.2254 0.2417 -0.0687 0.0600  -0.0282 9   TYR   B O   
4482 C CB  . TYR   B 9   ? 0.2860 0.1885 0.2341 -0.0632 0.0778  -0.0581 9   TYR   B CB  
4483 C CG  . TYR   B 9   ? 0.2762 0.1758 0.2284 -0.0577 0.0705  -0.0524 9   TYR   B CG  
4484 C CD1 . TYR   B 9   ? 0.2806 0.1731 0.2351 -0.0737 0.0726  -0.0442 9   TYR   B CD1 
4485 C CD2 . TYR   B 9   ? 0.2580 0.1679 0.2117 -0.0515 0.0600  -0.0533 9   TYR   B CD2 
4486 C CE1 . TYR   B 9   ? 0.2718 0.1834 0.2397 -0.0786 0.0736  -0.0572 9   TYR   B CE1 
4487 C CE2 . TYR   B 9   ? 0.2569 0.1761 0.2204 -0.0535 0.0603  -0.0468 9   TYR   B CE2 
4488 C CZ  . TYR   B 9   ? 0.2610 0.1862 0.2358 -0.0723 0.0693  -0.0608 9   TYR   B CZ  
4489 O OH  . TYR   B 9   ? 0.2632 0.2047 0.2497 -0.0822 0.0673  -0.0725 9   TYR   B OH  
4499 N N   . LEU   B 10  ? 0.2724 0.1868 0.1908 -0.0607 0.0393  -0.0486 10  LEU   B N   
4500 C CA  . LEU   B 10  ? 0.2751 0.1852 0.1898 -0.0683 0.0021  -0.0373 10  LEU   B CA  
4501 C C   . LEU   B 10  ? 0.2619 0.1818 0.1958 -0.0652 -0.0115 -0.0341 10  LEU   B C   
4502 O O   . LEU   B 10  ? 0.2429 0.1835 0.1994 -0.0529 0.0017  -0.0270 10  LEU   B O   
4503 C CB  . LEU   B 10  ? 0.2969 0.1824 0.2043 -0.0761 -0.0202 -0.0205 10  LEU   B CB  
4504 C CG  . LEU   B 10  ? 0.3189 0.1926 0.2356 -0.0753 -0.0528 -0.0042 10  LEU   B CG  
4505 C CD1 . LEU   B 10  ? 0.3344 0.2016 0.2496 -0.0700 -0.0520 -0.0034 10  LEU   B CD1 
4506 C CD2 . LEU   B 10  ? 0.3253 0.2013 0.2575 -0.0749 -0.0550 0.0160  10  LEU   B CD2 
4518 N N   . LYS   B 11  ? 0.2800 0.2103 0.1985 -0.0608 -0.0293 -0.0245 11  LYS   B N   
4519 C CA  . LYS   B 11  ? 0.3008 0.2407 0.2405 -0.0535 -0.0435 -0.0370 11  LYS   B CA  
4520 C C   . LYS   B 11  ? 0.2823 0.2190 0.2473 -0.0741 -0.0400 -0.0440 11  LYS   B C   
4521 O O   . LYS   B 11  ? 0.2993 0.2354 0.2835 -0.0910 -0.0409 -0.0675 11  LYS   B O   
4522 C CB  . LYS   B 11  ? 0.3408 0.2951 0.3134 -0.0287 -0.0456 -0.0409 11  LYS   B CB  
4523 C CG  . LYS   B 11  ? 0.3727 0.3313 0.3876 -0.0138 -0.0442 -0.0487 11  LYS   B CG  
4524 C CD  . LYS   B 11  ? 0.3976 0.3568 0.4519 -0.0048 -0.0425 -0.0566 11  LYS   B CD  
4525 C CE  . LYS   B 11  ? 0.4144 0.3732 0.5031 -0.0022 -0.0444 -0.0622 11  LYS   B CE  
4526 N NZ  . LYS   B 11  ? 0.4240 0.3824 0.5313 -0.0016 -0.0453 -0.0635 11  LYS   B NZ  
4540 N N   . LEU   B 12  ? 0.2452 0.1918 0.2398 -0.0709 -0.0410 -0.0396 12  LEU   B N   
4541 C CA  . LEU   B 12  ? 0.2239 0.1734 0.2464 -0.0633 -0.0248 -0.0401 12  LEU   B CA  
4542 C C   . LEU   B 12  ? 0.2061 0.1774 0.2511 -0.0588 -0.0361 -0.0319 12  LEU   B C   
4543 O O   . LEU   B 12  ? 0.2041 0.1838 0.2698 -0.0620 -0.0479 -0.0295 12  LEU   B O   
4544 C CB  . LEU   B 12  ? 0.2268 0.1586 0.2427 -0.0394 -0.0137 -0.0365 12  LEU   B CB  
4545 C CG  . LEU   B 12  ? 0.2284 0.1534 0.2382 -0.0401 -0.0050 -0.0235 12  LEU   B CG  
4546 C CD1 . LEU   B 12  ? 0.2373 0.1595 0.2366 -0.0281 -0.0102 -0.0023 12  LEU   B CD1 
4547 C CD2 . LEU   B 12  ? 0.2338 0.1523 0.2504 -0.0466 0.0019  -0.0260 12  LEU   B CD2 
4559 N N   . THR   B 13  ? 0.1985 0.1816 0.2548 -0.0571 -0.0377 -0.0342 13  THR   B N   
4560 C CA  . THR   B 13  ? 0.1952 0.1873 0.2369 -0.0619 -0.0475 -0.0194 13  THR   B CA  
4561 C C   . THR   B 13  ? 0.2315 0.2032 0.2368 -0.0748 -0.0679 -0.0150 13  THR   B C   
4562 O O   . THR   B 13  ? 0.2511 0.2081 0.2632 -0.0697 -0.0325 -0.0230 13  THR   B O   
4563 C CB  . THR   B 13  ? 0.1843 0.1925 0.2386 -0.0509 -0.0409 -0.0079 13  THR   B CB  
4564 O OG1 . THR   B 13  ? 0.1731 0.1873 0.2513 -0.0563 -0.0363 -0.0101 13  THR   B OG1 
4565 C CG2 . THR   B 13  ? 0.1927 0.1987 0.2510 -0.0431 -0.0319 -0.0055 13  THR   B CG2 
4573 N N   . ASP   B 14  ? 0.2582 0.2192 0.2630 -0.0797 -0.0993 0.0076  14  ASP   B N   
4574 C CA  . ASP   B 14  ? 0.2801 0.2379 0.2910 -0.0813 -0.1104 0.0243  14  ASP   B CA  
4575 C C   . ASP   B 14  ? 0.2622 0.2159 0.2523 -0.0779 -0.0877 0.0209  14  ASP   B C   
4576 O O   . ASP   B 14  ? 0.2931 0.2374 0.2576 -0.0837 -0.0817 0.0269  14  ASP   B O   
4577 C CB  . ASP   B 14  ? 0.3126 0.2842 0.3789 -0.0801 -0.1291 0.0254  14  ASP   B CB  
4578 C CG  . ASP   B 14  ? 0.3485 0.3301 0.4602 -0.0749 -0.1268 0.0107  14  ASP   B CG  
4579 O OD1 . ASP   B 14  ? 0.3616 0.3383 0.4717 -0.0769 -0.1334 -0.0053 14  ASP   B OD1 
4580 O OD2 . ASP   B 14  ? 0.3545 0.3491 0.5008 -0.0737 -0.1179 0.0110  14  ASP   B OD2 
4585 N N   . ASN   B 15  ? 0.2165 0.1830 0.2252 -0.0588 -0.0712 0.0138  15  ASN   B N   
4586 C CA  . ASN   B 15  ? 0.1824 0.1624 0.2146 -0.0368 -0.0538 -0.0001 15  ASN   B CA  
4587 C C   . ASN   B 15  ? 0.1608 0.1492 0.2003 -0.0285 -0.0394 -0.0032 15  ASN   B C   
4588 O O   . ASN   B 15  ? 0.1577 0.1402 0.2168 -0.0285 -0.0420 -0.0135 15  ASN   B O   
4589 C CB  . ASN   B 15  ? 0.1644 0.1497 0.2292 -0.0177 -0.0536 0.0060  15  ASN   B CB  
4590 C CG  . ASN   B 15  ? 0.1560 0.1523 0.2376 -0.0242 -0.0271 0.0115  15  ASN   B CG  
4591 O OD1 . ASN   B 15  ? 0.1670 0.1858 0.2716 -0.0459 -0.0345 0.0159  15  ASN   B OD1 
4592 N ND2 . ASN   B 15  ? 0.1526 0.1392 0.2234 -0.0191 0.0005  -0.0070 15  ASN   B ND2 
4599 N N   . VAL   B 16  ? 0.1593 0.1418 0.2073 -0.0362 -0.0448 -0.0028 16  VAL   B N   
4600 C CA  . VAL   B 16  ? 0.1591 0.1384 0.1861 -0.0299 -0.0353 -0.0158 16  VAL   B CA  
4601 C C   . VAL   B 16  ? 0.1589 0.1568 0.1897 -0.0405 -0.0305 -0.0136 16  VAL   B C   
4602 O O   . VAL   B 16  ? 0.1623 0.1667 0.2114 -0.0370 -0.0254 -0.0217 16  VAL   B O   
4603 C CB  . VAL   B 16  ? 0.1656 0.1402 0.1989 -0.0172 -0.0259 -0.0232 16  VAL   B CB  
4604 C CG1 . VAL   B 16  ? 0.1728 0.1417 0.2007 -0.0128 -0.0155 -0.0153 16  VAL   B CG1 
4605 C CG2 . VAL   B 16  ? 0.1684 0.1368 0.2246 -0.0074 -0.0208 -0.0172 16  VAL   B CG2 
4615 N N   . TYR   B 17  ? 0.1687 0.1568 0.1785 -0.0377 -0.0259 -0.0147 17  TYR   B N   
4616 C CA  . TYR   B 17  ? 0.1777 0.1763 0.1826 -0.0434 -0.0258 0.0034  17  TYR   B CA  
4617 C C   . TYR   B 17  ? 0.1691 0.1434 0.1900 -0.0489 -0.0123 -0.0146 17  TYR   B C   
4618 O O   . TYR   B 17  ? 0.1695 0.1496 0.1877 -0.0386 -0.0181 -0.0343 17  TYR   B O   
4619 C CB  . TYR   B 17  ? 0.2098 0.2204 0.2171 -0.0314 -0.0229 0.0376  17  TYR   B CB  
4620 C CG  . TYR   B 17  ? 0.2366 0.2669 0.2485 -0.0242 -0.0412 0.0592  17  TYR   B CG  
4621 C CD1 . TYR   B 17  ? 0.2555 0.2850 0.2755 -0.0235 -0.0564 0.0690  17  TYR   B CD1 
4622 C CD2 . TYR   B 17  ? 0.2586 0.2945 0.2769 -0.0136 -0.0548 0.0634  17  TYR   B CD2 
4623 C CE1 . TYR   B 17  ? 0.2766 0.3086 0.2934 -0.0132 -0.0681 0.0738  17  TYR   B CE1 
4624 C CE2 . TYR   B 17  ? 0.2769 0.3140 0.3001 -0.0023 -0.0686 0.0707  17  TYR   B CE2 
4625 C CZ  . TYR   B 17  ? 0.2888 0.3292 0.3042 -0.0009 -0.0762 0.0762  17  TYR   B CZ  
4626 O OH  . TYR   B 17  ? 0.3093 0.3480 0.3209 0.0065  -0.0808 0.0741  17  TYR   B OH  
4636 N N   . ILE   B 18  ? 0.1754 0.1487 0.1776 -0.0360 -0.0067 -0.0175 18  ILE   B N   
4637 C CA  . ILE   B 18  ? 0.1787 0.1462 0.1845 -0.0403 0.0025  -0.0287 18  ILE   B CA  
4638 C C   . ILE   B 18  ? 0.1909 0.1453 0.1897 -0.0516 0.0032  -0.0317 18  ILE   B C   
4639 O O   . ILE   B 18  ? 0.2134 0.1587 0.1883 -0.0430 0.0077  -0.0314 18  ILE   B O   
4640 C CB  . ILE   B 18  ? 0.1825 0.1511 0.1887 -0.0476 -0.0038 -0.0200 18  ILE   B CB  
4641 C CG1 . ILE   B 18  ? 0.1900 0.1542 0.1977 -0.0459 0.0022  -0.0082 18  ILE   B CG1 
4642 C CG2 . ILE   B 18  ? 0.1956 0.1613 0.1885 -0.0439 -0.0064 -0.0204 18  ILE   B CG2 
4643 C CD1 . ILE   B 18  ? 0.1975 0.1812 0.2278 -0.0400 -0.0148 0.0202  18  ILE   B CD1 
4655 N N   . LYS   B 19  ? 0.1941 0.1471 0.1929 -0.0344 0.0336  -0.0377 19  LYS   B N   
4656 C CA  . LYS   B 19  ? 0.2038 0.1592 0.2107 -0.0361 0.0222  -0.0453 19  LYS   B CA  
4657 C C   . LYS   B 19  ? 0.1858 0.1534 0.2259 -0.0287 0.0373  -0.0551 19  LYS   B C   
4658 O O   . LYS   B 19  ? 0.1839 0.1611 0.2117 -0.0204 0.0334  -0.0578 19  LYS   B O   
4659 C CB  . LYS   B 19  ? 0.2270 0.1766 0.2067 -0.0414 0.0378  -0.0375 19  LYS   B CB  
4660 C CG  . LYS   B 19  ? 0.2562 0.2015 0.2284 -0.0498 0.0549  -0.0413 19  LYS   B CG  
4661 C CD  . LYS   B 19  ? 0.2861 0.2345 0.2392 -0.0540 0.0720  -0.0381 19  LYS   B CD  
4662 C CE  . LYS   B 19  ? 0.3090 0.2583 0.2669 -0.0552 0.0717  -0.0425 19  LYS   B CE  
4663 N NZ  . LYS   B 19  ? 0.3232 0.2674 0.2726 -0.0589 0.0668  -0.0402 19  LYS   B NZ  
4677 N N   . ASN   B 20  ? 0.1784 0.1623 0.2582 -0.0250 0.0434  -0.0699 20  ASN   B N   
4678 C CA  . ASN   B 20  ? 0.1852 0.1762 0.2759 -0.0189 0.0500  -0.0804 20  ASN   B CA  
4679 C C   . ASN   B 20  ? 0.1843 0.1938 0.2729 -0.0224 0.0589  -0.0879 20  ASN   B C   
4680 O O   . ASN   B 20  ? 0.2040 0.2304 0.2848 -0.0352 0.0550  -0.0837 20  ASN   B O   
4681 C CB  . ASN   B 20  ? 0.2128 0.1792 0.3051 0.0033  0.0372  -0.0802 20  ASN   B CB  
4682 C CG  . ASN   B 20  ? 0.2372 0.1851 0.3262 0.0311  0.0323  -0.0877 20  ASN   B CG  
4683 O OD1 . ASN   B 20  ? 0.2632 0.2160 0.3458 0.0482  0.0265  -0.0874 20  ASN   B OD1 
4684 N ND2 . ASN   B 20  ? 0.2309 0.1846 0.3223 0.0280  0.0321  -0.0800 20  ASN   B ND2 
4691 N N   . ALA   B 21  ? 0.1853 0.1839 0.2587 -0.0313 0.0636  -0.0767 21  ALA   B N   
4692 C CA  . ALA   B 21  ? 0.1924 0.1859 0.2659 -0.0408 0.0521  -0.0584 21  ALA   B CA  
4693 C C   . ALA   B 21  ? 0.1887 0.1636 0.2524 -0.0263 0.0491  -0.0405 21  ALA   B C   
4694 O O   . ALA   B 21  ? 0.2001 0.1557 0.2347 -0.0296 0.0392  -0.0326 21  ALA   B O   
4695 C CB  . ALA   B 21  ? 0.2094 0.2142 0.2856 -0.0569 0.0398  -0.0410 21  ALA   B CB  
4701 N N   . ASP   B 22  ? 0.1823 0.1536 0.2507 -0.0262 0.0388  -0.0369 22  ASP   B N   
4702 C CA  . ASP   B 22  ? 0.1721 0.1454 0.2390 -0.0150 0.0242  -0.0298 22  ASP   B CA  
4703 C C   . ASP   B 22  ? 0.1653 0.1467 0.1890 -0.0160 0.0272  -0.0138 22  ASP   B C   
4704 O O   . ASP   B 22  ? 0.1710 0.1520 0.1978 -0.0153 0.0231  -0.0120 22  ASP   B O   
4705 C CB  . ASP   B 22  ? 0.1796 0.1523 0.2786 -0.0080 0.0270  -0.0162 22  ASP   B CB  
4706 C CG  . ASP   B 22  ? 0.1794 0.1717 0.3152 0.0032  0.0080  -0.0147 22  ASP   B CG  
4707 O OD1 . ASP   B 22  ? 0.1867 0.1631 0.3162 0.0037  -0.0161 -0.0053 22  ASP   B OD1 
4708 O OD2 . ASP   B 22  ? 0.1885 0.2069 0.3684 0.0158  -0.0055 -0.0334 22  ASP   B OD2 
4713 N N   . ILE   B 23  ? 0.1755 0.1441 0.1710 -0.0143 0.0151  0.0050  23  ILE   B N   
4714 C CA  . ILE   B 23  ? 0.1625 0.1372 0.1641 -0.0162 0.0061  0.0024  23  ILE   B CA  
4715 C C   . ILE   B 23  ? 0.1564 0.1335 0.1677 -0.0119 -0.0079 0.0024  23  ILE   B C   
4716 O O   . ILE   B 23  ? 0.1480 0.1377 0.1571 -0.0098 -0.0043 -0.0005 23  ILE   B O   
4717 C CB  . ILE   B 23  ? 0.1556 0.1411 0.1734 -0.0264 0.0028  0.0151  23  ILE   B CB  
4718 C CG1 . ILE   B 23  ? 0.1508 0.1539 0.1837 -0.0160 0.0119  0.0296  23  ILE   B CG1 
4719 C CG2 . ILE   B 23  ? 0.1636 0.1604 0.1804 -0.0157 0.0043  0.0101  23  ILE   B CG2 
4720 C CD1 . ILE   B 23  ? 0.1603 0.1655 0.1956 -0.0106 0.0148  0.0282  23  ILE   B CD1 
4732 N N   . VAL   B 24  ? 0.1593 0.1368 0.1661 -0.0135 -0.0058 0.0033  24  VAL   B N   
4733 C CA  . VAL   B 24  ? 0.1532 0.1441 0.1838 -0.0081 -0.0089 -0.0011 24  VAL   B CA  
4734 C C   . VAL   B 24  ? 0.1551 0.1477 0.1829 -0.0117 -0.0089 0.0061  24  VAL   B C   
4735 O O   . VAL   B 24  ? 0.1519 0.1563 0.2018 -0.0186 -0.0049 0.0140  24  VAL   B O   
4736 C CB  . VAL   B 24  ? 0.1604 0.1570 0.1955 -0.0011 -0.0224 -0.0045 24  VAL   B CB  
4737 C CG1 . VAL   B 24  ? 0.1642 0.1630 0.2206 -0.0123 -0.0262 -0.0052 24  VAL   B CG1 
4738 C CG2 . VAL   B 24  ? 0.1708 0.1896 0.2079 0.0047  -0.0266 -0.0045 24  VAL   B CG2 
4748 N N   . GLU   B 25  ? 0.1742 0.1573 0.1950 -0.0117 0.0085  -0.0006 25  GLU   B N   
4749 C CA  . GLU   B 25  ? 0.1797 0.1872 0.1971 -0.0002 0.0159  -0.0124 25  GLU   B CA  
4750 C C   . GLU   B 25  ? 0.1784 0.1789 0.1710 -0.0182 0.0161  -0.0016 25  GLU   B C   
4751 O O   . GLU   B 25  ? 0.1876 0.1900 0.1943 -0.0179 0.0310  0.0010  25  GLU   B O   
4752 C CB  . GLU   B 25  ? 0.2227 0.2380 0.2673 0.0296  0.0339  -0.0254 25  GLU   B CB  
4753 C CG  . GLU   B 25  ? 0.2705 0.3054 0.3823 0.0375  0.0314  -0.0294 25  GLU   B CG  
4754 C CD  . GLU   B 25  ? 0.3081 0.3751 0.4790 0.0329  0.0159  -0.0282 25  GLU   B CD  
4755 O OE1 . GLU   B 25  ? 0.3344 0.4007 0.5077 0.0348  0.0147  -0.0257 25  GLU   B OE1 
4756 O OE2 . GLU   B 25  ? 0.3291 0.3954 0.5108 0.0285  0.0062  -0.0326 25  GLU   B OE2 
4763 N N   A GLU   B 26  ? 0.1769 0.1661 0.1506 -0.0304 0.0162  -0.0068 26  GLU   B N   
4764 N N   B GLU   B 26  ? 0.1733 0.1685 0.1580 -0.0298 0.0209  0.0000  26  GLU   B N   
4765 C CA  A GLU   B 26  ? 0.1788 0.1732 0.1566 -0.0384 0.0043  -0.0062 26  GLU   B CA  
4766 C CA  B GLU   B 26  ? 0.1719 0.1845 0.1851 -0.0345 0.0087  0.0093  26  GLU   B CA  
4767 C C   A GLU   B 26  ? 0.1640 0.1731 0.1553 -0.0299 0.0090  0.0100  26  GLU   B C   
4768 C C   B GLU   B 26  ? 0.1591 0.1799 0.1647 -0.0273 0.0137  0.0204  26  GLU   B C   
4769 O O   A GLU   B 26  ? 0.1766 0.1926 0.1635 -0.0255 0.0059  0.0162  26  GLU   B O   
4770 O O   B GLU   B 26  ? 0.1737 0.2045 0.1706 -0.0206 0.0107  0.0277  26  GLU   B O   
4771 C CB  A GLU   B 26  ? 0.2019 0.1810 0.1557 -0.0446 0.0064  -0.0032 26  GLU   B CB  
4772 C CB  B GLU   B 26  ? 0.1916 0.2048 0.2239 -0.0340 0.0138  0.0284  26  GLU   B CB  
4773 C CG  A GLU   B 26  ? 0.2303 0.1905 0.1910 -0.0435 0.0090  -0.0102 26  GLU   B CG  
4774 C CG  B GLU   B 26  ? 0.2134 0.2275 0.2954 -0.0230 0.0162  0.0306  26  GLU   B CG  
4775 C CD  A GLU   B 26  ? 0.2464 0.1904 0.1812 -0.0543 0.0277  -0.0232 26  GLU   B CD  
4776 C CD  B GLU   B 26  ? 0.2138 0.2306 0.3175 -0.0241 0.0336  0.0309  26  GLU   B CD  
4777 O OE1 A GLU   B 26  ? 0.2507 0.1750 0.1595 -0.0503 0.0656  -0.0353 26  GLU   B OE1 
4778 O OE1 B GLU   B 26  ? 0.2176 0.2345 0.3526 -0.0249 0.0569  0.0219  26  GLU   B OE1 
4779 O OE2 A GLU   B 26  ? 0.2585 0.2081 0.1922 -0.0569 0.0299  0.0033  26  GLU   B OE2 
4780 O OE2 B GLU   B 26  ? 0.2109 0.2292 0.3155 -0.0164 0.0380  0.0167  26  GLU   B OE2 
4793 N N   . ALA   B 27  ? 0.1476 0.1629 0.1592 -0.0229 0.0095  0.0173  27  ALA   B N   
4794 C CA  . ALA   B 27  ? 0.1465 0.1597 0.1775 -0.0150 0.0012  0.0276  27  ALA   B CA  
4795 C C   . ALA   B 27  ? 0.1467 0.1727 0.2038 -0.0173 0.0168  0.0454  27  ALA   B C   
4796 O O   . ALA   B 27  ? 0.1591 0.1748 0.2102 -0.0116 0.0081  0.0510  27  ALA   B O   
4797 C CB  . ALA   B 27  ? 0.1612 0.1474 0.1725 -0.0157 -0.0003 0.0226  27  ALA   B CB  
4804 N N   . LYS   B 28  ? 0.1375 0.1908 0.2434 -0.0158 0.0203  0.0697  28  LYS   B N   
4805 C CA  . LYS   B 28  ? 0.1593 0.2332 0.2707 -0.0116 0.0502  0.0966  28  LYS   B CA  
4806 C C   . LYS   B 28  ? 0.1861 0.2532 0.2448 -0.0008 0.0600  0.0841  28  LYS   B C   
4807 O O   . LYS   B 28  ? 0.2094 0.2626 0.2549 0.0002  0.0628  0.0784  28  LYS   B O   
4808 C CB  . LYS   B 28  ? 0.1858 0.2708 0.3354 -0.0018 0.0770  0.1210  28  LYS   B CB  
4809 C CG  . LYS   B 28  ? 0.2157 0.3166 0.3903 0.0103  0.0927  0.1380  28  LYS   B CG  
4810 C CD  . LYS   B 28  ? 0.2714 0.3734 0.4555 0.0145  0.1162  0.1460  28  LYS   B CD  
4811 C CE  . LYS   B 28  ? 0.3342 0.4202 0.5142 0.0197  0.1131  0.1537  28  LYS   B CE  
4812 N NZ  . LYS   B 28  ? 0.3689 0.4441 0.5395 0.0240  0.1063  0.1610  28  LYS   B NZ  
4826 N N   . LYS   B 29  ? 0.2016 0.2780 0.2384 0.0140  0.0627  0.0711  29  LYS   B N   
4827 C CA  . LYS   B 29  ? 0.2406 0.3090 0.2651 0.0165  0.0621  0.0666  29  LYS   B CA  
4828 C C   . LYS   B 29  ? 0.2342 0.3029 0.2350 0.0140  0.0427  0.0723  29  LYS   B C   
4829 O O   . LYS   B 29  ? 0.2581 0.3258 0.2427 0.0228  0.0391  0.0728  29  LYS   B O   
4830 C CB  . LYS   B 29  ? 0.3000 0.3500 0.3527 0.0191  0.0618  0.0512  29  LYS   B CB  
4831 C CG  . LYS   B 29  ? 0.3504 0.3871 0.4471 0.0162  0.0594  0.0413  29  LYS   B CG  
4832 C CD  . LYS   B 29  ? 0.3895 0.4140 0.5244 0.0133  0.0661  0.0316  29  LYS   B CD  
4833 C CE  . LYS   B 29  ? 0.4230 0.4358 0.5738 0.0112  0.0742  0.0252  29  LYS   B CE  
4834 N NZ  . LYS   B 29  ? 0.4399 0.4461 0.6077 0.0104  0.0751  0.0207  29  LYS   B NZ  
4848 N N   . VAL   B 30  ? 0.2018 0.2726 0.2153 -0.0046 0.0300  0.0772  30  VAL   B N   
4849 C CA  . VAL   B 30  ? 0.1911 0.2571 0.2530 -0.0179 -0.0046 0.0795  30  VAL   B CA  
4850 C C   . VAL   B 30  ? 0.1626 0.2450 0.2396 -0.0230 -0.0034 0.0852  30  VAL   B C   
4851 O O   . VAL   B 30  ? 0.1769 0.2627 0.2348 -0.0178 0.0036  0.0911  30  VAL   B O   
4852 C CB  . VAL   B 30  ? 0.2059 0.2519 0.3204 -0.0315 -0.0320 0.0832  30  VAL   B CB  
4853 C CG1 . VAL   B 30  ? 0.2151 0.2614 0.3274 -0.0290 -0.0302 0.0784  30  VAL   B CG1 
4854 C CG2 . VAL   B 30  ? 0.2240 0.2508 0.3496 -0.0381 -0.0404 0.0600  30  VAL   B CG2 
4864 N N   A LYS   B 31  ? 0.1636 0.2256 0.2547 -0.0277 -0.0057 0.0858  31  LYS   B N   
4865 N N   B LYS   B 31  ? 0.1522 0.2157 0.2587 -0.0340 -0.0002 0.0940  31  LYS   B N   
4866 C CA  A LYS   B 31  ? 0.1686 0.2204 0.2749 -0.0309 -0.0126 0.0824  31  LYS   B CA  
4867 C CA  B LYS   B 31  ? 0.1484 0.2113 0.2844 -0.0398 -0.0065 0.0936  31  LYS   B CA  
4868 C C   A LYS   B 31  ? 0.1604 0.1892 0.2440 -0.0338 -0.0226 0.0732  31  LYS   B C   
4869 C C   B LYS   B 31  ? 0.1444 0.1834 0.2533 -0.0399 -0.0167 0.0834  31  LYS   B C   
4870 O O   A LYS   B 31  ? 0.1624 0.1943 0.2479 -0.0270 -0.0221 0.0785  31  LYS   B O   
4871 O O   B LYS   B 31  ? 0.1441 0.1903 0.2666 -0.0296 -0.0114 0.0937  31  LYS   B O   
4872 C CB  A LYS   B 31  ? 0.1877 0.2523 0.3194 -0.0284 0.0051  0.0839  31  LYS   B CB  
4873 C CB  B LYS   B 31  ? 0.1620 0.2470 0.3267 -0.0389 0.0218  0.0999  31  LYS   B CB  
4874 C CG  A LYS   B 31  ? 0.2121 0.2820 0.3651 -0.0266 0.0154  0.0761  31  LYS   B CG  
4875 C CG  B LYS   B 31  ? 0.1893 0.2844 0.3726 -0.0346 0.0308  0.0876  31  LYS   B CG  
4876 C CD  A LYS   B 31  ? 0.2341 0.3075 0.4028 -0.0243 0.0174  0.0661  31  LYS   B CD  
4877 C CD  B LYS   B 31  ? 0.2146 0.3144 0.4130 -0.0346 0.0288  0.0751  31  LYS   B CD  
4878 C CE  A LYS   B 31  ? 0.2498 0.3249 0.4364 -0.0210 0.0126  0.0553  31  LYS   B CE  
4879 C CE  B LYS   B 31  ? 0.2311 0.3341 0.4515 -0.0332 0.0197  0.0625  31  LYS   B CE  
4880 N NZ  A LYS   B 31  ? 0.2610 0.3362 0.4499 -0.0158 0.0061  0.0469  31  LYS   B NZ  
4881 N NZ  B LYS   B 31  ? 0.2447 0.3464 0.4651 -0.0262 0.0077  0.0523  31  LYS   B NZ  
4908 N N   . PRO   B 32  ? 0.1601 0.1570 0.2072 -0.0383 -0.0353 0.0534  32  PRO   B N   
4909 C CA  . PRO   B 32  ? 0.1678 0.1516 0.1624 -0.0400 -0.0383 0.0302  32  PRO   B CA  
4910 C C   . PRO   B 32  ? 0.1757 0.1444 0.1613 -0.0424 -0.0509 0.0335  32  PRO   B C   
4911 O O   . PRO   B 32  ? 0.1877 0.1397 0.1953 -0.0441 -0.0688 0.0364  32  PRO   B O   
4912 C CB  . PRO   B 32  ? 0.1908 0.1456 0.1486 -0.0472 -0.0328 0.0136  32  PRO   B CB  
4913 C CG  . PRO   B 32  ? 0.2027 0.1320 0.1701 -0.0379 -0.0471 0.0226  32  PRO   B CG  
4914 C CD  . PRO   B 32  ? 0.1844 0.1358 0.1931 -0.0280 -0.0487 0.0364  32  PRO   B CD  
4922 N N   . THR   B 33  ? 0.1815 0.1329 0.1459 -0.0387 -0.0447 0.0173  33  THR   B N   
4923 C CA  . THR   B 33  ? 0.1919 0.1397 0.1368 -0.0425 -0.0436 0.0264  33  THR   B CA  
4924 C C   . THR   B 33  ? 0.1934 0.1293 0.1366 -0.0415 -0.0431 0.0153  33  THR   B C   
4925 O O   . THR   B 33  ? 0.2189 0.1318 0.1484 -0.0510 -0.0532 0.0218  33  THR   B O   
4926 C CB  . THR   B 33  ? 0.1993 0.1460 0.1472 -0.0295 -0.0461 0.0313  33  THR   B CB  
4927 O OG1 . THR   B 33  ? 0.1907 0.1549 0.1604 -0.0350 -0.0437 0.0370  33  THR   B OG1 
4928 C CG2 . THR   B 33  ? 0.2310 0.1561 0.1571 -0.0173 -0.0390 0.0234  33  THR   B CG2 
4936 N N   . VAL   B 34  ? 0.1774 0.1289 0.1284 -0.0350 -0.0362 0.0101  34  VAL   B N   
4937 C CA  . VAL   B 34  ? 0.1612 0.1289 0.1361 -0.0323 -0.0323 0.0069  34  VAL   B CA  
4938 C C   . VAL   B 34  ? 0.1466 0.1212 0.1197 -0.0308 -0.0190 0.0048  34  VAL   B C   
4939 O O   . VAL   B 34  ? 0.1671 0.1245 0.1261 -0.0276 -0.0272 0.0096  34  VAL   B O   
4940 C CB  . VAL   B 34  ? 0.1690 0.1381 0.1648 -0.0183 -0.0275 0.0096  34  VAL   B CB  
4941 C CG1 . VAL   B 34  ? 0.1643 0.1478 0.1641 -0.0131 -0.0151 0.0087  34  VAL   B CG1 
4942 C CG2 . VAL   B 34  ? 0.1795 0.1427 0.1886 -0.0128 -0.0305 0.0060  34  VAL   B CG2 
4952 N N   . VAL   B 35  ? 0.1363 0.1149 0.1177 -0.0284 -0.0125 0.0097  35  VAL   B N   
4953 C CA  . VAL   B 35  ? 0.1345 0.1178 0.1154 -0.0213 -0.0062 0.0054  35  VAL   B CA  
4954 C C   . VAL   B 35  ? 0.1251 0.1130 0.1087 -0.0189 -0.0045 0.0022  35  VAL   B C   
4955 O O   . VAL   B 35  ? 0.1290 0.1202 0.1199 -0.0225 0.0024  -0.0035 35  VAL   B O   
4956 C CB  . VAL   B 35  ? 0.1356 0.1372 0.1114 -0.0197 0.0032  0.0042  35  VAL   B CB  
4957 C CG1 . VAL   B 35  ? 0.1304 0.1502 0.1272 -0.0277 -0.0047 0.0094  35  VAL   B CG1 
4958 C CG2 . VAL   B 35  ? 0.1406 0.1346 0.1335 -0.0084 0.0034  0.0000  35  VAL   B CG2 
4968 N N   . VAL   B 36  ? 0.1310 0.1139 0.1068 -0.0204 -0.0072 0.0101  36  VAL   B N   
4969 C CA  . VAL   B 36  ? 0.1238 0.1114 0.1140 -0.0149 0.0010  0.0049  36  VAL   B CA  
4970 C C   . VAL   B 36  ? 0.1175 0.1127 0.1030 -0.0116 -0.0001 0.0064  36  VAL   B C   
4971 O O   . VAL   B 36  ? 0.1273 0.1172 0.1271 -0.0092 -0.0034 -0.0059 36  VAL   B O   
4972 C CB  . VAL   B 36  ? 0.1214 0.1104 0.1155 -0.0157 -0.0006 0.0056  36  VAL   B CB  
4973 C CG1 . VAL   B 36  ? 0.1193 0.1307 0.1326 -0.0140 -0.0011 0.0054  36  VAL   B CG1 
4974 C CG2 . VAL   B 36  ? 0.1289 0.1225 0.1304 -0.0149 -0.0112 0.0096  36  VAL   B CG2 
4984 N N   . ASN   B 37  ? 0.1249 0.1129 0.1052 -0.0035 -0.0059 0.0088  37  ASN   B N   
4985 C CA  . ASN   B 37  ? 0.1221 0.1174 0.1128 0.0011  -0.0095 -0.0008 37  ASN   B CA  
4986 C C   . ASN   B 37  ? 0.1223 0.1214 0.1104 0.0038  -0.0044 0.0001  37  ASN   B C   
4987 O O   . ASN   B 37  ? 0.1313 0.1265 0.1292 0.0035  0.0046  0.0128  37  ASN   B O   
4988 C CB  . ASN   B 37  ? 0.1220 0.1159 0.1152 0.0033  -0.0034 -0.0003 37  ASN   B CB  
4989 C CG  . ASN   B 37  ? 0.1224 0.1213 0.1173 0.0044  -0.0026 0.0035  37  ASN   B CG  
4990 O OD1 . ASN   B 37  ? 0.1351 0.1253 0.1397 0.0140  -0.0089 0.0054  37  ASN   B OD1 
4991 N ND2 . ASN   B 37  ? 0.1326 0.1212 0.1262 0.0026  -0.0107 0.0050  37  ASN   B ND2 
4998 N N   . ALA   B 38  ? 0.1357 0.1132 0.1180 0.0122  0.0062  0.0050  38  ALA   B N   
4999 C CA  . ALA   B 38  ? 0.1441 0.1222 0.1189 0.0011  0.0137  0.0109  38  ALA   B CA  
5000 C C   . ALA   B 38  ? 0.1340 0.1163 0.1120 0.0007  0.0106  0.0084  38  ALA   B C   
5001 O O   . ALA   B 38  ? 0.1462 0.1279 0.1363 0.0116  0.0070  0.0093  38  ALA   B O   
5002 C CB  . ALA   B 38  ? 0.1644 0.1307 0.1331 -0.0118 0.0130  0.0046  38  ALA   B CB  
5008 N N   . ALA   B 39  ? 0.1319 0.1225 0.1097 0.0058  -0.0038 0.0084  39  ALA   B N   
5009 C CA  . ALA   B 39  ? 0.1353 0.1303 0.1194 0.0097  -0.0054 0.0033  39  ALA   B CA  
5010 C C   . ALA   B 39  ? 0.1404 0.1389 0.1056 0.0120  -0.0047 0.0042  39  ALA   B C   
5011 O O   . ALA   B 39  ? 0.1443 0.1407 0.1275 0.0046  0.0023  0.0071  39  ALA   B O   
5012 C CB  . ALA   B 39  ? 0.1428 0.1313 0.1309 0.0024  -0.0018 0.0024  39  ALA   B CB  
5018 N N   . ASN   B 40  ? 0.1454 0.1538 0.1124 0.0066  0.0057  0.0016  40  ASN   B N   
5019 C CA  . ASN   B 40  ? 0.1550 0.1561 0.1271 0.0119  0.0012  0.0051  40  ASN   B CA  
5020 C C   . ASN   B 40  ? 0.1561 0.1563 0.1077 0.0119  0.0001  0.0068  40  ASN   B C   
5021 O O   . ASN   B 40  ? 0.1514 0.1461 0.1230 0.0150  -0.0086 0.0026  40  ASN   B O   
5022 C CB  . ASN   B 40  ? 0.1674 0.1494 0.1460 0.0166  -0.0050 0.0163  40  ASN   B CB  
5023 C CG  . ASN   B 40  ? 0.1748 0.1608 0.1725 0.0126  -0.0132 0.0199  40  ASN   B CG  
5024 O OD1 . ASN   B 40  ? 0.1664 0.1590 0.2582 0.0008  -0.0306 0.0202  40  ASN   B OD1 
5025 N ND2 . ASN   B 40  ? 0.1781 0.1664 0.1793 0.0147  -0.0072 0.0124  40  ASN   B ND2 
5032 N N   . VAL   B 41  ? 0.1648 0.1620 0.1142 0.0199  0.0120  0.0059  41  VAL   B N   
5033 C CA  . VAL   B 41  ? 0.1677 0.1727 0.1104 0.0182  0.0061  -0.0070 41  VAL   B CA  
5034 C C   . VAL   B 41  ? 0.1656 0.1687 0.1057 0.0219  -0.0042 -0.0055 41  VAL   B C   
5035 O O   . VAL   B 41  ? 0.1599 0.1689 0.1232 0.0219  -0.0085 -0.0053 41  VAL   B O   
5036 C CB  . VAL   B 41  ? 0.1821 0.1909 0.1397 0.0050  0.0205  -0.0116 41  VAL   B CB  
5037 C CG1 . VAL   B 41  ? 0.1802 0.1956 0.1616 0.0035  0.0250  -0.0154 41  VAL   B CG1 
5038 C CG2 . VAL   B 41  ? 0.1982 0.2099 0.1367 -0.0031 0.0295  -0.0069 41  VAL   B CG2 
5048 N N   . TYR   B 42  ? 0.1746 0.1699 0.1142 0.0203  -0.0071 -0.0082 42  TYR   B N   
5049 C CA  . TYR   B 42  ? 0.1764 0.1727 0.1216 0.0236  -0.0221 -0.0127 42  TYR   B CA  
5050 C C   . TYR   B 42  ? 0.1621 0.1628 0.1338 0.0256  -0.0205 -0.0103 42  TYR   B C   
5051 O O   . TYR   B 42  ? 0.1636 0.1688 0.1540 0.0190  -0.0276 -0.0204 42  TYR   B O   
5052 C CB  . TYR   B 42  ? 0.2033 0.2012 0.1396 0.0109  -0.0349 0.0022  42  TYR   B CB  
5053 C CG  . TYR   B 42  ? 0.2046 0.2139 0.1306 -0.0019 -0.0281 0.0089  42  TYR   B CG  
5054 C CD1 . TYR   B 42  ? 0.1970 0.2155 0.0993 -0.0097 -0.0115 0.0063  42  TYR   B CD1 
5055 C CD2 . TYR   B 42  ? 0.2165 0.2232 0.1667 -0.0039 -0.0125 0.0218  42  TYR   B CD2 
5056 C CE1 . TYR   B 42  ? 0.2112 0.2331 0.1045 -0.0079 -0.0129 0.0040  42  TYR   B CE1 
5057 C CE2 . TYR   B 42  ? 0.2152 0.2376 0.1661 -0.0021 0.0178  0.0390  42  TYR   B CE2 
5058 C CZ  . TYR   B 42  ? 0.2265 0.2556 0.1349 0.0089  0.0165  0.0184  42  TYR   B CZ  
5059 O OH  . TYR   B 42  ? 0.2593 0.2895 0.1876 0.0273  0.0231  0.0230  42  TYR   B OH  
5069 N N   . LEU   B 43  ? 0.1510 0.1472 0.1147 0.0161  -0.0128 -0.0068 43  LEU   B N   
5070 C CA  . LEU   B 43  ? 0.1502 0.1474 0.1150 0.0084  -0.0100 -0.0002 43  LEU   B CA  
5071 C C   . LEU   B 43  ? 0.1509 0.1488 0.1207 0.0133  -0.0102 0.0035  43  LEU   B C   
5072 O O   . LEU   B 43  ? 0.1519 0.1534 0.1458 0.0135  -0.0196 0.0111  43  LEU   B O   
5073 C CB  . LEU   B 43  ? 0.1419 0.1384 0.1312 0.0041  -0.0162 -0.0041 43  LEU   B CB  
5074 C CG  . LEU   B 43  ? 0.1512 0.1354 0.1334 0.0026  -0.0205 -0.0067 43  LEU   B CG  
5075 C CD1 . LEU   B 43  ? 0.1591 0.1440 0.1647 0.0001  -0.0395 -0.0082 43  LEU   B CD1 
5076 C CD2 . LEU   B 43  ? 0.1489 0.1379 0.1451 -0.0052 -0.0258 -0.0011 43  LEU   B CD2 
5088 N N   . LYS   B 44  ? 0.1515 0.1446 0.1232 0.0134  -0.0078 0.0001  44  LYS   B N   
5089 C CA  . LYS   B 44  ? 0.1650 0.1523 0.1331 0.0186  -0.0043 0.0023  44  LYS   B CA  
5090 C C   . LYS   B 44  ? 0.1593 0.1466 0.1251 0.0209  -0.0132 0.0042  44  LYS   B C   
5091 O O   . LYS   B 44  ? 0.1862 0.1443 0.1528 0.0113  0.0061  0.0054  44  LYS   B O   
5092 C CB  . LYS   B 44  ? 0.1950 0.1777 0.1400 0.0261  -0.0173 0.0019  44  LYS   B CB  
5093 C CG  . LYS   B 44  ? 0.2315 0.2071 0.1774 0.0128  -0.0435 0.0064  44  LYS   B CG  
5094 C CD  . LYS   B 44  ? 0.2682 0.2301 0.2441 -0.0004 -0.0572 0.0064  44  LYS   B CD  
5095 C CE  . LYS   B 44  ? 0.2987 0.2536 0.2968 -0.0045 -0.0652 0.0189  44  LYS   B CE  
5096 N NZ  . LYS   B 44  ? 0.3095 0.2602 0.3170 0.0001  -0.0782 0.0426  44  LYS   B NZ  
5110 N N   . HIS   B 45  ? 0.1469 0.1504 0.1250 0.0147  -0.0074 0.0015  45  HIS   B N   
5111 C CA  . HIS   B 45  ? 0.1553 0.1528 0.1248 0.0127  -0.0122 -0.0001 45  HIS   B CA  
5112 C C   . HIS   B 45  ? 0.1764 0.1712 0.1652 0.0243  -0.0182 -0.0026 45  HIS   B C   
5113 O O   . HIS   B 45  ? 0.1907 0.2106 0.2125 0.0515  0.0157  -0.0004 45  HIS   B O   
5114 C CB  . HIS   B 45  ? 0.1502 0.1559 0.1297 0.0047  -0.0041 -0.0027 45  HIS   B CB  
5115 C CG  . HIS   B 45  ? 0.1476 0.1478 0.1279 0.0060  -0.0077 0.0033  45  HIS   B CG  
5116 N ND1 . HIS   B 45  ? 0.1478 0.1422 0.1353 0.0081  -0.0163 0.0001  45  HIS   B ND1 
5117 C CD2 . HIS   B 45  ? 0.1566 0.1520 0.1416 -0.0019 -0.0113 -0.0043 45  HIS   B CD2 
5118 C CE1 . HIS   B 45  ? 0.1538 0.1350 0.1180 0.0026  -0.0155 -0.0049 45  HIS   B CE1 
5119 N NE2 . HIS   B 45  ? 0.1624 0.1349 0.1346 0.0012  -0.0115 -0.0026 45  HIS   B NE2 
5127 N N   A GLY   B 46  ? 0.1825 0.1698 0.1948 0.0272  -0.0318 0.0090  46  GLY   B N   
5128 N N   B GLY   B 46  ? 0.1852 0.1661 0.1906 0.0304  -0.0358 0.0169  46  GLY   B N   
5129 C CA  A GLY   B 46  ? 0.1927 0.1801 0.2353 0.0226  -0.0364 0.0066  46  GLY   B CA  
5130 C CA  B GLY   B 46  ? 0.1975 0.1775 0.2305 0.0244  -0.0406 0.0151  46  GLY   B CA  
5131 C C   A GLY   B 46  ? 0.1981 0.1979 0.2803 0.0234  -0.0331 0.0002  46  GLY   B C   
5132 C C   B GLY   B 46  ? 0.2025 0.1996 0.2798 0.0254  -0.0361 0.0094  46  GLY   B C   
5133 O O   A GLY   B 46  ? 0.2031 0.2114 0.3431 0.0242  -0.0228 -0.0231 46  GLY   B O   
5134 O O   B GLY   B 46  ? 0.2105 0.2194 0.3437 0.0234  -0.0206 -0.0082 46  GLY   B O   
5141 N N   . GLY   B 47  ? 0.1994 0.2044 0.2662 0.0164  -0.0208 -0.0020 47  GLY   B N   
5142 C CA  . GLY   B 47  ? 0.1877 0.1767 0.2207 0.0071  -0.0117 -0.0094 47  GLY   B CA  
5143 C C   . GLY   B 47  ? 0.1682 0.1519 0.1821 0.0045  -0.0059 0.0038  47  GLY   B C   
5144 O O   . GLY   B 47  ? 0.1782 0.1438 0.1862 0.0070  -0.0059 0.0060  47  GLY   B O   
5149 N N   . GLY   B 48  ? 0.1513 0.1399 0.1799 0.0046  -0.0049 0.0108  48  GLY   B N   
5150 C CA  . GLY   B 48  ? 0.1498 0.1408 0.1713 -0.0003 -0.0044 0.0065  48  GLY   B CA  
5151 C C   . GLY   B 48  ? 0.1466 0.1371 0.1692 0.0037  -0.0016 -0.0069 48  GLY   B C   
5152 O O   . GLY   B 48  ? 0.1476 0.1383 0.1789 0.0062  -0.0062 0.0048  48  GLY   B O   
5156 N N   . VAL   B 49  ? 0.1483 0.1422 0.1521 0.0065  0.0001  -0.0018 49  VAL   B N   
5157 C CA  . VAL   B 49  ? 0.1431 0.1507 0.1446 0.0132  -0.0088 -0.0111 49  VAL   B CA  
5158 C C   . VAL   B 49  ? 0.1355 0.1447 0.1235 0.0164  -0.0019 0.0048  49  VAL   B C   
5159 O O   . VAL   B 49  ? 0.1463 0.1497 0.1446 0.0090  0.0002  0.0030  49  VAL   B O   
5160 C CB  . VAL   B 49  ? 0.1519 0.1672 0.1663 0.0034  -0.0152 -0.0039 49  VAL   B CB  
5161 C CG1 . VAL   B 49  ? 0.1499 0.1801 0.1658 0.0066  -0.0157 -0.0020 49  VAL   B CG1 
5162 C CG2 . VAL   B 49  ? 0.1685 0.1836 0.1738 -0.0076 -0.0350 -0.0035 49  VAL   B CG2 
5172 N N   . ALA   B 50  ? 0.1319 0.1393 0.1283 0.0059  0.0034  0.0065  50  ALA   B N   
5173 C CA  . ALA   B 50  ? 0.1325 0.1237 0.1373 0.0101  0.0063  0.0059  50  ALA   B CA  
5174 C C   . ALA   B 50  ? 0.1394 0.1335 0.1270 0.0075  0.0069  0.0015  50  ALA   B C   
5175 O O   . ALA   B 50  ? 0.1414 0.1351 0.1293 0.0103  0.0018  -0.0004 50  ALA   B O   
5176 C CB  . ALA   B 50  ? 0.1403 0.1305 0.1425 0.0039  0.0003  0.0073  50  ALA   B CB  
5182 N N   . GLY   B 51  ? 0.1424 0.1433 0.1440 0.0154  -0.0068 0.0059  51  GLY   B N   
5183 C CA  . GLY   B 51  ? 0.1432 0.1549 0.1710 0.0160  -0.0046 0.0072  51  GLY   B CA  
5184 C C   . GLY   B 51  ? 0.1370 0.1470 0.1651 0.0191  -0.0024 0.0045  51  GLY   B C   
5185 O O   . GLY   B 51  ? 0.1422 0.1534 0.1804 0.0162  -0.0032 -0.0067 51  GLY   B O   
5189 N N   . ALA   B 52  ? 0.1414 0.1410 0.1466 0.0152  -0.0038 -0.0011 52  ALA   B N   
5190 C CA  . ALA   B 52  ? 0.1409 0.1452 0.1525 0.0199  0.0051  -0.0053 52  ALA   B CA  
5191 C C   . ALA   B 52  ? 0.1374 0.1443 0.1436 0.0158  0.0088  -0.0048 52  ALA   B C   
5192 O O   . ALA   B 52  ? 0.1399 0.1491 0.1595 0.0137  0.0026  -0.0019 52  ALA   B O   
5193 C CB  . ALA   B 52  ? 0.1587 0.1514 0.1580 0.0079  0.0043  -0.0101 52  ALA   B CB  
5199 N N   . LEU   B 53  ? 0.1319 0.1411 0.1379 0.0189  0.0055  0.0032  53  LEU   B N   
5200 C CA  . LEU   B 53  ? 0.1342 0.1552 0.1374 0.0138  0.0040  0.0020  53  LEU   B CA  
5201 C C   . LEU   B 53  ? 0.1370 0.1425 0.1374 0.0110  0.0086  -0.0019 53  LEU   B C   
5202 O O   . LEU   B 53  ? 0.1416 0.1514 0.1490 0.0038  0.0111  0.0063  53  LEU   B O   
5203 C CB  . LEU   B 53  ? 0.1302 0.1628 0.1497 0.0136  0.0102  0.0108  53  LEU   B CB  
5204 C CG  . LEU   B 53  ? 0.1276 0.1715 0.1484 0.0033  0.0038  0.0226  53  LEU   B CG  
5205 C CD1 . LEU   B 53  ? 0.1364 0.1891 0.1631 0.0143  0.0031  0.0072  53  LEU   B CD1 
5206 C CD2 . LEU   B 53  ? 0.1413 0.2003 0.1722 0.0011  -0.0026 -0.0060 53  LEU   B CD2 
5218 N N   . ASN   B 54  ? 0.1382 0.1358 0.1363 0.0077  0.0022  0.0047  54  ASN   B N   
5219 C CA  . ASN   B 54  ? 0.1351 0.1512 0.1398 0.0077  -0.0006 -0.0008 54  ASN   B CA  
5220 C C   . ASN   B 54  ? 0.1349 0.1545 0.1514 0.0043  0.0057  -0.0040 54  ASN   B C   
5221 O O   . ASN   B 54  ? 0.1304 0.1546 0.1659 0.0016  0.0028  -0.0036 54  ASN   B O   
5222 C CB  . ASN   B 54  ? 0.1369 0.1563 0.1555 0.0112  0.0082  -0.0082 54  ASN   B CB  
5223 C CG  . ASN   B 54  ? 0.1423 0.1629 0.1476 0.0078  -0.0058 -0.0015 54  ASN   B CG  
5224 O OD1 . ASN   B 54  ? 0.1329 0.1606 0.1671 0.0045  -0.0141 -0.0168 54  ASN   B OD1 
5225 N ND2 . ASN   B 54  ? 0.1564 0.1828 0.1836 0.0032  -0.0223 0.0129  54  ASN   B ND2 
5232 N N   . LYS   B 55  ? 0.1369 0.1557 0.1760 0.0145  0.0039  0.0005  55  LYS   B N   
5233 C CA  . LYS   B 55  ? 0.1416 0.1715 0.1781 0.0241  0.0001  -0.0112 55  LYS   B CA  
5234 C C   . LYS   B 55  ? 0.1360 0.1719 0.1847 0.0174  0.0043  -0.0146 55  LYS   B C   
5235 O O   . LYS   B 55  ? 0.1334 0.1827 0.1963 0.0138  0.0084  -0.0130 55  LYS   B O   
5236 C CB  . LYS   B 55  ? 0.1536 0.1797 0.2055 0.0394  0.0187  -0.0052 55  LYS   B CB  
5237 C CG  . LYS   B 55  ? 0.1991 0.2081 0.2947 0.0423  0.0262  0.0061  55  LYS   B CG  
5238 C CD  . LYS   B 55  ? 0.2337 0.2359 0.3697 0.0500  0.0388  0.0217  55  LYS   B CD  
5239 C CE  . LYS   B 55  ? 0.2553 0.2611 0.4367 0.0517  0.0502  0.0329  55  LYS   B CE  
5240 N NZ  . LYS   B 55  ? 0.2599 0.2812 0.4707 0.0502  0.0349  0.0485  55  LYS   B NZ  
5254 N N   . ALA   B 56  ? 0.1393 0.1768 0.1731 0.0136  -0.0010 -0.0166 56  ALA   B N   
5255 C CA  . ALA   B 56  ? 0.1484 0.1912 0.1669 0.0076  0.0115  -0.0103 56  ALA   B CA  
5256 C C   . ALA   B 56  ? 0.1476 0.1850 0.1508 0.0060  0.0192  -0.0054 56  ALA   B C   
5257 O O   . ALA   B 56  ? 0.1581 0.1959 0.1736 0.0079  0.0305  0.0015  56  ALA   B O   
5258 C CB  . ALA   B 56  ? 0.1598 0.2111 0.1721 -0.0093 0.0121  -0.0108 56  ALA   B CB  
5264 N N   . THR   B 57  ? 0.1471 0.1752 0.1617 0.0048  0.0210  -0.0154 57  THR   B N   
5265 C CA  . THR   B 57  ? 0.1500 0.1705 0.1621 -0.0023 0.0283  -0.0109 57  THR   B CA  
5266 C C   . THR   B 57  ? 0.1495 0.1843 0.1825 -0.0040 0.0315  -0.0131 57  THR   B C   
5267 O O   . THR   B 57  ? 0.1582 0.1816 0.1922 -0.0108 0.0248  -0.0049 57  THR   B O   
5268 C CB  . THR   B 57  ? 0.1567 0.1565 0.1580 -0.0029 0.0189  0.0072  57  THR   B CB  
5269 O OG1 . THR   B 57  ? 0.1492 0.1497 0.1556 -0.0011 0.0148  0.0028  57  THR   B OG1 
5270 C CG2 . THR   B 57  ? 0.1521 0.1614 0.1621 0.0027  0.0265  0.0049  57  THR   B CG2 
5278 N N   . ASN   B 58  ? 0.1368 0.2046 0.2179 -0.0079 0.0256  -0.0300 58  ASN   B N   
5279 C CA  . ASN   B 58  ? 0.1422 0.2382 0.2554 -0.0184 0.0444  -0.0303 58  ASN   B CA  
5280 C C   . ASN   B 58  ? 0.1319 0.2160 0.2028 -0.0087 0.0117  -0.0254 58  ASN   B C   
5281 O O   . ASN   B 58  ? 0.1373 0.2258 0.2082 -0.0103 0.0072  -0.0252 58  ASN   B O   
5282 C CB  . ASN   B 58  ? 0.2242 0.3031 0.3699 -0.0270 0.0953  -0.0265 58  ASN   B CB  
5283 C CG  . ASN   B 58  ? 0.3464 0.3810 0.5189 -0.0331 0.1075  0.0026  58  ASN   B CG  
5284 O OD1 . ASN   B 58  ? 0.3991 0.4156 0.5699 -0.0339 0.1079  0.0089  58  ASN   B OD1 
5285 N ND2 . ASN   B 58  ? 0.3768 0.3931 0.5698 -0.0349 0.1105  0.0116  58  ASN   B ND2 
5292 N N   . ASN   B 59  ? 0.1319 0.2017 0.1833 -0.0056 0.0041  -0.0165 59  ASN   B N   
5293 C CA  . ASN   B 59  ? 0.1331 0.1965 0.1709 -0.0051 -0.0110 0.0020  59  ASN   B CA  
5294 C C   . ASN   B 59  ? 0.1309 0.1890 0.1568 -0.0108 -0.0090 -0.0022 59  ASN   B C   
5295 O O   . ASN   B 59  ? 0.1366 0.1863 0.1601 -0.0102 -0.0046 -0.0088 59  ASN   B O   
5296 C CB  . ASN   B 59  ? 0.1463 0.2174 0.1883 0.0009  -0.0227 0.0103  59  ASN   B CB  
5297 C CG  . ASN   B 59  ? 0.1584 0.2300 0.1881 0.0106  -0.0288 0.0152  59  ASN   B CG  
5298 O OD1 . ASN   B 59  ? 0.1632 0.2348 0.1964 0.0112  -0.0115 0.0291  59  ASN   B OD1 
5299 N ND2 . ASN   B 59  ? 0.1641 0.2390 0.1923 0.0056  -0.0224 0.0031  59  ASN   B ND2 
5306 N N   . ALA   B 60  ? 0.1368 0.1768 0.1629 -0.0109 0.0017  -0.0070 60  ALA   B N   
5307 C CA  . ALA   B 60  ? 0.1488 0.1680 0.1714 -0.0186 0.0019  0.0026  60  ALA   B CA  
5308 C C   . ALA   B 60  ? 0.1477 0.1558 0.1580 -0.0065 0.0016  -0.0034 60  ALA   B C   
5309 O O   . ALA   B 60  ? 0.1509 0.1558 0.1841 -0.0150 0.0022  -0.0083 60  ALA   B O   
5310 C CB  . ALA   B 60  ? 0.1632 0.1776 0.1943 -0.0187 0.0059  0.0019  60  ALA   B CB  
5316 N N   . MET   B 61  ? 0.1395 0.1488 0.1593 -0.0062 -0.0033 0.0022  61  MET   B N   
5317 C CA  . MET   B 61  ? 0.1332 0.1431 0.1421 -0.0045 -0.0034 0.0034  61  MET   B CA  
5318 C C   . MET   B 61  ? 0.1356 0.1409 0.1434 -0.0110 -0.0053 0.0014  61  MET   B C   
5319 O O   . MET   B 61  ? 0.1394 0.1416 0.1358 -0.0022 -0.0045 -0.0137 61  MET   B O   
5320 C CB  . MET   B 61  ? 0.1339 0.1428 0.1296 0.0021  -0.0093 -0.0011 61  MET   B CB  
5321 C CG  . MET   B 61  ? 0.1281 0.1441 0.1399 0.0019  -0.0050 -0.0022 61  MET   B CG  
5322 S SD  . MET   B 61  ? 0.1308 0.1447 0.1630 -0.0017 -0.0032 -0.0127 61  MET   B SD  
5323 C CE  . MET   B 61  ? 0.1354 0.1666 0.1887 0.0017  -0.0122 -0.0151 61  MET   B CE  
5333 N N   . GLN   B 62  ? 0.1357 0.1474 0.1362 -0.0009 -0.0141 0.0043  62  GLN   B N   
5334 C CA  . GLN   B 62  ? 0.1428 0.1489 0.1433 0.0017  -0.0099 0.0035  62  GLN   B CA  
5335 C C   . GLN   B 62  ? 0.1350 0.1583 0.1346 0.0064  -0.0228 -0.0044 62  GLN   B C   
5336 O O   . GLN   B 62  ? 0.1425 0.1658 0.1427 0.0023  -0.0189 -0.0129 62  GLN   B O   
5337 C CB  . GLN   B 62  ? 0.1458 0.1535 0.1534 0.0114  -0.0055 -0.0035 62  GLN   B CB  
5338 C CG  . GLN   B 62  ? 0.1503 0.1594 0.1486 0.0095  -0.0230 -0.0066 62  GLN   B CG  
5339 C CD  . GLN   B 62  ? 0.1482 0.1538 0.1343 0.0160  -0.0220 0.0072  62  GLN   B CD  
5340 O OE1 . GLN   B 62  ? 0.1491 0.1538 0.1567 0.0136  -0.0222 -0.0068 62  GLN   B OE1 
5341 N NE2 . GLN   B 62  ? 0.1500 0.1578 0.1413 0.0116  -0.0144 -0.0036 62  GLN   B NE2 
5350 N N   . VAL   B 63  ? 0.1294 0.1620 0.1605 -0.0033 -0.0192 -0.0099 63  VAL   B N   
5351 C CA  . VAL   B 63  ? 0.1447 0.1665 0.1755 -0.0086 -0.0236 -0.0119 63  VAL   B CA  
5352 C C   . VAL   B 63  ? 0.1493 0.1531 0.1539 -0.0128 -0.0215 -0.0118 63  VAL   B C   
5353 O O   . VAL   B 63  ? 0.1532 0.1577 0.1626 -0.0053 -0.0337 -0.0150 63  VAL   B O   
5354 C CB  . VAL   B 63  ? 0.1462 0.1781 0.2020 -0.0131 -0.0224 -0.0131 63  VAL   B CB  
5355 C CG1 . VAL   B 63  ? 0.1526 0.1824 0.2175 -0.0258 -0.0098 -0.0120 63  VAL   B CG1 
5356 C CG2 . VAL   B 63  ? 0.1422 0.1950 0.2134 -0.0061 -0.0241 -0.0190 63  VAL   B CG2 
5366 N N   . GLU   B 64  ? 0.1405 0.1453 0.1536 -0.0036 -0.0182 -0.0074 64  GLU   B N   
5367 C CA  . GLU   B 64  ? 0.1444 0.1380 0.1481 -0.0078 -0.0206 -0.0119 64  GLU   B CA  
5368 C C   . GLU   B 64  ? 0.1445 0.1380 0.1419 -0.0039 -0.0300 -0.0163 64  GLU   B C   
5369 O O   . GLU   B 64  ? 0.1578 0.1409 0.1483 -0.0052 -0.0215 -0.0139 64  GLU   B O   
5370 C CB  . GLU   B 64  ? 0.1429 0.1478 0.1414 -0.0093 -0.0139 -0.0036 64  GLU   B CB  
5371 C CG  . GLU   B 64  ? 0.1526 0.1520 0.1406 -0.0177 -0.0214 -0.0134 64  GLU   B CG  
5372 C CD  . GLU   B 64  ? 0.1588 0.1597 0.1534 -0.0227 -0.0209 -0.0061 64  GLU   B CD  
5373 O OE1 . GLU   B 64  ? 0.1570 0.1709 0.1657 -0.0248 -0.0134 -0.0283 64  GLU   B OE1 
5374 O OE2 . GLU   B 64  ? 0.1740 0.1708 0.1680 -0.0270 -0.0361 -0.0053 64  GLU   B OE2 
5381 N N   . SER   B 65  ? 0.1373 0.1331 0.1438 -0.0022 -0.0146 -0.0210 65  SER   B N   
5382 C CA  . SER   B 65  ? 0.1377 0.1407 0.1427 0.0022  -0.0148 -0.0109 65  SER   B CA  
5383 C C   . SER   B 65  ? 0.1374 0.1377 0.1412 0.0019  -0.0156 -0.0181 65  SER   B C   
5384 O O   . SER   B 65  ? 0.1457 0.1516 0.1411 0.0058  -0.0193 -0.0217 65  SER   B O   
5385 C CB  . SER   B 65  ? 0.1439 0.1436 0.1506 -0.0059 -0.0142 -0.0059 65  SER   B CB  
5386 O OG  . SER   B 65  ? 0.1472 0.1424 0.1428 -0.0056 -0.0124 -0.0165 65  SER   B OG  
5392 N N   . ASP   B 66  ? 0.1508 0.1484 0.1439 0.0018  -0.0224 -0.0158 66  ASP   B N   
5393 C CA  . ASP   B 66  ? 0.1662 0.1556 0.1370 0.0077  -0.0298 -0.0118 66  ASP   B CA  
5394 C C   . ASP   B 66  ? 0.1612 0.1572 0.1289 -0.0000 -0.0277 -0.0151 66  ASP   B C   
5395 O O   . ASP   B 66  ? 0.1664 0.1602 0.1486 0.0069  -0.0226 -0.0226 66  ASP   B O   
5396 C CB  . ASP   B 66  ? 0.1767 0.1666 0.1466 0.0136  -0.0438 -0.0232 66  ASP   B CB  
5397 C CG  . ASP   B 66  ? 0.1917 0.1853 0.1801 0.0184  -0.0582 -0.0128 66  ASP   B CG  
5398 O OD1 . ASP   B 66  ? 0.2117 0.1767 0.1858 0.0120  -0.0458 -0.0098 66  ASP   B OD1 
5399 O OD2 . ASP   B 66  ? 0.2026 0.2105 0.2416 0.0397  -0.0566 -0.0114 66  ASP   B OD2 
5404 N N   . ASP   B 67  ? 0.1561 0.1493 0.1371 -0.0023 -0.0246 -0.0250 67  ASP   B N   
5405 C CA  . ASP   B 67  ? 0.1709 0.1479 0.1457 -0.0022 -0.0231 -0.0176 67  ASP   B CA  
5406 C C   . ASP   B 67  ? 0.1691 0.1477 0.1485 0.0051  -0.0202 -0.0214 67  ASP   B C   
5407 O O   . ASP   B 67  ? 0.1726 0.1540 0.1635 0.0008  -0.0156 -0.0302 67  ASP   B O   
5408 C CB  . ASP   B 67  ? 0.1925 0.1541 0.1578 -0.0094 -0.0345 -0.0105 67  ASP   B CB  
5409 C CG  . ASP   B 67  ? 0.2276 0.1562 0.1674 -0.0048 -0.0557 -0.0171 67  ASP   B CG  
5410 O OD1 . ASP   B 67  ? 0.2472 0.1607 0.1888 -0.0101 -0.0520 -0.0087 67  ASP   B OD1 
5411 O OD2 . ASP   B 67  ? 0.2426 0.1629 0.1952 0.0078  -0.0593 -0.0094 67  ASP   B OD2 
5416 N N   . TYR   B 68  ? 0.1641 0.1530 0.1379 0.0061  -0.0298 -0.0250 68  TYR   B N   
5417 C CA  . TYR   B 68  ? 0.1589 0.1639 0.1515 0.0121  -0.0316 -0.0306 68  TYR   B CA  
5418 C C   . TYR   B 68  ? 0.1524 0.1564 0.1569 0.0071  -0.0281 -0.0383 68  TYR   B C   
5419 O O   . TYR   B 68  ? 0.1585 0.1649 0.1582 0.0122  -0.0237 -0.0446 68  TYR   B O   
5420 C CB  . TYR   B 68  ? 0.1597 0.1819 0.1591 0.0148  -0.0400 -0.0415 68  TYR   B CB  
5421 C CG  . TYR   B 68  ? 0.1753 0.1981 0.1781 0.0174  -0.0356 -0.0585 68  TYR   B CG  
5422 C CD1 . TYR   B 68  ? 0.1745 0.2000 0.1908 0.0003  -0.0232 -0.0575 68  TYR   B CD1 
5423 C CD2 . TYR   B 68  ? 0.1854 0.2145 0.1950 0.0210  -0.0431 -0.0491 68  TYR   B CD2 
5424 C CE1 . TYR   B 68  ? 0.1837 0.2081 0.2175 -0.0005 -0.0206 -0.0458 68  TYR   B CE1 
5425 C CE2 . TYR   B 68  ? 0.1889 0.2163 0.1891 0.0212  -0.0293 -0.0586 68  TYR   B CE2 
5426 C CZ  . TYR   B 68  ? 0.1843 0.2162 0.2070 0.0060  -0.0278 -0.0551 68  TYR   B CZ  
5427 O OH  . TYR   B 68  ? 0.1767 0.2303 0.2236 0.0074  -0.0228 -0.0333 68  TYR   B OH  
5437 N N   . ILE   B 69  ? 0.1537 0.1448 0.1513 0.0094  -0.0309 -0.0279 69  ILE   B N   
5438 C CA  . ILE   B 69  ? 0.1587 0.1526 0.1506 0.0050  -0.0220 -0.0301 69  ILE   B CA  
5439 C C   . ILE   B 69  ? 0.1610 0.1523 0.1500 0.0093  -0.0304 -0.0232 69  ILE   B C   
5440 O O   . ILE   B 69  ? 0.1648 0.1608 0.1530 0.0016  -0.0113 -0.0294 69  ILE   B O   
5441 C CB  . ILE   B 69  ? 0.1638 0.1601 0.1713 0.0016  -0.0044 -0.0258 69  ILE   B CB  
5442 C CG1 . ILE   B 69  ? 0.1649 0.1650 0.1909 -0.0052 0.0061  -0.0244 69  ILE   B CG1 
5443 C CG2 . ILE   B 69  ? 0.1747 0.1665 0.1874 0.0054  -0.0094 -0.0187 69  ILE   B CG2 
5444 C CD1 . ILE   B 69  ? 0.1652 0.1658 0.2001 -0.0094 0.0048  -0.0326 69  ILE   B CD1 
5456 N N   . ALA   B 70  ? 0.1565 0.1565 0.1529 0.0121  -0.0338 -0.0257 70  ALA   B N   
5457 C CA  . ALA   B 70  ? 0.1582 0.1612 0.1440 0.0040  -0.0277 -0.0217 70  ALA   B CA  
5458 C C   . ALA   B 70  ? 0.1627 0.1570 0.1438 -0.0025 -0.0390 -0.0321 70  ALA   B C   
5459 O O   . ALA   B 70  ? 0.1775 0.1581 0.1525 -0.0009 -0.0287 -0.0376 70  ALA   B O   
5460 C CB  . ALA   B 70  ? 0.1511 0.1746 0.1603 0.0037  -0.0249 -0.0310 70  ALA   B CB  
5466 N N   . THR   B 71  ? 0.1712 0.1563 0.1549 0.0009  -0.0409 -0.0304 71  THR   B N   
5467 C CA  . THR   B 71  ? 0.1821 0.1494 0.1800 0.0112  -0.0568 -0.0301 71  THR   B CA  
5468 C C   . THR   B 71  ? 0.1815 0.1530 0.2011 0.0235  -0.0548 -0.0466 71  THR   B C   
5469 O O   . THR   B 71  ? 0.1877 0.1651 0.2352 0.0211  -0.0479 -0.0603 71  THR   B O   
5470 C CB  . THR   B 71  ? 0.2033 0.1775 0.2020 0.0048  -0.0609 -0.0162 71  THR   B CB  
5471 O OG1 . THR   B 71  ? 0.2152 0.2076 0.2256 -0.0118 -0.0557 0.0112  71  THR   B OG1 
5472 C CG2 . THR   B 71  ? 0.2208 0.1752 0.2314 0.0075  -0.0546 -0.0045 71  THR   B CG2 
5480 N N   . ASN   B 72  ? 0.1684 0.1572 0.2010 0.0171  -0.0517 -0.0579 72  ASN   B N   
5481 C CA  . ASN   B 72  ? 0.1656 0.1732 0.2113 0.0169  -0.0382 -0.0684 72  ASN   B CA  
5482 C C   . ASN   B 72  ? 0.1619 0.1840 0.2085 0.0042  -0.0152 -0.0702 72  ASN   B C   
5483 O O   . ASN   B 72  ? 0.1571 0.2003 0.2426 -0.0010 -0.0030 -0.0608 72  ASN   B O   
5484 C CB  . ASN   B 72  ? 0.1754 0.1867 0.2196 0.0139  -0.0544 -0.0529 72  ASN   B CB  
5485 C CG  . ASN   B 72  ? 0.1959 0.2044 0.2291 0.0273  -0.0575 -0.0361 72  ASN   B CG  
5486 O OD1 . ASN   B 72  ? 0.2202 0.2255 0.2284 0.0136  -0.0398 -0.0426 72  ASN   B OD1 
5487 N ND2 . ASN   B 72  ? 0.2011 0.2147 0.2735 0.0470  -0.0487 -0.0028 72  ASN   B ND2 
5494 N N   . GLY   B 73  ? 0.1684 0.1896 0.1848 0.0064  -0.0217 -0.0611 73  GLY   B N   
5495 C CA  . GLY   B 73  ? 0.1674 0.1992 0.1611 -0.0006 -0.0107 -0.0571 73  GLY   B CA  
5496 C C   . GLY   B 73  ? 0.1625 0.1930 0.1269 0.0046  -0.0114 -0.0445 73  GLY   B C   
5497 O O   . GLY   B 73  ? 0.1573 0.1723 0.1450 0.0073  -0.0148 -0.0255 73  GLY   B O   
5501 N N   . PRO   B 74  ? 0.1627 0.1973 0.1267 0.0001  -0.0107 -0.0350 74  PRO   B N   
5502 C CA  . PRO   B 74  ? 0.1542 0.1970 0.1135 0.0039  -0.0124 -0.0252 74  PRO   B CA  
5503 C C   . PRO   B 74  ? 0.1504 0.1836 0.1185 0.0044  -0.0040 -0.0178 74  PRO   B C   
5504 O O   . PRO   B 74  ? 0.1550 0.1883 0.1618 0.0032  -0.0042 -0.0296 74  PRO   B O   
5505 C CB  . PRO   B 74  ? 0.1632 0.2148 0.1193 0.0055  -0.0102 -0.0148 74  PRO   B CB  
5506 C CG  . PRO   B 74  ? 0.1912 0.2267 0.1520 0.0016  -0.0042 -0.0116 74  PRO   B CG  
5507 C CD  . PRO   B 74  ? 0.1879 0.2207 0.1334 0.0026  -0.0015 -0.0252 74  PRO   B CD  
5515 N N   . LEU   B 75  ? 0.1470 0.1750 0.1151 0.0084  -0.0167 -0.0162 75  LEU   B N   
5516 C CA  . LEU   B 75  ? 0.1451 0.1721 0.1187 0.0046  -0.0157 -0.0043 75  LEU   B CA  
5517 C C   . LEU   B 75  ? 0.1513 0.1856 0.1302 0.0051  -0.0073 -0.0037 75  LEU   B C   
5518 O O   . LEU   B 75  ? 0.1699 0.1964 0.1367 0.0025  -0.0075 0.0040  75  LEU   B O   
5519 C CB  . LEU   B 75  ? 0.1515 0.1750 0.1059 -0.0054 -0.0190 0.0093  75  LEU   B CB  
5520 C CG  . LEU   B 75  ? 0.1871 0.1936 0.1232 -0.0274 -0.0136 0.0050  75  LEU   B CG  
5521 C CD1 . LEU   B 75  ? 0.2225 0.2154 0.1527 -0.0338 0.0152  -0.0001 75  LEU   B CD1 
5522 C CD2 . LEU   B 75  ? 0.2300 0.2121 0.1968 -0.0166 0.0003  0.0150  75  LEU   B CD2 
5534 N N   . LYS   B 76  ? 0.1513 0.2082 0.1547 -0.0008 0.0014  0.0081  76  LYS   B N   
5535 C CA  . LYS   B 76  ? 0.1620 0.2155 0.1694 -0.0026 0.0209  0.0022  76  LYS   B CA  
5536 C C   . LYS   B 76  ? 0.1594 0.2051 0.1500 0.0101  0.0166  0.0249  76  LYS   B C   
5537 O O   . LYS   B 76  ? 0.1630 0.1859 0.1438 0.0069  0.0134  0.0178  76  LYS   B O   
5538 C CB  . LYS   B 76  ? 0.1796 0.2241 0.2408 -0.0025 0.0474  -0.0379 76  LYS   B CB  
5539 C CG  . LYS   B 76  ? 0.1880 0.2418 0.2894 0.0035  0.0368  -0.0519 76  LYS   B CG  
5540 C CD  . LYS   B 76  ? 0.1860 0.2477 0.3308 0.0086  0.0251  -0.0749 76  LYS   B CD  
5541 C CE  . LYS   B 76  ? 0.1945 0.2586 0.3899 0.0079  0.0010  -0.0891 76  LYS   B CE  
5542 N NZ  . LYS   B 76  ? 0.1869 0.2646 0.4076 0.0047  -0.0241 -0.1093 76  LYS   B NZ  
5556 N N   . VAL   B 77  ? 0.1684 0.2157 0.1460 0.0159  0.0135  0.0292  77  VAL   B N   
5557 C CA  . VAL   B 77  ? 0.1721 0.2066 0.1593 0.0240  0.0225  0.0557  77  VAL   B CA  
5558 C C   . VAL   B 77  ? 0.1579 0.1789 0.1530 0.0221  0.0325  0.0397  77  VAL   B C   
5559 O O   . VAL   B 77  ? 0.1596 0.1748 0.1604 0.0261  0.0341  0.0282  77  VAL   B O   
5560 C CB  . VAL   B 77  ? 0.1862 0.2217 0.1919 0.0281  0.0376  0.0787  77  VAL   B CB  
5561 C CG1 . VAL   B 77  ? 0.1921 0.2202 0.2335 0.0220  0.0430  0.0982  77  VAL   B CG1 
5562 C CG2 . VAL   B 77  ? 0.1925 0.2387 0.2137 0.0270  0.0157  0.0747  77  VAL   B CG2 
5572 N N   . GLY   B 78  ? 0.1491 0.1660 0.1548 0.0184  0.0229  0.0344  78  GLY   B N   
5573 C CA  . GLY   B 78  ? 0.1512 0.1633 0.1555 0.0191  0.0286  0.0272  78  GLY   B CA  
5574 C C   . GLY   B 78  ? 0.1369 0.1531 0.1453 0.0171  0.0260  0.0260  78  GLY   B C   
5575 O O   . GLY   B 78  ? 0.1432 0.1447 0.1596 0.0180  0.0201  0.0243  78  GLY   B O   
5579 N N   . GLY   B 79  ? 0.1343 0.1519 0.1510 0.0149  0.0176  0.0219  79  GLY   B N   
5580 C CA  . GLY   B 79  ? 0.1350 0.1461 0.1401 0.0161  0.0103  0.0212  79  GLY   B CA  
5581 C C   . GLY   B 79  ? 0.1307 0.1392 0.1431 0.0169  0.0116  0.0143  79  GLY   B C   
5582 O O   . GLY   B 79  ? 0.1394 0.1369 0.1497 0.0176  0.0180  0.0220  79  GLY   B O   
5586 N N   . SER   B 80  ? 0.1316 0.1307 0.1441 0.0110  0.0197  0.0099  80  SER   B N   
5587 C CA  . SER   B 80  ? 0.1242 0.1271 0.1452 0.0086  0.0047  0.0060  80  SER   B CA  
5588 C C   . SER   B 80  ? 0.1266 0.1253 0.1336 0.0069  -0.0020 -0.0010 80  SER   B C   
5589 O O   . SER   B 80  ? 0.1433 0.1341 0.1622 0.0119  0.0077  -0.0058 80  SER   B O   
5590 C CB  . SER   B 80  ? 0.1298 0.1305 0.1393 0.0001  0.0067  0.0037  80  SER   B CB  
5591 O OG  . SER   B 80  ? 0.1362 0.1464 0.1615 -0.0037 -0.0113 0.0128  80  SER   B OG  
5597 N N   . CYS   B 81  ? 0.1271 0.1193 0.1371 0.0029  -0.0051 0.0005  81  CYS   B N   
5598 C CA  . CYS   B 81  ? 0.1336 0.1212 0.1511 0.0023  -0.0096 0.0030  81  CYS   B CA  
5599 C C   . CYS   B 81  ? 0.1289 0.1135 0.1293 -0.0013 -0.0163 -0.0010 81  CYS   B C   
5600 O O   . CYS   B 81  ? 0.1469 0.1163 0.1429 0.0101  -0.0036 -0.0024 81  CYS   B O   
5601 C CB  . CYS   B 81  ? 0.1457 0.1328 0.1555 -0.0054 -0.0091 -0.0064 81  CYS   B CB  
5602 S SG  . CYS   B 81  ? 0.1442 0.1467 0.1413 -0.0012 -0.0227 -0.0074 81  CYS   B SG  
5608 N N   . VAL   B 82  ? 0.1375 0.1155 0.1448 -0.0003 -0.0130 0.0004  82  VAL   B N   
5609 C CA  . VAL   B 82  ? 0.1410 0.1202 0.1297 -0.0040 -0.0056 0.0094  82  VAL   B CA  
5610 C C   . VAL   B 82  ? 0.1478 0.1093 0.1421 -0.0028 -0.0095 0.0048  82  VAL   B C   
5611 O O   . VAL   B 82  ? 0.1508 0.1129 0.1735 -0.0025 -0.0046 -0.0126 82  VAL   B O   
5612 C CB  . VAL   B 82  ? 0.1485 0.1432 0.1564 -0.0048 -0.0145 0.0091  82  VAL   B CB  
5613 C CG1 . VAL   B 82  ? 0.1604 0.1643 0.1642 -0.0010 -0.0084 0.0213  82  VAL   B CG1 
5614 C CG2 . VAL   B 82  ? 0.1514 0.1558 0.1760 -0.0028 -0.0314 0.0198  82  VAL   B CG2 
5624 N N   . LEU   B 83  ? 0.1379 0.1129 0.1353 -0.0124 -0.0180 -0.0015 83  LEU   B N   
5625 C CA  . LEU   B 83  ? 0.1386 0.1203 0.1295 -0.0103 -0.0177 -0.0001 83  LEU   B CA  
5626 C C   . LEU   B 83  ? 0.1387 0.1197 0.1317 -0.0155 -0.0185 0.0049  83  LEU   B C   
5627 O O   . LEU   B 83  ? 0.1401 0.1294 0.1184 -0.0205 -0.0184 -0.0001 83  LEU   B O   
5628 C CB  . LEU   B 83  ? 0.1460 0.1320 0.1221 -0.0124 -0.0113 -0.0017 83  LEU   B CB  
5629 C CG  . LEU   B 83  ? 0.1595 0.1524 0.1407 -0.0171 -0.0155 -0.0047 83  LEU   B CG  
5630 C CD1 . LEU   B 83  ? 0.1632 0.1591 0.1396 -0.0176 -0.0269 0.0062  83  LEU   B CD1 
5631 C CD2 . LEU   B 83  ? 0.1831 0.1602 0.1664 -0.0075 -0.0144 -0.0246 83  LEU   B CD2 
5643 N N   . SER   B 84  ? 0.1371 0.1355 0.1448 -0.0229 -0.0156 0.0044  84  SER   B N   
5644 C CA  . SER   B 84  ? 0.1434 0.1520 0.1440 -0.0265 -0.0131 0.0150  84  SER   B CA  
5645 C C   . SER   B 84  ? 0.1333 0.1673 0.1068 -0.0222 -0.0141 0.0123  84  SER   B C   
5646 O O   . SER   B 84  ? 0.1468 0.1512 0.1138 -0.0184 -0.0066 -0.0030 84  SER   B O   
5647 C CB  . SER   B 84  ? 0.1604 0.1553 0.1809 -0.0275 0.0044  0.0155  84  SER   B CB  
5648 O OG  . SER   B 84  ? 0.1627 0.1687 0.2204 -0.0362 0.0072  0.0181  84  SER   B OG  
5654 N N   . GLY   B 85  ? 0.1407 0.1896 0.1211 -0.0224 -0.0138 0.0151  85  GLY   B N   
5655 C CA  . GLY   B 85  ? 0.1414 0.1937 0.1387 -0.0343 -0.0016 -0.0085 85  GLY   B CA  
5656 C C   . GLY   B 85  ? 0.1415 0.1766 0.1236 -0.0445 -0.0051 0.0069  85  GLY   B C   
5657 O O   . GLY   B 85  ? 0.1550 0.1808 0.1356 -0.0589 0.0146  -0.0081 85  GLY   B O   
5661 N N   . HIS   B 86  ? 0.1352 0.1619 0.1341 -0.0324 -0.0079 0.0128  86  HIS   B N   
5662 C CA  . HIS   B 86  ? 0.1407 0.1628 0.1333 -0.0332 -0.0128 0.0082  86  HIS   B CA  
5663 C C   . HIS   B 86  ? 0.1415 0.1726 0.1329 -0.0454 0.0005  0.0213  86  HIS   B C   
5664 O O   . HIS   B 86  ? 0.1549 0.1866 0.1396 -0.0374 0.0137  0.0239  86  HIS   B O   
5665 C CB  . HIS   B 86  ? 0.1495 0.1674 0.1420 -0.0190 -0.0141 0.0036  86  HIS   B CB  
5666 C CG  . HIS   B 86  ? 0.1473 0.1759 0.1359 -0.0118 -0.0111 0.0078  86  HIS   B CG  
5667 N ND1 . HIS   B 86  ? 0.1550 0.1948 0.1574 -0.0200 -0.0120 -0.0144 86  HIS   B ND1 
5668 C CD2 . HIS   B 86  ? 0.1560 0.1758 0.1329 -0.0037 -0.0108 -0.0012 86  HIS   B CD2 
5669 C CE1 . HIS   B 86  ? 0.1639 0.1874 0.1529 -0.0146 -0.0079 -0.0192 86  HIS   B CE1 
5670 N NE2 . HIS   B 86  ? 0.1637 0.1781 0.1364 0.0015  -0.0024 -0.0026 86  HIS   B NE2 
5678 N N   . ASN   B 87  ? 0.1438 0.1726 0.1443 -0.0355 0.0084  0.0122  87  ASN   B N   
5679 C CA  . ASN   B 87  ? 0.1566 0.1909 0.1532 -0.0318 0.0274  0.0102  87  ASN   B CA  
5680 C C   . ASN   B 87  ? 0.1682 0.1752 0.1301 -0.0368 0.0240  0.0139  87  ASN   B C   
5681 O O   . ASN   B 87  ? 0.1998 0.1815 0.1611 -0.0295 0.0469  0.0032  87  ASN   B O   
5682 C CB  . ASN   B 87  ? 0.1556 0.2195 0.1908 -0.0241 0.0383  0.0055  87  ASN   B CB  
5683 C CG  . ASN   B 87  ? 0.1637 0.2368 0.1888 0.0037  0.0381  0.0193  87  ASN   B CG  
5684 O OD1 . ASN   B 87  ? 0.1562 0.2218 0.1769 0.0134  0.0498  0.0285  87  ASN   B OD1 
5685 N ND2 . ASN   B 87  ? 0.2013 0.2477 0.2298 0.0116  0.0400  0.0187  87  ASN   B ND2 
5692 N N   . LEU   B 88  ? 0.1577 0.1660 0.1243 -0.0410 0.0138  0.0096  88  LEU   B N   
5693 C CA  . LEU   B 88  ? 0.1724 0.1598 0.1256 -0.0403 0.0081  0.0032  88  LEU   B CA  
5694 C C   . LEU   B 88  ? 0.1696 0.1486 0.1294 -0.0443 0.0021  0.0006  88  LEU   B C   
5695 O O   . LEU   B 88  ? 0.1930 0.1545 0.1555 -0.0280 -0.0258 -0.0082 88  LEU   B O   
5696 C CB  . LEU   B 88  ? 0.1899 0.1747 0.1508 -0.0511 -0.0128 0.0133  88  LEU   B CB  
5697 C CG  . LEU   B 88  ? 0.2293 0.1995 0.1690 -0.0420 -0.0283 0.0306  88  LEU   B CG  
5698 C CD1 . LEU   B 88  ? 0.2324 0.2320 0.1976 -0.0497 -0.0190 0.0486  88  LEU   B CD1 
5699 C CD2 . LEU   B 88  ? 0.2717 0.2254 0.2340 -0.0087 -0.0479 0.0161  88  LEU   B CD2 
5711 N N   . ALA   B 89  ? 0.1544 0.1496 0.1263 -0.0437 0.0149  -0.0063 89  ALA   B N   
5712 C CA  . ALA   B 89  ? 0.1515 0.1464 0.1145 -0.0367 0.0062  0.0057  89  ALA   B CA  
5713 C C   . ALA   B 89  ? 0.1621 0.1497 0.1134 -0.0483 0.0128  0.0017  89  ALA   B C   
5714 O O   . ALA   B 89  ? 0.1431 0.1598 0.1459 -0.0419 0.0192  -0.0320 89  ALA   B O   
5715 C CB  . ALA   B 89  ? 0.1414 0.1462 0.1293 -0.0359 0.0075  0.0135  89  ALA   B CB  
5721 N N   . LYS   B 90  ? 0.1994 0.1406 0.1179 -0.0507 -0.0104 0.0117  90  LYS   B N   
5722 C CA  . LYS   B 90  ? 0.2091 0.1356 0.1200 -0.0459 -0.0173 0.0089  90  LYS   B CA  
5723 C C   . LYS   B 90  ? 0.1888 0.1252 0.1327 -0.0413 -0.0091 0.0030  90  LYS   B C   
5724 O O   . LYS   B 90  ? 0.1904 0.1451 0.1432 -0.0516 -0.0055 0.0060  90  LYS   B O   
5725 C CB  . LYS   B 90  ? 0.2239 0.1421 0.1407 -0.0399 -0.0029 0.0159  90  LYS   B CB  
5726 C CG  . LYS   B 90  ? 0.2188 0.1532 0.1611 -0.0270 0.0250  0.0142  90  LYS   B CG  
5727 C CD  . LYS   B 90  ? 0.2422 0.1778 0.2113 -0.0129 0.0414  -0.0030 90  LYS   B CD  
5728 C CE  . LYS   B 90  ? 0.2538 0.1905 0.2634 -0.0168 0.0516  -0.0168 90  LYS   B CE  
5729 N NZ  . LYS   B 90  ? 0.2618 0.1857 0.2598 -0.0228 0.0754  -0.0097 90  LYS   B NZ  
5743 N N   . HIS   B 91  ? 0.1623 0.1172 0.1186 -0.0312 -0.0164 0.0078  91  HIS   B N   
5744 C CA  . HIS   B 91  ? 0.1542 0.1221 0.1250 -0.0259 -0.0147 0.0062  91  HIS   B CA  
5745 C C   . HIS   B 91  ? 0.1411 0.1202 0.1123 -0.0261 -0.0044 -0.0008 91  HIS   B C   
5746 O O   . HIS   B 91  ? 0.1514 0.1265 0.1177 -0.0297 -0.0097 0.0023  91  HIS   B O   
5747 C CB  . HIS   B 91  ? 0.1706 0.1249 0.1672 -0.0114 -0.0129 0.0166  91  HIS   B CB  
5748 C CG  . HIS   B 91  ? 0.2117 0.1397 0.2338 0.0011  0.0232  0.0282  91  HIS   B CG  
5749 N ND1 . HIS   B 91  ? 0.2442 0.1431 0.2887 0.0016  0.0369  0.0097  91  HIS   B ND1 
5750 C CD2 . HIS   B 91  ? 0.2228 0.1657 0.2823 0.0169  0.0002  0.0604  91  HIS   B CD2 
5751 C CE1 . HIS   B 91  ? 0.2502 0.1575 0.3072 0.0166  0.0305  0.0242  91  HIS   B CE1 
5752 N NE2 . HIS   B 91  ? 0.2444 0.1745 0.3058 0.0231  0.0140  0.0619  91  HIS   B NE2 
5760 N N   . CYS   B 92  ? 0.1318 0.1199 0.1144 -0.0238 -0.0024 -0.0045 92  CYS   B N   
5761 C CA  . CYS   B 92  ? 0.1293 0.1212 0.1162 -0.0176 -0.0024 0.0048  92  CYS   B CA  
5762 C C   . CYS   B 92  ? 0.1258 0.1145 0.1065 -0.0120 -0.0072 0.0030  92  CYS   B C   
5763 O O   . CYS   B 92  ? 0.1349 0.1229 0.1248 -0.0146 -0.0036 -0.0011 92  CYS   B O   
5764 C CB  . CYS   B 92  ? 0.1320 0.1341 0.1204 -0.0127 -0.0079 0.0027  92  CYS   B CB  
5765 S SG  . CYS   B 92  ? 0.1309 0.1303 0.1187 -0.0099 -0.0071 0.0065  92  CYS   B SG  
5771 N N   . LEU   B 93  ? 0.1182 0.1151 0.1077 -0.0119 -0.0062 -0.0020 93  LEU   B N   
5772 C CA  . LEU   B 93  ? 0.1230 0.1097 0.1191 -0.0023 -0.0093 -0.0004 93  LEU   B CA  
5773 C C   . LEU   B 93  ? 0.1155 0.1100 0.1100 -0.0028 -0.0028 0.0055  93  LEU   B C   
5774 O O   . LEU   B 93  ? 0.1224 0.1126 0.1273 -0.0058 -0.0038 0.0011  93  LEU   B O   
5775 C CB  . LEU   B 93  ? 0.1298 0.1093 0.1299 -0.0019 -0.0099 0.0065  93  LEU   B CB  
5776 C CG  . LEU   B 93  ? 0.1256 0.1249 0.1400 -0.0055 -0.0070 0.0174  93  LEU   B CG  
5777 C CD1 . LEU   B 93  ? 0.1283 0.1382 0.1442 0.0042  -0.0078 0.0015  93  LEU   B CD1 
5778 C CD2 . LEU   B 93  ? 0.1279 0.1271 0.1668 -0.0021 -0.0065 0.0141  93  LEU   B CD2 
5790 N N   . HIS   B 94  ? 0.1211 0.1099 0.1087 -0.0066 -0.0084 0.0078  94  HIS   B N   
5791 C CA  . HIS   B 94  ? 0.1241 0.1152 0.1047 0.0027  -0.0061 0.0045  94  HIS   B CA  
5792 C C   . HIS   B 94  ? 0.1232 0.1127 0.1125 0.0037  0.0009  0.0124  94  HIS   B C   
5793 O O   . HIS   B 94  ? 0.1202 0.1203 0.1601 -0.0002 0.0097  -0.0025 94  HIS   B O   
5794 C CB  . HIS   B 94  ? 0.1235 0.1215 0.1175 0.0009  -0.0073 0.0018  94  HIS   B CB  
5795 C CG  . HIS   B 94  ? 0.1225 0.1176 0.1138 -0.0024 -0.0181 0.0043  94  HIS   B CG  
5796 N ND1 . HIS   B 94  ? 0.1281 0.1219 0.1160 0.0019  -0.0171 0.0020  94  HIS   B ND1 
5797 C CD2 . HIS   B 94  ? 0.1310 0.1191 0.1322 0.0004  -0.0159 0.0023  94  HIS   B CD2 
5798 C CE1 . HIS   B 94  ? 0.1272 0.1234 0.1188 -0.0067 -0.0117 0.0060  94  HIS   B CE1 
5799 N NE2 . HIS   B 94  ? 0.1224 0.1274 0.1303 -0.0104 -0.0095 0.0023  94  HIS   B NE2 
5807 N N   . VAL   B 95  ? 0.1131 0.1125 0.1264 0.0030  0.0021  0.0104  95  VAL   B N   
5808 C CA  . VAL   B 95  ? 0.1213 0.1182 0.1252 0.0010  0.0036  0.0100  95  VAL   B CA  
5809 C C   . VAL   B 95  ? 0.1281 0.1222 0.1176 0.0076  0.0084  0.0064  95  VAL   B C   
5810 O O   . VAL   B 95  ? 0.1298 0.1176 0.1410 0.0104  0.0069  0.0173  95  VAL   B O   
5811 C CB  . VAL   B 95  ? 0.1238 0.1199 0.1268 -0.0008 -0.0071 0.0072  95  VAL   B CB  
5812 C CG1 . VAL   B 95  ? 0.1343 0.1366 0.1346 -0.0120 0.0016  0.0082  95  VAL   B CG1 
5813 C CG2 . VAL   B 95  ? 0.1294 0.1211 0.1262 -0.0033 -0.0150 0.0018  95  VAL   B CG2 
5823 N N   . VAL   B 96  ? 0.1391 0.1239 0.1224 0.0146  0.0063  0.0196  96  VAL   B N   
5824 C CA  . VAL   B 96  ? 0.1409 0.1394 0.1170 0.0137  0.0082  0.0221  96  VAL   B CA  
5825 C C   . VAL   B 96  ? 0.1431 0.1426 0.1300 0.0106  0.0179  0.0214  96  VAL   B C   
5826 O O   . VAL   B 96  ? 0.1433 0.1445 0.1545 0.0061  0.0190  0.0086  96  VAL   B O   
5827 C CB  . VAL   B 96  ? 0.1454 0.1597 0.1220 0.0154  0.0112  0.0104  96  VAL   B CB  
5828 C CG1 . VAL   B 96  ? 0.1447 0.1698 0.1357 0.0144  0.0076  0.0157  96  VAL   B CG1 
5829 C CG2 . VAL   B 96  ? 0.1569 0.1674 0.1387 0.0112  0.0065  0.0092  96  VAL   B CG2 
5839 N N   . GLY   B 97  ? 0.1484 0.1418 0.1301 0.0103  0.0086  0.0228  97  GLY   B N   
5840 C CA  . GLY   B 97  ? 0.1709 0.1410 0.1376 0.0156  0.0089  0.0241  97  GLY   B CA  
5841 C C   . GLY   B 97  ? 0.1898 0.1478 0.1452 0.0248  0.0144  0.0257  97  GLY   B C   
5842 O O   . GLY   B 97  ? 0.2044 0.1563 0.1393 0.0188  0.0112  0.0226  97  GLY   B O   
5846 N N   . PRO   B 98  ? 0.2018 0.1545 0.1655 0.0187  0.0399  0.0374  98  PRO   B N   
5847 C CA  . PRO   B 98  ? 0.2184 0.1732 0.1805 0.0331  0.0564  0.0417  98  PRO   B CA  
5848 C C   . PRO   B 98  ? 0.2306 0.1781 0.1491 0.0535  0.0651  0.0568  98  PRO   B C   
5849 O O   . PRO   B 98  ? 0.2182 0.1740 0.1667 0.0436  0.0652  0.0498  98  PRO   B O   
5850 C CB  . PRO   B 98  ? 0.2083 0.1817 0.2093 0.0249  0.0646  0.0383  98  PRO   B CB  
5851 C CG  . PRO   B 98  ? 0.2024 0.1745 0.1972 0.0173  0.0560  0.0534  98  PRO   B CG  
5852 C CD  . PRO   B 98  ? 0.1894 0.1603 0.1859 0.0218  0.0472  0.0481  98  PRO   B CD  
5860 N N   . ASN   B 99  ? 0.2511 0.1991 0.1548 0.0684  0.0595  0.0405  99  ASN   B N   
5861 C CA  . ASN   B 99  ? 0.2732 0.2131 0.1631 0.0793  0.0475  0.0637  99  ASN   B CA  
5862 C C   . ASN   B 99  ? 0.2987 0.2445 0.1923 0.0776  0.0739  0.0911  99  ASN   B C   
5863 O O   . ASN   B 99  ? 0.3156 0.2491 0.1985 0.0824  0.0673  0.0805  99  ASN   B O   
5864 C CB  . ASN   B 99  ? 0.2795 0.2072 0.1660 0.0805  0.0342  0.0523  99  ASN   B CB  
5865 C CG  . ASN   B 99  ? 0.2875 0.2147 0.1829 0.0749  0.0331  0.0405  99  ASN   B CG  
5866 O OD1 . ASN   B 99  ? 0.2930 0.2118 0.2075 0.0832  0.0365  0.0504  99  ASN   B OD1 
5867 N ND2 . ASN   B 99  ? 0.2899 0.2176 0.1872 0.0685  0.0024  0.0229  99  ASN   B ND2 
5874 N N   A VAL   B 100 ? 0.3169 0.2611 0.2439 0.0655  0.0685  0.1080  100 VAL   B N   
5875 N N   B VAL   B 100 ? 0.3141 0.2587 0.2461 0.0641  0.0750  0.1157  100 VAL   B N   
5876 C CA  A VAL   B 100 ? 0.3396 0.2806 0.2946 0.0534  0.0574  0.1201  100 VAL   B CA  
5877 C CA  B VAL   B 100 ? 0.3361 0.2779 0.2994 0.0502  0.0665  0.1327  100 VAL   B CA  
5878 C C   A VAL   B 100 ? 0.3577 0.2868 0.2912 0.0564  0.0554  0.1352  100 VAL   B C   
5879 C C   B VAL   B 100 ? 0.3559 0.2837 0.2865 0.0536  0.0632  0.1456  100 VAL   B C   
5880 O O   A VAL   B 100 ? 0.3636 0.2961 0.2990 0.0536  0.0579  0.1271  100 VAL   B O   
5881 O O   B VAL   B 100 ? 0.3628 0.2944 0.2884 0.0488  0.0683  0.1377  100 VAL   B O   
5882 C CB  A VAL   B 100 ? 0.3482 0.2951 0.3497 0.0362  0.0466  0.1187  100 VAL   B CB  
5883 C CB  B VAL   B 100 ? 0.3447 0.2938 0.3648 0.0288  0.0579  0.1389  100 VAL   B CB  
5884 C CG1 A VAL   B 100 ? 0.3519 0.2996 0.3700 0.0325  0.0421  0.1185  100 VAL   B CG1 
5885 C CG1 B VAL   B 100 ? 0.3490 0.2987 0.3906 0.0253  0.0522  0.1408  100 VAL   B CG1 
5886 C CG2 A VAL   B 100 ? 0.3510 0.3012 0.3640 0.0278  0.0447  0.1212  100 VAL   B CG2 
5887 C CG2 B VAL   B 100 ? 0.3470 0.3001 0.3782 0.0170  0.0587  0.1469  100 VAL   B CG2 
5906 N N   . ASN   B 101 ? 0.3714 0.2909 0.2913 0.0623  0.0475  0.1440  101 ASN   B N   
5907 C CA  . ASN   B 101 ? 0.4103 0.3105 0.2970 0.0642  0.0138  0.1503  101 ASN   B CA  
5908 C C   . ASN   B 101 ? 0.4624 0.3627 0.3145 0.0563  -0.0064 0.1465  101 ASN   B C   
5909 O O   . ASN   B 101 ? 0.4677 0.3732 0.3246 0.0612  -0.0048 0.1252  101 ASN   B O   
5910 C CB  . ASN   B 101 ? 0.4024 0.2906 0.3097 0.0604  0.0108  0.1314  101 ASN   B CB  
5911 C CG  . ASN   B 101 ? 0.3946 0.2676 0.3150 0.0570  0.0157  0.1237  101 ASN   B CG  
5912 O OD1 . ASN   B 101 ? 0.3961 0.2666 0.3363 0.0458  0.0325  0.1141  101 ASN   B OD1 
5913 N ND2 . ASN   B 101 ? 0.3891 0.2668 0.3134 0.0580  0.0149  0.0997  101 ASN   B ND2 
5921 N N   A LYS   B 102 ? 0.4836 0.3897 0.3460 0.0453  -0.0053 0.1300  102 LYS   B N   
5922 N N   B LYS   B 102 ? 0.4868 0.3893 0.3416 0.0470  -0.0082 0.1364  102 LYS   B N   
5923 C CA  A LYS   B 102 ? 0.5027 0.4196 0.3739 0.0325  -0.0020 0.1065  102 LYS   B CA  
5924 C CA  B LYS   B 102 ? 0.5089 0.4212 0.3670 0.0346  -0.0083 0.1139  102 LYS   B CA  
5925 C C   A LYS   B 102 ? 0.5024 0.4211 0.3489 0.0335  0.0011  0.1174  102 LYS   B C   
5926 C C   B LYS   B 102 ? 0.5061 0.4218 0.3391 0.0353  -0.0044 0.1245  102 LYS   B C   
5927 O O   A LYS   B 102 ? 0.5075 0.4234 0.3481 0.0345  -0.0078 0.1186  102 LYS   B O   
5928 O O   B LYS   B 102 ? 0.5118 0.4240 0.3336 0.0377  -0.0176 0.1288  102 LYS   B O   
5929 C CB  A LYS   B 102 ? 0.5189 0.4453 0.4324 0.0203  0.0039  0.0701  102 LYS   B CB  
5930 C CB  B LYS   B 102 ? 0.5302 0.4504 0.4291 0.0226  -0.0046 0.0760  102 LYS   B CB  
5931 C CG  A LYS   B 102 ? 0.5321 0.4673 0.4858 0.0106  0.0103  0.0376  102 LYS   B CG  
5932 C CG  B LYS   B 102 ? 0.5480 0.4758 0.4886 0.0129  -0.0001 0.0420  102 LYS   B CG  
5933 C CD  A LYS   B 102 ? 0.5433 0.4848 0.5360 0.0034  0.0162  0.0126  102 LYS   B CD  
5934 C CD  B LYS   B 102 ? 0.5633 0.4966 0.5482 0.0059  0.0049  0.0162  102 LYS   B CD  
5935 C CE  A LYS   B 102 ? 0.5511 0.4967 0.5710 -0.0018 0.0201  -0.0062 102 LYS   B CE  
5936 C CE  B LYS   B 102 ? 0.5743 0.5111 0.5907 0.0009  0.0078  -0.0038 102 LYS   B CE  
5937 N NZ  A LYS   B 102 ? 0.5556 0.5032 0.5914 -0.0040 0.0214  -0.0171 102 LYS   B NZ  
5938 N NZ  B LYS   B 102 ? 0.5808 0.5192 0.6168 -0.0012 0.0083  -0.0162 102 LYS   B NZ  
5965 N N   . GLY   B 103 ? 0.4943 0.4179 0.3366 0.0340  0.0155  0.1212  103 GLY   B N   
5966 C CA  . GLY   B 103 ? 0.4726 0.4106 0.3440 0.0353  0.0468  0.1050  103 GLY   B CA  
5967 C C   . GLY   B 103 ? 0.4473 0.3998 0.3370 0.0349  0.0775  0.0874  103 GLY   B C   
5968 O O   . GLY   B 103 ? 0.4505 0.4063 0.3388 0.0342  0.0879  0.0889  103 GLY   B O   
5973 N N   A GLU   B 104 ? 0.4331 0.3917 0.3360 0.0357  0.0800  0.0717  104 GLU   B N   
5974 N N   B GLU   B 104 ? 0.4294 0.3871 0.3240 0.0362  0.0906  0.0762  104 GLU   B N   
5975 C CA  A GLU   B 104 ? 0.4179 0.3838 0.3271 0.0384  0.0761  0.0518  104 GLU   B CA  
5976 C CA  B GLU   B 104 ? 0.4101 0.3753 0.3044 0.0407  0.0936  0.0607  104 GLU   B CA  
5977 C C   A GLU   B 104 ? 0.4179 0.3840 0.3423 0.0277  0.0974  0.0510  104 GLU   B C   
5978 C C   B GLU   B 104 ? 0.4106 0.3758 0.3202 0.0265  0.1265  0.0682  104 GLU   B C   
5979 O O   A GLU   B 104 ? 0.4190 0.3873 0.3520 0.0263  0.0985  0.0509  104 GLU   B O   
5980 O O   B GLU   B 104 ? 0.4128 0.3799 0.3386 0.0247  0.1268  0.0663  104 GLU   B O   
5981 C CB  A GLU   B 104 ? 0.4053 0.3751 0.3146 0.0518  0.0476  0.0252  104 GLU   B CB  
5982 C CB  B GLU   B 104 ? 0.3941 0.3616 0.2887 0.0604  0.0562  0.0269  104 GLU   B CB  
5983 C CG  A GLU   B 104 ? 0.3942 0.3682 0.3008 0.0653  0.0169  -0.0027 104 GLU   B CG  
5984 C CG  B GLU   B 104 ? 0.3791 0.3494 0.2688 0.0815  0.0151  -0.0087 104 GLU   B CG  
5985 C CD  A GLU   B 104 ? 0.3859 0.3628 0.2892 0.0763  -0.0098 -0.0229 104 GLU   B CD  
5986 C CD  B GLU   B 104 ? 0.3675 0.3388 0.2474 0.0992  -0.0179 -0.0332 104 GLU   B CD  
5987 O OE1 A GLU   B 104 ? 0.3798 0.3565 0.2619 0.0815  -0.0102 -0.0304 104 GLU   B OE1 
5988 O OE1 B GLU   B 104 ? 0.3570 0.3270 0.2018 0.1117  -0.0127 -0.0482 104 GLU   B OE1 
5989 O OE2 A GLU   B 104 ? 0.3846 0.3647 0.2901 0.0796  -0.0290 -0.0344 104 GLU   B OE2 
5990 O OE2 B GLU   B 104 ? 0.3658 0.3411 0.2442 0.1009  -0.0457 -0.0444 104 GLU   B OE2 
6003 N N   A ASP   B 105 ? 0.4146 0.3803 0.3415 0.0193  0.1138  0.0490  105 ASP   B N   
6004 N N   B ASP   B 105 ? 0.4054 0.3708 0.3059 0.0153  0.1539  0.0737  105 ASP   B N   
6005 C CA  A ASP   B 105 ? 0.4132 0.3774 0.3600 0.0126  0.1230  0.0365  105 ASP   B CA  
6006 C CA  B ASP   B 105 ? 0.4026 0.3669 0.3236 0.0073  0.1701  0.0606  105 ASP   B CA  
6007 C C   A ASP   B 105 ? 0.4017 0.3583 0.3255 0.0057  0.1291  0.0297  105 ASP   B C   
6008 C C   B ASP   B 105 ? 0.3836 0.3403 0.2774 -0.0033 0.1806  0.0532  105 ASP   B C   
6009 O O   A ASP   B 105 ? 0.3989 0.3560 0.3112 0.0081  0.1370  0.0325  105 ASP   B O   
6010 O O   B ASP   B 105 ? 0.3650 0.3332 0.2664 -0.0035 0.1738  0.0532  105 ASP   B O   
6011 C CB  A ASP   B 105 ? 0.4218 0.3913 0.4186 0.0146  0.1229  0.0282  105 ASP   B CB  
6012 C CB  B ASP   B 105 ? 0.4179 0.3867 0.3998 0.0123  0.1620  0.0484  105 ASP   B CB  
6013 C CG  A ASP   B 105 ? 0.4290 0.4031 0.4740 0.0143  0.1279  0.0224  105 ASP   B CG  
6014 C CG  B ASP   B 105 ? 0.4299 0.4029 0.4662 0.0128  0.1639  0.0427  105 ASP   B CG  
6015 O OD1 A ASP   B 105 ? 0.4296 0.4057 0.4847 0.0109  0.1347  0.0246  105 ASP   B OD1 
6016 O OD1 B ASP   B 105 ? 0.4316 0.4075 0.4805 0.0085  0.1692  0.0466  105 ASP   B OD1 
6017 O OD2 A ASP   B 105 ? 0.4321 0.4084 0.5011 0.0169  0.1257  0.0172  105 ASP   B OD2 
6018 O OD2 B ASP   B 105 ? 0.4341 0.4097 0.4937 0.0151  0.1642  0.0377  105 ASP   B OD2 
6027 N N   A ILE   B 106 ? 0.3912 0.3396 0.3244 -0.0022 0.1221  0.0244  106 ILE   B N   
6028 N N   B ILE   B 106 ? 0.3791 0.3191 0.2879 -0.0127 0.1724  0.0466  106 ILE   B N   
6029 C CA  A ILE   B 106 ? 0.3756 0.3196 0.3300 -0.0096 0.1207  0.0179  106 ILE   B CA  
6030 C CA  B ILE   B 106 ? 0.3642 0.2967 0.3061 -0.0236 0.1726  0.0370  106 ILE   B CA  
6031 C C   A ILE   B 106 ? 0.3528 0.3111 0.3247 -0.0064 0.1226  0.0051  106 ILE   B C   
6032 C C   B ILE   B 106 ? 0.3344 0.2881 0.2993 -0.0201 0.1776  0.0180  106 ILE   B C   
6033 O O   A ILE   B 106 ? 0.3489 0.2987 0.3236 -0.0090 0.1262  0.0052  106 ILE   B O   
6034 O O   B ILE   B 106 ? 0.3213 0.2651 0.2866 -0.0289 0.1737  0.0246  106 ILE   B O   
6035 C CB  A ILE   B 106 ? 0.3824 0.3105 0.3406 -0.0184 0.1175  0.0214  106 ILE   B CB  
6036 C CB  B ILE   B 106 ? 0.3791 0.2890 0.3291 -0.0332 0.1604  0.0369  106 ILE   B CB  
6037 C CG1 A ILE   B 106 ? 0.3846 0.3065 0.3373 -0.0172 0.1128  0.0199  106 ILE   B CG1 
6038 C CG1 B ILE   B 106 ? 0.3861 0.2891 0.3321 -0.0267 0.1486  0.0307  106 ILE   B CG1 
6039 C CG2 A ILE   B 106 ? 0.3852 0.3103 0.3520 -0.0237 0.1181  0.0248  106 ILE   B CG2 
6040 C CG2 B ILE   B 106 ? 0.3843 0.2888 0.3468 -0.0421 0.1581  0.0407  106 ILE   B CG2 
6041 C CD1 A ILE   B 106 ? 0.3855 0.3043 0.3342 -0.0150 0.1092  0.0209  106 ILE   B CD1 
6042 C CD1 B ILE   B 106 ? 0.3895 0.2889 0.3340 -0.0204 0.1402  0.0307  106 ILE   B CD1 
6065 N N   A GLN   B 107 ? 0.3344 0.3147 0.3310 -0.0053 0.1175  0.0001  107 GLN   B N   
6066 N N   B GLN   B 107 ? 0.3187 0.3001 0.3146 -0.0155 0.1682  0.0061  107 GLN   B N   
6067 C CA  A GLN   B 107 ? 0.3168 0.3171 0.3397 -0.0033 0.1068  0.0009  107 GLN   B CA  
6068 C CA  B GLN   B 107 ? 0.3029 0.3116 0.3294 -0.0125 0.1493  0.0046  107 GLN   B CA  
6069 C C   A GLN   B 107 ? 0.2812 0.2901 0.3086 0.0052  0.0999  0.0043  107 GLN   B C   
6070 C C   B GLN   B 107 ? 0.2714 0.2878 0.3027 -0.0015 0.1262  0.0060  107 GLN   B C   
6071 O O   A GLN   B 107 ? 0.2761 0.2899 0.3240 0.0101  0.0817  -0.0128 107 GLN   B O   
6072 O O   B GLN   B 107 ? 0.2645 0.2891 0.3289 0.0064  0.1047  -0.0178 107 GLN   B O   
6073 C CB  A GLN   B 107 ? 0.3404 0.3471 0.3953 -0.0042 0.0887  -0.0012 107 GLN   B CB  
6074 C CB  B GLN   B 107 ? 0.3324 0.3493 0.3943 -0.0106 0.1219  -0.0001 107 GLN   B CB  
6075 C CG  A GLN   B 107 ? 0.3627 0.3733 0.4483 -0.0033 0.0672  -0.0020 107 GLN   B CG  
6076 C CG  B GLN   B 107 ? 0.3623 0.3825 0.4568 -0.0061 0.0877  -0.0040 107 GLN   B CG  
6077 C CD  A GLN   B 107 ? 0.3788 0.3937 0.4922 -0.0042 0.0531  -0.0004 107 GLN   B CD  
6078 C CD  B GLN   B 107 ? 0.3846 0.4085 0.5075 -0.0050 0.0656  -0.0043 107 GLN   B CD  
6079 O OE1 A GLN   B 107 ? 0.3843 0.4013 0.5091 -0.0050 0.0516  -0.0000 107 GLN   B OE1 
6080 O OE1 B GLN   B 107 ? 0.3933 0.4182 0.5269 -0.0060 0.0633  -0.0036 107 GLN   B OE1 
6081 N NE2 A GLN   B 107 ? 0.3855 0.4007 0.5075 -0.0035 0.0478  0.0008  107 GLN   B NE2 
6082 N NE2 B GLN   B 107 ? 0.3931 0.4177 0.5244 -0.0034 0.0572  -0.0041 107 GLN   B NE2 
6099 N N   . LEU   B 108 ? 0.2500 0.2613 0.2781 0.0180  0.1048  0.0176  108 LEU   B N   
6100 C CA  . LEU   B 108 ? 0.2246 0.2311 0.2276 0.0356  0.0818  0.0368  108 LEU   B CA  
6101 C C   . LEU   B 108 ? 0.1890 0.1856 0.2257 0.0364  0.0574  0.0398  108 LEU   B C   
6102 O O   . LEU   B 108 ? 0.1852 0.1727 0.2045 0.0316  0.0371  0.0304  108 LEU   B O   
6103 C CB  . LEU   B 108 ? 0.2421 0.2586 0.1987 0.0377  0.0873  0.0398  108 LEU   B CB  
6104 C CG  . LEU   B 108 ? 0.2609 0.2946 0.2197 0.0344  0.0704  0.0208  108 LEU   B CG  
6105 C CD1 . LEU   B 108 ? 0.2720 0.3098 0.2080 0.0287  0.0661  0.0238  108 LEU   B CD1 
6106 C CD2 . LEU   B 108 ? 0.2712 0.3070 0.2329 0.0392  0.0555  0.0056  108 LEU   B CD2 
6119 N N   . LEU   B 109 ? 0.1722 0.1603 0.2230 0.0262  0.0504  0.0393  109 LEU   B N   
6120 C CA  . LEU   B 109 ? 0.1539 0.1384 0.2283 0.0189  0.0425  0.0373  109 LEU   B CA  
6121 C C   . LEU   B 109 ? 0.1431 0.1213 0.2208 0.0059  0.0398  0.0259  109 LEU   B C   
6122 O O   . LEU   B 109 ? 0.1361 0.1244 0.2131 0.0077  0.0396  0.0403  109 LEU   B O   
6123 C CB  . LEU   B 109 ? 0.1613 0.1326 0.2328 0.0122  0.0322  0.0334  109 LEU   B CB  
6124 C CG  . LEU   B 109 ? 0.1607 0.1282 0.2273 0.0078  0.0265  0.0202  109 LEU   B CG  
6125 C CD1 . LEU   B 109 ? 0.1537 0.1333 0.2157 0.0011  0.0343  0.0232  109 LEU   B CD1 
6126 C CD2 . LEU   B 109 ? 0.1769 0.1412 0.2368 0.0104  0.0252  0.0174  109 LEU   B CD2 
6138 N N   . LYS   B 110 ? 0.1379 0.1236 0.2030 0.0011  0.0407  0.0207  110 LYS   B N   
6139 C CA  . LYS   B 110 ? 0.1385 0.1188 0.2038 0.0006  0.0369  0.0166  110 LYS   B CA  
6140 C C   . LYS   B 110 ? 0.1303 0.1226 0.2046 0.0002  0.0319  0.0169  110 LYS   B C   
6141 O O   . LYS   B 110 ? 0.1285 0.1237 0.1979 -0.0072 0.0280  0.0092  110 LYS   B O   
6142 C CB  . LYS   B 110 ? 0.1406 0.1220 0.2162 -0.0018 0.0367  0.0158  110 LYS   B CB  
6143 C CG  . LYS   B 110 ? 0.1388 0.1302 0.2249 -0.0066 0.0242  0.0252  110 LYS   B CG  
6144 C CD  . LYS   B 110 ? 0.1427 0.1274 0.2412 -0.0046 0.0228  0.0180  110 LYS   B CD  
6145 C CE  . LYS   B 110 ? 0.1400 0.1386 0.2697 0.0001  0.0149  0.0093  110 LYS   B CE  
6146 N NZ  . LYS   B 110 ? 0.1367 0.1502 0.2587 0.0012  0.0089  0.0074  110 LYS   B NZ  
6160 N N   . SER   B 111 ? 0.1378 0.1237 0.2051 0.0020  0.0261  0.0169  111 SER   B N   
6161 C CA  . SER   B 111 ? 0.1458 0.1279 0.1882 0.0032  0.0241  0.0184  111 SER   B CA  
6162 C C   . SER   B 111 ? 0.1360 0.1251 0.1682 -0.0035 0.0124  0.0101  111 SER   B C   
6163 O O   . SER   B 111 ? 0.1367 0.1258 0.1808 -0.0040 0.0104  0.0103  111 SER   B O   
6164 C CB  . SER   B 111 ? 0.1624 0.1475 0.1904 0.0071  0.0356  0.0215  111 SER   B CB  
6165 O OG  . SER   B 111 ? 0.1784 0.1724 0.2048 0.0099  0.0459  0.0259  111 SER   B OG  
6171 N N   . ALA   B 112 ? 0.1324 0.1306 0.1783 0.0042  0.0255  0.0216  112 ALA   B N   
6172 C CA  . ALA   B 112 ? 0.1305 0.1342 0.1718 0.0026  0.0138  0.0082  112 ALA   B CA  
6173 C C   . ALA   B 112 ? 0.1254 0.1258 0.1743 0.0028  0.0135  0.0086  112 ALA   B C   
6174 O O   . ALA   B 112 ? 0.1237 0.1217 0.1820 -0.0001 0.0176  0.0099  112 ALA   B O   
6175 C CB  . ALA   B 112 ? 0.1334 0.1376 0.1666 0.0080  0.0084  0.0207  112 ALA   B CB  
6181 N N   . TYR   B 113 ? 0.1204 0.1141 0.1777 0.0001  0.0152  0.0174  113 TYR   B N   
6182 C CA  . TYR   B 113 ? 0.1203 0.1140 0.1780 -0.0007 0.0196  0.0051  113 TYR   B CA  
6183 C C   . TYR   B 113 ? 0.1163 0.1072 0.1640 -0.0079 0.0132  0.0046  113 TYR   B C   
6184 O O   . TYR   B 113 ? 0.1217 0.1115 0.1634 -0.0061 0.0076  -0.0007 113 TYR   B O   
6185 C CB  . TYR   B 113 ? 0.1262 0.1060 0.1790 -0.0016 0.0194  0.0100  113 TYR   B CB  
6186 C CG  . TYR   B 113 ? 0.1258 0.1099 0.1969 -0.0050 0.0130  0.0154  113 TYR   B CG  
6187 C CD1 . TYR   B 113 ? 0.1339 0.1085 0.2003 -0.0058 0.0194  0.0219  113 TYR   B CD1 
6188 C CD2 . TYR   B 113 ? 0.1358 0.1134 0.2003 -0.0064 0.0136  0.0137  113 TYR   B CD2 
6189 C CE1 . TYR   B 113 ? 0.1317 0.1149 0.1998 -0.0015 0.0270  0.0120  113 TYR   B CE1 
6190 C CE2 . TYR   B 113 ? 0.1333 0.1096 0.2069 0.0005  0.0216  0.0186  113 TYR   B CE2 
6191 C CZ  . TYR   B 113 ? 0.1328 0.1106 0.2152 0.0047  0.0224  0.0083  113 TYR   B CZ  
6192 O OH  . TYR   B 113 ? 0.1411 0.1121 0.2393 0.0059  0.0260  0.0061  113 TYR   B OH  
6202 N N   . GLU   B 114 ? 0.1134 0.1050 0.1770 -0.0049 0.0119  0.0082  114 GLU   B N   
6203 C CA  . GLU   B 114 ? 0.1170 0.1041 0.1716 -0.0023 0.0065  0.0081  114 GLU   B CA  
6204 C C   . GLU   B 114 ? 0.1177 0.1051 0.1593 -0.0010 0.0101  0.0058  114 GLU   B C   
6205 O O   . GLU   B 114 ? 0.1154 0.1069 0.1734 -0.0005 0.0012  0.0097  114 GLU   B O   
6206 C CB  . GLU   B 114 ? 0.1157 0.1079 0.1810 -0.0014 0.0196  0.0067  114 GLU   B CB  
6207 C CG  . GLU   B 114 ? 0.1222 0.1103 0.1943 0.0014  0.0126  0.0064  114 GLU   B CG  
6208 C CD  . GLU   B 114 ? 0.1118 0.1170 0.1979 -0.0064 0.0121  0.0119  114 GLU   B CD  
6209 O OE1 . GLU   B 114 ? 0.1183 0.1282 0.1929 -0.0054 0.0182  0.0091  114 GLU   B OE1 
6210 O OE2 . GLU   B 114 ? 0.1180 0.1391 0.2114 -0.0144 0.0167  0.0144  114 GLU   B OE2 
6217 N N   . ASN   B 115 ? 0.1156 0.1079 0.1599 -0.0054 0.0035  0.0088  115 ASN   B N   
6218 C CA  . ASN   B 115 ? 0.1179 0.1125 0.1549 -0.0039 0.0077  0.0049  115 ASN   B CA  
6219 C C   . ASN   B 115 ? 0.1163 0.1050 0.1619 -0.0064 -0.0039 0.0061  115 ASN   B C   
6220 O O   . ASN   B 115 ? 0.1266 0.1091 0.1571 -0.0101 0.0032  0.0040  115 ASN   B O   
6221 C CB  . ASN   B 115 ? 0.1261 0.1228 0.1618 -0.0040 0.0095  0.0024  115 ASN   B CB  
6222 C CG  . ASN   B 115 ? 0.1366 0.1271 0.1558 0.0052  0.0029  0.0019  115 ASN   B CG  
6223 O OD1 . ASN   B 115 ? 0.1739 0.1401 0.1784 0.0043  0.0122  -0.0040 115 ASN   B OD1 
6224 N ND2 . ASN   B 115 ? 0.1367 0.1395 0.1549 0.0006  0.0040  0.0148  115 ASN   B ND2 
6231 N N   . PHE   B 116 ? 0.1230 0.1032 0.1500 -0.0059 0.0008  0.0043  116 PHE   B N   
6232 C CA  . PHE   B 116 ? 0.1185 0.1085 0.1480 -0.0090 -0.0017 0.0046  116 PHE   B CA  
6233 C C   . PHE   B 116 ? 0.1243 0.1031 0.1511 -0.0084 -0.0017 0.0055  116 PHE   B C   
6234 O O   . PHE   B 116 ? 0.1283 0.1141 0.1591 -0.0069 -0.0001 0.0072  116 PHE   B O   
6235 C CB  . PHE   B 116 ? 0.1168 0.1095 0.1539 -0.0000 0.0016  0.0003  116 PHE   B CB  
6236 C CG  . PHE   B 116 ? 0.1119 0.1107 0.1550 -0.0101 0.0001  0.0061  116 PHE   B CG  
6237 C CD1 . PHE   B 116 ? 0.1230 0.1138 0.1735 -0.0082 -0.0003 0.0059  116 PHE   B CD1 
6238 C CD2 . PHE   B 116 ? 0.1206 0.1215 0.1391 -0.0054 0.0015  0.0000  116 PHE   B CD2 
6239 C CE1 . PHE   B 116 ? 0.1273 0.1169 0.1759 -0.0075 -0.0071 0.0138  116 PHE   B CE1 
6240 C CE2 . PHE   B 116 ? 0.1178 0.1157 0.1562 -0.0007 0.0068  0.0022  116 PHE   B CE2 
6241 C CZ  . PHE   B 116 ? 0.1137 0.1154 0.1618 -0.0029 -0.0015 0.0145  116 PHE   B CZ  
6251 N N   . ASN   B 117 ? 0.1255 0.1050 0.1620 -0.0029 -0.0069 0.0103  117 ASN   B N   
6252 C CA  . ASN   B 117 ? 0.1340 0.1090 0.1622 0.0017  -0.0082 0.0023  117 ASN   B CA  
6253 C C   . ASN   B 117 ? 0.1286 0.1116 0.1761 -0.0026 -0.0127 0.0116  117 ASN   B C   
6254 O O   . ASN   B 117 ? 0.1360 0.1175 0.2023 -0.0053 -0.0297 0.0158  117 ASN   B O   
6255 C CB  . ASN   B 117 ? 0.1291 0.1114 0.1623 -0.0014 -0.0103 -0.0014 117 ASN   B CB  
6256 C CG  . ASN   B 117 ? 0.1234 0.1191 0.1731 0.0013  0.0040  -0.0003 117 ASN   B CG  
6257 O OD1 . ASN   B 117 ? 0.1409 0.1210 0.1819 -0.0139 0.0004  -0.0018 117 ASN   B OD1 
6258 N ND2 . ASN   B 117 ? 0.1262 0.1210 0.1756 -0.0044 0.0080  -0.0054 117 ASN   B ND2 
6265 N N   . GLN   B 118 ? 0.1353 0.1008 0.1585 -0.0049 -0.0143 0.0061  118 GLN   B N   
6266 C CA  . GLN   B 118 ? 0.1349 0.1079 0.1727 -0.0024 -0.0155 0.0003  118 GLN   B CA  
6267 C C   . GLN   B 118 ? 0.1337 0.1051 0.1740 -0.0032 -0.0012 0.0031  118 GLN   B C   
6268 O O   . GLN   B 118 ? 0.1502 0.1126 0.2071 -0.0054 0.0027  0.0084  118 GLN   B O   
6269 C CB  . GLN   B 118 ? 0.1412 0.1151 0.1811 0.0019  -0.0140 0.0008  118 GLN   B CB  
6270 C CG  . GLN   B 118 ? 0.1516 0.1163 0.1695 0.0070  -0.0166 -0.0088 118 GLN   B CG  
6271 C CD  . GLN   B 118 ? 0.1539 0.1115 0.1701 0.0027  -0.0086 -0.0043 118 GLN   B CD  
6272 O OE1 . GLN   B 118 ? 0.1604 0.1123 0.2033 0.0041  0.0056  0.0090  118 GLN   B OE1 
6273 N NE2 . GLN   B 118 ? 0.1558 0.1160 0.1854 -0.0014 -0.0179 0.0043  118 GLN   B NE2 
6282 N N   . HIS   B 119 ? 0.1375 0.1143 0.1533 -0.0150 -0.0077 0.0180  119 HIS   B N   
6283 C CA  . HIS   B 119 ? 0.1475 0.1272 0.1478 -0.0093 -0.0157 0.0151  119 HIS   B CA  
6284 C C   . HIS   B 119 ? 0.1479 0.1259 0.1479 -0.0071 -0.0278 0.0138  119 HIS   B C   
6285 O O   . HIS   B 119 ? 0.1551 0.1314 0.1582 -0.0251 -0.0151 0.0082  119 HIS   B O   
6286 C CB  . HIS   B 119 ? 0.1516 0.1424 0.1437 0.0004  -0.0214 0.0054  119 HIS   B CB  
6287 C CG  . HIS   B 119 ? 0.1547 0.1627 0.1707 0.0096  -0.0365 -0.0089 119 HIS   B CG  
6288 N ND1 . HIS   B 119 ? 0.1599 0.1767 0.2203 0.0041  -0.0463 -0.0363 119 HIS   B ND1 
6289 C CD2 . HIS   B 119 ? 0.1786 0.1845 0.1642 0.0379  -0.0436 -0.0127 119 HIS   B CD2 
6290 C CE1 . HIS   B 119 ? 0.1786 0.1912 0.2159 0.0230  -0.0584 -0.0453 119 HIS   B CE1 
6291 N NE2 . HIS   B 119 ? 0.1915 0.2014 0.1902 0.0369  -0.0483 -0.0328 119 HIS   B NE2 
6299 N N   A GLU   B 120 ? 0.1675 0.1366 0.1587 -0.0149 -0.0307 0.0117  120 GLU   B N   
6300 N N   B GLU   B 120 ? 0.1653 0.1245 0.1518 -0.0158 -0.0366 0.0145  120 GLU   B N   
6301 C CA  A GLU   B 120 ? 0.1936 0.1521 0.1792 -0.0121 -0.0382 0.0187  120 GLU   B CA  
6302 C CA  B GLU   B 120 ? 0.1915 0.1313 0.1638 -0.0084 -0.0531 0.0322  120 GLU   B CA  
6303 C C   A GLU   B 120 ? 0.1753 0.1381 0.1554 -0.0187 -0.0302 0.0173  120 GLU   B C   
6304 C C   B GLU   B 120 ? 0.1718 0.1237 0.1465 -0.0155 -0.0401 0.0291  120 GLU   B C   
6305 O O   A GLU   B 120 ? 0.1682 0.1473 0.1566 -0.0209 -0.0251 0.0063  120 GLU   B O   
6306 O O   B GLU   B 120 ? 0.1619 0.1379 0.1550 -0.0158 -0.0385 0.0160  120 GLU   B O   
6307 C CB  A GLU   B 120 ? 0.2400 0.1825 0.2466 -0.0029 -0.0510 0.0299  120 GLU   B CB  
6308 C CB  B GLU   B 120 ? 0.2410 0.1501 0.2265 0.0022  -0.0731 0.0543  120 GLU   B CB  
6309 C CG  A GLU   B 120 ? 0.2776 0.2219 0.3310 0.0034  -0.0577 0.0401  120 GLU   B CG  
6310 C CG  B GLU   B 120 ? 0.2765 0.1923 0.3119 0.0112  -0.0885 0.0686  120 GLU   B CG  
6311 C CD  A GLU   B 120 ? 0.3055 0.2580 0.4098 0.0044  -0.0609 0.0541  120 GLU   B CD  
6312 C CD  B GLU   B 120 ? 0.3024 0.2344 0.4040 0.0084  -0.0885 0.0839  120 GLU   B CD  
6313 O OE1 A GLU   B 120 ? 0.3186 0.2728 0.4379 0.0056  -0.0577 0.0643  120 GLU   B OE1 
6314 O OE1 B GLU   B 120 ? 0.3163 0.2568 0.4386 0.0052  -0.0751 0.0903  120 GLU   B OE1 
6315 O OE2 A GLU   B 120 ? 0.3184 0.2761 0.4466 0.0038  -0.0618 0.0517  120 GLU   B OE2 
6316 O OE2 B GLU   B 120 ? 0.3160 0.2567 0.4498 0.0018  -0.0899 0.0799  120 GLU   B OE2 
6329 N N   . VAL   B 121 ? 0.1655 0.1294 0.1475 -0.0225 -0.0258 0.0184  121 VAL   B N   
6330 C CA  . VAL   B 121 ? 0.1566 0.1402 0.1318 -0.0213 -0.0188 0.0157  121 VAL   B CA  
6331 C C   . VAL   B 121 ? 0.1502 0.1365 0.1355 -0.0267 -0.0146 0.0082  121 VAL   B C   
6332 O O   . VAL   B 121 ? 0.1620 0.1353 0.1498 -0.0340 -0.0254 0.0137  121 VAL   B O   
6333 C CB  . VAL   B 121 ? 0.1790 0.1797 0.1498 -0.0099 -0.0205 0.0214  121 VAL   B CB  
6334 C CG1 . VAL   B 121 ? 0.1822 0.1903 0.1806 -0.0178 -0.0106 0.0239  121 VAL   B CG1 
6335 C CG2 . VAL   B 121 ? 0.2005 0.2033 0.1609 -0.0032 -0.0139 0.0123  121 VAL   B CG2 
6346 N N   . LEU   B 122 ? 0.1378 0.1267 0.1375 -0.0132 -0.0161 0.0084  122 LEU   B N   
6347 C CA  . LEU   B 122 ? 0.1353 0.1332 0.1223 -0.0153 -0.0130 0.0082  122 LEU   B CA  
6348 C C   . LEU   B 122 ? 0.1328 0.1227 0.1292 -0.0266 -0.0099 0.0103  122 LEU   B C   
6349 O O   . LEU   B 122 ? 0.1457 0.1241 0.1604 -0.0334 -0.0219 0.0028  122 LEU   B O   
6350 C CB  . LEU   B 122 ? 0.1530 0.1457 0.1606 -0.0034 -0.0148 0.0089  122 LEU   B CB  
6351 C CG  . LEU   B 122 ? 0.1444 0.1489 0.1579 -0.0131 -0.0023 0.0124  122 LEU   B CG  
6352 C CD1 . LEU   B 122 ? 0.1532 0.1725 0.1530 -0.0227 -0.0025 0.0038  122 LEU   B CD1 
6353 C CD2 . LEU   B 122 ? 0.1408 0.1571 0.1443 -0.0076 -0.0138 0.0023  122 LEU   B CD2 
6365 N N   . LEU   B 123 ? 0.1353 0.1150 0.1196 -0.0242 -0.0170 0.0072  123 LEU   B N   
6366 C CA  . LEU   B 123 ? 0.1400 0.1154 0.1247 -0.0249 -0.0107 -0.0000 123 LEU   B CA  
6367 C C   . LEU   B 123 ? 0.1353 0.1131 0.1244 -0.0242 -0.0058 0.0047  123 LEU   B C   
6368 O O   . LEU   B 123 ? 0.1446 0.1164 0.1300 -0.0315 -0.0087 0.0020  123 LEU   B O   
6369 C CB  . LEU   B 123 ? 0.1425 0.1214 0.1394 -0.0294 -0.0069 -0.0045 123 LEU   B CB  
6370 C CG  . LEU   B 123 ? 0.1444 0.1268 0.1449 -0.0192 -0.0037 0.0115  123 LEU   B CG  
6371 C CD1 . LEU   B 123 ? 0.1491 0.1282 0.1559 -0.0205 -0.0015 -0.0019 123 LEU   B CD1 
6372 C CD2 . LEU   B 123 ? 0.1576 0.1357 0.1646 -0.0118 -0.0005 0.0164  123 LEU   B CD2 
6384 N N   . ALA   B 124 ? 0.1304 0.1125 0.1216 -0.0193 -0.0037 0.0034  124 ALA   B N   
6385 C CA  . ALA   B 124 ? 0.1239 0.1161 0.1346 -0.0143 -0.0082 -0.0030 124 ALA   B CA  
6386 C C   . ALA   B 124 ? 0.1201 0.1127 0.1255 -0.0152 -0.0036 -0.0005 124 ALA   B C   
6387 O O   . ALA   B 124 ? 0.1332 0.1181 0.1475 -0.0143 -0.0021 0.0009  124 ALA   B O   
6388 C CB  . ALA   B 124 ? 0.1320 0.1175 0.1465 -0.0110 0.0049  -0.0005 124 ALA   B CB  
6394 N N   . PRO   B 125 ? 0.1298 0.1153 0.1383 -0.0153 -0.0090 0.0085  125 PRO   B N   
6395 C CA  . PRO   B 125 ? 0.1349 0.1117 0.1485 -0.0168 -0.0103 0.0133  125 PRO   B CA  
6396 C C   . PRO   B 125 ? 0.1383 0.1061 0.1554 -0.0111 0.0057  0.0082  125 PRO   B C   
6397 O O   . PRO   B 125 ? 0.1357 0.1103 0.1757 -0.0089 0.0068  0.0166  125 PRO   B O   
6398 C CB  . PRO   B 125 ? 0.1386 0.1383 0.1649 -0.0208 -0.0173 0.0314  125 PRO   B CB  
6399 C CG  . PRO   B 125 ? 0.1496 0.1433 0.1518 -0.0232 -0.0188 0.0159  125 PRO   B CG  
6400 C CD  . PRO   B 125 ? 0.1454 0.1248 0.1420 -0.0230 -0.0121 0.0079  125 PRO   B CD  
6408 N N   . LEU   B 126 ? 0.1461 0.1068 0.1751 -0.0096 0.0202  0.0186  126 LEU   B N   
6409 C CA  . LEU   B 126 ? 0.1494 0.1136 0.1795 -0.0071 0.0323  0.0128  126 LEU   B CA  
6410 C C   . LEU   B 126 ? 0.1458 0.1253 0.1936 0.0027  0.0269  0.0165  126 LEU   B C   
6411 O O   . LEU   B 126 ? 0.1689 0.1592 0.2170 0.0190  -0.0016 -0.0022 126 LEU   B O   
6412 C CB  . LEU   B 126 ? 0.1672 0.1223 0.2097 -0.0174 0.0363  0.0114  126 LEU   B CB  
6413 C CG  . LEU   B 126 ? 0.1841 0.1348 0.2250 -0.0288 0.0292  -0.0035 126 LEU   B CG  
6414 C CD1 . LEU   B 126 ? 0.1953 0.1345 0.2771 -0.0267 0.0262  -0.0208 126 LEU   B CD1 
6415 C CD2 . LEU   B 126 ? 0.1832 0.1531 0.2337 -0.0376 0.0231  -0.0040 126 LEU   B CD2 
6427 N N   . LEU   B 127 ? 0.1435 0.1177 0.1978 0.0002  0.0346  0.0099  127 LEU   B N   
6428 C CA  . LEU   B 127 ? 0.1448 0.1251 0.2124 -0.0034 0.0298  0.0228  127 LEU   B CA  
6429 C C   . LEU   B 127 ? 0.1371 0.1195 0.2087 0.0001  0.0297  0.0167  127 LEU   B C   
6430 O O   . LEU   B 127 ? 0.1445 0.1213 0.2099 -0.0127 0.0201  0.0185  127 LEU   B O   
6431 C CB  . LEU   B 127 ? 0.1561 0.1180 0.2078 -0.0030 0.0279  0.0225  127 LEU   B CB  
6432 C CG  . LEU   B 127 ? 0.1614 0.1180 0.2187 0.0026  0.0345  0.0115  127 LEU   B CG  
6433 C CD1 . LEU   B 127 ? 0.1658 0.1254 0.2327 0.0066  0.0250  0.0180  127 LEU   B CD1 
6434 C CD2 . LEU   B 127 ? 0.1710 0.1310 0.2300 -0.0028 0.0360  0.0197  127 LEU   B CD2 
6446 N N   . SER   B 128 ? 0.1441 0.1166 0.2024 0.0017  0.0096  0.0194  128 SER   B N   
6447 C CA  . SER   B 128 ? 0.1555 0.1231 0.2077 0.0144  0.0071  0.0264  128 SER   B CA  
6448 C C   . SER   B 128 ? 0.1697 0.1327 0.2342 0.0069  -0.0107 0.0284  128 SER   B C   
6449 O O   . SER   B 128 ? 0.1851 0.1357 0.2825 0.0088  -0.0163 0.0382  128 SER   B O   
6450 C CB  . SER   B 128 ? 0.1625 0.1330 0.1963 0.0109  0.0169  0.0332  128 SER   B CB  
6451 O OG  . SER   B 128 ? 0.1685 0.1522 0.1932 0.0158  0.0169  0.0360  128 SER   B OG  
6457 N N   . ALA   B 129 ? 0.1835 0.1415 0.2508 0.0306  -0.0067 0.0072  129 ALA   B N   
6458 C CA  . ALA   B 129 ? 0.2052 0.1505 0.2603 0.0373  -0.0007 -0.0000 129 ALA   B CA  
6459 C C   . ALA   B 129 ? 0.1876 0.1399 0.2492 0.0278  0.0152  0.0001  129 ALA   B C   
6460 O O   . ALA   B 129 ? 0.1725 0.1448 0.2372 0.0203  0.0059  0.0057  129 ALA   B O   
6461 C CB  . ALA   B 129 ? 0.2260 0.1731 0.2873 0.0420  0.0046  -0.0096 129 ALA   B CB  
6467 N N   . GLY   B 130 ? 0.1858 0.1382 0.2561 0.0313  0.0214  -0.0002 130 GLY   B N   
6468 C CA  . GLY   B 130 ? 0.1879 0.1504 0.2631 0.0292  0.0357  0.0027  130 GLY   B CA  
6469 C C   . GLY   B 130 ? 0.1894 0.1510 0.2573 0.0277  0.0273  0.0118  130 GLY   B C   
6470 O O   . GLY   B 130 ? 0.2007 0.1613 0.2565 0.0230  0.0209  0.0202  130 GLY   B O   
6474 N N   . ILE   B 131 ? 0.1814 0.1657 0.2598 0.0414  0.0194  0.0073  131 ILE   B N   
6475 C CA  . ILE   B 131 ? 0.1991 0.1838 0.2614 0.0359  0.0114  0.0213  131 ILE   B CA  
6476 C C   . ILE   B 131 ? 0.2124 0.1741 0.2253 0.0293  0.0121  0.0329  131 ILE   B C   
6477 O O   . ILE   B 131 ? 0.2361 0.1913 0.2298 0.0329  -0.0050 0.0329  131 ILE   B O   
6478 C CB  . ILE   B 131 ? 0.1981 0.2181 0.2950 0.0255  0.0022  0.0250  131 ILE   B CB  
6479 C CG1 . ILE   B 131 ? 0.2043 0.2389 0.3068 -0.0032 0.0081  0.0376  131 ILE   B CG1 
6480 C CG2 . ILE   B 131 ? 0.2015 0.2320 0.3129 0.0310  0.0106  0.0091  131 ILE   B CG2 
6481 C CD1 . ILE   B 131 ? 0.2150 0.2597 0.3272 -0.0222 0.0119  0.0401  131 ILE   B CD1 
6493 N N   . PHE   B 132 ? 0.2019 0.1561 0.2168 0.0239  0.0342  0.0274  132 PHE   B N   
6494 C CA  . PHE   B 132 ? 0.2128 0.1593 0.2138 0.0133  0.0491  0.0196  132 PHE   B CA  
6495 C C   . PHE   B 132 ? 0.2272 0.1708 0.2380 0.0131  0.0551  0.0221  132 PHE   B C   
6496 O O   . PHE   B 132 ? 0.2398 0.1927 0.2584 0.0100  0.0641  0.0232  132 PHE   B O   
6497 C CB  . PHE   B 132 ? 0.1994 0.1506 0.2024 0.0188  0.0453  0.0221  132 PHE   B CB  
6498 C CG  . PHE   B 132 ? 0.1938 0.1510 0.1894 0.0187  0.0328  0.0252  132 PHE   B CG  
6499 C CD1 . PHE   B 132 ? 0.2000 0.1512 0.2330 0.0118  0.0333  0.0218  132 PHE   B CD1 
6500 C CD2 . PHE   B 132 ? 0.1968 0.1626 0.1571 0.0199  0.0257  0.0211  132 PHE   B CD2 
6501 C CE1 . PHE   B 132 ? 0.2020 0.1531 0.2395 0.0102  0.0251  0.0250  132 PHE   B CE1 
6502 C CE2 . PHE   B 132 ? 0.2046 0.1635 0.1540 0.0156  0.0160  0.0210  132 PHE   B CE2 
6503 C CZ  . PHE   B 132 ? 0.2073 0.1548 0.2095 0.0109  0.0132  0.0326  132 PHE   B CZ  
6513 N N   . GLY   B 133 ? 0.2275 0.1575 0.2486 0.0110  0.0482  0.0339  133 GLY   B N   
6514 C CA  . GLY   B 133 ? 0.2344 0.1623 0.2695 -0.0034 0.0485  0.0504  133 GLY   B CA  
6515 C C   . GLY   B 133 ? 0.2409 0.1750 0.2745 -0.0212 0.0575  0.0539  133 GLY   B C   
6516 O O   . GLY   B 133 ? 0.2600 0.1911 0.3153 -0.0391 0.0537  0.0633  133 GLY   B O   
6520 N N   . ALA   B 134 ? 0.2196 0.1666 0.2594 -0.0195 0.0615  0.0324  134 ALA   B N   
6521 C CA  . ALA   B 134 ? 0.2124 0.1659 0.2599 -0.0139 0.0554  0.0180  134 ALA   B CA  
6522 C C   . ALA   B 134 ? 0.2204 0.1523 0.2438 -0.0057 0.0458  0.0209  134 ALA   B C   
6523 O O   . ALA   B 134 ? 0.2257 0.1761 0.2502 0.0059  0.0375  0.0197  134 ALA   B O   
6524 C CB  . ALA   B 134 ? 0.2119 0.1747 0.2879 -0.0093 0.0348  0.0159  134 ALA   B CB  
6530 N N   . ASP   B 135 ? 0.2305 0.1553 0.2401 -0.0082 0.0269  0.0293  135 ASP   B N   
6531 C CA  . ASP   B 135 ? 0.2478 0.1448 0.2679 -0.0012 0.0122  0.0364  135 ASP   B CA  
6532 C C   . ASP   B 135 ? 0.2293 0.1347 0.2518 0.0069  0.0159  0.0345  135 ASP   B C   
6533 O O   . ASP   B 135 ? 0.2181 0.1417 0.2640 0.0034  0.0193  0.0375  135 ASP   B O   
6534 C CB  . ASP   B 135 ? 0.2784 0.1583 0.2962 -0.0274 0.0119  0.0351  135 ASP   B CB  
6535 C CG  . ASP   B 135 ? 0.3033 0.1632 0.3442 -0.0485 0.0102  0.0237  135 ASP   B CG  
6536 O OD1 . ASP   B 135 ? 0.3103 0.1548 0.3396 -0.0361 0.0079  0.0234  135 ASP   B OD1 
6537 O OD2 . ASP   B 135 ? 0.3194 0.1968 0.4000 -0.0631 0.0068  -0.0044 135 ASP   B OD2 
6542 N N   . PRO   B 136 ? 0.2194 0.1384 0.2630 0.0231  0.0007  0.0293  136 PRO   B N   
6543 C CA  . PRO   B 136 ? 0.2002 0.1370 0.2662 0.0183  0.0009  0.0143  136 PRO   B CA  
6544 C C   . PRO   B 136 ? 0.1835 0.1228 0.2780 0.0114  0.0099  0.0119  136 PRO   B C   
6545 O O   . PRO   B 136 ? 0.1663 0.1219 0.2687 0.0089  0.0054  0.0177  136 PRO   B O   
6546 C CB  . PRO   B 136 ? 0.2021 0.1601 0.2763 0.0313  0.0027  0.0073  136 PRO   B CB  
6547 C CG  . PRO   B 136 ? 0.2205 0.1679 0.3018 0.0349  0.0095  0.0065  136 PRO   B CG  
6548 C CD  . PRO   B 136 ? 0.2271 0.1569 0.2887 0.0352  0.0075  0.0144  136 PRO   B CD  
6556 N N   . ILE   B 137 ? 0.1963 0.1147 0.2720 0.0068  0.0051  0.0082  137 ILE   B N   
6557 C CA  . ILE   B 137 ? 0.1986 0.1162 0.2815 -0.0026 0.0030  0.0060  137 ILE   B CA  
6558 C C   . ILE   B 137 ? 0.1806 0.1254 0.2797 -0.0068 0.0137  0.0118  137 ILE   B C   
6559 O O   . ILE   B 137 ? 0.1683 0.1290 0.2757 -0.0055 0.0182  0.0108  137 ILE   B O   
6560 C CB  . ILE   B 137 ? 0.2285 0.1187 0.3280 -0.0012 0.0037  0.0119  137 ILE   B CB  
6561 C CG1 . ILE   B 137 ? 0.2586 0.1353 0.3746 0.0058  0.0086  -0.0039 137 ILE   B CG1 
6562 C CG2 . ILE   B 137 ? 0.2326 0.1256 0.3380 -0.0273 0.0075  0.0189  137 ILE   B CG2 
6563 C CD1 . ILE   B 137 ? 0.2771 0.1622 0.4084 0.0144  0.0046  0.0016  137 ILE   B CD1 
6575 N N   . HIS   B 138 ? 0.1882 0.1174 0.2714 -0.0066 0.0257  0.0169  138 HIS   B N   
6576 C CA  . HIS   B 138 ? 0.1986 0.1263 0.2669 -0.0046 0.0378  0.0249  138 HIS   B CA  
6577 C C   . HIS   B 138 ? 0.1805 0.1238 0.2521 -0.0065 0.0356  0.0336  138 HIS   B C   
6578 O O   . HIS   B 138 ? 0.1747 0.1351 0.2660 0.0020  0.0423  0.0377  138 HIS   B O   
6579 C CB  . HIS   B 138 ? 0.2314 0.1390 0.2838 -0.0089 0.0582  0.0294  138 HIS   B CB  
6580 C CG  . HIS   B 138 ? 0.2568 0.1563 0.2923 -0.0096 0.0743  0.0445  138 HIS   B CG  
6581 N ND1 . HIS   B 138 ? 0.2682 0.1746 0.3194 -0.0061 0.0808  0.0374  138 HIS   B ND1 
6582 C CD2 . HIS   B 138 ? 0.2735 0.1628 0.2877 -0.0106 0.0799  0.0356  138 HIS   B CD2 
6583 C CE1 . HIS   B 138 ? 0.2758 0.1791 0.3130 -0.0013 0.0884  0.0338  138 HIS   B CE1 
6584 N NE2 . HIS   B 138 ? 0.2835 0.1659 0.2905 0.0015  0.0879  0.0267  138 HIS   B NE2 
6592 N N   . SER   B 139 ? 0.1714 0.1180 0.2511 0.0004  0.0329  0.0216  139 SER   B N   
6593 C CA  . SER   B 139 ? 0.1675 0.1082 0.2325 0.0005  0.0300  0.0051  139 SER   B CA  
6594 C C   . SER   B 139 ? 0.1433 0.1042 0.2350 -0.0045 0.0315  0.0114  139 SER   B C   
6595 O O   . SER   B 139 ? 0.1431 0.1124 0.2433 -0.0060 0.0142  0.0071  139 SER   B O   
6596 C CB  . SER   B 139 ? 0.1762 0.1100 0.2336 -0.0045 0.0150  0.0045  139 SER   B CB  
6597 O OG  . SER   B 139 ? 0.1720 0.1185 0.2394 -0.0017 -0.0001 0.0116  139 SER   B OG  
6603 N N   . LEU   B 140 ? 0.1448 0.1040 0.2493 -0.0029 0.0294  0.0062  140 LEU   B N   
6604 C CA  . LEU   B 140 ? 0.1430 0.1089 0.2445 -0.0034 0.0212  0.0126  140 LEU   B CA  
6605 C C   . LEU   B 140 ? 0.1480 0.1113 0.2575 -0.0102 0.0184  0.0011  140 LEU   B C   
6606 O O   . LEU   B 140 ? 0.1457 0.1149 0.2440 -0.0074 0.0084  0.0100  140 LEU   B O   
6607 C CB  . LEU   B 140 ? 0.1396 0.1115 0.2517 -0.0104 0.0292  0.0032  140 LEU   B CB  
6608 C CG  . LEU   B 140 ? 0.1560 0.1128 0.2483 -0.0082 0.0168  0.0089  140 LEU   B CG  
6609 C CD1 . LEU   B 140 ? 0.1648 0.1190 0.2709 -0.0081 0.0264  -0.0009 140 LEU   B CD1 
6610 C CD2 . LEU   B 140 ? 0.1702 0.1232 0.2504 -0.0097 0.0156  0.0018  140 LEU   B CD2 
6622 N N   . ARG   B 141 ? 0.1466 0.1117 0.2662 -0.0144 0.0263  0.0019  141 ARG   B N   
6623 C CA  . ARG   B 141 ? 0.1410 0.1121 0.3030 -0.0141 0.0337  -0.0025 141 ARG   B CA  
6624 C C   . ARG   B 141 ? 0.1350 0.1096 0.2836 -0.0143 0.0179  0.0020  141 ARG   B C   
6625 O O   . ARG   B 141 ? 0.1397 0.1100 0.2788 -0.0102 0.0115  -0.0066 141 ARG   B O   
6626 C CB  . ARG   B 141 ? 0.1537 0.1180 0.3293 -0.0202 0.0400  -0.0035 141 ARG   B CB  
6627 C CG  . ARG   B 141 ? 0.1829 0.1514 0.3437 -0.0332 0.0394  0.0003  141 ARG   B CG  
6628 C CD  . ARG   B 141 ? 0.2367 0.1778 0.3297 -0.0283 0.0238  -0.0132 141 ARG   B CD  
6629 N NE  . ARG   B 141 ? 0.2692 0.1759 0.3060 -0.0419 0.0279  -0.0172 141 ARG   B NE  
6630 C CZ  . ARG   B 141 ? 0.2991 0.1571 0.2804 -0.0292 0.0270  -0.0305 141 ARG   B CZ  
6631 N NH1 . ARG   B 141 ? 0.3112 0.1510 0.2697 -0.0231 0.0270  -0.0284 141 ARG   B NH1 
6632 N NH2 . ARG   B 141 ? 0.3253 0.1606 0.2960 -0.0159 0.0127  -0.0152 141 ARG   B NH2 
6646 N N   . VAL   B 142 ? 0.1410 0.1065 0.2693 -0.0119 0.0272  0.0036  142 VAL   B N   
6647 C CA  . VAL   B 142 ? 0.1348 0.1120 0.2561 -0.0043 0.0311  0.0024  142 VAL   B CA  
6648 C C   . VAL   B 142 ? 0.1326 0.1088 0.2443 -0.0097 0.0199  -0.0061 142 VAL   B C   
6649 O O   . VAL   B 142 ? 0.1375 0.1086 0.2518 -0.0039 0.0176  -0.0029 142 VAL   B O   
6650 C CB  . VAL   B 142 ? 0.1496 0.1203 0.2589 -0.0009 0.0288  0.0112  142 VAL   B CB  
6651 C CG1 . VAL   B 142 ? 0.1484 0.1170 0.2619 0.0023  0.0288  0.0067  142 VAL   B CG1 
6652 C CG2 . VAL   B 142 ? 0.1771 0.1203 0.2590 0.0012  0.0249  0.0147  142 VAL   B CG2 
6662 N N   . CYS   B 143 ? 0.1362 0.1129 0.2389 -0.0035 0.0192  0.0114  143 CYS   B N   
6663 C CA  . CYS   B 143 ? 0.1345 0.1132 0.2341 -0.0082 0.0151  0.0087  143 CYS   B CA  
6664 C C   . CYS   B 143 ? 0.1277 0.1155 0.2378 -0.0110 0.0089  -0.0022 143 CYS   B C   
6665 O O   . CYS   B 143 ? 0.1249 0.1155 0.2396 -0.0068 -0.0020 -0.0015 143 CYS   B O   
6666 C CB  . CYS   B 143 ? 0.1318 0.1176 0.2215 -0.0105 0.0115  0.0080  143 CYS   B CB  
6667 S SG  . CYS   B 143 ? 0.1343 0.1317 0.2262 -0.0074 0.0132  0.0061  143 CYS   B SG  
6673 N N   . VAL   B 144 ? 0.1286 0.1141 0.2481 -0.0050 -0.0003 -0.0113 144 VAL   B N   
6674 C CA  . VAL   B 144 ? 0.1389 0.1239 0.2725 -0.0122 -0.0009 -0.0206 144 VAL   B CA  
6675 C C   . VAL   B 144 ? 0.1342 0.1251 0.2782 -0.0122 0.0059  -0.0011 144 VAL   B C   
6676 O O   . VAL   B 144 ? 0.1455 0.1460 0.2969 0.0046  0.0041  0.0192  144 VAL   B O   
6677 C CB  . VAL   B 144 ? 0.1622 0.1300 0.3189 -0.0136 -0.0119 -0.0414 144 VAL   B CB  
6678 C CG1 . VAL   B 144 ? 0.1836 0.1673 0.3422 -0.0032 -0.0252 -0.0312 144 VAL   B CG1 
6679 C CG2 . VAL   B 144 ? 0.1761 0.1373 0.3252 -0.0097 -0.0273 -0.0451 144 VAL   B CG2 
6689 N N   . ASP   B 145 ? 0.1312 0.1218 0.2860 -0.0166 0.0065  -0.0166 145 ASP   B N   
6690 C CA  . ASP   B 145 ? 0.1316 0.1283 0.3047 -0.0121 0.0180  -0.0126 145 ASP   B CA  
6691 C C   . ASP   B 145 ? 0.1291 0.1319 0.2810 -0.0142 0.0159  -0.0057 145 ASP   B C   
6692 O O   . ASP   B 145 ? 0.1315 0.1435 0.3319 -0.0155 0.0224  -0.0215 145 ASP   B O   
6693 C CB  . ASP   B 145 ? 0.1442 0.1348 0.3355 -0.0187 0.0320  0.0077  145 ASP   B CB  
6694 C CG  . ASP   B 145 ? 0.1641 0.1416 0.3816 -0.0308 0.0279  0.0055  145 ASP   B CG  
6695 O OD1 . ASP   B 145 ? 0.1694 0.1409 0.3922 -0.0261 0.0034  -0.0086 145 ASP   B OD1 
6696 O OD2 . ASP   B 145 ? 0.1884 0.1534 0.4164 -0.0360 0.0390  0.0147  145 ASP   B OD2 
6701 N N   . THR   B 146 ? 0.1232 0.1193 0.2341 -0.0104 0.0076  0.0003  146 THR   B N   
6702 C CA  . THR   B 146 ? 0.1287 0.1125 0.2157 -0.0014 0.0152  0.0010  146 THR   B CA  
6703 C C   . THR   B 146 ? 0.1278 0.1107 0.2056 -0.0048 0.0144  0.0058  146 THR   B C   
6704 O O   . THR   B 146 ? 0.1330 0.1145 0.2182 -0.0045 0.0089  -0.0023 146 THR   B O   
6705 C CB  . THR   B 146 ? 0.1325 0.1153 0.2306 -0.0010 0.0265  0.0115  146 THR   B CB  
6706 O OG1 . THR   B 146 ? 0.1362 0.1168 0.2405 -0.0043 0.0311  0.0179  146 THR   B OG1 
6707 C CG2 . THR   B 146 ? 0.1387 0.1249 0.2140 -0.0013 0.0221  0.0009  146 THR   B CG2 
6715 N N   . VAL   B 147 ? 0.1341 0.1213 0.1906 -0.0088 0.0166  0.0027  147 VAL   B N   
6716 C CA  . VAL   B 147 ? 0.1299 0.1173 0.1828 -0.0112 0.0062  -0.0048 147 VAL   B CA  
6717 C C   . VAL   B 147 ? 0.1297 0.1191 0.2030 -0.0173 -0.0006 -0.0044 147 VAL   B C   
6718 O O   . VAL   B 147 ? 0.1419 0.1251 0.2223 -0.0192 -0.0201 -0.0060 147 VAL   B O   
6719 C CB  . VAL   B 147 ? 0.1299 0.1256 0.1807 -0.0081 -0.0007 -0.0012 147 VAL   B CB  
6720 C CG1 . VAL   B 147 ? 0.1285 0.1404 0.1738 -0.0118 -0.0070 0.0079  147 VAL   B CG1 
6721 C CG2 . VAL   B 147 ? 0.1344 0.1203 0.1964 -0.0142 0.0037  0.0117  147 VAL   B CG2 
6731 N N   . ARG   B 148 ? 0.1303 0.1204 0.1928 -0.0135 -0.0105 -0.0091 148 ARG   B N   
6732 C CA  . ARG   B 148 ? 0.1349 0.1300 0.2001 -0.0085 -0.0215 -0.0170 148 ARG   B CA  
6733 C C   . ARG   B 148 ? 0.1364 0.1364 0.1829 -0.0083 -0.0247 -0.0066 148 ARG   B C   
6734 O O   . ARG   B 148 ? 0.1548 0.1605 0.1911 -0.0193 -0.0258 0.0040  148 ARG   B O   
6735 C CB  . ARG   B 148 ? 0.1351 0.1344 0.2164 -0.0013 -0.0239 -0.0222 148 ARG   B CB  
6736 C CG  . ARG   B 148 ? 0.1345 0.1535 0.2199 -0.0030 -0.0271 -0.0336 148 ARG   B CG  
6737 C CD  . ARG   B 148 ? 0.1446 0.1741 0.2270 0.0049  -0.0290 -0.0344 148 ARG   B CD  
6738 N NE  . ARG   B 148 ? 0.1548 0.1698 0.2107 0.0206  -0.0250 -0.0382 148 ARG   B NE  
6739 C CZ  . ARG   B 148 ? 0.1484 0.1574 0.2004 0.0195  -0.0147 -0.0256 148 ARG   B CZ  
6740 N NH1 . ARG   B 148 ? 0.1410 0.1606 0.2076 0.0023  -0.0029 -0.0231 148 ARG   B NH1 
6741 N NH2 . ARG   B 148 ? 0.1644 0.1453 0.1934 0.0212  -0.0158 -0.0199 148 ARG   B NH2 
6755 N N   . THR   B 149 ? 0.1396 0.1275 0.1911 -0.0144 -0.0227 0.0042  149 THR   B N   
6756 C CA  . THR   B 149 ? 0.1439 0.1255 0.1747 -0.0146 -0.0183 0.0089  149 THR   B CA  
6757 C C   . THR   B 149 ? 0.1406 0.1248 0.1667 -0.0183 -0.0241 0.0053  149 THR   B C   
6758 O O   . THR   B 149 ? 0.1541 0.1301 0.1824 -0.0231 -0.0066 0.0047  149 THR   B O   
6759 C CB  . THR   B 149 ? 0.1492 0.1268 0.1751 -0.0145 -0.0195 0.0078  149 THR   B CB  
6760 O OG1 . THR   B 149 ? 0.1448 0.1329 0.1678 -0.0201 -0.0191 0.0000  149 THR   B OG1 
6761 C CG2 . THR   B 149 ? 0.1604 0.1257 0.1914 -0.0127 -0.0113 -0.0025 149 THR   B CG2 
6769 N N   . ASN   B 150 ? 0.1474 0.1243 0.1584 -0.0177 -0.0295 0.0009  150 ASN   B N   
6770 C CA  . ASN   B 150 ? 0.1578 0.1463 0.1604 -0.0237 -0.0258 -0.0024 150 ASN   B CA  
6771 C C   . ASN   B 150 ? 0.1462 0.1430 0.1538 -0.0174 -0.0176 -0.0009 150 ASN   B C   
6772 O O   . ASN   B 150 ? 0.1526 0.1357 0.1841 -0.0239 -0.0372 0.0051  150 ASN   B O   
6773 C CB  . ASN   B 150 ? 0.1764 0.1850 0.1822 -0.0276 -0.0352 0.0092  150 ASN   B CB  
6774 C CG  . ASN   B 150 ? 0.2072 0.2262 0.2126 -0.0224 -0.0445 0.0287  150 ASN   B CG  
6775 O OD1 . ASN   B 150 ? 0.2149 0.2425 0.2149 -0.0322 -0.0616 0.0263  150 ASN   B OD1 
6776 N ND2 . ASN   B 150 ? 0.2241 0.2496 0.2471 -0.0162 -0.0519 0.0695  150 ASN   B ND2 
6783 N N   . VAL   B 151 ? 0.1433 0.1358 0.1600 -0.0227 -0.0240 0.0014  151 VAL   B N   
6784 C CA  . VAL   B 151 ? 0.1491 0.1299 0.1615 -0.0229 -0.0180 0.0041  151 VAL   B CA  
6785 C C   . VAL   B 151 ? 0.1474 0.1269 0.1544 -0.0301 -0.0238 0.0012  151 VAL   B C   
6786 O O   . VAL   B 151 ? 0.1535 0.1434 0.1843 -0.0260 -0.0102 -0.0085 151 VAL   B O   
6787 C CB  . VAL   B 151 ? 0.1633 0.1439 0.1774 -0.0128 -0.0127 -0.0017 151 VAL   B CB  
6788 C CG1 . VAL   B 151 ? 0.1736 0.1473 0.1920 -0.0177 -0.0010 -0.0068 151 VAL   B CG1 
6789 C CG2 . VAL   B 151 ? 0.1686 0.1627 0.1731 0.0026  -0.0138 0.0128  151 VAL   B CG2 
6799 N N   . TYR   B 152 ? 0.1395 0.1176 0.1532 -0.0262 -0.0145 -0.0041 152 TYR   B N   
6800 C CA  . TYR   B 152 ? 0.1413 0.1358 0.1563 -0.0256 -0.0078 -0.0051 152 TYR   B CA  
6801 C C   . TYR   B 152 ? 0.1368 0.1192 0.1443 -0.0215 -0.0088 -0.0082 152 TYR   B C   
6802 O O   . TYR   B 152 ? 0.1472 0.1235 0.1459 -0.0289 -0.0150 0.0011  152 TYR   B O   
6803 C CB  . TYR   B 152 ? 0.1521 0.1526 0.1542 -0.0290 -0.0004 0.0067  152 TYR   B CB  
6804 C CG  . TYR   B 152 ? 0.1650 0.1620 0.1513 -0.0411 -0.0013 0.0074  152 TYR   B CG  
6805 C CD1 . TYR   B 152 ? 0.1778 0.1735 0.1436 -0.0356 -0.0233 0.0114  152 TYR   B CD1 
6806 C CD2 . TYR   B 152 ? 0.1874 0.1802 0.1662 -0.0376 -0.0043 -0.0009 152 TYR   B CD2 
6807 C CE1 . TYR   B 152 ? 0.1937 0.1929 0.1651 -0.0322 -0.0250 0.0196  152 TYR   B CE1 
6808 C CE2 . TYR   B 152 ? 0.1998 0.1997 0.1585 -0.0370 -0.0172 -0.0009 152 TYR   B CE2 
6809 C CZ  . TYR   B 152 ? 0.2033 0.2152 0.1492 -0.0355 -0.0351 0.0192  152 TYR   B CZ  
6810 O OH  . TYR   B 152 ? 0.2308 0.2496 0.1871 -0.0281 -0.0350 0.0278  152 TYR   B OH  
6820 N N   . LEU   B 153 ? 0.1429 0.1179 0.1506 -0.0299 -0.0061 -0.0095 153 LEU   B N   
6821 C CA  . LEU   B 153 ? 0.1446 0.1162 0.1428 -0.0228 0.0030  -0.0052 153 LEU   B CA  
6822 C C   . LEU   B 153 ? 0.1463 0.1151 0.1612 -0.0267 0.0041  -0.0143 153 LEU   B C   
6823 O O   . LEU   B 153 ? 0.1550 0.1381 0.1766 -0.0169 -0.0002 -0.0310 153 LEU   B O   
6824 C CB  . LEU   B 153 ? 0.1429 0.1222 0.1615 -0.0241 0.0028  -0.0049 153 LEU   B CB  
6825 C CG  . LEU   B 153 ? 0.1373 0.1337 0.1805 -0.0250 -0.0008 -0.0093 153 LEU   B CG  
6826 C CD1 . LEU   B 153 ? 0.1447 0.1457 0.1908 -0.0238 -0.0012 0.0053  153 LEU   B CD1 
6827 C CD2 . LEU   B 153 ? 0.1409 0.1438 0.1918 -0.0234 0.0138  0.0043  153 LEU   B CD2 
6839 N N   . ALA   B 154 ? 0.1431 0.1164 0.1707 -0.0115 -0.0023 -0.0118 154 ALA   B N   
6840 C CA  . ALA   B 154 ? 0.1489 0.1294 0.1767 -0.0024 -0.0031 -0.0222 154 ALA   B CA  
6841 C C   . ALA   B 154 ? 0.1587 0.1294 0.1784 0.0061  -0.0064 -0.0229 154 ALA   B C   
6842 O O   . ALA   B 154 ? 0.1845 0.1358 0.1956 0.0047  0.0051  -0.0039 154 ALA   B O   
6843 C CB  . ALA   B 154 ? 0.1460 0.1487 0.1989 -0.0063 -0.0001 -0.0289 154 ALA   B CB  
6849 N N   . VAL   B 155 ? 0.1336 0.1249 0.2050 0.0005  -0.0012 -0.0160 155 VAL   B N   
6850 C CA  . VAL   B 155 ? 0.1295 0.1261 0.2154 -0.0054 -0.0061 -0.0063 155 VAL   B CA  
6851 C C   . VAL   B 155 ? 0.1351 0.1258 0.2232 -0.0071 -0.0056 -0.0276 155 VAL   B C   
6852 O O   . VAL   B 155 ? 0.1522 0.1419 0.2633 0.0055  -0.0000 -0.0427 155 VAL   B O   
6853 C CB  . VAL   B 155 ? 0.1385 0.1395 0.2508 -0.0046 -0.0054 0.0013  155 VAL   B CB  
6854 C CG1 . VAL   B 155 ? 0.1475 0.1369 0.2505 -0.0076 -0.0045 0.0062  155 VAL   B CG1 
6855 C CG2 . VAL   B 155 ? 0.1394 0.1488 0.2828 -0.0090 -0.0083 0.0336  155 VAL   B CG2 
6865 N N   . PHE   B 156 ? 0.1287 0.1314 0.2384 -0.0007 0.0017  -0.0212 156 PHE   B N   
6866 C CA  . PHE   B 156 ? 0.1339 0.1404 0.2598 0.0069  -0.0001 -0.0186 156 PHE   B CA  
6867 C C   . PHE   B 156 ? 0.1344 0.1496 0.2865 0.0085  0.0005  -0.0384 156 PHE   B C   
6868 O O   . PHE   B 156 ? 0.1568 0.1690 0.3132 0.0173  0.0070  -0.0428 156 PHE   B O   
6869 C CB  . PHE   B 156 ? 0.1339 0.1385 0.2506 0.0027  -0.0110 -0.0055 156 PHE   B CB  
6870 C CG  . PHE   B 156 ? 0.1371 0.1494 0.2715 0.0027  -0.0165 0.0035  156 PHE   B CG  
6871 C CD1 . PHE   B 156 ? 0.1376 0.1773 0.3033 0.0100  0.0008  0.0247  156 PHE   B CD1 
6872 C CD2 . PHE   B 156 ? 0.1478 0.1587 0.2794 0.0080  -0.0197 0.0037  156 PHE   B CD2 
6873 C CE1 . PHE   B 156 ? 0.1454 0.1910 0.3179 0.0081  -0.0032 0.0272  156 PHE   B CE1 
6874 C CE2 . PHE   B 156 ? 0.1495 0.1799 0.2926 0.0127  -0.0242 0.0170  156 PHE   B CE2 
6875 C CZ  . PHE   B 156 ? 0.1399 0.1867 0.3121 0.0126  -0.0184 0.0160  156 PHE   B CZ  
6885 N N   . ASP   B 157 ? 0.1307 0.1422 0.3147 0.0080  -0.0154 -0.0252 157 ASP   B N   
6886 C CA  . ASP   B 157 ? 0.1415 0.1459 0.3277 0.0083  -0.0230 -0.0362 157 ASP   B CA  
6887 C C   . ASP   B 157 ? 0.1476 0.1447 0.3357 0.0055  -0.0114 -0.0512 157 ASP   B C   
6888 O O   . ASP   B 157 ? 0.1358 0.1434 0.3290 0.0040  -0.0162 -0.0384 157 ASP   B O   
6889 C CB  . ASP   B 157 ? 0.1684 0.1652 0.3329 0.0042  -0.0455 -0.0210 157 ASP   B CB  
6890 C CG  . ASP   B 157 ? 0.2037 0.1824 0.3630 0.0049  -0.0379 -0.0207 157 ASP   B CG  
6891 O OD1 . ASP   B 157 ? 0.2151 0.1732 0.3776 0.0184  -0.0198 -0.0109 157 ASP   B OD1 
6892 O OD2 . ASP   B 157 ? 0.2339 0.2043 0.3941 0.0018  -0.0202 -0.0226 157 ASP   B OD2 
6897 N N   A LYS   B 158 ? 0.1591 0.1651 0.3327 0.0025  -0.0065 -0.0634 158 LYS   B N   
6898 N N   B LYS   B 158 ? 0.1511 0.1683 0.3421 0.0080  -0.0034 -0.0660 158 LYS   B N   
6899 C CA  A LYS   B 158 ? 0.1735 0.1800 0.3305 0.0030  -0.0057 -0.0715 158 LYS   B CA  
6900 C CA  B LYS   B 158 ? 0.1631 0.1869 0.3474 0.0146  -0.0000 -0.0758 158 LYS   B CA  
6901 C C   A LYS   B 158 ? 0.1703 0.1698 0.3335 -0.0007 -0.0123 -0.0670 158 LYS   B C   
6902 C C   B LYS   B 158 ? 0.1593 0.1751 0.3557 0.0105  -0.0084 -0.0699 158 LYS   B C   
6903 O O   A LYS   B 158 ? 0.1690 0.1658 0.3334 -0.0082 -0.0114 -0.0755 158 LYS   B O   
6904 O O   B LYS   B 158 ? 0.1595 0.1763 0.3554 0.0017  -0.0081 -0.0780 158 LYS   B O   
6905 C CB  A LYS   B 158 ? 0.1980 0.2062 0.3280 0.0081  0.0006  -0.0837 158 LYS   B CB  
6906 C CB  B LYS   B 158 ? 0.1896 0.2206 0.3417 0.0232  0.0120  -0.0940 158 LYS   B CB  
6907 C CG  A LYS   B 158 ? 0.2219 0.2335 0.3338 0.0070  0.0009  -0.0949 158 LYS   B CG  
6908 C CG  B LYS   B 158 ? 0.2186 0.2542 0.3434 0.0226  0.0149  -0.1099 158 LYS   B CG  
6909 C CD  A LYS   B 158 ? 0.2404 0.2595 0.3476 0.0069  -0.0012 -0.0929 158 LYS   B CD  
6910 C CD  B LYS   B 158 ? 0.2439 0.2907 0.3585 0.0186  0.0092  -0.1056 158 LYS   B CD  
6911 C CE  A LYS   B 158 ? 0.2538 0.2778 0.3590 0.0097  -0.0031 -0.0886 158 LYS   B CE  
6912 C CE  B LYS   B 158 ? 0.2627 0.3151 0.3687 0.0219  0.0070  -0.0995 158 LYS   B CE  
6913 N NZ  A LYS   B 158 ? 0.2534 0.2862 0.3610 0.0078  -0.0026 -0.0878 158 LYS   B NZ  
6914 N NZ  B LYS   B 158 ? 0.2653 0.3281 0.3703 0.0214  0.0124  -0.0951 158 LYS   B NZ  
6941 N N   A ASN   B 159 ? 0.1729 0.1616 0.3517 0.0016  -0.0205 -0.0543 159 ASN   B N   
6942 N N   B ASN   B 159 ? 0.1636 0.1635 0.3739 0.0116  -0.0173 -0.0572 159 ASN   B N   
6943 C CA  A ASN   B 159 ? 0.1797 0.1559 0.3670 0.0120  -0.0378 -0.0415 159 ASN   B CA  
6944 C CA  B ASN   B 159 ? 0.1730 0.1519 0.3866 0.0262  -0.0340 -0.0472 159 ASN   B CA  
6945 C C   A ASN   B 159 ? 0.1654 0.1457 0.3642 0.0106  -0.0478 -0.0372 159 ASN   B C   
6946 C C   B ASN   B 159 ? 0.1604 0.1386 0.3798 0.0208  -0.0389 -0.0458 159 ASN   B C   
6947 O O   A ASN   B 159 ? 0.1656 0.1448 0.3729 -0.0067 -0.0560 -0.0243 159 ASN   B O   
6948 O O   B ASN   B 159 ? 0.1586 0.1299 0.3987 0.0063  -0.0323 -0.0362 159 ASN   B O   
6949 C CB  A ASN   B 159 ? 0.2023 0.1697 0.3848 0.0141  -0.0426 -0.0419 159 ASN   B CB  
6950 C CB  B ASN   B 159 ? 0.1959 0.1674 0.4021 0.0326  -0.0442 -0.0464 159 ASN   B CB  
6951 C CG  A ASN   B 159 ? 0.2243 0.1856 0.4034 0.0094  -0.0490 -0.0554 159 ASN   B CG  
6952 C CG  B ASN   B 159 ? 0.2194 0.1887 0.4192 0.0276  -0.0545 -0.0612 159 ASN   B CG  
6953 O OD1 A ASN   B 159 ? 0.2413 0.1973 0.4127 0.0123  -0.0433 -0.0625 159 ASN   B OD1 
6954 O OD1 B ASN   B 159 ? 0.2350 0.2024 0.4223 0.0308  -0.0515 -0.0665 159 ASN   B OD1 
6955 N ND2 A ASN   B 159 ? 0.2258 0.1915 0.4101 0.0089  -0.0540 -0.0514 159 ASN   B ND2 
6956 N ND2 B ASN   B 159 ? 0.2219 0.2007 0.4325 0.0311  -0.0585 -0.0523 159 ASN   B ND2 
6969 N N   . LEU   B 160 ? 0.1589 0.1411 0.3613 0.0127  -0.0410 -0.0415 160 LEU   B N   
6970 C CA  . LEU   B 160 ? 0.1507 0.1398 0.3227 0.0132  -0.0323 -0.0226 160 LEU   B CA  
6971 C C   . LEU   B 160 ? 0.1412 0.1318 0.3120 0.0026  -0.0152 -0.0336 160 LEU   B C   
6972 O O   . LEU   B 160 ? 0.1318 0.1415 0.3138 -0.0046 -0.0257 -0.0133 160 LEU   B O   
6973 C CB  . LEU   B 160 ? 0.1515 0.1508 0.3049 0.0088  -0.0332 -0.0127 160 LEU   B CB  
6974 C CG  . LEU   B 160 ? 0.1544 0.1638 0.2855 0.0084  -0.0346 -0.0046 160 LEU   B CG  
6975 C CD1 . LEU   B 160 ? 0.1708 0.1776 0.2889 0.0019  -0.0194 -0.0111 160 LEU   B CD1 
6976 C CD2 . LEU   B 160 ? 0.1543 0.1669 0.2846 0.0187  -0.0321 -0.0126 160 LEU   B CD2 
6989 N N   . TYR   B 161 ? 0.1422 0.1382 0.3139 -0.0074 0.0025  -0.0366 161 TYR   B N   
6990 C CA  . TYR   B 161 ? 0.1448 0.1408 0.3047 -0.0136 0.0194  -0.0405 161 TYR   B CA  
6991 C C   . TYR   B 161 ? 0.1513 0.1399 0.2986 -0.0145 0.0226  -0.0365 161 TYR   B C   
6992 O O   . TYR   B 161 ? 0.1533 0.1402 0.2959 -0.0207 0.0097  -0.0325 161 TYR   B O   
6993 C CB  . TYR   B 161 ? 0.1616 0.1456 0.3068 -0.0268 0.0302  -0.0502 161 TYR   B CB  
6994 C CG  . TYR   B 161 ? 0.1889 0.1484 0.2928 -0.0329 0.0342  -0.0473 161 TYR   B CG  
6995 C CD1 . TYR   B 161 ? 0.1954 0.1456 0.2831 -0.0420 0.0412  -0.0393 161 TYR   B CD1 
6996 C CD2 . TYR   B 161 ? 0.2121 0.1561 0.2897 -0.0265 0.0314  -0.0494 161 TYR   B CD2 
6997 C CE1 . TYR   B 161 ? 0.2155 0.1669 0.2917 -0.0385 0.0371  -0.0369 161 TYR   B CE1 
6998 C CE2 . TYR   B 161 ? 0.2290 0.1690 0.2961 -0.0312 0.0345  -0.0443 161 TYR   B CE2 
6999 C CZ  . TYR   B 161 ? 0.2314 0.1760 0.2871 -0.0410 0.0336  -0.0386 161 TYR   B CZ  
7000 O OH  . TYR   B 161 ? 0.2551 0.2002 0.3090 -0.0397 0.0291  -0.0384 161 TYR   B OH  
7010 N N   . ASP   B 162 ? 0.1556 0.1398 0.3081 -0.0090 0.0084  -0.0547 162 ASP   B N   
7011 C CA  . ASP   B 162 ? 0.1671 0.1481 0.3240 -0.0100 0.0027  -0.0544 162 ASP   B CA  
7012 C C   . ASP   B 162 ? 0.1610 0.1355 0.3252 -0.0118 -0.0012 -0.0455 162 ASP   B C   
7013 O O   . ASP   B 162 ? 0.1644 0.1431 0.3350 -0.0201 -0.0145 -0.0288 162 ASP   B O   
7014 C CB  . ASP   B 162 ? 0.1818 0.1643 0.3404 -0.0049 0.0007  -0.0724 162 ASP   B CB  
7015 C CG  . ASP   B 162 ? 0.1904 0.1880 0.3596 0.0013  0.0018  -0.0853 162 ASP   B CG  
7016 O OD1 . ASP   B 162 ? 0.1905 0.2100 0.3427 -0.0082 0.0201  -0.0803 162 ASP   B OD1 
7017 O OD2 . ASP   B 162 ? 0.1972 0.2165 0.3892 0.0222  -0.0052 -0.0846 162 ASP   B OD2 
7022 N N   . LYS   B 163 ? 0.1566 0.1232 0.3189 -0.0077 -0.0102 -0.0319 163 LYS   B N   
7023 C CA  . LYS   B 163 ? 0.1692 0.1278 0.3192 -0.0147 -0.0092 -0.0144 163 LYS   B CA  
7024 C C   . LYS   B 163 ? 0.1428 0.1305 0.3035 -0.0168 -0.0131 0.0010  163 LYS   B C   
7025 O O   . LYS   B 163 ? 0.1475 0.1426 0.3254 -0.0201 -0.0157 0.0087  163 LYS   B O   
7026 C CB  . LYS   B 163 ? 0.2162 0.1601 0.3624 -0.0111 -0.0042 0.0008  163 LYS   B CB  
7027 C CG  . LYS   B 163 ? 0.2919 0.2454 0.4207 -0.0143 0.0108  0.0006  163 LYS   B CG  
7028 C CD  . LYS   B 163 ? 0.3653 0.3170 0.4809 -0.0218 0.0170  0.0031  163 LYS   B CD  
7029 C CE  . LYS   B 163 ? 0.4273 0.3818 0.5197 -0.0274 0.0238  0.0045  163 LYS   B CE  
7030 N NZ  . LYS   B 163 ? 0.4627 0.4118 0.5453 -0.0305 0.0270  0.0004  163 LYS   B NZ  
7044 N N   . LEU   B 164 ? 0.1345 0.1280 0.2746 -0.0113 -0.0084 0.0024  164 LEU   B N   
7045 C CA  . LEU   B 164 ? 0.1358 0.1255 0.2579 -0.0136 -0.0180 0.0042  164 LEU   B CA  
7046 C C   . LEU   B 164 ? 0.1432 0.1300 0.2570 -0.0218 -0.0170 0.0085  164 LEU   B C   
7047 O O   . LEU   B 164 ? 0.1457 0.1547 0.2672 -0.0155 -0.0176 0.0083  164 LEU   B O   
7048 C CB  . LEU   B 164 ? 0.1326 0.1270 0.2578 -0.0121 -0.0175 -0.0042 164 LEU   B CB  
7049 C CG  . LEU   B 164 ? 0.1405 0.1429 0.2634 -0.0068 -0.0052 0.0024  164 LEU   B CG  
7050 C CD1 . LEU   B 164 ? 0.1514 0.1410 0.2585 -0.0115 -0.0052 -0.0093 164 LEU   B CD1 
7051 C CD2 . LEU   B 164 ? 0.1539 0.1805 0.2848 -0.0043 0.0004  -0.0058 164 LEU   B CD2 
7063 N N   . VAL   B 165 ? 0.1678 0.1376 0.2802 -0.0280 -0.0246 -0.0056 165 VAL   B N   
7064 C CA  . VAL   B 165 ? 0.2001 0.1441 0.2922 -0.0374 -0.0479 -0.0068 165 VAL   B CA  
7065 C C   . VAL   B 165 ? 0.2270 0.1574 0.3158 -0.0450 -0.0638 0.0035  165 VAL   B C   
7066 O O   . VAL   B 165 ? 0.2394 0.1738 0.3145 -0.0476 -0.0665 0.0015  165 VAL   B O   
7067 C CB  . VAL   B 165 ? 0.2239 0.1601 0.2972 -0.0222 -0.0207 -0.0223 165 VAL   B CB  
7068 C CG1 . VAL   B 165 ? 0.2438 0.1670 0.3143 -0.0174 -0.0191 -0.0247 165 VAL   B CG1 
7069 C CG2 . VAL   B 165 ? 0.2221 0.1742 0.2901 -0.0197 0.0012  -0.0261 165 VAL   B CG2 
7079 N N   . SER   B 166 ? 0.2412 0.1493 0.3454 -0.0424 -0.0736 -0.0129 166 SER   B N   
7080 C CA  . SER   B 166 ? 0.2347 0.1501 0.3932 -0.0450 -0.0618 -0.0240 166 SER   B CA  
7081 C C   . SER   B 166 ? 0.2231 0.1607 0.3946 -0.0424 -0.0599 -0.0123 166 SER   B C   
7082 O O   . SER   B 166 ? 0.2257 0.1841 0.4165 -0.0541 -0.0671 -0.0374 166 SER   B O   
7083 C CB  . SER   B 166 ? 0.2365 0.1598 0.4245 -0.0373 -0.0646 -0.0352 166 SER   B CB  
7084 O OG  . SER   B 166 ? 0.2344 0.1574 0.4469 -0.0256 -0.0646 -0.0191 166 SER   B OG  
7090 N N   . SER   B 167 ? 0.2040 0.1496 0.3653 -0.0417 -0.0650 0.0254  167 SER   B N   
7091 C CA  . SER   B 167 ? 0.1953 0.1527 0.3578 -0.0363 -0.0444 0.0304  167 SER   B CA  
7092 C C   . SER   B 167 ? 0.1875 0.1619 0.3332 -0.0447 -0.0403 0.0530  167 SER   B C   
7093 O O   . SER   B 167 ? 0.1868 0.1758 0.3283 -0.0427 -0.0324 0.0500  167 SER   B O   
7094 C CB  . SER   B 167 ? 0.1844 0.1654 0.3627 -0.0324 -0.0153 0.0251  167 SER   B CB  
7095 O OG  . SER   B 167 ? 0.1768 0.1734 0.3602 -0.0173 0.0024  0.0201  167 SER   B OG  
7101 N N   . PHE   B 168 ? 0.1935 0.1644 0.3270 -0.0424 -0.0351 0.0456  168 PHE   B N   
7102 C CA  . PHE   B 168 ? 0.1988 0.1654 0.3080 -0.0439 -0.0248 0.0280  168 PHE   B CA  
7103 C C   . PHE   B 168 ? 0.1741 0.1520 0.2600 -0.0238 -0.0033 0.0138  168 PHE   B C   
7104 O O   . PHE   B 168 ? 0.2064 0.1504 0.2546 0.0002  -0.0026 -0.0002 168 PHE   B O   
7105 C CB  . PHE   B 168 ? 0.2111 0.1736 0.3135 -0.0520 -0.0408 0.0383  168 PHE   B CB  
7106 C CG  . PHE   B 168 ? 0.2357 0.1583 0.3035 -0.0519 -0.0415 0.0104  168 PHE   B CG  
7107 C CD1 . PHE   B 168 ? 0.2636 0.1557 0.3220 -0.0502 -0.0474 0.0061  168 PHE   B CD1 
7108 C CD2 . PHE   B 168 ? 0.2242 0.1477 0.3073 -0.0407 -0.0372 0.0200  168 PHE   B CD2 
7109 C CE1 . PHE   B 168 ? 0.2740 0.1609 0.3125 -0.0379 -0.0370 0.0178  168 PHE   B CE1 
7110 C CE2 . PHE   B 168 ? 0.2486 0.1511 0.3053 -0.0221 -0.0397 0.0216  168 PHE   B CE2 
7111 C CZ  . PHE   B 168 ? 0.2622 0.1411 0.3090 -0.0170 -0.0438 0.0318  168 PHE   B CZ  
7121 N N   . LEU   B 169 ? 0.1700 0.1645 0.2535 -0.0060 0.0083  -0.0003 169 LEU   B N   
7122 C CA  . LEU   B 169 ? 0.1983 0.1921 0.2856 -0.0098 0.0133  -0.0269 169 LEU   B CA  
7123 C C   . LEU   B 169 ? 0.2277 0.2189 0.3467 0.0044  0.0094  -0.0634 169 LEU   B C   
7124 O O   . LEU   B 169 ? 0.2441 0.2368 0.4040 -0.0016 -0.0021 -0.0933 169 LEU   B O   
7125 C CB  . LEU   B 169 ? 0.2149 0.2287 0.2983 -0.0129 0.0015  -0.0056 169 LEU   B CB  
7126 C CG  . LEU   B 169 ? 0.2571 0.2706 0.3441 -0.0073 -0.0043 -0.0054 169 LEU   B CG  
7127 C CD1 . LEU   B 169 ? 0.2709 0.2884 0.3442 -0.0054 -0.0112 0.0040  169 LEU   B CD1 
7128 C CD2 . LEU   B 169 ? 0.2576 0.2752 0.3525 0.0012  0.0021  -0.0222 169 LEU   B CD2 
7129 O OXT . LEU   B 169 ? 0.2507 0.2387 0.3584 0.0320  0.0132  -0.0561 169 LEU   B OXT 
7141 N N2  B A1A76 C .   ? 0.1067 0.1031 0.1572 -0.0033 -0.0077 0.0298  201 A1A76 A N2  
7142 C C3  B A1A76 C .   ? 0.1343 0.1151 0.1756 -0.0083 -0.0326 0.0378  201 A1A76 A C3  
7143 C C6  B A1A76 C .   ? 0.1794 0.1627 0.1983 -0.0049 -0.0186 0.0409  201 A1A76 A C6  
7144 C C9  B A1A76 C .   ? 0.1009 0.1004 0.1412 0.0021  -0.0084 0.0239  201 A1A76 A C9  
7145 C C12 B A1A76 C .   ? 0.0977 0.1009 0.1478 0.0001  -0.0038 0.0237  201 A1A76 A C12 
7146 C C14 B A1A76 C .   ? 0.1122 0.1147 0.1493 -0.0003 -0.0088 0.0375  201 A1A76 A C14 
7147 C C1  B A1A76 C .   ? 0.1199 0.1088 0.1374 -0.0023 -0.0038 0.0193  201 A1A76 A C1  
7148 C C10 B A1A76 C .   ? 0.1057 0.1081 0.1604 0.0007  0.0017  0.0360  201 A1A76 A C10 
7149 C C11 B A1A76 C .   ? 0.1055 0.1060 0.1489 0.0063  0.0007  0.0219  201 A1A76 A C11 
7150 C C13 B A1A76 C .   ? 0.1098 0.1080 0.1512 -0.0009 -0.0073 0.0283  201 A1A76 A C13 
7151 C C2  B A1A76 C .   ? 0.1211 0.1024 0.1397 -0.0030 -0.0220 0.0343  201 A1A76 A C2  
7152 C C4  B A1A76 C .   ? 0.1459 0.1247 0.1821 -0.0055 -0.0489 0.0492  201 A1A76 A C4  
7153 C C5  B A1A76 C .   ? 0.1786 0.1522 0.1939 -0.0039 -0.0391 0.0484  201 A1A76 A C5  
7154 C C7  B A1A76 C .   ? 0.1454 0.1382 0.1758 -0.0019 -0.0151 0.0398  201 A1A76 A C7  
7155 C C8  B A1A76 C .   ? 0.1254 0.1104 0.1758 -0.0023 -0.0342 0.0437  201 A1A76 A C8  
7156 N N1  B A1A76 C .   ? 0.1052 0.0950 0.1532 -0.0011 -0.0210 0.0298  201 A1A76 A N1  
7157 N N3  B A1A76 C .   ? 0.1081 0.1071 0.1485 0.0019  0.0112  0.0358  201 A1A76 A N3  
7158 N N4  B A1A76 C .   ? 0.1182 0.1146 0.1387 0.0075  -0.0115 0.0246  201 A1A76 A N4  
7159 O O1  B A1A76 C .   ? 0.1222 0.1272 0.1452 0.0029  -0.0086 0.0120  201 A1A76 A O1  
7178 O O   . HOH   D .   ? 0.5098 0.2946 0.4458 0.1818  -0.1177 -0.0575 301 HOH   A O   
7179 O O   . HOH   D .   ? 0.4129 0.3593 0.3845 0.0855  -0.1349 -0.0262 302 HOH   A O   
7180 O O   A HOH   D .   ? 0.3076 0.5097 0.3036 -0.0405 0.0186  0.1239  303 HOH   A O   
7181 O O   B HOH   D .   ? 0.2032 0.2123 0.2507 -0.0214 -0.0232 0.0461  304 HOH   A O   
7182 O O   . HOH   D .   ? 0.5497 0.3971 0.2943 0.1606  -0.0876 0.0329  305 HOH   A O   
7183 O O   . HOH   D .   ? 0.4422 0.5403 0.3910 -0.1551 0.1516  0.0891  306 HOH   A O   
7184 O O   . HOH   D .   ? 0.2695 0.2743 0.2137 -0.1111 -0.0543 0.1137  307 HOH   A O   
7185 O O   . HOH   D .   ? 0.7321 0.7787 0.5867 -0.0793 -0.1335 -0.1073 308 HOH   A O   
7186 O O   . HOH   D .   ? 0.3343 0.2773 0.1631 -0.0901 0.0210  0.0523  309 HOH   A O   
7187 O O   A HOH   D .   ? 0.3518 0.1332 0.3332 -0.0061 -0.0805 0.0120  310 HOH   A O   
7188 O O   . HOH   D .   ? 0.2150 0.2852 0.3009 0.0050  0.0685  -0.0057 311 HOH   A O   
7189 O O   . HOH   D .   ? 0.5797 0.5724 0.5537 -0.0595 0.2830  -0.1198 312 HOH   A O   
7190 O O   . HOH   D .   ? 0.5530 0.5109 0.6360 -0.0396 0.1668  0.2235  313 HOH   A O   
7191 O O   A HOH   D .   ? 0.2873 0.3712 0.3415 -0.0778 -0.0698 -0.0517 314 HOH   A O   
7192 O O   . HOH   D .   ? 0.2554 0.2638 0.5443 -0.0126 -0.0853 0.1650  315 HOH   A O   
7193 O O   B HOH   D .   ? 0.0988 0.2300 0.1670 0.0103  0.0013  0.0472  316 HOH   A O   
7194 O O   . HOH   D .   ? 0.4506 0.5981 0.3121 0.2459  0.0292  -0.0841 317 HOH   A O   
7195 O O   . HOH   D .   ? 0.3379 0.5955 0.7073 -0.0485 -0.1417 0.2358  318 HOH   A O   
7196 O O   . HOH   D .   ? 0.6492 0.5007 0.5372 -0.1270 0.2206  0.1768  319 HOH   A O   
7197 O O   . HOH   D .   ? 0.6931 0.5339 0.5936 -0.0224 0.2280  0.2585  320 HOH   A O   
7198 O O   . HOH   D .   ? 0.7541 0.6902 0.8101 -0.1087 -0.0399 0.1715  321 HOH   A O   
7199 O O   . HOH   D .   ? 0.5996 0.6651 0.3774 -0.0978 -0.0579 0.1511  322 HOH   A O   
7200 O O   . HOH   D .   ? 0.4737 0.3864 0.5424 -0.0208 0.1901  0.0080  323 HOH   A O   
7201 O O   . HOH   D .   ? 0.2801 0.2468 0.7243 -0.0040 0.1623  -0.0235 324 HOH   A O   
7202 O O   . HOH   D .   ? 0.4962 0.1852 0.4955 0.0877  -0.0790 -0.0142 325 HOH   A O   
7203 O O   . HOH   D .   ? 0.2062 0.1726 0.3476 -0.0419 0.0096  -0.0025 326 HOH   A O   
7204 O O   A HOH   D .   ? 0.4335 0.2822 0.2735 -0.0567 -0.0321 0.0223  327 HOH   A O   
7205 O O   . HOH   D .   ? 0.1738 0.3381 0.2597 0.0299  -0.0154 0.0091  328 HOH   A O   
7206 O O   . HOH   D .   ? 0.1807 0.1552 0.2165 0.0185  -0.0279 0.0078  329 HOH   A O   
7207 O O   . HOH   D .   ? 0.3158 0.3143 0.3008 -0.1181 -0.0257 0.0967  330 HOH   A O   
7208 O O   . HOH   D .   ? 0.2304 0.2044 0.2471 0.0552  0.0284  0.0404  331 HOH   A O   
7209 O O   . HOH   D .   ? 0.8334 0.7122 0.6762 -0.1289 0.0071  -0.0775 332 HOH   A O   
7210 O O   B HOH   D .   ? 0.2182 0.2453 0.3969 0.0406  0.0110  0.0249  333 HOH   A O   
7211 O O   A HOH   D .   ? 0.5021 0.4072 0.4373 -0.1023 0.0771  0.1065  334 HOH   A O   
7212 O O   . HOH   D .   ? 0.2252 0.4112 0.3376 0.0915  -0.0512 -0.0052 335 HOH   A O   
7213 O O   . HOH   D .   ? 0.2036 0.4240 0.3819 -0.0431 -0.0750 0.1508  336 HOH   A O   
7214 O O   . HOH   D .   ? 0.5148 0.4071 0.5411 0.1487  -0.0647 0.0433  337 HOH   A O   
7215 O O   . HOH   D .   ? 0.3023 0.4545 0.6454 0.1236  0.1006  -0.1373 338 HOH   A O   
7216 O O   . HOH   D .   ? 0.5301 0.1626 0.3511 0.0091  -0.0826 0.0552  339 HOH   A O   
7217 O O   A HOH   D .   ? 0.4399 0.5509 0.2725 0.1814  -0.0311 -0.0356 340 HOH   A O   
7218 O O   A HOH   D .   ? 0.1876 0.4027 0.3177 -0.0078 -0.0587 0.0874  341 HOH   A O   
7219 O O   A HOH   D .   ? 0.3065 0.4080 0.3595 0.1297  -0.1246 -0.0368 342 HOH   A O   
7220 O O   . HOH   D .   ? 0.2058 0.2752 0.4819 -0.0267 0.0380  -0.0606 343 HOH   A O   
7221 O O   . HOH   D .   ? 0.1609 0.1473 0.1855 0.0083  -0.0243 0.0184  344 HOH   A O   
7222 O O   . HOH   D .   ? 0.3198 0.3763 0.3988 -0.1494 -0.0961 0.1972  345 HOH   A O   
7223 O O   B HOH   D .   ? 0.2241 0.2336 0.2390 -0.0579 -0.0199 0.0795  346 HOH   A O   
7224 O O   . HOH   D .   ? 0.3635 0.6314 0.2793 0.1494  0.0872  -0.0422 347 HOH   A O   
7225 O O   . HOH   D .   ? 1.1126 1.0036 0.9060 -0.0636 -0.0733 0.0502  348 HOH   A O   
7226 O O   A HOH   D .   ? 0.1612 0.2015 0.1658 -0.0241 -0.0077 -0.0107 349 HOH   A O   
7227 O O   . HOH   D .   ? 0.6556 0.5993 0.4314 0.1637  -0.1257 -0.0679 350 HOH   A O   
7228 O O   . HOH   D .   ? 0.5121 0.3091 0.2912 0.0292  0.0791  0.0765  351 HOH   A O   
7229 O O   . HOH   D .   ? 0.3330 0.3579 0.2203 -0.0999 -0.0264 -0.0696 352 HOH   A O   
7230 O O   . HOH   D .   ? 0.3157 0.4459 0.4219 -0.0926 0.1757  0.0258  353 HOH   A O   
7231 O O   A HOH   D .   ? 0.1247 0.1632 0.3171 0.0135  -0.0693 -0.0224 354 HOH   A O   
7232 O O   . HOH   D .   ? 0.1347 0.2303 0.2153 0.0072  -0.0111 0.0676  355 HOH   A O   
7233 O O   . HOH   D .   ? 0.3049 0.3912 0.2130 -0.0140 0.0746  0.0256  356 HOH   A O   
7234 O O   . HOH   D .   ? 0.4310 0.2733 0.2688 -0.1147 0.0231  0.0549  357 HOH   A O   
7235 O O   . HOH   D .   ? 0.2923 0.2246 0.2547 -0.0509 -0.1071 0.0427  358 HOH   A O   
7236 O O   . HOH   D .   ? 0.6231 0.6616 0.7266 0.0254  -0.0616 0.0568  359 HOH   A O   
7237 O O   . HOH   D .   ? 0.2669 0.4499 0.3134 -0.1321 -0.0360 -0.0103 360 HOH   A O   
7238 O O   . HOH   D .   ? 0.2877 0.4435 0.3440 -0.0311 -0.0781 0.0632  361 HOH   A O   
7239 O O   . HOH   D .   ? 0.3036 0.3424 0.3746 -0.0592 -0.0619 -0.0879 362 HOH   A O   
7240 O O   . HOH   D .   ? 0.1508 0.1565 0.1998 -0.0150 0.0103  0.0314  363 HOH   A O   
7241 O O   A HOH   D .   ? 0.2151 0.2716 0.2411 -0.0174 -0.0130 -0.0267 364 HOH   A O   
7242 O O   . HOH   D .   ? 0.1819 0.1881 0.3574 0.0124  0.0770  -0.0261 365 HOH   A O   
7243 O O   . HOH   D .   ? 0.4222 0.2469 0.3431 -0.1547 0.1545  -0.0711 366 HOH   A O   
7244 O O   . HOH   D .   ? 0.6203 0.7858 0.3726 -0.1266 -0.1195 -0.1039 367 HOH   A O   
7245 O O   . HOH   D .   ? 0.1790 0.1681 0.2253 -0.0251 0.0135  0.0231  368 HOH   A O   
7246 O O   . HOH   D .   ? 0.1786 0.5519 0.2889 -0.0519 0.0248  0.0293  369 HOH   A O   
7247 O O   . HOH   D .   ? 0.3085 0.4258 0.3377 -0.0787 0.0557  -0.0340 370 HOH   A O   
7248 O O   . HOH   D .   ? 0.1329 0.1809 0.2574 0.0051  -0.0060 0.0036  371 HOH   A O   
7249 O O   . HOH   D .   ? 0.1809 0.2360 0.3094 0.0361  0.0624  -0.0248 372 HOH   A O   
7250 O O   . HOH   D .   ? 0.4237 0.7195 0.6793 -0.1022 -0.1345 -0.0462 373 HOH   A O   
7251 O O   . HOH   D .   ? 0.1308 0.1503 0.1457 -0.0055 -0.0152 0.0037  374 HOH   A O   
7252 O O   . HOH   D .   ? 0.1438 0.1239 0.1994 -0.0048 0.0249  -0.0006 375 HOH   A O   
7253 O O   B HOH   D .   ? 0.1252 0.1534 0.2131 -0.0033 0.0022  0.0578  376 HOH   A O   
7254 O O   . HOH   D .   ? 0.1750 0.2152 0.2104 -0.0145 -0.0439 0.0417  377 HOH   A O   
7255 O O   . HOH   D .   ? 0.1322 0.1322 0.1573 -0.0062 0.0069  0.0165  378 HOH   A O   
7256 O O   . HOH   D .   ? 0.3995 0.2108 0.4051 -0.1089 0.0828  0.0193  379 HOH   A O   
7257 O O   . HOH   D .   ? 0.8658 0.6103 0.7396 -0.0729 -0.1014 0.1073  380 HOH   A O   
7258 O O   . HOH   D .   ? 0.3246 0.2716 0.2119 0.0624  0.0636  0.0330  381 HOH   A O   
7259 O O   . HOH   D .   ? 0.3311 0.4946 0.3279 0.1756  0.0818  0.0954  382 HOH   A O   
7260 O O   B HOH   D .   ? 0.3218 0.3126 0.3571 0.0527  -0.0601 0.0050  383 HOH   A O   
7261 O O   . HOH   D .   ? 0.1648 0.1356 0.1542 -0.0215 0.0162  0.0048  384 HOH   A O   
7262 O O   . HOH   D .   ? 0.3413 0.2243 0.5030 -0.0748 0.0143  -0.0090 385 HOH   A O   
7263 O O   . HOH   D .   ? 0.2579 0.4459 0.3399 0.0920  0.1018  0.2116  386 HOH   A O   
7264 O O   B HOH   D .   ? 0.1798 0.1242 0.2458 0.0101  -0.0518 0.0065  387 HOH   A O   
7265 O O   A HOH   D .   ? 0.1471 0.1860 0.2653 -0.0178 0.0415  0.0687  388 HOH   A O   
7266 O O   B HOH   D .   ? 0.1572 0.1378 0.2177 -0.0258 -0.0148 0.0256  389 HOH   A O   
7267 O O   . HOH   D .   ? 0.4025 0.3162 0.3500 -0.0839 -0.0224 -0.0014 390 HOH   A O   
7268 O O   . HOH   D .   ? 0.2657 0.1834 0.2516 -0.0273 0.0282  0.0233  391 HOH   A O   
7269 O O   . HOH   D .   ? 0.1890 0.2003 0.2636 -0.0148 -0.0065 0.0897  392 HOH   A O   
7270 O O   A HOH   D .   ? 0.1125 0.1820 0.2679 0.0174  0.0618  0.0955  393 HOH   A O   
7271 O O   . HOH   D .   ? 0.2835 0.3259 0.4234 -0.1013 0.1419  -0.0313 394 HOH   A O   
7272 O O   A HOH   D .   ? 0.2364 0.4365 0.3914 0.0701  0.0082  0.1122  395 HOH   A O   
7273 O O   . HOH   D .   ? 0.2119 0.1759 0.1755 -0.0329 0.0179  0.0246  396 HOH   A O   
7274 O O   B HOH   D .   ? 0.3647 0.1679 0.2999 0.0065  -0.0804 0.0497  397 HOH   A O   
7275 O O   . HOH   D .   ? 0.1275 0.1306 0.1714 0.0017  -0.0199 0.0031  398 HOH   A O   
7276 O O   . HOH   D .   ? 0.6244 0.4913 0.3645 -0.0583 -0.1595 -0.0027 399 HOH   A O   
7277 O O   . HOH   D .   ? 0.2030 0.5445 0.4380 0.0411  0.0257  0.0337  400 HOH   A O   
7278 O O   . HOH   D .   ? 0.2129 0.1591 0.1582 -0.0139 0.0036  0.0192  401 HOH   A O   
7279 O O   . HOH   D .   ? 0.4524 0.5594 0.1832 0.0156  0.0567  0.0682  402 HOH   A O   
7280 O O   . HOH   D .   ? 0.1698 0.1817 0.4182 0.0371  0.1084  0.1116  403 HOH   A O   
7281 O O   B HOH   D .   ? 0.4363 0.4160 0.4150 0.1289  -0.0218 -0.0872 404 HOH   A O   
7282 O O   . HOH   D .   ? 0.2102 0.1593 0.2674 0.0135  -0.0317 0.0014  405 HOH   A O   
7283 O O   A HOH   D .   ? 0.4291 0.3169 0.2526 -0.0963 0.0392  0.0763  406 HOH   A O   
7284 O O   A HOH   D .   ? 0.1209 0.1024 0.0893 0.0072  -0.0034 0.0200  407 HOH   A O   
7285 O O   . HOH   D .   ? 0.2214 0.4236 0.3398 -0.0523 0.1062  -0.0915 408 HOH   A O   
7286 O O   . HOH   D .   ? 0.3142 0.2322 0.3115 -0.0055 -0.0482 0.0890  409 HOH   A O   
7287 O O   A HOH   D .   ? 0.4236 0.5112 0.3940 -0.0983 0.0402  0.0203  410 HOH   A O   
7288 O O   . HOH   D .   ? 0.2447 0.1985 0.2312 -0.0465 -0.0110 0.0527  411 HOH   A O   
7289 O O   . HOH   D .   ? 0.3688 0.2979 0.5666 -0.0002 -0.0682 -0.0551 412 HOH   A O   
7290 O O   . HOH   D .   ? 0.1941 0.2024 0.1912 -0.0262 0.0090  0.0195  413 HOH   A O   
7291 O O   A HOH   D .   ? 0.1983 0.3392 0.1476 0.1384  0.0414  0.0751  414 HOH   A O   
7292 O O   . HOH   D .   ? 0.1813 0.2491 0.2712 -0.0304 -0.0014 0.0329  415 HOH   A O   
7293 O O   . HOH   D .   ? 0.3273 0.5118 0.3520 0.0004  0.0167  0.0790  416 HOH   A O   
7294 O O   . HOH   D .   ? 0.2121 0.3777 0.7451 -0.0491 0.0162  -0.0116 417 HOH   A O   
7295 O O   . HOH   D .   ? 0.1932 0.2453 0.2574 0.0009  -0.0481 0.0433  418 HOH   A O   
7296 O O   . HOH   D .   ? 0.4696 0.4024 0.4065 0.1563  -0.1096 -0.1762 419 HOH   A O   
7297 O O   A HOH   D .   ? 0.1658 0.2108 0.2924 0.0417  -0.0840 -0.0465 420 HOH   A O   
7298 O O   A HOH   D .   ? 0.4580 0.4354 0.3954 -0.0833 0.0036  -0.0351 421 HOH   A O   
7299 O O   . HOH   D .   ? 0.4069 0.7325 0.3035 -0.1196 -0.0198 0.1321  422 HOH   A O   
7300 O O   . HOH   D .   ? 0.3772 0.2842 0.2625 -0.0133 0.0203  0.0403  423 HOH   A O   
7301 O O   . HOH   D .   ? 0.5476 0.7493 0.4053 0.0514  0.2656  -0.0588 424 HOH   A O   
7302 O O   . HOH   D .   ? 0.4038 0.2244 0.5398 -0.0655 -0.2250 0.1165  425 HOH   A O   
7303 O O   . HOH   D .   ? 0.3712 0.1208 0.1904 -0.0084 -0.0688 0.0116  426 HOH   A O   
7304 O O   . HOH   D .   ? 0.2771 0.5437 0.1643 -0.0228 0.0598  0.0205  427 HOH   A O   
7305 O O   . HOH   D .   ? 0.1680 0.2443 0.4026 -0.0061 -0.0232 0.0463  428 HOH   A O   
7306 O O   . HOH   D .   ? 0.2424 0.4173 0.2619 0.1767  0.0019  0.0207  429 HOH   A O   
7307 O O   . HOH   D .   ? 0.1493 0.1573 0.2819 -0.0018 0.0099  0.0245  430 HOH   A O   
7308 O O   . HOH   D .   ? 0.1652 0.1496 0.2267 0.0173  -0.0281 0.0248  431 HOH   A O   
7309 O O   . HOH   D .   ? 0.4811 0.6574 0.4016 0.1925  -0.0555 -0.0532 432 HOH   A O   
7310 O O   A HOH   D .   ? 0.1587 0.3484 0.3089 0.0222  0.0527  0.1120  433 HOH   A O   
7311 O O   . HOH   D .   ? 0.3535 0.3603 0.5883 0.0433  0.0799  -0.0696 434 HOH   A O   
7312 O O   . HOH   D .   ? 0.5443 0.5984 0.6272 0.0129  -0.0487 -0.0001 435 HOH   A O   
7313 O O   . HOH   D .   ? 0.1919 0.2109 0.4314 -0.0286 -0.0898 0.0373  436 HOH   A O   
7314 O O   A HOH   D .   ? 0.2514 0.2395 0.2635 0.0366  0.0431  0.0824  437 HOH   A O   
7315 O O   A HOH   D .   ? 0.1241 0.1650 0.1748 0.0066  0.0142  -0.0556 438 HOH   A O   
7316 O O   . HOH   D .   ? 0.6661 0.6401 0.6811 0.3323  0.1335  0.1566  439 HOH   A O   
7317 O O   . HOH   D .   ? 0.3600 0.2330 0.1699 -0.0828 0.0349  0.0404  440 HOH   A O   
7318 O O   . HOH   D .   ? 0.6897 0.6948 0.6229 -0.1013 0.1407  0.2641  441 HOH   A O   
7319 O O   . HOH   D .   ? 0.3784 0.5390 0.4382 0.0466  -0.0840 -0.1371 442 HOH   A O   
7320 O O   . HOH   D .   ? 0.2357 0.1481 0.2649 0.0099  0.0019  0.0137  443 HOH   A O   
7321 O O   . HOH   D .   ? 0.8442 0.7574 0.8460 0.0263  0.0264  0.0071  444 HOH   A O   
7322 O O   . HOH   D .   ? 0.6405 0.4165 0.4534 0.1730  -0.0600 0.1326  445 HOH   A O   
7323 O O   B HOH   D .   ? 0.1752 0.2388 0.2120 -0.0285 0.0008  0.0031  446 HOH   A O   
7324 O O   . HOH   D .   ? 0.4615 0.3317 0.3085 0.2244  -0.0670 -0.0326 447 HOH   A O   
7325 O O   A HOH   D .   ? 0.5406 0.4287 0.5184 0.0972  0.0172  -0.0429 448 HOH   A O   
7326 O O   B HOH   D .   ? 0.4384 0.4916 0.4976 0.0841  -0.1219 0.0650  449 HOH   A O   
7327 O O   . HOH   D .   ? 0.2196 0.2306 0.2457 0.0190  0.0219  0.0651  450 HOH   A O   
7328 O O   . HOH   D .   ? 0.2129 0.4600 0.5616 0.0285  0.0554  -0.1983 451 HOH   A O   
7329 O O   . HOH   D .   ? 0.1896 0.2804 0.2474 -0.0014 0.0038  -0.0475 452 HOH   A O   
7330 O O   A HOH   D .   ? 0.4990 0.2395 0.3043 0.1009  -0.1252 -0.0574 453 HOH   A O   
7331 O O   . HOH   D .   ? 0.7234 0.6330 0.6243 -0.1224 0.1065  -0.1249 454 HOH   A O   
7332 O O   . HOH   D .   ? 0.6231 0.6556 0.6614 -0.1243 -0.0967 -0.1216 455 HOH   A O   
7333 O O   . HOH   D .   ? 0.5296 0.6184 0.7852 0.0708  -0.1011 0.1721  456 HOH   A O   
7334 O O   . HOH   D .   ? 0.8509 0.9391 0.6277 0.2786  -0.1365 0.1822  457 HOH   A O   
7335 O O   . HOH   D .   ? 0.4313 0.3706 0.4415 0.1089  0.1629  -0.0009 458 HOH   A O   
7336 O O   A HOH   D .   ? 0.5611 0.3992 0.3922 0.0899  0.1076  0.1484  459 HOH   A O   
7337 O O   B HOH   D .   ? 0.2976 0.3778 0.4623 -0.0983 0.0137  0.0282  460 HOH   A O   
7338 O O   . HOH   D .   ? 0.2966 0.3080 0.3367 -0.0740 0.0506  -0.0765 461 HOH   A O   
7339 O O   . HOH   D .   ? 0.4246 0.4962 0.4918 -0.0206 -0.0148 0.1509  462 HOH   A O   
7340 O O   . HOH   D .   ? 0.2615 0.2643 0.3839 0.0628  -0.0444 0.0116  463 HOH   A O   
7341 O O   . HOH   D .   ? 0.4488 0.3358 0.4045 0.0377  0.0382  0.0260  464 HOH   A O   
7342 O O   . HOH   D .   ? 0.4874 0.4555 0.4517 -0.0463 -0.0019 0.0137  465 HOH   A O   
7343 O O   . HOH   D .   ? 0.8936 0.8193 0.5522 -0.0235 -0.0926 -0.0110 466 HOH   A O   
7344 O O   . HOH   D .   ? 0.3115 0.4053 0.4796 0.0337  -0.1809 0.0860  467 HOH   A O   
7345 O O   . HOH   D .   ? 0.3001 0.5600 0.4822 -0.1429 0.0781  -0.0674 468 HOH   A O   
7346 O O   B HOH   D .   ? 0.1177 0.1259 0.2149 -0.0190 -0.0261 0.0394  469 HOH   A O   
7347 O O   . HOH   D .   ? 0.6630 0.6441 0.6146 0.1494  0.1837  0.1804  470 HOH   A O   
7348 O O   . HOH   D .   ? 0.3805 0.4479 0.3142 -0.1540 0.0022  0.0235  471 HOH   A O   
7349 O O   . HOH   D .   ? 0.2414 0.4908 0.3862 0.0557  -0.0205 -0.2133 472 HOH   A O   
7350 O O   B HOH   D .   ? 0.1500 0.1140 0.1658 -0.0276 0.0068  0.0027  473 HOH   A O   
7351 O O   B HOH   D .   ? 0.2298 0.2007 0.2417 0.0195  -0.0239 -0.0048 474 HOH   A O   
7352 O O   . HOH   D .   ? 0.5010 0.3064 0.6999 0.0249  0.1847  0.1938  475 HOH   A O   
7353 O O   . HOH   D .   ? 0.2647 0.1664 0.2608 0.0491  -0.0955 -0.0398 476 HOH   A O   
7354 O O   . HOH   D .   ? 0.2539 0.2206 0.3075 -0.0656 0.0384  -0.0154 477 HOH   A O   
7355 O O   . HOH   D .   ? 0.3789 0.5797 0.4326 -0.0446 -0.1001 0.2012  478 HOH   A O   
7356 O O   . HOH   D .   ? 0.2747 0.2989 0.2744 0.0013  0.0328  0.0168  479 HOH   A O   
7357 O O   . HOH   D .   ? 0.4253 0.5091 0.3939 0.0491  -0.0945 -0.0939 480 HOH   A O   
7358 O O   . HOH   D .   ? 0.6119 0.6222 0.4783 0.1892  -0.1117 -0.0974 481 HOH   A O   
7359 O O   . HOH   D .   ? 0.5807 0.4697 0.4547 -0.0548 0.1475  0.0020  482 HOH   A O   
7360 O O   B HOH   D .   ? 0.3319 0.3148 0.2542 0.0072  -0.0944 0.0648  483 HOH   A O   
7361 O O   . HOH   D .   ? 0.5690 0.7500 0.5692 -0.1500 -0.1375 0.0095  484 HOH   A O   
7362 O O   A HOH   D .   ? 0.2977 0.3289 0.4638 -0.0599 -0.0988 -0.0389 485 HOH   A O   
7363 O O   A HOH   D .   ? 0.2170 0.2940 0.1480 0.0831  0.0356  0.0415  486 HOH   A O   
7364 O O   . HOH   D .   ? 0.4556 0.4439 0.5095 -0.2156 -0.0240 -0.0418 487 HOH   A O   
7365 O O   B HOH   D .   ? 0.2014 0.4081 0.3905 -0.0441 -0.0610 -0.1060 488 HOH   A O   
7366 O O   . HOH   D .   ? 0.4548 0.2685 0.3840 -0.0809 -0.0775 0.0567  489 HOH   A O   
7367 O O   . HOH   D .   ? 0.6276 0.3680 0.5131 -0.0364 0.1107  0.0311  490 HOH   A O   
7368 O O   . HOH   D .   ? 0.5226 0.4757 0.2922 -0.0348 -0.0655 0.0615  491 HOH   A O   
7369 O O   . HOH   D .   ? 0.5593 0.5175 0.6736 -0.1222 0.0354  -0.0572 492 HOH   A O   
7370 O O   . HOH   D .   ? 0.7997 0.3696 0.3237 -0.0329 -0.1267 0.0053  493 HOH   A O   
7371 O O   . HOH   D .   ? 0.4725 0.4171 0.4675 0.0093  -0.0566 -0.0930 494 HOH   A O   
7372 O O   . HOH   D .   ? 0.4478 0.4391 0.4366 0.0147  0.2044  0.1269  495 HOH   A O   
7373 O O   . HOH   D .   ? 0.7109 0.6745 0.5082 -0.0276 0.2137  0.0866  496 HOH   A O   
7374 O O   . HOH   D .   ? 0.2684 0.2192 0.6921 0.0107  -0.1144 -0.0010 497 HOH   A O   
7375 O O   . HOH   D .   ? 0.2993 0.5095 0.3500 -0.0171 -0.0426 -0.0247 498 HOH   A O   
7376 O O   . HOH   D .   ? 0.2615 0.4995 0.3802 0.1117  0.0917  0.2479  499 HOH   A O   
7377 O O   . HOH   D .   ? 0.5859 0.6529 0.7885 0.0571  0.1428  -0.1218 500 HOH   A O   
7378 O O   . HOH   D .   ? 0.3874 0.3026 0.2280 -0.0726 0.1055  -0.0208 501 HOH   A O   
7379 O O   . HOH   D .   ? 0.2861 0.2265 0.4705 0.0247  0.0570  -0.0327 502 HOH   A O   
7380 O O   . HOH   D .   ? 0.5746 0.4193 0.4435 -0.0898 0.1408  0.1067  503 HOH   A O   
7381 O O   . HOH   D .   ? 0.4566 0.6434 0.5022 -0.0484 -0.0907 0.0339  504 HOH   A O   
7382 O O   . HOH   D .   ? 0.2712 0.1815 0.5450 -0.0029 0.0735  0.0452  505 HOH   A O   
7383 O O   . HOH   D .   ? 0.4966 0.3070 0.3848 -0.0524 0.1971  0.0139  506 HOH   A O   
7384 O O   . HOH   D .   ? 0.6039 0.2625 0.4791 -0.0814 0.0796  0.0594  507 HOH   A O   
7385 O O   . HOH   D .   ? 0.4754 0.2216 0.4420 -0.1294 0.0538  -0.0150 508 HOH   A O   
7386 O O   B HOH   D .   ? 0.2196 0.2550 0.1957 0.0751  0.0306  0.0378  509 HOH   A O   
7387 O O   . HOH   D .   ? 0.2612 0.4470 0.4847 -0.0049 -0.1043 0.0004  510 HOH   A O   
7388 O O   . HOH   D .   ? 0.4597 0.8903 0.5929 -0.1008 -0.0051 0.1588  511 HOH   A O   
7389 O O   . HOH   D .   ? 0.2205 0.2829 0.3306 0.0109  -0.0376 0.0558  512 HOH   A O   
7390 O O   B HOH   D .   ? 0.3099 0.4374 0.3008 -0.1099 0.0662  -0.0558 513 HOH   A O   
7391 O O   . HOH   D .   ? 0.5227 0.7101 0.5833 0.1031  0.0304  0.1817  514 HOH   A O   
7392 O O   . HOH   D .   ? 0.4816 0.4238 0.3897 0.0097  -0.1044 0.1864  515 HOH   A O   
7393 O O   A HOH   D .   ? 0.3205 0.4962 0.4574 0.1205  -0.0706 0.1639  516 HOH   A O   
7394 O O   . HOH   D .   ? 0.5541 0.6510 0.4102 0.3271  -0.0631 0.0532  517 HOH   A O   
7395 O O   . HOH   D .   ? 0.3188 0.1992 0.4456 -0.0024 0.0513  0.0380  518 HOH   A O   
7396 O O   B HOH   D .   ? 0.4635 0.2264 0.3769 -0.0718 0.1263  -0.0091 519 HOH   A O   
7397 O O   . HOH   D .   ? 0.5473 0.7795 0.4401 -0.0978 -0.1045 -0.1102 520 HOH   A O   
7398 O O   B HOH   D .   ? 0.4339 0.4169 0.4621 -0.0124 -0.0121 0.1930  521 HOH   A O   
7399 O O   A HOH   D .   ? 0.2769 0.4085 0.1899 0.0759  -0.0815 -0.0553 522 HOH   A O   
7400 O O   . HOH   D .   ? 0.3612 0.7097 0.4380 0.1597  0.0082  -0.0483 523 HOH   A O   
7401 O O   . HOH   D .   ? 0.6209 0.5132 0.5493 0.0780  0.1508  0.0916  524 HOH   A O   
7402 O O   . HOH   D .   ? 0.5613 0.7162 0.5298 0.0084  0.0359  0.1973  525 HOH   A O   
7403 O O   B HOH   D .   ? 0.2477 0.3846 0.3092 0.0068  -0.0263 0.0520  526 HOH   A O   
7404 O O   . HOH   D .   ? 0.3667 0.4463 0.5007 -0.0861 -0.0148 0.2494  527 HOH   A O   
7405 O O   . HOH   E .   ? 0.2235 0.1925 0.2942 0.0231  0.0806  0.0262  201 HOH   B O   
7406 O O   . HOH   E .   ? 0.3597 0.3071 0.6837 -0.0521 0.1002  -0.0023 202 HOH   B O   
7407 O O   . HOH   E .   ? 0.4677 0.3720 0.3952 -0.0559 -0.0263 -0.1582 203 HOH   B O   
7408 O O   . HOH   E .   ? 0.2758 0.6111 0.5605 0.0064  0.1598  -0.1554 204 HOH   B O   
7409 O O   . HOH   E .   ? 0.2527 0.6408 0.3921 0.0629  -0.0161 0.2400  205 HOH   B O   
7410 O O   . HOH   E .   ? 0.6304 0.5973 0.5292 0.2398  0.0168  0.0366  206 HOH   B O   
7411 O O   . HOH   E .   ? 0.3193 0.1957 0.4773 0.0208  0.1951  0.0821  207 HOH   B O   
7412 O O   . HOH   E .   ? 0.5667 0.3675 0.6127 -0.0002 -0.1217 0.2468  208 HOH   B O   
7413 O O   . HOH   E .   ? 0.5066 0.5820 0.3226 0.3215  -0.0611 -0.0628 209 HOH   B O   
7414 O O   . HOH   E .   ? 0.7967 0.3819 0.4611 -0.0382 0.1332  0.0214  210 HOH   B O   
7415 O O   . HOH   E .   ? 0.2063 0.2276 0.2820 0.0138  0.0248  -0.0540 211 HOH   B O   
7416 O O   . HOH   E .   ? 0.4707 0.5316 0.2135 0.0584  -0.0168 -0.0997 212 HOH   B O   
7417 O O   . HOH   E .   ? 0.5302 0.4436 0.3946 0.0562  0.1194  -0.1509 213 HOH   B O   
7418 O O   . HOH   E .   ? 0.1619 0.1898 0.2598 -0.0265 -0.0053 0.0210  214 HOH   B O   
7419 O O   . HOH   E .   ? 0.4498 0.4172 0.5127 0.0209  -0.0650 0.0010  215 HOH   B O   
7420 O O   . HOH   E .   ? 0.3409 0.4215 0.2921 0.0404  -0.1020 0.0542  216 HOH   B O   
7421 O O   . HOH   E .   ? 0.3772 0.2323 0.3982 0.0793  0.0005  -0.0344 217 HOH   B O   
7422 O O   . HOH   E .   ? 0.1760 0.1942 0.2840 -0.0244 0.0186  -0.0163 218 HOH   B O   
7423 O O   . HOH   E .   ? 0.6084 0.3858 0.2748 -0.0583 -0.0143 0.0256  219 HOH   B O   
7424 O O   . HOH   E .   ? 0.3132 0.4200 0.4067 0.1403  -0.0046 -0.0273 220 HOH   B O   
7425 O O   . HOH   E .   ? 0.3864 0.3771 0.5130 -0.1212 -0.0359 0.0873  221 HOH   B O   
7426 O O   . HOH   E .   ? 0.1461 0.1416 0.2096 -0.0228 0.0104  0.0017  222 HOH   B O   
7427 O O   . HOH   E .   ? 0.2658 0.2718 0.5420 0.0676  -0.0602 0.0547  223 HOH   B O   
7428 O O   . HOH   E .   ? 0.3477 0.4030 0.5006 -0.1202 -0.0201 -0.1439 224 HOH   B O   
7429 O O   . HOH   E .   ? 0.3134 0.2146 0.4906 0.0029  0.1847  0.0211  225 HOH   B O   
7430 O O   . HOH   E .   ? 0.2497 0.1685 0.2733 -0.0206 0.1150  -0.0014 226 HOH   B O   
7431 O O   . HOH   E .   ? 0.3778 0.6000 0.4823 0.2569  0.0183  -0.0848 227 HOH   B O   
7432 O O   . HOH   E .   ? 0.4016 0.2008 0.2020 0.1192  0.0355  0.0258  228 HOH   B O   
7433 O O   . HOH   E .   ? 0.2099 0.2173 0.3918 -0.0304 0.0204  -0.0577 229 HOH   B O   
7434 O O   . HOH   E .   ? 0.4788 0.1892 0.3076 0.0037  -0.0816 0.0108  230 HOH   B O   
7435 O O   . HOH   E .   ? 0.3520 0.2436 0.4056 -0.0044 -0.0408 -0.1315 231 HOH   B O   
7436 O O   . HOH   E .   ? 0.5478 0.2967 0.4483 -0.1855 -0.0378 -0.0294 232 HOH   B O   
7437 O O   . HOH   E .   ? 0.1950 0.3679 0.3201 -0.0477 -0.0478 -0.0676 233 HOH   B O   
7438 O O   . HOH   E .   ? 0.2858 0.1662 0.5999 -0.0038 -0.1292 -0.0314 234 HOH   B O   
7439 O O   . HOH   E .   ? 0.3727 0.1738 0.1709 0.0188  -0.0845 -0.0184 235 HOH   B O   
7440 O O   . HOH   E .   ? 0.2581 0.3400 0.2959 -0.0710 0.0569  -0.0914 236 HOH   B O   
7441 O O   . HOH   E .   ? 0.2171 0.1242 0.3077 0.0047  -0.0584 -0.0104 237 HOH   B O   
7442 O O   . HOH   E .   ? 0.3239 0.3149 0.2170 0.0452  0.0678  0.0492  238 HOH   B O   
7443 O O   . HOH   E .   ? 0.2314 0.2235 0.2375 0.0825  -0.0802 -0.0676 239 HOH   B O   
7444 O O   . HOH   E .   ? 0.5321 0.4535 0.4290 0.1002  0.0239  -0.0311 240 HOH   B O   
7445 O O   . HOH   E .   ? 0.2096 0.3718 0.2148 -0.0423 -0.0061 0.0530  241 HOH   B O   
7446 O O   . HOH   E .   ? 0.2288 0.2561 0.2839 0.0090  0.0387  -0.0768 242 HOH   B O   
7447 O O   . HOH   E .   ? 0.2039 0.1781 0.1970 -0.0215 -0.0419 0.0100  243 HOH   B O   
7448 O O   . HOH   E .   ? 0.1404 0.1378 0.1409 -0.0102 -0.0049 -0.0045 244 HOH   B O   
7449 O O   . HOH   E .   ? 0.6036 0.5901 0.3053 0.1173  0.0948  0.0003  245 HOH   B O   
7450 O O   . HOH   E .   ? 0.5316 0.2952 0.3631 -0.2135 0.0567  -0.0067 246 HOH   B O   
7451 O O   . HOH   E .   ? 0.2398 0.2126 0.1938 0.0226  -0.0155 0.0044  247 HOH   B O   
7452 O O   . HOH   E .   ? 0.2380 0.2648 0.2806 -0.0805 0.0209  -0.0180 248 HOH   B O   
7453 O O   . HOH   E .   ? 0.1494 0.1403 0.2601 -0.0086 0.0135  -0.0084 249 HOH   B O   
7454 O O   . HOH   E .   ? 0.2833 0.4040 0.5019 0.1481  -0.0621 -0.1032 250 HOH   B O   
7455 O O   . HOH   E .   ? 0.2939 0.2474 0.2774 0.1024  0.0926  0.0132  251 HOH   B O   
7456 O O   . HOH   E .   ? 0.1715 0.2638 0.2413 0.0346  0.0358  0.0959  252 HOH   B O   
7457 O O   . HOH   E .   ? 0.2061 0.1501 0.1776 -0.0285 -0.0355 0.0236  253 HOH   B O   
7458 O O   . HOH   E .   ? 0.2125 0.2898 0.2212 -0.0483 0.0226  0.0462  254 HOH   B O   
7459 O O   . HOH   E .   ? 0.2479 0.4302 0.2700 -0.0806 -0.0325 -0.0632 255 HOH   B O   
7460 O O   . HOH   E .   ? 0.4842 0.6608 0.3904 0.2712  0.0762  0.0574  256 HOH   B O   
7461 O O   . HOH   E .   ? 0.1429 0.1272 0.1479 0.0012  0.0006  0.0087  257 HOH   B O   
7462 O O   . HOH   E .   ? 0.3166 0.4691 0.6101 0.0628  0.1108  0.0554  258 HOH   B O   
7463 O O   . HOH   E .   ? 0.2155 0.4968 0.4273 -0.0867 -0.0344 -0.1285 259 HOH   B O   
7464 O O   . HOH   E .   ? 0.2366 0.1966 0.2626 -0.0424 0.0166  -0.0022 260 HOH   B O   
7465 O O   . HOH   E .   ? 0.4203 0.3270 0.2187 0.0118  0.1338  0.0041  261 HOH   B O   
7466 O O   . HOH   E .   ? 0.1278 0.1472 0.1966 -0.0068 0.0047  0.0139  262 HOH   B O   
7467 O O   . HOH   E .   ? 0.1571 0.1718 0.2845 -0.0300 -0.0131 0.0121  263 HOH   B O   
7468 O O   . HOH   E .   ? 0.4221 0.4180 0.6302 0.0077  -0.1493 -0.1394 264 HOH   B O   
7469 O O   . HOH   E .   ? 0.3241 0.2511 0.2855 -0.0534 0.0248  -0.0535 265 HOH   B O   
7470 O O   . HOH   E .   ? 0.3652 0.2851 0.3798 -0.0550 -0.0838 -0.0345 266 HOH   B O   
7471 O O   . HOH   E .   ? 0.6012 0.5279 0.4750 0.2492  -0.0563 0.0260  267 HOH   B O   
7472 O O   . HOH   E .   ? 0.1630 0.1344 0.4685 -0.0059 -0.0311 -0.0172 268 HOH   B O   
7473 O O   . HOH   E .   ? 0.2217 0.1872 0.1788 0.0236  0.0081  0.0008  269 HOH   B O   
7474 O O   . HOH   E .   ? 0.2964 0.4789 0.2774 -0.0363 -0.0615 0.0792  270 HOH   B O   
7475 O O   . HOH   E .   ? 0.2120 0.3153 0.2792 -0.0359 0.0400  -0.1003 271 HOH   B O   
7476 O O   . HOH   E .   ? 0.4812 0.2562 0.4009 -0.0253 -0.0732 -0.1077 272 HOH   B O   
7477 O O   . HOH   E .   ? 0.2020 0.1487 0.2234 -0.0299 -0.0167 0.0169  273 HOH   B O   
7478 O O   . HOH   E .   ? 0.1978 0.1866 0.4203 0.0126  -0.0564 -0.0542 274 HOH   B O   
7479 O O   . HOH   E .   ? 0.2179 0.2379 0.2509 0.0618  -0.0504 -0.0296 275 HOH   B O   
7480 O O   . HOH   E .   ? 0.2092 0.2727 0.2211 -0.0506 -0.0493 -0.0379 276 HOH   B O   
7481 O O   . HOH   E .   ? 0.4000 0.5138 0.4261 0.0277  -0.1623 -0.0121 277 HOH   B O   
7482 O O   . HOH   E .   ? 0.2787 0.3907 0.4209 0.0232  0.1669  0.0231  278 HOH   B O   
7483 O O   . HOH   E .   ? 0.2352 0.2526 0.2206 -0.0270 -0.0685 0.0187  279 HOH   B O   
7484 O O   . HOH   E .   ? 0.2567 0.4345 0.5158 -0.1051 -0.1349 0.0807  280 HOH   B O   
7485 O O   . HOH   E .   ? 0.1862 0.1705 0.1663 -0.0492 -0.0413 0.0117  281 HOH   B O   
7486 O O   . HOH   E .   ? 0.3422 0.2648 0.1804 0.0448  -0.0654 0.0011  282 HOH   B O   
7487 O O   . HOH   E .   ? 0.4463 0.3669 0.3171 0.0517  0.0009  -0.1176 283 HOH   B O   
7488 O O   . HOH   E .   ? 0.3720 0.1872 0.3771 -0.0549 -0.2007 0.0535  284 HOH   B O   
7489 O O   . HOH   E .   ? 0.1642 0.1920 0.2794 0.0208  0.0056  -0.0048 285 HOH   B O   
7490 O O   . HOH   E .   ? 0.3109 0.6259 0.7271 0.1165  -0.0019 -0.1021 286 HOH   B O   
7491 O O   . HOH   E .   ? 0.3936 0.3716 0.4458 0.1488  -0.0698 -0.1145 287 HOH   B O   
7492 O O   . HOH   E .   ? 0.2653 0.6796 0.2206 0.1227  -0.0410 -0.0916 288 HOH   B O   
7493 O O   . HOH   E .   ? 0.3090 0.4013 0.5560 0.0318  0.0181  -0.1000 289 HOH   B O   
7494 O O   . HOH   E .   ? 0.1647 0.1450 0.1761 -0.0016 0.0144  0.0010  290 HOH   B O   
7495 O O   . HOH   E .   ? 0.1531 0.1950 0.1488 -0.0092 -0.0067 0.0090  291 HOH   B O   
7496 O O   . HOH   E .   ? 0.2494 0.2554 0.2648 0.0154  -0.0630 0.0230  292 HOH   B O   
7497 O O   . HOH   E .   ? 0.1549 0.1476 0.3083 -0.0143 0.0174  -0.0103 293 HOH   B O   
7498 O O   . HOH   E .   ? 0.5418 0.6093 0.2691 0.0874  -0.0784 0.0054  294 HOH   B O   
7499 O O   . HOH   E .   ? 0.3285 0.5485 0.3226 0.1970  -0.0636 -0.0456 295 HOH   B O   
7500 O O   . HOH   E .   ? 0.4583 0.5071 0.2281 0.0247  0.1079  0.1146  296 HOH   B O   
7501 O O   . HOH   E .   ? 0.5459 0.3404 0.5175 0.0286  0.1764  -0.1529 297 HOH   B O   
7502 O O   . HOH   E .   ? 0.2770 0.2010 0.4962 0.0244  0.0783  0.0487  298 HOH   B O   
7503 O O   . HOH   E .   ? 0.1718 0.3208 0.4899 0.0180  -0.0017 -0.1366 299 HOH   B O   
7504 O O   . HOH   E .   ? 0.4266 0.3330 0.3609 -0.1088 0.1032  -0.0618 300 HOH   B O   
7505 O O   . HOH   E .   ? 0.1558 0.1389 0.3043 0.0047  0.0092  0.0015  301 HOH   B O   
7506 O O   . HOH   E .   ? 0.4080 0.2563 0.2267 -0.1426 0.0564  -0.0177 302 HOH   B O   
7507 O O   . HOH   E .   ? 0.2210 0.3060 0.5790 0.0830  -0.0654 -0.1295 303 HOH   B O   
7508 O O   . HOH   E .   ? 0.2938 0.2838 0.2880 -0.0274 0.0393  -0.1177 304 HOH   B O   
7509 O O   . HOH   E .   ? 0.3295 0.3612 0.4534 -0.1197 0.1581  -0.0850 305 HOH   B O   
7510 O O   . HOH   E .   ? 0.4200 0.4029 0.2222 0.1035  -0.0587 0.0920  306 HOH   B O   
7511 O O   . HOH   E .   ? 0.2132 0.1667 0.2400 -0.0289 -0.0187 -0.0090 307 HOH   B O   
7512 O O   . HOH   E .   ? 0.2172 0.3413 0.5062 -0.0192 -0.0958 -0.0385 308 HOH   B O   
7513 O O   . HOH   E .   ? 0.3274 0.1678 0.3390 0.0550  0.1256  0.0367  309 HOH   B O   
7514 O O   . HOH   E .   ? 0.2859 0.2980 0.5978 -0.0687 -0.1867 0.1818  310 HOH   B O   
7515 O O   . HOH   E .   ? 0.1775 0.1578 0.2301 0.0151  0.0121  0.0288  311 HOH   B O   
7516 O O   . HOH   E .   ? 0.5753 0.3909 0.3238 0.2621  0.1420  0.0951  312 HOH   B O   
7517 O O   . HOH   E .   ? 0.2562 0.2848 0.5328 -0.0130 -0.0762 0.1170  313 HOH   B O   
7518 O O   . HOH   E .   ? 0.2405 0.1496 0.2346 -0.0218 0.0020  0.0366  314 HOH   B O   
7519 O O   . HOH   E .   ? 0.3657 0.2056 0.2602 0.1238  0.0837  0.0198  315 HOH   B O   
7520 O O   . HOH   E .   ? 0.2824 0.2825 0.3516 -0.0465 0.1133  -0.0954 316 HOH   B O   
7521 O O   . HOH   E .   ? 0.2093 0.1894 0.1741 -0.0066 0.0248  0.0105  317 HOH   B O   
7522 O O   . HOH   E .   ? 0.2028 0.1487 0.3319 0.0358  -0.0941 -0.0135 318 HOH   B O   
7523 O O   . HOH   E .   ? 0.4877 0.3731 0.2028 0.0988  -0.0667 -0.0072 319 HOH   B O   
7524 O O   . HOH   E .   ? 0.4281 0.4249 0.4201 0.0074  0.1029  0.1562  320 HOH   B O   
7525 O O   . HOH   E .   ? 0.1509 0.2887 0.2127 -0.0131 -0.0214 0.0564  321 HOH   B O   
7526 O O   . HOH   E .   ? 0.2193 0.2379 0.5474 -0.0560 -0.0022 0.1331  322 HOH   B O   
7527 O O   . HOH   E .   ? 0.1546 0.1777 0.2865 -0.0231 0.0010  0.0087  323 HOH   B O   
7528 O O   . HOH   E .   ? 0.4545 0.2384 0.3260 0.0349  0.0633  0.0889  324 HOH   B O   
7529 O O   . HOH   E .   ? 0.5287 0.4209 0.5045 0.1404  0.1736  0.0524  325 HOH   B O   
7530 O O   . HOH   E .   ? 0.4799 0.3655 0.2688 0.0280  -0.0045 -0.0556 326 HOH   B O   
7531 O O   . HOH   E .   ? 0.2254 0.6320 0.5046 -0.1174 0.0145  -0.0117 327 HOH   B O   
7532 O O   . HOH   E .   ? 0.5611 0.5688 0.4602 -0.1254 -0.0839 0.1439  328 HOH   B O   
7533 O O   . HOH   E .   ? 0.4695 0.5532 0.5823 0.1306  -0.0756 0.2197  329 HOH   B O   
7534 O O   . HOH   E .   ? 0.5610 0.3451 0.4021 0.0224  0.1655  0.1551  330 HOH   B O   
7535 O O   . HOH   E .   ? 0.1419 0.1627 0.2811 -0.0122 0.0050  -0.0216 331 HOH   B O   
7536 O O   . HOH   E .   ? 0.1956 0.2993 0.3274 0.0421  -0.0038 -0.0998 332 HOH   B O   
7537 O O   . HOH   E .   ? 0.2677 0.2075 0.4881 0.0135  0.0012  0.0028  333 HOH   B O   
7538 O O   . HOH   E .   ? 0.2930 0.2348 0.2297 0.0395  -0.0451 0.0371  334 HOH   B O   
7539 O O   . HOH   E .   ? 0.4944 0.4175 0.5408 0.1370  -0.0037 0.0258  335 HOH   B O   
7540 O O   . HOH   E .   ? 0.1874 0.1821 0.2731 0.0254  0.0422  0.0165  336 HOH   B O   
7541 O O   . HOH   E .   ? 0.3547 0.3826 0.7963 -0.0209 -0.0991 0.2151  337 HOH   B O   
7542 O O   . HOH   E .   ? 0.6217 0.4460 0.5630 -0.1131 -0.1062 -0.1062 338 HOH   B O   
7543 O O   . HOH   E .   ? 0.4709 0.3214 0.5262 0.1442  0.2178  0.1765  339 HOH   B O   
7544 O O   . HOH   E .   ? 0.4952 0.5434 0.3322 0.0591  -0.1065 0.0107  340 HOH   B O   
7545 O O   . HOH   E .   ? 0.3856 0.3826 0.5660 -0.0403 -0.0039 0.0881  341 HOH   B O   
7546 O O   . HOH   E .   ? 0.7550 0.2608 0.3898 -0.0166 -0.0763 -0.0488 342 HOH   B O   
7547 O O   . HOH   E .   ? 0.1839 0.1452 0.2203 0.0103  -0.0136 0.0049  343 HOH   B O   
7548 O O   . HOH   E .   ? 0.3828 0.6264 0.3351 -0.0443 -0.0565 0.1026  344 HOH   B O   
7549 O O   . HOH   E .   ? 0.6452 0.5906 0.3051 0.0847  -0.0177 0.1177  345 HOH   B O   
7550 O O   . HOH   E .   ? 0.5256 0.3189 0.2737 0.0549  -0.0926 -0.0487 346 HOH   B O   
7551 O O   . HOH   E .   ? 0.4091 0.5698 0.4058 -0.0786 -0.1132 -0.0547 347 HOH   B O   
7552 O O   . HOH   E .   ? 0.2025 0.1899 0.2517 -0.0151 0.0506  -0.0099 348 HOH   B O   
7553 O O   . HOH   E .   ? 0.5254 0.5603 0.5025 -0.1290 0.0591  0.1175  349 HOH   B O   
7554 O O   . HOH   E .   ? 0.4369 0.5869 0.4989 -0.0452 -0.0858 0.1072  350 HOH   B O   
7555 O O   . HOH   E .   ? 0.2898 0.4750 0.4673 -0.1212 0.0691  -0.0744 351 HOH   B O   
7556 O O   . HOH   E .   ? 0.2797 0.1798 0.3757 0.0303  -0.1137 -0.0508 352 HOH   B O   
7557 O O   . HOH   E .   ? 0.2943 0.2136 0.4663 -0.0314 -0.0640 -0.0532 353 HOH   B O   
7558 O O   . HOH   E .   ? 0.4618 0.2488 0.4967 -0.0748 0.1732  0.0188  354 HOH   B O   
7559 O O   . HOH   E .   ? 0.5138 0.6920 0.7961 0.0899  0.2043  -0.0105 355 HOH   B O   
7560 O O   . HOH   E .   ? 0.3941 0.2117 0.2803 -0.0735 0.0173  -0.0662 356 HOH   B O   
7561 O O   . HOH   E .   ? 0.2115 0.4120 0.4482 0.0069  0.0337  -0.0376 357 HOH   B O   
7562 O O   . HOH   E .   ? 0.1972 0.5816 0.2949 0.1138  -0.0426 -0.1273 358 HOH   B O   
7563 O O   . HOH   E .   ? 0.4284 0.3144 0.3608 -0.0148 0.0910  -0.0406 359 HOH   B O   
7564 O O   . HOH   E .   ? 0.3406 0.2522 0.3907 -0.0644 -0.0055 -0.0547 360 HOH   B O   
7565 O O   . HOH   E .   ? 0.4140 0.4885 0.5153 0.1530  -0.1107 0.1511  361 HOH   B O   
7566 O O   . HOH   E .   ? 0.6052 0.4041 0.5964 0.0729  0.1445  0.1210  362 HOH   B O   
7567 O O   . HOH   E .   ? 0.5526 0.3809 0.5002 0.0888  -0.1579 -0.1059 363 HOH   B O   
7568 O O   . HOH   E .   ? 0.2048 0.4878 0.6023 -0.1017 -0.0414 -0.0852 364 HOH   B O   
7569 O O   . HOH   E .   ? 0.4954 0.6361 0.3282 0.2750  0.0047  0.0425  365 HOH   B O   
7570 O O   . HOH   E .   ? 0.6116 0.4833 0.4671 0.1162  0.0725  0.0828  366 HOH   B O   
7571 O O   . HOH   E .   ? 0.5736 0.6685 0.3321 0.1137  -0.1183 0.0370  367 HOH   B O   
7572 O O   . HOH   E .   ? 0.6134 0.5288 0.4192 0.1996  0.0927  0.1157  368 HOH   B O   
7573 O O   . HOH   E .   ? 0.6223 0.2237 0.3309 0.0140  0.0659  0.0579  369 HOH   B O   
7574 O O   . HOH   E .   ? 0.5360 0.6172 0.4652 -0.0160 -0.0480 -0.1225 370 HOH   B O   
7575 O O   . HOH   E .   ? 0.5878 0.3110 0.4730 -0.1129 0.0093  -0.0074 371 HOH   B O   
7576 O O   . HOH   E .   ? 0.4779 0.3718 0.5650 0.0559  -0.1625 0.0098  372 HOH   B O   
7577 O O   . HOH   E .   ? 0.4534 0.6122 0.5198 0.2981  0.0526  0.1172  373 HOH   B O   
7578 O O   . HOH   E .   ? 0.6137 0.4101 0.2838 -0.0652 -0.1171 -0.0728 374 HOH   B O   
7579 O O   . HOH   E .   ? 0.4119 0.2748 0.3125 0.0608  -0.0976 -0.0022 375 HOH   B O   
7580 O O   . HOH   E .   ? 0.7702 0.7575 0.5265 0.2412  -0.1045 0.0008  376 HOH   B O   
7581 O O   . HOH   E .   ? 0.4024 0.6496 0.5323 0.1293  0.0100  0.2372  377 HOH   B O   
7582 O O   . HOH   E .   ? 0.4604 0.5399 0.4429 -0.1010 -0.0765 0.0180  378 HOH   B O   
7583 O O   . HOH   E .   ? 0.3492 0.6228 0.5705 0.1027  -0.0904 -0.0090 379 HOH   B O   
7584 O O   . HOH   E .   ? 0.2997 0.5935 0.2102 0.0065  0.0158  0.0418  380 HOH   B O   
7585 O O   . HOH   E .   ? 0.2402 0.4230 0.3491 0.0413  -0.0355 -0.0707 381 HOH   B O   
7586 O O   . HOH   E .   ? 0.4798 0.7193 0.3618 -0.1366 0.0357  -0.1491 382 HOH   B O   
7587 O O   . HOH   E .   ? 0.4977 0.6683 0.5379 -0.0211 0.1911  0.1520  383 HOH   B O   
7588 O O   . HOH   E .   ? 0.4013 0.7936 0.4575 0.1802  0.1260  0.1208  384 HOH   B O   
7589 O O   . HOH   E .   ? 0.6396 0.3291 0.5160 -0.0221 -0.1229 -0.0288 385 HOH   B O   
7590 O O   . HOH   E .   ? 0.2819 0.2623 0.3449 0.0032  0.0182  0.0137  386 HOH   B O   
7591 O O   . HOH   E .   ? 0.7029 0.3212 0.4802 -0.0112 0.0597  -0.0970 387 HOH   B O   
7592 O O   . HOH   E .   ? 0.5782 0.5628 0.4312 0.0675  -0.0787 -0.0402 388 HOH   B O   
7593 O O   . HOH   E .   ? 0.6049 0.4775 0.5532 -0.1112 0.0003  0.0050  389 HOH   B O   
7594 O O   . HOH   E .   ? 0.4252 0.4409 0.3039 0.0083  0.0701  0.0180  390 HOH   B O   
7595 O O   . HOH   E .   ? 0.2102 0.4237 0.3901 -0.0400 -0.0797 -0.0389 391 HOH   B O   
7596 O O   . HOH   E .   ? 0.7308 0.5052 0.4167 0.1778  -0.0083 0.0070  392 HOH   B O   
7597 O O   . HOH   E .   ? 0.3821 0.2232 0.2904 0.0728  -0.0514 0.0035  393 HOH   B O   
7598 O O   . HOH   E .   ? 0.4734 0.4340 0.3589 0.0477  0.0354  0.0744  394 HOH   B O   
7599 O O   . HOH   E .   ? 0.4935 0.2240 0.4795 -0.0869 0.0226  0.0938  395 HOH   B O   
7600 O O   . HOH   E .   ? 0.2279 0.3915 0.7004 -0.0939 -0.0709 0.0120  396 HOH   B O   
7601 O O   . HOH   E .   ? 0.3276 0.4045 0.3592 0.0101  0.0207  -0.1069 397 HOH   B O   
7602 O O   . HOH   E .   ? 0.3920 0.7038 0.4238 -0.0527 -0.0347 -0.1178 398 HOH   B O   
7603 O O   . HOH   E .   ? 0.4606 0.4698 0.3750 0.0864  0.0881  0.0635  399 HOH   B O   
7604 O O   . HOH   E .   ? 0.2309 0.2393 0.5701 -0.0379 -0.0611 0.0392  400 HOH   B O   
7605 O O   . HOH   E .   ? 0.5639 0.3721 0.3001 -0.1773 -0.0482 0.0655  401 HOH   B O   
7606 O O   . HOH   E .   ? 0.5280 0.5694 0.5382 -0.0281 -0.1160 0.3069  402 HOH   B O   
7607 O O   . HOH   E .   ? 0.6563 0.5597 0.3504 0.0751  -0.0175 0.0347  403 HOH   B O   
# 
